Patent Publication Number: US-7214527-B2

Title: Compositions and methods for hydroxylating epothilones

Description:
BASIS FOR PRIORITY CLAIM 
     This application is a divisional application of U.S. application Ser. No. 10/321,188 filed Dec. 17, 2002 now U.S. Pat. No. 6,884,608, and claims the benefit of U.S. Provisional Application No. 60,344,271, filed December 26, 2001, which is herein incorporated by reference in its entirety. 
    
    
     FIELD OF THE INVENTION 
     The present invention relates to isolated nucleic acids sequences and polypeptides encoded thereby for epothilone B hydroxylase and mutants and variants thereof, and a ferredoxin located downstream from the epothilone B hydroxylase gene. The present invention also relates to recombinant microorganisms expressing epothilone B hydroxylase or a mutant or variant thereof and/or ferredoxin which are capable of hydroxylating small organic molecule compounds, such as epothilones, having a terminal alkyl group to produce compounds having a terminal hydroxyalkyl group. Also provided are methods for recombinantly producing such microorganisms as well as methods for using these recombinant microorganisms in the synthesis of compounds having a terminal hydroxylalkyl group. The compositions and methods of the present invention are useful in preparation of epothilones having a variety of utilities in the pharmaceutical field. A novel epothilone analog produced using a mutant of epothilone B hydroxylase of the present invention is also described. 
     BACKGROUND OF THE INVENTION 
     Epothilones are macrolide compounds that find utility in the pharmaceutical field. For example, epothilones A and B having the structures: 
                         
have been found to exert microtubule-stabilizing effects similar to paclitaxel (TAXOL®) and hence cytotoxic activity against rapidly proliferating cells, such as, tumor cells or cells associated with other hyperproliferative cellular diseases, see Bollag et al.,  Cancer Res ., Vol. 55, No. 11, 2325–2333 (1995).
 
     Epothilones A and B are natural anticancer agents produced by  Sorangium cellulosum  that were first isolated and characterized by Hofle et al., DE 4138042; WO 93/10121 ; Angew. Chem. Int. Ed. Engl . Vol. 35, No13/14, 1567–1569 (1996); and  J. Antibiot ., Vol. 49, No. 6, 560–563 (1996). Subsequently, the total syntheses of epothilones A and B have been published by Balog et al.,  Angew. Chem. Int. Ed. Engl ., Vol. 35, No. 23/24, 2801–2803, 1996; Meng et al.,  J. Am. Chem. Soc ., Vol. 119, No. 42, 10073–10092 (1997); Nicolaou et al.,  J. Am. Chem. Soc ., Vol. 119, No. 34, 7974–7991 (1997); Schinzer et al.,  Angew. Chem. Int. Ed. Eng ., Vol. 36, No. 5, 523–524 (1997); and Yang et al.,  Angew. Chem. Int. Ed. Engl ., Vol. 36, No. 1/2, 166–168, 1997. WO 98/25929 disclosed the methods for chemical synthesis of epothilone A, epothilone B, analogs of epothilone and libraries of epothilone analogs. The structure and production from  Sorangium cellulosum  DSM 6773 of epothilones C, D, E, and F was disclosed in WO 98/22461.  FIG. 1  provides a diagram of the biotransformation as described in WO 00/39276 of epothilone B to epothilone F in  Actinomycetes  species strain SC15847 (ATCC PT-1043), subsequently identified as  Amycolatopsis orientalis.    
     Cytochrome P450 enzymes are found in prokaryotes and eukaryotic cells and have in common a heme binding domain which can be distinguished by an absorbance peak at 450 nm when complexed with carbon monoxide. Cytochrome P450 enzymes perform a broad spectrum of oxidative reactions on primarily hydrophobic substrates including aromatic and benzylic rings, and alkanes. In prokaryotes they are found as detoxifying systems and as a first enzymatic step in metabolizing substrates such as toluene, benzene and camphor. Cytochrome P450 genes have also been found in biosynthetic pathways of secondary metabolites such as nikkomycin in  Streptomyces tendae  (Bruntner, C. et al, 1999, Mol. Gen. Genet. 262: 102–114), doxorubicin (Dickens, M. L, Strohl, W. R., 1996, J. Bacteriol, 178: 3389-3395) and in the epothilone biosynthetic cluster of  Sorangium cellulosum  (Julien, B. et al., 2000, Gene, 249: 153–160). With a few exceptions, the cytochrome P450 systems in prokaryotes are composed of three proteins; a ferredoxin NADH or NADPH dependent reductase, an iron-sulfur ferredoxin and the cytochrome P450 enzyme (Lewis, D. F., Hlavica, P., 2000, Biochim. Biophys. Acta., 1460: 353–374). Electrons are transferred from ferredoxin reductase to the ferredoxin and finally to the cytochrome P450 enzyme for the splitting of molecular oxygen. 
     SUMMARY OF THE INVENTION 
     An object of the present invention is to provide isolated nucleic acid sequences encoding epothilone B hydroxylase and variants or mutants thereof and isolated nucleic acid sequences encoding ferredoxin or variants or mutants thereof. 
     Another object of the present invention is to provide isolated polypeptides comprising amino acid sequences of epothilone B hydroxylase and variants or mutants thereof and isolated polypeptides comprising amino acid sequences of ferredoxin and variants or mutants thereof. 
     Another object of the present invention is to provide structure coordinates of the homology model of the epothilone B hydroxylase. The structure coordinates are listed in Appendix 1. This model of the present invention provides a means for designing modulators of a biological function of epothilone B hydroxylase as well as additional mutants of epothilone B hydroxylase with altered specificities. 
     Another object of the present invention is to provide vectors comprising nucleic acid sequences encoding epothilone B hydroxylase or a variant or mutant thereof and/or ferredoxin or a variant or mutant thereof. In a preferred embodiment, these vectors further comprise a nucleic acid sequence encoding ferredoxin. 
     Another object of the present invention is to provide host cells comprising a vector containing a nucleic acid sequence encoding epothilone B hydroxylase or a variant or mutant thereof and/or ferredoxin or a variant or mutant thereof. 
     Another object of the present invention is to provide a method for producing recombinant microorganisms that are capable of hydroxylating compounds, and in particular epothilones, having a terminal alkyl group to produce compounds having a terminal hydroxyalkyl group. 
     Another object of the present invention is to provide microorganisms produced recombinantly which are capable of hydroxylating compounds, and in particular epothilones, having a terminal alkyl group to produce compounds having a terminal hydroxyalkyl group. 
     Another object of the present invention is to provide methods for hydroxylating compounds in these recombinant microorganisms. In particular, the present invention provides a method for the preparation of hydroxyalkyl-bearing epothilones, which compounds find utility as antitumor agents and as starting materials in the preparation of other epothilone analogs. 
     Yet another object of the present invention is to provide a compound of Formula A: 
                         
referred to herein as 24-OH epothilone B or 24-OH EpoB, as well as compositions and methods for production of compositions comprising the compound of Formula A.
 
    
    
     
       BRIEF DESCRIPTION OF THE FIGURES 
         FIG. 1  provides a schematic of the biotransformation as set forth in WO 00/39276, U.S. application Ser. No. 09/468,854, filed Dec. 21, 1999, of epothilone B to epothilone F by  Amycolatopsis orientalis  strain SC 15847 (PTA 1043). 
         FIG. 2  shows the nucleic acid sequence alignments of SEQ ID NO:5 through SEQ ID NO:22 used to design the PCR primers for cloning of the nucleic acid sequence encoding epothilone B hydroxylase. 
         FIG. 3  shows the sequence alignment between epothilone B hydroxylase (SEQ ID NO:2) and EryF (PDB code 1JIN chain A; SEQ ID NO:76). The asterisks indicate sequence identities, the colons (:) similar residues. 
         FIG. 4  provides a homology model of epothilone B hydroxylase based upon sequence alignment with EryF as shown in  FIG. 3 . 
         FIG. 5  shows an energy plot of the epothilone B hydroxylase model (indicated by dashed line) relative to EryF (PDB code 1JIN; indicated by solid line). An averaging window size of 51 residues was used, i.e., the energy at a given residue position is calculated as the average of the energies of the 51 residues in the sequence that lie with the given residue at the central positions. 
     
    
    
     DETAILED DESCRIPTION OF THE INVENTION 
     The present invention relates to isolated nucleic acid sequences and polypeptides and methods for obtaining compounds with desired substituents at a terminal carbon position. In particular, the present invention provides compositions and methods for the preparation of hydroxyalkyl-bearing epothilones, which compounds find utility as antitumor agents and as starting materials in the preparation of other epothilone analogs. 
     The term “epothilone,” as used herein, denotes compounds containing an epothilone core and a side chain group as defined herein. The term “epothilone core,” as used herein, denotes a moiety containing the core structure (with the numbering of ring system positions used herein shown): 
                         
wherein the substituents are as follows:
 
     Q is selected from the group consisting of 
     
       
         
         
             
             
         
       
     
     W is O or NR 6 ; 
     X is selected from the group consisting of 0, H and OR 7 ; 
     M is O, S, NR 8 , CR 9 R 10 ; 
     B 1  and B 2  are selected from the group consisting of OR 11 , OCOR 12 ; 
     R 1 –R 5  and R 12 –R 17  are selected from the group consisting of H, alkyl, substituted alkyl, aryl, and heterocyclo, and wherein R 1  and R 2  are alkyl they can be joined to form a cycloalkyl; 
     R 6  is selected from the group consisting of H, alkyl, and substituted alkyl; 
     R 7  and R 11  are selected from the group consisting of H, alkyl, substituted alkyl, trialkylsilyl, alkyldiarylsilyl and dialkylarylsilyl; 
     R 8  is selected from the group consisting of H, alkyl, substituted alkyl, R 13 C═O, R 14 OC═O and R 15 SO 2 ; and 
     R 9  and R 10  are selected from the group consisting of H, halogen, alkyl, substituted alkyl, aryl, heterocyclo, hydroxy, R 16 C═O, and R 17 OC═O. 
     The term “side chain group” refers to substituent G as defined above for Epothilone A or B or G 1  and G 2  as shown below. 
     G 1  is the following formula V
 
HO—CH 2 -(A 1 ) n -(Q) m -(A 2 ) o   (V),
 
and
 
     G 2  is the following formula VI
 
CH 3 -(A 1 ) n -(Q) m -(A 2 ) o   (VI),
 
     where 
     A 1  and A 2  are independently selected from the group of optionally substituted C 1 –C 3  alkyl and alkenyl; 
     Q is optionally substituted ring system containing one to three rings and at least one carbon to carbon double bond in at least one ring; and 
     n, m, and o are integers independently selected from the group consisting of zero and 1, where at least one of m, n or o is 1. 
     The term “terminal carbon” or “terminal alkyl group” refers to the terminal carbon or terminal methyl group of the moiety either directly bonded to the epothilone core at position 15 or to the terminal carbon or terminal alkyl group of the side chain group bonded at position 15. It is understood that the term “alkyl group” includes alkyl and substituted alkyl as defined herein. 
     The term “alkyl” refers to optionally substituted, straight or branched chain saturated hydrocarbon groups of 1 to 20 carbon atoms, preferably 1 to 7 carbon atoms. The expression “lower alkyl” refers to optionally substituted alkyl groups of 1 to 4 carbon atoms. 
     The term “substituted alkyl” refers to an alkyl group substituted by, for example, one to four substituents, such as, halo, trifluoromethyl, trifluoromethoxy, hydroxy, alkoxy, cycloalkyloxy, heterocyclooxy, oxo, alkanoyl, aryloxy, alkanoyloxy, amino, alkylamino, arylamino, aralkylamino, cycloalkylamino, heterocycloamino, disubstituted amines in which the 2 amino substituents are selected from alkyl, aryl or aralkyl, alkanoylamino, aroylamino, aralkanoylamino, substituted alkanoylamino, substituted arylamino, substituted aralkanoylamino, thiol, alkylthio, arylthio, aralkylthio, cycloalkylthio, heterocyclothio, alkylthiono, arylthiono, aralkylthiono, alkylsulfonyl, arylsulfonyl, aralkylsulfonyl, sulfonamido (e.g. SO 2 NH 2 ), substituted sulfonamido, nitro, cyano, carboxy, carbamyl (e.g. CONH 2 ), substituted carbamyl (e.g. CONH alkyl, CONH aryl, CONH aralkyl or cases where there are two substituents on the nitrogen selected from alkyl, aryl or aralkyl), alkoxycarbonyl, aryl, substituted aryl, guanidino and heterocyclos, such as, indolyl, imidazolyl, furyl, thienyl, thiazolyl, pyrrolidyl, pyridyl, pyrimidyl and the like. Where noted above where the substituent is further substituted it will be with halogen, alkyl, alkoxy, aryl or aralkyl. 
     In accordance with one aspect of the present invention there are provided isolated polynucleotides that encode epothilone B hydroxylase, an enzyme capable of hydroxylating epothilones having a terminal alkyl group to produce epothilones having a terminal hydroxyalkyl group. 
     In accordance with another aspect of the present invention there are provided isolated polynucleotides that encode a ferredoxin, the gene for which is located downstream from the epothilone B hydroxylase gene. Ferredoxin is a protein of the cytochrome P450 system. 
     By “polynucleotides”, as used herein, it is meant to include any form of DNA or RNA such as cDNA or genomic DNA or mRNA, respectively, encoding these enzymes or an active fragment thereof which are obtained by cloning or produced synthetically by well known chemical techniques. DNA may be double- or single-stranded. Single-stranded DNA may comprise the coding or sense strand or the non-coding or antisense strand. Thus, the term polynucleotide also includes polynucleotides exhibiting at least 60% or more, preferably at least 80%, homology to sequences disclosed herein, and which hybridize under stringent conditions to the above-described polynucleotides. As used herein, the term “stringent conditions” means hybridization conditions of 60° C. at 2×SSC buffer. More preferred are isolated nucleic acid molecules capable of hybridizing to the nucleic acid sequence set forth in 1, 30, 32, 34, 36, 37, 38, 39, 40, 41, 42, 60, 62, 64, 66, 68, 70, 72, or 74 or SEQ ID NO:3, or to the complementary sequence of the nucleic acid sequence set forth in SEQ ID NO:1, 30, 32, 34, 36, 37, 38, 39, 40, 41, 42, 60, 62, 64, 66, 68, 70, 72, or 74 or SEQ ID NO:3, under hybridization conditions of 3×SSC at 65° C. for 16 hours, and which are capable of remaining hybridized to the nucleic acid sequence set forth in SEQ ID NO:1, 30, 32, 34, 36, 37, 38, 39, 40, 41, 42, 60, 62, 64, 66, 68, 70, 72 or 74 or SEQ ID NO:3, or to the complementary sequence of the nucleic acid sequence set forth in SEQ ID NO:1, 30, 32, 34, 36, 37, 38, 39, 40, 41 or 42, 60, 62, 64, 66, 68, 70, 72 or 74 or SEQ ID NO:3, under wash conditions of 0.5×SSC, 55° C. for 30 minutes. 
     In one embodiment, a polynucleotide of the present invention comprises the genomic DNA depicted in SEQ ID NO:1 or a homologous sequence or fragment thereof which encodes a polypeptide having similar activity to that of this epothilone B hydroxylase. Alternatively, a polynucleotide of the present invention may comprise the genomic DNA depicted in SEQ ID NO:3 or a homologous sequence or fragment thereof which encodes a polypeptide having similar activity to this ferredoxin. Due to the degeneracy of the genetic code, polynucleotides of the present invention may also comprise other nucleic acid sequences encoding this enzyme and derivatives, variants or active fragments thereof. 
     The present invention also relates to variants of these polynucleotides which may be naturally occurring, i.e., present in microorganisms such as  Amycolatopsis orientalis  and  Amycolata autotrophica , or in soil or other sources from which nucleic acids can be isolated, or mutants prepared by well known mutagenesis techniques. Exemplary variants polynucleotides of the present invention are depicted in SEQ ID NO: 36–42. 
     By “mutants” as used herein it is meant to be inclusive of nucleic acid sequences with one or more point mutations, or deletions or additions of nucleic acids as compared to SEQ ID NO: 1 or 3, but which still encode a polypeptide or fragment with similar activity to the polypeptides encoded by SEQ ID NO: 1 or 3. In a preferred embodiment, mutations are made which alter the substrate specificity and/or yield of the enzyme. A preferred region of mutation with respect to the epothilone B hydroxylase gene is that region of the nucleic acid sequence coding for the approximately 113 amino acids residues comprising the active site of the enzyme. Also preferred are mutants encoding a polypeptide with at least one amino acid substitution at amino acid position GLU31, ARG67, ARG88, ILE92, ALA93, VAL106, ILE130, ALA140, MET176, PHE190, GLU 231, SER294, PHE237, or ILE365 of SEQ ID NO:1. Exemplary polynucleotide mutants of the present invention are depicted in SEQ ID NO: 30, 32, 34, 60, 62, 64, 66, 68, 70, 72 and 74. 
     Cloning of the nucleic acid sequence of SEQ ID NO:1 encoding epothilone B hydroxylase was performed using PCR primers designed by aligning the nucleic acid sequences of six cytochrome P450 genes from bacteria. The following cytochrome P450 genes were aligned:
         Sequence: Locus: STMSUACB; Accession number: M32238; Reference: Omer, C. A., J. Bacteriol. 172: 3335–3345 (1990)   Sequence: Locus: STMSUBCB; Accession number: M32239; Reference: Omer, C. A., J. Bacteriol. 172: 3335–3345 (1990)   Sequence: Locus: AB018074 (formerly STMORFA); Accession number: AB018074; Reference: Ueda, K., J. Antibiot. 48: 638–646 (1995)   Sequence: Locus: SSU65940; Accession number: U65940; Reference: Motamedi, H., J. Bacteriol. 178: 5243–5248 (1996)   Sequence: Locus: STMOLEP; Accession number: L37200; Reference: Rodriguez, A. M., FEMS Microbiol. Lett. 127: 117–120 (1995)   Sequence: Locus: SERCP450A; Accession number: M83110; Reference: Andersen, J. F. and Hutchinson, C. R., J. Bacteriol. 174: 725–735 (1992)       

     Alignments were performed using an implementation of the algorithm of Myers, E. W. and W. Miller. 1988 . CABIOS  4:1, 11–17., the Align program from Scientific and Educational Software (Durham, N.C., USA). Three highly conserved regions were identified in the I-helix, containing the oxygen binding domain, in the K-helix, and spanning the B-bulge and L-helix containing the conserved heme binding domain. Primers were designed to the three conserved regions identified in the alignment. Primers P450-1 +  (SEQ ID NO:23) and P450-1a +  (SEQ ID NO:24) were designed from the I helix, Primer P450-2 +  (SEQ ID NO:25) was designed from the B-Bulge and L-helix region and Primer P450-3 −  (SEQ ID NO:27) was designed as the reverse complement to the heme binding protein. 
     Genomic fragments were then amplified via polymerase chain reaction (PCR). After PCR amplification, the reaction products were separated by gel electrophoresis and fragments of the expected size were excised. The DNA was extracted from the agarose gel slices using the Qiaquick gel extraction procedure (Qiagen, Santa Clarita, Calif., USA). The fragments were then cloned into the PCRscript vector (Stratagene, La Jolla, Calif., USA) using the PCRscript Amp cloning kit (Stratagene). Colonies containing inserts were picked to 1–2 ml of LB broth with 100 μg/ml ampicillin, 30–37° C., 16–24 hours, 230–300 rpm. Plasmid isolation was performed using the Mo Bio miniplasmid prep kit (Mo Bio, Solano Beach, Calif., USA). This plasmid DNA was used as a PCR and sequencing template and for restriction digest analysis. 
     The cloned PCR products were sequenced using the Big-Dye sequencing kit from Applied Biosystems, (Foster City, Calif., USA) and were analyzed using the AB1310 sequencer (Applied Biosystems, Foster City, Calif., USA). The sequence of the inserts was used to perform a TblastX search, using the protocol of Altschul, S. F, et al.,  Mol. Biol.  215:403–410 (1990), of the non-redundant protein database. Unique sequences having a significant similarity to known cytochrome P450 proteins were retained. Using this approach, a total of nine different P450 sequences were identified from SC15847, seven from the genomic DNA template and two from the cDNA. Two P450 sequences were found in common between the DNA and cDNA templates. Of the fifty cDNA clones analyzed, two sequences were predominant, with twenty clones each. These two genes were then cloned from the genomic DNA. 
     The nucleic acid sequence of the genomic DNA was determined using the Big-Dye sequencing system (Applied Biosystems) and analyzed using an ABI310 sequencer. This sequence is depicted in SEQ ID NO:1. An open reading frame coding for a protein of 404 amino acids and a predicted molecular weight of 44.7 kDa was found within the cloned BglII fragment. The deduced amino acid sequence of this polypeptide is depicted in SEQ ID NO: 2. The amino acid sequence of this polypeptide was found to share 51% identity with the NikF protein of  Streptomyces tendae  (Bruntner, C. et al, 1999, Mol. Gen. Genet. 262: 102–114) and 48% identity with the Sca-2 protein of  S. carbophilus  (Watanabe, I. Et al, 1995, Gene 163: 81–85). Both of these enzymes belong to the cytochrome P450 family 105. The invariable cysteine found in the heme-binding domain of all cytochrome P450 enzymes is found at residue 356. This gene for epothilone B hydroxylase has been named ebh. The ATG start codon of a putative ferredoxin gene of 64 amino acids is found nine basepairs downstream from the stop codon of ebh. This enzyme was found to share 50% identity with ferredoxin genes of  S. griseoulus  (O&#39;Keefe, D. P., et al, 1991, Biochemistry 30: 447–455) and  S. noursei  (Brautaset, T., et al, 2000, Chem. Biol. 7: 395–403). The nucleic acid sequence encoding this ferredoxin is depicted in SEQ ID NO:3 and the amino acid sequence for this ferredoxin polypeptide is depicted in SEQ ID NO:4. 
     The ebh gene sequence was also used to isolate variant cytochrome P450 genes from other microorganisms. Exemplary variant polynucleotides ebh43491, ebh14930, ebh53630, ebh53550, ebh39444, ebh43333 and ebh35165 of the present invention and the species from which they were isolated are depicted in Table 1 below. The nucleic acid sequences for these variants are depicted in SEQ ID NO:36-42, respectively. 
     
       
         
           
               
             
               
                 TABLE 1 
               
             
            
               
                   
               
               
                 Variant polynucleotides 
               
            
           
           
               
               
               
            
               
                 ATCC ID 
                 Species 
                 ebh gene designation 
               
               
                   
               
            
           
           
               
               
               
            
               
                 43491 
                 
                   Amycolatopsis orientalis 
                 
                 ebh43491 
               
               
                 14930 
                 
                   Amycolatopsis orientalis 
                 
                 ebh14930 
               
               
                 53630 
                 
                   Amycolatopsis orientalis 
                 
                 ebh53630 
               
               
                 53550 
                 
                   Amycolatopsis orientalis 
                 
                 ebh53550 
               
               
                 39444 
                 
                   Amycolatopsis orientalis 
                 
                 ebh39444 
               
               
                 43333 
                 
                   Amycolatopsis orientalis 
                 
                 ebh43333 
               
               
                 35165 
                 
                   Amycolatopsis orientalis 
                 
                 ebh35165 
               
               
                   
               
            
           
         
       
     
     The amino acid sequences encoded by the exemplary variants ebh43491, ebh14930, ebh53630, ebh53550, ebh39444, ebh43333 and ebh35165 are depicted in SEQ ID NO:43–49, respectively. Table 2 provides a summary of the amino acid substitutions of these exemplary variants. 
     
       
         
           
               
             
               
                 TABLE 2 
               
             
            
               
                   
               
               
                 Amino acid Substitutions 
               
            
           
           
               
               
               
               
            
               
                 Position 
                 ebh 
                 Substitution 
                 ebh variant 
               
               
                   
               
            
           
           
               
               
               
               
            
               
                 100 
                 Gly 
                 Ser 
                 ebh14930, ebh43333, ebh53550, 
               
               
                   
                   
                   
                 ebh43491 
               
               
                 101 
                 Lys 
                 Arg 
                 ebh14930 
               
               
                 130 
                 Ile 
                 Leu 
                 ebh14930 
               
               
                 192 
                 Ser 
                 Gln 
                 ebh14930 
               
               
                 224 
                 Ser 
                 Thr 
                 ebh14930, ebh43333, ebh53550, 
               
               
                   
                   
                   
                 ebh43491 
               
               
                 285 
                 Ile 
                 Val 
                 ebh14930, ebh43333, ebh53550, 
               
               
                   
                   
                   
                 ebh43491 
               
               
                 69 
                 Ser 
                 Asn 
                 ebh43333 
               
               
                 256 
                 Val 
                 Ala 
                 ebh43333, ebh53550, ebh43491 
               
               
                 93 
                 Ala 
                 Ser 
                 ebh53550 
               
               
                 326 
                 Asp 
                 Glu 
                 ebh53550, ebh43491 
               
               
                 333 
                 Thr 
                 Ala 
                 ebh53550, ebh43491 
               
               
                 133 
                 Leu 
                 Met 
                 ebh43491 
               
               
                 398 
                 His 
                 Arg 
                 ebh39444 
               
               
                   
               
            
           
         
       
     
     Mutations were also introduced into the coding region of the ebh gene to identify mutants with improved yield, and/or rate of bioconversion and/or altered substrate specificity. Exemplary mutant nucleic acid sequences of the present invention are depicted in SEQ ID NO:30, 32, 34, 60, 62, 64, 66, 68, 70, 72 and 74. 
     The nucleic acid sequence of SEQ ID NO:30 encodes a mutant ebh25-1 which exhibits altered substrate specificity. Plasmid pANT849ebh25-1 containing this mutant gene was deposited and accepted by an International Depository Authority under the provisions of the Budapest Treaty. The deposit was made on Nov. 21, 2002 to the American Type Culture Collection at 10801 University Boulevard in Manassas, Va. 20110-2209. The ATCC Accession Number is PTA-4809. All restrictions upon public access to this plasmid will be irrevocably removed upon granting of this patent application. The Deposit will be maintained in a public depository for a period of thirty years after the date of deposit or five years after the last request for a sample or for the enforceable life of the patent, whichever is longer. The above-referenced plasmid was viable at the time of the deposit. The deposit will be replaced if viable samples cannot be dispensed by the depository. 
     This  S. lividans  transformant identified in the screening of mutation 25 (primers NPB29-mut25f (SEQ ID NO:58) and NPB29-mut25r (SEQ ID NO:59)) was found to produce a product with a different HPLC elution time than epothilone B or epothilone F. A sample of this unknown was analyzed by LC-MS and was found to have a molecular weight of 523 (M.W.), consistent with a single hydroxylation of epothilone B. Plasmid DNA was isolated from the  S. lividans  culture and used as a template for PCR amplification using primers NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29) (see Example 17). The expected fragment was obtained and sequenced using the Big-Dye sequencing system. The ebh25-1 mutant was found to have two mutations resulting in changes in the amino acid sequence of the protein, asparagine 195 is changed to serine and serine 294 is changed to proline. The position targeted for mutation at codon 238 was found to have a two nucleotide change, which did not result in a change of the amino acid sequence of the protein. The amino acid sequence of the mutant polypeptide encoded by SEQ ID NO:30 is depicted in SEQ ID NO:31. 
     The nucleic acid sequence of SEQ ID NO:32 encodes a mutant ebh10-53, which exhibits improved bioconversion yield. This  S. lividans  transformant identified in the screening of mutation 10 (primers NPB29-mut10f (SEQ ID NO:54) and NPB29-mut10r (SEQ ID NO:55)) produced a greater yield of epothilone F. Plasmid DNA was isolated from the  S. lividans  culture and used as a template for PCR amplification using primers NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29)(see Example 16). The expected fragment was obtained and sequenced using the Big-Dye sequencing system. The ebh10-53 mutant was found to have two mutations resulting in changes in the amino acid sequence of the protein, glutamic acid 231 is changed to arginine and phenylalanine 190 is changed to tyrosine. The position 231 was the target of the mutagenesis, the change at residue 190 is an inadvertent change that is an artifact of the mutagenesis procedure. The amino acid sequence of the mutant polypeptide encoded by SEQ ID NO:32 is depicted in SEQ ID NO:33. 
     The nucleic acid sequence of SEQ ID NO:34 encodes a mutant ebh24-16, which also exhibits improved bioconversion yield. This  S. lividans  transformant, ebh24-16 identified in the screening of mutation 24 (primers NPB29-mut24f (SEQ ID NO:56) and NPB29-mut24r (SEQ ID NO:57) also produced a greater yield of epothilone F. Plasmid DNA was isolated from the  S. lividans  culture and used as a template for PCR amplification using primers NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29). The expected fragment was obtained and sequenced using the Big-Dye sequencing system. The ebh24-16 mutant was found to have two mutations resulting in changes in the amino acid sequence of the protein, phenylalanine 237 is changed to alanine and isoleucine 92 is changed to valine. The position 237 was the target of the mutagenesis, the change at residue 92 is an inadvertent change that is an artifact of the mutagenesis procedure. The amino acid sequence of the mutant polypeptide encoded by SEQ ID NO:34 is depicted in SEQ ID NO:35. 
     The nucleic acid sequence of SEQ ID NO:60 encodes a mutant ebh24-16d8, which also exhibits improved bioconversion yield. This  S. rimosus  transformant, ebh24-16d8 identified in the screening of mutation 59 (primer NPB29mut59 (SEQ ID NO:70)) also produced a greater yield of epothilone F. Plasmid DNA was isolated from the  S. rimosus  culture and used as a template for PCR amplification using primers NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29). The expected fragment was obtained and sequenced using the Big-Dye sequencing system. The ebh24-16d8 mutant was found to have one mutation resulting in a change in the amino acid sequence of the protein, arginine 67 is changed to glutamine. This change is an artifact of the mutagenesis procedure. The amino acid sequence of the mutant polypeptide encoded by SEQ ID NO:60 is SEQ ID NO:61. 
     The nucleic acid sequence of SEQ ID NO:62 encodes a mutant ebh24-16c11, which also exhibits improved bioconversion yield. This  S. rimosus  transformant, ebh24-16c11 identified in the screening of mutation 59 (primer NPB29mut59 (SEQ ID NO:70)) also produced a greater yield of epothilone F. Plasmid DNA was isolated from the  S. rimosus  culture and used as a template for PCR amplification using primers NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29). The expected fragment was obtained and sequenced using the Big-Dye sequencing system. The ebh24-16c11 mutant was found to have two additional mutations resulting in changes in the amino acid sequence of the protein, alanine 93 is changed to glycine and isoleucine 365 is changed to threonine. The position 93 is the target of the mutagenesis, the change at 365 is an artifact of the mutagenesis procedure. The amino acid sequence of the mutant polypeptide encoded by SEQ ID NO:62 is depicted in SEQ ID NO:63. 
     The nucleic acid sequence of SEQ ID NO:64 encodes a mutant ebh24-16-16, which also exhibits improved bioconversion yield. This  S. rimosus  transformant, ebh24-16-16 identified in the screening of random mutants of ebh24-16 also produced a greater yield of epothilone F. Plasmid DNA was isolated from the  S. rimosus  culture and used as a template for PCR amplification using primers NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29). The expected fragment was obtained and sequenced using the Big-Dye sequencing system. The ebh24-16-16 mutant was found to have one additional mutation resulting in changes in the amino acid sequence of the protein, valine 106 is changed to alanine. The amino acid sequence of the mutant polypeptide encoded by SEQ ID NO:64 is depicted in SEQ ID NO:65. 
     The nucleic acid sequence of SEQ ID NO:66 encodes a mutant ebh24-16-74, which also exhibits improved bioconversion yield. This  S. rimosus  transformant, ebh24-16-74 identified in the screening of random mutants of ebh24-16 also produced a greater yield of epothilone F. Plasmid DNA was isolated from the  S. rimosus  culture and used as a template for PCR amplification using primers NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29). The expected fragment was obtained and sequenced using the Big-Dye sequencing system. The ebh24-16-74 mutant was found to have one additional mutation resulting in changes in the amino acid sequence of the protein, arginine 88 is changed to histidine. The amino acid sequence of the mutant polypeptide encoded by SEQ ID NO:66 is SEQ ID NO:67. 
     The nucleic acid sequence of SEQ ID NO:68 encodes a mutant ebh24-M18, which also exhibits improved bioconversion yield. This  S. rimosus  transformant, ebhM-18 identified in the screening of random mutants of ebh also produced a greater yield of epothilone F. Plasmid DNA was isolated from the  S. rimosus  culture and used as a template for PCR amplification using primers NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29). The expected fragment was obtained and sequenced using the Big-Dye sequencing system. The ebhM-18 mutant was found to have two mutations resulting in changes in the amino acid sequence of the protein, glutamic acid 31 is changed to lysine and methionine 176 is changed to valine. The amino acid sequence of the mutant polypeptide encoded by SEQ ID NO:68 is depicted in SEQ ID NO:69. 
     The nucleic acid sequence of SEQ ID NO:72 encodes a mutant ebh24-16g8, which also exhibits improved bioconversion yield. This  S. rimosus  transformant, ebh24-16g8 identified in the screening of mutation 50 (primer NPB29mut50 (SEQ ID NO:71)) also produced a greater yield of epothilone F. Plasmid DNA was isolated from the  S. rimosus  culture and used as a template for PCR amplification using primers NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29). The expected fragment was obtained and sequenced using the Big-Dye sequencing system. The ebh24-16g8 mutant was found to have two additional mutations resulting in changes in the amino acid sequence of the protein, methionine 176 is changed to alanine and isoleucine 130 is changed to threonine. The position 176 is the target of the mutagenesis, the change at 130 is an artifact of the mutagenesis procedure. The amino acid sequence of the mutant polypeptide encoded by SEQ ID NO:72 is depicted in SEQ ID NO:73. 
     The nucleic acid sequence of SEQ ID NO:74 encodes a mutant ebh24-16b9, which also exhibits improved bioconversion yield. This  S. rimosus  transformant, ebh24-16b9 identified in the screening of mutation 50 (primer NPB29mut50 (SEQ ID NO:71)) also produced a greater yield of epothilone F. Plasmid DNA was isolated from the  S. rimosus  culture and used as a template for PCR amplification using primers NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29). The expected fragment was obtained and sequenced using the Big-Dye sequencing system. The ebh24-16b9 mutant was found to have two additional mutations resulting in changes in the amino acid sequence of the protein, methionine 176 is changed to serine and alanine 140 is changed to threonine. The position 176 is the target of the mutagenesis, the change at 140 is an artifact of the mutagenesis procedure. The amino acid sequence of the mutant polypeptide encoded by SEQ ID NO:74 is depicted in SEQ ID NO:75. 
     A mixture composed of the plasmids pANT849ebh-24-16, pANT849ebh-10-53, pANT849ebh-24-16d8, pANT849ebh-24-16c11, pANT849ebh-24-16-16, pant849ebh-24-16-74, pANT849ebh-24-16b9, pANT849ebh-M18 and pANT849ebh-24-16g8 for these nine mutant genes was deposited and accepted by an International Depository Authority under the provisions of the Budapest Treaty. The deposit was made on Nov. 21, 2002 to the American Type Culture Collection at 10801 University Boulevard in Manassas, Va. 20110-2209. The ATCC Accession Number is PTA-4808. All restrictions upon public access to this mixture of plasmids will be irrevocably removed upon granting of this patent application. The deposit will be maintained in a public depository for a period of thirty years after the date of deposit or five years after the last request for a sample or for the enforceable life of the patent, whichever is longer. The above-referenced mixture of plasmids was viable at the time of the deposit. The deposit will be replaced if viable samples cannot be dispensed by the depository. 
     Thus, in accordance with another aspect of the present invention, there are provided isolated polypeptides of epothilone B hydroxylase and variants and mutants thereof and isolated polypeptides of ferredoxin or variants thereof. In one embodiment of the present invention, by “polypeptide” it is meant to include the amino acid sequence of SEQ ID NO: 2, and fragments or variants, which retain essentially the same biological activity and/or function as this epothilone B hydroxylase. In another embodiment of the present invention, by “polypeptide” it is meant to include the amino acid sequence of SEQ ID NO:4, and fragments and/or variants, which retain essentially the same biological activity and/or function as this ferredoxin. 
     By “variants” as used herein it is meant to include polypeptides with amino acid sequences with conservative amino acid substitutions as compared to SEQ ID NO: 2 or 4 which are demonstrated to exhibit similar biological activity and/or function to SEQ ID NO:2 or 4. By “conservative amino acid substitutions” it is meant to include replacement, one for another, of the aliphatic amino acids such as Ala, Val, Leu and Ile, the hydroxyl residues Ser and Thr, the acidic residues Asp and Glu, and the amide residues Asn and Gln. Exemplary variant amino acid sequences of the present invention are depicted in SEQ ID NO:43–49 and the amino acid substitutions of these exemplary variants are described in Table 2, supra. 
     By “mutants” as used herein it is meant to include polypeptides encoded by nucleic acid sequences with one or more point mutations, or deletions or additions of nucleic acids as compared to SEQ ID NO: 1 or 3, but which still have similar activity to the polypeptides encoded by SEQ ID NO: 1 or 3. In a preferred embodiment, mutations are made to the nucleic acid that alter the substrate specificity and/or yield from the polypeptide encoded thereby. A preferred region of mutation with respect to the epothilone B hydroxylase gene is that region of the nucleic acid sequence coding for the approximately 113 amino acid residues comprising the active site of the enzyme. Also preferred are mutants with at least one amino acid substitution at amino acid position GLU31, ARG67, ARG88, ILE92, ALA93, VAL106, ILE130, ALA140, MET176, PHE190, GLU 231, SER294, PHE237, or ILE365 of SEQ ID NO:1 Exemplary mutants ebh25-1, ebh10-53, ebh24-16, ebh24-16d8, ebh24-16c11, ebh24-16-16, ebh24-16-74, ebh24-16g8, ebh24-16b9 and the nucleic acid sequences encoding such mutants of the present invention are depicted in SEQ ID NO:31, 33, 35, 61, 63, 65, 67, 69, 71, 73 and 75, and SEQ ID NO:30, 32, 34, 60, 62, 64, 66, 68, 70, 72 and 74, respectively. 
     A 3-dimensional model of epothilone B hydroxylase has also been constructed in accordance with general teachings of Greer et al. (Comparative modeling of homologous proteins. Methods In Enzymology 202239-52, 1991), Lesk et al. (Homology Modeling: Inferences from Tables of Aligned Sequences. Curr. Op. Struc. Biol. (2) 242–247, 1992), and Cardozo et al. (Homology modeling by the ICM method. Proteins 23, 403–14, 1995) on the basis of the known structure of a homologous protein EryF (PDB Code 1KIN chain A). Homology between these sequences is 34%. Alignment of the sequences of epothilone B hydroxylase (SEQ ID NO:2) and EryF (PDB Code 1KIN chain A; SEQ ID NO:76) is depicted in  FIG. 3 . A homology model of epothilone B hydroxylase based upon sequence alignment with EryF is depicted in  FIG. 4 . 
     An energy plot of the epothilone B hydroxylase model relative to EryF (PDB code 1JIN) was also prepared and is depicted in  FIG. 5 . An averaging window size of 51 residues was used at a given residue position to calculate the average of the energies of the 51 residues in the sequence that lie with the given residue at the central position. As shown in  FIG. 5 , all energies along the sequence lie below zero thus indicating that the modeled structure as set forth in  FIG. 4  and Appendix 1 is reasonable. 
     The three-dimensional structure represented in the homology model of epothilone B hydroxylase of  FIG. 4  is defined by a set of structure coordinates as set forth in Appendix 1. The term “structure coordinates” refers to Cartesian coordinates generated from the building of a homology model. As will be understood by those of skill in the art, however, a set of structure coordinates for a protein is a relative set of points that define a shape in three dimensions. Thus, it is possible that an entirely different set of coordinates could define a similar or identical shape. Moreover, slight variations in the individual coordinates, as emanate from generation of similar homology models using different alignment templates and/or using different methods in generating the homology model, will have minor effects on the overall shape. Variations in coordinates may also be generated because of mathematical manipulations of the structure coordinates. For example, the structure coordinates set forth in Appendix 1 could be manipulated by fractionalization of the structure coordinates; integer additions or subtractions to sets of the structure coordinates, inversion of the structure coordinates or any combination of the above. 
     Various computational analyses are therefore necessary to determine whether a molecule or a portion thereof is sufficiently similar to all or parts of epothilone B hydroxylase described above as to be considered the same. Such analyses may be carried out in current software applications, such as SYBYL version 6.7 or INSIGHTII (Molecular Simulations Inc., San Diego, Calif.) version 2000 and as described in the accompanying User&#39;s Guides. 
     For example, the superimposition tool in the program SYBYL allows comparisons to be made between different structures and different conformations of the same structure. The procedure used in SYBYL to compare structures is divided into four steps: 1) load the structures to be compared; 2) define the atom equivalencies in these structures; 3) perform a fitting operation; and 4) analyze the results. Each structure is identified by a name. One structure is identified as the target (i.e., the fixed structure); the second structure (i.e., moving structure) is identified as the source structure. Since atom equivalency within SYBYL is defined by user input, for the purpose of this aspect of the present invention equivalent atoms are defined as protein backbone atoms (N, Cα, C and O) for all conserved residues between the two structures being compared. Further, only rigid fitting operations are considered. When a rigid fitting method is used, the working structure is translated and rotated to obtain an optimum fit with the target structure. The fitting operation uses an algorithm that computes the optimum translation and rotation to be applied to the moving structure, such that the root mean square difference of the fit over the specified pairs of equivalent atoms is an absolute minimum. This number, given in angstroms, is reported by SYBYL. 
     For the purposes of the present invention, any homology model of epothilone B hydroxylase that has a root mean square deviation of conserved residue backbone atoms (N, Cα, C, O) of less than about 4.0 Å when superimposed on the corresponding backbone atoms described by structure coordinates listed in Appendix 1 are considered identical. More preferably, the root mean square deviation is less than about 3.0 Å. More preferably the root mean square deviation is less than about 2.0 Å. 
     For the purpose of this invention, any homology model of epothilone B hydroxylase that has a root mean square deviation of conserved residue backbone atoms (N, Cα, C, O) of less than about 2.0 Å when superimposed on the corresponding backbone atoms described by structure coordinates listed in Appendix 1 are considered identical. More preferably, the root mean square deviation is less than about 1.0 Å. 
     In another embodiment of the present invention, structural models wherein backbone atoms have been substituted with other elements which when superimposed on the corresponding backbone atoms have low root mean square deviations are considered to be identical. For example, an homology model where the original backbone carbon, and/or nitrogen and/or oxygen atoms are replaced with other elements having a root mean square deviation of about 4.0 Å, more preferably about 3.0 Å, even more preferably less than about 2 Å, when superimposed on the corresponding backbone atoms described by structure coordinates listed in Appendix 1 is considered identical. 
     The term “root mean square deviation” means the square root of the arithmetic mean of the squares of the deviations from the mean. It is a way to express the deviation or variation from a trend or object. For purposes of this invention, the “root mean square deviation” defines the variation in the backbone of a protein from the relevant portion of the backbone of the epothilone B hydroxylase portion of the complex as defined by the structure coordinates described herein. 
     The present invention as embodied by the homology model enables the structure-based design of additional mutants of epothilone B hydroxylase. For example, using the homology model of the present invention, residues lying within 10 Å of the binding site of epothilone B hydroxylase have now been defined. These residues include LEU39, GLN43, ALA45, MET57, LEU58, HIS62, PHE63, SER64, SER65, ASP66, ARG67, GLN68, SER69, LEU74, MET75, VAL76, ALA77, ARG78, GLN79, ILE80, ASP84, LYS85, PRO86, PHE87, ARG88, PRO89, SER90, LEU91, ILE92, ALA93, MET94, ASP95, HIS99, ARG103, PHE110, ILE155, PHE169, GLN170, CYS172, SER173, SER174, ARG175, MET176, LEU177, SER178, ARG179, ARG186, PHE190, LEU193, VAL233, GLY234, LEU235, ALA236, PHE237, LEU238, LEU239, LEU240, ILE241, ALA242, GLY243, HIS244, GLU245, THR246, THR247, ALA248, ASN249, MET250, LEU283, THR287, ILE288, ALA289, GLU290, THR291, ALA292, THR293, SER294, ARG295, PHE296, ALA297, THR298, GLU312, GLY313, VAL314, VAL315, GLY316, VAL344, ALA345, PHE346, GLY347, PHE348, VAL350, HIS351, GLN352, CYS353, LEU354, GLY355, GLN356, LEU358, ALA359, GLU362, LYS389, ASP391, SER392, THR393, ILE394 and TYR395 as set forth in Appendix 1. Mutants with mutations at one or more of these positions are expected to exhibit altered biological function and/or specificity and thus comprise another embodiment of preferred mutants of the present invention. Another embodiment of preferred mutants are molecules that have a root mean square deviation from the backbone atoms of said epothilone B hydroxylase of not more than about 4.0 Å. 
     The structure coordinates of an epothilone B hydroxylase homology model or portions thereof are stored in a machine-readable storage medium. Such data may be used for a variety of purposes, such as drug discovery. 
     Accordingly, another aspect of the present invention relates to machine-readable data storage medium comprising a data storage material encoded with the structure coordinates set forth in Appendix 1. 
     The three-dimensional model structure of epothilone B hydroxylase can also be used to identify modulators of biological function and potential substrates of the enzyme. Various methods or combinations thereof can be used to identify such modulators. 
     For example, a test compound can be modeled that fits spatially into a binding site in epothilone B hydroxylase, according to Appendix 1. Structure coordinates of amino acids within 10 Å of the binding region of epothilone B hydroxylase defined by amino acids LEU39, GLN43, ALA45, MET57, LEU58, HIS62, PHE63, SER64, SER65, ASP66, ARG67, GLN68, SER69, LEU74, MET75, VAL76, ALA77, ARG78, GLN79, ILE80, ASP84, LYS85, PRO86, PHE87, ARG88, PRO89, SER90, LEU91, ILE92, ALA93, MET94, ASP95, HIS99, ARG103, PHE110, ILE155, PHE169, GLN170, CYS172, SER173, SER174, ARG175, MET176, LEU177, SER178, ARG179, ARG186, PHE190, LEU193, VAL233, GLY234, LEU235, ALA236, PHE237, LEU238, LEU239, LEU240, ILE241, ALA242, GLY243, HIS244, GLU245, THR246, THR247, ALA248, ASN249, MET250, LEU283, THR287, ILE288, ALA289, GLU290, THR291, ALA292, THR293, SER294, ARG295, PHE296, ALA297, THR298, GLU312, GLY313, VAL314, VAL315, GLY316, VAL344, ALA345, PHE346, GLY347, PHE348, VAL350, HIS351, GLN352, CYS353, LEU354, GLY355, GLN356, LEU358, ALA359, GLU362, LYS389, ASP391, SER392, THR393, ILE394 and TYR395, and the coordinated heme group, HEM1 can also be used to identify desirable structural and chemical features of such modulators. Identified structural or chemical features can then be employed to design or select compounds as potential epothilone B hydroxylase ligands. By structural and chemical features it is meant to include, but is not limited to, covalent bonding, van der Waals interactions, hydrogen bonding interactions, charge interaction, hydrophobic bonding interaction, and dipole interaction. Compounds identified as potential epothilone B hydroxylase ligands can then be synthesized and screened in an assay characterized by binding of a test compound to epothilone B hydroxylase, or in characterizing the ability of epothilone B hydroxylase to modulate a protease target in the presence of a small molecule. Examples of assays useful in screening of potential epothilone B hydroxylase ligands include, but are not limited to, screening in silico, in vitro assays and high throughput assays. 
     As will be understood by those of skill in the art upon this disclosure, other structure-based design methods can be used. Various computational structure-based design methods have been disclosed in the art. For example, a number of computer modeling systems are available in which the sequence of epothilone B hydroxylase and the epothilone B hydroxylase structure (i.e., atomic coordinates of epothilone B hydroxylase as provided in Appendix 1 and/or the atomic coordinates within 10 Å of the binding region as provided above) can be input. This computer system then generates the structural details of one or more these regions in which a potential epothilone B hydroxylase modulator binds so that complementary structural details of the potential modulators can be determined. Design in these modeling systems is generally based upon the compound being capable of physically and structurally associating with epothilone B hydroxylase. In addition, the compound must be able to assume a conformation that allows it to associate with epothilone B hydroxylase. Some modeling systems estimate the potential inhibitory or binding effect of a potential epothilone B hydroxylase substrate or modulator prior to actual synthesis and testing. 
     Methods for screening chemical entities or fragments for their ability to associate with a given protein target are also well known. Often these methods begin by visual inspection of the binding site on the computer screen. Selected fragments or chemical entities are then positioned in a binding region of epothilone B hydroxylase. Docking is accomplished using software such as INSIGHTII, QUANTA and SYBYL, following by energy minimization and molecular dynamics with standard molecular mechanic force fields such as, MMFF, CHARMM and AMBER. Examples of computer programs which assist in the selection of chemical fragment or chemical entities useful in the present invention include, but are not limited to, GRID (Goodford, 1985), AUTODOCK (Goodsell, 1990), and DOCK (Kuntz et al. 1982). 
     Upon selection of preferred chemical entities or fragments, their relationship to each other and epothilone B hydroxylase can be visualized and then assembled into a single potential modulator. Programs useful in assembling the individual chemical entities include, but are not limited to CAVEAT (Bartlett et al. 1989) and 3D Database systems (Martin 1992). 
     Alternatively, compounds may be designed de novo using either an empty active site or optionally including some portion of a known inhibitor. Methods of this type of design include, but are not limited to LUDI (Bohm 1992) and LeapFrog (Tripos Inc., St. Louis Mo.). 
     Programs such as DOCK (Kuntz et al. 1982) can be used with the atomic coordinates from the homology model to identify potential ligands from databases or virtual databases which potentially bind the in the active site binding region which may therefore be suitable candidates for synthesis and testing. 
     Also provided in the present invention are vectors comprising polynucleotides of the present invention and host cells which are genetically engineered with vectors of the present invention to produce epothilone B hydroxylase or active fragments and variants or mutants of this enzyme and/or ferredoxin or active fragments thereof. Generally, any vector suitable to maintain, propagate or express polynucleotides to produce these polypeptides in the host cell may be used for expression in this regard. In accordance with this aspect of the invention the vector may be, for example, a plasmid vector, a single- or double-stranded phage vector, or a single- or double-stranded RNA or DNA viral vector. Vectors may be extra-chromosomal or designed for integration into the host chromosome. Such vectors include, but are not limited to, chromosomal, episomal and virus-derived vectors e.g., vectors derived from bacterial plasmids, bacteriophages, yeast episomes, yeast chromosomal elements, and viruses such as baculoviruses, papova viruses, SV40, vaccinia viruses, adenoviruses, fowl pox viruses, pseudorabies viruses and retroviruses, and vectors derived from combinations thereof, such as those derived from plasmid and bacteriophage genetic elements, cosmids and phagemids. 
     Useful expression vectors for prokaryotic hosts include, but are not limited to, bacterial plasmids, such as those from  E. coli, Bacillus  or  Streptomyces , including pBluescript, pGEX-2T, pUC vectors, pET vectors, ColE1, pCR1, pBR322, pMB9, pCW, pBMS200, pBMS2020, PIJ101, PIJ702, pANT849, pOJ260, pOJ446, pSET152, pKC1139, pKC1218, pFD666 and their derivatives, wider host range plasmids, such as RP4, phage DNAs, e.g., the numerous derivatives of phage lambda, e.g., NM989, λGT10 and λGT11, and other phages, e.g., M13 and filamentous single stranded phage DNA. 
     Vectors of the present invention for use in yeast will typically contain an origin of replication suitable for use in yeast and a selectable marker that is functional in yeast. Examples of yeast vectors useful in the present invention include, but are not limited to, Yeast Integrating plasmids (e.g., YIp5) and Yeast Replicating plasmids (the YRp and YEp series plasmids), Yeast Centromere plasmids (the YCp series plasmids), Yeast Artificial Chromosomes (YACs) which are based on yeast linear plasmids, denoted YLp, pGPD-2, 2μ plasmids and derivatives thereof, and improved shuttle vectors such as those described in Gietz et al.,  Gene,  74: 527–34 (1988) (YIplac, YEplac and YCplac). 
     Mammalian vectors useful for recombinant expression may include a viral origin, such as the SV40 origin (for replication in cell lines expressing the large T-antigen, such as COS1 and COS7 cells), the papillomavirus origin, or the EBV origin for long term episomal replication (for use, e.g., in 293-EBNA cells, which constitutively express the EBV EBNA-1 gene product and adenovirus E1A). Expression in mammalian cells can be achieved using a variety of plasmids, including, but not limited to, pSV2, pBC12BI, and p91023, pCDNA vectors as well as lytic virus vectors (e.g., vaccinia virus, adeno virus, and baculovirus), episomal virus vectors (e.g., bovine papillomavirus), and retroviral vectors (e.g., murine retroviruses). Useful vectors for insect cells include baculoviral vectors and pVL941. 
     Selection of an appropriate promoter to direct mRNA transcription and construction of expression vectors are well known. In general, however, expression constructs will contain sites for transcription initiation and termination, and, in the transcribed region, a ribosome binding site for translation. The coding portion of the mature transcripts expressed by the constructs will include a translation initiating codon at the beginning and a termination codon appropriately positioned at the end of the polypeptide to be translated. 
     Examples of useful promoters for prokaryotes include, but are not limited to phage promoters such as phage lambda pL promoter, the trc promoter, a hybrid derived from the trp and lac promoters, the bacteriophage T7 promoter, the TAC or TRC system, the major operator and promoter regions of phage lambda, the control regions of fd coat protein, snpA promoter, melC promotor, ermE* promoter or the araBAD operon. Examples of useful promoters for yeast include, but are not limited to, the CYC1 promoter, the GAL1 promoter, the GAL10 promoter, ADH1 promoter, the promoters of the yeast α-mating system, and the GPD promoter. Examples of promoters routinely used in mammalian expression vectors include, but are not limited to, the CMV immediate early promoter, the HSV thymidine kinase promoter, the early and late SV40 promoters, the promoters of retroviral LTRs, such as those of the Rous Sarcoma Virus (RSV), and metallothionein promoters, such as the mouse metallothionein-I promoter. 
     Vectors comprising the polynucleotides can be introduced into host cells using any number of well known techniques including infection, transduction, transfection, transvection and transformation. The polynucleotides may be introduced into a host alone or with additional polynucleotides encoding, for example, a selectable marker or ferredoxin reductase. In a preferred embodiment of the present invention the polynucleotide for epothilone B hydroxylase and ferredoxin are introduced into the host cell. Host cells for the various expression constructs are well known, and those of skill can routinely select a host cell for expressing the epothilone B hydroxylase and/or ferredoxin in accordance with this aspect of the present invention. Examples of mammalian expression systems useful in the present invention include, but are not limited to, the C127, 3T3, CHO, HeLa, human kidney 293 and BHK cell lines, and the COS-7 line of monkey kidney fibroblasts. 
     Alternatively, as exemplified herein, epothilone B hydroxylase and ferredoxin can be expressed recombinantly in microorganisms. 
     Accordingly, another aspect of the present invention relates to recombinantly produced microorganisms which express epothilone B hydroxylase alone or in conjunction with the ferredoxin and which are capable of hydroxylating a compound, and in particular an epothilone, having a terminal alkyl group to produce ones having a terminal hydroxyalkyl group. The recombinantly produced microorganisms are produced by transforming cells such as bacterial cells with a plasmid comprising a nucleic acid sequence encoding epothilone B hydroxylase. In a preferred embodiment, the cells are transformed with a plasmid comprising a nucleic acid encoding epothilone B hydroxylase or mutants or variants thereof as well as the nucleic acid sequence encoding ferredoxin located downstream of the epothilone B hydroxylase gene. Examples of microorganisms which can be transformed with these plasmids to produce the recombinant microorganisms of the present invention include, but are not limited,  Escherichia coli, Bacillus megaterium, Amycolatopsis orientalis, Sorangium cellulosum, Rhodococcus erythropolis , and  Streptomyces  species such as  Streptomyces lividans, Streptomyces virginiae, Streptomyces venezuelae, Streptomyces albus, Streptomyces coelicolor, Streptomyces rimosus  and  Streptomyces griseus.    
     The recombinantly produced microorganisms of the present invention are useful in microbial processes or methods for production of compounds, and in particular epothilones, containing a terminal hydroxyalkyl group. In general, the hydroxyalkyl-bearing product can be produced by culturing the recombinantly produced microorganism or enzyme derived therefrom, capable of selectively hydroxylating a terminal carbon or alkyl, in the presence of a suitable substrate in an aqueous nutrient medium containing sources of assimilable carbon and nitrogen, under submerged aerobic conditions. 
     Suitable epothilones employed as substrate for the method of the present invention may be any such compound having a terminal carbon or terminal alkyl group capable of undergoing the enzymatic hydroxylation of the present invention. The starting material, or substrate, can be isolated from natural sources, such as  Sorangium cellulosum , or they can be synthetically formed epothilones. Other substrates having a terminal carbon or terminal alkyl group capable of undergoing an enzymatic hydroxylation can be employed by the methods herein. For example, compactin can be used as a substrate, which upon hydroxylation forms the compound pravastatin. Methods for hydroxylating compactin to pravastatin via an  Actinomadura  strain are set forth in U.S. Pat. No. 5,942,423 and U.S. Pat. No. 6,274,360. 
     For example, using the recombinant microorganisms of the present invention at least one epothilone can be prepared as described in WO 00/39276, U.S. Ser. No. 09/468,854, filed Dec. 21, 1999, the text of which is incorporated herein as if set forth at length. An epothilone of the following Formula I
 
HO—CH 2 -(A 1 ) n -(Q) m -(A 2 ) o -E  (I)
 
where
 
     A 1  and A 2  are independently selected from the group of optionally substituted C 1 –C 3  alkyl and alkenyl; 
     Q is an optionally substituted ring system containing one to three rings and at least one carbon to carbon double bond in at least one ring; 
     n, m, and o are integers selected from the group consisting of zero and 1, where at least one of m or n or o is 1; and 
     E is an epothilone core; can be prepared. 
     This method comprises the steps of contacting at least one epothilone of the following formula II
 
CH 3 -(A 1 ) n -(Q) m -(A 2 ) o -E  (II)
 
     where A 1 , Q, A 2 , E, n, m, and o are defined as above; 
     with a recombinantly produced microorganism, or an enzyme derived therefrom, which is capable of selectively catalyzing the hydroxylation of formula II, and effecting said hydroxylation. 
     In a preferred embodiment, the starting material is epothilone B. Epothilone B can be obtained from the fermentation of  Sorangium cellulosum  So ce90, as described in DE 41 38 042 and WO 93/10121. The strain has been deposited at the Deutsche Sammlung von Mikroorganismen (German Collection of Microorganisms) (DSM) under No. 6773. The process of fermentation is also described in Hofle, G., et al.,  Angew. Chem. Int. Ed. Engl ., Vol 35, No. 13/14, 1567–1569 (1996). Epothilone B can also be obtained by chemical means, such as those disclosed by Meng, D., et al.,  J. Am. Chem. Soc ., Vol. 119, No. 42, 10073–10092 (1996); Nicolaou, K., et al.,  J. Am. Chem. Soc ., Vol. 119, No. 34, 7974–7991 (1997) and Schinzer, D., et al.,  Chem. Eur. J ., Vol. 5, No. 9, 2483–2491 (1999). 
     Growth of the recombinantly produced microorganism selected for use in the process may be achieved by one of ordinary skill in the art by the use of appropriate nutrient medium. Appropriate media for the growing of the recombinantly produced microorganisms include those that provide nutrients necessary for the growth of microbial cells. See, for example, T. Nagodawithana and J. M. Wasileski, Chapter 2: “Media Design for Industrial Fermentations,”  Nutritional Requirements of Commercially Important Microorganism , edited by T. W. Nagodawithana and G. Reed, Esteekay Associates, Inc., Milwaukee, Wis., 18–45 (1998); T. L. Miller and B. W. Churchill, Chapter 10: “Substrates for Large-Scale Fermentations,”  Manual of Industrial Microbiology and Biotechnology , edited by A. L. Demain and N. A. Solomon, American Society for Microbiology, Washington, D.C., 122–136 (1986). A typical medium for growth includes necessary carbon sources, nitrogen sources, and trace elements. Inducers may also be added to the medium. The term inducer as used herein, includes any compound enhancing formation of the desired enzymatic activity within the recombinantly produced microbial cell. Typical inducers as used herein may include solvents used to dissolve substrates, such as dimethyl sulfoxide, dimethyl formamide, dioxane, ethanol and acetone. Further, some substrates, such as epothilone B, may also be considered to be inducers. 
     Carbon sources may include sugars such as glucose, fructose, galactose, maltose, sucrose, mannitol, sorbital, glycerol starch and the like; organic acids such as sodium acetate, sodium citrate, and the like; and alcohols such as ethanol, propanol and the like. Preferred carbon sources include, but are not limited to, glucose, fructose, sucrose, glycerol and starch. 
     Nitrogen sources may include an N-Z amine A, corn steeped liquor, soybean meal, beef extract, yeast extract, tryptone, peptone, cottonseed meal, peanut meal, amino acids such as sodium glutamate and the like, sodium nitrate, ammonium sulfate and the like. 
     Trace elements may include magnesium, manganese, calcium, cobalt, nickel, iron, sodium and potassium salts. Phosphates may also be added in trace or preferably, greater than trace amounts. 
     The medium employed for the fermentation may include more than one carbon or nitrogen source or other nutrient. 
     For growth of the recombinantly produced microorganisms and/or hydroxylation according to the method of the present invention, the pH of the medium is preferably from about 5 to about 8 and the temperature is from about 14° C. to about 37° C., preferably the temperature is 28° C. The duration of the reaction is 1 to 100 hours, preferably 8 to 72 hours. 
     The medium is incubated for a period of time necessary to complete the biotransformation as monitored by high performance liquid chromatography (HPLC). Typically, the period of time needed to complete the transformation is twelve to one hundred hours and preferably about 72 hours after the addition of the substrate. The medium is placed on a rotary shaker (New Brunswick Scientific Innova 5000) operating at 150 to 300 rpm and preferably about 250 rpm with a throw of 2 inches. 
     The hydroxyalkyl-bearing product can be recovered from the fermentation broth by conventional means that are commonly used for the recovery of other known biologically active substances. Examples of such recovery means include, but are not limited to, isolation and purification by extraction with a conventional solvent, such as ethyl acetate and the like; by pH adjustment; by treatment with a conventional resin, for example, by treatment with an anion or cation exchange resin or a non-ionic adsorption resin; by treatment with a conventional adsorbent, for example, by distillation, by crystallization; or by recrystallization, and the like. 
     The extract obtained above from the biotransformation reaction mixture can be further isolated and purified by column chromatography and analytical thin layer chromatography. 
     The ability of a recombinantly produced microorganism of the present invention to biotransform an epothilone having a terminal alkyl group to an epothilone having a terminal hydroxyalkyl group was demonstrated. In these experiments, a culture comprising a  Streptomyces lividans  clone containing a plasmid with the ebh gene as described in more detail in Example 11 was incubated with an epothilone B suspension for 3 days at 30° with agitation. A sample of the incubate was extracted with an equal volume of 25% methanol: 75% n-butanol, vortexed and allowed to settle for 5 minutes. Two hundred μl of the organic phase was transferred to an HPLC vial and analyzed by HPLC/MS (Example 12). A product peak of epothilone F eluted at a retention time of 15.9 minutes and had a protonated molecular weight of 524. The epothilone B substrate eluted at 19.0 minutes and had a protonated molecular weight of 508. The peak retention times and molecular weights were confirmed using known standards. 
     Rates of biotransformation of epothilone B by cells expressing ebh were also compared to rates of biotransformation by ebh mutants. Cells expressing ebh comprised a frozen spore preparation of.  S. lividans  (pANT849-ebh). Cells expressing mutants comprises frozen spore preparations of  S. lividans  (pANT849-ebh10-53) and  S. lividans  (pANT849-ebh24-16). A frozen spore preparation of  S. lividans  TK24 was used as the control. The cells were pre-incubated for several days at 30° C. Following this pre-incubation, epothilone B in 100% EtOH was added to each culture to a final concentration of 0.05% weight/volume. Samples were then taken at 0, 24, 48 and 72 hours with the exception of the  S. lividans  (pANT849-ebh24-16) culture, in which the epothilone B had been completely converted to epothilone F at 48 hours. The samples were analyzed by HPLC. The results are calculated as a percentage of the epothilone B at time 0 hours. 
     
       
         
           
               
               
               
               
               
             
               
                   
               
               
                   
                   
                   
                   
                 pANT849- 
               
               
                 Time (hours) 
                 TK24 
                 pANT849-ebh 
                 pANT849-ebh10-53 
                 ebh24-16 
               
               
                   
               
             
            
               
                   
               
            
           
           
               
               
               
               
               
            
               
                 0 
                 100% 
                 100% 
                 100% 
                 100% 
               
               
                 24 
                  99% 
                  78% 
                  69% 
                  56% 
               
               
                 48 
                  87% 
                  19% 
                  39% 
                  0% 
               
               
                 72 
                  87% 
                  0% 
                  3% 
                 — 
               
               
                   
               
            
           
         
       
     
     
       
         
           
               
               
               
               
               
             
               
                   
               
               
                   
                   
                   
                   
                 pANT849- 
               
               
                 Time (hours) 
                 TK24 
                 pANT849-ebh 
                 pANT849-ebh10-53 
                 ebh24-16 
               
               
                   
               
             
            
               
                   
               
            
           
           
               
               
               
               
               
            
               
                 0 
                 0% 
                  0% 
                  0% 
                  0% 
               
               
                 24 
                 0% 
                  4% 
                  9% 
                 23% 
               
               
                 48 
                 0% 
                 21% 
                 29% 
                 52% 
               
               
                 72 
                 0% 
                 14% 
                 41% 
                 — 
               
               
                   
               
            
           
         
       
     
     The ability of cells expressing ebh to biotransform compactin to pravastatin was also examined. In these experiments, frozen spore preparations of  S. lividans  (pANT849) or  S. lividans  (pANT849-ebh) were grown for several days at 30° C. Following the pre-incubation, an aliquot of each cell culture was transferred to a polypropylene culture tube, compactin was added to each culture tube, and the tubes were incubated for 24 hours, 30° C., 250 rpm. An aliquot of the culture broth was then extracted and compactin and pravastatin values relative to the control  S. lividans  (pANT849) culture were measured via HPLC. 
     Compactin and pravastatin as a percentage of starting compactin concentration: 
     
       
         
           
               
               
               
             
               
                   
                   
               
               
                   
                   S. lividans  (pANT849) 
                   S. lividans  (pANT849-ebh) 
               
               
                   
                   
               
             
            
               
                   
               
            
           
           
               
               
               
            
               
                 Compactin 
                 36% 
                 11% 
               
               
                 Pravastatin 
                 11% 
                 53% 
               
               
                   
               
            
           
         
       
     
     As discussed supra, mutant ebh25-1 (SEQ ID NO:30) exhibits altered substrate specificity and biotransformation of epothilone B by this mutant resulted in a product with a different HPLC elution time than epothilone B or epothilone F. A sample of this unknown was analyzed by LC-MS and was found to have a molecular weight of 523 (M.W.), consistent with a single hydroxylation of epothilone B. The structure of the biotransformation product was determined as 24-hydroxyl-epothilone B, based on MS and NMR data (compared with data of epothilone B): 
     
       
         
         
             
             
         
       
     
     Molecular Formula: C 27 H 41 NO 7 S Molecular Weight: 523 Mass Spectrum: ES+ (m/z): 524([M+H] + ), 506. LC/MS/MS: +ESI (m/z): 524, 506, 476, 436, 320 HRMS: Calculated for [M+H] + : 524.2682; Found: 524.2701 HPLC (Rt) 7.3 minutes (on the analytical HPLC system) LC/NMR Observed Chemical Shifts Varian AS-600 (Proton: 599.624 MHz), Solvent D 2 O/CD 3 CN (δ 1.94): ˜4/6 Proton: δ7.30 (s, 1H), 6.43 (s, 1H), 5.30 (m, 1H), 4.35 (m, 1H), 3.81 (m, 1H), 3.74 (m, 1H), 3.68 (m, 1H), 3.43 (m, 1H), 2.87 (m, 1H), 2.66 (s, 3H), 2.40 (m, 2H), 1.58 (b, 1H), 1.48 (b, 1H), 1.35 (m, 3H), 1.18 (s, 3H), 1.13 (s, 3H), 0.87 (m, 6H) *Peaks between 1.8–2.1 ppm were not observed due to solvent suppression. 
     The proton chemical shift was assigned as follows: 
     
       
         
           
               
               
               
             
               
                   
               
               
                 Position 
                 Proton 
                 Pattern 
               
               
                   
               
             
            
               
                   
               
            
           
           
               
               
               
            
               
                 1 
                 — 
                   
               
               
                 2 
                 2.40 
                 m 
               
               
                 3 
                 4.35 
                 m 
               
               
                 4 
                 — 
               
               
                 5 
                 — 
               
               
                 6 
                 3.43 
                 m 
               
               
                 7 
                 3.68 
                 m 
               
               
                 8 
                 1.58 
                 m 
               
               
                 9 
                 1.35 
                 b 
               
               
                 10 
                 1.48 
                 b 
               
               
                 10 
                 1.35 
                 b 
               
               
                 11 
                 SSP 
               
               
                 12 
                 — 
               
               
                 13 
                 2.87 
                 m 
               
               
                 14 
                 SSP 
               
               
                 15 
                 5.30 
                 m 
               
               
                 16 
                 — 
               
               
                 17 
                 6.43 
                 s 
               
               
                 18 
                 — 
               
               
                 19 
                 7.30 
                 s 
               
               
                 20 
                 — 
               
               
                 21 
                 2.66 
                 s 
               
               
                 22 
                 1.18 
                 s 
               
               
                 23 
                 0.87 
                 m 
               
               
                 24 
                 3.81 
                 m 
               
               
                 24 
                 3.74 
                 m 
               
               
                 25 
                 0.87 
                 m 
               
               
                 26 
                 1.13 
                 s 
               
               
                 27 
                 SSP 
               
               
                   
               
               
                 *SSP: no observed due to solvent suppression. 
               
            
           
         
       
     
     Accordingly, the compositions and methods of the present invention are useful in producing known compounds that are microtubule-stabilizing agents as well as new compounds comprising epothilone analogs such as 24-hydroxyl-epothilone B (Formula A) and pharmaceutically acceptable salts thereof expected to be useful as microtubule-stabilizing agents. The microtubule stabilizing agents produced using these compositions and methods are useful in the treatment of a variety of cancers and other proliferative diseases including, but not limited to, the following;
         carcinoma, including that of the bladder, breast, colon, kidney, liver, lung, ovary, pancreas, stomach, cervix, thyroid and skin; including squamous cell carcinoma;   hematopoietic tumors of lymphoid lineage, including leukemia, acute lymphocytic leukemia, acute lymphoblastic leukemia, B-cell lymphoma, T-cell lymphoma, Hodgkins lymphoma, non-Hodgkins lymphoma, hairy cell lymphoma and Burketts lymphoma;   hematopoietic tumors of myeloid lineage, including acute and chronic myelogenous leukemias and promyelocytic leukemia;   tumors of mesenchymal origin, including fibrosarcoma and rhabdomyoscarcoma;   other tumors, including melanoma, seminoma, tetratocarcinoma, neuroblastoma and glioma;   tumors of the central and peripheral nervous system, including astrocytoma, neuroblastoma, glioma, and schwannomas;   tumors of mesenchymal origin, including fibrosarcoma, rhabdomyosarcoma, and osteosarcoma; and   other tumors, including melanoma, xenoderma pigmentosum, keratoactanthoma, seminoma, thyroid follicular cancer and teratocarcinoma.       

     Microtubule stabilizing agents produced using the compositions and methods of the present invention will also inhibit angiogenesis, thereby affecting the growth of tumors and providing treatment of tumors and tumor-related disorders. Such anti-angiogenesis properties of these compounds will also be useful in the treatment of other conditions responsive to anti-angiogenesis agents including, but not limited to, certain forms of blindness related to retinal vascularization, arthritis, especially inflammatory arthritis, multiple sclerosis, restinosis and psoriasis. 
     Microtubule stabilizing agents produced using the compositions and methods of the present invention will induce or inhibit apoptosis, a physiological cell death process critical for normal development and homeostasis. Alterations of apoptotic pathways contribute to the pathogenesis of a variety of human diseases. Compounds of the present invention such as those set forth in formula I and II and Formula A, as modulators of apoptosis, will be useful in the treatment of a variety of human diseases with aberrations in apoptosis including, but not limited to, cancer and precancerous lesions, immune response related diseases, viral infections, degenerative diseases of the musculoskeletal system and kidney disease. 
     Without wishing to be bound to any mechanism or morphology, microtubule stabilizing agents produced using the compositions and methods of the present invention may also be used to treat conditions other than cancer or other proliferative diseases. Such conditions include, but are not limited to viral infections such as herpesvirus, poxvirus, Epstein-Barr virus, Sindbis virus and adenovirus; autoimmune diseases such as systemic lupus erythematosus, immune mediated glomerulonephritis, rheumatoid arthritis, psoriasis, inflammatory bowel diseases and autoimmune diabetes mellitus; neurodegenerative disorders such as Alzheimer&#39;s disease, AIDS-related dementia, Parkinson&#39;s disease, amyotrophic lateral sclerosis, retinitis pigmentosa, spinal muscular atrophy and cerebellar degeneration; AIDS; myelodysplastic syndromes; aplastic anemia; ischemic injury associated myocardial infarctions; stroke and reperfusion injury; restenosis; arrhythmia; atherosclerosis; toxin-induced or alcohol induced liver diseases; hematological diseases such as chronic anemia and aplastic anemia; degenerative diseases of the musculoskeletal system such as osteoporosis and arthritis; aspirin-sensitive rhinosinusitis; cystic fibrosis; multiple sclerosis; kidney diseases; and cancer pain. 
     The following nonlimiting examples are provided to further illustrate the present invention. 
     EXAMPLES 
     Example 1 
     Reagents 
     R2 Medium was prepared as follows: 
     A solution containing sucrose (103 grams), K 2 SO 4  (0.25 grams) MgCl 2 .6H 2 O (10.12 grams), glucose (10 grams), Difco Casaminoacids (0.1 grams) and distilled water (800 ml) was prepared. Eighty ml of this solution was then poured into a 200 ml screw capped bottle containing 2.2 grams Difco Bacto agar. The bottle was capped and autoclaved. At time of use, the medium was remelted and the following autoclaved solutions were added in the order listed: 
     1 ml KH 2 PO 4  (0.5%) 
     8 ml CaCl 2 .2H 2 O (3.68%) 
     1.5 ml L-proline (20%) 
     10 ml TES buffer (5.73%, adjusted to pH 7.2) 
     0.2 ml Trace element solution containing ZnCl 2  (40 mg), FeCl 3 .6H 2 O (200 mg), CuCl 2 .2H 2 O (10 mg), MnCl 2 .4H 2 O (10 mg), Na 2 B 4 O 7 .10H 2 O (10 mg), and (NH 4 ) 6 Mo 7 O 24 .H 2 O 
     0.5 ml NaOH (1N)(sterilization not required) 
     0.5 ml Required growth factors for auxotrophs (Histidine (50 μg/ml); Cysteine (37 μg/ml); adenine, guanine, thymidine and uracil (7.5 μg/ml); and Vitamins (0.5 μg/ml). 
     R2YE medium was prepared in the same fashion as R2 medium. However, 5 ml of Difco yeast extract (10%) was added to each 100 ml flask at time of use. 
     P (protoplast) buffer was prepared as follows: 
     A basal solution made up of the following was prepared: 
     Sucrose (103 grams) 
     K 2 SO 4  (0.25 grams) 
     MgCl 2 .6H 2 O (2.02 grams) 
     Trace Element Solution as described for R2 medium (2 ml) 
     Distilled water to 800 ml 
     Eighty ml aliquots of the basal solution were then dispensed and autoclaved. Before use, the following was added to each flask in the order listed: 
     1 ml KH 2 PO 4  (0.5%) 
     10 ml CaCl 2 .2H 2 O (3.68%) 
     TES buffer (5.75%, adjusted to pH 7.2) 
     T (transformation) buffer was prepared by mixing the following sterile solutions: 
     25 ml Sucrose (10.3%) 
     75 ml distilled water 
     1 ml Trace Element Solution as described for R2 medium 
     1 ml K 2 SO 4  (2.5%) 
     The following are then added to 9.3 mls of this solution: 
     0.2 ml CaCl 2  (5M) 
     0.5 ml Tris maleic acid buffer prepared from 1 M solution of Tris adjusted to pH 8.0 by adding maleic acid. 
     For use, 3 parts by volume of the above solution are added to 1 part by weight of PEG 1000, previously sterilized by autoclaving. 
     L (lysis) buffer was prepared by mixing the following sterile solutions: 
     100 ml Sucrose (10.3%) 
     10 ml TES buffer (5.73%, adjusted to pH 7.2) 
     1 ml K 2 SO 4  (2.5%) 
     1 ml Trace Element Solution as described for R2 medium 
     1 ml KH 2 PO 4  (0.5%) 
     0.1 ml MgCl 2 .6H 2 O (2.5 M) 
     1 ml CaCl 2  (0.25 M) 
     CRM Medium 
     A solution containing the following components was prepared in 1 liter of dH 2 O: glucose (10 grams), sucrose (103 grams), MgCl 2 .6H 2 O (10.12 grams), BBL™ trypticase soy broth (15 grams) (Becton Dickinson Microbiology Systems, Sparks, Md., USA), and BBL™ yeast extract (5 grams) (Becton Dickinson Microbiology Systems). The solution was autoclaved for 30 minutes. Thiostrepton was added to a concentration of 10 μg/ml for cultures propagated with plasmids. 
     Electroporation Buffer 
     A solution containing 30% (wt/vol) PEG 1000, 10% glycerol, and 6.5% sucrose was prepared in dH 2 O. The solution was sterilized by vacuum filtration through a 0.22 μm cellulose acetate filter. 
     Example 2 
     Extraction of Chromosomal DNA from Strain SC15847 
     Genomic DNA was isolated from an  Amycolatopsis orientalis  soil isolate strain designation SC15847 (ATCC PT-1043) using a guanidine-detergent lysis method, DNAzol reagent (Invitrogen, Carlsbad, Calif., USA). The SC15847 culture was grown 24 hours at 28° C. in F7 medium (glucose 2.2%, yeast extract 1.0%, malt extract 1.0%, peptone 0.1%, pH 7.0). Twenty ml of culture was harvested by centrifugation and resuspended in 20 ml of DNAzol, mixed by pipetting and centrifuged 10 minutes in the Beckman TJ6 centrifuge. Ten ml of 100% ethanol was added, inverted several times and stored at room temperature 3 minutes. The DNA was spooled on a glass pipette washed in 100% ethanol and allowed to air dry 10 minutes. The pellet was resuspended in 500 μl of 8 mM NaOH and once dissolved it was neutralized with 30 μl of 1M HEPES pH7.2. 
     Example 3 
     PCR Reactions 
     PCR reactions were prepared in a volume of 50 μl, containing 200–500 ng of genomic DNA or 1.0 μl of the cDNA, a forward and reverse primer, and the forward primer being either P450-1 +  (SEQ ID NO:23) or P450-1a +  (SEQ ID NO:24) or P450-2 +  (SEQ ID NO:25) and the reverse primer P450-3 −  (SEQ ID NO:27) or P450-2 −  (SEQ ID NO:26). All primers were added to a final concentration of 1.4–2.0 μM. The PCR reaction was prepared with 1 μl of Taq enzyme (2.5 units) (Stratagene), 5 μl of Taq buffer and 4 μl of 2.5 mM of dNTPs with dH 2 O to 50 μl. The cycling reactions were performed on a Geneamp® PCR system with the following protocol: 95° C. for 5 minutes, 5 cycles [95° C. 30 seconds, 37° C. 15 seconds (30% ramp), 72° C. 30 seconds], 35 cycles (94° C. 30 seconds, 65° C. 15 seconds, 72° C. 30 seconds), 72° C. 7 minutes. The expected sizes for the reactions are 340 bp for the P450-1 +  (SEQ ID NO:23) or P450-1a +  (SEQ ID NO:24) and P450-3 −  (SEQ ID NO:27) primer pairs, 240 bp for the P450-1 +  (SEQ ID NO:23) and P450-2 −  (SEQ ID NO:26) primer pairs and 130 bp for the P450-2 +  (SEQ ID NO:25) and P450-3 −  (SEQ ID NO:27) primer pairs. 
     Example 4 
     Cloning of Epothilone B Hydroxylase and Ferredoxin Genes 
     Twenty μg of SC15847 genomic DNA was digested with BglII restriction enzyme for 6 hours at 37° C. A 30k nanosep column (Gelman Sciences, Ann Arbor, Mich., USA) was used to concentrate the DNA and remove the enzyme and buffer. The reactions were concentrated to 40 μl and washed with 200 μl of TE. The digestion products were then separated a 0.7% agarose gel and genomic DNA in the range of 12˜15 kb was excised from the gel and purified using the Qiagen gel extraction method. The genomic DNA was then ligated to plasmid pWB19N (U.S. Pat. No. 5,516,679), which had been digested with BamHI and dephosphorylated using the SAP I enzyme (Roche Molecular Biochemicals, Indianapolis, Ind., catalog#1 758 250). Ligation reactions were performed in a 15 μl volume with 1 U of T4 DNA ligase (Invitrogen) for 1 hour at room temperature. One μl of the ligation was transformed to 100 μl of chemically competent DH10B cells (Invitrogen) and 100 μl plated to five LB agar plates with 30 μg/ml of neomycin, 37° C. overnight. 
     Five nylon membrane circles (Roche Molecular Biochemicals, Indianapolis, Ind.) were numbered and marked for orientation. The membranes were placed on the plates 2 minutes and then allowed to dry for 5 minutes. The membranes were then placed on Whatman filter disks saturated with 10% SDS for 5 minutes, 0.5N NaOH with 1.5 M NaCl for 5 minutes, 1.5 M NaCl with 1.0 M Tris pH 8.0 for 5 minutes, and 15 minutes on 2×SSC. The filters were hybridized as described previously for the Southern hybridization. Hybridizing colonies were picked to 2 ml of TB with 30 μg/ml neomycin and grown overnight at 37° C. Plasmid DNA was isolated using a miniprep column procedure (Mo Bio). This plasmid was named NPB29-1. 
     Example 5 
     DNA Sequencing and Analysis 
     The cloned PCR products were sequenced using fluorescent-dye-labeled terminator cycle sequencing, Big-Dye sequencing kit (Applied Biosystems, Foster city, Calif., USA) and were analyzed using laser-induced fluorescence capillary electrophoresis, ABI Prism 310 sequencer (Applied Biosystems). 
     Example 6 
     Extraction of Total RNA 
     Total RNA was isolated from the SC15847 culture using a modification of the Chomczynski and Sacchi method with a mono-phasic solution of phenol and guanidine isothiocyanate, Trizol reagent (Invitrogen). Five ml of an SC15847 frozen stock culture was thawed and used to inoculate 100 ml of F7 media in a 500 ml Erlenmeyer flask. The culture was grown in a shaker incubator at 230 rpm, 30° C. for 20 hours to an optical density at 600 nm (OD 600 ) of 9.0. The culture was placed in a 16° C. shaker incubator at 230 rpm for 20 minutes. Fifty-five milligrams of epothilone B was dissolved in 1 ml of 100% ethanol and added to the culture. A second ml of ethanol was used to rinse the residual epothilone B from the tube and added to the culture. The culture was incubated at 16° C., 230 rpm for 30 hours. Thirty ml of the culture was transferred to a 50 ml tube, 150 mg of lysozyme was added to the culture and the culture was incubated 5 minutes at room temperature. Ten ml of the culture was placed in a 50 ml Falcon tube and centrifuged 5 minutes, 4° C. in a TJ6 centrifuge. Two ml of chloroform was added and the tube was mixed vigorously for 15 seconds. The tube was incubated 2 minutes at room temperature and centrifuged 10 minutes, top speed in the TJ6 centrifuge. The aqueous layer was transferred to a fresh tube and 2.5 ml of isopropanol was added to precipitate the RNA. The tube was incubated 10 minutes at room temperature and centrifuged 10 minutes, 4° C. The supernatant was removed, the pellet was rinsed with 70% ethanol and dried briefly under vacuum. The pellet was resuspended in 150 μl of RNase-free dH 2 O. Fifty μl of 7.5M LiCl was added to the RNA and incubated at −20° C. for 30 minutes. The RNA was pelleted by centrifugation 10 minutes, 4° C. in a microcentrifuge. The pellet was rinsed with 200 μl of 70% ethanol, dried briefly under vacuum and resuspended in 150 μl of RNase free dH 2 O. 
     The RNA was treated with DNaseI (Ambion, Austin, Tex., USA). Twenty-five μl of total RNA (5.3 μg/μl), 2.5 μl of DNaseI buffer, 1.0 μl of DNase I added and incubated at 37° C. for 25 minutes. Five μl of DNase I inactivation buffer added, incubated 2 minutes, centrifuged 1 minute, the supernatant was transferred to a fresh tube. 
     Example 7 
     cDNA Synthesis 
     cDNA was synthesized from the total RNA using the Superscript II enzyme (Invitrogen). The reaction was prepared with 1 μl of total RNA (5.3 μg/μl), 9 μl of dH 2 O, 1 μl of dNTP mix (10 mM), and 1 μl of random hexamers. The reaction was incubated at 65° C. for 5 minutes then placed on ice. The following components were then added: 4 μl of 1 st  strand buffer, 1 μl of RNase Inhibitor, 2.0 μl of 0.1 M DTT, and 1 μl of Superscript II enzyme. The reaction was incubated at room temperature 10 minutes, 42° C. for 50 minutes and 70° C. for 15 minutes. One μl of RNaseH was added and incubated 20 minutes at 37° C., 15 minutes at 70° C. and stored at 4° C. 
     Example 8 
     DNA Labeling 
     The PCR conditions used to amplify the P450 specific products from genomic DNA and cDNA were used to amplify the insert of plasmid pCRscript-29. Plasmid pCRscript-29 contains a 340 bp PCR fragment amplified from SC15847 genomic DNA using primers P450 1 +  (SEQ ID NO:23) and P450 3 −  (SEQ ID NO:27). Two μl of the plasmid prep was used as a template, with a total of 25 cycles. The amplified product was gel purified using the Qiaquick gel extraction system (Qiagen). The extracted DNA was ethanol precipitated and resuspended in 5 μl of TE, the yield was estimated to be 500 ng. This fragment was labeled with digoxigenin using the chem link labeling reagent (Roche Molecular Biochemicals, Indianapolis, Ind. catalog #1 836 463). Five μl of the PCR product was mixed with 0.5 μl of Dig-chem link and dH 2 O added to 20 μl. The reaction was incubated 30 minutes at 85° C. and 5 μl of stop solution added. The probe concentration was estimated at 20 ng/μl. 
     Example 9 
     Southern DNA Hybridization 
     Ten μl of genomic DNA (0.5 μg/l) was digested with BamHI, BglII, EcoRI, HindIII or NotI and separated at 12 volts for 16 hours. The gel was depurinated 10 minutes in 0.25 N HCl and transferred by vacuum to a nylon membrane (Roche Molecular Biochemicals) in 0.4 N NaOH 5″ Hg, 90 minutes using a vacuum blotter (Bio-Rad Laboratories, Inc. Hercules, Calif., USA catalog # 165-5000). The membrane was rinsed in 1 M ammonium acetate and UV-crosslinked using the Stratalinker UV Crosslinker (Stratagene). The membrane was rinsed in 2×SSC and stored at room temperature. 
     The membrane was prehybridized 1 hour at 42° C. in 20 ml of Dig Easy Hyb buffer (Roche Molecular Biochemicals). The probe was denatured 10 minutes at 65° C. and then placed on ice. Five ml of probe in Dig-Easy Hyb at an approximate concentration on 20 ng/ml was incubated with the membrane at 42° C. overnight. The membrane was washed 2 times in 2×SCC with 0.1% SDS at room temperature, then 2 times in 0.5×SSC with 0.1% SDS at 65° C. The membrane was equilibrated in Genius buffer 1 (10 mM maleic acid, 15 mM NaCl; pH 7.5; 0.3% v/v Tween 20) (Roche Molecular Biochemicals, Indianapolis, Ind.) for 2 minutes, then incubated with 2% blocking solution (2% Blocking reagent in Genius Buffer 1)(Roche Molecular Biochemicals Indianapolis, Ind.) for 1 hour at room temperature. The membrane was incubated with a 1:20,000 dilution of anti-dig antibody in 50 ml of blocking solution for 30 minutes. The membrane was washed 2 times, 15 minutes each in 50 ml of Genius buffer 1. The membrane was equilibrated for two minutes in Genius Buffer 3 (10 mM Tris-HCl, 10 mM NaCl; pH 9.5). One ml of a 1:100 dilution of CSPD (disodium 3-(4-methoxyspiro{1,2-dioxetane-3,2′-(5′-chloro)tricyclo[3.3.1.1 3,7 ]decan}-4-yl)phenyl phosphate) (Roche Molecular Biochemicals) in Genius buffer 3 was added to the membrane and incubated 5 minutes at room temperature, then placed at 37° C. for 15 minutes. The membrane was exposed to Biomax ML film (Kodak, Rochester, N.Y., USA) for 1 hour. 
     Example 10 
       E. coli  Transformation 
     Competent cells were purchased from Invitrogen.  E. coli  strain DH10B was used as a host for genomic cloning. The chemically competent cells were thawed on ice and 100 μl aliquoted to a 17×100-mm polypropylene tube on ice. One μl of the ligation mixture was added to the cells and incubated on ice for 30 minutes. The cells were incubated at 42° C. for 45 seconds, then placed on ice 1–2 minutes. 0.9 ml pf SOC. medium (Invitrogen) was added and the cells were incubated one hour at 30–37° C. at 200–240 rpm. Cells were plated on a selective medium (Luria agar with neomycin or ampicillin at a concentration of 30 μg/ml or 100 μg/ml respectively). 
     Example 11 
     Transformation of  Streptomyces lividans  TK24 
     Plasmid pWB19N849 was constructed by digesting plasmid pWB19N with HindIII and treating with SAP I and digesting plasmid pANT849 (Keiser, et al., 2000, Practical  Streptomyces  Genetics, John Innes) with HindIII. The two linearized fragments were ligated 1 hour at room temperature with 1 U of T4 DNA ligase. One μl of the ligation reaction was used to transform XL-1 Blue electrocompetent cells (Stratagene). The recovered cells were plated to LB neomycin (30 μg/ml) overnight at 37° C. Colonies were picked to 2 ml of LB with 30 μg/ml neomycin and incubated overnight at 30° C. MoBio plasmid minipreps were performed on all cultures. Plasmids constructed from the ligation of pWB19N and pANT849 were determined by electrophoretic mobility on 0.7% agarose. The plasmid pWB19N849 was digested with HindIII and BglII to excise a 5.3 kb fragment equivalent to plasmid pANT849 digested with BglII and HindIII. This 5.3 kb fragment was purified on an agarose gel and extracted using the Qiaquick gel extraction system. 
     A 1.469 kb DNA fragment containing the epothilone B hydroxylase gene and the downstream ferredoxin gene was amplified using PCR. The 50 μl PCR reaction was composed of 5 μl of Taq buffer, 2.5 μl glycerol, 1 μl of 20 ng/μl NPB29-1 plasmid, 0.4 μl of 25 mM dNTPs, 1.0 μl each of primers NPB29-6F (SEQ ID NO:28) and NPB29-7R (SEQ ID NO:29) (5 pmole/μl), 38.1 μl of dH 2 O and 0.5 μl of Taq enzyme (Stratagene). The reactions were performed on a Perkin Elmer 9700, 95° C. for 5 minutes, then 30 cycles (96° C. for 30 seconds, 60° C. 30 seconds, 72° C. for 2 minutes), and 72° C. for 7 minutes. The PCR product was purified using a Qiagen minielute column with the PCR cleanup procedure. The purified product was digested with BglII and HindIII and purified on a 0.7% agarose gel. A 1.469 kb band was excised from the gel and eluted using a Qiagen minielute column. Five μl of this PCR product was ligated with 2 μl of the BglII, HindIII digested pANT849 vector in a 10 μl ligation reaction. The reaction was incubated at room temperature for 24 hours and then transformed to  S. lividans  TK24 protoplasts. 
     Twenty ml of YEME media was inoculated with a frozen spore suspension of  S. lividans  TK24 and grown 48 hours in a 125 ml bi-indent flask. Protoplasts were prepared as described in Practical  Streptomyces  Genetics. The ligation reaction was mixed with protoplasts, then 500 μl of transformation buffer was added, followed immediately by 5 ml of P buffer. The transformation reactions were spun down 7 minutes at 2,750 rpm, resuspended in 100 μl of P buffer and plated to one R2YE plate. The plate was incubated at 28° C. for 20 hours then overlaid with 5 ml of LB 0.7% agar with 250 μg/ml thiostrepton. After 7 days colonies were picked to an R2YE grid plate with 50 μg/ml of thiostrepton. The colonies were grown an additional 5 days at 28° C., then stored at 4° C. 
     This recombinant microorganism has been deposited with the ATCC and designated PTA-4022. 
     Example 12 
     Transformation of  Streptomyces rimosus    
     The procedure of Pigac and Schrempf Appl. Environ Microb., Vol. 61, No. 1, 352–356 (1995) was used to transform  S. rimosus. S. rimosus  strain R6 593 was cultivated in 20 ml of CRM medium at 30° C. on a rotary shaker (250 rpm). The cells were harvested at 24 hrs by centrifugation for 5 minutes, 5,000 rpm, 4° C., and resuspended in 20 ml of 10% sucrose, 4° C., and centrifuged for 5 minutes, 5,000 rpm, 4° C. The pellet was resuspended in 10 ml of 15% glycerol, 4° C. and centrifuged for 5 minutes, 5,000 rpm, 4° C. The pellet was resuspended in 2 ml of 15% glycerol, 4° C. with 100 μg/ml lysozyme and incubated at 37° C. for 30 minutes, centrifuged for 5 minutes, 5,000 rpm, 4° C. and resuspended in 2 ml of 15% glycerol, 4° C. The 15% glycerol wash was repeated once and the pellet was resuspended in 1 to 2 ml of Electroporation Buffer. The cells were stored at −80° C. in 50–200 μl aliquots. 
     The ligations were prepared as described for the  S. lividans  transformation. After the incubation of the ligation reaction, the volume was brought to 100 μl with dH 2 O, NaCl was added to 0.3M, and the reaction extracted with an equal volume of 24:1:1 phenol:choroform isoamyl alcohol. Twenty μg of glycogen was added and the ligated DNA was precipitated with 2 volumes of 100% ethanol at −20° C. for 30 minutes. The DNA was pelleted 10 minutes in a microcentrifuge, washed once with 70% ethanol, dried 5 minutes in a speed-vac concentrator and resuspended in 5 μl of dH 2 O. 
     One frozen aliquot of cells was thawed at room temperature and divided, 50 μl/tube for each DNA sample for electroporation. The cells were stored on ice until use. DNA in 1 to 2 μl of dH 2 O was added and mixed. The cell and DNA mixture was transferred to a 2 mm gapped electrocuvette (Bio-Rad Laboratories, Richmond Calif. USA) that was pre-chilled on ice. The cells were electroporated at a setting of 2 kV (10 kV/cm), 25 μF, 400 Ω using a Gene Pulser™ (Bio-Rad Laboratories). The cells were diluted with 0.75 to 1.0 ml of CRM (0–4° C.), transferred to 15 ml culture tubes and incubated with agitation 3 hrs at 30° C. The cells were plated on trypticase soy broth agar plates with 10–30 μg/ml of thiostrepton. 
     Example 13 
     High Performance Liquid Chromatography 
     The liquid chromatography separation was performed using a Waters 2690 Separation Module system (Waters Corp., Milford, Mass., USA) and a column, 4.6×150 mm, filled with SymmetryShield RP 8 , particle size 3.5 μm (Waters Corp., Milford, Mass., USA). The gradient mobile phase programming was used with a flow rate of 1.0 ml/minute. Eluent A was water/acetonitrile (20:1)+10 mM ammonium acetate. Eluent B was acetonitrile/water (20:1). The mobile phase was a linear gradient from 12% B to 28% B over 6 minutes and held isocratic at 28% B over 4 minutes. This was followed by a 28% B to 100% B linear gradient over 20 minutes and a linear gradient to 12% B over two minutes with a 3 minute hold at 12% B. 
     Example 14 
     Mass Spectrometry 
     The column effluent was introduced directly into the electrospray ion source of a ZMD mass spectrometer (Micromass, Manchester, UK). The instrument was calibrated-using Test Juice reference standard (Waters Corp, Milford, Mass., USA) and was delivered at a flow of 10 μl/minute from a syringe pump (Harvard Apparatus, Holliston, Mass., USA). The mass spectrometer was operated at a low mass resolution of 13.2 and a high mass resolution of 11.2. Spectra were acquired from using a scan range of m/z 100 to 600 at an acquisition rate of 10 spectra/second. The ionization technique employed was positive electrospray (ES). The sprayer voltage was kept at 2900 V and the cone voltage of the ion source was kept at a potential of 17 V. 
     Example 15 
     Use of the ebh Gene Sequence (SEQ ID NO:1) to Isolate Cytochrome P450 Genes from Other Microorganisms 
     Genomic DNA was isolated from a set of cultures (ATCC43491, ATCC14930, ATCC53630, ATCC53550, ATCC39444, ATCC43333, ATCC35165) using the DNAzol reagent. The DNA was used as a template for PCR reactions using primers designed to the sequence of the ebh gene. Three sets of primers were used for amplification; NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29), NPB29-16f (SEQ ID NO:50) and NPB29-17r (SEQ ID NO:51), and NPB29-19f (SEQ ID NO:52) and NPB29-20r (SEQ ID NO:53). 
     PCR reactions were prepared in a volume of 20 μl, containing 200–500 ng of genomic DNA and a forward and reverse primer. All primers were added to a final concentration of 1.4–2.0 μM. The PCR reaction was prepared with 0.2 μl of Advantage™ 2 Taq enzyme (BD Biosciences Clontech, Palo Alto, Calif., USA), 2 μl of Advantage™ 2 Taq buffer and 0.2 μl of 2.5 mM of dNTPs with dH 2 O to 20 μl. The cycling reactions were performed on a Geneamp® 9700 PCR system or a Mastercycler® gradient (Eppendorf, Westbury, N.Y., USA) with the following protocol: 95° C. for 5 minutes, 35 cycles (96° C. 20 seconds, 54–69° C. 30 seconds, 72° C. 2 minutes), 72° C. for 7 minutes. The expected size of the PCR products is approximately 1469 bp for the NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29) primer pair, 1034 bp for the NPB29-16f (SEQ ID NO:50) and NPB29-17r (SEQ ID NO:51) primer pair and 1318 bp for the NPB29-19f (SEQ ID NO:52) and NPB29-20r (SEQ ID NO:53) primer pair. The PCR reactions were analyzed on 0.7% agarose gels. PCR products of the expected size were excised from the gel and purified using the Qiagen gel extraction method. The purified products were sequenced using the Big-Dye sequencing kit and analyzed using an AB1310 sequencer. 
     Example 16 
     Construction of Plasmid pPCRscript-ebh 
     A 1.469 kb DNA fragment containing the epothilone B hydroxylase gene and the downstream ferredoxin gene was amplified using PCR. The 50 μl PCR reaction was composed of 5 μl of Taq buffer, 2.5 μl glycerol, 1 μl of 20 ng/μl NPB29-1 plasmid, 0.4 μl of 25 mM dNTPs, 1.0 μl each of primers NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29) (5 pmole/μl), 38.1 μl of dH 2 O and 0.5 μl of Taq enzyme (Stratagene). The reactions were performed on a Geneamp® 9700 PCR system, with the following conditions; 95° C. for 5 minutes, then 30 cycles (96° C. for 30 seconds, 60° C. 30 seconds, 72° C. for 2 minutes), and 72° C. for 7 minutes. The PCR product was purified using a Qiagen Qiaquick column with the PCR cleanup procedure. The purified product was digested with BglII and HindIII and purified on a 0.7% agarose gel. A 1.469 kb band was excised from the gel and eluted using a Qiagen Qiaquick gel extraction procedure. The fragments were then cloned into the pPCRscript Amp vector using the PCRscript Amp cloning kit. Colonies containing inserts were picked to 1–2 ml of LB (Luria Broth) with 100 μg/ml ampicillin, 30–37° C., 16–24 hours, 230–300 rpm. Plasmid isolation was performed using the Mo Bio miniplasmid prep kit. The sequence of the insert was confirmed by cycle sequencing with the Big-Dye sequencing kit. This plasmid was named pPCRscript-ebh. 
     Example 17 
     Mutagenesis of the ebh Gene for Improved Yield or Altered Specificity 
     The Quikchange® XL Site-Directed Mutagenesis Kit and the Quikchange® Multi Site-Directed Mutagenesis kit, both from Stratagene were used to introduce mutations in the coding region of the ebh gene. Both of these methods employ DNA primers 35–45 bases in length containing the desired mutation (SEQ ID NO:54–59 and 70), a methylated circular plasmid template and PfuTurbo® DNA Polymerase (U.S. Pat. Nos. 5,545,552 and 5,866,395 and 5,948,663) to generate copies of the plasmid template incorporating the mutation carried on the mutagenic primers. Subsequent digestion of the reaction with the restriction endonuclease enzyme DpnI, selectively digests the methylated plasmid template, but leaves the non-methylated mutated plasmid intact. The manufacturer&#39;s instructions were followed for all procedures with the exception of the DpnI digestion step in which the incubation time was increased from 1 hr to 3 hrs. The pPCRscript-ebh vector was used as the template for mutagenesis. 
     One to two μl of the reaction was transformed to either XL1-Blue® electrocompetent or XL10-Gold® ultracompetent cells (Stratagene). Cells were plated to a density of greater than 100 colonies per plate on LA (Luria Agar) 100 μg/ml ampicillin plates, and incubated 24–48 hrs at 30–37° C. The entire plate was resuspended in 5 ml of LB containing 100 μg/ml ampicillin. Plasmid was isolated directly from the resuspended cells by centrifuging the cells and then purifying the plasmid using the Mo Bio miniprep procedure. This plasmid was then used as a template for PCR with primers NPB29-6f (SEQ ID NO:28) and NPB29-7r (SEQ ID NO:29) to amplify a mutated expression cassette. Digestion of the 1.469 kb PCR product with the restriction enzymes BglII and HindIII was used to prepare this fragment for ligation to vector pANT849 also digested with BglII and HindIII. Alternatively, the resuspended cells were used to inoculate 20–50 ml of LB containing 100 μg/ml ampicillin and grown 18–24 hrs at 30–37° C. Qiagen midi-preps were performed on the cultures to isolate plasmid DNA containing the desired mutation. Digestion with the restriction enzymes BglII and HindIII was used to excise the mutated expression cassette for ligation to BglII and HindIII digested plasmid pANT849. Screening of mutants was performed in  S. lividans  or  S. rimosus  as described. 
     Alternatively, the method of Leung et al., Technique— A Journal of Methods in Cell and Molecular Biology , Vol. 1, No. 1, 11–15 (1989) was used to generate random mutation libraries of the ebh gene. Manganese and/or reduced dATP concentration is used to control the mutagenesis frequency of the Taq polymerase. The plasmid pCRscript-ebh was digested with NotI to linearize the plasmid. The Polymerase buffer was prepared with 0.166 M (NH 4 ) 2 SO 4 , 0.67M Tris-HCl pH 8.8, 61 mM MgCl 2 , 67 μM EDTA pH8.0, 1.7 mg/ml Bovine Serum Albumin). The PCR reaction was prepared with 10 μl of Not I digested pCRscript-ebh (0.1 ng/μl), 10 μl of polymerase buffer, 1.0 μl of 1M β-mercaptoethanol, 10.0 μl of DMSO, 1.0 μl of NPB29-6f (SEQ ID NO:28) primer (100 pmole/μl), 1.0 μl of NPB29-7r (SEQ ID NO:29) primer (100 pmole/μl), 10 μl of 5 mM MnCl 2 , 10.0 μl 10 mM dGTP, 10.0 μl 2 mM dATP, 10 mM dTTp, 10.0 μl Taq polymerase. dH 2 O was added to 100 μl. Reactions were also prepared as described above but without MnCl 2 . The cycling reactions were performed a GeneAmp® PCR system with the following protocol: 95° C. for 1 minute, 55° C. for 30 seconds, 72° C. for 4 minutes), 72° C. for 7 minutes. The PCR reactions were separated on an agarose gel using a Qiagen spin column. The fragments were then digested with BglII and HindIII and purified using a Qiagen spin column. The purified fragments were then ligated to BglII and HindIII digested pANT849 plasmids. Screening of mutants was performed in  S. lividans  and  S. rimousus . 
     
       
         
           
               
            
               
                   
               
               
                 Table of Characterized Mutants 
               
            
           
           
               
               
               
               
               
            
               
                   
                 Mutant 
                 Position 
                 Substitution 
                 Wild-type 
               
               
                   
                   
               
            
           
           
               
               
               
               
               
            
               
                   
                 ebh24-16 
                 92 
                 Valine 
                 Isoleucine 
               
               
                   
                   
                 237 
                 Alanine 
                 Phenylalanine 
               
               
                   
                 ebh25-1 
                 195 
                 Serine 
                 Asparagine 
               
               
                   
                   
                 294 
                 Proline 
                 Serine 
               
               
                   
                 ebh10-53 
                 190 
                 Tyrosine 
                 Phenylalanine 
               
               
                   
                   
                 231 
                 Arginine 
                 Glutamic acid 
               
               
                   
                 ebh24-16d8 
                 92 
                 Valine 
                 Isoleucine 
               
               
                   
                   
                 237 
                 Alanine 
                 Phenylalanine 
               
               
                   
                   
                 67 
                 Glutamine 
                 Arginine 
               
               
                   
                 ebh24-16c11 
                 92 
                 Valine 
                 Isoleucine 
               
               
                   
                   
                 93 
                 Glycine 
                 Alanine 
               
               
                   
                   
                 237 
                 Alanine 
                 Phenylalanine 
               
               
                   
                   
                 365 
                 Threonine 
                 Isoleucine 
               
               
                   
                 ebh24-16-16 
                 92 
                 Valine 
                 Isoleucine 
               
               
                   
                   
                 106 
                 Alanine 
                 Valine 
               
               
                   
                   
                 237 
                 Alanine 
                 Phenylalanine 
               
               
                   
                 ebh24-16-74 
                 88 
                 Histidine 
                 Arginine 
               
               
                   
                   
                 92 
                 Valine 
                 Isoleucine 
               
               
                   
                   
                 237 
                 Alanine 
                 Phenylalanine 
               
               
                   
                 ebh-M18 
                 31 
                 Lysine 
                 Glutamic acid 
               
               
                   
                   
                 176 
                 Valine 
                 Methionine 
               
               
                   
                 ebh24-16g8 
                 92 
                 Valine 
                 Isoleucine 
               
               
                   
                   
                 237 
                 Alanine 
                 Phenylalanine 
               
               
                   
                   
                 67 
                 Glutamine 
                 Arginine 
               
               
                   
                   
                 130 
                 Threonine 
                 Isoleucine 
               
               
                   
                   
                 176 
                 Alanine 
                 Methionine 
               
               
                   
                 ebh24-16b9 
                 92 
                 Valine 
                 Isoleucine 
               
               
                   
                   
                 237 
                 Alanine 
                 Phenylalanine 
               
               
                   
                   
                 67 
                 Glutamine 
                 Arginine 
               
               
                   
                   
                 140 
                 Threonine 
                 Alanine 
               
               
                   
                   
                 176 
                 Serine 
                 Methionine 
               
               
                   
                   
               
            
           
         
       
     
     Example 18 
     Comparison of Epothilone B Transformation in Cells Expressing ebh and Mutants Thereof 
     In these experiments, twenty ml of YEME medium in a 125 ml bi-indented flask was inoculated with 200 μl of a frozen spore preparation of  S. lividans  TK24 , S. lividans  (pANT849-ebh),  S. lividans  (pANT849-ebh10-53) or  S. lividans  (pANT849-ebh24-16) and incubated 48 hours at 230 rpm, 30° C. Thiostrepton, 10 μg/ml was added to media inoculated with  S. lividans  (pANT849-ebh),  S. lividans  (pANT849-ebh10-53) and  S. lividans  (pANT849-ebh24-16). Four ml of culture was transferred to 20 ml of R5 medium in a 125 ml Erlenmeyer flask and incubated 18 hrs at 230 rpm, 30° C. Epothilone B in 100% EtOH was added to each culture to a final concentration of 0.05% weight/volume. Samples were taken at 0, 24, 48 and 72 hours with the exception of the  S. lividans  (pANT849-ebh24-16) culture, in which the epothilone B had been completely converted to epothilone F at 48 hours. The samples were analyzed by HPLC. Results were calculated as a percentage of the epothilone B at time 0 hours. 
     Epothilone B: 
                                                             pANT849-       Time (hours)   TK24   pANT849-ebh   pANT849-ebh10-53   ebh24-16                                                    0   100%   100%   100%   100%       24    99%    78%    69%    56%       48    87%    19%    39%    0%       72    87%    0%    3%   —                    
Epothilone F:
 
     
       
         
           
               
               
               
               
               
             
               
                   
               
               
                   
                   
                   
                   
                 pANT849- 
               
               
                 Time (hours) 
                 TK24 
                 pANT849-ebh 
                 pANT849-ebh10-53 
                 ebh24-16 
               
               
                   
               
             
            
               
                 0 
                 0% 
                  0% 
                  0% 
                  0% 
               
               
                 24 
                 0% 
                  4% 
                  9% 
                 23% 
               
               
                 48 
                 0% 
                 21% 
                 29% 
                 52% 
               
               
                 72 
                 0% 
                 14% 
                 41% 
                 — 
               
               
                   
               
            
           
         
       
     
     Alternatively, the bioconversion of epothilone B to epothilone F was performed in  S. rimosus  host cells transformed with expression plasmids containing the ebh gene and its variants or mutants. One-hundred μl of a frozen  S. rimosus  transformant culture was inoculated to 20 ml CRM media with 10 μg/ml thiostrepton 10 and cultivated 16–24 hr, 30° C., 230–300 rpm. Epothilone B in 100% ethanol was added to each culture to a final concentration of 0.05% weight/volume. The reaction was typically incubated 20–40 hrs at 30° C., 230–300 rpm. The concentration of epothilones B and F was determined by HPLC analysis. 
     Evaluation of Mutants in  S. rimosus   
     
       
         
           
               
               
               
             
               
                   
                   
               
               
                   
                 Mutant 
                 Epothilone F yield 
               
               
                   
                   
               
             
            
               
                   
                 ebh-M18 
                 55% 
               
               
                   
                 ebh24-16d8 
                 75% 
               
               
                   
                 ebh24-16c11 
                 75% 
               
               
                   
                 ebh24-16-16 
                 75% 
               
               
                   
                 ebh24-16-74 
                 75% 
               
               
                   
                 ebh24-16b9 
                 80% 
               
               
                   
                 ebh24-16g8 
                 85% 
               
               
                   
                   
               
            
           
         
       
     
     Example 19 
     Biotransformation of Compactin to Pravastatin 
     Twenty ml of R2YE media with 10 μg/ml thiostrepton in a 125 ml flask was inoculated with 200 μl of a frozen spore preparation of  S. lividans  (pANT849),  S. lividans  (pANT849-ebh) and incubated 72 hours at 230 rpm, 28° C. Four ml of culture was inoculated to 20 ml of R2YE media and grown 24 hours at 230 rpm, 28° C. One ml of culture was transferred to a 15 ml polypropylene culture tube, 10 μl of compactin (40 mg/ml) was added to each culture and incubated for 24 hours, 28° C., 250 rpm. Five hundred μl of the culture broth was transferred to a fresh 15 ml polypropylene culture tube. Five hundred μl of 50 mM sodium hydroxide was added and vortexed. Three ml of methanol was added and vortexed, the tube was centrifuged 10 minutes at 3000 rpm in a TJ-6 table-top centrifuge. The organic phase was analyzed by HPLC. Compactin and pravastatin values were assessed relative to the control  S. lividans  (pANT849) culture. 
     Compactin and Pravastatin as a Percentage of Starting Compactin Concentration: 
     
       
         
           
               
               
               
             
               
                   
                   
               
               
                   
                   S. lividans  (pANT849) 
                   S. lividans  (pANT849-ebh) 
               
               
                   
                   
               
             
            
               
                   
               
            
           
           
               
               
               
            
               
                 Compactin 
                 36% 
                 11% 
               
               
                 Pravastatin 
                 11% 
                 53% 
               
               
                   
               
            
           
         
       
     
     Example 20 
     High Performance Liquid Chromatography Method for Compactin and Pravastatin Detection 
     The liquid chromatography separation was performed using a Hewlett Packard1090 Series Separation system (Agilent Technologies, Palo Alto, Calif., USA) and a column, 50×46 mm, filled with Spherisorb ODS2, particle size 5 μM (Keystone Scientific, Inc, Bellefonte, Pa., USA). The gradient mobile phase programming was used with a flow rate of 2.0 ml/minute. Eluent A was water, 10 mM ammonium acetate and 0.05% Phosphoric Acid. Eluent B was acetonitrile. The mobile phase was a linear gradient from 20% B to 90% B over 4 minutes. 
     Example 21 
     Structure Determination of the Biotransformation Product of Mutant ebh25-1 
     Analytical HPLC was performed using a Hewlett Packard 1100 Series Liquid Chromatograph with a YMC Packed ODS-AQ column, 4.6 mm i.d.×15 cm 1. A gradient system of water (solvent A) and acetonitrile (solvent B) was used: 20% to 90% B linear gradient, 10 minutes; 90% to 20% linear gradient, 2 minutes. The flow rate was 1 ml/minute and UV detection was at 254 nm. 
     Preparative HPLC was performed using the following equipment and conditions:
     Pump: Varian ProStar Solvent Delivery Module (Varian Inc., Palo Alto, Calif., USA). Detector: Gynkotek UVD340S.   Column: YMC ODS-A column (30 mmID×100 mm length, 5μ particle size).   Elution flow rate: 30 ml/minute   Elution gradient: (solvent A: water; solvent B: acetonitrile), 20% B, 2 minutes; 20% to 60% B linear gradient, 18 minutes; 60% B, 2 minutes; 60% to 90% B linear gradient, 1 minute; 90% B, 3 minutes; 90% to 20% B linear gradient, 2 minutes.   Detection: UV, 210 nm.   

     LC/NMR was performed as follows: 40 μl of sample was injected onto a YMC Packed ODS-AQ column (4.6 mm i.d.×15 cm 1). The column was eluted at 1 ml/minute flow rate with a gradient system of D 2 O (solvent A) and acetonitrile-d 3  (solvent B): 30% B, 1 minute; 30% to 80% B linear gradient, 11 minutes. The eluent passed a UV detection cell (monitored at 254 nm) before flowing through a F19/H 1 NMR probe (60 μl active volume) in Varian AS-600 NMR spectrometer. The biotransformation product was eluted at around 7.5 minutes and the flow was stopped manually to allow the eluent to remain in the NMR probe for NMR data acquisition. 
     Isolation and analysis was performed as follows. The butanol/methanol extract (about 10 ml) was evaporated to dryness under nitrogen stream. One ml methanol was added to the residue (38 mg) and insoluble material was removed by centrifugation (13000 rpm, 2 min). 0.1 ml of the supernatant was used for LC/NMR study and the rest of 0.9 ml was subjected to the preparative HPLC (0.2–0.4 ml per injection). Two major peaks were observed and collected: peak A was eluted between 14 and 15 minutes, while peak B was eluted between 16.5 and 17.5 minutes. Analytical HPLC analysis indicated that peak B was the parent compound, epothilone B (Rt 8.5 minutes), and peak A was the biotransformation product (Rt 7.3 minutes). The peak A fractions were pooled and MS analysis data was obtained with the pooled fractions. The pooled fraction was evaporated to a small volume, then was lyophilized to give 3 mg of white solid. NMR and HPLC analysis of the white solid (dissolved in methanol) revealed that the biotransformation product was partially decomposed during the drying process. 
     
       
         
           
               
               
               
               
               
               
             
               
                 APPENDIX 1 
               
               
                   
               
               
                 Atom No. 
                 Residue 
                 Atom Name 
                 X-coord 
                 Y-coord 
                 Z-coord 
               
               
                   
               
             
            
               
                   
               
            
           
           
               
               
               
               
               
               
            
               
                 1 
                 ALA9 
                 N 
                 −39.918 
                 −4.913 
                 −1.651 
               
               
                 2 
                 ALA9 
                 CA 
                 −38.454 
                 −5.033 
                 −1.537 
               
               
                 3 
                 ALA9 
                 C 
                 −37.953 
                 −4.886 
                 −0.099 
               
               
                 4 
                 ALA9 
                 O 
                 −38.625 
                 −4.31 
                 0.765 
               
               
                 5 
                 ALA9 
                 CB 
                 −37.809 
                 −3.967 
                 −2.415 
               
               
                 6 
                 THR10 
                 N 
                 −36.781 
                 −5.447 
                 0.146 
               
               
                 7 
                 THR10 
                 CA 
                 −36.187 
                 −5.437 
                 1.49 
               
               
                 8 
                 THR10 
                 C 
                 −34.916 
                 −4.585 
                 1.553 
               
               
                 9 
                 THR10 
                 O 
                 −34.016 
                 −4.735 
                 0.72 
               
               
                 10 
                 THR10 
                 CB 
                 −35.871 
                 −6.887 
                 1.846 
               
               
                 11 
                 THR10 
                 OG1 
                 −37.075 
                 −7.631 
                 1.717 
               
               
                 12 
                 THR10 
                 CG2 
                 −35.355 
                 −7.053 
                 3.271 
               
               
                 13 
                 LEU11 
                 N 
                 −34.858 
                 −3.699 
                 2.536 
               
               
                 14 
                 LEU11 
                 CA 
                 −33.669 
                 −2.853 
                 2.745 
               
               
                 15 
                 LEU11 
                 C 
                 −32.511 
                 −3.649 
                 3.353 
               
               
                 16 
                 LEU11 
                 O 
                 −32.706 
                 −4.468 
                 4.259 
               
               
                 17 
                 LEU11 
                 CB 
                 −34.033 
                 −1.707 
                 3.687 
               
               
                 18 
                 LEU11 
                 CG 
                 −35.079 
                 −0.78 
                 3.078 
               
               
                 19 
                 LEU11 
                 CD1 
                 −35.53 
                 0.265 
                 4.091 
               
               
                 20 
                 LEU11 
                 CD2 
                 −34.555 
                 −0.111 
                 1.81 
               
               
                 21 
                 PRO12 
                 N 
                 −31.32 
                 −3.422 
                 2.823 
               
               
                 22 
                 PRO12 
                 CA 
                 −30.121 
                 −4.119 
                 3.302 
               
               
                 23 
                 PRO12 
                 C 
                 −29.652 
                 −3.606 
                 4.663 
               
               
                 24 
                 PRO12 
                 O 
                 −29.656 
                 −2.397 
                 4.918 
               
               
                 25 
                 PRO12 
                 CB 
                 −29.081 
                 −3.842 
                 2.259 
               
               
                 26 
                 PRO12 
                 CG 
                 −29.597 
                 −2.771 
                 1.309 
               
               
                 27 
                 PRO12 
                 CD 
                 −31.031 
                 −2.493 
                 1.729 
               
               
                 28 
                 LEU13 
                 N 
                 −29.278 
                 −4.522 
                 5.54 
               
               
                 29 
                 LEU13 
                 CA 
                 −28.676 
                 −4.118 
                 6.819 
               
               
                 30 
                 LEU13 
                 C 
                 −27.183 
                 −3.88 
                 6.627 
               
               
                 31 
                 LEU13 
                 O 
                 −26.449 
                 −4.806 
                 6.267 
               
               
                 32 
                 LEU13 
                 CB 
                 −28.898 
                 −5.196 
                 7.872 
               
               
                 33 
                 LEU13 
                 CG 
                 −30.374 
                 −5.354 
                 8.217 
               
               
                 34 
                 LEU13 
                 CD1 
                 −30.587 
                 −6.516 
                 9.181 
               
               
                 35 
                 LEU13 
                 CD2 
                 −30.945 
                 −4.067 
                 8.802 
               
               
                 36 
                 ALA14 
                 N 
                 −26.72 
                 −2.741 
                 7.112 
               
               
                 37 
                 ALA14 
                 CA 
                 −25.355 
                 −2.266 
                 6.825 
               
               
                 38 
                 ALA14 
                 C 
                 −24.244 
                 −2.941 
                 7.634 
               
               
                 39 
                 ALA14 
                 O 
                 −23.058 
                 −2.719 
                 7.372 
               
               
                 40 
                 ALA14 
                 CB 
                 −25.311 
                 −0.764 
                 7.075 
               
               
                 41 
                 ARG15 
                 N 
                 −24.628 
                 −3.792 
                 8.569 
               
               
                 42 
                 ARG15 
                 CA 
                 −23.664 
                 −4.537 
                 9.379 
               
               
                 43 
                 ARG15 
                 C 
                 −23.478 
                 −5.983 
                 8.91 
               
               
                 44 
                 ARG15 
                 O 
                 −22.815 
                 −6.767 
                 9.599 
               
               
                 45 
                 ARG15 
                 CB 
                 −24.174 
                 −4.519 
                 10.81 
               
               
                 46 
                 ARG15 
                 CG 
                 −25.655 
                 −4.879 
                 10.84 
               
               
                 47 
                 ARG15 
                 CD 
                 −26.2 
                 −4.843 
                 12.26 
               
               
                 48 
                 ARG15 
                 NE 
                 −27.657 
                 −5.039 
                 12.256 
               
               
                 49 
                 ARG15 
                 CZ 
                 −28.358 
                 −5.301 
                 13.36 
               
               
                 50 
                 ARG15 
                 NH1 
                 −29.69 
                 −5.376 
                 13.3 
               
               
                 51 
                 ARG15 
                 NH2 
                 −27.735 
                 −5.412 
                 14.536 
               
               
                 52 
                 LYS16 
                 N 
                 −24.096 
                 −6.351 
                 7.798 
               
               
                 53 
                 LYS16 
                 CA 
                 −24.016 
                 −7.741 
                 7.335 
               
               
                 54 
                 LYS16 
                 C 
                 −22.639 
                 −8.128 
                 6.807 
               
               
                 55 
                 LYS16 
                 O 
                 −21.959 
                 −7.359 
                 6.115 
               
               
                 56 
                 LYS16 
                 CB 
                 −25.061 
                 −7.977 
                 6.252 
               
               
                 57 
                 LYS16 
                 CG 
                 −26.466 
                 −7.985 
                 6.839 
               
               
                 58 
                 LYS16 
                 CD 
                 −26.605 
                 −9.079 
                 7.892 
               
               
                 59 
                 LYS16 
                 CE 
                 −28.002 
                 −9.092 
                 8.499 
               
               
                 60 
                 LYS16 
                 NZ 
                 −28.113 
                 −10.128 
                 9.537 
               
               
                 61 
                 CYS17 
                 N 
                 −22.317 
                 −9.392 
                 7.036 
               
               
                 62 
                 CYS17 
                 CA 
                 −21.061 
                 −10.004 
                 6.56 
               
               
                 63 
                 CYS17 
                 C 
                 −20.737 
                 −9.771 
                 5.066 
               
               
                 64 
                 CYS17 
                 O 
                 −19.662 
                 −9.205 
                 4.833 
               
               
                 65 
                 CYS17 
                 CB 
                 −21.096 
                 −11.501 
                 6.864 
               
               
                 66 
                 CYS17 
                 SG 
                 −21.33 
                 −11.937 
                 8.602 
               
               
                 67 
                 PRO18 
                 N 
                 −21.635 
                 −10.003 
                 4.1 
               
               
                 68 
                 PRO18 
                 CA 
                 −21.293 
                 −9.756 
                 2.683 
               
               
                 69 
                 PRO18 
                 C 
                 −21.123 
                 −8.291 
                 2.246 
               
               
                 70 
                 PRO18 
                 O 
                 −21.013 
                 −8.061 
                 1.036 
               
               
                 71 
                 PRO18 
                 CB 
                 −22.388 
                 −10.383 
                 1.878 
               
               
                 72 
                 PRO18 
                 CG 
                 −23.509 
                 −10.812 
                 2.802 
               
               
                 73 
                 PRO18 
                 CD 
                 −23.002 
                 −10.554 
                 4.207 
               
               
                 74 
                 PHE19 
                 N 
                 −21.137 
                 −7.33 
                 3.162 
               
               
                 75 
                 PHE19 
                 CA 
                 −20.792 
                 −5.947 
                 2.834 
               
               
                 76 
                 PHE19 
                 C 
                 −19.279 
                 −5.777 
                 2.788 
               
               
                 77 
                 PHE19 
                 O 
                 −18.789 
                 −4.92 
                 2.036 
               
               
                 78 
                 PHE19 
                 CB 
                 −21.36 
                 −5.007 
                 3.894 
               
               
                 79 
                 PHE19 
                 CG 
                 −22.8 
                 −4.568 
                 3.654 
               
               
                 80 
                 PHE19 
                 CD1 
                 −23.051 
                 −3.27 
                 3.232 
               
               
                 81 
                 PHE19 
                 CD2 
                 −23.856 
                 −5.444 
                 3.867 
               
               
                 82 
                 PHE19 
                 CE1 
                 −24.355 
                 −2.853 
                 3.003 
               
               
                 83 
                 PHE19 
                 CE2 
                 −25.159 
                 −5.03 
                 3.629 
               
               
                 84 
                 PHE19 
                 CZ 
                 −25.409 
                 −3.735 
                 3.197 
               
               
                 85 
                 SER20 
                 N 
                 −18.573 
                 −6.687 
                 3.449 
               
               
                 86 
                 SER20 
                 CA 
                 −17.102 
                 −6.717 
                 3.446 
               
               
                 87 
                 SER20 
                 C 
                 −16.569 
                 −7.839 
                 4.342 
               
               
                 88 
                 SER20 
                 O 
                 −16.632 
                 −7.723 
                 5.573 
               
               
                 89 
                 SER20 
                 CB 
                 −16.557 
                 −5.371 
                 3.929 
               
               
                 90 
                 SER20 
                 OG 
                 −17.236 
                 −5.019 
                 5.129 
               
               
                 91 
                 PRO21 
                 N 
                 −15.974 
                 −8.867 
                 3.753 
               
               
                 92 
                 PRO21 
                 CA 
                 −15.978 
                 −9.134 
                 2.304 
               
               
                 93 
                 PRO21 
                 C 
                 −17.267 
                 −9.836 
                 1.856 
               
               
                 94 
                 PRO21 
                 O 
                 −18.026 
                 −10.327 
                 2.702 
               
               
                 95 
                 PRO21 
                 CB 
                 −14.8 
                 −10.047 
                 2.111 
               
               
                 96 
                 PRO21 
                 CG 
                 −14.442 
                 −10.669 
                 3.455 
               
               
                 97 
                 PRO21 
                 CD 
                 −15.306 
                 −9.949 
                 4.481 
               
               
                 98 
                 PRO22 
                 N 
                 −17.551 
                 −9.859 
                 0.561 
               
               
                 99 
                 PRO22 
                 CA 
                 −16.897 
                 −9.007 
                 −0.445 
               
               
                 100 
                 PRO22 
                 C 
                 −17.4 
                 −7.575 
                 −0.296 
               
               
                 101 
                 PRO22 
                 O 
                 −18.341 
                 −7.371 
                 0.469 
               
               
                 102 
                 PRO22 
                 CB 
                 −17.32 
                 −9.591 
                 −1.762 
               
               
                 103 
                 PRO22 
                 CG 
                 −18.478 
                 −10.549 
                 −1.528 
               
               
                 104 
                 PRO22 
                 CD 
                 −18.669 
                 −10.604 
                 −0.021 
               
               
                 105 
                 PRO23 
                 N 
                 −16.687 
                 −6.605 
                 −0.842 
               
               
                 106 
                 PRO23 
                 CA 
                 −17.224 
                 −5.241 
                 −0.897 
               
               
                 107 
                 PRO23 
                 C 
                 −18.525 
                 −5.21 
                 −1.693 
               
               
                 108 
                 PRO23 
                 O 
                 −18.524 
                 −5.083 
                 −2.925 
               
               
                 109 
                 PRO23 
                 CB 
                 −16.159 
                 −4.417 
                 −1.547 
               
               
                 110 
                 PRO23 
                 CG 
                 −15.004 
                 −5.321 
                 −1.95 
               
               
                 111 
                 PRO23 
                 CD 
                 −15.388 
                 −6.725 
                 −1.509 
               
               
                 112 
                 GLU24 
                 N 
                 −19.62 
                 −5.122 
                 −0.956 
               
               
                 113 
                 GLU24 
                 CA 
                 −20.963 
                 −5.192 
                 −1.547 
               
               
                 114 
                 GLU24 
                 C 
                 −21.415 
                 −3.843 
                 −2.088 
               
               
                 115 
                 GLU24 
                 O 
                 −22.323 
                 −3.794 
                 −2.93 
               
               
                 116 
                 GLU24 
                 CB 
                 −21.934 
                 −5.68 
                 −0.48 
               
               
                 117 
                 GLU24 
                 CG 
                 −23.27 
                 −6.137 
                 −1.052 
               
               
                 118 
                 GLU24 
                 CD 
                 −23.982 
                 −7.017 
                 −0.024 
               
               
                 119 
                 GLU24 
                 OE1 
                 −24.613 
                 −7.981 
                 −0.433 
               
               
                 120 
                 GLU24 
                 OE2 
                 −23.833 
                 −6.745 
                 1.158 
               
               
                 121 
                 TYR25 
                 N 
                 −20.573 
                 −2.843 
                 −1.878 
               
               
                 122 
                 TYR25 
                 CA 
                 −20.842 
                 −1.47 
                 −2.303 
               
               
                 123 
                 TYR25 
                 C 
                 −20.704 
                 −1.311 
                 −3.816 
               
               
                 124 
                 TYR25 
                 O 
                 −21.364 
                 −0.436 
                 −4.385 
               
               
                 125 
                 TYR25 
                 CB 
                 −19.828 
                 −0.568 
                 −1.608 
               
               
                 126 
                 TYR25 
                 CG 
                 −19.616 
                 −0.882 
                 −0.128 
               
               
                 127 
                 TYR25 
                 CD1 
                 −20.662 
                 −0.753 
                 0.779 
               
               
                 128 
                 TYR25 
                 CD2 
                 −18.364 
                 −1.298 
                 0.311 
               
               
                 129 
                 TYR25 
                 CE1 
                 −20.461 
                 −1.062 
                 2.119 
               
               
                 130 
                 TYR25 
                 CE2 
                 −18.163 
                 −1.605 
                 1.65 
               
               
                 131 
                 TYR25 
                 CZ 
                 −19.213 
                 −1.492 
                 2.55 
               
               
                 132 
                 TYR25 
                 OH 
                 −19.026 
                 −1.859 
                 3.866 
               
               
                 133 
                 GLU26 
                 N 
                 −20.1 
                 −2.296 
                 −4.468 
               
               
                 134 
                 GLU26 
                 CA 
                 −20.009 
                 −2.293 
                 −5.928 
               
               
                 135 
                 GLU26 
                 C 
                 −21.404 
                 −2.483 
                 −6.52 
               
               
                 136 
                 GLU26 
                 O 
                 −21.92 
                 −1.572 
                 −7.177 
               
               
                 137 
                 GLU26 
                 CB 
                 −19.129 
                 −3.454 
                 −6.39 
               
               
                 138 
                 GLU26 
                 CG 
                 −17.813 
                 −3.593 
                 −5.628 
               
               
                 139 
                 GLU26 
                 CD 
                 −16.94 
                 −2.342 
                 −5.707 
               
               
                 140 
                 GLU26 
                 OE1 
                 −16.345 
                 −2.12 
                 −6.749 
               
               
                 141 
                 GLU26 
                 OE2 
                 −16.773 
                 −1.731 
                 −4.657 
               
               
                 142 
                 ARG27 
                 N 
                 −22.105 
                 −3.488 
                 −6.017 
               
               
                 143 
                 ARG27 
                 CA 
                 −23.437 
                 −3.805 
                 −6.538 
               
               
                 144 
                 ARG27 
                 C 
                 −24.504 
                 −2.909 
                 −5.921 
               
               
                 145 
                 ARG27 
                 O 
                 −25.496 
                 −2.591 
                 −6.59 
               
               
                 146 
                 ARG27 
                 CB 
                 −23.752 
                 −5.26 
                 −6.22 
               
               
                 147 
                 ARG27 
                 CG 
                 −22.7 
                 −6.189 
                 −6.812 
               
               
                 148 
                 ARG27 
                 CD 
                 −23.031 
                 −7.653 
                 −6.55 
               
               
                 149 
                 ARG27 
                 NE 
                 −23.146 
                 −7.926 
                 −5.108 
               
               
                 150 
                 ARG27 
                 CZ 
                 −22.251 
                 −8.648 
                 −4.428 
               
               
                 151 
                 ARG27 
                 NH1 
                 −21.16 
                 −9.11 
                 −5.043 
               
               
                 152 
                 ARG27 
                 NH2 
                 −22.428 
                 −8.879 
                 −3.126 
               
               
                 153 
                 LEU28 
                 N 
                 −24.197 
                 −2.331 
                 −4.771 
               
               
                 154 
                 LEU28 
                 CA 
                 −25.11 
                 −1.358 
                 −4.168 
               
               
                 155 
                 LEU28 
                 C 
                 −25.131 
                 −0.079 
                 −4.987 
               
               
                 156 
                 LEU28 
                 O 
                 −26.214 
                 0.286 
                 −5.45 
               
               
                 157 
                 LEU28 
                 CB 
                 −24.67 
                 −1.039 
                 −2.746 
               
               
                 158 
                 LEU28 
                 CG 
                 −24.868 
                 −2.224 
                 −1.81 
               
               
                 159 
                 LEU28 
                 CD1 
                 −24.303 
                 −1.916 
                 −0.43 
               
               
                 160 
                 LEU28 
                 CD2 
                 −26.34 
                 −2.609 
                 −1.716 
               
               
                 161 
                 ARG29 
                 N 
                 −23.969 
                 0.307 
                 −5.49 
               
               
                 162 
                 ARG29 
                 CA 
                 −23.835 
                 1.502 
                 −6.327 
               
               
                 163 
                 ARG29 
                 C 
                 −24.521 
                 1.334 
                 −7.677 
               
               
                 164 
                 ARG29 
                 O 
                 −25.271 
                 2.226 
                 −8.096 
               
               
                 165 
                 ARG29 
                 CB 
                 −22.345 
                 1.682 
                 −6.568 
               
               
                 166 
                 ARG29 
                 CG 
                 −21.997 
                 2.947 
                 −7.336 
               
               
                 167 
                 ARG29 
                 CD 
                 −20.519 
                 2.941 
                 −7.711 
               
               
                 168 
                 ARG29 
                 NE 
                 −19.696 
                 2.563 
                 −6.551 
               
               
                 169 
                 ARG29 
                 CZ 
                 −18.945 
                 1.459 
                 −6.523 
               
               
                 170 
                 ARG29 
                 NH1 
                 −18.872 
                 0.673 
                 −7.6 
               
               
                 171 
                 ARG29 
                 NH2 
                 −18.265 
                 1.145 
                 −5.421 
               
               
                 172 
                 ARG30 
                 N 
                 −24.494 
                 0.109 
                 −8.182 
               
               
                 173 
                 ARG30 
                 CA 
                 −25.112 
                 −0.208 
                 −9.475 
               
               
                 174 
                 ARG30 
                 C 
                 −26.629 
                 −0.386 
                 −9.407 
               
               
                 175 
                 ARG30 
                 O 
                 −27.282 
                 −0.429 
                 −10.455 
               
               
                 176 
                 ARG30 
                 CB 
                 −24.503 
                 −1.512 
                 −9.971 
               
               
                 177 
                 ARG30 
                 CG 
                 −22.992 
                 −1.401 
                 −10.1 
               
               
                 178 
                 ARG30 
                 CD 
                 −22.376 
                 −2.745 
                 −10.463 
               
               
                 179 
                 ARG30 
                 NE 
                 −20.909 
                 −2.659 
                 −10.479 
               
               
                 180 
                 ARG30 
                 CZ 
                 −20.12 
                 −3.648 
                 −10.054 
               
               
                 181 
                 ARG30 
                 NH1 
                 −20.658 
                 −4.772 
                 −9.576 
               
               
                 182 
                 ARG30 
                 NH2 
                 −18.793 
                 −3.508 
                 −10.099 
               
               
                 183 
                 GLU31 
                 N 
                 −27.194 
                 −0.493 
                 −8.215 
               
               
                 184 
                 GLU31 
                 CA 
                 −28.653 
                 −0.576 
                 −8.109 
               
               
                 185 
                 GLU31 
                 C 
                 −29.207 
                 0.713 
                 −7.51 
               
               
                 186 
                 GLU31 
                 O 
                 −30.393 
                 1.032 
                 −7.656 
               
               
                 187 
                 GLU31 
                 CB 
                 −29.025 
                 −1.746 
                 −7.203 
               
               
                 188 
                 GLU31 
                 CG 
                 −28.381 
                 −3.055 
                 −7.65 
               
               
                 189 
                 GLU31 
                 CD 
                 −28.814 
                 −3.443 
                 −9.061 
               
               
                 190 
                 GLU31 
                 OE1 
                 −30.013 
                 −3.448 
                 −9.301 
               
               
                 191 
                 GLU31 
                 OE2 
                 −27.961 
                 −3.944 
                 −9.782 
               
               
                 192 
                 SER32 
                 N 
                 −28.319 
                 1.439 
                 −6.855 
               
               
                 193 
                 SER32 
                 CA 
                 −28.652 
                 2.672 
                 −6.147 
               
               
                 194 
                 SER32 
                 C 
                 −27.386 
                 3.393 
                 −5.683 
               
               
                 195 
                 SER32 
                 O 
                 −26.706 
                 2.984 
                 −4.731 
               
               
                 196 
                 SER32 
                 CB 
                 −29.509 
                 2.309 
                 −4.939 
               
               
                 197 
                 SER32 
                 OG 
                 −28.842 
                 1.268 
                 −4.234 
               
               
                 198 
                 PRO33 
                 N 
                 −27.148 
                 4.543 
                 −6.292 
               
               
                 199 
                 PRO33 
                 CA 
                 −26.039 
                 5.408 
                 −5.869 
               
               
                 200 
                 PRO33 
                 C 
                 −26.227 
                 5.972 
                 −4.454 
               
               
                 201 
                 PRO33 
                 O 
                 −25.241 
                 6.254 
                 −3.758 
               
               
                 202 
                 PRO33 
                 CB 
                 −26.023 
                 6.511 
                 −6.879 
               
               
                 203 
                 PRO33 
                 CG 
                 −27.203 
                 6.364 
                 −7.829 
               
               
                 204 
                 PRO33 
                 CD 
                 −27.933 
                 5.107 
                 −7.394 
               
               
                 205 
                 VAL34 
                 N 
                 −27.478 
                 6.094 
                 −4.033 
               
               
                 206 
                 VAL34 
                 CA 
                 −27.83 
                 6.472 
                 −2.661 
               
               
                 207 
                 VAL34 
                 C 
                 −28.828 
                 5.447 
                 −2.122 
               
               
                 208 
                 VAL34 
                 O 
                 −30.01 
                 5.467 
                 −2.487 
               
               
                 209 
                 VAL34 
                 CB 
                 −28.483 
                 7.85 
                 −2.686 
               
               
                 210 
                 VAL34 
                 CG1 
                 −28.789 
                 8.339 
                 −1.275 
               
               
                 211 
                 VAL34 
                 CG2 
                 −27.616 
                 8.865 
                 −3.42 
               
               
                 212 
                 SER35 
                 N 
                 −28.344 
                 4.546 
                 −1.286 
               
               
                 213 
                 SER35 
                 CA 
                 −29.186 
                 3.438 
                 −0.802 
               
               
                 214 
                 SER35 
                 C 
                 −29.512 
                 3.536 
                 0.688 
               
               
                 215 
                 SER35 
                 O 
                 −28.615 
                 3.692 
                 1.521 
               
               
                 216 
                 SER35 
                 CB 
                 −28.456 
                 2.126 
                 −1.077 
               
               
                 217 
                 SER35 
                 OG 
                 −27.19 
                 2.169 
                 −0.43 
               
               
                 218 
                 ARG36 
                 N 
                 −30.785 
                 3.413 
                 1.025 
               
               
                 219 
                 ARG36 
                 CA 
                 −31.168 
                 3.431 
                 2.443 
               
               
                 220 
                 ARG36 
                 C 
                 −30.894 
                 2.072 
                 3.082 
               
               
                 221 
                 ARG36 
                 O 
                 −31.516 
                 1.059 
                 2.741 
               
               
                 222 
                 ARG36 
                 CB 
                 −32.645 
                 3.779 
                 2.597 
               
               
                 223 
                 ARG36 
                 CG 
                 −33.016 
                 3.857 
                 4.076 
               
               
                 224 
                 ARG36 
                 CD 
                 −34.513 
                 4.047 
                 4.295 
               
               
                 225 
                 ARG36 
                 NE 
                 −34.987 
                 5.35 
                 3.804 
               
               
                 226 
                 ARG36 
                 CZ 
                 −36.272 
                 5.582 
                 3.523 
               
               
                 227 
                 ARG36 
                 NH1 
                 −37.16 
                 4.59 
                 3.609 
               
               
                 228 
                 ARG36 
                 NH2 
                 −36.662 
                 6.791 
                 3.113 
               
               
                 229 
                 VAL37 
                 N 
                 −29.921 
                 2.067 
                 3.974 
               
               
                 230 
                 VAL37 
                 CA 
                 −29.543 
                 0.855 
                 4.695 
               
               
                 231 
                 VAL37 
                 C 
                 −29.982 
                 0.926 
                 6.152 
               
               
                 232 
                 VAL37 
                 O 
                 −30.313 
                 1.995 
                 6.684 
               
               
                 233 
                 VAL37 
                 CB 
                 −28.03 
                 0.681 
                 4.608 
               
               
                 234 
                 VAL37 
                 CG1 
                 −27.591 
                 0.391 
                 3.177 
               
               
                 235 
                 VAL37 
                 CG2 
                 −27.298 
                 1.898 
                 5.163 
               
               
                 236 
                 GLY38 
                 N 
                 −30.064 
                 −0.24 
                 6.761 
               
               
                 237 
                 GLY38 
                 CA 
                 −30.404 
                 −0.332 
                 8.18 
               
               
                 238 
                 GLY38 
                 C 
                 −29.151 
                 −0.563 
                 9.016 
               
               
                 239 
                 GLY38 
                 O 
                 −28.562 
                 −1.652 
                 9.003 
               
               
                 240 
                 LEU39 
                 N 
                 −28.764 
                 0.463 
                 9.75 
               
               
                 241 
                 LEU39 
                 CA 
                 −27.607 
                 0.399 
                 10.656 
               
               
                 242 
                 LEU39 
                 C 
                 −27.911 
                 −0.554 
                 11.817 
               
               
                 243 
                 LEU39 
                 O 
                 −29.028 
                 −1.085 
                 11.882 
               
               
                 244 
                 LEU39 
                 CB 
                 −27.353 
                 1.814 
                 11.187 
               
               
                 245 
                 LEU39 
                 CG 
                 −26.198 
                 2.546 
                 10.5 
               
               
                 246 
                 LEU39 
                 CD1 
                 −26.368 
                 2.665 
                 8.988 
               
               
                 247 
                 LEU39 
                 CD2 
                 −26.011 
                 3.925 
                 11.12 
               
               
                 248 
                 PRO40 
                 N 
                 −26.919 
                 −0.869 
                 12.643 
               
               
                 249 
                 PRO40 
                 CA 
                 −27.183 
                 −1.62 
                 13.875 
               
               
                 250 
                 PRO40 
                 C 
                 −28.423 
                 −1.116 
                 14.614 
               
               
                 251 
                 PRO40 
                 O 
                 −28.771 
                 0.073 
                 14.574 
               
               
                 252 
                 PRO40 
                 CB 
                 −25.933 
                 −1.51 
                 14.691 
               
               
                 253 
                 PRO40 
                 CG 
                 −24.84 
                 −0.886 
                 13.837 
               
               
                 254 
                 PRO40 
                 CD 
                 −25.497 
                 −0.52 
                 12.516 
               
               
                 255 
                 SER41 
                 N 
                 −29.188 
                 −2.109 
                 15.042 
               
               
                 256 
                 SER41 
                 CA 
                 −30.511 
                 −1.986 
                 15.686 
               
               
                 257 
                 SER41 
                 C 
                 −31.548 
                 −1.213 
                 14.856 
               
               
                 258 
                 SER41 
                 O 
                 −32.379 
                 −0.492 
                 15.419 
               
               
                 259 
                 SER41 
                 CB 
                 −30.387 
                 −1.382 
                 17.087 
               
               
                 260 
                 SER41 
                 OG 
                 −30.036 
                 −0.008 
                 17.001 
               
               
                 261 
                 GLY42 
                 N 
                 −31.474 
                 −1.34 
                 13.539 
               
               
                 262 
                 GLY42 
                 CA 
                 −32.521 
                 −0.831 
                 12.644 
               
               
                 263 
                 GLY42 
                 C 
                 −32.557 
                 0.686 
                 12.434 
               
               
                 264 
                 GLY42 
                 O 
                 −33.59 
                 1.208 
                 11.997 
               
               
                 265 
                 GLN43 
                 N 
                 −31.471 
                 1.392 
                 12.713 
               
               
                 266 
                 GLN43 
                 CA 
                 −31.501 
                 2.847 
                 12.494 
               
               
                 267 
                 GLN43 
                 C 
                 −31.201 
                 3.16 
                 11.025 
               
               
                 268 
                 GLN43 
                 O 
                 −30.079 
                 2.955 
                 10.551 
               
               
                 269 
                 GLN43 
                 CB 
                 −30.507 
                 3.53 
                 13.437 
               
               
                 270 
                 GLN43 
                 CG 
                 −30.681 
                 5.05 
                 13.439 
               
               
                 271 
                 GLN43 
                 CD 
                 −29.873 
                 5.699 
                 14.567 
               
               
                 272 
                 GLN43 
                 OE1 
                 −30.31 
                 6.682 
                 15.184 
               
               
                 273 
                 GLN43 
                 NE2 
                 −28.723 
                 5.116 
                 14.852 
               
               
                 274 
                 THR44 
                 N 
                 −32.227 
                 3.582 
                 10.304 
               
               
                 275 
                 THR44 
                 CA 
                 −32.096 
                 3.832 
                 8.859 
               
               
                 276 
                 THR44 
                 C 
                 −31.194 
                 5.02 
                 8.534 
               
               
                 277 
                 THR44 
                 O 
                 −31.231 
                 6.071 
                 9.187 
               
               
                 278 
                 THR44 
                 CB 
                 −33.475 
                 4.077 
                 8.258 
               
               
                 279 
                 THR44 
                 OG1 
                 −34.009 
                 5.268 
                 8.823 
               
               
                 280 
                 THR44 
                 CG2 
                 −34.428 
                 2.923 
                 8.551 
               
               
                 281 
                 ALA45 
                 N 
                 −30.35 
                 4.799 
                 7.541 
               
               
                 282 
                 ALA45 
                 CA 
                 −29.426 
                 5.833 
                 7.07 
               
               
                 283 
                 ALA45 
                 C 
                 −29.16 
                 5.718 
                 5.572 
               
               
                 284 
                 ALA45 
                 O 
                 −29.105 
                 4.619 
                 5.009 
               
               
                 285 
                 ALA45 
                 CB 
                 −28.115 
                 5.705 
                 7.836 
               
               
                 286 
                 TRP46 
                 N 
                 −28.989 
                 6.859 
                 4.931 
               
               
                 287 
                 TRP46 
                 CA 
                 −28.702 
                 6.865 
                 3.492 
               
               
                 288 
                 TRP46 
                 C 
                 −27.212 
                 6.698 
                 3.221 
               
               
                 289 
                 TRP46 
                 O 
                 −26.408 
                 7.589 
                 3.517 
               
               
                 290 
                 TRP46 
                 CB 
                 −29.185 
                 8.173 
                 2.881 
               
               
                 291 
                 TRP46 
                 CG 
                 −30.693 
                 8.309 
                 2.805 
               
               
                 292 
                 TRP46 
                 CD1 
                 −31.509 
                 9.009 
                 3.665 
               
               
                 293 
                 TRP46 
                 CD2 
                 −31.552 
                 7.723 
                 1.804 
               
               
                 294 
                 TRP46 
                 NE1 
                 −32.788 
                 8.894 
                 3.228 
               
               
                 295 
                 TRP46 
                 CE2 
                 −32.862 
                 8.146 
                 2.116 
               
               
                 296 
                 TRP46 
                 CE3 
                 −31.324 
                 6.922 
                 0.701 
               
               
                 297 
                 TRP46 
                 CZ2 
                 −33.913 
                 7.774 
                 1.295 
               
               
                 298 
                 TRP46 
                 CZ3 
                 −32.389 
                 6.538 
                 −0.105 
               
               
                 299 
                 TRP46 
                 CH2 
                 −33.68 
                 6.967 
                 0.19 
               
               
                 300 
                 ALA47 
                 N 
                 −26.863 
                 5.559 
                 2.652 
               
               
                 301 
                 ALA47 
                 CA 
                 −25.475 
                 5.257 
                 2.302 
               
               
                 302 
                 ALA47 
                 C 
                 −25.153 
                 5.708 
                 0.882 
               
               
                 303 
                 ALA47 
                 O 
                 −25.772 
                 5.272 
                 −0.1 
               
               
                 304 
                 ALA47 
                 CB 
                 −25.248 
                 3.756 
                 2.427 
               
               
                 305 
                 LEU48 
                 N 
                 −24.185 
                 6.602 
                 0.797 
               
               
                 306 
                 LEU48 
                 CA 
                 −23.751 
                 7.129 
                 −0.501 
               
               
                 307 
                 LEU48 
                 C 
                 −22.648 
                 6.252 
                 −1.067 
               
               
                 308 
                 LEU48 
                 O 
                 −21.546 
                 6.197 
                 −0.511 
               
               
                 309 
                 LEU48 
                 CB 
                 −23.222 
                 8.543 
                 −0.317 
               
               
                 310 
                 LEU48 
                 CG 
                 −24.27 
                 9.464 
                 0.289 
               
               
                 311 
                 LEU48 
                 CD1 
                 −23.707 
                 10.863 
                 0.454 
               
               
                 312 
                 LEU48 
                 CD2 
                 −25.524 
                 9.515 
                 −0.569 
               
               
                 313 
                 THR49 
                 N 
                 −22.948 
                 5.601 
                 −2.176 
               
               
                 314 
                 THR49 
                 CA 
                 −22.01 
                 4.636 
                 −2.75 
               
               
                 315 
                 THR49 
                 C 
                 −21.197 
                 5.214 
                 −3.907 
               
               
                 316 
                 THR49 
                 O 
                 −20.047 
                 4.803 
                 −4.09 
               
               
                 317 
                 THR49 
                 CB 
                 −22.774 
                 3.391 
                 −3.196 
               
               
                 318 
                 THR49 
                 OG1 
                 −23.783 
                 3.769 
                 −4.125 
               
               
                 319 
                 THR49 
                 CG2 
                 −23.458 
                 2.703 
                 −2.02 
               
               
                 320 
                 ARG50 
                 N 
                 −21.724 
                 6.2 
                 −4.616 
               
               
                 321 
                 ARG50 
                 CA 
                 −20.899 
                 6.838 
                 −5.655 
               
               
                 322 
                 ARG50 
                 C 
                 −20.007 
                 7.927 
                 −5.081 
               
               
                 323 
                 ARG50 
                 O 
                 −20.456 
                 8.712 
                 −4.234 
               
               
                 324 
                 ARG50 
                 CB 
                 −21.737 
                 7.467 
                 −6.758 
               
               
                 325 
                 ARG50 
                 CG 
                 −22.426 
                 6.441 
                 −7.639 
               
               
                 326 
                 ARG50 
                 CD 
                 −22.852 
                 7.085 
                 −8.951 
               
               
                 327 
                 ARG50 
                 NE 
                 −23.597 
                 8.327 
                 −8.704 
               
               
                 328 
                 ARG50 
                 CZ 
                 −23.779 
                 9.27 
                 −9.629 
               
               
                 329 
                 ARG50 
                 NH1 
                 −24.462 
                 10.375 
                 −9.326 
               
               
                 330 
                 ARG50 
                 NH2 
                 −23.274 
                 9.111 
                 −10.854 
               
               
                 331 
                 LEU51 
                 N 
                 −18.92 
                 8.175 
                 −5.797 
               
               
                 332 
                 LEU51 
                 CA 
                 −17.931 
                 9.19 
                 −5.399 
               
               
                 333 
                 LEU51 
                 C 
                 −18.52 
                 10.584 
                 −5.583 
               
               
                 334 
                 LEU51 
                 O 
                 −18.42 
                 11.426 
                 −4.682 
               
               
                 335 
                 LEU51 
                 CB 
                 −16.726 
                 9.066 
                 −6.33 
               
               
                 336 
                 LEU51 
                 CG 
                 −15.377 
                 9.193 
                 −5.621 
               
               
                 337 
                 LEU51 
                 CD1 
                 −14.233 
                 9.154 
                 −6.628 
               
               
                 338 
                 LEU51 
                 CD2 
                 −15.267 
                 10.433 
                 −4.746 
               
               
                 339 
                 GLU52 
                 N 
                 −19.404 
                 10.68 
                 −6.562 
               
               
                 340 
                 GLU52 
                 CA 
                 −20.088 
                 11.93 
                 −6.891 
               
               
                 341 
                 GLU52 
                 C 
                 −21.101 
                 12.314 
                 −5.811 
               
               
                 342 
                 GLU52 
                 O 
                 −21.114 
                 13.477 
                 −5.389 
               
               
                 343 
                 GLU52 
                 CB 
                 −20.821 
                 11.759 
                 −8.229 
               
               
                 344 
                 GLU52 
                 CG 
                 −19.897 
                 11.56 
                 −9.439 
               
               
                 345 
                 GLU52 
                 CD 
                 −19.749 
                 10.09 
                 −9.853 
               
               
                 346 
                 GLU52 
                 OE1 
                 −19.796 
                 9.24 
                 −8.971 
               
               
                 347 
                 GLU52 
                 OE2 
                 −19.502 
                 9.849 
                 −11.025 
               
               
                 348 
                 ASP53 
                 N 
                 −21.659 
                 11.313 
                 −5.146 
               
               
                 349 
                 ASP53 
                 CA 
                 −22.646 
                 11.572 
                 −4.096 
               
               
                 350 
                 ASP53 
                 C 
                 −21.953 
                 11.905 
                 −2.783 
               
               
                 351 
                 ASP53 
                 O 
                 −22.4 
                 12.804 
                 −2.063 
               
               
                 352 
                 ASP53 
                 CB 
                 −23.493 
                 10.322 
                 −3.876 
               
               
                 353 
                 ASP53 
                 CG 
                 −24.263 
                 9.94 
                 −5.133 
               
               
                 354 
                 ASP53 
                 OD1 
                 −24.319 
                 8.749 
                 −5.405 
               
               
                 355 
                 ASP53 
                 OD2 
                 −24.633 
                 10.838 
                 −5.878 
               
               
                 356 
                 ILE54 
                 N 
                 −20.75 
                 11.382 
                 −2.614 
               
               
                 357 
                 ILE54 
                 CA 
                 −19.991 
                 11.62 
                 −1.387 
               
               
                 358 
                 ILE54 
                 C 
                 −19.301 
                 12.976 
                 −1.41 
               
               
                 359 
                 ILE54 
                 O 
                 −19.36 
                 13.7 
                 −0.409 
               
               
                 360 
                 ILE54 
                 CB 
                 −18.963 
                 10.509 
                 −1.269 
               
               
                 361 
                 ILE54 
                 CG1 
                 −19.674 
                 9.167 
                 −1.252 
               
               
                 362 
                 ILE54 
                 CG2 
                 −18.113 
                 10.671 
                 −0.015 
               
               
                 363 
                 ILE54 
                 CD1 
                 −18.677 
                 8.03 
                 −1.365 
               
               
                 364 
                 ARG55 
                 N 
                 −18.916 
                 13.43 
                 −2.592 
               
               
                 365 
                 ARG55 
                 CA 
                 −18.346 
                 14.776 
                 −2.704 
               
               
                 366 
                 ARG55 
                 C 
                 −19.44 
                 15.836 
                 −2.679 
               
               
                 367 
                 ARG55 
                 O 
                 −19.252 
                 16.893 
                 −2.065 
               
               
                 368 
                 ARG55 
                 CB 
                 −17.551 
                 14.883 
                 −3.998 
               
               
                 369 
                 ARG55 
                 CG 
                 −16.293 
                 14.028 
                 −3.94 
               
               
                 370 
                 ARG55 
                 CD 
                 −15.498 
                 14.133 
                 −5.235 
               
               
                 371 
                 ARG55 
                 NE 
                 −16.277 
                 13.61 
                 −6.367 
               
               
                 372 
                 ARG55 
                 CZ 
                 −15.712 
                 13.028 
                 −7.427 
               
               
                 373 
                 ARG55 
                 NH1 
                 −14.383 
                 12.947 
                 −7.513 
               
               
                 374 
                 ARG55 
                 NH2 
                 −16.475 
                 12.553 
                 −8.413 
               
               
                 375 
                 GLU56 
                 N 
                 −20.64 
                 15.438 
                 −3.068 
               
               
                 376 
                 GLU56 
                 CA 
                 −21.795 
                 16.331 
                 −2.984 
               
               
                 377 
                 GLU56 
                 C 
                 −22.287 
                 16.444 
                 −1.539 
               
               
                 378 
                 GLU56 
                 O 
                 −22.628 
                 17.546 
                 −1.095 
               
               
                 379 
                 GLU56 
                 CB 
                 −22.875 
                 15.722 
                 −3.866 
               
               
                 380 
                 GLU56 
                 CG 
                 −24.103 
                 16.605 
                 −4.028 
               
               
                 381 
                 GLU56 
                 CD 
                 −25.112 
                 15.838 
                 −4.874 
               
               
                 382 
                 GLU56 
                 OE1 
                 −25.906 
                 16.463 
                 −5.56 
               
               
                 383 
                 GLU56 
                 OE2 
                 −25.055 
                 14.616 
                 −4.834 
               
               
                 384 
                 MET57 
                 N 
                 −22.065 
                 15.392 
                 −0.767 
               
               
                 385 
                 MET57 
                 CA 
                 −22.379 
                 15.386 
                 0.665 
               
               
                 386 
                 MET57 
                 C 
                 −21.4 
                 16.241 
                 1.459 
               
               
                 387 
                 MET57 
                 O 
                 −21.827 
                 17.091 
                 2.248 
               
               
                 388 
                 MET57 
                 CB 
                 −22.242 
                 13.948 
                 1.141 
               
               
                 389 
                 MET57 
                 CG 
                 −22.423 
                 13.805 
                 2.646 
               
               
                 390 
                 MET57 
                 SD 
                 −21.979 
                 12.184 
                 3.306 
               
               
                 391 
                 MET57 
                 CE 
                 −20.221 
                 12.196 
                 2.89 
               
               
                 392 
                 LEU58 
                 N 
                 −20.14 
                 16.197 
                 1.056 
               
               
                 393 
                 LEU58 
                 CA 
                 −19.089 
                 16.973 
                 1.726 
               
               
                 394 
                 LEU58 
                 C 
                 −19.07 
                 18.444 
                 1.307 
               
               
                 395 
                 LEU58 
                 O 
                 −18.398 
                 19.263 
                 1.946 
               
               
                 396 
                 LEU58 
                 CB 
                 −17.751 
                 16.327 
                 1.389 
               
               
                 397 
                 LEU58 
                 CG 
                 −17.638 
                 14.941 
                 2.013 
               
               
                 398 
                 LEU58 
                 CD1 
                 −16.504 
                 14.133 
                 1.394 
               
               
                 399 
                 LEU58 
                 CD2 
                 −17.49 
                 15.03 
                 3.528 
               
               
                 400 
                 SER59 
                 N 
                 −19.807 
                 18.776 
                 0.261 
               
               
                 401 
                 SER59 
                 CA 
                 −19.959 
                 20.171 
                 −0.144 
               
               
                 402 
                 SER59 
                 C 
                 −21.305 
                 20.739 
                 0.304 
               
               
                 403 
                 SER59 
                 O 
                 −21.531 
                 21.951 
                 0.204 
               
               
                 404 
                 SER59 
                 CB 
                 −19.852 
                 20.24 
                 −1.661 
               
               
                 405 
                 SER59 
                 OG 
                 −18.59 
                 19.697 
                 −2.022 
               
               
                 406 
                 SER60 
                 N 
                 −22.175 
                 19.879 
                 0.807 
               
               
                 407 
                 SER60 
                 CA 
                 −23.5 
                 20.318 
                 1.246 
               
               
                 408 
                 SER60 
                 C 
                 −23.505 
                 20.806 
                 2.685 
               
               
                 409 
                 SER60 
                 O 
                 −23.464 
                 19.996 
                 3.62 
               
               
                 410 
                 SER60 
                 CB 
                 −24.477 
                 19.156 
                 1.138 
               
               
                 411 
                 SER60 
                 OG 
                 −25.689 
                 19.581 
                 1.749 
               
               
                 412 
                 PRO61 
                 N 
                 −23.91 
                 22.058 
                 2.835 
               
               
                 413 
                 PRO61 
                 CA 
                 −24.023 
                 22.695 
                 4.154 
               
               
                 414 
                 PRO61 
                 C 
                 −25.231 
                 22.233 
                 4.983 
               
               
                 415 
                 PRO61 
                 O 
                 −25.41 
                 22.7 
                 6.113 
               
               
                 416 
                 PRO61 
                 CB 
                 −24.145 
                 24.157 
                 3.853 
               
               
                 417 
                 PRO61 
                 CG 
                 −24.401 
                 24.343 
                 2.364 
               
               
                 418 
                 PRO61 
                 CD 
                 −24.301 
                 22.959 
                 1.747 
               
               
                 419 
                 HIS62 
                 N 
                 −26.044 
                 21.333 
                 4.451 
               
               
                 420 
                 HIS62 
                 CA 
                 −27.21 
                 20.856 
                 5.18 
               
               
                 421 
                 HIS62 
                 C 
                 −26.949 
                 19.497 
                 5.813 
               
               
                 422 
                 HIS62 
                 O 
                 −27.863 
                 18.935 
                 6.427 
               
               
                 423 
                 HIS62 
                 CB 
                 −28.379 
                 20.764 
                 4.214 
               
               
                 424 
                 HIS62 
                 CG 
                 −28.703 
                 22.084 
                 3.55 
               
               
                 425 
                 HIS62 
                 ND1 
                 −28.955 
                 23.252 
                 4.171 
               
               
                 426 
                 HIS62 
                 CD2 
                 −28.796 
                 22.32 
                 2.198 
               
               
                 427 
                 HIS62 
                 CE1 
                 −29.197 
                 24.205 
                 3.248 
               
               
                 428 
                 HIS62 
                 NE2 
                 −29.098 
                 23.627 
                 2.029 
               
               
                 429 
                 PHE63 
                 N 
                 −25.765 
                 18.945 
                 5.596 
               
               
                 430 
                 PHE63 
                 CA 
                 −25.385 
                 17.693 
                 6.258 
               
               
                 431 
                 PHE63 
                 C 
                 −24.492 
                 17.977 
                 7.456 
               
               
                 432 
                 PHE63 
                 O 
                 −23.261 
                 17.885 
                 7.396 
               
               
                 433 
                 PHE63 
                 CB 
                 −24.686 
                 16.783 
                 5.262 
               
               
                 434 
                 PHE63 
                 CG 
                 −25.651 
                 16.13 
                 4.284 
               
               
                 435 
                 PHE63 
                 CD1 
                 −26.92 
                 15.76 
                 4.71 
               
               
                 436 
                 PHE63 
                 CD2 
                 −25.265 
                 15.901 
                 2.972 
               
               
                 437 
                 PHE63 
                 CE1 
                 −27.804 
                 15.161 
                 3.824 
               
               
                 438 
                 PHE63 
                 CE2 
                 −26.147 
                 15.298 
                 2.087 
               
               
                 439 
                 PHE63 
                 CZ 
                 −27.415 
                 14.928 
                 2.512 
               
               
                 440 
                 SER64 
                 N 
                 −25.159 
                 18.211 
                 8.569 
               
               
                 441 
                 SER64 
                 CA 
                 −24.502 
                 18.656 
                 9.795 
               
               
                 442 
                 SER64 
                 C 
                 −23.765 
                 17.525 
                 10.507 
               
               
                 443 
                 SER64 
                 O 
                 −24.07 
                 16.34 
                 10.339 
               
               
                 444 
                 SER64 
                 CB 
                 −25.587 
                 19.225 
                 10.7 
               
               
                 445 
                 SER64 
                 OG 
                 −24.96 
                 19.785 
                 11.84 
               
               
                 446 
                 SER65 
                 N 
                 −22.719 
                 17.898 
                 11.218 
               
               
                 447 
                 SER65 
                 CA 
                 −22.006 
                 16.938 
                 12.053 
               
               
                 448 
                 SER65 
                 C 
                 −22.463 
                 17.032 
                 13.513 
               
               
                 449 
                 SER65 
                 O 
                 −22.031 
                 16.247 
                 14.365 
               
               
                 450 
                 SER65 
                 CB 
                 −20.522 
                 17.234 
                 11.936 
               
               
                 451 
                 SER65 
                 OG 
                 −20.167 
                 17.174 
                 10.564 
               
               
                 452 
                 ASP66 
                 N 
                 −23.368 
                 17.961 
                 13.782 
               
               
                 453 
                 ASP66 
                 CA 
                 −23.901 
                 18.186 
                 15.122 
               
               
                 454 
                 ASP66 
                 C 
                 −25.388 
                 18.496 
                 14.919 
               
               
                 455 
                 ASP66 
                 O 
                 −25.978 
                 18.026 
                 13.938 
               
               
                 456 
                 ASP66 
                 CB 
                 −23.149 
                 19.393 
                 15.69 
               
               
                 457 
                 ASP66 
                 CG 
                 −22.904 
                 19.311 
                 17.192 
               
               
                 458 
                 ASP66 
                 OD1 
                 −21.835 
                 19.724 
                 17.618 
               
               
                 459 
                 ASP66 
                 OD2 
                 −23.871 
                 19.048 
                 17.899 
               
               
                 460 
                 ARG67 
                 N 
                 −25.972 
                 19.246 
                 15.842 
               
               
                 461 
                 ARG67 
                 CA 
                 −27.32 
                 19.831 
                 15.692 
               
               
                 462 
                 ARG67 
                 C 
                 −28.423 
                 18.78 
                 15.619 
               
               
                 463 
                 ARG67 
                 O 
                 −28.768 
                 18.296 
                 14.533 
               
               
                 464 
                 ARG67 
                 CB 
                 −27.384 
                 20.684 
                 14.423 
               
               
                 465 
                 ARG67 
                 CG 
                 −26.263 
                 21.716 
                 14.336 
               
               
                 466 
                 ARG67 
                 CD 
                 −26.329 
                 22.778 
                 15.428 
               
               
                 467 
                 ARG67 
                 NE 
                 −25.137 
                 23.64 
                 15.358 
               
               
                 468 
                 ARG67 
                 CZ 
                 −25.091 
                 24.799 
                 14.695 
               
               
                 469 
                 ARG67 
                 NH1 
                 −26.189 
                 25.28 
                 14.107 
               
               
                 470 
                 ARG67 
                 NH2 
                 −23.957 
                 25.503 
                 14.663 
               
               
                 471 
                 GLN68 
                 N 
                 −28.983 
                 18.45 
                 16.768 
               
               
                 472 
                 GLN68 
                 CA 
                 −30.127 
                 17.538 
                 16.79 
               
               
                 473 
                 GLN68 
                 C 
                 −31.414 
                 18.348 
                 16.65 
               
               
                 474 
                 GLN68 
                 O 
                 −31.728 
                 19.187 
                 17.503 
               
               
                 475 
                 GLN68 
                 CB 
                 −30.116 
                 16.757 
                 18.1 
               
               
                 476 
                 GLN68 
                 CG 
                 −31.207 
                 15.692 
                 18.12 
               
               
                 477 
                 GLN68 
                 CD 
                 −31.109 
                 14.852 
                 19.389 
               
               
                 478 
                 GLN68 
                 OE1 
                 −31.941 
                 14.973 
                 20.296 
               
               
                 479 
                 GLN68 
                 NE2 
                 −30.137 
                 13.955 
                 19.406 
               
               
                 480 
                 SER69 
                 N 
                 −32.129 
                 18.102 
                 15.565 
               
               
                 481 
                 SER69 
                 CA 
                 −33.37 
                 18.833 
                 15.272 
               
               
                 482 
                 SER69 
                 C 
                 −34.444 
                 18.558 
                 16.32 
               
               
                 483 
                 SER69 
                 O 
                 −34.447 
                 17.495 
                 16.958 
               
               
                 484 
                 SER69 
                 CB 
                 −33.885 
                 18.387 
                 13.91 
               
               
                 485 
                 SER69 
                 OG 
                 −34.261 
                 17.025 
                 14.033 
               
               
                 486 
                 PRO70 
                 N 
                 −35.332 
                 19.526 
                 16.499 
               
               
                 487 
                 PRO70 
                 CA 
                 −36.438 
                 19.385 
                 17.447 
               
               
                 488 
                 PRO70 
                 C 
                 −37.244 
                 18.122 
                 17.171 
               
               
                 489 
                 PRO70 
                 O 
                 −37.547 
                 17.795 
                 16.018 
               
               
                 490 
                 PRO70 
                 CB 
                 −37.267 
                 20.622 
                 17.291 
               
               
                 491 
                 PRO70 
                 CG 
                 −36.6 
                 21.547 
                 16.285 
               
               
                 492 
                 PRO70 
                 CD 
                 −35.348 
                 20.824 
                 15.815 
               
               
                 493 
                 SER71 
                 N 
                 −37.424 
                 17.369 
                 18.245 
               
               
                 494 
                 SER71 
                 CA 
                 −38.115 
                 16.065 
                 18.289 
               
               
                 495 
                 SER71 
                 C 
                 −37.589 
                 15.02 
                 17.298 
               
               
                 496 
                 SER71 
                 O 
                 −38.378 
                 14.228 
                 16.769 
               
               
                 497 
                 SER71 
                 CB 
                 −39.625 
                 16.244 
                 18.111 
               
               
                 498 
                 SER71 
                 OG 
                 −39.919 
                 16.638 
                 16.777 
               
               
                 499 
                 PHE72 
                 N 
                 −36.282 
                 14.985 
                 17.081 
               
               
                 500 
                 PHE72 
                 CA 
                 −35.679 
                 13.876 
                 16.321 
               
               
                 501 
                 PHE72 
                 C 
                 −34.364 
                 13.43 
                 16.957 
               
               
                 502 
                 PHE72 
                 O 
                 −33.281 
                 13.768 
                 16.458 
               
               
                 503 
                 PHE72 
                 CB 
                 −35.428 
                 14.283 
                 14.872 
               
               
                 504 
                 PHE72 
                 CG 
                 −36.682 
                 14.456 
                 14.018 
               
               
                 505 
                 PHE72 
                 CD1 
                 −37.097 
                 15.724 
                 13.63 
               
               
                 506 
                 PHE72 
                 CD2 
                 −37.402 
                 13.339 
                 13.617 
               
               
                 507 
                 PHE72 
                 CE1 
                 −38.238 
                 15.875 
                 12.853 
               
               
                 508 
                 PHE72 
                 CE2 
                 −38.544 
                 13.489 
                 12.84 
               
               
                 509 
                 PHE72 
                 CZ 
                 −38.962 
                 14.758 
                 12.459 
               
               
                 510 
                 PRO73 
                 N 
                 −34.469 
                 12.59 
                 17.979 
               
               
                 511 
                 PRO73 
                 CA 
                 −33.31 
                 12.19 
                 18.786 
               
               
                 512 
                 PRO73 
                 C 
                 −32.522 
                 11.027 
                 18.18 
               
               
                 513 
                 PRO73 
                 O 
                 −32.606 
                 9.895 
                 18.668 
               
               
                 514 
                 PRO73 
                 CB 
                 −33.898 
                 11.776 
                 20.099 
               
               
                 515 
                 PRO73 
                 CG 
                 −35.392 
                 11.555 
                 19.917 
               
               
                 516 
                 PRO73 
                 CD 
                 −35.708 
                 12.004 
                 18.5 
               
               
                 517 
                 LEU74 
                 N 
                 −31.772 
                 11.304 
                 17.127 
               
               
                 518 
                 LEU74 
                 CA 
                 −30.933 
                 10.263 
                 16.521 
               
               
                 519 
                 LEU74 
                 C 
                 −29.707 
                 9.976 
                 17.375 
               
               
                 520 
                 LEU74 
                 O 
                 −29.08 
                 10.892 
                 17.926 
               
               
                 521 
                 LEU74 
                 CB 
                 −30.474 
                 10.697 
                 15.135 
               
               
                 522 
                 LEU74 
                 CG 
                 −31.627 
                 10.794 
                 14.146 
               
               
                 523 
                 LEU74 
                 CD1 
                 −31.094 
                 11.194 
                 12.776 
               
               
                 524 
                 LEU74 
                 CD2 
                 −32.381 
                 9.471 
                 14.05 
               
               
                 525 
                 MET75 
                 N 
                 −29.359 
                 8.705 
                 17.454 
               
               
                 526 
                 MET75 
                 CA 
                 −28.167 
                 8.306 
                 18.208 
               
               
                 527 
                 MET75 
                 C 
                 −27.099 
                 7.808 
                 17.243 
               
               
                 528 
                 MET75 
                 O 
                 −27.166 
                 6.675 
                 16.746 
               
               
                 529 
                 MET75 
                 CB 
                 −28.539 
                 7.208 
                 19.198 
               
               
                 530 
                 MET75 
                 CG 
                 −27.367 
                 6.867 
                 20.114 
               
               
                 531 
                 MET75 
                 SD 
                 −27.678 
                 5.549 
                 21.31 
               
               
                 532 
                 MET75 
                 CE 
                 −28.002 
                 4.197 
                 20.154 
               
               
                 533 
                 VAL76 
                 N 
                 −26.117 
                 8.657 
                 16.992 
               
               
                 534 
                 VAL76 
                 CA 
                 −25.071 
                 8.327 
                 16.017 
               
               
                 535 
                 VAL76 
                 C 
                 −24.274 
                 7.103 
                 16.455 
               
               
                 536 
                 VAL76 
                 O 
                 −23.953 
                 6.925 
                 17.636 
               
               
                 537 
                 VAL76 
                 CB 
                 −24.151 
                 9.527 
                 15.809 
               
               
                 538 
                 VAL76 
                 CG1 
                 −24.904 
                 10.676 
                 15.149 
               
               
                 539 
                 VAL76 
                 CG2 
                 −23.504 
                 9.986 
                 17.109 
               
               
                 540 
                 ALA77 
                 N 
                 −23.836 
                 6.34 
                 15.467 
               
               
                 541 
                 ALA77 
                 CA 
                 −23.158 
                 5.062 
                 15.727 
               
               
                 542 
                 ALA77 
                 C 
                 −21.703 
                 5.203 
                 16.177 
               
               
                 543 
                 ALA77 
                 O 
                 −21.033 
                 4.194 
                 16.42 
               
               
                 544 
                 ALA77 
                 CB 
                 −23.22 
                 4.212 
                 14.465 
               
               
                 545 
                 ARG78 
                 N 
                 −21.218 
                 6.431 
                 16.271 
               
               
                 546 
                 ARG78 
                 CA 
                 −19.868 
                 6.689 
                 16.762 
               
               
                 547 
                 ARG78 
                 C 
                 −19.868 
                 7.178 
                 18.215 
               
               
                 548 
                 ARG78 
                 O 
                 −18.816 
                 7.163 
                 18.865 
               
               
                 549 
                 ARG78 
                 CB 
                 −19.274 
                 7.772 
                 15.874 
               
               
                 550 
                 ARG78 
                 CG 
                 −19.445 
                 7.436 
                 14.398 
               
               
                 551 
                 ARG78 
                 CD 
                 −19.068 
                 8.629 
                 13.528 
               
               
                 552 
                 ARG78 
                 NE 
                 −19.848 
                 9.81 
                 13.932 
               
               
                 553 
                 ARG78 
                 CZ 
                 −19.36 
                 11.053 
                 13.921 
               
               
                 554 
                 ARG78 
                 NH1 
                 −18.114 
                 11.278 
                 13.497 
               
               
                 555 
                 ARG78 
                 NH2 
                 −20.12 
                 12.072 
                 14.33 
               
               
                 556 
                 GLN79 
                 N 
                 −21.028 
                 7.577 
                 18.722 
               
               
                 557 
                 GLN79 
                 CA 
                 −21.128 
                 8.129 
                 20.088 
               
               
                 558 
                 GLN79 
                 C 
                 −22.484 
                 7.818 
                 20.715 
               
               
                 559 
                 GLN79 
                 O 
                 −23.48 
                 8.503 
                 20.45 
               
               
                 560 
                 GLN79 
                 CB 
                 −20.937 
                 9.651 
                 20.09 
               
               
                 561 
                 GLN79 
                 CG 
                 −19.486 
                 10.085 
                 19.884 
               
               
                 562 
                 GLN79 
                 CD 
                 −19.353 
                 11.607 
                 19.931 
               
               
                 563 
                 GLN79 
                 OE1 
                 −19.071 
                 12.193 
                 20.986 
               
               
                 564 
                 GLN79 
                 NE2 
                 −19.508 
                 12.226 
                 18.773 
               
               
                 565 
                 ILE80 
                 N 
                 −22.504 
                 6.806 
                 21.562 
               
               
                 566 
                 ILE80 
                 CA 
                 −23.733 
                 6.44 
                 22.273 
               
               
                 567 
                 ILE80 
                 C 
                 −23.732 
                 7.034 
                 23.679 
               
               
                 568 
                 ILE80 
                 O 
                 −22.666 
                 7.316 
                 24.24 
               
               
                 569 
                 ILE80 
                 CB 
                 −23.847 
                 4.919 
                 22.333 
               
               
                 570 
                 ILE80 
                 CG1 
                 −22.684 
                 4.305 
                 23.109 
               
               
                 571 
                 ILE80 
                 CG2 
                 −23.905 
                 4.35 
                 20.92 
               
               
                 572 
                 ILE80 
                 CD1 
                 −22.794 
                 2.788 
                 23.191 
               
               
                 573 
                 ARG81 
                 N 
                 −24.932 
                 7.278 
                 24.188 
               
               
                 574 
                 ARG81 
                 CA 
                 −25.15 
                 7.84 
                 25.535 
               
               
                 575 
                 ARG81 
                 C 
                 −24.657 
                 9.276 
                 25.691 
               
               
                 576 
                 ARG81 
                 O 
                 −23.493 
                 9.571 
                 25.411 
               
               
                 577 
                 ARG81 
                 CB 
                 −24.51 
                 6.964 
                 26.603 
               
               
                 578 
                 ARG81 
                 CG 
                 −25.437 
                 5.843 
                 27.046 
               
               
                 579 
                 ARG81 
                 CD 
                 −25.685 
                 5.92 
                 28.555 
               
               
                 580 
                 ARG81 
                 NE 
                 −26.269 
                 7.22 
                 28.93 
               
               
                 581 
                 ARG81 
                 CZ 
                 −25.651 
                 8.095 
                 29.722 
               
               
                 582 
                 ARG81 
                 NH1 
                 −24.439 
                 7.82 
                 30.204 
               
               
                 583 
                 ARG81 
                 NH2 
                 −26.234 
                 9.257 
                 30.008 
               
               
                 584 
                 ARG82 
                 N 
                 −25.448 
                 10.076 
                 26.389 
               
               
                 585 
                 ARG82 
                 CA 
                 −25.192 
                 11.523 
                 26.511 
               
               
                 586 
                 ARG82 
                 C 
                 −23.872 
                 11.866 
                 27.204 
               
               
                 587 
                 ARG82 
                 O 
                 −23.108 
                 12.684 
                 26.682 
               
               
                 588 
                 ARG82 
                 CB 
                 −26.32 
                 12.122 
                 27.333 
               
               
                 589 
                 ARG82 
                 CG 
                 −27.683 
                 11.796 
                 26.74 
               
               
                 590 
                 ARG82 
                 CD 
                 −28.801 
                 12.301 
                 27.643 
               
               
                 591 
                 ARG82 
                 NE 
                 −28.71 
                 11.659 
                 28.967 
               
               
                 592 
                 ARG82 
                 CZ 
                 −28.623 
                 12.34 
                 30.114 
               
               
                 593 
                 ARG82 
                 NH1 
                 −28.477 
                 11.689 
                 31.271 
               
               
                 594 
                 ARG82 
                 NH2 
                 −28.606 
                 13.675 
                 30.096 
               
               
                 595 
                 GLU83 
                 N 
                 −23.495 
                 11.077 
                 28.198 
               
               
                 596 
                 GLU83 
                 CA 
                 −22.237 
                 11.334 
                 28.909 
               
               
                 597 
                 GLU83 
                 C 
                 −21.03 
                 10.69 
                 28.227 
               
               
                 598 
                 GLU83 
                 O 
                 −19.894 
                 10.902 
                 28.657 
               
               
                 599 
                 GLU83 
                 CB 
                 −22.361 
                 10.828 
                 30.338 
               
               
                 600 
                 GLU83 
                 CG 
                 −23.385 
                 11.651 
                 31.114 
               
               
                 601 
                 GLU83 
                 CD 
                 −23.478 
                 11.172 
                 32.56 
               
               
                 602 
                 GLU83 
                 OE1 
                 −23.428 
                 9.967 
                 32.761 
               
               
                 603 
                 GLU83 
                 OE2 
                 −23.71 
                 12.011 
                 33.418 
               
               
                 604 
                 ASP84 
                 N 
                 −21.274 
                 9.941 
                 27.165 
               
               
                 605 
                 ASP84 
                 CA 
                 −20.201 
                 9.327 
                 26.386 
               
               
                 606 
                 ASP84 
                 C 
                 −20.095 
                 10.012 
                 25.024 
               
               
                 607 
                 ASP84 
                 O 
                 −19.257 
                 9.646 
                 24.19 
               
               
                 608 
                 ASP84 
                 CB 
                 −20.481 
                 7.841 
                 26.237 
               
               
                 609 
                 ASP84 
                 CG 
                 −20.585 
                 7.191 
                 27.613 
               
               
                 610 
                 ASP84 
                 OD1 
                 −19.547 
                 6.906 
                 28.193 
               
               
                 611 
                 ASP84 
                 OD2 
                 −21.704 
                 7.048 
                 28.092 
               
               
                 612 
                 LYS85 
                 N 
                 −20.939 
                 11.017 
                 24.831 
               
               
                 613 
                 LYS85 
                 CA 
                 −20.846 
                 11.928 
                 23.681 
               
               
                 614 
                 LYS85 
                 C 
                 −19.997 
                 13.228 
                 23.804 
               
               
                 615 
                 LYS85 
                 O 
                 −20.236 
                 14.084 
                 22.942 
               
               
                 616 
                 LYS85 
                 CB 
                 −22.27 
                 12.347 
                 23.327 
               
               
                 617 
                 LYS85 
                 CG 
                 −23.107 
                 11.173 
                 22.832 
               
               
                 618 
                 LYS85 
                 CD 
                 −24.573 
                 11.567 
                 22.679 
               
               
                 619 
                 LYS85 
                 CE 
                 −25.408 
                 10.408 
                 22.148 
               
               
                 620 
                 LYS85 
                 NZ 
                 −26.824 
                 10.785 
                 22.036 
               
               
                 621 
                 PRO86 
                 N 
                 −19.054 
                 13.455 
                 24.73 
               
               
                 622 
                 PRO86 
                 CA 
                 −18.316 
                 14.731 
                 24.698 
               
               
                 623 
                 PRO86 
                 C 
                 −17.168 
                 14.8 
                 23.679 
               
               
                 624 
                 PRO86 
                 O 
                 −16.339 
                 15.713 
                 23.772 
               
               
                 625 
                 PRO86 
                 CB 
                 −17.779 
                 14.922 
                 26.08 
               
               
                 626 
                 PRO86 
                 CG 
                 −17.866 
                 13.6 
                 26.815 
               
               
                 627 
                 PRO86 
                 CD 
                 −18.543 
                 12.646 
                 25.852 
               
               
                 628 
                 PHE87 
                 N 
                 −17.14 
                 13.906 
                 22.701 
               
               
                 629 
                 PHE87 
                 CA 
                 −16.12 
                 13.963 
                 21.653 
               
               
                 630 
                 PHE87 
                 C 
                 −16.67 
                 14.817 
                 20.51 
               
               
                 631 
                 PHE87 
                 O 
                 −15.963 
                 15.16 
                 19.559 
               
               
                 632 
                 PHE87 
                 CB 
                 −15.848 
                 12.556 
                 21.128 
               
               
                 633 
                 PHE87 
                 CG 
                 −15.724 
                 11.449 
                 22.174 
               
               
                 634 
                 PHE87 
                 CD1 
                 −16.447 
                 10.277 
                 21.996 
               
               
                 635 
                 PHE87 
                 CD2 
                 −14.904 
                 11.591 
                 23.286 
               
               
                 636 
                 PHE87 
                 CE1 
                 −16.358 
                 9.254 
                 22.93 
               
               
                 637 
                 PHE87 
                 CE2 
                 −14.817 
                 10.567 
                 24.22 
               
               
                 638 
                 PHE87 
                 CZ 
                 −15.544 
                 9.399 
                 24.044 
               
               
                 639 
                 ARG88 
                 N 
                 −17.948 
                 15.143 
                 20.627 
               
               
                 640 
                 ARG88 
                 CA 
                 −18.629 
                 16.037 
                 19.686 
               
               
                 641 
                 ARG88 
                 C 
                 −18.178 
                 17.519 
                 19.7 
               
               
                 642 
                 ARG88 
                 O 
                 −18.118 
                 18.064 
                 18.59 
               
               
                 643 
                 ARG88 
                 CB 
                 −20.122 
                 15.915 
                 19.965 
               
               
                 644 
                 ARG88 
                 CG 
                 −20.964 
                 16.678 
                 18.953 
               
               
                 645 
                 ARG88 
                 CD 
                 −22.429 
                 16.294 
                 19.089 
               
               
                 646 
                 ARG88 
                 NE 
                 −22.593 
                 14.851 
                 18.868 
               
               
                 647 
                 ARG88 
                 CZ 
                 −23.307 
                 14.07 
                 19.679 
               
               
                 648 
                 ARG88 
                 NH1 
                 −23.373 
                 12.757 
                 19.45 
               
               
                 649 
                 ARG88 
                 NH2 
                 −23.922 
                 14.598 
                 20.739 
               
               
                 650 
                 PRO89 
                 N 
                 −17.919 
                 18.194 
                 20.826 
               
               
                 651 
                 PRO89 
                 CA 
                 −17.186 
                 19.48 
                 20.763 
               
               
                 652 
                 PRO89 
                 C 
                 −15.737 
                 19.333 
                 20.277 
               
               
                 653 
                 PRO89 
                 O 
                 −14.786 
                 19.454 
                 21.057 
               
               
                 654 
                 PRO89 
                 CB 
                 −17.206 
                 20.033 
                 22.154 
               
               
                 655 
                 PRO89 
                 CG 
                 −17.798 
                 19.004 
                 23.096 
               
               
                 656 
                 PRO89 
                 CD 
                 −18.208 
                 17.832 
                 22.224 
               
               
                 657 
                 SER90 
                 N 
                 −15.606 
                 19.29 
                 18.963 
               
               
                 658 
                 SER90 
                 CA 
                 −14.334 
                 19.04 
                 18.296 
               
               
                 659 
                 SER90 
                 C 
                 −14.43 
                 19.413 
                 16.824 
               
               
                 660 
                 SER90 
                 O 
                 −15.534 
                 19.592 
                 16.293 
               
               
                 661 
                 SER90 
                 CB 
                 −14.069 
                 17.55 
                 18.375 
               
               
                 662 
                 SER90 
                 OG 
                 −15.095 
                 16.928 
                 17.609 
               
               
                 663 
                 LEU91 
                 N 
                 −13.326 
                 19.173 
                 16.14 
               
               
                 664 
                 LEU91 
                 CA 
                 −13.154 
                 19.564 
                 14.737 
               
               
                 665 
                 LEU91 
                 C 
                 −14.042 
                 18.804 
                 13.745 
               
               
                 666 
                 LEU91 
                 O 
                 −14.491 
                 19.39 
                 12.754 
               
               
                 667 
                 LEU91 
                 CB 
                 −11.702 
                 19.238 
                 14.405 
               
               
                 668 
                 LEU91 
                 CG 
                 −11.325 
                 19.637 
                 12.988 
               
               
                 669 
                 LEU91 
                 CD1 
                 −11.253 
                 21.153 
                 12.877 
               
               
                 670 
                 LEU91 
                 CD2 
                 −9.989 
                 19.012 
                 12.606 
               
               
                 671 
                 ILE92 
                 N 
                 −14.422 
                 17.582 
                 14.076 
               
               
                 672 
                 ILE92 
                 CA 
                 −15.199 
                 16.791 
                 13.12 
               
               
                 673 
                 ILE92 
                 C 
                 −16.712 
                 16.857 
                 13.368 
               
               
                 674 
                 ILE92 
                 O 
                 −17.487 
                 16.497 
                 12.474 
               
               
                 675 
                 ILE92 
                 CB 
                 −14.682 
                 15.351 
                 13.173 
               
               
                 676 
                 ILE92 
                 CG1 
                 −15.288 
                 14.488 
                 12.07 
               
               
                 677 
                 ILE92 
                 CG2 
                 −14.932 
                 14.719 
                 14.539 
               
               
                 678 
                 ILE92 
                 CD1 
                 −14.775 
                 13.055 
                 12.137 
               
               
                 679 
                 ALA93 
                 N 
                 −17.14 
                 17.407 
                 14.494 
               
               
                 680 
                 ALA93 
                 CA 
                 −18.578 
                 17.414 
                 14.759 
               
               
                 681 
                 ALA93 
                 C 
                 −19.15 
                 18.822 
                 14.872 
               
               
                 682 
                 ALA93 
                 O 
                 −20.335 
                 19.048 
                 14.589 
               
               
                 683 
                 ALA93 
                 CB 
                 −18.865 
                 16.593 
                 16.004 
               
               
                 684 
                 MET94 
                 N 
                 −18.294 
                 19.776 
                 15.191 
               
               
                 685 
                 MET94 
                 CA 
                 −18.739 
                 21.168 
                 15.216 
               
               
                 686 
                 MET94 
                 C 
                 −18.99 
                 21.683 
                 13.811 
               
               
                 687 
                 MET94 
                 O 
                 −18.221 
                 21.436 
                 12.88 
               
               
                 688 
                 MET94 
                 CB 
                 −17.695 
                 22.042 
                 15.893 
               
               
                 689 
                 MET94 
                 CG 
                 −17.822 
                 21.982 
                 17.407 
               
               
                 690 
                 MET94 
                 SD 
                 −16.686 
                 23.058 
                 18.31 
               
               
                 691 
                 MET94 
                 CE 
                 −17.561 
                 23.095 
                 19.891 
               
               
                 692 
                 ASP95 
                 N 
                 −20.089 
                 22.398 
                 13.672 
               
               
                 693 
                 ASP95 
                 CA 
                 −20.42 
                 23.024 
                 12.393 
               
               
                 694 
                 ASP95 
                 C 
                 −19.831 
                 24.427 
                 12.371 
               
               
                 695 
                 ASP95 
                 O 
                 −19.589 
                 25.001 
                 13.438 
               
               
                 696 
                 ASP95 
                 CB 
                 −21.938 
                 23.082 
                 12.258 
               
               
                 697 
                 ASP95 
                 CG 
                 −22.52 
                 21.677 
                 12.373 
               
               
                 698 
                 ASP95 
                 OD1 
                 −22.276 
                 20.87 
                 11.484 
               
               
                 699 
                 ASP95 
                 OD2 
                 −23.173 
                 21.412 
                 13.37 
               
               
                 700 
                 PRO96 
                 N 
                 −19.488 
                 24.936 
                 11.201 
               
               
                 701 
                 PRO96 
                 CA 
                 −19.076 
                 26.343 
                 11.099 
               
               
                 702 
                 PRO96 
                 C 
                 −20.177 
                 27.263 
                 11.641 
               
               
                 703 
                 PRO96 
                 O 
                 −21.353 
                 26.892 
                 11.581 
               
               
                 704 
                 PRO96 
                 CB 
                 −18.812 
                 26.567 
                 9.64 
               
               
                 705 
                 PRO96 
                 CG 
                 −19.078 
                 25.278 
                 8.875 
               
               
                 706 
                 PRO96 
                 CD 
                 −19.532 
                 24.256 
                 9.905 
               
               
                 707 
                 PRO97 
                 N 
                 −19.817 
                 28.38 
                 12.263 
               
               
                 708 
                 PRO97 
                 CA 
                 −18.428 
                 28.85 
                 12.436 
               
               
                 709 
                 PRO97 
                 C 
                 −17.649 
                 28.271 
                 13.631 
               
               
                 710 
                 PRO97 
                 O 
                 −16.462 
                 28.595 
                 13.772 
               
               
                 711 
                 PRO97 
                 CB 
                 −18.567 
                 30.329 
                 12.615 
               
               
                 712 
                 PRO97 
                 CG 
                 −20.013 
                 30.649 
                 12.964 
               
               
                 713 
                 PRO97 
                 CD 
                 −20.777 
                 29.345 
                 12.804 
               
               
                 714 
                 GLU98 
                 N 
                 −18.233 
                 27.353 
                 14.389 
               
               
                 715 
                 GLU98 
                 CA 
                 −17.555 
                 26.761 
                 15.556 
               
               
                 716 
                 GLU98 
                 C 
                 −16.353 
                 25.946 
                 15.099 
               
               
                 717 
                 GLU98 
                 O 
                 −15.224 
                 26.174 
                 15.555 
               
               
                 718 
                 GLU98 
                 CB 
                 −18.513 
                 25.782 
                 16.223 
               
               
                 719 
                 GLU98 
                 CG 
                 −19.894 
                 26.372 
                 16.474 
               
               
                 720 
                 GLU98 
                 CD 
                 −20.857 
                 25.236 
                 16.811 
               
               
                 721 
                 GLU98 
                 OE1 
                 −20.697 
                 24.171 
                 16.227 
               
               
                 722 
                 GLU98 
                 OE2 
                 −21.799 
                 25.49 
                 17.544 
               
               
                 723 
                 HIS99 
                 N 
                 −16.575 
                 25.223 
                 14.013 
               
               
                 724 
                 HIS99 
                 CA 
                 −15.52 
                 24.448 
                 13.359 
               
               
                 725 
                 HIS99 
                 C 
                 −14.43 
                 25.323 
                 12.743 
               
               
                 726 
                 HIS99 
                 O 
                 −13.249 
                 24.993 
                 12.887 
               
               
                 727 
                 HIS99 
                 CB 
                 −16.19 
                 23.646 
                 12.252 
               
               
                 728 
                 HIS99 
                 CG 
                 −15.238 
                 23.09 
                 11.22 
               
               
                 729 
                 HIS99 
                 ND1 
                 −14.522 
                 21.957 
                 11.317 
               
               
                 730 
                 HIS99 
                 CD2 
                 −14.946 
                 23.649 
                 9.998 
               
               
                 731 
                 HIS99 
                 CE1 
                 −13.779 
                 21.805 
                 10.203 
               
               
                 732 
                 HIS99 
                 NE2 
                 −14.042 
                 22.852 
                 9.39 
               
               
                 733 
                 GLY100 
                 N 
                 −14.792 
                 26.524 
                 12.322 
               
               
                 734 
                 GLY100 
                 CA 
                 −13.832 
                 27.439 
                 11.702 
               
               
                 735 
                 GLY100 
                 C 
                 −12.859 
                 27.944 
                 12.756 
               
               
                 736 
                 GLY100 
                 O 
                 −11.648 
                 27.716 
                 12.64 
               
               
                 737 
                 LYS101 
                 N 
                 −13.419 
                 28.385 
                 13.872 
               
               
                 738 
                 LYS101 
                 CA 
                 −12.626 
                 28.895 
                 14.993 
               
               
                 739 
                 LYS101 
                 C 
                 −11.711 
                 27.823 
                 15.579 
               
               
                 740 
                 LYS101 
                 O 
                 −10.485 
                 28.02 
                 15.622 
               
               
                 741 
                 LYS101 
                 CB 
                 −13.608 
                 29.33 
                 16.07 
               
               
                 742 
                 LYS101 
                 CG 
                 −12.893 
                 29.892 
                 17.291 
               
               
                 743 
                 LYS101 
                 CD 
                 −13.829 
                 29.939 
                 18.492 
               
               
                 744 
                 LYS101 
                 CE 
                 −14.189 
                 28.531 
                 18.955 
               
               
                 745 
                 LYS101 
                 NZ 
                 −12.986 
                 27.796 
                 19.381 
               
               
                 746 
                 ALA102 
                 N 
                 −12.251 
                 26.624 
                 15.738 
               
               
                 747 
                 ALA102 
                 CA 
                 −11.474 
                 25.523 
                 16.313 
               
               
                 748 
                 ALA102 
                 C 
                 −10.381 
                 25.022 
                 15.373 
               
               
                 749 
                 ALA102 
                 O 
                 −9.243 
                 24.859 
                 15.828 
               
               
                 750 
                 ALA102 
                 CB 
                 −12.425 
                 24.379 
                 16.645 
               
               
                 751 
                 ARG103 
                 N 
                 −10.622 
                 25.091 
                 14.074 
               
               
                 752 
                 ARG103 
                 CA 
                 −9.63 
                 24.64 
                 13.097 
               
               
                 753 
                 ARG103 
                 C 
                 −8.492 
                 25.644 
                 12.958 
               
               
                 754 
                 ARG103 
                 O 
                 −7.325 
                 25.236 
                 13.033 
               
               
                 755 
                 ARG103 
                 CB 
                 −10.347 
                 24.476 
                 11.762 
               
               
                 756 
                 ARG103 
                 CG 
                 −9.496 
                 23.785 
                 10.705 
               
               
                 757 
                 ARG103 
                 CD 
                 −10.366 
                 23.455 
                 9.496 
               
               
                 758 
                 ARG103 
                 NE 
                 −9.651 
                 22.682 
                 8.467 
               
               
                 759 
                 ARG103 
                 CZ 
                 −9.807 
                 21.367 
                 8.287 
               
               
                 760 
                 ARG103 
                 NH1 
                 −10.493 
                 20.645 
                 9.175 
               
               
                 761 
                 ARG103 
                 NH2 
                 −9.174 
                 20.755 
                 7.285 
               
               
                 762 
                 ARG104 
                 N 
                 −8.811 
                 26.923 
                 13.087 
               
               
                 763 
                 ARG104 
                 CA 
                 −7.775 
                 27.957 
                 13.006 
               
               
                 764 
                 ARG104 
                 C 
                 −6.906 
                 27.966 
                 14.256 
               
               
                 765 
                 ARG104 
                 O 
                 −5.675 
                 28.083 
                 14.149 
               
               
                 766 
                 ARG104 
                 CB 
                 −8.442 
                 29.316 
                 12.84 
               
               
                 767 
                 ARG104 
                 CG 
                 −9.166 
                 29.412 
                 11.502 
               
               
                 768 
                 ARG104 
                 CD 
                 −9.828 
                 30.772 
                 11.319 
               
               
                 769 
                 ARG104 
                 NE 
                 −10.874 
                 30.999 
                 12.329 
               
               
                 770 
                 ARG104 
                 CZ 
                 −11.061 
                 32.171 
                 12.941 
               
               
                 771 
                 ARG104 
                 NH1 
                 −10.231 
                 33.188 
                 12.701 
               
               
                 772 
                 ARG104 
                 NH2 
                 −12.048 
                 32.31 
                 13.829 
               
               
                 773 
                 ASP105 
                 N 
                 −7.5 
                 27.625 
                 15.388 
               
               
                 774 
                 ASP105 
                 CA 
                 −6.718 
                 27.493 
                 16.616 
               
               
                 775 
                 ASP105 
                 C 
                 −5.828 
                 26.253 
                 16.594 
               
               
                 776 
                 ASP105 
                 O 
                 −4.602 
                 26.392 
                 16.716 
               
               
                 777 
                 ASP105 
                 CB 
                 −7.67 
                 27.427 
                 17.806 
               
               
                 778 
                 ASP105 
                 CG 
                 −8.198 
                 28.814 
                 18.165 
               
               
                 779 
                 ASP105 
                 OD1 
                 −7.389 
                 29.588 
                 18.666 
               
               
                 780 
                 ASP105 
                 OD2 
                 −9.411 
                 28.938 
                 18.257 
               
               
                 781 
                 VAL106 
                 N 
                 −6.379 
                 25.125 
                 16.173 
               
               
                 782 
                 VAL106 
                 CA 
                 −5.636 
                 23.86 
                 16.236 
               
               
                 783 
                 VAL106 
                 C 
                 −4.51 
                 23.761 
                 15.214 
               
               
                 784 
                 VAL106 
                 O 
                 −3.414 
                 23.348 
                 15.612 
               
               
                 785 
                 VAL106 
                 CB 
                 −6.611 
                 22.703 
                 16.046 
               
               
                 786 
                 VAL106 
                 CG1 
                 −5.886 
                 21.37 
                 15.89 
               
               
                 787 
                 VAL106 
                 CG2 
                 −7.587 
                 22.637 
                 17.212 
               
               
                 788 
                 VAL107 
                 N 
                 −4.641 
                 24.427 
                 14.075 
               
               
                 789 
                 VAL107 
                 CA 
                 −3.565 
                 24.397 
                 13.071 
               
               
                 790 
                 VAL107 
                 C 
                 −2.362 
                 25.259 
                 13.474 
               
               
                 791 
                 VAL107 
                 O 
                 −1.225 
                 24.918 
                 13.123 
               
               
                 792 
                 VAL107 
                 CB 
                 −4.142 
                 24.869 
                 11.737 
               
               
                 793 
                 VAL107 
                 CG1 
                 −3.06 
                 25.104 
                 10.687 
               
               
                 794 
                 VAL107 
                 CG2 
                 −5.175 
                 23.879 
                 11.213 
               
               
                 795 
                 GLY108 
                 N 
                 −2.576 
                 26.155 
                 14.426 
               
               
                 796 
                 GLY108 
                 CA 
                 −1.49 
                 26.985 
                 14.953 
               
               
                 797 
                 GLY108 
                 C 
                 −0.511 
                 26.183 
                 15.813 
               
               
                 798 
                 GLY108 
                 O 
                 0.685 
                 26.491 
                 15.837 
               
               
                 799 
                 GLU109 
                 N 
                 −1.006 
                 25.191 
                 16.537 
               
               
                 800 
                 GLU109 
                 CA 
                 −0.109 
                 24.388 
                 17.376 
               
               
                 801 
                 GLU109 
                 C 
                 0.121 
                 22.976 
                 16.836 
               
               
                 802 
                 GLU109 
                 O 
                 1.086 
                 22.311 
                 17.229 
               
               
                 803 
                 GLU109 
                 CB 
                 −0.677 
                 24.35 
                 18.784 
               
               
                 804 
                 GLU109 
                 CG 
                 −0.577 
                 25.728 
                 19.424 
               
               
                 805 
                 GLU109 
                 CD 
                 0.886 
                 26.1 
                 19.659 
               
               
                 806 
                 GLU109 
                 OE1 
                 1.612 
                 25.244 
                 20.147 
               
               
                 807 
                 GLU109 
                 OE2 
                 1.22 
                 27.255 
                 19.442 
               
               
                 808 
                 PHE110 
                 N 
                 −0.686 
                 22.572 
                 15.873 
               
               
                 809 
                 PHE110 
                 CA 
                 −0.511 
                 21.269 
                 15.221 
               
               
                 810 
                 PHE110 
                 C 
                 0.017 
                 21.468 
                 13.798 
               
               
                 811 
                 PHE110 
                 O 
                 −0.547 
                 20.963 
                 12.819 
               
               
                 812 
                 PHE110 
                 CB 
                 −1.866 
                 20.568 
                 15.206 
               
               
                 813 
                 PHE110 
                 CG 
                 −1.834 
                 19.088 
                 14.838 
               
               
                 814 
                 PHE110 
                 CD1 
                 −0.842 
                 18.264 
                 15.352 
               
               
                 815 
                 PHE110 
                 CD2 
                 −2.808 
                 18.564 
                 13.998 
               
               
                 816 
                 PHE110 
                 CE1 
                 −0.819 
                 16.915 
                 15.019 
               
               
                 817 
                 PHE110 
                 CE2 
                 −2.784 
                 17.216 
                 13.665 
               
               
                 818 
                 PHE110 
                 CZ 
                 −1.79 
                 16.392 
                 14.176 
               
               
                 819 
                 THR111 
                 N 
                 1.103 
                 22.217 
                 13.706 
               
               
                 820 
                 THR111 
                 CA 
                 1.68 
                 22.585 
                 12.409 
               
               
                 821 
                 THR111 
                 C 
                 2.353 
                 21.411 
                 11.71 
               
               
                 822 
                 THR111 
                 O 
                 2.846 
                 20.47 
                 12.346 
               
               
                 823 
                 THR111 
                 CB 
                 2.745 
                 23.65 
                 12.628 
               
               
                 824 
                 THR111 
                 OG1 
                 3.887 
                 23.019 
                 13.193 
               
               
                 825 
                 THR111 
                 CG2 
                 2.27 
                 24.756 
                 13.561 
               
               
                 826 
                 VAL112 
                 N 
                 2.564 
                 21.605 
                 10.417 
               
               
                 827 
                 VAL112 
                 CA 
                 3.302 
                 20.63 
                 9.605 
               
               
                 828 
                 VAL112 
                 C 
                 4.802 
                 20.712 
                 9.887 
               
               
                 829 
                 VAL112 
                 O 
                 5.492 
                 19.689 
                 9.86 
               
               
                 830 
                 VAL112 
                 CB 
                 3.026 
                 20.929 
                 8.134 
               
               
                 831 
                 VAL112 
                 CG1 
                 3.819 
                 20.01 
                 7.21 
               
               
                 832 
                 VAL112 
                 CG2 
                 1.535 
                 20.833 
                 7.832 
               
               
                 833 
                 LYS113 
                 N 
                 5.227 
                 21.845 
                 10.425 
               
               
                 834 
                 LYS113 
                 CA 
                 6.608 
                 22.003 
                 10.884 
               
               
                 835 
                 LYS113 
                 C 
                 6.892 
                 21.096 
                 12.082 
               
               
                 836 
                 LYS113 
                 O 
                 7.864 
                 20.332 
                 12.044 
               
               
                 837 
                 LYS113 
                 CB 
                 6.795 
                 23.456 
                 11.298 
               
               
                 838 
                 LYS113 
                 CG 
                 8.168 
                 23.696 
                 11.914 
               
               
                 839 
                 LYS113 
                 CD 
                 8.232 
                 25.064 
                 12.582 
               
               
                 840 
                 LYS113 
                 CE 
                 7.189 
                 25.184 
                 13.692 
               
               
                 841 
                 LYS113 
                 NZ 
                 7.407 
                 24.178 
                 14.747 
               
               
                 842 
                 ARG114 
                 N 
                 5.945 
                 21.013 
                 13.008 
               
               
                 843 
                 ARG114 
                 CA 
                 6.085 
                 20.094 
                 14.141 
               
               
                 844 
                 ARG114 
                 C 
                 6.098 
                 18.627 
                 13.713 
               
               
                 845 
                 ARG114 
                 O 
                 7.034 
                 17.912 
                 14.09 
               
               
                 846 
                 ARG114 
                 CB 
                 4.916 
                 20.313 
                 15.096 
               
               
                 847 
                 ARG114 
                 CG 
                 4.939 
                 19.283 
                 16.22 
               
               
                 848 
                 ARG114 
                 CD 
                 3.721 
                 19.388 
                 17.131 
               
               
                 849 
                 ARG114 
                 NE 
                 3.696 
                 20.666 
                 17.858 
               
               
                 850 
                 ARG114 
                 CZ 
                 4.078 
                 20.792 
                 19.131 
               
               
                 851 
                 ARG114 
                 NH1 
                 3.903 
                 21.953 
                 19.766 
               
               
                 852 
                 ARG114 
                 NH2 
                 4.537 
                 19.73 
                 19.798 
               
               
                 853 
                 MET115 
                 N 
                 5.28 
                 18.265 
                 12.737 
               
               
                 854 
                 MET115 
                 CA 
                 5.23 
                 16.862 
                 12.311 
               
               
                 855 
                 MET115 
                 C 
                 6.438 
                 16.467 
                 11.456 
               
               
                 856 
                 MET115 
                 O 
                 6.99 
                 15.378 
                 11.662 
               
               
                 857 
                 MET115 
                 CB 
                 3.926 
                 16.642 
                 11.555 
               
               
                 858 
                 MET115 
                 CG 
                 2.739 
                 16.915 
                 12.474 
               
               
                 859 
                 MET115 
                 SD 
                 1.093 
                 16.637 
                 11.78 
               
               
                 860 
                 MET115 
                 CE 
                 1.057 
                 17.94 
                 10.532 
               
               
                 861 
                 LYS116 
                 N 
                 7.027 
                 17.445 
                 10.787 
               
               
                 862 
                 LYS116 
                 CA 
                 8.25 
                 17.222 
                 10.01 
               
               
                 863 
                 LYS116 
                 C 
                 9.492 
                 17.156 
                 10.902 
               
               
                 864 
                 LYS116 
                 O 
                 10.434 
                 16.413 
                 10.59 
               
               
                 865 
                 LYS116 
                 CB 
                 8.372 
                 18.392 
                 9.042 
               
               
                 866 
                 LYS116 
                 CG 
                 9.635 
                 18.337 
                 8.194 
               
               
                 867 
                 LYS116 
                 CD 
                 9.738 
                 19.592 
                 7.338 
               
               
                 868 
                 LYS116 
                 CE 
                 9.703 
                 20.841 
                 8.213 
               
               
                 869 
                 LYS116 
                 NZ 
                 9.753 
                 22.063 
                 7.395 
               
               
                 870 
                 ALA117 
                 N 
                 9.404 
                 17.748 
                 12.084 
               
               
                 871 
                 ALA117 
                 CA 
                 10.49 
                 17.663 
                 13.066 
               
               
                 872 
                 ALA117 
                 C 
                 10.354 
                 16.43 
                 13.962 
               
               
                 873 
                 ALA117 
                 O 
                 11.331 
                 16 
                 14.587 
               
               
                 874 
                 ALA117 
                 CB 
                 10.469 
                 18.924 
                 13.922 
               
               
                 875 
                 LEU118 
                 N 
                 9.185 
                 15.81 
                 13.933 
               
               
                 876 
                 LEU118 
                 CA 
                 8.975 
                 14.544 
                 14.64 
               
               
                 877 
                 LEU118 
                 C 
                 9.351 
                 13.359 
                 13.76 
               
               
                 878 
                 LEU118 
                 O 
                 9.591 
                 12.26 
                 14.275 
               
               
                 879 
                 LEU118 
                 CB 
                 7.512 
                 14.434 
                 15.05 
               
               
                 880 
                 LEU118 
                 CG 
                 7.153 
                 15.474 
                 16.104 
               
               
                 881 
                 LEU118 
                 CD1 
                 5.654 
                 15.48 
                 16.372 
               
               
                 882 
                 LEU118 
                 CD2 
                 7.934 
                 15.246 
                 17.393 
               
               
                 883 
                 GLN119 
                 N 
                 9.563 
                 13.632 
                 12.483 
               
               
                 884 
                 GLN119 
                 CA 
                 10.052 
                 12.633 
                 11.518 
               
               
                 885 
                 GLN119 
                 C 
                 11.263 
                 11.797 
                 11.989 
               
               
                 886 
                 GLN119 
                 O 
                 11.09 
                 10.573 
                 12.041 
               
               
                 887 
                 GLN119 
                 CB 
                 10.378 
                 13.373 
                 10.227 
               
               
                 888 
                 GLN119 
                 CG 
                 10.944 
                 12.471 
                 9.144 
               
               
                 889 
                 GLN119 
                 CD 
                 11.394 
                 13.351 
                 7.985 
               
               
                 890 
                 GLN119 
                 OE1 
                 11.701 
                 12.857 
                 6.894 
               
               
                 891 
                 GLN119 
                 NE2 
                 11.444 
                 14.647 
                 8.243 
               
               
                 892 
                 PRO120 
                 N 
                 12.388 
                 12.361 
                 12.439 
               
               
                 893 
                 PRO120 
                 CA 
                 13.485 
                 11.486 
                 12.885 
               
               
                 894 
                 PRO120 
                 C 
                 13.211 
                 10.732 
                 14.195 
               
               
                 895 
                 PRO120 
                 O 
                 13.761 
                 9.639 
                 14.381 
               
               
                 896 
                 PRO120 
                 CB 
                 14.672 
                 12.386 
                 13.05 
               
               
                 897 
                 PRO120 
                 CG 
                 14.237 
                 13.832 
                 12.892 
               
               
                 898 
                 PRO120 
                 CD 
                 12.764 
                 13.785 
                 12.533 
               
               
                 899 
                 ARG121 
                 N 
                 12.229 
                 11.159 
                 14.974 
               
               
                 900 
                 ARG121 
                 CA 
                 11.917 
                 10.438 
                 16.203 
               
               
                 901 
                 ARG121 
                 C 
                 11.02 
                 9.25 
                 15.868 
               
               
                 902 
                 ARG121 
                 O 
                 11.331 
                 8.136 
                 16.303 
               
               
                 903 
                 ARG121 
                 CB 
                 11.218 
                 11.385 
                 17.174 
               
               
                 904 
                 ARG121 
                 CG 
                 11.741 
                 11.209 
                 18.597 
               
               
                 905 
                 ARG121 
                 CD 
                 11.481 
                 9.812 
                 19.149 
               
               
                 906 
                 ARG121 
                 NE 
                 12.184 
                 9.613 
                 20.424 
               
               
                 907 
                 ARG121 
                 CZ 
                 12.714 
                 8.443 
                 20.784 
               
               
                 908 
                 ARG121 
                 NH1 
                 13.415 
                 8.346 
                 21.915 
               
               
                 909 
                 ARG121 
                 NH2 
                 12.601 
                 7.386 
                 19.977 
               
               
                 910 
                 ILE122 
                 N 
                 10.18 
                 9.421 
                 14.857 
               
               
                 911 
                 ILE122 
                 CA 
                 9.316 
                 8.332 
                 14.381 
               
               
                 912 
                 ILE122 
                 C 
                 10.135 
                 7.27 
                 13.656 
               
               
                 913 
                 ILE122 
                 O 
                 9.975 
                 6.073 
                 13.928 
               
               
                 914 
                 ILE122 
                 CB 
                 8.309 
                 8.918 
                 13.396 
               
               
                 915 
                 ILE122 
                 CG1 
                 7.456 
                 9.995 
                 14.052 
               
               
                 916 
                 ILE122 
                 CG2 
                 7.422 
                 7.825 
                 12.807 
               
               
                 917 
                 ILE122 
                 CD1 
                 6.509 
                 10.636 
                 13.044 
               
               
                 918 
                 GLN123 
                 N 
                 11.179 
                 7.724 
                 12.982 
               
               
                 919 
                 GLN123 
                 CA 
                 12.088 
                 6.827 
                 12.269 
               
               
                 920 
                 GLN123 
                 C 
                 12.914 
                 5.997 
                 13.245 
               
               
                 921 
                 GLN123 
                 O 
                 12.897 
                 4.76 
                 13.156 
               
               
                 922 
                 GLN123 
                 CB 
                 12.989 
                 7.717 
                 11.423 
               
               
                 923 
                 GLN123 
                 CG 
                 13.978 
                 6.941 
                 10.567 
               
               
                 924 
                 GLN123 
                 CD 
                 14.72 
                 7.939 
                 9.684 
               
               
                 925 
                 GLN123 
                 OE1 
                 15.954 
                 7.96 
                 9.626 
               
               
                 926 
                 GLN123 
                 NE2 
                 13.946 
                 8.8 
                 9.044 
               
               
                 927 
                 GLN124 
                 N 
                 13.295 
                 6.633 
                 14.34 
               
               
                 928 
                 GLN124 
                 CA 
                 14.049 
                 5.959 
                 15.394 
               
               
                 929 
                 GLN124 
                 C 
                 13.184 
                 4.947 
                 16.144 
               
               
                 930 
                 GLN124 
                 O 
                 13.621 
                 3.798 
                 16.284 
               
               
                 931 
                 GLN124 
                 CB 
                 14.544 
                 7.04 
                 16.345 
               
               
                 932 
                 GLN124 
                 CG 
                 15.429 
                 6.495 
                 17.455 
               
               
                 933 
                 GLN124 
                 CD 
                 15.912 
                 7.668 
                 18.3 
               
               
                 934 
                 GLN124 
                 OE1 
                 16.786 
                 7.524 
                 19.162 
               
               
                 935 
                 GLN124 
                 NE2 
                 15.357 
                 8.832 
                 18.008 
               
               
                 936 
                 ILE125 
                 N 
                 11.904 
                 5.252 
                 16.299 
               
               
                 937 
                 ILE125 
                 CA 
                 10.961 
                 4.328 
                 16.947 
               
               
                 938 
                 ILE125 
                 C 
                 10.716 
                 3.072 
                 16.112 
               
               
                 939 
                 ILE125 
                 O 
                 10.861 
                 1.961 
                 16.642 
               
               
                 940 
                 ILE125 
                 CB 
                 9.638 
                 5.064 
                 17.148 
               
               
                 941 
                 ILE125 
                 CG1 
                 9.792 
                 6.214 
                 18.13 
               
               
                 942 
                 ILE125 
                 CG2 
                 8.543 
                 4.122 
                 17.628 
               
               
                 943 
                 ILE125 
                 CD1 
                 8.487 
                 6.984 
                 18.275 
               
               
                 944 
                 VAL126 
                 N 
                 10.649 
                 3.229 
                 14.797 
               
               
                 945 
                 VAL126 
                 CA 
                 10.44 
                 2.064 
                 13.928 
               
               
                 946 
                 VAL126 
                 C 
                 11.693 
                 1.2 
                 13.87 
               
               
                 947 
                 VAL126 
                 O 
                 11.603 
                 −0.021 
                 14.062 
               
               
                 948 
                 VAL126 
                 CB 
                 10.119 
                 2.529 
                 12.513 
               
               
                 949 
                 VAL126 
                 CG1 
                 9.754 
                 1.334 
                 11.641 
               
               
                 950 
                 VAL126 
                 CG2 
                 8.988 
                 3.544 
                 12.503 
               
               
                 951 
                 ASP127 
                 N 
                 12.843 
                 1.855 
                 13.909 
               
               
                 952 
                 ASP127 
                 CA 
                 14.121 
                 1.141 
                 13.889 
               
               
                 953 
                 ASP127 
                 C 
                 14.314 
                 0.34 
                 15.17 
               
               
                 954 
                 ASP127 
                 O 
                 14.537 
                 −0.876 
                 15.088 
               
               
                 955 
                 ASP127 
                 CB 
                 15.258 
                 2.153 
                 13.769 
               
               
                 956 
                 ASP127 
                 CG 
                 15.158 
                 2.967 
                 12.481 
               
               
                 957 
                 ASP127 
                 OD1 
                 15.632 
                 4.097 
                 12.49 
               
               
                 958 
                 ASP127 
                 OD2 
                 14.686 
                 2.426 
                 11.489 
               
               
                 959 
                 GLU128 
                 N 
                 13.903 
                 0.919 
                 16.288 
               
               
                 960 
                 GLU128 
                 CA 
                 14.048 
                 0.26 
                 17.589 
               
               
                 961 
                 GLU128 
                 C 
                 13.094 
                 −0.915 
                 17.762 
               
               
                 962 
                 GLU128 
                 O 
                 13.527 
                 −1.952 
                 18.281 
               
               
                 963 
                 GLU128 
                 CB 
                 13.764 
                 1.281 
                 18.684 
               
               
                 964 
                 GLU128 
                 CG 
                 14.807 
                 2.39 
                 18.707 
               
               
                 965 
                 GLU128 
                 CD 
                 14.367 
                 3.489 
                 19.668 
               
               
                 966 
                 GLU128 
                 OE1 
                 13.584 
                 4.333 
                 19.247 
               
               
                 967 
                 GLU128 
                 OE2 
                 14.794 
                 3.452 
                 20.812 
               
               
                 968 
                 HIS129 
                 N 
                 11.934 
                 −0.861 
                 17.128 
               
               
                 969 
                 HIS129 
                 CA 
                 11.002 
                 −1.985 
                 17.237 
               
               
                 970 
                 HIS129 
                 C 
                 11.411 
                 −3.142 
                 16.333 
               
               
                 971 
                 HIS129 
                 O 
                 11.344 
                 −4.297 
                 16.772 
               
               
                 972 
                 HIS129 
                 CB 
                 9.592 
                 −1.533 
                 16.885 
               
               
                 973 
                 HIS129 
                 CG 
                 8.963 
                 −0.57 
                 17.87 
               
               
                 974 
                 HIS129 
                 ND1 
                 7.942 
                 0.266 
                 17.612 
               
               
                 975 
                 HIS129 
                 CD2 
                 9.3 
                 −0.394 
                 19.192 
               
               
                 976 
                 HIS129 
                 CE1 
                 7.647 
                 0.969 
                 18.724 
               
               
                 977 
                 HIS129 
                 NE2 
                 8.488 
                 0.561 
                 19.701 
               
               
                 978 
                 ILE130 
                 N 
                 12.061 
                 −2.848 
                 15.218 
               
               
                 979 
                 ILE130 
                 CA 
                 12.564 
                 −3.95 
                 14.394 
               
               
                 980 
                 ILE130 
                 C 
                 13.768 
                 −4.577 
                 15.089 
               
               
                 981 
                 ILE130 
                 O 
                 13.69 
                 −5.756 
                 15.459 
               
               
                 982 
                 ILE130 
                 CB 
                 12.968 
                 −3.449 
                 13.012 
               
               
                 983 
                 ILE130 
                 CG1 
                 11.841 
                 −2.659 
                 12.36 
               
               
                 984 
                 ILE130 
                 CG2 
                 13.341 
                 −4.632 
                 12.125 
               
               
                 985 
                 ILE130 
                 CD1 
                 12.258 
                 −2.117 
                 10.996 
               
               
                 986 
                 ASP131 
                 N 
                 14.65 
                 −3.712 
                 15.575 
               
               
                 987 
                 ASP131 
                 CA 
                 15.874 
                 −4.12 
                 16.283 
               
               
                 988 
                 ASP131 
                 C 
                 15.604 
                 −5.033 
                 17.473 
               
               
                 989 
                 ASP131 
                 O 
                 15.932 
                 −6.226 
                 17.435 
               
               
                 990 
                 ASP131 
                 CB 
                 16.565 
                 −2.874 
                 16.84 
               
               
                 991 
                 ASP131 
                 CG 
                 17.175 
                 −1.999 
                 15.749 
               
               
                 992 
                 ASP131 
                 OD1 
                 17.222 
                 −0.791 
                 15.952 
               
               
                 993 
                 ASP131 
                 OD2 
                 17.743 
                 −2.564 
                 14.826 
               
               
                 994 
                 ALA132 
                 N 
                 14.882 
                 −4.505 
                 18.448 
               
               
                 995 
                 ALA132 
                 CA 
                 14.708 
                 −5.198 
                 19.727 
               
               
                 996 
                 ALA132 
                 C 
                 13.582 
                 −6.228 
                 19.763 
               
               
                 997 
                 ALA132 
                 O 
                 13.489 
                 −6.983 
                 20.738 
               
               
                 998 
                 ALA132 
                 CB 
                 14.465 
                 −4.147 
                 20.803 
               
               
                 999 
                 LEU133 
                 N 
                 12.752 
                 −6.286 
                 18.736 
               
               
                 1000 
                 LEU133 
                 CA 
                 11.712 
                 −7.311 
                 18.741 
               
               
                 1001 
                 LEU133 
                 C 
                 12.08 
                 −8.444 
                 17.798 
               
               
                 1002 
                 LEU133 
                 O 
                 12.567 
                 −9.492 
                 18.239 
               
               
                 1003 
                 LEU133 
                 CB 
                 10.366 
                 −6.697 
                 18.372 
               
               
                 1004 
                 LEU133 
                 CG 
                 9.925 
                 −5.686 
                 19.427 
               
               
                 1005 
                 LEU133 
                 CD1 
                 8.679 
                 −4.93 
                 18.987 
               
               
                 1006 
                 LEU133 
                 CD2 
                 9.698 
                 −6.366 
                 20.773 
               
               
                 1007 
                 LEU134 
                 N 
                 11.901 
                 −8.215 
                 16.511 
               
               
                 1008 
                 LEU134 
                 CA 
                 12.139 
                 −9.288 
                 15.539 
               
               
                 1009 
                 LEU134 
                 C 
                 12.895 
                 −8.777 
                 14.32 
               
               
                 1010 
                 LEU134 
                 O 
                 12.319 
                 −8.632 
                 13.237 
               
               
                 1011 
                 LEU134 
                 CB 
                 10.808 
                 −9.885 
                 15.087 
               
               
                 1012 
                 LEU134 
                 CG 
                 10.481 
                 −11.234 
                 15.731 
               
               
                 1013 
                 LEU134 
                 CD1 
                 11.66 
                 −12.193 
                 15.635 
               
               
                 1014 
                 LEU134 
                 CD2 
                 9.997 
                 −11.115 
                 17.173 
               
               
                 1015 
                 ALA135 
                 N 
                 14.194 
                 −8.586 
                 14.486 
               
               
                 1016 
                 ALA135 
                 CA 
                 15.038 
                 −8.142 
                 13.371 
               
               
                 1017 
                 ALA135 
                 C 
                 15.606 
                 −9.293 
                 12.538 
               
               
                 1018 
                 ALA135 
                 O 
                 16.184 
                 −9.051 
                 11.472 
               
               
                 1019 
                 ALA135 
                 CB 
                 16.193 
                 −7.323 
                 13.935 
               
               
                 1020 
                 GLY136 
                 N 
                 15.402 
                 −10.522 
                 12.984 
               
               
                 1021 
                 GLY136 
                 CA 
                 15.957 
                 −11.679 
                 12.272 
               
               
                 1022 
                 GLY136 
                 C 
                 14.865 
                 −12.524 
                 11.62 
               
               
                 1023 
                 GLY136 
                 O 
                 14.069 
                 −12.022 
                 10.829 
               
               
                 1024 
                 PRO137 
                 N 
                 14.906 
                 −13.813 
                 11.903 
               
               
                 1025 
                 PRO137 
                 CA 
                 13.938 
                 −14.772 
                 11.353 
               
               
                 1026 
                 PRO137 
                 C 
                 12.589 
                 −14.709 
                 12.067 
               
               
                 1027 
                 PRO137 
                 O 
                 12.21 
                 −13.679 
                 12.637 
               
               
                 1028 
                 PRO137 
                 CB 
                 14.573 
                 −16.111 
                 11.568 
               
               
                 1029 
                 PRO137 
                 CG 
                 15.748 
                 −15.953 
                 12.524 
               
               
                 1030 
                 PRO137 
                 CD 
                 15.899 
                 −14.46 
                 12.763 
               
               
                 1031 
                 LYS138 
                 N 
                 11.86 
                 −15.811 
                 11.945 
               
               
                 1032 
                 LYS138 
                 CA 
                 10.575 
                 −16.043 
                 12.639 
               
               
                 1033 
                 LYS138 
                 C 
                 9.412 
                 −15.227 
                 12.069 
               
               
                 1034 
                 LYS138 
                 O 
                 9.605 
                 −14.143 
                 11.508 
               
               
                 1035 
                 LYS138 
                 CB 
                 10.733 
                 −15.765 
                 14.135 
               
               
                 1036 
                 LYS138 
                 CG 
                 11.795 
                 −16.66 
                 14.765 
               
               
                 1037 
                 LYS138 
                 CD 
                 12.022 
                 −16.303 
                 16.23 
               
               
                 1038 
                 LYS138 
                 CE 
                 13.155 
                 −17.128 
                 16.829 
               
               
                 1039 
                 LYS138 
                 NZ 
                 12.859 
                 −18.567 
                 16.746 
               
               
                 1040 
                 PRO139 
                 N 
                 8.256 
                 −15.868 
                 12.022 
               
               
                 1041 
                 PRO139 
                 CA 
                 6.996 
                 −15.155 
                 11.797 
               
               
                 1042 
                 PRO139 
                 C 
                 6.612 
                 −14.289 
                 12.995 
               
               
                 1043 
                 PRO139 
                 O 
                 6.167 
                 −14.795 
                 14.031 
               
               
                 1044 
                 PRO139 
                 CB 
                 5.979 
                 −16.232 
                 11.583 
               
               
                 1045 
                 PRO139 
                 CG 
                 6.595 
                 −17.575 
                 11.948 
               
               
                 1046 
                 PRO139 
                 CD 
                 8.04 
                 −17.286 
                 12.322 
               
               
                 1047 
                 ALA140 
                 N 
                 6.749 
                 −12.987 
                 12.824 
               
               
                 1048 
                 ALA140 
                 CA 
                 6.355 
                 −12.036 
                 13.868 
               
               
                 1049 
                 ALA140 
                 C 
                 5.006 
                 −11.411 
                 13.552 
               
               
                 1050 
                 ALA140 
                 O 
                 4.591 
                 −11.359 
                 12.391 
               
               
                 1051 
                 ALA140 
                 CB 
                 7.395 
                 −10.931 
                 13.953 
               
               
                 1052 
                 ASP141 
                 N 
                 4.297 
                 −10.989 
                 14.582 
               
               
                 1053 
                 ASP141 
                 CA 
                 3.051 
                 −10.264 
                 14.336 
               
               
                 1054 
                 ASP141 
                 C 
                 3.363 
                 −8.779 
                 14.165 
               
               
                 1055 
                 ASP141 
                 O 
                 3.466 
                 −8.032 
                 15.149 
               
               
                 1056 
                 ASP141 
                 CB 
                 2.073 
                 −10.492 
                 15.481 
               
               
                 1057 
                 ASP141 
                 CG 
                 0.741 
                 −9.84 
                 15.132 
               
               
                 1058 
                 ASP141 
                 OD1 
                 0.583 
                 −8.673 
                 15.465 
               
               
                 1059 
                 ASP141 
                 OD2 
                 0.016 
                 −10.426 
                 14.338 
               
               
                 1060 
                 LEU142 
                 N 
                 3.261 
                 −8.332 
                 12.923 
               
               
                 1061 
                 LEU142 
                 CA 
                 3.692 
                 −6.983 
                 12.541 
               
               
                 1062 
                 LEU142 
                 C 
                 2.753 
                 −5.893 
                 13.048 
               
               
                 1063 
                 LEU142 
                 O 
                 3.232 
                 −4.806 
                 13.4 
               
               
                 1064 
                 LEU142 
                 CB 
                 3.78 
                 −6.96 
                 11.012 
               
               
                 1065 
                 LEU142 
                 CG 
                 4.336 
                 −5.66 
                 10.428 
               
               
                 1066 
                 LEU142 
                 CD1 
                 5.227 
                 −5.944 
                 9.225 
               
               
                 1067 
                 LEU142 
                 CD2 
                 3.241 
                 −4.659 
                 10.063 
               
               
                 1068 
                 VAL143 
                 N 
                 1.509 
                 −6.243 
                 13.329 
               
               
                 1069 
                 VAL143 
                 CA 
                 0.585 
                 −5.247 
                 13.868 
               
               
                 1070 
                 VAL143 
                 C 
                 0.992 
                 −4.867 
                 15.287 
               
               
                 1071 
                 VAL143 
                 O 
                 1.481 
                 −3.748 
                 15.477 
               
               
                 1072 
                 VAL143 
                 CB 
                 −0.829 
                 −5.809 
                 13.859 
               
               
                 1073 
                 VAL143 
                 CG1 
                 −1.823 
                 −4.772 
                 14.374 
               
               
                 1074 
                 VAL143 
                 CG2 
                 −1.212 
                 −6.26 
                 12.457 
               
               
                 1075 
                 GLN144 
                 N 
                 1.184 
                 −5.874 
                 16.119 
               
               
                 1076 
                 GLN144 
                 CA 
                 1.491 
                 −5.656 
                 17.535 
               
               
                 1077 
                 GLN144 
                 C 
                 2.945 
                 −5.249 
                 17.797 
               
               
                 1078 
                 GLN144 
                 O 
                 3.212 
                 −4.566 
                 18.791 
               
               
                 1079 
                 GLN144 
                 CB 
                 1.203 
                 −6.982 
                 18.23 
               
               
                 1080 
                 GLN144 
                 CG 
                 1.485 
                 −6.966 
                 19.726 
               
               
                 1081 
                 GLN144 
                 CD 
                 1.232 
                 −8.364 
                 20.277 
               
               
                 1082 
                 GLN144 
                 OE1 
                 1.815 
                 −8.777 
                 21.285 
               
               
                 1083 
                 GLN144 
                 NE2 
                 0.374 
                 −9.091 
                 19.582 
               
               
                 1084 
                 ALA145 
                 N 
                 3.842 
                 −5.539 
                 16.87 
               
               
                 1085 
                 ALA145 
                 CA 
                 5.246 
                 −5.186 
                 17.088 
               
               
                 1086 
                 ALA145 
                 C 
                 5.672 
                 −3.884 
                 16.412 
               
               
                 1087 
                 ALA145 
                 O 
                 6.594 
                 −3.211 
                 16.888 
               
               
                 1088 
                 ALA145 
                 CB 
                 6.108 
                 −6.329 
                 16.561 
               
               
                 1089 
                 LEU146 
                 N 
                 4.988 
                 −3.499 
                 15.349 
               
               
                 1090 
                 LEU146 
                 CA 
                 5.424 
                 −2.324 
                 14.588 
               
               
                 1091 
                 LEU146 
                 C 
                 4.294 
                 −1.342 
                 14.317 
               
               
                 1092 
                 LEU146 
                 O 
                 4.308 
                 −0.207 
                 14.815 
               
               
                 1093 
                 LEU146 
                 CB 
                 5.964 
                 −2.825 
                 13.252 
               
               
                 1094 
                 LEU146 
                 CG 
                 7.225 
                 −3.659 
                 13.433 
               
               
                 1095 
                 LEU146 
                 CD1 
                 7.467 
                 −4.589 
                 12.254 
               
               
                 1096 
                 LEU146 
                 CD2 
                 8.432 
                 −2.772 
                 13.705 
               
               
                 1097 
                 SER147 
                 N 
                 3.245 
                 −1.868 
                 13.71 
               
               
                 1098 
                 SER147 
                 CA 
                 2.169 
                 −1.053 
                 13.134 
               
               
                 1099 
                 SER147 
                 C 
                 1.274 
                 −0.369 
                 14.164 
               
               
                 1100 
                 SER147 
                 O 
                 0.727 
                 0.708 
                 13.911 
               
               
                 1101 
                 SER147 
                 CB 
                 1.325 
                 −2.001 
                 12.301 
               
               
                 1102 
                 SER147 
                 OG 
                 0.198 
                 −1.277 
                 11.856 
               
               
                 1103 
                 LEU148 
                 N 
                 1.174 
                 −0.97 
                 15.331 
               
               
                 1104 
                 LEU148 
                 CA 
                 0.484 
                 −0.358 
                 16.464 
               
               
                 1105 
                 LEU148 
                 C 
                 1.433 
                 0.51 
                 17.316 
               
               
                 1106 
                 LEU148 
                 O 
                 1.132 
                 1.707 
                 17.436 
               
               
                 1107 
                 LEU148 
                 CB 
                 −0.204 
                 −1.475 
                 17.259 
               
               
                 1108 
                 LEU148 
                 CG 
                 −1.13 
                 −0.987 
                 18.372 
               
               
                 1109 
                 LEU148 
                 CD1 
                 −2.317 
                 −1.93 
                 18.53 
               
               
                 1110 
                 LEU148 
                 CD2 
                 −0.404 
                 −0.81 
                 19.703 
               
               
                 1111 
                 PRO149 
                 N 
                 2.553 
                 0.008 
                 17.848 
               
               
                 1112 
                 PRO149 
                 CA 
                 3.299 
                 0.829 
                 18.809 
               
               
                 1113 
                 PRO149 
                 C 
                 3.987 
                 2.052 
                 18.203 
               
               
                 1114 
                 PRO149 
                 O 
                 4.043 
                 3.07 
                 18.9 
               
               
                 1115 
                 PRO149 
                 CB 
                 4.31 
                 −0.075 
                 19.439 
               
               
                 1116 
                 PRO149 
                 CG 
                 4.261 
                 −1.43 
                 18.764 
               
               
                 1117 
                 PRO149 
                 CD 
                 3.122 
                 −1.352 
                 17.766 
               
               
                 1118 
                 VAL150 
                 N 
                 4.316 
                 2.051 
                 16.918 
               
               
                 1119 
                 VAL150 
                 CA 
                 4.873 
                 3.276 
                 16.323 
               
               
                 1120 
                 VAL150 
                 C 
                 3.867 
                 4.442 
                 16.385 
               
               
                 1121 
                 VAL150 
                 O 
                 4.127 
                 5.334 
                 17.201 
               
               
                 1122 
                 VAL150 
                 CB 
                 5.399 
                 3.041 
                 14.905 
               
               
                 1123 
                 VAL150 
                 CG1 
                 5.892 
                 4.345 
                 14.284 
               
               
                 1124 
                 VAL150 
                 CG2 
                 6.514 
                 2.004 
                 14.891 
               
               
                 1125 
                 PRO151 
                 N 
                 2.695 
                 4.396 
                 15.75 
               
               
                 1126 
                 PRO151 
                 CA 
                 1.816 
                 5.574 
                 15.799 
               
               
                 1127 
                 PRO151 
                 C 
                 1.187 
                 5.843 
                 17.167 
               
               
                 1128 
                 PRO151 
                 O 
                 1.009 
                 7.014 
                 17.532 
               
               
                 1129 
                 PRO151 
                 CB 
                 0.742 
                 5.307 
                 14.799 
               
               
                 1130 
                 PRO151 
                 CG 
                 0.88 
                 3.895 
                 14.266 
               
               
                 1131 
                 PRO151 
                 CD 
                 2.136 
                 3.336 
                 14.896 
               
               
                 1132 
                 SER152 
                 N 
                 1.059 
                 4.817 
                 17.993 
               
               
                 1133 
                 SER152 
                 CA 
                 0.504 
                 5.027 
                 19.326 
               
               
                 1134 
                 SER152 
                 C 
                 1.506 
                 5.73 
                 20.241 
               
               
                 1135 
                 SER152 
                 O 
                 1.136 
                 6.724 
                 20.879 
               
               
                 1136 
                 SER152 
                 CB 
                 0.117 
                 3.671 
                 19.898 
               
               
                 1137 
                 SER152 
                 OG 
                 −0.849 
                 3.09 
                 19.031 
               
               
                 1138 
                 LEU153 
                 N 
                 2.785 
                 5.428 
                 20.079 
               
               
                 1139 
                 LEU153 
                 CA 
                 3.817 
                 6.088 
                 20.883 
               
               
                 1140 
                 LEU153 
                 C 
                 4.17 
                 7.458 
                 20.312 
               
               
                 1141 
                 LEU153 
                 O 
                 4.34 
                 8.406 
                 21.091 
               
               
                 1142 
                 LEU153 
                 CB 
                 5.06 
                 5.206 
                 20.899 
               
               
                 1143 
                 LEU153 
                 CG 
                 6.168 
                 5.789 
                 21.769 
               
               
                 1144 
                 LEU153 
                 CD1 
                 5.708 
                 5.934 
                 23.216 
               
               
                 1145 
                 LEU153 
                 CD2 
                 7.424 
                 4.928 
                 21.689 
               
               
                 1146 
                 VAL154 
                 N 
                 3.995 
                 7.622 
                 19.009 
               
               
                 1147 
                 VAL154 
                 CA 
                 4.232 
                 8.925 
                 18.383 
               
               
                 1148 
                 VAL154 
                 C 
                 3.185 
                 9.944 
                 18.813 
               
               
                 1149 
                 VAL154 
                 O 
                 3.566 
                 11.036 
                 19.256 
               
               
                 1150 
                 VAL154 
                 CB 
                 4.205 
                 8.777 
                 16.864 
               
               
                 1151 
                 VAL154 
                 CG1 
                 4.148 
                 10.134 
                 16.169 
               
               
                 1152 
                 VAL154 
                 CG2 
                 5.402 
                 7.976 
                 16.368 
               
               
                 1153 
                 ILE155 
                 N 
                 1.945 
                 9.513 
                 18.977 
               
               
                 1154 
                 ILE155 
                 CA 
                 0.935 
                 10.467 
                 19.431 
               
               
                 1155 
                 ILE155 
                 C 
                 0.932 
                 10.621 
                 20.956 
               
               
                 1156 
                 ILE155 
                 O 
                 0.6 
                 11.709 
                 21.446 
               
               
                 1157 
                 ILE155 
                 CB 
                 −0.433 
                 10.065 
                 18.902 
               
               
                 1158 
                 ILE155 
                 CG1 
                 −1.405 
                 11.218 
                 19.089 
               
               
                 1159 
                 ILE155 
                 CG2 
                 −0.956 
                 8.814 
                 19.593 
               
               
                 1160 
                 ILE155 
                 CD1 
                 −0.954 
                 12.46 
                 18.327 
               
               
                 1161 
                 CYS156 
                 N 
                 1.569 
                 9.697 
                 21.66 
               
               
                 1162 
                 CYS156 
                 CA 
                 1.787 
                 9.891 
                 23.093 
               
               
                 1163 
                 CYS156 
                 C 
                 2.835 
                 10.973 
                 23.317 
               
               
                 1164 
                 CYS156 
                 O 
                 2.551 
                 11.93 
                 24.047 
               
               
                 1165 
                 CYS156 
                 CB 
                 2.261 
                 8.59 
                 23.732 
               
               
                 1166 
                 CYS156 
                 SG 
                 1.018 
                 7.295 
                 23.935 
               
               
                 1167 
                 GLU157 
                 N 
                 3.838 
                 11.005 
                 22.454 
               
               
                 1168 
                 GLU157 
                 CA 
                 4.902 
                 12.011 
                 22.559 
               
               
                 1169 
                 GLU157 
                 C 
                 4.512 
                 13.364 
                 21.957 
               
               
                 1170 
                 GLU157 
                 O 
                 5.08 
                 14.393 
                 22.339 
               
               
                 1171 
                 GLU157 
                 CB 
                 6.109 
                 11.474 
                 21.801 
               
               
                 1172 
                 GLU157 
                 CG 
                 6.57 
                 10.14 
                 22.372 
               
               
                 1173 
                 GLU157 
                 CD 
                 7.588 
                 9.499 
                 21.434 
               
               
                 1174 
                 GLU157 
                 OE1 
                 8.764 
                 9.522 
                 21.767 
               
               
                 1175 
                 GLU157 
                 OE2 
                 7.162 
                 8.932 
                 20.437 
               
               
                 1176 
                 LEU158 
                 N 
                 3.5 
                 13.37 
                 21.107 
               
               
                 1177 
                 LEU158 
                 CA 
                 3.042 
                 14.616 
                 20.492 
               
               
                 1178 
                 LEU158 
                 C 
                 2.03 
                 15.308 
                 21.401 
               
               
                 1179 
                 LEU158 
                 O 
                 2.089 
                 16.535 
                 21.586 
               
               
                 1180 
                 LEU158 
                 CB 
                 2.412 
                 14.232 
                 19.149 
               
               
                 1181 
                 LEU158 
                 CG 
                 2.171 
                 15.389 
                 18.175 
               
               
                 1182 
                 LEU158 
                 CD1 
                 2.086 
                 14.868 
                 16.745 
               
               
                 1183 
                 LEU158 
                 CD2 
                 0.93 
                 16.213 
                 18.504 
               
               
                 1184 
                 LEU159 
                 N 
                 1.211 
                 14.518 
                 22.072 
               
               
                 1185 
                 LEU159 
                 CA 
                 0.183 
                 15.099 
                 22.929 
               
               
                 1186 
                 LEU159 
                 C 
                 0.747 
                 15.411 
                 24.309 
               
               
                 1187 
                 LEU159 
                 O 
                 0.832 
                 16.594 
                 24.66 
               
               
                 1188 
                 LEU159 
                 CB 
                 −0.979 
                 14.12 
                 23.044 
               
               
                 1189 
                 LEU159 
                 CG 
                 −2.24 
                 14.827 
                 23.524 
               
               
                 1190 
                 LEU159 
                 CD1 
                 −2.637 
                 15.915 
                 22.535 
               
               
                 1191 
                 LEU159 
                 CD2 
                 −3.385 
                 13.84 
                 23.707 
               
               
                 1192 
                 GLY160 
                 N 
                 1.347 
                 14.417 
                 24.943 
               
               
                 1193 
                 GLY160 
                 CA 
                 1.874 
                 14.572 
                 26.306 
               
               
                 1194 
                 GLY160 
                 C 
                 1.433 
                 13.413 
                 27.2 
               
               
                 1195 
                 GLY160 
                 O 
                 1.183 
                 13.581 
                 28.398 
               
               
                 1196 
                 VAL161 
                 N 
                 1.366 
                 12.238 
                 26.601 
               
               
                 1197 
                 VAL161 
                 CA 
                 0.869 
                 11.037 
                 27.284 
               
               
                 1198 
                 VAL161 
                 C 
                 2.006 
                 10.078 
                 27.635 
               
               
                 1199 
                 VAL161 
                 O 
                 2.715 
                 9.58 
                 26.752 
               
               
                 1200 
                 VAL161 
                 CB 
                 −0.111 
                 10.348 
                 26.338 
               
               
                 1201 
                 VAL161 
                 CG1 
                 −0.763 
                 9.125 
                 26.976 
               
               
                 1202 
                 VAL161 
                 CG2 
                 −1.175 
                 11.327 
                 25.866 
               
               
                 1203 
                 PRO162 
                 N 
                 2.15 
                 9.806 
                 28.922 
               
               
                 1204 
                 PRO162 
                 CA 
                 3.13 
                 8.826 
                 29.4 
               
               
                 1205 
                 PRO162 
                 C 
                 2.838 
                 7.41 
                 28.901 
               
               
                 1206 
                 PRO162 
                 O 
                 1.68 
                 7.021 
                 28.689 
               
               
                 1207 
                 PRO162 
                 CB 
                 3.066 
                 8.899 
                 30.894 
               
               
                 1208 
                 PRO162 
                 CG 
                 1.972 
                 9.874 
                 31.302 
               
               
                 1209 
                 PRO162 
                 CD 
                 1.358 
                 10.384 
                 30.009 
               
               
                 1210 
                 TYR163 
                 N 
                 3.882 
                 6.593 
                 28.912 
               
               
                 1211 
                 TYR163 
                 CA 
                 3.793 
                 5.209 
                 28.41 
               
               
                 1212 
                 TYR163 
                 C 
                 3.104 
                 4.257 
                 29.393 
               
               
                 1213 
                 TYR163 
                 O 
                 2.72 
                 3.153 
                 29.002 
               
               
                 1214 
                 TYR163 
                 CB 
                 5.192 
                 4.684 
                 28.071 
               
               
                 1215 
                 TYR163 
                 CG 
                 6.111 
                 4.367 
                 29.254 
               
               
                 1216 
                 TYR163 
                 CD1 
                 6.895 
                 5.363 
                 29.826 
               
               
                 1217 
                 TYR163 
                 CD2 
                 6.181 
                 3.067 
                 29.743 
               
               
                 1218 
                 TYR163 
                 CE1 
                 7.726 
                 5.066 
                 30.898 
               
               
                 1219 
                 TYR163 
                 CE2 
                 7.011 
                 2.768 
                 30.815 
               
               
                 1220 
                 TYR163 
                 CZ 
                 7.78 
                 3.77 
                 31.392 
               
               
                 1221 
                 TYR163 
                 OH 
                 8.589 
                 3.478 
                 32.467 
               
               
                 1222 
                 SER164 
                 N 
                 2.806 
                 4.747 
                 30.589 
               
               
                 1223 
                 SER164 
                 CA 
                 2.007 
                 3.992 
                 31.561 
               
               
                 1224 
                 SER164 
                 C 
                 0.51 
                 4.158 
                 31.301 
               
               
                 1225 
                 SER164 
                 O 
                 −0.319 
                 3.566 
                 32 
               
               
                 1226 
                 SER164 
                 CB 
                 2.303 
                 4.538 
                 32.952 
               
               
                 1227 
                 SER164 
                 OG 
                 1.766 
                 5.854 
                 33.017 
               
               
                 1228 
                 ASP165 
                 N 
                 0.173 
                 5.056 
                 30.389 
               
               
                 1229 
                 ASP165 
                 CA 
                 −1.215 
                 5.273 
                 30.002 
               
               
                 1230 
                 ASP165 
                 C 
                 −1.445 
                 4.619 
                 28.649 
               
               
                 1231 
                 ASP165 
                 O 
                 −2.542 
                 4.126 
                 28.344 
               
               
                 1232 
                 ASP165 
                 CB 
                 −1.463 
                 6.775 
                 29.944 
               
               
                 1233 
                 ASP165 
                 CG 
                 −1.331 
                 7.38 
                 31.343 
               
               
                 1234 
                 ASP165 
                 OD1 
                 −2.358 
                 7.592 
                 31.968 
               
               
                 1235 
                 ASP165 
                 OD2 
                 −0.21 
                 7.683 
                 31.732 
               
               
                 1236 
                 HIS166 
                 N 
                 −0.343 
                 4.475 
                 27.929 
               
               
                 1237 
                 HIS166 
                 CA 
                 −0.299 
                 3.666 
                 26.71 
               
               
                 1238 
                 HIS166 
                 C 
                 −0.63 
                 2.223 
                 27.09 
               
               
                 1239 
                 HIS166 
                 O 
                 −0.515 
                 1.86 
                 28.266 
               
               
                 1240 
                 HIS166 
                 CB 
                 1.11 
                 3.792 
                 26.129 
               
               
                 1241 
                 HIS166 
                 CG 
                 1.387 
                 3.018 
                 24.856 
               
               
                 1242 
                 HIS166 
                 ND1 
                 0.916 
                 3.295 
                 23.626 
               
               
                 1243 
                 HIS166 
                 CD2 
                 2.174 
                 1.896 
                 24.741 
               
               
                 1244 
                 HIS166 
                 CE1 
                 1.378 
                 2.374 
                 22.756 
               
               
                 1245 
                 HIS166 
                 NE2 
                 2.156 
                 1.51 
                 23.445 
               
               
                 1246 
                 GLU167 
                 N 
                 −1.239 
                 1.506 
                 26.155 
               
               
                 1247 
                 GLU167 
                 CA 
                 −1.754 
                 0.127 
                 26.342 
               
               
                 1248 
                 GLU167 
                 C 
                 −3.12 
                 0.07 
                 27.045 
               
               
                 1249 
                 GLU167 
                 O 
                 −4.04 
                 −0.549 
                 26.498 
               
               
                 1250 
                 GLU167 
                 CB 
                 −0.743 
                 −0.752 
                 27.077 
               
               
                 1251 
                 GLU167 
                 CG 
                 0.54 
                 −0.919 
                 26.271 
               
               
                 1252 
                 GLU167 
                 CD 
                 1.593 
                 −1.638 
                 27.107 
               
               
                 1253 
                 GLU167 
                 OE1 
                 1.207 
                 −2.478 
                 27.907 
               
               
                 1254 
                 GLU167 
                 OE2 
                 2.766 
                 −1.386 
                 26.875 
               
               
                 1255 
                 PHE168 
                 N 
                 −3.329 
                 0.846 
                 28.097 
               
               
                 1256 
                 PHE168 
                 CA 
                 −4.652 
                 0.854 
                 28.729 
               
               
                 1257 
                 PHE168 
                 C 
                 −5.586 
                 1.779 
                 27.954 
               
               
                 1258 
                 PHE168 
                 O 
                 −6.692 
                 1.36 
                 27.587 
               
               
                 1259 
                 PHE168 
                 CB 
                 −4.53 
                 1.304 
                 30.179 
               
               
                 1260 
                 PHE168 
                 CG 
                 −5.824 
                 1.165 
                 30.977 
               
               
                 1261 
                 PHE168 
                 CD1 
                 −6.696 
                 0.117 
                 30.709 
               
               
                 1262 
                 PHE168 
                 CD2 
                 −6.126 
                 2.078 
                 31.979 
               
               
                 1263 
                 PHE168 
                 CE1 
                 −7.875 
                 −0.01 
                 31.432 
               
               
                 1264 
                 PHE168 
                 CE2 
                 −7.305 
                 1.951 
                 32.703 
               
               
                 1265 
                 PHE168 
                 CZ 
                 −8.18 
                 0.908 
                 32.428 
               
               
                 1266 
                 PHE169 
                 N 
                 −5.016 
                 2.851 
                 27.423 
               
               
                 1267 
                 PHE169 
                 CA 
                 −5.773 
                 3.717 
                 26.514 
               
               
                 1268 
                 PHE169 
                 C 
                 −5.944 
                 3.029 
                 25.162 
               
               
                 1269 
                 PHE169 
                 O 
                 −7.031 
                 3.098 
                 24.579 
               
               
                 1270 
                 PHE169 
                 CB 
                 −5.003 
                 5.024 
                 26.316 
               
               
                 1271 
                 PHE169 
                 CG 
                 −5.736 
                 6.088 
                 25.497 
               
               
                 1272 
                 PHE169 
                 CD1 
                 −6.361 
                 7.145 
                 26.147 
               
               
                 1273 
                 PHE169 
                 CD2 
                 −5.758 
                 6.022 
                 24.109 
               
               
                 1274 
                 PHE169 
                 CE1 
                 −7.037 
                 8.111 
                 25.413 
               
               
                 1275 
                 PHE169 
                 CE2 
                 −6.436 
                 6.985 
                 23.375 
               
               
                 1276 
                 PHE169 
                 CZ 
                 −7.082 
                 8.028 
                 24.027 
               
               
                 1277 
                 GLN170 
                 N 
                 −5.019 
                 2.134 
                 24.851 
               
               
                 1278 
                 GLN170 
                 CA 
                 −5.042 
                 1.407 
                 23.584 
               
               
                 1279 
                 GLN170 
                 C 
                 −6.148 
                 0.359 
                 23.564 
               
               
                 1280 
                 GLN170 
                 O 
                 −6.903 
                 0.281 
                 22.588 
               
               
                 1281 
                 GLN170 
                 CB 
                 −3.705 
                 0.693 
                 23.444 
               
               
                 1282 
                 GLN170 
                 CG 
                 −3.611 
                 −0.121 
                 22.163 
               
               
                 1283 
                 GLN170 
                 CD 
                 −3.411 
                 0.818 
                 20.985 
               
               
                 1284 
                 GLN170 
                 OE1 
                 −2.392 
                 1.516 
                 20.917 
               
               
                 1285 
                 GLN170 
                 NE2 
                 −4.408 
                 0.885 
                 20.125 
               
               
                 1286 
                 SER171 
                 N 
                 −6.372 
                 −0.281 
                 24.698 
               
               
                 1287 
                 SER171 
                 CA 
                 −7.424 
                 −1.295 
                 24.769 
               
               
                 1288 
                 SER171 
                 C 
                 −8.811 
                 −0.665 
                 24.856 
               
               
                 1289 
                 SER171 
                 O 
                 −9.706 
                 −1.107 
                 24.125 
               
               
                 1290 
                 SER171 
                 CB 
                 −7.171 
                 −2.209 
                 25.967 
               
               
                 1291 
                 SER171 
                 OG 
                 −7.132 
                 −1.427 
                 27.155 
               
               
                 1292 
                 CYS172 
                 N 
                 −8.906 
                 0.511 
                 25.457 
               
               
                 1293 
                 CYS172 
                 CA 
                 −10.204 
                 1.184 
                 25.525 
               
               
                 1294 
                 CYS172 
                 C 
                 −10.569 
                 1.806 
                 24.18 
               
               
                 1295 
                 CYS172 
                 O 
                 −11.691 
                 1.593 
                 23.703 
               
               
                 1296 
                 CYS172 
                 CB 
                 −10.149 
                 2.266 
                 26.593 
               
               
                 1297 
                 CYS172 
                 SG 
                 −9.817 
                 1.701 
                 28.277 
               
               
                 1298 
                 SER173 
                 N 
                 −9.559 
                 2.253 
                 23.453 
               
               
                 1299 
                 SER173 
                 CA 
                 −9.781 
                 2.826 
                 22.121 
               
               
                 1300 
                 SER173 
                 C 
                 −9.949 
                 1.765 
                 21.033 
               
               
                 1301 
                 SER173 
                 O 
                 −10.363 
                 2.096 
                 19.916 
               
               
                 1302 
                 SER173 
                 CB 
                 −8.612 
                 3.741 
                 21.775 
               
               
                 1303 
                 SER173 
                 OG 
                 −7.418 
                 2.972 
                 21.747 
               
               
                 1304 
                 SER174 
                 N 
                 −9.687 
                 0.509 
                 21.356 
               
               
                 1305 
                 SER174 
                 CA 
                 −10.001 
                 −0.575 
                 20.427 
               
               
                 1306 
                 SER174 
                 C 
                 −11.395 
                 −1.133 
                 20.713 
               
               
                 1307 
                 SER174 
                 O 
                 −12.128 
                 −1.464 
                 19.771 
               
               
                 1308 
                 SER174 
                 CB 
                 −8.949 
                 −1.668 
                 20.566 
               
               
                 1309 
                 SER174 
                 OG 
                 −7.691 
                 −1.099 
                 20.225 
               
               
                 1310 
                 ARG175 
                 N 
                 −11.85 
                 −0.974 
                 21.949 
               
               
                 1311 
                 ARG175 
                 CA 
                 −13.224 
                 −1.373 
                 22.294 
               
               
                 1312 
                 ARG175 
                 C 
                 −14.226 
                 −0.342 
                 21.787 
               
               
                 1313 
                 ARG175 
                 O 
                 −15.298 
                 −0.72 
                 21.298 
               
               
                 1314 
                 ARG175 
                 CB 
                 −13.371 
                 −1.514 
                 23.805 
               
               
                 1315 
                 ARG175 
                 CG 
                 −12.486 
                 −2.622 
                 24.36 
               
               
                 1316 
                 ARG175 
                 CD 
                 −12.761 
                 −2.871 
                 25.837 
               
               
                 1317 
                 ARG175 
                 NE 
                 −12.544 
                 −1.662 
                 26.646 
               
               
                 1318 
                 ARG175 
                 CZ 
                 −13.06 
                 −1.512 
                 27.869 
               
               
                 1319 
                 ARG175 
                 NH1 
                 −12.78 
                 −0.421 
                 28.584 
               
               
                 1320 
                 ARG175 
                 NH2 
                 −13.816 
                 −2.478 
                 28.397 
               
               
                 1321 
                 MET176 
                 N 
                 −13.739 
                 0.876 
                 21.611 
               
               
                 1322 
                 MET176 
                 CA 
                 −14.516 
                 1.951 
                 20.985 
               
               
                 1323 
                 MET176 
                 C 
                 −14.649 
                 1.843 
                 19.467 
               
               
                 1324 
                 MET176 
                 O 
                 −15.284 
                 2.71 
                 18.855 
               
               
                 1325 
                 MET176 
                 CB 
                 −13.806 
                 3.259 
                 21.259 
               
               
                 1326 
                 MET176 
                 CG 
                 −13.86 
                 3.657 
                 22.721 
               
               
                 1327 
                 MET176 
                 SD 
                 −13.036 
                 5.228 
                 23.009 
               
               
                 1328 
                 MET176 
                 CE 
                 −13.493 
                 5.972 
                 21.425 
               
               
                 1329 
                 LEU177 
                 N 
                 −14.036 
                 0.846 
                 18.853 
               
               
                 1330 
                 LEU177 
                 CA 
                 −14.184 
                 0.676 
                 17.411 
               
               
                 1331 
                 LEU177 
                 C 
                 −15.219 
                 −0.388 
                 17.059 
               
               
                 1332 
                 LEU177 
                 O 
                 −15.593 
                 −0.533 
                 15.886 
               
               
                 1333 
                 LEU177 
                 CB 
                 −12.836 
                 0.29 
                 16.827 
               
               
                 1334 
                 LEU177 
                 CG 
                 −11.824 
                 1.426 
                 16.9 
               
               
                 1335 
                 LEU177 
                 CD1 
                 −10.568 
                 1.035 
                 16.135 
               
               
                 1336 
                 LEU177 
                 CD2 
                 −12.4 
                 2.713 
                 16.32 
               
               
                 1337 
                 SER178 
                 N 
                 −15.706 
                 −1.099 
                 18.062 
               
               
                 1338 
                 SER178 
                 CA 
                 −16.693 
                 −2.149 
                 17.793 
               
               
                 1339 
                 SER178 
                 C 
                 −18.117 
                 −1.673 
                 18.08 
               
               
                 1340 
                 SER178 
                 O 
                 −18.628 
                 −1.797 
                 19.2 
               
               
                 1341 
                 SER178 
                 CB 
                 −16.344 
                 −3.402 
                 18.599 
               
               
                 1342 
                 SER178 
                 OG 
                 −16.323 
                 −3.095 
                 19.988 
               
               
                 1343 
                 ARG179 
                 N 
                 −18.765 
                 −1.209 
                 17.022 
               
               
                 1344 
                 ARG179 
                 CA 
                 −20.148 
                 −0.697 
                 17.082 
               
               
                 1345 
                 ARG179 
                 C 
                 −21.17 
                 −1.832 
                 17.192 
               
               
                 1346 
                 ARG179 
                 O 
                 −21.743 
                 −2.266 
                 16.187 
               
               
                 1347 
                 ARG179 
                 CB 
                 −20.4 
                 0.027 
                 15.768 
               
               
                 1348 
                 ARG179 
                 CG 
                 −19.286 
                 1.01 
                 15.431 
               
               
                 1349 
                 ARG179 
                 CD 
                 −19.098 
                 1.114 
                 13.922 
               
               
                 1350 
                 ARG179 
                 NE 
                 −18.628 
                 −0.179 
                 13.39 
               
               
                 1351 
                 ARG179 
                 CZ 
                 −19.337 
                 −0.967 
                 12.576 
               
               
                 1352 
                 ARG179 
                 NH1 
                 −18.903 
                 −2.2 
                 12.307 
               
               
                 1353 
                 ARG179 
                 NH2 
                 −20.546 
                 −0.583 
                 12.156 
               
               
                 1354 
                 GLU180 
                 N 
                 −21.375 
                 −2.313 
                 18.405 
               
               
                 1355 
                 GLU180 
                 CA 
                 −22.261 
                 −3.454 
                 18.627 
               
               
                 1356 
                 GLU180 
                 C 
                 −23.553 
                 −3.038 
                 19.318 
               
               
                 1357 
                 GLU180 
                 O 
                 −23.676 
                 −1.923 
                 19.833 
               
               
                 1358 
                 GLU180 
                 CB 
                 −21.517 
                 −4.449 
                 19.508 
               
               
                 1359 
                 GLU180 
                 CG 
                 −20.175 
                 −4.838 
                 18.899 
               
               
                 1360 
                 GLU180 
                 CD 
                 −19.442 
                 −5.795 
                 19.828 
               
               
                 1361 
                 GLU180 
                 OE1 
                 −20.124 
                 −6.592 
                 20.457 
               
               
                 1362 
                 GLU180 
                 OE2 
                 −18.219 
                 −5.763 
                 19.834 
               
               
                 1363 
                 VAL181 
                 N 
                 −24.492 
                 −3.969 
                 19.374 
               
               
                 1364 
                 VAL181 
                 CA 
                 −25.72 
                 −3.744 
                 20.147 
               
               
                 1365 
                 VAL181 
                 C 
                 −25.463 
                 −4.084 
                 21.616 
               
               
                 1366 
                 VAL181 
                 O 
                 −26.012 
                 −3.452 
                 22.525 
               
               
                 1367 
                 VAL181 
                 CB 
                 −26.823 
                 −4.627 
                 19.569 
               
               
                 1368 
                 VAL181 
                 CG1 
                 −28.119 
                 −4.498 
                 20.362 
               
               
                 1369 
                 VAL181 
                 CG2 
                 −27.062 
                 −4.297 
                 18.099 
               
               
                 1370 
                 THR182 
                 N 
                 −24.438 
                 −4.897 
                 21.822 
               
               
                 1371 
                 THR182 
                 CA 
                 −23.936 
                 −5.215 
                 23.166 
               
               
                 1372 
                 THR182 
                 C 
                 −22.767 
                 −4.302 
                 23.547 
               
               
                 1373 
                 THR182 
                 O 
                 −21.827 
                 −4.739 
                 24.222 
               
               
                 1374 
                 THR182 
                 CB 
                 −23.459 
                 −6.664 
                 23.183 
               
               
                 1375 
                 THR182 
                 OG1 
                 −22.348 
                 −6.789 
                 22.302 
               
               
                 1376 
                 THR182 
                 CG2 
                 −24.551 
                 −7.622 
                 22.719 
               
               
                 1377 
                 ALA183 
                 N 
                 −22.882 
                 −3.025 
                 23.214 
               
               
                 1378 
                 ALA183 
                 CA 
                 −21.777 
                 −2.062 
                 23.352 
               
               
                 1379 
                 ALA183 
                 C 
                 −21.585 
                 −1.459 
                 24.748 
               
               
                 1380 
                 ALA183 
                 O 
                 −21.031 
                 −0.36 
                 24.855 
               
               
                 1381 
                 ALA183 
                 CB 
                 −21.993 
                 −0.933 
                 22.352 
               
               
                 1382 
                 GLU184 
                 N 
                 −21.832 
                 −2.224 
                 25.799 
               
               
                 1383 
                 GLU184 
                 CA 
                 −21.706 
                 −1.688 
                 27.158 
               
               
                 1384 
                 GLU184 
                 C 
                 −20.242 
                 −1.537 
                 27.568 
               
               
                 1385 
                 GLU184 
                 O 
                 −19.888 
                 −0.536 
                 28.199 
               
               
                 1386 
                 GLU184 
                 CB 
                 −22.415 
                 −2.636 
                 28.117 
               
               
                 1387 
                 GLU184 
                 CG 
                 −22.387 
                 −2.118 
                 29.551 
               
               
                 1388 
                 GLU184 
                 CD 
                 −23.145 
                 −3.086 
                 30.454 
               
               
                 1389 
                 GLU184 
                 OE1 
                 −22.924 
                 −3.047 
                 31.655 
               
               
                 1390 
                 GLU184 
                 OE2 
                 −23.953 
                 −3.832 
                 29.917 
               
               
                 1391 
                 GLU185 
                 N 
                 −19.374 
                 −2.344 
                 26.978 
               
               
                 1392 
                 GLU185 
                 CA 
                 −17.936 
                 −2.201 
                 27.244 
               
               
                 1393 
                 GLU185 
                 C 
                 −17.307 
                 −1.143 
                 26.337 
               
               
                 1394 
                 GLU185 
                 O 
                 −16.294 
                 −0.542 
                 26.708 
               
               
                 1395 
                 GLU185 
                 CB 
                 −17.216 
                 −3.541 
                 27.073 
               
               
                 1396 
                 GLU185 
                 CG 
                 −17.189 
                 −4.388 
                 28.351 
               
               
                 1397 
                 GLU185 
                 CD 
                 −18.561 
                 −4.959 
                 28.705 
               
               
                 1398 
                 GLU185 
                 OE1 
                 −19.308 
                 −5.237 
                 27.774 
               
               
                 1399 
                 GLU185 
                 OE2 
                 −18.899 
                 −4.953 
                 29.879 
               
               
                 1400 
                 ARG186 
                 N 
                 −18.044 
                 −0.74 
                 25.316 
               
               
                 1401 
                 ARG186 
                 CA 
                 −17.607 
                 0.339 
                 24.434 
               
               
                 1402 
                 ARG186 
                 C 
                 −18.008 
                 1.676 
                 25.049 
               
               
                 1403 
                 ARG186 
                 O 
                 −17.213 
                 2.624 
                 25.056 
               
               
                 1404 
                 ARG186 
                 CB 
                 −18.317 
                 0.135 
                 23.103 
               
               
                 1405 
                 ARG186 
                 CG 
                 −17.936 
                 1.175 
                 22.064 
               
               
                 1406 
                 ARG186 
                 CD 
                 −18.718 
                 0.942 
                 20.779 
               
               
                 1407 
                 ARG186 
                 NE 
                 −18.234 
                 1.82 
                 19.708 
               
               
                 1408 
                 ARG186 
                 CZ 
                 −19.002 
                 2.705 
                 19.073 
               
               
                 1409 
                 ARG186 
                 NH1 
                 −20.296 
                 2.816 
                 19.386 
               
               
                 1410 
                 ARG186 
                 NH2 
                 −18.474 
                 3.477 
                 18.122 
               
               
                 1411 
                 MET187 
                 N 
                 −19.086 
                 1.627 
                 25.817 
               
               
                 1412 
                 MET187 
                 CA 
                 −19.545 
                 2.775 
                 26.601 
               
               
                 1413 
                 MET187 
                 C 
                 −18.651 
                 2.978 
                 27.82 
               
               
                 1414 
                 MET187 
                 O 
                 −18.251 
                 4.113 
                 28.111 
               
               
                 1415 
                 MET187 
                 CB 
                 −20.958 
                 2.459 
                 27.07 
               
               
                 1416 
                 MET187 
                 CG 
                 −21.569 
                 3.594 
                 27.88 
               
               
                 1417 
                 MET187 
                 SD 
                 −23.104 
                 3.161 
                 28.726 
               
               
                 1418 
                 MET187 
                 CE 
                 −23.995 
                 2.43 
                 27.333 
               
               
                 1419 
                 THR188 
                 N 
                 −18.13 
                 1.874 
                 28.332 
               
               
                 1420 
                 THR188 
                 CA 
                 −17.174 
                 1.925 
                 29.44 
               
               
                 1421 
                 THR188 
                 C 
                 −15.819 
                 2.442 
                 28.969 
               
               
                 1422 
                 THR188 
                 O 
                 −15.237 
                 3.307 
                 29.634 
               
               
                 1423 
                 THR188 
                 CB 
                 −17.013 
                 0.516 
                 30 
               
               
                 1424 
                 THR188 
                 OG1 
                 −18.274 
                 0.091 
                 30.499 
               
               
                 1425 
                 THR188 
                 CG2 
                 −16.011 
                 0.473 
                 31.149 
               
               
                 1426 
                 ALA189 
                 N 
                 −15.477 
                 2.139 
                 27.726 
               
               
                 1427 
                 ALA189 
                 CA 
                 −14.243 
                 2.652 
                 27.133 
               
               
                 1428 
                 ALA189 
                 C 
                 −14.333 
                 4.147 
                 26.838 
               
               
                 1429 
                 ALA189 
                 O 
                 −13.403 
                 4.884 
                 27.192 
               
               
                 1430 
                 ALA189 
                 CB 
                 −13.996 
                 1.884 
                 25.844 
               
               
                 1431 
                 PHE190 
                 N 
                 −15.518 
                 4.605 
                 26.461 
               
               
                 1432 
                 PHE190 
                 CA 
                 −15.762 
                 6.042 
                 26.26 
               
               
                 1433 
                 PHE190 
                 C 
                 −15.632 
                 6.81 
                 27.572 
               
               
                 1434 
                 PHE190 
                 O 
                 −14.815 
                 7.736 
                 27.678 
               
               
                 1435 
                 PHE190 
                 CB 
                 −17.194 
                 6.258 
                 25.773 
               
               
                 1436 
                 PHE190 
                 CG 
                 −17.566 
                 5.772 
                 24.375 
               
               
                 1437 
                 PHE190 
                 CD1 
                 −16.652 
                 5.837 
                 23.334 
               
               
                 1438 
                 PHE190 
                 CD2 
                 −18.848 
                 5.293 
                 24.139 
               
               
                 1439 
                 PHE190 
                 CE1 
                 −17.013 
                 5.406 
                 22.063 
               
               
                 1440 
                 PHE190 
                 CE2 
                 −19.208 
                 4.861 
                 22.871 
               
               
                 1441 
                 PHE190 
                 CZ 
                 −18.291 
                 4.917 
                 21.832 
               
               
                 1442 
                 GLU191 
                 N 
                 −16.281 
                 6.297 
                 28.605 
               
               
                 1443 
                 GLU191 
                 CA 
                 −16.292 
                 6.969 
                 29.908 
               
               
                 1444 
                 GLU191 
                 C 
                 −14.921 
                 6.971 
                 30.575 
               
               
                 1445 
                 GLU191 
                 O 
                 −14.432 
                 8.05 
                 30.936 
               
               
                 1446 
                 GLU191 
                 CB 
                 −17.28 
                 6.233 
                 30.802 
               
               
                 1447 
                 GLU191 
                 CG 
                 −17.348 
                 6.853 
                 32.193 
               
               
                 1448 
                 GLU191 
                 CD 
                 −18.28 
                 6.023 
                 33.069 
               
               
                 1449 
                 GLU191 
                 OE1 
                 −18.424 
                 4.843 
                 32.777 
               
               
                 1450 
                 GLU191 
                 OE2 
                 −18.894 
                 6.597 
                 33.957 
               
               
                 1451 
                 SER192 
                 N 
                 −14.202 
                 5.866 
                 30.453 
               
               
                 1452 
                 SER192 
                 CA 
                 −12.877 
                 5.76 
                 31.071 
               
               
                 1453 
                 SER192 
                 C 
                 −11.82 
                 6.545 
                 30.301 
               
               
                 1454 
                 SER192 
                 O 
                 −10.892 
                 7.077 
                 30.921 
               
               
                 1455 
                 SER192 
                 CB 
                 −12.467 
                 4.291 
                 31.126 
               
               
                 1456 
                 SER192 
                 OG 
                 −12.37 
                 3.801 
                 29.792 
               
               
                 1457 
                 LEU193 
                 N 
                 −12.082 
                 6.827 
                 29.036 
               
               
                 1458 
                 LEU193 
                 CA 
                 −11.152 
                 7.64 
                 28.256 
               
               
                 1459 
                 LEU193 
                 C 
                 −11.441 
                 9.127 
                 28.435 
               
               
                 1460 
                 LEU193 
                 O 
                 −10.514 
                 9.943 
                 28.377 
               
               
                 1461 
                 LEU193 
                 CB 
                 −11.243 
                 7.218 
                 26.798 
               
               
                 1462 
                 LEU193 
                 CG 
                 −9.95 
                 6.547 
                 26.343 
               
               
                 1463 
                 LEU193 
                 CD1 
                 −9.372 
                 5.603 
                 27.391 
               
               
                 1464 
                 LEU193 
                 CD2 
                 −10.117 
                 5.842 
                 25.003 
               
               
                 1465 
                 GLU194 
                 N 
                 −12.63 
                 9.438 
                 28.923 
               
               
                 1466 
                 GLU194 
                 CA 
                 −12.93 
                 10.811 
                 29.327 
               
               
                 1467 
                 GLU194 
                 C 
                 −12.368 
                 11.096 
                 30.711 
               
               
                 1468 
                 GLU194 
                 O 
                 −11.82 
                 12.182 
                 30.938 
               
               
                 1469 
                 GLU194 
                 CB 
                 −14.437 
                 11.017 
                 29.337 
               
               
                 1470 
                 GLU194 
                 CG 
                 −14.97 
                 11.164 
                 27.922 
               
               
                 1471 
                 GLU194 
                 CD 
                 −14.35 
                 12.405 
                 27.287 
               
               
                 1472 
                 GLU194 
                 OE1 
                 −13.524 
                 12.237 
                 26.403 
               
               
                 1473 
                 GLU194 
                 OE2 
                 −14.826 
                 13.487 
                 27.596 
               
               
                 1474 
                 ASN195 
                 N 
                 −12.26 
                 10.058 
                 31.523 
               
               
                 1475 
                 ASN195 
                 CA 
                 −11.645 
                 10.215 
                 32.844 
               
               
                 1476 
                 ASN195 
                 C 
                 −10.126 
                 10.268 
                 32.715 
               
               
                 1477 
                 ASN195 
                 O 
                 −9.479 
                 11.112 
                 33.356 
               
               
                 1478 
                 ASN195 
                 CB 
                 −12.076 
                 9.054 
                 33.736 
               
               
                 1479 
                 ASN195 
                 CG 
                 −13.582 
                 9.104 
                 34.008 
               
               
                 1480 
                 ASN195 
                 OD1 
                 −14.272 
                 8.076 
                 33.958 
               
               
                 1481 
                 ASN195 
                 ND2 
                 −14.076 
                 10.3 
                 34.287 
               
               
                 1482 
                 TYR196 
                 N 
                 −9.64 
                 9.613 
                 31.673 
               
               
                 1483 
                 TYR196 
                 CA 
                 −8.236 
                 9.692 
                 31.267 
               
               
                 1484 
                 TYR196 
                 C 
                 −7.88 
                 11.104 
                 30.817 
               
               
                 1485 
                 TYR196 
                 O 
                 −6.953 
                 11.707 
                 31.371 
               
               
                 1486 
                 TYR196 
                 CB 
                 −8.065 
                 8.757 
                 30.078 
               
               
                 1487 
                 TYR196 
                 CG 
                 −7.054 
                 7.633 
                 30.253 
               
               
                 1488 
                 TYR196 
                 CD1 
                 −5.806 
                 7.739 
                 29.658 
               
               
                 1489 
                 TYR196 
                 CD2 
                 −7.39 
                 6.5 
                 30.982 
               
               
                 1490 
                 TYR196 
                 CE1 
                 −4.884 
                 6.711 
                 29.799 
               
               
                 1491 
                 TYR196 
                 CE2 
                 −6.466 
                 5.472 
                 31.126 
               
               
                 1492 
                 TYR196 
                 CZ 
                 −5.216 
                 5.581 
                 30.532 
               
               
                 1493 
                 TYR196 
                 OH 
                 −4.301 
                 4.56 
                 30.661 
               
               
                 1494 
                 LEU197 
                 N 
                 −8.76 
                 11.708 
                 30.032 
               
               
                 1495 
                 LEU197 
                 CA 
                 −8.543 
                 13.084 
                 29.57 
               
               
                 1496 
                 LEU197 
                 C 
                 −8.718 
                 14.131 
                 30.663 
               
               
                 1497 
                 LEU197 
                 O 
                 −7.966 
                 15.11 
                 30.658 
               
               
                 1498 
                 LEU197 
                 CB 
                 −9.53 
                 13.394 
                 28.458 
               
               
                 1499 
                 LEU197 
                 CG 
                 −9.196 
                 12.63 
                 27.188 
               
               
                 1500 
                 LEU197 
                 CD1 
                 −10.305 
                 12.816 
                 26.168 
               
               
                 1501 
                 LEU197 
                 CD2 
                 −7.852 
                 13.072 
                 26.619 
               
               
                 1502 
                 ASP198 
                 N 
                 −9.49 
                 13.83 
                 31.695 
               
               
                 1503 
                 ASP198 
                 CA 
                 −9.6 
                 14.749 
                 32.834 
               
               
                 1504 
                 ASP198 
                 C 
                 −8.257 
                 14.841 
                 33.551 
               
               
                 1505 
                 ASP198 
                 O 
                 −7.698 
                 15.938 
                 33.694 
               
               
                 1506 
                 ASP198 
                 CB 
                 −10.627 
                 14.209 
                 33.829 
               
               
                 1507 
                 ASP198 
                 CG 
                 −12.016 
                 14.052 
                 33.214 
               
               
                 1508 
                 ASP198 
                 OD1 
                 −12.428 
                 14.949 
                 32.492 
               
               
                 1509 
                 ASP198 
                 OD2 
                 −12.706 
                 13.123 
                 33.627 
               
               
                 1510 
                 GLU199 
                 N 
                 −7.629 
                 13.685 
                 33.696 
               
               
                 1511 
                 GLU199 
                 CA 
                 −6.334 
                 13.598 
                 34.368 
               
               
                 1512 
                 GLU199 
                 C 
                 −5.221 
                 14.182 
                 33.506 
               
               
                 1513 
                 GLU199 
                 O 
                 −4.521 
                 15.091 
                 33.965 
               
               
                 1514 
                 GLU199 
                 CB 
                 −6.053 
                 12.121 
                 34.608 
               
               
                 1515 
                 GLU199 
                 CG 
                 −7.157 
                 11.486 
                 35.444 
               
               
                 1516 
                 GLU199 
                 CD 
                 −7.084 
                 9.966 
                 35.341 
               
               
                 1517 
                 GLU199 
                 OE1 
                 −7.502 
                 9.312 
                 36.287 
               
               
                 1518 
                 GLU199 
                 OE2 
                 −6.717 
                 9.484 
                 34.277 
               
               
                 1519 
                 LEU200 
                 N 
                 −5.26 
                 13.885 
                 32.219 
               
               
                 1520 
                 LEU200 
                 CA 
                 −4.209 
                 14.315 
                 31.289 
               
               
                 1521 
                 LEU200 
                 C 
                 −4.22 
                 15.821 
                 31.02 
               
               
                 1522 
                 LEU200 
                 O 
                 −3.168 
                 16.467 
                 31.128 
               
               
                 1523 
                 LEU200 
                 CB 
                 −4.459 
                 13.57 
                 29.982 
               
               
                 1524 
                 LEU200 
                 CG 
                 −3.421 
                 13.888 
                 28.914 
               
               
                 1525 
                 LEU200 
                 CD1 
                 −2.036 
                 13.415 
                 29.338 
               
               
                 1526 
                 LEU200 
                 CD2 
                 −3.815 
                 13.251 
                 27.587 
               
               
                 1527 
                 VAL201 
                 N 
                 −5.406 
                 16.402 
                 30.938 
               
               
                 1528 
                 VAL201 
                 CA 
                 −5.521 
                 17.832 
                 30.642 
               
               
                 1529 
                 VAL201 
                 C 
                 −5.196 
                 18.69 
                 31.859 
               
               
                 1530 
                 VAL201 
                 O 
                 −4.491 
                 19.7 
                 31.709 
               
               
                 1531 
                 VAL201 
                 CB 
                 −6.945 
                 18.094 
                 30.153 
               
               
                 1532 
                 VAL201 
                 CG1 
                 −7.324 
                 19.57 
                 30.184 
               
               
                 1533 
                 VAL201 
                 CG2 
                 −7.159 
                 17.508 
                 28.761 
               
               
                 1534 
                 THR202 
                 N 
                 −5.431 
                 18.149 
                 33.045 
               
               
                 1535 
                 THR202 
                 CA 
                 −5.103 
                 18.884 
                 34.267 
               
               
                 1536 
                 THR202 
                 C 
                 −3.643 
                 18.677 
                 34.654 
               
               
                 1537 
                 THR202 
                 O 
                 −2.981 
                 19.624 
                 35.101 
               
               
                 1538 
                 THR202 
                 CB 
                 −6.02 
                 18.391 
                 35.378 
               
               
                 1539 
                 THR202 
                 OG1 
                 −7.359 
                 18.589 
                 34.945 
               
               
                 1540 
                 THR202 
                 CG2 
                 −5.814 
                 19.173 
                 36.671 
               
               
                 1541 
                 LYS203 
                 N 
                 −3.08 
                 17.579 
                 34.182 
               
               
                 1542 
                 LYS203 
                 CA 
                 −1.672 
                 17.284 
                 34.434 
               
               
                 1543 
                 LYS203 
                 C 
                 −0.755 
                 18.113 
                 33.539 
               
               
                 1544 
                 LYS203 
                 O 
                 0.305 
                 18.539 
                 34.015 
               
               
                 1545 
                 LYS203 
                 CB 
                 −1.474 
                 15.79 
                 34.209 
               
               
                 1546 
                 LYS203 
                 CG 
                 −0.041 
                 15.331 
                 34.439 
               
               
                 1547 
                 LYS203 
                 CD 
                 0.025 
                 13.812 
                 34.569 
               
               
                 1548 
                 LYS203 
                 CE 
                 −0.557 
                 13.099 
                 33.352 
               
               
                 1549 
                 LYS203 
                 NZ 
                 0.265 
                 13.325 
                 32.154 
               
               
                 1550 
                 LYS204 
                 N 
                 −1.256 
                 18.545 
                 32.391 
               
               
                 1551 
                 LYS204 
                 CA 
                 −0.505 
                 19.493 
                 31.553 
               
               
                 1552 
                 LYS204 
                 C 
                 −0.788 
                 20.954 
                 31.896 
               
               
                 1553 
                 LYS204 
                 O 
                 −0.031 
                 21.846 
                 31.499 
               
               
                 1554 
                 LYS204 
                 CB 
                 −0.821 
                 19.218 
                 30.092 
               
               
                 1555 
                 LYS204 
                 CG 
                 −0.076 
                 17.965 
                 29.664 
               
               
                 1556 
                 LYS204 
                 CD 
                 1.425 
                 18.213 
                 29.729 
               
               
                 1557 
                 LYS204 
                 CE 
                 2.202 
                 16.906 
                 29.69 
               
               
                 1558 
                 LYS204 
                 NZ 
                 1.918 
                 16.115 
                 30.896 
               
               
                 1559 
                 GLU205 
                 N 
                 −1.781 
                 21.179 
                 32.741 
               
               
                 1560 
                 GLU205 
                 CA 
                 −2.033 
                 22.524 
                 33.264 
               
               
                 1561 
                 GLU205 
                 C 
                 −1.215 
                 22.777 
                 34.526 
               
               
                 1562 
                 GLU205 
                 O 
                 −1.027 
                 23.931 
                 34.927 
               
               
                 1563 
                 GLU205 
                 CB 
                 −3.518 
                 22.66 
                 33.57 
               
               
                 1564 
                 GLU205 
                 CG 
                 −4.309 
                 22.726 
                 32.273 
               
               
                 1565 
                 GLU205 
                 CD 
                 −5.788 
                 22.444 
                 32.51 
               
               
                 1566 
                 GLU205 
                 OE1 
                 −6.547 
                 22.661 
                 31.573 
               
               
                 1567 
                 GLU205 
                 OE2 
                 −6.093 
                 21.798 
                 33.504 
               
               
                 1568 
                 ALA206 
                 N 
                 −0.712 
                 21.707 
                 35.12 
               
               
                 1569 
                 ALA206 
                 CA 
                 0.208 
                 21.844 
                 36.249 
               
               
                 1570 
                 ALA206 
                 C 
                 1.649 
                 21.772 
                 35.756 
               
               
                 1571 
                 ALA206 
                 O 
                 2.464 
                 22.661 
                 36.034 
               
               
                 1572 
                 ALA206 
                 CB 
                 −0.059 
                 20.711 
                 37.233 
               
               
                 1573 
                 ASN207 
                 N 
                 1.92 
                 20.765 
                 34.945 
               
               
                 1574 
                 ASN207 
                 CA 
                 3.253 
                 20.587 
                 34.366 
               
               
                 1575 
                 ASN207 
                 C 
                 3.307 
                 21.204 
                 32.976 
               
               
                 1576 
                 ASN207 
                 O 
                 2.922 
                 20.574 
                 31.982 
               
               
                 1577 
                 ASN207 
                 CB 
                 3.568 
                 19.096 
                 34.27 
               
               
                 1578 
                 ASN207 
                 CG 
                 3.565 
                 18.441 
                 35.65 
               
               
                 1579 
                 ASN207 
                 OD1 
                 4.361 
                 18.793 
                 36.527 
               
               
                 1580 
                 ASN207 
                 ND2 
                 2.641 
                 17.515 
                 35.835 
               
               
                 1581 
                 ALA208 
                 N 
                 3.786 
                 22.435 
                 32.932 
               
               
                 1582 
                 ALA208 
                 CA 
                 3.924 
                 23.166 
                 31.668 
               
               
                 1583 
                 ALA208 
                 C 
                 5.045 
                 22.601 
                 30.795 
               
               
                 1584 
                 ALA208 
                 O 
                 6.235 
                 22.809 
                 31.052 
               
               
                 1585 
                 ALA208 
                 CB 
                 4.202 
                 24.631 
                 31.982 
               
               
                 1586 
                 THR209 
                 N 
                 4.636 
                 21.874 
                 29.77 
               
               
                 1587 
                 THR209 
                 CA 
                 5.581 
                 21.251 
                 28.834 
               
               
                 1588 
                 THR209 
                 C 
                 5.499 
                 21.873 
                 27.446 
               
               
                 1589 
                 THR209 
                 O 
                 4.665 
                 22.737 
                 27.168 
               
               
                 1590 
                 THR209 
                 CB 
                 5.253 
                 19.774 
                 28.706 
               
               
                 1591 
                 THR209 
                 OG1 
                 3.938 
                 19.693 
                 28.18 
               
               
                 1592 
                 THR209 
                 CG2 
                 5.296 
                 19.059 
                 30.052 
               
               
                 1593 
                 GLU210 
                 N 
                 6.34 
                 21.363 
                 26.562 
               
               
                 1594 
                 GLU210 
                 CA 
                 6.411 
                 21.861 
                 25.18 
               
               
                 1595 
                 GLU210 
                 C 
                 5.542 
                 21.076 
                 24.19 
               
               
                 1596 
                 GLU210 
                 O 
                 5.586 
                 21.361 
                 22.989 
               
               
                 1597 
                 GLU210 
                 CB 
                 7.861 
                 21.818 
                 24.692 
               
               
                 1598 
                 GLU210 
                 CG 
                 8.791 
                 22.752 
                 25.467 
               
               
                 1599 
                 GLU210 
                 CD 
                 9.689 
                 21.967 
                 26.424 
               
               
                 1600 
                 GLU210 
                 OE1 
                 9.258 
                 20.906 
                 26.861 
               
               
                 1601 
                 GLU210 
                 OE2 
                 10.778 
                 22.442 
                 26.707 
               
               
                 1602 
                 ASP211 
                 N 
                 4.786 
                 20.097 
                 24.662 
               
               
                 1603 
                 ASP211 
                 CA 
                 3.977 
                 19.273 
                 23.746 
               
               
                 1604 
                 ASP211 
                 C 
                 2.732 
                 20.003 
                 23.249 
               
               
                 1605 
                 ASP211 
                 O 
                 2.331 
                 21.027 
                 23.817 
               
               
                 1606 
                 ASP211 
                 CB 
                 3.605 
                 17.956 
                 24.418 
               
               
                 1607 
                 ASP211 
                 CG 
                 2.942 
                 18.154 
                 25.781 
               
               
                 1608 
                 ASP211 
                 OD1 
                 2.12 
                 19.054 
                 25.925 
               
               
                 1609 
                 ASP211 
                 OD2 
                 3.336 
                 17.427 
                 26.681 
               
               
                 1610 
                 ASP212 
                 N 
                 2.034 
                 19.382 
                 22.309 
               
               
                 1611 
                 ASP212 
                 CA 
                 0.906 
                 20.044 
                 21.64 
               
               
                 1612 
                 ASP212 
                 C 
                 −0.365 
                 20.067 
                 22.496 
               
               
                 1613 
                 ASP212 
                 O 
                 −1.223 
                 20.928 
                 22.262 
               
               
                 1614 
                 ASP212 
                 CB 
                 0.653 
                 19.331 
                 20.312 
               
               
                 1615 
                 ASP212 
                 CG 
                 −0.355 
                 20.078 
                 19.435 
               
               
                 1616 
                 ASP212 
                 OD1 
                 −0.505 
                 21.277 
                 19.623 
               
               
                 1617 
                 ASP212 
                 OD2 
                 −1.022 
                 19.415 
                 18.653 
               
               
                 1618 
                 LEU213 
                 N 
                 −0.398 
                 19.318 
                 23.589 
               
               
                 1619 
                 LEU213 
                 CA 
                 −1.529 
                 19.451 
                 24.508 
               
               
                 1620 
                 LEU213 
                 C 
                 −1.474 
                 20.819 
                 25.18 
               
               
                 1621 
                 LEU213 
                 O 
                 −2.372 
                 21.628 
                 24.907 
               
               
                 1622 
                 LEU213 
                 CB 
                 −1.498 
                 18.346 
                 25.557 
               
               
                 1623 
                 LEU213 
                 CG 
                 −2.75 
                 18.365 
                 26.427 
               
               
                 1624 
                 LEU213 
                 CD1 
                 −4.011 
                 18.334 
                 25.574 
               
               
                 1625 
                 LEU213 
                 CD2 
                 −2.751 
                 17.202 
                 27.41 
               
               
                 1626 
                 LEU214 
                 N 
                 −0.306 
                 21.193 
                 25.691 
               
               
                 1627 
                 LEU214 
                 CA 
                 −0.187 
                 22.52 
                 26.307 
               
               
                 1628 
                 LEU214 
                 C 
                 −0.094 
                 23.607 
                 25.241 
               
               
                 1629 
                 LEU214 
                 O 
                 −0.613 
                 24.711 
                 25.445 
               
               
                 1630 
                 LEU214 
                 CB 
                 1.034 
                 22.608 
                 27.21 
               
               
                 1631 
                 LEU214 
                 CG 
                 0.987 
                 23.94 
                 27.954 
               
               
                 1632 
                 LEU214 
                 CD1 
                 −0.18 
                 23.972 
                 28.934 
               
               
                 1633 
                 LEU214 
                 CD2 
                 2.288 
                 24.25 
                 28.671 
               
               
                 1634 
                 GLY215 
                 N 
                 0.35 
                 23.222 
                 24.056 
               
               
                 1635 
                 GLY215 
                 CA 
                 0.292 
                 24.093 
                 22.882 
               
               
                 1636 
                 GLY215 
                 C 
                 −1.121 
                 24.618 
                 22.629 
               
               
                 1637 
                 GLY215 
                 O 
                 −1.327 
                 25.838 
                 22.586 
               
               
                 1638 
                 ARG216 
                 N 
                 −2.103 
                 23.733 
                 22.582 
               
               
                 1639 
                 ARG216 
                 CA 
                 −3.473 
                 24.198 
                 22.351 
               
               
                 1640 
                 ARG216 
                 C 
                 −4.154 
                 24.727 
                 23.616 
               
               
                 1641 
                 ARG216 
                 O 
                 −5.077 
                 25.542 
                 23.506 
               
               
                 1642 
                 ARG216 
                 CB 
                 −4.3 
                 23.068 
                 21.765 
               
               
                 1643 
                 ARG216 
                 CG 
                 −3.636 
                 22.456 
                 20.539 
               
               
                 1644 
                 ARG216 
                 CD 
                 −4.555 
                 21.415 
                 19.912 
               
               
                 1645 
                 ARG216 
                 NE 
                 −5.402 
                 20.812 
                 20.953 
               
               
                 1646 
                 ARG216 
                 CZ 
                 −5.073 
                 19.756 
                 21.699 
               
               
                 1647 
                 ARG216 
                 NH1 
                 −3.937 
                 19.093 
                 21.471 
               
               
                 1648 
                 ARG216 
                 NH2 
                 −5.905 
                 19.342 
                 22.652 
               
               
                 1649 
                 GLN217 
                 N 
                 −3.583 
                 24.445 
                 24.776 
               
               
                 1650 
                 GLN217 
                 CA 
                 −4.102 
                 25.002 
                 26.031 
               
               
                 1651 
                 GLN217 
                 C 
                 −3.624 
                 26.435 
                 26.28 
               
               
                 1652 
                 GLN217 
                 O 
                 −4.198 
                 27.131 
                 27.125 
               
               
                 1653 
                 GLN217 
                 CB 
                 −3.648 
                 24.109 
                 27.181 
               
               
                 1654 
                 GLN217 
                 CG 
                 −4.235 
                 22.711 
                 27.043 
               
               
                 1655 
                 GLN217 
                 CD 
                 −3.691 
                 21.772 
                 28.114 
               
               
                 1656 
                 GLN217 
                 OE1 
                 −2.544 
                 21.311 
                 28.052 
               
               
                 1657 
                 GLN217 
                 NE2 
                 −4.552 
                 21.446 
                 29.059 
               
               
                 1658 
                 ILE218 
                 N 
                 −2.608 
                 26.875 
                 25.551 
               
               
                 1659 
                 ILE218 
                 CA 
                 −2.179 
                 28.276 
                 25.625 
               
               
                 1660 
                 ILE218 
                 C 
                 −2.638 
                 29.086 
                 24.409 
               
               
                 1661 
                 ILE218 
                 O 
                 −2.242 
                 30.25 
                 24.267 
               
               
                 1662 
                 ILE218 
                 CB 
                 −0.66 
                 28.352 
                 25.774 
               
               
                 1663 
                 ILE218 
                 CG1 
                 0.061 
                 27.755 
                 24.572 
               
               
                 1664 
                 ILE218 
                 CG2 
                 −0.211 
                 27.665 
                 27.059 
               
               
                 1665 
                 ILE218 
                 CD1 
                 1.574 
                 27.781 
                 24.754 
               
               
                 1666 
                 LEU219 
                 N 
                 −3.431 
                 28.478 
                 23.538 
               
               
                 1667 
                 LEU219 
                 CA 
                 −3.953 
                 29.194 
                 22.365 
               
               
                 1668 
                 LEU219 
                 C 
                 −4.858 
                 30.352 
                 22.75 
               
               
                 1669 
                 LEU219 
                 O 
                 −5.716 
                 30.229 
                 23.629 
               
               
                 1670 
                 LEU219 
                 CB 
                 −4.756 
                 28.24 
                 21.493 
               
               
                 1671 
                 LEU219 
                 CG 
                 −3.859 
                 27.411 
                 20.59 
               
               
                 1672 
                 LEU219 
                 CD1 
                 −4.674 
                 26.345 
                 19.873 
               
               
                 1673 
                 LEU219 
                 CD2 
                 −3.135 
                 28.304 
                 19.588 
               
               
                 1674 
                 LYS220 
                 N 
                 −4.667 
                 31.454 
                 22.047 
               
               
                 1675 
                 LYS220 
                 CA 
                 −5.484 
                 32.654 
                 22.234 
               
               
                 1676 
                 LYS220 
                 C 
                 −5.341 
                 33.562 
                 21.012 
               
               
                 1677 
                 LYS220 
                 O 
                 −4.556 
                 34.519 
                 21.016 
               
               
                 1678 
                 LYS220 
                 CB 
                 −5.01 
                 33.38 
                 23.489 
               
               
                 1679 
                 LYS220 
                 CG 
                 −5.91 
                 34.56 
                 23.842 
               
               
                 1680 
                 LYS220 
                 CD 
                 −5.389 
                 35.289 
                 25.074 
               
               
                 1681 
                 LYS220 
                 CE 
                 −6.258 
                 36.494 
                 25.418 
               
               
                 1682 
                 LYS220 
                 NZ 
                 −5.74 
                 37.191 
                 26.607 
               
               
                 1683 
                 GLN221 
                 N 
                 −6.048 
                 33.217 
                 19.951 
               
               
                 1684 
                 GLN221 
                 CA 
                 −5.987 
                 34.031 
                 18.732 
               
               
                 1685 
                 GLN221 
                 C 
                 −6.904 
                 35.234 
                 18.892 
               
               
                 1686 
                 GLN221 
                 O 
                 −7.981 
                 35.112 
                 19.48 
               
               
                 1687 
                 GLN221 
                 CB 
                 −6.389 
                 33.179 
                 17.535 
               
               
                 1688 
                 GLN221 
                 CG 
                 −5.417 
                 32.015 
                 17.369 
               
               
                 1689 
                 GLN221 
                 CD 
                 −5.828 
                 31.088 
                 16.227 
               
               
                 1690 
                 GLN221 
                 OE1 
                 −7.019 
                 30.872 
                 15.966 
               
               
                 1691 
                 GLN221 
                 NE2 
                 −4.823 
                 30.508 
                 15.595 
               
               
                 1692 
                 ARG222 
                 N 
                 −6.553 
                 36.345 
                 18.268 
               
               
                 1693 
                 ARG222 
                 CA 
                 −7.309 
                 37.589 
                 18.486 
               
               
                 1694 
                 ARG222 
                 C 
                 −8.774 
                 37.467 
                 18.066 
               
               
                 1695 
                 ARG222 
                 O 
                 −9.669 
                 37.72 
                 18.877 
               
               
                 1696 
                 ARG222 
                 CB 
                 −6.649 
                 38.705 
                 17.685 
               
               
                 1697 
                 ARG222 
                 CG 
                 −7.362 
                 40.034 
                 17.911 
               
               
                 1698 
                 ARG222 
                 CD 
                 −6.787 
                 41.134 
                 17.026 
               
               
                 1699 
                 ARG222 
                 NE 
                 −7.505 
                 42.401 
                 17.232 
               
               
                 1700 
                 ARG222 
                 CZ 
                 −8.368 
                 42.909 
                 16.349 
               
               
                 1701 
                 ARG222 
                 NH1 
                 −8.626 
                 42.255 
                 15.213 
               
               
                 1702 
                 ARG222 
                 NH2 
                 −8.98 
                 44.068 
                 16.604 
               
               
                 1703 
                 GLU223 
                 N 
                 −9.009 
                 36.864 
                 16.912 
               
               
                 1704 
                 GLU223 
                 CA 
                 −10.382 
                 36.702 
                 16.426 
               
               
                 1705 
                 GLU223 
                 C 
                 −10.985 
                 35.329 
                 16.735 
               
               
                 1706 
                 GLU223 
                 O 
                 −12.083 
                 35.029 
                 16.257 
               
               
                 1707 
                 GLU223 
                 CB 
                 −10.395 
                 36.959 
                 14.926 
               
               
                 1708 
                 GLU223 
                 CG 
                 −9.977 
                 38.396 
                 14.634 
               
               
                 1709 
                 GLU223 
                 CD 
                 −9.946 
                 38.649 
                 13.13 
               
               
                 1710 
                 GLU223 
                 OE1 
                 −9.041 
                 39.35 
                 12.701 
               
               
                 1711 
                 GLU223 
                 OE2 
                 −10.749 
                 38.047 
                 12.434 
               
               
                 1712 
                 SER224 
                 N 
                 −10.28 
                 34.5 
                 17.488 
               
               
                 1713 
                 SER224 
                 CA 
                 −10.803 
                 33.162 
                 17.775 
               
               
                 1714 
                 SER224 
                 C 
                 −11.036 
                 32.957 
                 19.266 
               
               
                 1715 
                 SER224 
                 O 
                 −11.791 
                 32.067 
                 19.67 
               
               
                 1716 
                 SER224 
                 CB 
                 −9.789 
                 32.13 
                 17.308 
               
               
                 1717 
                 SER224 
                 OG 
                 −9.509 
                 32.374 
                 15.941 
               
               
                 1718 
                 GLY225 
                 N 
                 −10.409 
                 33.796 
                 20.069 
               
               
                 1719 
                 GLY225 
                 CA 
                 −10.436 
                 33.613 
                 21.517 
               
               
                 1720 
                 GLY225 
                 C 
                 −9.539 
                 32.435 
                 21.884 
               
               
                 1721 
                 GLY225 
                 O 
                 −8.577 
                 32.109 
                 21.174 
               
               
                 1722 
                 GLU226 
                 N 
                 −9.863 
                 31.807 
                 22.998 
               
               
                 1723 
                 GLU226 
                 CA 
                 −9.128 
                 30.613 
                 23.422 
               
               
                 1724 
                 GLU226 
                 C 
                 −10.067 
                 29.417 
                 23.535 
               
               
                 1725 
                 GLU226 
                 O 
                 −11.22 
                 29.553 
                 23.963 
               
               
                 1726 
                 GLU226 
                 CB 
                 −8.424 
                 30.894 
                 24.745 
               
               
                 1727 
                 GLU226 
                 CG 
                 −9.368 
                 31.316 
                 25.86 
               
               
                 1728 
                 GLU226 
                 CD 
                 −8.548 
                 31.714 
                 27.084 
               
               
                 1729 
                 GLU226 
                 OE1 
                 −8.364 
                 30.873 
                 27.952 
               
               
                 1730 
                 GLU226 
                 OE2 
                 −8.166 
                 32.875 
                 27.147 
               
               
                 1731 
                 ALA227 
                 N 
                 −9.567 
                 28.262 
                 23.127 
               
               
                 1732 
                 ALA227 
                 CA 
                 −10.372 
                 27.035 
                 23.163 
               
               
                 1733 
                 ALA227 
                 C 
                 −10.725 
                 26.657 
                 24.598 
               
               
                 1734 
                 ALA227 
                 O 
                 −9.859 
                 26.603 
                 25.477 
               
               
                 1735 
                 ALA227 
                 CB 
                 −9.587 
                 25.904 
                 22.508 
               
               
                 1736 
                 ASP228 
                 N 
                 −12.009 
                 26.456 
                 24.833 
               
               
                 1737 
                 ASP228 
                 CA 
                 −12.471 
                 26.085 
                 26.175 
               
               
                 1738 
                 ASP228 
                 C 
                 −12.163 
                 24.618 
                 26.455 
               
               
                 1739 
                 ASP228 
                 O 
                 −11.944 
                 23.836 
                 25.52 
               
               
                 1740 
                 ASP228 
                 CB 
                 −13.961 
                 26.399 
                 26.323 
               
               
                 1741 
                 ASP228 
                 CG 
                 −14.816 
                 25.698 
                 25.268 
               
               
                 1742 
                 ASP228 
                 OD1 
                 −14.745 
                 24.475 
                 25.201 
               
               
                 1743 
                 ASP228 
                 OD2 
                 −15.656 
                 26.364 
                 24.686 
               
               
                 1744 
                 HIS229 
                 N 
                 −12.329 
                 24.215 
                 27.704 
               
               
                 1745 
                 HIS229 
                 CA 
                 −11.958 
                 22.854 
                 28.129 
               
               
                 1746 
                 HIS229 
                 C 
                 −12.84 
                 21.733 
                 27.559 
               
               
                 1747 
                 HIS229 
                 O 
                 −12.334 
                 20.622 
                 27.37 
               
               
                 1748 
                 HIS229 
                 CB 
                 −11.971 
                 22.807 
                 29.658 
               
               
                 1749 
                 HIS229 
                 CG 
                 −13.265 
                 23.255 
                 30.319 
               
               
                 1750 
                 HIS229 
                 ND1 
                 −14.34 
                 22.487 
                 30.584 
               
               
                 1751 
                 HIS229 
                 CD2 
                 −13.557 
                 24.519 
                 30.78 
               
               
                 1752 
                 HIS229 
                 CE1 
                 −15.293 
                 23.238 
                 31.171 
               
               
                 1753 
                 HIS229 
                 NE2 
                 −14.808 
                 24.494 
                 31.292 
               
               
                 1754 
                 GLY230 
                 N 
                 −14.024 
                 22.066 
                 27.068 
               
               
                 1755 
                 GLY230 
                 CA 
                 −14.88 
                 21.073 
                 26.412 
               
               
                 1756 
                 GLY230 
                 C 
                 −14.27 
                 20.684 
                 25.07 
               
               
                 1757 
                 GLY230 
                 O 
                 −13.958 
                 19.508 
                 24.84 
               
               
                 1758 
                 GLU231 
                 N 
                 −13.866 
                 21.704 
                 24.329 
               
               
                 1759 
                 GLU231 
                 CA 
                 −13.239 
                 21.508 
                 23.021 
               
               
                 1760 
                 GLU231 
                 C 
                 −11.809 
                 21.001 
                 23.152 
               
               
                 1761 
                 GLU231 
                 O 
                 −11.365 
                 20.21 
                 22.315 
               
               
                 1762 
                 GLU231 
                 CB 
                 −13.196 
                 22.856 
                 22.318 
               
               
                 1763 
                 GLU231 
                 CG 
                 −14.589 
                 23.417 
                 22.086 
               
               
                 1764 
                 GLU231 
                 CD 
                 −14.471 
                 24.888 
                 21.707 
               
               
                 1765 
                 GLU231 
                 OE1 
                 −15.12 
                 25.296 
                 20.756 
               
               
                 1766 
                 GLU231 
                 OE2 
                 −13.758 
                 25.592 
                 22.418 
               
               
                 1767 
                 LEU232 
                 N 
                 −11.181 
                 21.28 
                 24.281 
               
               
                 1768 
                 LEU232 
                 CA 
                 −9.822 
                 20.803 
                 24.524 
               
               
                 1769 
                 LEU232 
                 C 
                 −9.841 
                 19.292 
                 24.755 
               
               
                 1770 
                 LEU232 
                 O 
                 −9.061 
                 18.578 
                 24.112 
               
               
                 1771 
                 LEU232 
                 CB 
                 −9.297 
                 21.541 
                 25.756 
               
               
                 1772 
                 LEU232 
                 CG 
                 −7.777 
                 21.685 
                 25.784 
               
               
                 1773 
                 LEU232 
                 CD1 
                 −7.057 
                 20.385 
                 26.124 
               
               
                 1774 
                 LEU232 
                 CD2 
                 −7.256 
                 22.293 
                 24.486 
               
               
                 1775 
                 VAL233 
                 N 
                 −10.877 
                 18.804 
                 25.419 
               
               
                 1776 
                 VAL233 
                 CA 
                 −11.016 
                 17.36 
                 25.627 
               
               
                 1777 
                 VAL233 
                 C 
                 −11.406 
                 16.646 
                 24.331 
               
               
                 1778 
                 VAL233 
                 O 
                 −10.729 
                 15.676 
                 23.963 
               
               
                 1779 
                 VAL233 
                 CB 
                 −12.066 
                 17.13 
                 26.71 
               
               
                 1780 
                 VAL233 
                 CG1 
                 −12.478 
                 15.667 
                 26.802 
               
               
                 1781 
                 VAL233 
                 CG2 
                 −11.571 
                 17.632 
                 28.062 
               
               
                 1782 
                 GLY234 
                 N 
                 −12.258 
                 17.278 
                 23.536 
               
               
                 1783 
                 GLY234 
                 CA 
                 −12.641 
                 16.729 
                 22.227 
               
               
                 1784 
                 GLY234 
                 C 
                 −11.443 
                 16.59 
                 21.287 
               
               
                 1785 
                 GLY234 
                 O 
                 −11.116 
                 15.477 
                 20.849 
               
               
                 1786 
                 LEU235 
                 N 
                 −10.687 
                 17.668 
                 21.146 
               
               
                 1787 
                 LEU235 
                 CA 
                 −9.532 
                 17.691 
                 20.238 
               
               
                 1788 
                 LEU235 
                 C 
                 −8.375 
                 16.809 
                 20.702 
               
               
                 1789 
                 LEU235 
                 O 
                 −7.846 
                 16.046 
                 19.882 
               
               
                 1790 
                 LEU235 
                 CB 
                 −9.04 
                 19.13 
                 20.146 
               
               
                 1791 
                 LEU235 
                 CG 
                 −10.08 
                 20.034 
                 19.495 
               
               
                 1792 
                 LEU235 
                 CD1 
                 −9.781 
                 21.505 
                 19.761 
               
               
                 1793 
                 LEU235 
                 CD2 
                 −10.2 
                 19.75 
                 18.003 
               
               
                 1794 
                 ALA236 
                 N 
                 −8.162 
                 16.713 
                 22.006 
               
               
                 1795 
                 ALA236 
                 CA 
                 −7.065 
                 15.885 
                 22.523 
               
               
                 1796 
                 ALA236 
                 C 
                 −7.38 
                 14.407 
                 22.375 
               
               
                 1797 
                 ALA236 
                 O 
                 −6.525 
                 13.633 
                 21.922 
               
               
                 1798 
                 ALA236 
                 CB 
                 −6.861 
                 16.193 
                 24.002 
               
               
                 1799 
                 PHE237 
                 N 
                 −8.66 
                 14.095 
                 22.475 
               
               
                 1800 
                 PHE237 
                 CA 
                 −9.11 
                 12.723 
                 22.306 
               
               
                 1801 
                 PHE237 
                 C 
                 −8.956 
                 12.273 
                 20.864 
               
               
                 1802 
                 PHE237 
                 O 
                 −8.27 
                 11.274 
                 20.617 
               
               
                 1803 
                 PHE237 
                 CB 
                 −10.58 
                 12.657 
                 22.682 
               
               
                 1804 
                 PHE237 
                 CG 
                 −11.12 
                 11.24 
                 22.674 
               
               
                 1805 
                 PHE237 
                 CD1 
                 −10.824 
                 10.394 
                 23.733 
               
               
                 1806 
                 PHE237 
                 CD2 
                 −11.885 
                 10.786 
                 21.608 
               
               
                 1807 
                 PHE237 
                 CE1 
                 −11.305 
                 9.095 
                 23.736 
               
               
                 1808 
                 PHE237 
                 CE2 
                 −12.366 
                 9.486 
                 21.61 
               
               
                 1809 
                 PHE237 
                 CZ 
                 −12.076 
                 8.644 
                 22.676 
               
               
                 1810 
                 LEU238 
                 N 
                 −9.329 
                 13.135 
                 19.931 
               
               
                 1811 
                 LEU238 
                 CA 
                 −9.272 
                 12.754 
                 18.516 
               
               
                 1812 
                 LEU238 
                 C 
                 −7.845 
                 12.681 
                 17.984 
               
               
                 1813 
                 LEU238 
                 O 
                 −7.532 
                 11.745 
                 17.236 
               
               
                 1814 
                 LEU238 
                 CB 
                 −10.056 
                 13.766 
                 17.695 
               
               
                 1815 
                 LEU238 
                 CG 
                 −11.539 
                 13.75 
                 18.042 
               
               
                 1816 
                 LEU238 
                 CD1 
                 −12.279 
                 14.795 
                 17.221 
               
               
                 1817 
                 LEU238 
                 CD2 
                 −12.145 
                 12.369 
                 17.814 
               
               
                 1818 
                 LEU239 
                 N 
                 −6.947 
                 13.467 
                 18.554 
               
               
                 1819 
                 LEU239 
                 CA 
                 −5.551 
                 13.397 
                 18.122 
               
               
                 1820 
                 LEU239 
                 C 
                 −4.861 
                 12.158 
                 18.68 
               
               
                 1821 
                 LEU239 
                 O 
                 −4.202 
                 11.444 
                 17.913 
               
               
                 1822 
                 LEU239 
                 CB 
                 −4.821 
                 14.652 
                 18.586 
               
               
                 1823 
                 LEU239 
                 CG 
                 −5.364 
                 15.898 
                 17.894 
               
               
                 1824 
                 LEU239 
                 CD1 
                 −4.722 
                 17.162 
                 18.454 
               
               
                 1825 
                 LEU239 
                 CD2 
                 −5.169 
                 15.82 
                 16.384 
               
               
                 1826 
                 LEU240 
                 N 
                 −5.275 
                 11.736 
                 19.864 
               
               
                 1827 
                 LEU240 
                 CA 
                 −4.667 
                 10.56 
                 20.485 
               
               
                 1828 
                 LEU240 
                 C 
                 −5.217 
                 9.265 
                 19.877 
               
               
                 1829 
                 LEU240 
                 O 
                 −4.445 
                 8.316 
                 19.674 
               
               
                 1830 
                 LEU240 
                 CB 
                 −4.952 
                 10.634 
                 21.981 
               
               
                 1831 
                 LEU240 
                 CG 
                 −3.966 
                 9.808 
                 22.798 
               
               
                 1832 
                 LEU240 
                 CD1 
                 −2.53 
                 10.2 
                 22.479 
               
               
                 1833 
                 LEU240 
                 CD2 
                 −4.227 
                 9.976 
                 24.289 
               
               
                 1834 
                 ILE241 
                 N 
                 −6.425 
                 9.337 
                 19.333 
               
               
                 1835 
                 ILE241 
                 CA 
                 −7.027 
                 8.197 
                 18.621 
               
               
                 1836 
                 ILE241 
                 C 
                 −6.509 
                 8.091 
                 17.184 
               
               
                 1837 
                 ILE241 
                 O 
                 −6.406 
                 6.98 
                 16.64 
               
               
                 1838 
                 ILE241 
                 CB 
                 −8.544 
                 8.391 
                 18.599 
               
               
                 1839 
                 ILE241 
                 CG1 
                 −9.122 
                 8.403 
                 20.008 
               
               
                 1840 
                 ILE241 
                 CG2 
                 −9.233 
                 7.311 
                 17.771 
               
               
                 1841 
                 ILE241 
                 CD1 
                 −8.939 
                 7.06 
                 20.699 
               
               
                 1842 
                 ALA242 
                 N 
                 −5.959 
                 9.182 
                 16.676 
               
               
                 1843 
                 ALA242 
                 CA 
                 −5.353 
                 9.154 
                 15.345 
               
               
                 1844 
                 ALA242 
                 C 
                 −4.049 
                 8.363 
                 15.361 
               
               
                 1845 
                 ALA242 
                 O 
                 −3.842 
                 7.511 
                 14.487 
               
               
                 1846 
                 ALA242 
                 CB 
                 −5.09 
                 10.583 
                 14.884 
               
               
                 1847 
                 GLY243 
                 N 
                 −3.34 
                 8.426 
                 16.473 
               
               
                 1848 
                 GLY243 
                 CA 
                 −2.135 
                 7.612 
                 16.614 
               
               
                 1849 
                 GLY243 
                 C 
                 −2.461 
                 6.175 
                 17.012 
               
               
                 1850 
                 GLY243 
                 O 
                 −2.095 
                 5.238 
                 16.289 
               
               
                 1851 
                 HIS244 
                 N 
                 −3.274 
                 6.021 
                 18.047 
               
               
                 1852 
                 HIS244 
                 CA 
                 −3.556 
                 4.687 
                 18.603 
               
               
                 1853 
                 HIS244 
                 C 
                 −4.424 
                 3.78 
                 17.729 
               
               
                 1854 
                 HIS244 
                 O 
                 −4.288 
                 2.555 
                 17.808 
               
               
                 1855 
                 HIS244 
                 CB 
                 −4.271 
                 4.846 
                 19.946 
               
               
                 1856 
                 HIS244 
                 CG 
                 −3.394 
                 5.206 
                 21.132 
               
               
                 1857 
                 HIS244 
                 ND1 
                 −2.995 
                 6.436 
                 21.502 
               
               
                 1858 
                 HIS244 
                 CD2 
                 −2.87 
                 4.327 
                 22.051 
               
               
                 1859 
                 HIS244 
                 CE1 
                 −2.232 
                 6.348 
                 22.61 
               
               
                 1860 
                 HIS244 
                 NE2 
                 −2.156 
                 5.042 
                 22.95 
               
               
                 1861 
                 GLU245 
                 N 
                 −5.298 
                 4.33 
                 16.905 
               
               
                 1862 
                 GLU245 
                 CA 
                 −6.157 
                 3.454 
                 16.101 
               
               
                 1863 
                 GLU245 
                 C 
                 −6.041 
                 3.723 
                 14.61 
               
               
                 1864 
                 GLU245 
                 O 
                 −5.883 
                 2.788 
                 13.812 
               
               
                 1865 
                 GLU245 
                 CB 
                 −7.616 
                 3.66 
                 16.504 
               
               
                 1866 
                 GLU245 
                 CG 
                 −7.895 
                 3.313 
                 17.963 
               
               
                 1867 
                 GLU245 
                 CD 
                 −7.613 
                 1.839 
                 18.255 
               
               
                 1868 
                 GLU245 
                 OE1 
                 −7.721 
                 1.028 
                 17.348 
               
               
                 1869 
                 GLU245 
                 OE2 
                 −7.228 
                 1.562 
                 19.381 
               
               
                 1870 
                 THR246 
                 N 
                 −5.987 
                 4.996 
                 14.26 
               
               
                 1871 
                 THR246 
                 CA 
                 −6.101 
                 5.374 
                 12.849 
               
               
                 1872 
                 THR246 
                 C 
                 −4.863 
                 4.962 
                 12.066 
               
               
                 1873 
                 THR246 
                 O 
                 −4.949 
                 4.04 
                 11.244 
               
               
                 1874 
                 THR246 
                 CB 
                 −6.314 
                 6.88 
                 12.759 
               
               
                 1875 
                 THR246 
                 OG1 
                 −7.415 
                 7.225 
                 13.59 
               
               
                 1876 
                 THR246 
                 CG2 
                 −6.614 
                 7.344 
                 11.338 
               
               
                 1877 
                 THR247 
                 N 
                 −3.702 
                 5.384 
                 12.532 
               
               
                 1878 
                 THR247 
                 CA 
                 −2.48 
                 5.072 
                 11.792 
               
               
                 1879 
                 THR247 
                 C 
                 −2.013 
                 3.634 
                 12.044 
               
               
                 1880 
                 THR247 
                 O 
                 −1.437 
                 3.032 
                 11.132 
               
               
                 1881 
                 THR247 
                 CB 
                 −1.4 
                 6.078 
                 12.171 
               
               
                 1882 
                 THR247 
                 OG1 
                 −1.937 
                 7.39 
                 12.062 
               
               
                 1883 
                 THR247 
                 CG2 
                 −0.192 
                 5.981 
                 11.246 
               
               
                 1884 
                 ALA248 
                 N 
                 −2.533 
                 3.007 
                 13.09 
               
               
                 1885 
                 ALA248 
                 CA 
                 −2.225 
                 1.596 
                 13.35 
               
               
                 1886 
                 ALA248 
                 C 
                 −2.915 
                 0.676 
                 12.342 
               
               
                 1887 
                 ALA248 
                 O 
                 −2.236 
                 −0.089 
                 11.643 
               
               
                 1888 
                 ALA248 
                 CB 
                 −2.678 
                 1.25 
                 14.763 
               
               
                 1889 
                 ASN249 
                 N 
                 −4.175 
                 0.958 
                 12.049 
               
               
                 1890 
                 ASN249 
                 CA 
                 −4.878 
                 0.157 
                 11.042 
               
               
                 1891 
                 ASN249 
                 C 
                 −4.453 
                 0.517 
                 9.624 
               
               
                 1892 
                 ASN249 
                 O 
                 −4.313 
                 −0.39 
                 8.791 
               
               
                 1893 
                 ASN249 
                 CB 
                 −6.377 
                 0.361 
                 11.199 
               
               
                 1894 
                 ASN249 
                 CG 
                 −6.902 
                 −0.561 
                 12.291 
               
               
                 1895 
                 ASN249 
                 OD1 
                 −6.261 
                 −1.569 
                 12.613 
               
               
                 1896 
                 ASN249 
                 ND2 
                 −8.133 
                 −0.32 
                 12.703 
               
               
                 1897 
                 MET250 
                 N 
                 −3.945 
                 1.727 
                 9.463 
               
               
                 1898 
                 MET250 
                 CA 
                 −3.472 
                 2.183 
                 8.159 
               
               
                 1899 
                 MET250 
                 C 
                 −2.137 
                 1.529 
                 7.787 
               
               
                 1900 
                 MET250 
                 O 
                 −2.018 
                 1.009 
                 6.669 
               
               
                 1901 
                 MET250 
                 CB 
                 −3.231 
                 3.702 
                 8.255 
               
               
                 1902 
                 MET250 
                 CG 
                 −3.343 
                 4.33 
                 6.851 
               
               
                 1903 
                 MET250 
                 SD 
                 −2.234 
                 5.768 
                 6.665 
               
               
                 1904 
                 MET250 
                 CE 
                 −1.954 
                 6.241 
                 8.406 
               
               
                 1905 
                 ILE251 
                 N 
                 −1.267 
                 1.317 
                 8.764 
               
               
                 1906 
                 ILE251 
                 CA 
                 0.019 
                 0.667 
                 8.477 
               
               
                 1907 
                 ILE251 
                 C 
                 −0.132 
                 −0.844 
                 8.328 
               
               
                 1908 
                 ILE251 
                 O 
                 0.449 
                 −1.427 
                 7.402 
               
               
                 1909 
                 ILE251 
                 CB 
                 1.001 
                 0.949 
                 9.613 
               
               
                 1910 
                 ILE251 
                 CG1 
                 1.293 
                 2.434 
                 9.757 
               
               
                 1911 
                 ILE251 
                 CG2 
                 2.305 
                 0.188 
                 9.404 
               
               
                 1912 
                 ILE251 
                 CD1 
                 2.264 
                 2.698 
                 10.902 
               
               
                 1913 
                 SER252 
                 N 
                 −1.081 
                 −1.421 
                 9.047 
               
               
                 1914 
                 SER252 
                 CA 
                 −1.254 
                 −2.875 
                 8.973 
               
               
                 1915 
                 SER252 
                 C 
                 −1.947 
                 −3.301 
                 7.679 
               
               
                 1916 
                 SER252 
                 O 
                 −1.444 
                 −4.204 
                 6.998 
               
               
                 1917 
                 SER252 
                 CB 
                 −2.03 
                 −3.36 
                 10.197 
               
               
                 1918 
                 SER252 
                 OG 
                 −3.28 
                 −2.684 
                 10.279 
               
               
                 1919 
                 LEU253 
                 N 
                 −2.85 
                 −2.465 
                 7.194 
               
               
                 1920 
                 LEU253 
                 CA 
                 −3.558 
                 −2.762 
                 5.948 
               
               
                 1921 
                 LEU253 
                 C 
                 −2.699 
                 −2.386 
                 4.739 
               
               
                 1922 
                 LEU253 
                 O 
                 −2.665 
                 −3.129 
                 3.748 
               
               
                 1923 
                 LEU253 
                 CB 
                 −4.857 
                 −1.963 
                 5.994 
               
               
                 1924 
                 LEU253 
                 CG 
                 −5.781 
                 −2.185 
                 4.804 
               
               
                 1925 
                 LEU253 
                 CD1 
                 −6.009 
                 −3.665 
                 4.521 
               
               
                 1926 
                 LEU253 
                 CD2 
                 −7.109 
                 −1.479 
                 5.058 
               
               
                 1927 
                 GLY254 
                 N 
                 −1.818 
                 −1.42 
                 4.948 
               
               
                 1928 
                 GLY254 
                 CA 
                 −0.841 
                 −1.031 
                 3.933 
               
               
                 1929 
                 GLY254 
                 C 
                 0.161 
                 −2.148 
                 3.671 
               
               
                 1930 
                 GLY254 
                 O 
                 0.267 
                 −2.62 
                 2.531 
               
               
                 1931 
                 THR255 
                 N 
                 0.707 
                 −2.706 
                 4.742 
               
               
                 1932 
                 THR255 
                 CA 
                 1.711 
                 −3.772 
                 4.62 
               
               
                 1933 
                 THR255 
                 C 
                 1.123 
                 −5.042 
                 4.017 
               
               
                 1934 
                 THR255 
                 O 
                 1.715 
                 −5.592 
                 3.079 
               
               
                 1935 
                 THR255 
                 CB 
                 2.255 
                 −4.105 
                 6.007 
               
               
                 1936 
                 THR255 
                 OG1 
                 2.837 
                 −2.935 
                 6.563 
               
               
                 1937 
                 THR255 
                 CG2 
                 3.334 
                 −5.18 
                 5.938 
               
               
                 1938 
                 VAL256 
                 N 
                 −0.133 
                 −5.321 
                 4.331 
               
               
                 1939 
                 VAL256 
                 CA 
                 −0.797 
                 −6.505 
                 3.781 
               
               
                 1940 
                 VAL256 
                 C 
                 −1.11 
                 −6.37 
                 2.291 
               
               
                 1941 
                 VAL256 
                 O 
                 −0.832 
                 −7.307 
                 1.531 
               
               
                 1942 
                 VAL256 
                 CB 
                 −2.083 
                 −6.706 
                 4.571 
               
               
                 1943 
                 VAL256 
                 CG1 
                 −3.028 
                 −7.693 
                 3.905 
               
               
                 1944 
                 VAL256 
                 CG2 
                 −1.774 
                 −7.144 
                 5.993 
               
               
                 1945 
                 THR257 
                 N 
                 −1.372 
                 −5.158 
                 1.833 
               
               
                 1946 
                 THR257 
                 CA 
                 −1.675 
                 −4.982 
                 0.413 
               
               
                 1947 
                 THR257 
                 C 
                 −0.401 
                 −4.902 
                 −0.427 
               
               
                 1948 
                 THR257 
                 O 
                 −0.357 
                 −5.499 
                 −1.512 
               
               
                 1949 
                 THR257 
                 CB 
                 −2.502 
                 −3.717 
                 0.248 
               
               
                 1950 
                 THR257 
                 OG1 
                 −3.63 
                 −3.818 
                 1.106 
               
               
                 1951 
                 THR257 
                 CG2 
                 −3.002 
                 −3.558 
                 −1.183 
               
               
                 1952 
                 LEU258 
                 N 
                 0.69 
                 −4.465 
                 0.185 
               
               
                 1953 
                 LEU258 
                 CA 
                 1.976 
                 −4.434 
                 −0.526 
               
               
                 1954 
                 LEU258 
                 C 
                 2.588 
                 −5.828 
                 −0.61 
               
               
                 1955 
                 LEU258 
                 O 
                 3.147 
                 −6.205 
                 −1.648 
               
               
                 1956 
                 LEU258 
                 CB 
                 2.936 
                 −3.524 
                 0.233 
               
               
                 1957 
                 LEU258 
                 CG 
                 2.45 
                 −2.08 
                 0.263 
               
               
                 1958 
                 LEU258 
                 CD1 
                 3.329 
                 −1.229 
                 1.172 
               
               
                 1959 
                 LEU258 
                 CD2 
                 2.391 
                 −1.492 
                 −1.141 
               
               
                 1960 
                 LEU259 
                 N 
                 2.248 
                 −6.652 
                 0.368 
               
               
                 1961 
                 LEU259 
                 CA 
                 2.721 
                 −8.034 
                 0.407 
               
               
                 1962 
                 LEU259 
                 C 
                 1.818 
                 −8.965 
                 −0.407 
               
               
                 1963 
                 LEU259 
                 O 
                 2.223 
                 −10.083 
                 −0.747 
               
               
                 1964 
                 LEU259 
                 CB 
                 2.742 
                 −8.462 
                 1.869 
               
               
                 1965 
                 LEU259 
                 CG 
                 3.979 
                 −9.291 
                 2.183 
               
               
                 1966 
                 LEU259 
                 CD1 
                 5.235 
                 −8.559 
                 1.727 
               
               
                 1967 
                 LEU259 
                 CD2 
                 4.05 
                 −9.61 
                 3.672 
               
               
                 1968 
                 GLU260 
                 N 
                 0.649 
                 −8.473 
                 −0.791 
               
               
                 1969 
                 GLU260 
                 CA 
                 −0.221 
                 −9.215 
                 −1.707 
               
               
                 1970 
                 GLU260 
                 C 
                 0.163 
                 −8.932 
                 −3.151 
               
               
                 1971 
                 GLU260 
                 O 
                 0.033 
                 −9.804 
                 −4.019 
               
               
                 1972 
                 GLU260 
                 CB 
                 −1.67 
                 −8.773 
                 −1.531 
               
               
                 1973 
                 GLU260 
                 CG 
                 −2.53 
                 −9.85 
                 −0.883 
               
               
                 1974 
                 GLU260 
                 CD 
                 −2.442 
                 −9.78 
                 0.637 
               
               
                 1975 
                 GLU260 
                 OE1 
                 −1.632 
                 −10.498 
                 1.204 
               
               
                 1976 
                 GLU260 
                 OE2 
                 −3.287 
                 −9.103 
                 1.202 
               
               
                 1977 
                 ASN261 
                 N 
                 0.693 
                 −7.743 
                 −3.382 
               
               
                 1978 
                 ASN261 
                 CA 
                 1.158 
                 −7.381 
                 −4.723 
               
               
                 1979 
                 ASN261 
                 C 
                 2.669 
                 −7.181 
                 −4.742 
               
               
                 1980 
                 ASN261 
                 O 
                 3.134 
                 −6.032 
                 −4.804 
               
               
                 1981 
                 ASN261 
                 CB 
                 0.468 
                 −6.089 
                 −5.161 
               
               
                 1982 
                 ASN261 
                 CG 
                 −0.986 
                 −6.311 
                 −5.586 
               
               
                 1983 
                 ASN261 
                 OD1 
                 −1.784 
                 −6.942 
                 −4.881 
               
               
                 1984 
                 ASN261 
                 ND2 
                 −1.339 
                 −5.701 
                 −6.705 
               
               
                 1985 
                 PRO262 
                 N 
                 3.404 
                 −8.259 
                 −4.986 
               
               
                 1986 
                 PRO262 
                 CA 
                 4.864 
                 −8.219 
                 −4.846 
               
               
                 1987 
                 PRO262 
                 C 
                 5.563 
                 −7.432 
                 −5.958 
               
               
                 1988 
                 PRO262 
                 O 
                 6.612 
                 −6.834 
                 −5.706 
               
               
                 1989 
                 PRO262 
                 CB 
                 5.298 
                 −9.652 
                 −4.871 
               
               
                 1990 
                 PRO262 
                 CG 
                 4.108 
                 −10.533 
                 −5.223 
               
               
                 1991 
                 PRO262 
                 CD 
                 2.912 
                 −9.601 
                 −5.319 
               
               
                 1992 
                 ASP263 
                 N 
                 4.884 
                 −7.222 
                 −7.077 
               
               
                 1993 
                 ASP263 
                 CA 
                 5.442 
                 −6.411 
                 −8.166 
               
               
                 1994 
                 ASP263 
                 C 
                 5.27 
                 −4.909 
                 −7.918 
               
               
                 1995 
                 ASP263 
                 O 
                 6.133 
                 −4.124 
                 −8.327 
               
               
                 1996 
                 ASP263 
                 CB 
                 4.783 
                 −6.822 
                 −9.488 
               
               
                 1997 
                 ASP263 
                 CG 
                 3.253 
                 −6.778 
                 −9.42 
               
               
                 1998 
                 ASP263 
                 OD1 
                 2.69 
                 −5.734 
                 −9.721 
               
               
                 1999 
                 ASP263 
                 OD2 
                 2.673 
                 −7.766 
                 −8.992 
               
               
                 2000 
                 GLN264 
                 N 
                 4.358 
                 −4.558 
                 −7.024 
               
               
                 2001 
                 GLN264 
                 CA 
                 4.149 
                 −3.154 
                 −6.675 
               
               
                 2002 
                 GLN264 
                 C 
                 5.104 
                 −2.803 
                 −5.545 
               
               
                 2003 
                 GLN264 
                 O 
                 5.782 
                 −1.769 
                 −5.59 
               
               
                 2004 
                 GLN264 
                 CB 
                 2.709 
                 −3.002 
                 −6.206 
               
               
                 2005 
                 GLN264 
                 CG 
                 1.723 
                 −3.483 
                 −7.265 
               
               
                 2006 
                 GLN264 
                 CD 
                 1.637 
                 −2.485 
                 −8.412 
               
               
                 2007 
                 GLN264 
                 OE1 
                 1.631 
                 −1.274 
                 −8.178 
               
               
                 2008 
                 GLN264 
                 NE2 
                 1.592 
                 −2.991 
                 −9.63 
               
               
                 2009 
                 LEU265 
                 N 
                 5.398 
                 −3.825 
                 −4.758 
               
               
                 2010 
                 LEU265 
                 CA 
                 6.389 
                 −3.701 
                 −3.693 
               
               
                 2011 
                 LEU265 
                 C 
                 7.808 
                 −3.677 
                 −4.263 
               
               
                 2012 
                 LEU265 
                 O 
                 8.639 
                 −2.888 
                 −3.798 
               
               
                 2013 
                 LEU265 
                 CB 
                 6.218 
                 −4.903 
                 −2.775 
               
               
                 2014 
                 LEU265 
                 CG 
                 7.134 
                 −4.809 
                 −1.565 
               
               
                 2015 
                 LEU265 
                 CD1 
                 6.869 
                 −3.518 
                 −0.802 
               
               
                 2016 
                 LEU265 
                 CD2 
                 6.958 
                 −6.023 
                 −0.662 
               
               
                 2017 
                 ALA266 
                 N 
                 7.993 
                 −4.309 
                 −5.411 
               
               
                 2018 
                 ALA266 
                 CA 
                 9.286 
                 −4.267 
                 −6.093 
               
               
                 2019 
                 ALA266 
                 C 
                 9.528 
                 −2.929 
                 −6.785 
               
               
                 2020 
                 ALA266 
                 O 
                 10.66 
                 −2.434 
                 −6.737 
               
               
                 2021 
                 ALA266 
                 CB 
                 9.333 
                 −5.39 
                 −7.123 
               
               
                 2022 
                 LYS267 
                 N 
                 8.466 
                 −2.235 
                 −7.167 
               
               
                 2023 
                 LYS267 
                 CA 
                 8.641 
                 −0.891 
                 −7.725 
               
               
                 2024 
                 LYS267 
                 C 
                 8.887 
                 0.136 
                 −6.625 
               
               
                 2025 
                 LYS267 
                 O 
                 9.706 
                 1.042 
                 −6.818 
               
               
                 2026 
                 LYS267 
                 CB 
                 7.406 
                 −0.501 
                 −8.523 
               
               
                 2027 
                 LYS267 
                 CG 
                 7.223 
                 −1.394 
                 −9.742 
               
               
                 2028 
                 LYS267 
                 CD 
                 6.072 
                 −0.894 
                 −10.604 
               
               
                 2029 
                 LYS267 
                 CE 
                 4.779 
                 −0.825 
                 −9.803 
               
               
                 2030 
                 LYS267 
                 NZ 
                 3.688 
                 −0.267 
                 −10.615 
               
               
                 2031 
                 ILE268 
                 N 
                 8.413 
                 −0.162 
                 −5.427 
               
               
                 2032 
                 ILE268 
                 CA 
                 8.717 
                 0.664 
                 −4.254 
               
               
                 2033 
                 ILE268 
                 C 
                 10.181 
                 0.531 
                 −3.84 
               
               
                 2034 
                 ILE268 
                 O 
                 10.879 
                 1.544 
                 −3.697 
               
               
                 2035 
                 ILE268 
                 CB 
                 7.827 
                 0.171 
                 −3.117 
               
               
                 2036 
                 ILE268 
                 CG1 
                 6.38 
                 0.576 
                 −3.335 
               
               
                 2037 
                 ILE268 
                 CG2 
                 8.311 
                 0.638 
                 −1.75 
               
               
                 2038 
                 ILE268 
                 CD1 
                 5.504 
                 0.057 
                 −2.205 
               
               
                 2039 
                 LYS269 
                 N 
                 10.693 
                 −0.688 
                 −3.902 
               
               
                 2040 
                 LYS269 
                 CA 
                 12.068 
                 −0.95 
                 −3.463 
               
               
                 2041 
                 LYS269 
                 C 
                 13.116 
                 −0.675 
                 −4.542 
               
               
                 2042 
                 LYS269 
                 O 
                 14.306 
                 −0.554 
                 −4.228 
               
               
                 2043 
                 LYS269 
                 CB 
                 12.126 
                 −2.405 
                 −3.021 
               
               
                 2044 
                 LYS269 
                 CG 
                 11.167 
                 −2.628 
                 −1.858 
               
               
                 2045 
                 LYS269 
                 CD 
                 10.997 
                 −4.107 
                 −1.542 
               
               
                 2046 
                 LYS269 
                 CE 
                 12.315 
                 −4.756 
                 −1.148 
               
               
                 2047 
                 LYS269 
                 NZ 
                 12.106 
                 −6.181 
                 −0.856 
               
               
                 2048 
                 ALA270 
                 N 
                 12.679 
                 −0.53 
                 −5.782 
               
               
                 2049 
                 ALA270 
                 CA 
                 13.585 
                 −0.106 
                 −6.851 
               
               
                 2050 
                 ALA270 
                 C 
                 13.478 
                 1.396 
                 −7.101 
               
               
                 2051 
                 ALA270 
                 O 
                 14.286 
                 1.974 
                 −7.838 
               
               
                 2052 
                 ALA270 
                 CB 
                 13.233 
                 −0.863 
                 −8.125 
               
               
                 2053 
                 ASP271 
                 N 
                 12.486 
                 2.017 
                 −6.486 
               
               
                 2054 
                 ASP271 
                 CA 
                 12.271 
                 3.453 
                 −6.649 
               
               
                 2055 
                 ASP271 
                 C 
                 11.505 
                 4.006 
                 −5.448 
               
               
                 2056 
                 ASP271 
                 O 
                 10.267 
                 4.02 
                 −5.445 
               
               
                 2057 
                 ASP271 
                 CB 
                 11.48 
                 3.653 
                 −7.944 
               
               
                 2058 
                 ASP271 
                 CG 
                 11.354 
                 5.125 
                 −8.337 
               
               
                 2059 
                 ASP271 
                 OD1 
                 10.975 
                 5.919 
                 −7.482 
               
               
                 2060 
                 ASP271 
                 OD2 
                 11.493 
                 5.405 
                 −9.517 
               
               
                 2061 
                 PRO272 
                 N 
                 12.238 
                 4.705 
                 −4.592 
               
               
                 2062 
                 PRO272 
                 CA 
                 11.686 
                 5.248 
                 −3.337 
               
               
                 2063 
                 PRO272 
                 C 
                 10.72 
                 6.438 
                 −3.497 
               
               
                 2064 
                 PRO272 
                 O 
                 9.973 
                 6.74 
                 −2.558 
               
               
                 2065 
                 PRO272 
                 CB 
                 12.887 
                 5.657 
                 −2.54 
               
               
                 2066 
                 PRO272 
                 CG 
                 14.133 
                 5.544 
                 −3.406 
               
               
                 2067 
                 PRO272 
                 CD 
                 13.673 
                 4.968 
                 −4.734 
               
               
                 2068 
                 GLY273 
                 N 
                 10.586 
                 6.971 
                 −4.702 
               
               
                 2069 
                 GLY273 
                 CA 
                 9.607 
                 8.03 
                 −4.968 
               
               
                 2070 
                 GLY273 
                 C 
                 8.207 
                 7.423 
                 −5.037 
               
               
                 2071 
                 GLY273 
                 O 
                 7.257 
                 7.968 
                 −4.456 
               
               
                 2072 
                 LYS274 
                 N 
                 8.167 
                 6.171 
                 −5.473 
               
               
                 2073 
                 LYS274 
                 CA 
                 6.916 
                 5.418 
                 −5.566 
               
               
                 2074 
                 LYS274 
                 C 
                 6.39 
                 4.954 
                 −4.21 
               
               
                 2075 
                 LYS274 
                 O 
                 5.225 
                 4.55 
                 −4.144 
               
               
                 2076 
                 LYS274 
                 CB 
                 7.138 
                 4.184 
                 −6.431 
               
               
                 2077 
                 LYS274 
                 CG 
                 7.528 
                 4.547 
                 −7.856 
               
               
                 2078 
                 LYS274 
                 CD 
                 7.755 
                 3.287 
                 −8.681 
               
               
                 2079 
                 LYS274 
                 CE 
                 8.177 
                 3.615 
                 −10.107 
               
               
                 2080 
                 LYS274 
                 NZ 
                 8.465 
                 2.383 
                 −10.858 
               
               
                 2081 
                 THR275 
                 N 
                 7.12 
                 5.182 
                 −3.127 
               
               
                 2082 
                 THR275 
                 CA 
                 6.593 
                 4.814 
                 −1.813 
               
               
                 2083 
                 THR275 
                 C 
                 5.522 
                 5.804 
                 −1.352 
               
               
                 2084 
                 THR275 
                 O 
                 4.516 
                 5.354 
                 −0.798 
               
               
                 2085 
                 THR275 
                 CB 
                 7.725 
                 4.76 
                 −0.789 
               
               
                 2086 
                 THR275 
                 OG1 
                 8.169 
                 6.074 
                 −0.485 
               
               
                 2087 
                 THR275 
                 CG2 
                 8.912 
                 3.963 
                 −1.305 
               
               
                 2088 
                 LEU276 
                 N 
                 5.564 
                 7.036 
                 −1.844 
               
               
                 2089 
                 LEU276 
                 CA 
                 4.543 
                 8.012 
                 −1.446 
               
               
                 2090 
                 LEU276 
                 C 
                 3.312 
                 7.905 
                 −2.346 
               
               
                 2091 
                 LEU276 
                 O 
                 2.175 
                 8.051 
                 −1.876 
               
               
                 2092 
                 LEU276 
                 CB 
                 5.14 
                 9.411 
                 −1.538 
               
               
                 2093 
                 LEU276 
                 CG 
                 4.182 
                 10.462 
                 −0.987 
               
               
                 2094 
                 LEU276 
                 CD1 
                 3.836 
                 10.177 
                 0.472 
               
               
                 2095 
                 LEU276 
                 CD2 
                 4.77 
                 11.861 
                 −1.133 
               
               
                 2096 
                 ALA277 
                 N 
                 3.53 
                 7.375 
                 −3.539 
               
               
                 2097 
                 ALA277 
                 CA 
                 2.417 
                 7.126 
                 −4.451 
               
               
                 2098 
                 ALA277 
                 C 
                 1.711 
                 5.836 
                 −4.052 
               
               
                 2099 
                 ALA277 
                 O 
                 0.475 
                 5.796 
                 −4.026 
               
               
                 2100 
                 ALA277 
                 CB 
                 2.963 
                 7.021 
                 −5.869 
               
               
                 2101 
                 ALA278 
                 N 
                 2.472 
                 4.947 
                 −3.431 
               
               
                 2102 
                 ALA278 
                 CA 
                 1.909 
                 3.727 
                 −2.859 
               
               
                 2103 
                 ALA278 
                 C 
                 1.12 
                 4.01 
                 −1.591 
               
               
                 2104 
                 ALA278 
                 O 
                 0.051 
                 3.416 
                 −1.427 
               
               
                 2105 
                 ALA278 
                 CB 
                 3.048 
                 2.773 
                 −2.523 
               
               
                 2106 
                 ILE279 
                 N 
                 1.472 
                 5.064 
                 −0.867 
               
               
                 2107 
                 ILE279 
                 CA 
                 0.698 
                 5.447 
                 0.324 
               
               
                 2108 
                 ILE279 
                 C 
                 −0.692 
                 5.926 
                 −0.078 
               
               
                 2109 
                 ILE279 
                 O 
                 −1.691 
                 5.368 
                 0.396 
               
               
                 2110 
                 ILE279 
                 CB 
                 1.401 
                 6.588 
                 1.063 
               
               
                 2111 
                 ILE279 
                 CG1 
                 2.806 
                 6.209 
                 1.513 
               
               
                 2112 
                 ILE279 
                 CG2 
                 0.577 
                 7.041 
                 2.264 
               
               
                 2113 
                 ILE279 
                 CD1 
                 2.805 
                 4.984 
                 2.416 
               
               
                 2114 
                 GLU280 
                 N 
                 −0.748 
                 6.688 
                 −1.159 
               
               
                 2115 
                 GLU280 
                 CA 
                 −2.037 
                 7.217 
                 −1.616 
               
               
                 2116 
                 GLU280 
                 C 
                 −2.849 
                 6.159 
                 −2.358 
               
               
                 2117 
                 GLU280 
                 O 
                 −4.075 
                 6.123 
                 −2.217 
               
               
                 2118 
                 GLU280 
                 CB 
                 −1.784 
                 8.404 
                 −2.537 
               
               
                 2119 
                 GLU280 
                 CG 
                 −0.943 
                 9.484 
                 −1.862 
               
               
                 2120 
                 GLU280 
                 CD 
                 −1.616 
                 9.992 
                 −0.587 
               
               
                 2121 
                 GLU280 
                 OE1 
                 −2.453 
                 10.875 
                 −0.699 
               
               
                 2122 
                 GLU280 
                 OE2 
                 −1.19 
                 9.569 
                 0.479 
               
               
                 2123 
                 GLU281 
                 N 
                 −2.169 
                 5.173 
                 −2.916 
               
               
                 2124 
                 GLU281 
                 CA 
                 −2.857 
                 4.083 
                 −3.604 
               
               
                 2125 
                 GLU281 
                 C 
                 −3.402 
                 3.048 
                 −2.616 
               
               
                 2126 
                 GLU281 
                 O 
                 −4.497 
                 2.514 
                 −2.842 
               
               
                 2127 
                 GLU281 
                 CB 
                 −1.846 
                 3.441 
                 −4.546 
               
               
                 2128 
                 GLU281 
                 CG 
                 −2.451 
                 2.329 
                 −5.39 
               
               
                 2129 
                 GLU281 
                 CD 
                 −3.395 
                 2.862 
                 −6.465 
               
               
                 2130 
                 GLU281 
                 OE1 
                 −3.893 
                 2.017 
                 −7.199 
               
               
                 2131 
                 GLU281 
                 OE2 
                 −3.446 
                 4.068 
                 −6.653 
               
               
                 2132 
                 LEU282 
                 N 
                 −2.776 
                 2.957 
                 −1.452 
               
               
                 2133 
                 LEU282 
                 CA 
                 −3.272 
                 2.102 
                 −0.369 
               
               
                 2134 
                 LEU282 
                 C 
                 −4.527 
                 2.703 
                 0.232 
               
               
                 2135 
                 LEU282 
                 O 
                 −5.563 
                 2.03 
                 0.269 
               
               
                 2136 
                 LEU282 
                 CB 
                 −2.212 
                 2.019 
                 0.727 
               
               
                 2137 
                 LEU282 
                 CG 
                 −1.025 
                 1.151 
                 0.332 
               
               
                 2138 
                 LEU282 
                 CD1 
                 0.163 
                 1.385 
                 1.256 
               
               
                 2139 
                 LEU282 
                 CD2 
                 −1.415 
                 −0.319 
                 0.305 
               
               
                 2140 
                 LEU283 
                 N 
                 −4.511 
                 4.018 
                 0.378 
               
               
                 2141 
                 LEU283 
                 CA 
                 −5.666 
                 4.738 
                 0.922 
               
               
                 2142 
                 LEU283 
                 C 
                 −6.823 
                 4.808 
                 −0.066 
               
               
                 2143 
                 LEU283 
                 O 
                 −7.989 
                 4.766 
                 0.346 
               
               
                 2144 
                 LEU283 
                 CB 
                 −5.202 
                 6.145 
                 1.257 
               
               
                 2145 
                 LEU283 
                 CG 
                 −4.178 
                 6.103 
                 2.379 
               
               
                 2146 
                 LEU283 
                 CD1 
                 −3.386 
                 7.399 
                 2.461 
               
               
                 2147 
                 LEU283 
                 CD2 
                 −4.848 
                 5.766 
                 3.706 
               
               
                 2148 
                 ARG284 
                 N 
                 −6.512 
                 4.723 
                 −1.346 
               
               
                 2149 
                 ARG284 
                 CA 
                 −7.561 
                 4.67 
                 −2.355 
               
               
                 2150 
                 ARG284 
                 C 
                 −8.306 
                 3.337 
                 −2.3 
               
               
                 2151 
                 ARG284 
                 O 
                 −9.482 
                 3.316 
                 −1.923 
               
               
                 2152 
                 ARG284 
                 CB 
                 −6.921 
                 4.824 
                 −3.726 
               
               
                 2153 
                 ARG284 
                 CG 
                 −7.99 
                 4.956 
                 −4.798 
               
               
                 2154 
                 ARG284 
                 CD 
                 −7.417 
                 4.674 
                 −6.18 
               
               
                 2155 
                 ARG284 
                 NE 
                 −6.879 
                 3.305 
                 −6.258 
               
               
                 2156 
                 ARG284 
                 CZ 
                 −7.603 
                 2.231 
                 −6.583 
               
               
                 2157 
                 ARG284 
                 NH1 
                 −8.911 
                 2.35 
                 −6.816 
               
               
                 2158 
                 ARG284 
                 NH2 
                 −7.021 
                 1.032 
                 −6.658 
               
               
                 2159 
                 ILE285 
                 N 
                 −7.588 
                 2.233 
                 −2.423 
               
               
                 2160 
                 ILE285 
                 CA 
                 −8.284 
                 0.942 
                 −2.519 
               
               
                 2161 
                 ILE285 
                 C 
                 −8.742 
                 0.397 
                 −1.155 
               
               
                 2162 
                 ILE285 
                 O 
                 −9.703 
                 −0.385 
                 −1.087 
               
               
                 2163 
                 ILE285 
                 CB 
                 −7.36 
                 −0.039 
                 −3.247 
               
               
                 2164 
                 ILE285 
                 CG1 
                 −8.033 
                 −1.383 
                 −3.499 
               
               
                 2165 
                 ILE285 
                 CG2 
                 −6.045 
                 −0.238 
                 −2.501 
               
               
                 2166 
                 ILE285 
                 CD1 
                 −7.119 
                 −2.327 
                 −4.272 
               
               
                 2167 
                 PHE286 
                 N 
                 −8.188 
                 0.934 
                 −0.082 
               
               
                 2168 
                 PHE286 
                 CA 
                 −8.543 
                 0.5 
                 1.268 
               
               
                 2169 
                 PHE286 
                 C 
                 −8.451 
                 1.645 
                 2.27 
               
               
                 2170 
                 PHE286 
                 O 
                 −7.544 
                 1.66 
                 3.115 
               
               
                 2171 
                 PHE286 
                 CB 
                 −7.575 
                 −0.594 
                 1.708 
               
               
                 2172 
                 PHE286 
                 CG 
                 −7.737 
                 −1.948 
                 1.025 
               
               
                 2173 
                 PHE286 
                 CD1 
                 −6.675 
                 −2.503 
                 0.323 
               
               
                 2174 
                 PHE286 
                 CD2 
                 −8.943 
                 −2.632 
                 1.117 
               
               
                 2175 
                 PHE286 
                 CE1 
                 −6.822 
                 −3.736 
                 −0.298 
               
               
                 2176 
                 PHE286 
                 CE2 
                 −9.09 
                 −3.865 
                 0.495 
               
               
                 2177 
                 PHE286 
                 CZ 
                 −8.03 
                 −4.417 
                 −0.213 
               
               
                 2178 
                 THR287 
                 N 
                 −9.377 
                 2.584 
                 2.193 
               
               
                 2179 
                 THR287 
                 CA 
                 −9.413 
                 3.636 
                 3.212 
               
               
                 2180 
                 THR287 
                 C 
                 −9.931 
                 3.053 
                 4.519 
               
               
                 2181 
                 THR287 
                 O 
                 −10.843 
                 2.216 
                 4.543 
               
               
                 2182 
                 THR287 
                 CB 
                 −10.294 
                 4.801 
                 2.77 
               
               
                 2183 
                 THR287 
                 OG1 
                 −10.207 
                 5.833 
                 3.745 
               
               
                 2184 
                 THR287 
                 CG2 
                 −11.759 
                 4.423 
                 2.643 
               
               
                 2185 
                 ILE288 
                 N 
                 −9.305 
                 3.459 
                 5.609 
               
               
                 2186 
                 ILE288 
                 CA 
                 −9.745 
                 2.966 
                 6.911 
               
               
                 2187 
                 ILE288 
                 C 
                 −10.966 
                 3.747 
                 7.391 
               
               
                 2188 
                 ILE288 
                 O 
                 −11.856 
                 3.155 
                 8.014 
               
               
                 2189 
                 ILE288 
                 CB 
                 −8.584 
                 3.044 
                 7.894 
               
               
                 2190 
                 ILE288 
                 CG1 
                 −8.04 
                 4.459 
                 8.013 
               
               
                 2191 
                 ILE288 
                 CG2 
                 −7.469 
                 2.097 
                 7.461 
               
               
                 2192 
                 ILE288 
                 CD1 
                 −6.938 
                 4.507 
                 9.052 
               
               
                 2193 
                 ALA289 
                 N 
                 −11.116 
                 4.965 
                 6.89 
               
               
                 2194 
                 ALA289 
                 CA 
                 −12.34 
                 5.743 
                 7.09 
               
               
                 2195 
                 ALA289 
                 C 
                 −13.315 
                 5.37 
                 5.982 
               
               
                 2196 
                 ALA289 
                 O 
                 −13.433 
                 6.062 
                 4.964 
               
               
                 2197 
                 ALA289 
                 CB 
                 −12.003 
                 7.228 
                 7.013 
               
               
                 2198 
                 GLU290 
                 N 
                 −13.969 
                 4.239 
                 6.174 
               
               
                 2199 
                 GLU290 
                 CA 
                 −14.796 
                 3.652 
                 5.128 
               
               
                 2200 
                 GLU290 
                 C 
                 −16.223 
                 4.179 
                 5.178 
               
               
                 2201 
                 GLU290 
                 O 
                 −16.891 
                 4.234 
                 4.138 
               
               
                 2202 
                 GLU290 
                 CB 
                 −14.766 
                 2.14 
                 5.34 
               
               
                 2203 
                 GLU290 
                 CG 
                 −15.669 
                 1.375 
                 4.381 
               
               
                 2204 
                 GLU290 
                 CD 
                 −15.736 
                 −0.091 
                 4.802 
               
               
                 2205 
                 GLU290 
                 OE1 
                 −16.751 
                 −0.475 
                 5.367 
               
               
                 2206 
                 GLU290 
                 OE2 
                 −14.809 
                 −0.819 
                 4.472 
               
               
                 2207 
                 THR291 
                 N 
                 −16.659 
                 4.619 
                 6.347 
               
               
                 2208 
                 THR291 
                 CA 
                 −17.992 
                 5.216 
                 6.481 
               
               
                 2209 
                 THR291 
                 C 
                 −17.983 
                 6.47 
                 7.349 
               
               
                 2210 
                 THR291 
                 O 
                 −17.68 
                 6.437 
                 8.55 
               
               
                 2211 
                 THR291 
                 CB 
                 −18.978 
                 4.219 
                 7.094 
               
               
                 2212 
                 THR291 
                 OG1 
                 −18.522 
                 3.832 
                 8.382 
               
               
                 2213 
                 THR291 
                 CG2 
                 −19.168 
                 2.961 
                 6.257 
               
               
                 2214 
                 ALA292 
                 N 
                 −18.397 
                 7.562 
                 6.734 
               
               
                 2215 
                 ALA292 
                 CA 
                 −18.676 
                 8.799 
                 7.471 
               
               
                 2216 
                 ALA292 
                 C 
                 −20.103 
                 8.704 
                 8.001 
               
               
                 2217 
                 ALA292 
                 O 
                 −21.051 
                 9.169 
                 7.355 
               
               
                 2218 
                 ALA292 
                 CB 
                 −18.552 
                 9.986 
                 6.521 
               
               
                 2219 
                 THR293 
                 N 
                 −20.231 
                 8.1 
                 9.172 
               
               
                 2220 
                 THR293 
                 CA 
                 −21.535 
                 7.709 
                 9.721 
               
               
                 2221 
                 THR293 
                 C 
                 −22.161 
                 8.802 
                 10.585 
               
               
                 2222 
                 THR293 
                 O 
                 −22.152 
                 8.733 
                 11.82 
               
               
                 2223 
                 THR293 
                 CB 
                 −21.308 
                 6.447 
                 10.546 
               
               
                 2224 
                 THR293 
                 OG1 
                 −20.564 
                 5.523 
                 9.756 
               
               
                 2225 
                 THR293 
                 CG2 
                 −22.617 
                 5.788 
                 10.962 
               
               
                 2226 
                 SER294 
                 N 
                 −22.703 
                 9.805 
                 9.913 
               
               
                 2227 
                 SER294 
                 CA 
                 −23.293 
                 10.956 
                 10.601 
               
               
                 2228 
                 SER294 
                 C 
                 −24.198 
                 11.766 
                 9.675 
               
               
                 2229 
                 SER294 
                 O 
                 −25.386 
                 11.443 
                 9.529 
               
               
                 2230 
                 SER294 
                 CB 
                 −22.167 
                 11.822 
                 11.164 
               
               
                 2231 
                 SER294 
                 OG 
                 −20.976 
                 11.559 
                 10.426 
               
               
                 2232 
                 ARG295 
                 N 
                 −23.598 
                 12.789 
                 9.076 
               
               
                 2233 
                 ARG295 
                 CA 
                 −24.233 
                 13.782 
                 8.187 
               
               
                 2234 
                 ARG295 
                 C 
                 −25.738 
                 13.903 
                 8.366 
               
               
                 2235 
                 ARG295 
                 O 
                 −26.524 
                 13.3 
                 7.627 
               
               
                 2236 
                 ARG295 
                 CB 
                 −23.905 
                 13.424 
                 6.747 
               
               
                 2237 
                 ARG295 
                 CG 
                 −22.4 
                 13.455 
                 6.518 
               
               
                 2238 
                 ARG295 
                 CD 
                 −21.819 
                 14.841 
                 6.786 
               
               
                 2239 
                 ARG295 
                 NE 
                 −20.362 
                 14.859 
                 6.577 
               
               
                 2240 
                 ARG295 
                 CZ 
                 −19.475 
                 14.679 
                 7.56 
               
               
                 2241 
                 ARG295 
                 NH1 
                 −19.892 
                 14.437 
                 8.805 
               
               
                 2242 
                 ARG295 
                 NH2 
                 −18.167 
                 14.719 
                 7.293 
               
               
                 2243 
                 PHE296 
                 N 
                 −26.119 
                 14.646 
                 9.387 
               
               
                 2244 
                 PHE296 
                 GA 
                 −27.528 
                 14.825 
                 9.712 
               
               
                 2245 
                 PHE296 
                 C 
                 −28.176 
                 15.754 
                 8.701 
               
               
                 2246 
                 PHE296 
                 O 
                 −27.736 
                 16.899 
                 8.529 
               
               
                 2247 
                 PHE296 
                 CB 
                 −27.623 
                 15.428 
                 11.11 
               
               
                 2248 
                 PHE296 
                 CG 
                 −29.052 
                 15.695 
                 11.562 
               
               
                 2249 
                 PHE296 
                 CD1 
                 −29.564 
                 16.985 
                 11.533 
               
               
                 2250 
                 PHE296 
                 CD2 
                 −29.843 
                 14.643 
                 12.002 
               
               
                 2251 
                 PHE296 
                 CE1 
                 −30.871 
                 17.221 
                 11.936 
               
               
                 2252 
                 PHE296 
                 CE2 
                 −31.149 
                 14.879 
                 12.406 
               
               
                 2253 
                 PHE296 
                 CZ 
                 −31.663 
                 16.167 
                 12.37 
               
               
                 2254 
                 ALA297 
                 N 
                 −29.2 
                 15.255 
                 8.032 
               
               
                 2255 
                 ALA297 
                 CA 
                 −29.931 
                 16.073 
                 7.065 
               
               
                 2256 
                 ALA297 
                 C 
                 −30.783 
                 17.111 
                 7.781 
               
               
                 2257 
                 ALA297 
                 O 
                 −31.769 
                 16.781 
                 8.45 
               
               
                 2258 
                 ALA297 
                 CB 
                 −30.819 
                 15.165 
                 6.224 
               
               
                 2259 
                 THR298 
                 N 
                 −30.369 
                 18.361 
                 7.668 
               
               
                 2260 
                 THR298 
                 CA 
                 −31.129 
                 19.47 
                 8.255 
               
               
                 2261 
                 THR298 
                 C 
                 −32.139 
                 20.005 
                 7.246 
               
               
                 2262 
                 THR298 
                 O 
                 −33.087 
                 20.712 
                 7.603 
               
               
                 2263 
                 THR298 
                 CB 
                 −30.17 
                 20.586 
                 8.659 
               
               
                 2264 
                 THR298 
                 OG1 
                 −29.565 
                 21.12 
                 7.488 
               
               
                 2265 
                 THR298 
                 CG2 
                 −29.068 
                 20.082 
                 9.582 
               
               
                 2266 
                 ALA299 
                 N 
                 −31.926 
                 19.649 
                 5.992 
               
               
                 2267 
                 ALA299 
                 CA 
                 −32.881 
                 19.968 
                 4.932 
               
               
                 2268 
                 ALA299 
                 C 
                 −33.091 
                 18.734 
                 4.068 
               
               
                 2269 
                 ALA299 
                 O 
                 −32.427 
                 17.712 
                 4.27 
               
               
                 2270 
                 ALA299 
                 CB 
                 −32.331 
                 21.11 
                 4.086 
               
               
                 2271 
                 ASP300 
                 N 
                 −34.041 
                 18.817 
                 3.151 
               
               
                 2272 
                 ASP300 
                 CA 
                 −34.256 
                 17.727 
                 2.191 
               
               
                 2273 
                 ASP300 
                 C 
                 −33.253 
                 17.852 
                 1.048 
               
               
                 2274 
                 ASP300 
                 O 
                 −33.498 
                 18.545 
                 0.053 
               
               
                 2275 
                 ASP300 
                 CB 
                 −35.679 
                 17.801 
                 1.648 
               
               
                 2276 
                 ASP300 
                 CG 
                 −36.682 
                 17.714 
                 2.793 
               
               
                 2277 
                 ASP300 
                 OD1 
                 −36.686 
                 16.69 
                 3.463 
               
               
                 2278 
                 ASP300 
                 OD2 
                 −37.289 
                 18.733 
                 3.09 
               
               
                 2279 
                 VAL301 
                 N 
                 −32.128 
                 17.177 
                 1.199 
               
               
                 2280 
                 VAL301 
                 CA 
                 −31.029 
                 17.337 
                 0.244 
               
               
                 2281 
                 VAL301 
                 C 
                 −31.065 
                 16.261 
                 −0.833 
               
               
                 2282 
                 VAL301 
                 O 
                 −30.956 
                 15.062 
                 −0.55 
               
               
                 2283 
                 VAL301 
                 CB 
                 −29.711 
                 17.263 
                 1.007 
               
               
                 2284 
                 VAL301 
                 CG1 
                 −28.543 
                 17.673 
                 0.118 
               
               
                 2285 
                 VAL301 
                 CG2 
                 −29.756 
                 18.154 
                 2.24 
               
               
                 2286 
                 GLU302 
                 N 
                 −31.242 
                 16.695 
                 −2.067 
               
               
                 2287 
                 GLU302 
                 CA 
                 −31.23 
                 15.75 
                 −3.184 
               
               
                 2288 
                 GLU302 
                 C 
                 −29.799 
                 15.413 
                 −3.603 
               
               
                 2289 
                 GLU302 
                 O 
                 −29.141 
                 16.178 
                 −4.318 
               
               
                 2290 
                 GLU302 
                 CB 
                 −31.98 
                 16.355 
                 −4.363 
               
               
                 2291 
                 GLU302 
                 CG 
                 −32.053 
                 15.344 
                 −5.497 
               
               
                 2292 
                 GLU302 
                 CD 
                 −32.662 
                 15.959 
                 −6.75 
               
               
                 2293 
                 GLU302 
                 OE1 
                 −33.484 
                 16.852 
                 −6.606 
               
               
                 2294 
                 GLU302 
                 OE2 
                 −32.169 
                 15.628 
                 −7.82 
               
               
                 2295 
                 ILE303 
                 N 
                 −29.365 
                 14.227 
                 −3.222 
               
               
                 2296 
                 ILE303 
                 CA 
                 −28.014 
                 13.766 
                 −3.539 
               
               
                 2297 
                 ILE303 
                 C 
                 −28.053 
                 12.812 
                 −4.726 
               
               
                 2298 
                 ILE303 
                 O 
                 −28.452 
                 11.647 
                 −4.6 
               
               
                 2299 
                 ILE303 
                 CB 
                 −27.438 
                 13.076 
                 −2.307 
               
               
                 2300 
                 ILE303 
                 CG1 
                 −27.329 
                 14.056 
                 −1.148 
               
               
                 2301 
                 ILE303 
                 CG2 
                 −26.066 
                 12.49 
                 −2.608 
               
               
                 2302 
                 ILE303 
                 CD1 
                 −26.305 
                 15.146 
                 −1.441 
               
               
                 2303 
                 GLY304 
                 N 
                 −27.715 
                 13.356 
                 −5.885 
               
               
                 2304 
                 GLY304 
                 CA 
                 −27.705 
                 12.592 
                 −7.139 
               
               
                 2305 
                 GLY304 
                 C 
                 −29.056 
                 11.935 
                 −7.402 
               
               
                 2306 
                 GLY304 
                 O 
                 −29.187 
                 10.708 
                 −7.311 
               
               
                 2307 
                 GLY305 
                 N 
                 −30.079 
                 12.757 
                 −7.573 
               
               
                 2308 
                 GLY305 
                 CA 
                 −31.432 
                 12.229 
                 −7.805 
               
               
                 2309 
                 GLY305 
                 C 
                 −32.226 
                 11.982 
                 −6.517 
               
               
                 2310 
                 GLY305 
                 O 
                 −33.289 
                 12.584 
                 −6.314 
               
               
                 2311 
                 THR306 
                 N 
                 −31.694 
                 11.132 
                 −5.653 
               
               
                 2312 
                 THR306 
                 CA 
                 −32.399 
                 10.717 
                 −4.431 
               
               
                 2313 
                 THR306 
                 C 
                 −32.569 
                 11.859 
                 −3.43 
               
               
                 2314 
                 THR306 
                 O 
                 −31.597 
                 12.497 
                 −3.015 
               
               
                 2315 
                 THR306 
                 CB 
                 −31.591 
                 9.598 
                 −3.782 
               
               
                 2316 
                 THR306 
                 OG1 
                 −31.461 
                 8.534 
                 −4.716 
               
               
                 2317 
                 THR306 
                 CG2 
                 −32.278 
                 9.051 
                 −2.537 
               
               
                 2318 
                 LEU307 
                 N 
                 −33.811 
                 12.127 
                 −3.066 
               
               
                 2319 
                 LEU307 
                 CA 
                 −34.093 
                 13.162 
                 −2.068 
               
               
                 2320 
                 LEU307 
                 C 
                 −33.971 
                 12.6 
                 −0.652 
               
               
                 2321 
                 LEU307 
                 O 
                 −34.803 
                 11.799 
                 −0.209 
               
               
                 2322 
                 LEU307 
                 CB 
                 −35.513 
                 13.67 
                 −2.295 
               
               
                 2323 
                 LEU307 
                 CG 
                 −35.845 
                 14.852 
                 −1.391 
               
               
                 2324 
                 LEU307 
                 CD1 
                 −34.946 
                 16.039 
                 −1.71 
               
               
                 2325 
                 LEU307 
                 CD2 
                 −37.31 
                 15.248 
                 −1.534 
               
               
                 2326 
                 ILE308 
                 N 
                 −32.93 
                 13.021 
                 0.045 
               
               
                 2327 
                 ILE308 
                 CA 
                 −32.738 
                 12.616 
                 1.439 
               
               
                 2328 
                 ILE308 
                 C 
                 −33.586 
                 13.486 
                 2.362 
               
               
                 2329 
                 ILE308 
                 O 
                 −33.481 
                 14.719 
                 2.356 
               
               
                 2330 
                 ILE308 
                 CB 
                 −31.253 
                 12.742 
                 1.764 
               
               
                 2331 
                 ILE308 
                 CG1 
                 −30.456 
                 11.77 
                 0.901 
               
               
                 2332 
                 ILE308 
                 CG2 
                 −30.976 
                 12.507 
                 3.245 
               
               
                 2333 
                 ILE308 
                 CD1 
                 −28.974 
                 11.794 
                 1.246 
               
               
                 2334 
                 ARG309 
                 N 
                 −34.466 
                 12.834 
                 3.101 
               
               
                 2335 
                 ARG309 
                 CA 
                 −35.386 
                 13.543 
                 3.993 
               
               
                 2336 
                 ARG309 
                 C 
                 −34.674 
                 14.125 
                 5.209 
               
               
                 2337 
                 ARG309 
                 O 
                 −33.807 
                 13.486 
                 5.824 
               
               
                 2338 
                 ARG309 
                 CB 
                 −36.447 
                 12.563 
                 4.474 
               
               
                 2339 
                 ARG309 
                 CG 
                 −37.117 
                 11.841 
                 3.312 
               
               
                 2340 
                 ARG309 
                 CD 
                 −38.079 
                 10.778 
                 3.83 
               
               
                 2341 
                 ARG309 
                 NE 
                 −38.721 
                 10.055 
                 2.721 
               
               
                 2342 
                 ARG309 
                 CZ 
                 −40.046 
                 9.951 
                 2.594 
               
               
                 2343 
                 ARG309 
                 NH1 
                 −40.85 
                 10.528 
                 3.49 
               
               
                 2344 
                 ARG309 
                 NH2 
                 −40.566 
                 9.278 
                 1.566 
               
               
                 2345 
                 ALA310 
                 N 
                 −35.099 
                 15.325 
                 5.566 
               
               
                 2346 
                 ALA310 
                 CA 
                 −34.597 
                 15.999 
                 6.763 
               
               
                 2347 
                 ALA310 
                 C 
                 −34.952 
                 15.189 
                 8.003 
               
               
                 2348 
                 ALA310 
                 O 
                 −36.005 
                 14.542 
                 8.07 
               
               
                 2349 
                 ALA310 
                 CB 
                 −35.223 
                 17.386 
                 6.853 
               
               
                 2350 
                 GLY311 
                 N 
                 −34 
                 15.115 
                 8.913 
               
               
                 2351 
                 GLY311 
                 CA 
                 −34.172 
                 14.325 
                 10.13 
               
               
                 2352 
                 GLY311 
                 C 
                 −33.475 
                 12.968 
                 10.042 
               
               
                 2353 
                 GLY311 
                 O 
                 −33.472 
                 12.217 
                 11.023 
               
               
                 2354 
                 GLU312 
                 N 
                 −32.982 
                 12.611 
                 8.866 
               
               
                 2355 
                 GLU312 
                 CA 
                 −32.294 
                 11.322 
                 8.719 
               
               
                 2356 
                 GLU312 
                 C 
                 −30.776 
                 11.471 
                 8.737 
               
               
                 2357 
                 GLU312 
                 O 
                 −30.236 
                 12.577 
                 8.599 
               
               
                 2358 
                 GLU312 
                 CB 
                 −32.743 
                 10.651 
                 7.429 
               
               
                 2359 
                 GLU312 
                 CG 
                 −34.243 
                 10.386 
                 7.453 
               
               
                 2360 
                 GLU312 
                 CD 
                 −34.639 
                 9.537 
                 6.252 
               
               
                 2361 
                 GLU312 
                 OE1 
                 −34.686 
                 10.083 
                 5.156 
               
               
                 2362 
                 GLU312 
                 OE2 
                 −34.723 
                 8.33 
                 6.419 
               
               
                 2363 
                 GLY313 
                 N 
                 −30.107 
                 10.356 
                 8.981 
               
               
                 2364 
                 GLY313 
                 CA 
                 −28.64 
                 10.335 
                 8.994 
               
               
                 2365 
                 GLY313 
                 C 
                 −28.079 
                 9.813 
                 7.673 
               
               
                 2366 
                 GLY313 
                 O 
                 −28.674 
                 8.944 
                 7.02 
               
               
                 2367 
                 VAL314 
                 N 
                 −26.996 
                 10.429 
                 7.237 
               
               
                 2368 
                 VAL314 
                 CA 
                 −26.33 
                 10.028 
                 5.994 
               
               
                 2369 
                 VAL314 
                 C 
                 −24.93 
                 9.467 
                 6.267 
               
               
                 2370 
                 VAL314 
                 O 
                 −24.127 
                 10.02 
                 7.033 
               
               
                 2371 
                 VAL314 
                 CB 
                 −26.28 
                 11.246 
                 5.073 
               
               
                 2372 
                 VAL314 
                 CG1 
                 −25.639 
                 10.942 
                 3.724 
               
               
                 2373 
                 VAL314 
                 CG2 
                 −27.681 
                 11.804 
                 4.861 
               
               
                 2374 
                 VAL315 
                 N 
                 −24.674 
                 8.328 
                 5.649 
               
               
                 2375 
                 VAL315 
                 CA 
                 −23.386 
                 7.646 
                 5.773 
               
               
                 2376 
                 VAL315 
                 C 
                 −22.647 
                 7.666 
                 4.435 
               
               
                 2377 
                 VAL315 
                 O 
                 −23.025 
                 6.975 
                 3.479 
               
               
                 2378 
                 VAL315 
                 CB 
                 −23.634 
                 6.207 
                 6.213 
               
               
                 2379 
                 VAL315 
                 CG1 
                 −22.325 
                 5.437 
                 6.347 
               
               
                 2380 
                 VAL315 
                 CG2 
                 −24.404 
                 6.163 
                 7.528 
               
               
                 2381 
                 GLY316 
                 N 
                 −21.6 
                 8.467 
                 4.374 
               
               
                 2382 
                 GLY316 
                 CA 
                 −20.789 
                 8.539 
                 3.152 
               
               
                 2383 
                 GLY316 
                 C 
                 −19.797 
                 7.382 
                 3.096 
               
               
                 2384 
                 GLY316 
                 O 
                 −18.903 
                 7.28 
                 3.946 
               
               
                 2385 
                 LEU317 
                 N 
                 −19.978 
                 6.508 
                 2.121 
               
               
                 2386 
                 LEU317 
                 CA 
                 −19.102 
                 5.343 
                 1.978 
               
               
                 2387 
                 LEU317 
                 C 
                 −17.841 
                 5.722 
                 1.218 
               
               
                 2388 
                 LEU317 
                 O 
                 −17.758 
                 5.485 
                 0.009 
               
               
                 2389 
                 LEU317 
                 CB 
                 −19.835 
                 4.256 
                 1.199 
               
               
                 2390 
                 LEU317 
                 CG 
                 −20.312 
                 3.094 
                 2.064 
               
               
                 2391 
                 LEU317 
                 CD1 
                 −19.129 
                 2.374 
                 2.697 
               
               
                 2392 
                 LEU317 
                 CD2 
                 −21.328 
                 3.519 
                 3.121 
               
               
                 2393 
                 SER318 
                 N 
                 −16.794 
                 6.056 
                 1.951 
               
               
                 2394 
                 SER318 
                 CA 
                 −15.563 
                 6.559 
                 1.34 
               
               
                 2395 
                 SER318 
                 C 
                 −14.789 
                 5.483 
                 0.588 
               
               
                 2396 
                 SER318 
                 O 
                 −14.286 
                 5.777 
                 −0.503 
               
               
                 2397 
                 SER318 
                 CB 
                 −14.689 
                 7.158 
                 2.434 
               
               
                 2398 
                 SER318 
                 OG 
                 −13.375 
                 7.32 
                 1.915 
               
               
                 2399 
                 ASN319 
                 N 
                 −14.954 
                 4.222 
                 0.954 
               
               
                 2400 
                 ASN319 
                 CA 
                 −14.267 
                 3.196 
                 0.162 
               
               
                 2401 
                 ASN319 
                 C 
                 −15.089 
                 2.774 
                 −1.058 
               
               
                 2402 
                 ASN319 
                 O 
                 −14.498 
                 2.343 
                 −2.052 
               
               
                 2403 
                 ASN319 
                 CB 
                 −13.899 
                 1.982 
                 1.004 
               
               
                 2404 
                 ASN319 
                 CG 
                 −12.531 
                 1.507 
                 0.516 
               
               
                 2405 
                 ASN319 
                 OD1 
                 −11.628 
                 2.333 
                 0.321 
               
               
                 2406 
                 ASN319 
                 ND2 
                 −12.378 
                 0.209 
                 0.332 
               
               
                 2407 
                 ALA320 
                 N 
                 −16.362 
                 3.139 
                 −1.091 
               
               
                 2408 
                 ALA320 
                 CA 
                 −17.181 
                 2.889 
                 −2.283 
               
               
                 2409 
                 ALA320 
                 C 
                 −17.001 
                 4.055 
                 −3.248 
               
               
                 2410 
                 ALA320 
                 O 
                 −16.897 
                 3.856 
                 −4.464 
               
               
                 2411 
                 ALA320 
                 CB 
                 −18.642 
                 2.78 
                 −1.875 
               
               
                 2412 
                 GLY321 
                 N 
                 −16.68 
                 5.197 
                 −2.666 
               
               
                 2413 
                 GLY321 
                 CA 
                 −16.233 
                 6.36 
                 −3.426 
               
               
                 2414 
                 GLY321 
                 C 
                 −14.942 
                 6.045 
                 −4.17 
               
               
                 2415 
                 GLY321 
                 O 
                 −14.924 
                 6.106 
                 −5.404 
               
               
                 2416 
                 ASN322 
                 N 
                 −13.958 
                 5.508 
                 −3.466 
               
               
                 2417 
                 ASN322 
                 CA 
                 −12.683 
                 5.172 
                 −4.113 
               
               
                 2418 
                 ASN322 
                 C 
                 −12.765 
                 3.924 
                 −5.006 
               
               
                 2419 
                 ASN322 
                 O 
                 −11.954 
                 3.769 
                 −5.927 
               
               
                 2420 
                 ASN322 
                 CB 
                 −11.651 
                 4.902 
                 −3.035 
               
               
                 2421 
                 ASN322 
                 CG 
                 −11.54 
                 6.013 
                 −1.994 
               
               
                 2422 
                 ASN322 
                 OD1 
                 −11.701 
                 7.211 
                 −2.278 
               
               
                 2423 
                 ASN322 
                 ND2 
                 −11.095 
                 5.595 
                 −0.824 
               
               
                 2424 
                 HIS323 
                 N 
                 −13.785 
                 3.103 
                 −4.807 
               
               
                 2425 
                 HIS323 
                 CA 
                 −14.068 
                 1.985 
                 −5.716 
               
               
                 2426 
                 HIS323 
                 C 
                 −15.037 
                 2.337 
                 −6.846 
               
               
                 2427 
                 HIS323 
                 O 
                 −15.541 
                 1.435 
                 −7.525 
               
               
                 2428 
                 HIS323 
                 CB 
                 −14.625 
                 0.804 
                 −4.939 
               
               
                 2429 
                 HIS323 
                 CG 
                 −13.581 
                 0.008 
                 −4.19 
               
               
                 2430 
                 HIS323 
                 ND1 
                 −13.802 
                 −0.807 
                 −3.144 
               
               
                 2431 
                 HIS323 
                 CD2 
                 −12.233 
                 −0.04 
                 −4.46 
               
               
                 2432 
                 HIS323 
                 CE1 
                 −12.634 
                 −1.351 
                 −2.748 
               
               
                 2433 
                 HIS323 
                 NE2 
                 −11.664 
                 −0.875 
                 −3.563 
               
               
                 2434 
                 ASP324 
                 N 
                 −15.353 
                 3.608 
                 −7.007 
               
               
                 2435 
                 ASP324 
                 CA 
                 −16.209 
                 4.041 
                 −8.109 
               
               
                 2436 
                 ASP324 
                 C 
                 −15.409 
                 4.076 
                 −9.411 
               
               
                 2437 
                 ASP324 
                 O 
                 −14.628 
                 5.012 
                 −9.642 
               
               
                 2438 
                 ASP324 
                 CB 
                 −16.72 
                 5.431 
                 −7.737 
               
               
                 2439 
                 ASP324 
                 CG 
                 −17.711 
                 6.002 
                 −8.74 
               
               
                 2440 
                 ASP324 
                 OD1 
                 −18.738 
                 6.476 
                 −8.275 
               
               
                 2441 
                 ASP324 
                 OD2 
                 −17.28 
                 6.257 
                 −9.859 
               
               
                 2442 
                 PRO325 
                 N 
                 −15.831 
                 3.237 
                 −10.349 
               
               
                 2443 
                 PRO325 
                 CA 
                 −15.082 
                 2.989 
                 −11.595 
               
               
                 2444 
                 PRO325 
                 C 
                 −15.201 
                 4.099 
                 −12.648 
               
               
                 2445 
                 PRO325 
                 O 
                 −14.504 
                 4.065 
                 −13.667 
               
               
                 2446 
                 PRO325 
                 CB 
                 −15.653 
                 1.713 
                 −12.134 
               
               
                 2447 
                 PRO325 
                 CG 
                 −16.9 
                 1.346 
                 −11.345 
               
               
                 2448 
                 PRO325 
                 CD 
                 −17.01 
                 2.374 
                 −10.232 
               
               
                 2449 
                 ASP326 
                 N 
                 −16.008 
                 5.11 
                 −12.361 
               
               
                 2450 
                 ASP326 
                 CA 
                 −16.206 
                 6.248 
                 −13.259 
               
               
                 2451 
                 ASP326 
                 C 
                 −15.146 
                 7.312 
                 −12.983 
               
               
                 2452 
                 ASP326 
                 O 
                 −14.924 
                 8.216 
                 −13.797 
               
               
                 2453 
                 ASP326 
                 CB 
                 −17.597 
                 6.826 
                 −12.994 
               
               
                 2454 
                 ASP326 
                 CG 
                 −18.675 
                 5.753 
                 −13.155 
               
               
                 2455 
                 ASP326 
                 OD1 
                 −19.125 
                 5.571 
                 −14.277 
               
               
                 2456 
                 ASP326 
                 OD2 
                 −18.963 
                 5.068 
                 −12.179 
               
               
                 2457 
                 GLY327 
                 N 
                 −14.468 
                 7.162 
                 −11.857 
               
               
                 2458 
                 GLY327 
                 CA 
                 −13.318 
                 8.005 
                 −11.542 
               
               
                 2459 
                 GLY327 
                 C 
                 −12.061 
                 7.145 
                 −11.594 
               
               
                 2460 
                 GLY327 
                 O 
                 −11.166 
                 7.366 
                 −12.418 
               
               
                 2461 
                 PHE328 
                 N 
                 −12.046 
                 6.12 
                 −10.76 
               
               
                 2462 
                 PHE328 
                 CA 
                 −10.893 
                 5.218 
                 −10.705 
               
               
                 2463 
                 PHE328 
                 C 
                 −11.119 
                 4.009 
                 −11.602 
               
               
                 2464 
                 PHE328 
                 O 
                 −11.92 
                 3.114 
                 −11.3 
               
               
                 2465 
                 PHE328 
                 CB 
                 −10.653 
                 4.81 
                 −9.257 
               
               
                 2466 
                 PHE328 
                 CG 
                 −10.261 
                 5.995 
                 −8.376 
               
               
                 2467 
                 PHE328 
                 CD1 
                 −9.098 
                 6.702 
                 −8.651 
               
               
                 2468 
                 PHE328 
                 CD2 
                 −11.07 
                 6.379 
                 −7.314 
               
               
                 2469 
                 PHE328 
                 CE1 
                 −8.737 
                 7.784 
                 −7.858 
               
               
                 2470 
                 PHE328 
                 CE2 
                 −10.709 
                 7.459 
                 −6.519 
               
               
                 2471 
                 PHE328 
                 CZ 
                 −9.542 
                 8.161 
                 −6.791 
               
               
                 2472 
                 GLU329 
                 N 
                 −10.377 
                 4.006 
                 −12.696 
               
               
                 2473 
                 GLU329 
                 CA 
                 −10.511 
                 2.993 
                 −13.752 
               
               
                 2474 
                 GLU329 
                 C 
                 −10.048 
                 1.63 
                 −13.253 
               
               
                 2475 
                 GLU329 
                 O 
                 −8.847 
                 1.399 
                 −13.092 
               
               
                 2476 
                 GLU329 
                 CB 
                 −9.673 
                 3.409 
                 −14.962 
               
               
                 2477 
                 GLU329 
                 CG 
                 −10.104 
                 4.752 
                 −15.557 
               
               
                 2478 
                 GLU329 
                 CD 
                 −9.106 
                 5.864 
                 −15.215 
               
               
                 2479 
                 GLU329 
                 OE1 
                 −8.54 
                 5.804 
                 −14.132 
               
               
                 2480 
                 GLU329 
                 OE2 
                 −8.904 
                 6.724 
                 −16.059 
               
               
                 2481 
                 ASN330 
                 N 
                 −10.987 
                 0.698 
                 −13.249 
               
               
                 2482 
                 ASN330 
                 CA 
                 −10.826 
                 −0.597 
                 −12.566 
               
               
                 2483 
                 ASN330 
                 C 
                 −10.252 
                 −0.375 
                 −11.171 
               
               
                 2484 
                 ASN330 
                 O 
                 −9.065 
                 −0.629 
                 −10.929 
               
               
                 2485 
                 ASN330 
                 CB 
                 −9.925 
                 −1.547 
                 −13.355 
               
               
                 2486 
                 ASN330 
                 CG 
                 −9.943 
                 −2.959 
                 −12.75 
               
               
                 2487 
                 ASN330 
                 OD1 
                 −9.958 
                 −3.151 
                 −11.523 
               
               
                 2488 
                 ASN330 
                 ND2 
                 −9.893 
                 −3.939 
                 −13.632 
               
               
                 2489 
                 PRO331 
                 N 
                 −11.157 
                 −0.201 
                 −10.224 
               
               
                 2490 
                 PRO331 
                 CA 
                 −10.787 
                 0.129 
                 −8.843 
               
               
                 2491 
                 PRO331 
                 C 
                 −10.287 
                 −1.061 
                 −8.012 
               
               
                 2492 
                 PRO331 
                 O 
                 −9.994 
                 −0.904 
                 −6.822 
               
               
                 2493 
                 PRO331 
                 CB 
                 −12.044 
                 0.673 
                 −8.25 
               
               
                 2494 
                 PRO331 
                 CG 
                 −13.21 
                 0.356 
                 −9.172 
               
               
                 2495 
                 PRO331 
                 CD 
                 −12.608 
                 −0.26 
                 −10.416 
               
               
                 2496 
                 ASP332 
                 N 
                 −10.198 
                 −2.236 
                 −8.615 
               
               
                 2497 
                 ASP332 
                 CA 
                 −9.742 
                 −3.417 
                 −7.889 
               
               
                 2498 
                 ASP332 
                 C 
                 −8.267 
                 −3.667 
                 −8.179 
               
               
                 2499 
                 ASP332 
                 O 
                 −7.609 
                 −4.447 
                 −7.478 
               
               
                 2500 
                 ASP332 
                 CB 
                 −10.557 
                 −4.617 
                 −8.358 
               
               
                 2501 
                 ASP332 
                 CG 
                 −12.048 
                 −4.356 
                 −8.173 
               
               
                 2502 
                 ASP332 
                 OD1 
                 −12.43 
                 −3.961 
                 −7.08 
               
               
                 2503 
                 ASP332 
                 OD2 
                 −12.784 
                 −4.566 
                 −9.127 
               
               
                 2504 
                 THR333 
                 N 
                 −7.744 
                 −2.97 
                 −9.173 
               
               
                 2505 
                 THR333 
                 CA 
                 −6.339 
                 −3.153 
                 −9.535 
               
               
                 2506 
                 THR333 
                 C 
                 −5.433 
                 −2.224 
                 −8.735 
               
               
                 2507 
                 THR333 
                 O 
                 −5.283 
                 −1.042 
                 −9.06 
               
               
                 2508 
                 THR333 
                 CB 
                 −6.189 
                 −2.877 
                 −11.026 
               
               
                 2509 
                 THR333 
                 OG1 
                 −7.072 
                 −3.748 
                 −11.718 
               
               
                 2510 
                 THR333 
                 CG2 
                 −4.769 
                 −3.147 
                 −11.514 
               
               
                 2511 
                 PHE334 
                 N 
                 −4.84 
                 −2.772 
                 −7.688 
               
               
                 2512 
                 PHE334 
                 CA 
                 −3.868 
                 −2.017 
                 −6.89 
               
               
                 2513 
                 PHE334 
                 C 
                 −2.589 
                 −1.762 
                 −7.684 
               
               
                 2514 
                 PHE334 
                 O 
                 −1.817 
                 −2.686 
                 −7.979 
               
               
                 2515 
                 PHE334 
                 CB 
                 −3.543 
                 −2.812 
                 −5.63 
               
               
                 2516 
                 PHE334 
                 CG 
                 −2.485 
                 −2.162 
                 −4.744 
               
               
                 2517 
                 PHE334 
                 CD1 
                 −2.784 
                 −1 
                 −4.047 
               
               
                 2518 
                 PHE334 
                 CD2 
                 −1.221 
                 −2.728 
                 −4.638 
               
               
                 2519 
                 PHE334 
                 CE1 
                 −1.82 
                 −0.404 
                 −3.246 
               
               
                 2520 
                 PHE334 
                 CE2 
                 −0.256 
                 −2.132 
                 −3.837 
               
               
                 2521 
                 PHE334 
                 CZ 
                 −0.556 
                 −0.969 
                 −3.142 
               
               
                 2522 
                 ASP335 
                 N 
                 −2.407 
                 −0.509 
                 −8.064 
               
               
                 2523 
                 ASP335 
                 CA 
                 −1.206 
                 −0.106 
                 −8.794 
               
               
                 2524 
                 ASP335 
                 C 
                 −0.697 
                 1.24 
                 −8.283 
               
               
                 2525 
                 ASP335 
                 O 
                 −1.322 
                 2.277 
                 −8.525 
               
               
                 2526 
                 ASP335 
                 CB 
                 −1.55 
                 −0.019 
                 −10.277 
               
               
                 2527 
                 ASP335 
                 CG 
                 −0.276 
                 0.2 
                 −11.084 
               
               
                 2528 
                 ASP335 
                 OD1 
                 0.34 
                 −0.792 
                 −11.448 
               
               
                 2529 
                 ASP335 
                 OD2 
                 0.15 
                 1.347 
                 −11.159 
               
               
                 2530 
                 ILE336 
                 N 
                 0.532 
                 1.249 
                 −7.794 
               
               
                 2531 
                 ILE336 
                 CA 
                 1.118 
                 2.426 
                 −7.127 
               
               
                 2532 
                 ILE336 
                 C 
                 1.596 
                 3.552 
                 −8.058 
               
               
                 2533 
                 ILE336 
                 O 
                 2.207 
                 4.512 
                 −7.579 
               
               
                 2534 
                 ILE336 
                 CB 
                 2.303 
                 1.948 
                 −6.301 
               
               
                 2535 
                 ILE336 
                 CG1 
                 3.437 
                 1.48 
                 −7.203 
               
               
                 2536 
                 ILE336 
                 CG2 
                 1.873 
                 0.817 
                 −5.375 
               
               
                 2537 
                 ILE336 
                 CD1 
                 4.676 
                 1.131 
                 −6.396 
               
               
                 2538 
                 GLU337 
                 N 
                 1.41 
                 3.407 
                 −9.361 
               
               
                 2539 
                 GLU337 
                 CA 
                 1.712 
                 4.496 
                 −10.291 
               
               
                 2540 
                 GLU337 
                 C 
                 0.434 
                 5.236 
                 −10.681 
               
               
                 2541 
                 GLU337 
                 O 
                 0.487 
                 6.246 
                 −11.393 
               
               
                 2542 
                 GLU337 
                 CB 
                 2.393 
                 3.936 
                 −11.533 
               
               
                 2543 
                 GLU337 
                 CG 
                 3.788 
                 3.412 
                 −11.213 
               
               
                 2544 
                 GLU337 
                 CD 
                 4.442 
                 2.871 
                 −12.481 
               
               
                 2545 
                 GLU337 
                 OE1 
                 3.934 
                 3.167 
                 −13.552 
               
               
                 2546 
                 GLU337 
                 OE2 
                 5.372 
                 2.089 
                 −12.348 
               
               
                 2547 
                 ARG338 
                 N 
                 −0.697 
                 4.719 
                 −10.229 
               
               
                 2548 
                 ARG338 
                 CA 
                 −1.982 
                 5.376 
                 −10.464 
               
               
                 2549 
                 ARG338 
                 C 
                 −2.095 
                 6.636 
                 −9.615 
               
               
                 2550 
                 ARG338 
                 O 
                 −1.809 
                 6.625 
                 −8.412 
               
               
                 2551 
                 ARG338 
                 CB 
                 −3.085 
                 4.393 
                 −10.082 
               
               
                 2552 
                 ARG338 
                 CG 
                 −4.484 
                 4.977 
                 −10.234 
               
               
                 2553 
                 ARG338 
                 CD 
                 −5.532 
                 3.961 
                 −9.809 
               
               
                 2554 
                 ARG338 
                 NE 
                 −5.375 
                 2.729 
                 −10.591 
               
               
                 2555 
                 ARG338 
                 CZ 
                 −6.357 
                 1.847 
                 −10.77 
               
               
                 2556 
                 ARG338 
                 NH1 
                 −7.549 
                 2.056 
                 −10.207 
               
               
                 2557 
                 ARG338 
                 NH2 
                 −6.143 
                 0.757 
                 −11.509 
               
               
                 2558 
                 GLY339 
                 N 
                 −2.423 
                 7.735 
                 −10.271 
               
               
                 2559 
                 GLY339 
                 CA 
                 −2.685 
                 8.98 
                 −9.55 
               
               
                 2560 
                 GLY339 
                 C 
                 −4.038 
                 8.895 
                 −8.852 
               
               
                 2561 
                 GLY339 
                 O 
                 −5.086 
                 9.045 
                 −9.489 
               
               
                 2562 
                 ALA340 
                 N 
                 −3.994 
                 8.767 
                 −7.534 
               
               
                 2563 
                 ALA340 
                 CA 
                 −5.202 
                 8.646 
                 −6.691 
               
               
                 2564 
                 ALA340 
                 C 
                 −5.871 
                 9.982 
                 −6.335 
               
               
                 2565 
                 ALA340 
                 O 
                 −6.419 
                 10.145 
                 −5.237 
               
               
                 2566 
                 ALA340 
                 CB 
                 −4.817 
                 7.907 
                 −5.414 
               
               
                 2567 
                 ARG341 
                 N 
                 −5.844 
                 10.917 
                 −7.27 
               
               
                 2568 
                 ARG341 
                 CA 
                 −6.395 
                 12.25 
                 −7.043 
               
               
                 2569 
                 ARG341 
                 C 
                 −7.904 
                 12.179 
                 −6.87 
               
               
                 2570 
                 ARG341 
                 O 
                 −8.571 
                 11.307 
                 −7.436 
               
               
                 2571 
                 ARG341 
                 CB 
                 −6.045 
                 13.131 
                 −8.235 
               
               
                 2572 
                 ARG341 
                 CG 
                 −4.535 
                 13.264 
                 −8.387 
               
               
                 2573 
                 ARG341 
                 CD 
                 −4.175 
                 14.135 
                 −9.583 
               
               
                 2574 
                 ARG341 
                 NE 
                 −2.718 
                 14.303 
                 −9.691 
               
               
                 2575 
                 ARG341 
                 CZ 
                 −2.142 
                 15.463 
                 −10.016 
               
               
                 2576 
                 ARG341 
                 NH1 
                 −2.898 
                 16.534 
                 −10.271 
               
               
                 2577 
                 ARG341 
                 NH2 
                 −0.813 
                 15.551 
                 −10.092 
               
               
                 2578 
                 HIS342 
                 N 
                 −8.378 
                 13.009 
                 −5.954 
               
               
                 2579 
                 HIS342 
                 CA 
                 −9.801 
                 13.12 
                 −5.603 
               
               
                 2580 
                 HIS342 
                 C 
                 −10.342 
                 11.888 
                 −4.88 
               
               
                 2581 
                 HIS342 
                 O 
                 −11.547 
                 11.621 
                 −4.961 
               
               
                 2582 
                 HIS342 
                 CB 
                 −10.644 
                 13.367 
                 −6.855 
               
               
                 2583 
                 HIS342 
                 CG 
                 −10.32 
                 14.641 
                 −7.606 
               
               
                 2584 
                 HIS342 
                 ND1 
                 −10.757 
                 15.877 
                 −7.303 
               
               
                 2585 
                 HIS342 
                 CD2 
                 −9.536 
                 14.758 
                 −8.731 
               
               
                 2586 
                 HIS342 
                 CE1 
                 −10.259 
                 16.758 
                 −8.195 
               
               
                 2587 
                 HIS342 
                 NE2 
                 −9.504 
                 16.064 
                 −9.078 
               
               
                 2588 
                 HIS343 
                 N 
                 −9.49 
                 11.15 
                 −4.184 
               
               
                 2589 
                 HIS343 
                 CA 
                 −10.02 
                 10.075 
                 −3.346 
               
               
                 2590 
                 HIS343 
                 C 
                 −10.572 
                 10.661 
                 −2.053 
               
               
                 2591 
                 HIS343 
                 O 
                 −9.984 
                 11.572 
                 −1.455 
               
               
                 2592 
                 HIS343 
                 CB 
                 −8.988 
                 8.965 
                 −3.085 
               
               
                 2593 
                 HIS343 
                 CG 
                 −7.691 
                 9.253 
                 −2.333 
               
               
                 2594 
                 HIS343 
                 ND1 
                 −7.374 
                 10.313 
                 −1.562 
               
               
                 2595 
                 HIS343 
                 CD2 
                 −6.597 
                 8.421 
                 −2.319 
               
               
                 2596 
                 HIS343 
                 CE1 
                 −6.125 
                 10.166 
                 −1.079 
               
               
                 2597 
                 HIS343 
                 NE2 
                 −5.643 
                 8.993 
                 −1.549 
               
               
                 2598 
                 VAL344 
                 N 
                 −11.634 
                 10.052 
                 −1.563 
               
               
                 2599 
                 VAL344 
                 CA 
                 −12.278 
                 10.521 
                 −0.331 
               
               
                 2600 
                 VAL344 
                 C 
                 −11.732 
                 9.82 
                 0.915 
               
               
                 2601 
                 VAL344 
                 O 
                 −12.271 
                 9.998 
                 2.015 
               
               
                 2602 
                 VAL344 
                 CB 
                 −13.787 
                 10.343 
                 −0.45 
               
               
                 2603 
                 VAL344 
                 CG1 
                 −14.412 
                 11.457 
                 −1.282 
               
               
                 2604 
                 VAL344 
                 CG2 
                 −14.141 
                 8.977 
                 −1.019 
               
               
                 2605 
                 ALA345 
                 N 
                 −10.581 
                 9.178 
                 0.768 
               
               
                 2606 
                 ALA345 
                 CA 
                 −9.947 
                 8.411 
                 1.849 
               
               
                 2607 
                 ALA345 
                 C 
                 −9.419 
                 9.24 
                 3.02 
               
               
                 2608 
                 ALA345 
                 O 
                 −9.242 
                 8.703 
                 4.12 
               
               
                 2609 
                 ALA345 
                 CB 
                 −8.757 
                 7.686 
                 1.237 
               
               
                 2610 
                 PHE346 
                 N 
                 −9.169 
                 10.518 
                 2.787 
               
               
                 2611 
                 PHE346 
                 CA 
                 −8.763 
                 11.424 
                 3.867 
               
               
                 2612 
                 PHE346 
                 C 
                 −9.885 
                 12.363 
                 4.291 
               
               
                 2613 
                 PHE346 
                 O 
                 −9.652 
                 13.29 
                 5.083 
               
               
                 2614 
                 PHE346 
                 CB 
                 −7.571 
                 12.253 
                 3.409 
               
               
                 2615 
                 PHE346 
                 CG 
                 −6.223 
                 11.583 
                 3.635 
               
               
                 2616 
                 PHE346 
                 CD1 
                 −5.295 
                 11.513 
                 2.605 
               
               
                 2617 
                 PHE346 
                 CD2 
                 −5.921 
                 11.048 
                 4.881 
               
               
                 2618 
                 PHE346 
                 CE1 
                 −4.061 
                 10.916 
                 2.825 
               
               
                 2619 
                 PHE346 
                 CE2 
                 −4.687 
                 10.451 
                 5.101 
               
               
                 2620 
                 PHE346 
                 CZ 
                 −3.756 
                 10.388 
                 4.073 
               
               
                 2621 
                 GLY347 
                 N 
                 −11.068 
                 12.169 
                 3.731 
               
               
                 2622 
                 GLY347 
                 CA 
                 −12.177 
                 13.091 
                 3.979 
               
               
                 2623 
                 GLY347 
                 C 
                 −12.007 
                 14.367 
                 3.158 
               
               
                 2624 
                 GLY347 
                 O 
                 −10.882 
                 14.764 
                 2.825 
               
               
                 2625 
                 PHE348 
                 N 
                 −13.123 
                 14.988 
                 2.822 
               
               
                 2626 
                 PHE348 
                 CA 
                 −13.084 
                 16.264 
                 2.097 
               
               
                 2627 
                 PHE348 
                 C 
                 −13.98 
                 17.307 
                 2.752 
               
               
                 2628 
                 PHE348 
                 O 
                 −14.185 
                 17.307 
                 3.976 
               
               
                 2629 
                 PHE348 
                 CB 
                 −13.497 
                 16.085 
                 0.64 
               
               
                 2630 
                 PHE348 
                 CG 
                 −12.375 
                 15.613 
                 −0.285 
               
               
                 2631 
                 PHE348 
                 CD1 
                 −12.654 
                 14.749 
                 −1.333 
               
               
                 2632 
                 PHE348 
                 CD2 
                 −11.075 
                 16.06 
                 −0.081 
               
               
                 2633 
                 PHE348 
                 CE1 
                 −11.633 
                 14.322 
                 −2.172 
               
               
                 2634 
                 PHE348 
                 CE2 
                 −10.054 
                 15.633 
                 −0.918 
               
               
                 2635 
                 PHE348 
                 CZ 
                 −10.332 
                 14.763 
                 −1.963 
               
               
                 2636 
                 GLY349 
                 N 
                 −14.438 
                 18.227 
                 1.918 
               
               
                 2637 
                 GLY349 
                 CA 
                 −15.269 
                 19.339 
                 2.376 
               
               
                 2638 
                 GLY349 
                 C 
                 −14.484 
                 20.194 
                 3.353 
               
               
                 2639 
                 GLY349 
                 O 
                 −13.286 
                 20.433 
                 3.165 
               
               
                 2640 
                 VAL350 
                 N 
                 −15.121 
                 20.525 
                 4.458 
               
               
                 2641 
                 VAL350 
                 CA 
                 −14.426 
                 21.29 
                 5.493 
               
               
                 2642 
                 VAL350 
                 C 
                 −13.865 
                 20.408 
                 6.613 
               
               
                 2643 
                 VAL350 
                 O 
                 −12.964 
                 20.854 
                 7.327 
               
               
                 2644 
                 VAL350 
                 CB 
                 −15.384 
                 22.334 
                 6.062 
               
               
                 2645 
                 VAL350 
                 CG1 
                 −15.675 
                 23.433 
                 5.047 
               
               
                 2646 
                 VAL350 
                 CG2 
                 −16.682 
                 21.709 
                 6.561 
               
               
                 2647 
                 HIS351 
                 N 
                 −14.217 
                 19.133 
                 6.631 
               
               
                 2648 
                 HIS351 
                 CA 
                 −13.875 
                 18.287 
                 7.784 
               
               
                 2649 
                 HIS351 
                 C 
                 −12.75 
                 17.284 
                 7.532 
               
               
                 2650 
                 HIS351 
                 O 
                 −12.711 
                 16.259 
                 8.223 
               
               
                 2651 
                 HIS351 
                 CB 
                 −15.113 
                 17.514 
                 8.23 
               
               
                 2652 
                 HIS351 
                 CG 
                 −16.205 
                 18.349 
                 8.87 
               
               
                 2653 
                 HIS351 
                 ND1 
                 −16.137 
                 18.987 
                 10.054 
               
               
                 2654 
                 HIS351 
                 CD2 
                 −17.46 
                 18.588 
                 8.36 
               
               
                 2655 
                 HIS351 
                 CE1 
                 −17.304 
                 19.619 
                 10.29 
               
               
                 2656 
                 HIS351 
                 NE2 
                 −18.122 
                 19.372 
                 9.242 
               
               
                 2657 
                 GLN352 
                 N 
                 −11.876 
                 17.53 
                 6.568 
               
               
                 2658 
                 GLN352 
                 CA 
                 −10.852 
                 16.518 
                 6.26 
               
               
                 2659 
                 GLN352 
                 C 
                 −9.793 
                 16.385 
                 7.357 
               
               
                 2660 
                 GLN352 
                 O 
                 −9.716 
                 17.193 
                 8.291 
               
               
                 2661 
                 GLN352 
                 CB 
                 −10.178 
                 16.785 
                 4.923 
               
               
                 2662 
                 GLN352 
                 CG 
                 −9.244 
                 17.98 
                 4.902 
               
               
                 2663 
                 GLN352 
                 CD 
                 −8.308 
                 17.803 
                 3.712 
               
               
                 2664 
                 GLN352 
                 OE1 
                 −7.316 
                 18.528 
                 3.568 
               
               
                 2665 
                 GLN352 
                 NE2 
                 −8.572 
                 16.766 
                 2.934 
               
               
                 2666 
                 CYS353 
                 N 
                 −9.049 
                 15.296 
                 7.271 
               
               
                 2667 
                 CYS353 
                 CA 
                 −8.044 
                 14.964 
                 8.287 
               
               
                 2668 
                 CYS353 
                 C 
                 −6.883 
                 15.962 
                 8.319 
               
               
                 2669 
                 CYS353 
                 O 
                 −6.101 
                 16.072 
                 7.366 
               
               
                 2670 
                 CYS353 
                 CB 
                 −7.524 
                 13.567 
                 7.961 
               
               
                 2671 
                 CYS353 
                 SG 
                 −6.412 
                 12.816 
                 9.17 
               
               
                 2672 
                 LEU354 
                 N 
                 −6.724 
                 16.61 
                 9.464 
               
               
                 2673 
                 LEU354 
                 CA 
                 −5.607 
                 17.549 
                 9.666 
               
               
                 2674 
                 LEU354 
                 C 
                 −4.308 
                 16.852 
                 10.059 
               
               
                 2675 
                 LEU354 
                 O 
                 −3.224 
                 17.358 
                 9.747 
               
               
                 2676 
                 LEU354 
                 CB 
                 −5.967 
                 18.561 
                 10.748 
               
               
                 2677 
                 LEU354 
                 CG 
                 −6.805 
                 19.7 
                 10.188 
               
               
                 2678 
                 LEU354 
                 CD1 
                 −7.148 
                 20.701 
                 11.284 
               
               
                 2679 
                 LEU354 
                 CD2 
                 −6.054 
                 20.396 
                 9.057 
               
               
                 2680 
                 GLY355 
                 N 
                 −4.414 
                 15.6 
                 10.478 
               
               
                 2681 
                 GLY355 
                 CA 
                 −3.223 
                 14.791 
                 10.772 
               
               
                 2682 
                 GLY355 
                 C 
                 −2.835 
                 13.936 
                 9.566 
               
               
                 2683 
                 GLY355 
                 O 
                 −2.119 
                 12.936 
                 9.702 
               
               
                 2684 
                 GLN356 
                 N 
                 −3.078 
                 14.499 
                 8.393 
               
               
                 2685 
                 GLN356 
                 CA 
                 −2.896 
                 13.81 
                 7.119 
               
               
                 2686 
                 GLN356 
                 C 
                 −1.414 
                 13.677 
                 6.799 
               
               
                 2687 
                 GLN356 
                 O 
                 −0.939 
                 12.562 
                 6.544 
               
               
                 2688 
                 GLN356 
                 CB 
                 −3.598 
                 14.696 
                 6.094 
               
               
                 2689 
                 GLN356 
                 CG 
                 −3.657 
                 14.117 
                 4.691 
               
               
                 2690 
                 GLN356 
                 CD 
                 −4.524 
                 15.024 
                 3.818 
               
               
                 2691 
                 GLN356 
                 OE1 
                 −4.609 
                 14.834 
                 2.599 
               
               
                 2692 
                 GLN356 
                 NE2 
                 −5.231 
                 15.939 
                 4.463 
               
               
                 2693 
                 ASN357 
                 N 
                 −0.67 
                 14.7 
                 7.191 
               
               
                 2694 
                 ASN357 
                 CA 
                 0.781 
                 14.7 
                 7.005 
               
               
                 2695 
                 ASN357 
                 C 
                 1.476 
                 13.761 
                 7.989 
               
               
                 2696 
                 ASN357 
                 O 
                 2.328 
                 12.977 
                 7.554 
               
               
                 2697 
                 ASN357 
                 CB 
                 1.258 
                 16.137 
                 7.203 
               
               
                 2698 
                 ASN357 
                 CG 
                 2.78 
                 16.244 
                 7.261 
               
               
                 2699 
                 ASN357 
                 OD1 
                 3.324 
                 16.808 
                 8.217 
               
               
                 2700 
                 ASN357 
                 ND2 
                 3.444 
                 15.745 
                 6.233 
               
               
                 2701 
                 LEU358 
                 N 
                 0.896 
                 13.592 
                 9.166 
               
               
                 2702 
                 LEU358 
                 CA 
                 1.515 
                 12.727 
                 10.168 
               
               
                 2703 
                 LEU358 
                 C 
                 1.271 
                 11.264 
                 9.826 
               
               
                 2704 
                 LEU358 
                 O 
                 2.234 
                 10.487 
                 9.791 
               
               
                 2705 
                 LEU358 
                 CB 
                 0.908 
                 13.034 
                 11.53 
               
               
                 2706 
                 LEU358 
                 CG 
                 1.612 
                 12.261 
                 12.639 
               
               
                 2707 
                 LEU358 
                 CD1 
                 3.089 
                 12.639 
                 12.712 
               
               
                 2708 
                 LEU358 
                 CD2 
                 0.931 
                 12.493 
                 13.982 
               
               
                 2709 
                 ALA359 
                 N 
                 0.102 
                 10.986 
                 9.272 
               
               
                 2710 
                 ALA359 
                 CA 
                 −0.235 
                 9.616 
                 8.887 
               
               
                 2711 
                 ALA359 
                 C 
                 0.571 
                 9.151 
                 7.679 
               
               
                 2712 
                 ALA359 
                 O 
                 1.204 
                 8.089 
                 7.756 
               
               
                 2713 
                 ALA359 
                 CB 
                 −1.723 
                 9.558 
                 8.566 
               
               
                 2714 
                 ARG360 
                 N 
                 0.794 
                 10.045 
                 6.728 
               
               
                 2715 
                 ARG360 
                 CA 
                 1.585 
                 9.681 
                 5.546 
               
               
                 2716 
                 ARG360 
                 C 
                 3.078 
                 9.603 
                 5.853 
               
               
                 2717 
                 ARG360 
                 O 
                 3.747 
                 8.677 
                 5.374 
               
               
                 2718 
                 ARG360 
                 CB 
                 1.354 
                 10.721 
                 4.459 
               
               
                 2719 
                 ARG360 
                 CG 
                 −0.081 
                 10.681 
                 3.954 
               
               
                 2720 
                 ARG360 
                 CD 
                 −0.325 
                 11.752 
                 2.898 
               
               
                 2721 
                 ARG360 
                 NE 
                 −0.144 
                 13.097 
                 3.463 
               
               
                 2722 
                 ARG360 
                 CZ 
                 0.509 
                 14.076 
                 2.833 
               
               
                 2723 
                 ARG360 
                 NH1 
                 0.602 
                 15.283 
                 3.393 
               
               
                 2724 
                 ARG360 
                 NH2 
                 1.045 
                 13.853 
                 1.631 
               
               
                 2725 
                 LEU361 
                 N 
                 3.518 
                 10.379 
                 6.83 
               
               
                 2726 
                 LEU361 
                 CA 
                 4.921 
                 10.356 
                 7.239 
               
               
                 2727 
                 LEU361 
                 C 
                 5.238 
                 9.078 
                 8.005 
               
               
                 2728 
                 LEU361 
                 O 
                 6.174 
                 8.36 
                 7.628 
               
               
                 2729 
                 LEU361 
                 CB 
                 5.159 
                 11.566 
                 8.133 
               
               
                 2730 
                 LEU361 
                 CG 
                 6.612 
                 11.69 
                 8.572 
               
               
                 2731 
                 LEU361 
                 CD1 
                 7.537 
                 11.811 
                 7.365 
               
               
                 2732 
                 LEU361 
                 CD2 
                 6.778 
                 12.888 
                 9.498 
               
               
                 2733 
                 GLU362 
                 N 
                 4.306 
                 8.658 
                 8.846 
               
               
                 2734 
                 GLU362 
                 CA 
                 4.499 
                 7.431 
                 9.622 
               
               
                 2735 
                 GLU362 
                 C 
                 4.413 
                 6.2 
                 8.73 
               
               
                 2736 
                 GLU362 
                 O 
                 5.31 
                 5.352 
                 8.793 
               
               
                 2737 
                 GLU362 
                 CB 
                 3.418 
                 7.347 
                 10.694 
               
               
                 2738 
                 GLU362 
                 CG 
                 3.519 
                 8.493 
                 11.693 
               
               
                 2739 
                 GLU362 
                 CD 
                 2.341 
                 8.447 
                 12.662 
               
               
                 2740 
                 GLU362 
                 OE1 
                 1.268 
                 8.901 
                 12.284 
               
               
                 2741 
                 GLU362 
                 OE2 
                 2.517 
                 7.891 
                 13.736 
               
               
                 2742 
                 LEU363 
                 N 
                 3.541 
                 6.253 
                 7.736 
               
               
                 2743 
                 LEU363 
                 CA 
                 3.389 
                 5.125 
                 6.814 
               
               
                 2744 
                 LEU363 
                 C 
                 4.61 
                 4.946 
                 5.927 
               
               
                 2745 
                 LEU363 
                 O 
                 5.174 
                 3.844 
                 5.889 
               
               
                 2746 
                 LEU363 
                 CB 
                 2.184 
                 5.364 
                 5.914 
               
               
                 2747 
                 LEU363 
                 CG 
                 0.977 
                 4.517 
                 6.298 
               
               
                 2748 
                 LEU363 
                 CD1 
                 0.35 
                 4.995 
                 7.601 
               
               
                 2749 
                 LEU363 
                 CD2 
                 −0.056 
                 4.54 
                 5.179 
               
               
                 2750 
                 GLN364 
                 N 
                 5.151 
                 6.047 
                 5.432 
               
               
                 2751 
                 GLN364 
                 CA 
                 6.296 
                 5.955 
                 4.529 
               
               
                 2752 
                 GLN364 
                 C 
                 7.559 
                 5.544 
                 5.276 
               
               
                 2753 
                 GLN364 
                 O 
                 8.219 
                 4.588 
                 4.843 
               
               
                 2754 
                 GLN364 
                 CB 
                 6.505 
                 7.308 
                 3.86 
               
               
                 2755 
                 GLN364 
                 CG 
                 7.624 
                 7.232 
                 2.83 
               
               
                 2756 
                 GLN364 
                 CD 
                 7.846 
                 8.592 
                 2.181 
               
               
                 2757 
                 GLN364 
                 OE1 
                 7.741 
                 9.637 
                 2.835 
               
               
                 2758 
                 GLN364 
                 NE2 
                 8.108 
                 8.565 
                 0.886 
               
               
                 2759 
                 ILE365 
                 N 
                 7.707 
                 6.019 
                 6.503 
               
               
                 2760 
                 ILE365 
                 CA 
                 8.879 
                 5.644 
                 7.298 
               
               
                 2761 
                 ILE365 
                 C 
                 8.835 
                 4.171 
                 7.691 
               
               
                 2762 
                 ILE365 
                 O 
                 9.772 
                 3.438 
                 7.339 
               
               
                 2763 
                 ILE365 
                 CB 
                 8.94 
                 6.511 
                 8.554 
               
               
                 2764 
                 ILE365 
                 CG1 
                 9.202 
                 7.973 
                 8.208 
               
               
                 2765 
                 ILE365 
                 CG2 
                 10.012 
                 5.996 
                 9.506 
               
               
                 2766 
                 ILE365 
                 CD1 
                 10.539 
                 8.151 
                 7.497 
               
               
                 2767 
                 VAL366 
                 N 
                 7.667 
                 3.695 
                 8.099 
               
               
                 2768 
                 VAL366 
                 CA 
                 7.555 
                 2.301 
                 8.53 
               
               
                 2769 
                 VAL366 
                 C 
                 7.703 
                 1.335 
                 7.361 
               
               
                 2770 
                 VAL366 
                 O 
                 8.611 
                 0.497 
                 7.417 
               
               
                 2771 
                 VAL366 
                 CB 
                 6.21 
                 2.076 
                 9.217 
               
               
                 2772 
                 VAL366 
                 CG1 
                 6.011 
                 0.606 
                 9.565 
               
               
                 2773 
                 VAL366 
                 CG2 
                 6.085 
                 2.923 
                 10.477 
               
               
                 2774 
                 PHE367 
                 N 
                 7.094 
                 1.641 
                 6.225 
               
               
                 2775 
                 PHE367 
                 CA 
                 7.145 
                 0.701 
                 5.097 
               
               
                 2776 
                 PHE367 
                 C 
                 8.524 
                 0.663 
                 4.453 
               
               
                 2777 
                 PHE367 
                 O 
                 9.066 
                 −0.434 
                 4.254 
               
               
                 2778 
                 PHE367 
                 CB 
                 6.125 
                 1.099 
                 4.034 
               
               
                 2779 
                 PHE367 
                 CG 
                 4.662 
                 1.012 
                 4.458 
               
               
                 2780 
                 PHE367 
                 CD1 
                 3.726 
                 1.83 
                 3.841 
               
               
                 2781 
                 PHE367 
                 CD2 
                 4.258 
                 0.112 
                 5.435 
               
               
                 2782 
                 PHE367 
                 CE1 
                 2.391 
                 1.767 
                 4.216 
               
               
                 2783 
                 PHE367 
                 CE2 
                 2.924 
                 0.052 
                 5.813 
               
               
                 2784 
                 PHE367 
                 CZ 
                 1.99 
                 0.88 
                 5.206 
               
               
                 2785 
                 ASP368 
                 N 
                 9.187 
                 1.808 
                 4.423 
               
               
                 2786 
                 ASP368 
                 CA 
                 10.522 
                 1.869 
                 3.83 
               
               
                 2787 
                 ASP368 
                 C 
                 11.52 
                 1.102 
                 4.686 
               
               
                 2788 
                 ASP368 
                 O 
                 12.115 
                 0.138 
                 4.185 
               
               
                 2789 
                 ASP368 
                 CB 
                 10.964 
                 3.326 
                 3.707 
               
               
                 2790 
                 ASP368 
                 CG 
                 10.101 
                 4.09 
                 2.701 
               
               
                 2791 
                 ASP368 
                 OD1 
                 10.208 
                 5.31 
                 2.678 
               
               
                 2792 
                 ASP368 
                 OD2 
                 9.508 
                 3.443 
                 1.847 
               
               
                 2793 
                 THR369 
                 N 
                 11.438 
                 1.285 
                 5.995 
               
               
                 2794 
                 THR369 
                 CA 
                 12.381 
                 0.606 
                 6.892 
               
               
                 2795 
                 THR369 
                 C 
                 12.07 
                 −0.88 
                 7.076 
               
               
                 2796 
                 THR369 
                 O 
                 13.004 
                 −1.658 
                 7.287 
               
               
                 2797 
                 THR369 
                 CB 
                 12.376 
                 1.294 
                 8.252 
               
               
                 2798 
                 THR369 
                 OG1 
                 11.058 
                 1.242 
                 8.778 
               
               
                 2799 
                 THR369 
                 CG2 
                 12.797 
                 2.756 
                 8.149 
               
               
                 2800 
                 LEU370 
                 N 
                 10.848 
                 −1.302 
                 6.793 
               
               
                 2801 
                 LEU370 
                 CA 
                 10.523 
                 −2.729 
                 6.862 
               
               
                 2802 
                 LEU370 
                 C 
                 11.145 
                 −3.486 
                 5.703 
               
               
                 2803 
                 LEU370 
                 O 
                 12.038 
                 −4.319 
                 5.916 
               
               
                 2804 
                 LEU370 
                 CB 
                 9.012 
                 −2.919 
                 6.78 
               
               
                 2805 
                 LEU370 
                 CG 
                 8.302 
                 −2.463 
                 8.044 
               
               
                 2806 
                 LEU370 
                 CD1 
                 6.792 
                 −2.589 
                 7.882 
               
               
                 2807 
                 LEU370 
                 CD2 
                 8.79 
                 −3.256 
                 9.248 
               
               
                 2808 
                 PHE371 
                 N 
                 10.872 
                 −3.006 
                 4.502 
               
               
                 2809 
                 PHE371 
                 CA 
                 11.266 
                 −3.75 
                 3.303 
               
               
                 2810 
                 PHE371 
                 C 
                 12.728 
                 −3.529 
                 2.918 
               
               
                 2811 
                 PHE371 
                 O 
                 13.332 
                 −4.398 
                 2.278 
               
               
                 2812 
                 PHE371 
                 CB 
                 10.333 
                 −3.34 
                 2.169 
               
               
                 2813 
                 PHE371 
                 CG 
                 8.861 
                 −3.634 
                 2.463 
               
               
                 2814 
                 PHE371 
                 CD1 
                 7.935 
                 −2.599 
                 2.503 
               
               
                 2815 
                 PHE371 
                 CD2 
                 8.447 
                 −4.94 
                 2.692 
               
               
                 2816 
                 PHE371 
                 CE1 
                 6.601 
                 −2.867 
                 2.784 
               
               
                 2817 
                 PHE371 
                 CE2 
                 7.112 
                 −5.209 
                 2.971 
               
               
                 2818 
                 PHE371 
                 CZ 
                 6.19 
                 −4.172 
                 3.019 
               
               
                 2819 
                 ARG372 
                 N 
                 13.335 
                 −2.472 
                 3.436 
               
               
                 2820 
                 ARG372 
                 CA 
                 14.773 
                 −2.281 
                 3.231 
               
               
                 2821 
                 ARG372 
                 C 
                 15.606 
                 −2.901 
                 4.353 
               
               
                 2822 
                 ARG372 
                 O 
                 16.834 
                 −2.982 
                 4.229 
               
               
                 2823 
                 ARG372 
                 CB 
                 15.084 
                 −0.795 
                 3.116 
               
               
                 2824 
                 ARG372 
                 CG 
                 14.397 
                 −0.176 
                 1.904 
               
               
                 2825 
                 ARG372 
                 CD 
                 14.777 
                 1.291 
                 1.76 
               
               
                 2826 
                 ARG372 
                 NE 
                 14.497 
                 2.015 
                 3.008 
               
               
                 2827 
                 ARG372 
                 CZ 
                 14.919 
                 3.257 
                 3.251 
               
               
                 2828 
                 ARG372 
                 NH1 
                 14.646 
                 3.835 
                 4.423 
               
               
                 2829 
                 ARG372 
                 NH2 
                 15.631 
                 3.911 
                 2.331 
               
               
                 2830 
                 ARG373 
                 N 
                 14.958 
                 −3.347 
                 5.418 
               
               
                 2831 
                 ARG373 
                 CA 
                 15.671 
                 −4.087 
                 6.457 
               
               
                 2832 
                 ARG373 
                 C 
                 15.659 
                 −5.559 
                 6.09 
               
               
                 2833 
                 ARG373 
                 O 
                 16.694 
                 −6.238 
                 6.097 
               
               
                 2834 
                 ARG373 
                 CB 
                 14.937 
                 −3.926 
                 7.783 
               
               
                 2835 
                 ARG373 
                 CG 
                 15.657 
                 −4.637 
                 8.922 
               
               
                 2836 
                 ARG373 
                 CD 
                 16.912 
                 −3.879 
                 9.335 
               
               
                 2837 
                 ARG373 
                 NE 
                 16.548 
                 −2.554 
                 9.862 
               
               
                 2838 
                 ARG373 
                 CZ 
                 16.405 
                 −2.304 
                 11.165 
               
               
                 2839 
                 ARG373 
                 NH1 
                 16.663 
                 −3.261 
                 12.059 
               
               
                 2840 
                 ARG373 
                 NH2 
                 16.046 
                 −1.087 
                 11.576 
               
               
                 2841 
                 VAL374 
                 N 
                 14.474 
                 −6.032 
                 5.749 
               
               
                 2842 
                 VAL374 
                 CA 
                 14.314 
                 −7.425 
                 5.338 
               
               
                 2843 
                 VAL374 
                 C 
                 13.644 
                 −7.499 
                 3.971 
               
               
                 2844 
                 VAL374 
                 O 
                 12.43 
                 −7.307 
                 3.841 
               
               
                 2845 
                 VAL374 
                 CB 
                 13.473 
                 −8.164 
                 6.376 
               
               
                 2846 
                 VAL374 
                 CG1 
                 13.297 
                 −9.625 
                 5.984 
               
               
                 2847 
                 VAL374 
                 CG2 
                 14.086 
                 −8.075 
                 7.77 
               
               
                 2848 
                 PRO375 
                 N 
                 14.432 
                 −7.873 
                 2.976 
               
               
                 2849 
                 PRO375 
                 CA 
                 13.929 
                 −8.036 
                 1.606 
               
               
                 2850 
                 PRO375 
                 C 
                 13.088 
                 −9.304 
                 1.369 
               
               
                 2851 
                 PRO375 
                 O 
                 12.539 
                 −9.472 
                 0.275 
               
               
                 2852 
                 PRO375 
                 CB 
                 15.165 
                 −8.072 
                 0.76 
               
               
                 2853 
                 PRO375 
                 CG 
                 16.384 
                 −8.221 
                 1.658 
               
               
                 2854 
                 PRO375 
                 CD 
                 15.865 
                 −8.159 
                 3.084 
               
               
                 2855 
                 GLY376 
                 N 
                 12.945 
                 −10.158 
                 2.371 
               
               
                 2856 
                 GLY376 
                 CA 
                 12.162 
                 −11.386 
                 2.21 
               
               
                 2857 
                 GLY376 
                 C 
                 11.071 
                 −11.52 
                 3.271 
               
               
                 2858 
                 GLY376 
                 O 
                 11.012 
                 −12.523 
                 3.992 
               
               
                 2859 
                 ILE377 
                 N 
                 10.225 
                 −10.508 
                 3.367 
               
               
                 2860 
                 ILE377 
                 CA 
                 9.092 
                 −10.568 
                 4.299 
               
               
                 2861 
                 ILE377 
                 C 
                 7.921 
                 −11.295 
                 3.645 
               
               
                 2862 
                 ILE377 
                 O 
                 7.217 
                 −10.731 
                 2.801 
               
               
                 2863 
                 ILE377 
                 CB 
                 8.663 
                 −9.148 
                 4.656 
               
               
                 2864 
                 ILE377 
                 CG1 
                 9.836 
                 −8.352 
                 5.203 
               
               
                 2865 
                 ILE377 
                 CG2 
                 7.529 
                 −9.169 
                 5.674 
               
               
                 2866 
                 ILE377 
                 CD1 
                 9.433 
                 −6.919 
                 5.526 
               
               
                 2867 
                 ARG378 
                 N 
                 7.743 
                 −12.55 
                 4.009 
               
               
                 2868 
                 ARG378 
                 CA 
                 6.648 
                 −13.342 
                 3.451 
               
               
                 2869 
                 ARG378 
                 C 
                 5.468 
                 −13.417 
                 4.409 
               
               
                 2870 
                 ARG378 
                 O 
                 5.629 
                 −13.304 
                 5.627 
               
               
                 2871 
                 ARG378 
                 CB 
                 7.186 
                 −14.734 
                 3.163 
               
               
                 2872 
                 ARG378 
                 CG 
                 8.265 
                 −14.671 
                 2.089 
               
               
                 2873 
                 ARG378 
                 CD 
                 8.975 
                 −16.01 
                 1.929 
               
               
                 2874 
                 ARG378 
                 NE 
                 9.756 
                 −16.33 
                 3.134 
               
               
                 2875 
                 ARG378 
                 CZ 
                 9.57 
                 −17.431 
                 3.864 
               
               
                 2876 
                 ARG378 
                 NH1 
                 8.587 
                 −18.28 
                 3.556 
               
               
                 2877 
                 ARG378 
                 NH2 
                 10.338 
                 −17.659 
                 4.931 
               
               
                 2878 
                 ILE379 
                 N 
                 4.277 
                 −13.531 
                 3.854 
               
               
                 2879 
                 ILE379 
                 CA 
                 3.096 
                 −13.713 
                 4.703 
               
               
                 2880 
                 ILE379 
                 C 
                 3.14 
                 −15.13 
                 5.272 
               
               
                 2881 
                 ILE379 
                 O 
                 3.519 
                 −16.07 
                 4.563 
               
               
                 2882 
                 ILE379 
                 CB 
                 1.841 
                 −13.536 
                 3.855 
               
               
                 2883 
                 ILE379 
                 CG1 
                 2.108 
                 −12.589 
                 2.692 
               
               
                 2884 
                 ILE379 
                 CG2 
                 0.702 
                 −12.984 
                 4.709 
               
               
                 2885 
                 ILE379 
                 CD1 
                 0.882 
                 −12.447 
                 1.798 
               
               
                 2886 
                 ALA380 
                 N 
                 2.872 
                 −15.267 
                 6.56 
               
               
                 2887 
                 ALA380 
                 CA 
                 2.895 
                 −16.598 
                 7.174 
               
               
                 2888 
                 ALA380 
                 C 
                 1.533 
                 −17.277 
                 7.07 
               
               
                 2889 
                 ALA380 
                 O 
                 1.435 
                 −18.51 
                 7.097 
               
               
                 2890 
                 ALA380 
                 CB 
                 3.306 
                 −16.471 
                 8.635 
               
               
                 2891 
                 VAL381 
                 N 
                 0.498 
                 −16.47 
                 6.917 
               
               
                 2892 
                 VAL381 
                 CA 
                 −0.839 
                 −17.005 
                 6.651 
               
               
                 2893 
                 VAL381 
                 C 
                 −1.231 
                 −16.745 
                 5.2 
               
               
                 2894 
                 VAL381 
                 O 
                 −0.782 
                 −15.768 
                 4.59 
               
               
                 2895 
                 VAL381 
                 CB 
                 −1.847 
                 −16.359 
                 7.599 
               
               
                 2896 
                 VAL381 
                 CG1 
                 −1.705 
                 −16.897 
                 9.018 
               
               
                 2897 
                 VAL381 
                 CG2 
                 −1.747 
                 −14.839 
                 7.57 
               
               
                 2898 
                 PRO382 
                 N 
                 −1.999 
                 −17.662 
                 4.635 
               
               
                 2899 
                 PRO382 
                 CA 
                 −2.615 
                 −17.424 
                 3.329 
               
               
                 2900 
                 PRO382 
                 C 
                 −3.477 
                 −16.166 
                 3.352 
               
               
                 2901 
                 PRO382 
                 O 
                 −4.045 
                 −15.802 
                 4.391 
               
               
                 2902 
                 PRO382 
                 CB 
                 −3.422 
                 −18.651 
                 3.039 
               
               
                 2903 
                 PRO382 
                 CG 
                 −3.29 
                 −19.627 
                 4.198 
               
               
                 2904 
                 PRO382 
                 CD 
                 −2.414 
                 −18.938 
                 5.231 
               
               
                 2905 
                 VAL383 
                 N 
                 −3.721 
                 −15.621 
                 2.172 
               
               
                 2906 
                 VAL383 
                 CA 
                 −4.415 
                 −14.327 
                 2.051 
               
               
                 2907 
                 VAL383 
                 C 
                 −5.892 
                 −14.388 
                 2.452 
               
               
                 2908 
                 VAL383 
                 O 
                 −6.376 
                 −13.473 
                 3.126 
               
               
                 2909 
                 VAL383 
                 CB 
                 −4.302 
                 −13.886 
                 0.593 
               
               
                 2910 
                 VAL383 
                 CG1 
                 −5.05 
                 −12.578 
                 0.343 
               
               
                 2911 
                 VAL383 
                 CG2 
                 −2.838 
                 −13.751 
                 0.177 
               
               
                 2912 
                 ASP384 
                 N 
                 −6.478 
                 −15.572 
                 2.355 
               
               
                 2913 
                 ASP384 
                 CA 
                 −7.876 
                 −15.767 
                 2.759 
               
               
                 2914 
                 ASP384 
                 C 
                 −8.031 
                 −15.962 
                 4.271 
               
               
                 2915 
                 ASP384 
                 O 
                 −9.156 
                 −16.094 
                 4.761 
               
               
                 2916 
                 ASP384 
                 CB 
                 −8.42 
                 −17.003 
                 2.048 
               
               
                 2917 
                 ASP384 
                 CG 
                 −8.293 
                 −16.849 
                 0.534 
               
               
                 2918 
                 ASP384 
                 OD1 
                 −9.1 
                 −16.128 
                 −0.032 
               
               
                 2919 
                 ASP384 
                 OD2 
                 −7.312 
                 −17.346 
                 −0.002 
               
               
                 2920 
                 GLU385 
                 N 
                 −6.926 
                 −15.995 
                 5 
               
               
                 2921 
                 GLU385 
                 CA 
                 −6.994 
                 −16.177 
                 6.448 
               
               
                 2922 
                 GLU385 
                 C 
                 −6.674 
                 −14.884 
                 7.194 
               
               
                 2923 
                 GLU385 
                 O 
                 −6.638 
                 −14.896 
                 8.429 
               
               
                 2924 
                 GLU385 
                 CB 
                 −6.01 
                 −17.259 
                 6.874 
               
               
                 2925 
                 GLU385 
                 CG 
                 −6.219 
                 −18.561 
                 6.111 
               
               
                 2926 
                 GLU385 
                 CD 
                 −7.651 
                 −19.079 
                 6.248 
               
               
                 2927 
                 GLU385 
                 OE1 
                 −8.017 
                 −19.462 
                 7.349 
               
               
                 2928 
                 GLU385 
                 OE2 
                 −8.266 
                 −19.256 
                 5.205 
               
               
                 2929 
                 LEU386 
                 N 
                 −6.406 
                 −13.81 
                 6.463 
               
               
                 2930 
                 LEU386 
                 CA 
                 −6.082 
                 −12.519 
                 7.093 
               
               
                 2931 
                 LEU386 
                 C 
                 −7.266 
                 −11.953 
                 7.874 
               
               
                 2932 
                 LEU386 
                 O 
                 −8.342 
                 −11.71 
                 7.315 
               
               
                 2933 
                 LEU386 
                 CB 
                 −5.676 
                 −11.542 
                 5.996 
               
               
                 2934 
                 LEU386 
                 CG 
                 −4.348 
                 −11.943 
                 5.365 
               
               
                 2935 
                 LEU386 
                 CD1 
                 −4.081 
                 −11.153 
                 4.091 
               
               
                 2936 
                 LEU386 
                 CD2 
                 −3.204 
                 −11.773 
                 6.357 
               
               
                 2937 
                 PRO387 
                 N 
                 −7.063 
                 −11.798 
                 9.173 
               
               
                 2938 
                 PRO387 
                 CA 
                 −8.132 
                 −11.39 
                 10.091 
               
               
                 2939 
                 PRO387 
                 C 
                 −8.419 
                 −9.89 
                 10.047 
               
               
                 2940 
                 PRO387 
                 O 
                 −7.84 
                 −9.095 
                 10.805 
               
               
                 2941 
                 PRO387 
                 CB 
                 −7.647 
                 −11.801 
                 11.445 
               
               
                 2942 
                 PRO387 
                 CG 
                 −6.191 
                 −12.224 
                 11.339 
               
               
                 2943 
                 PRO387 
                 CD 
                 −5.817 
                 −12.105 
                 9.873 
               
               
                 2944 
                 PHE388 
                 N 
                 −9.314 
                 −9.528 
                 9.143 
               
               
                 2945 
                 PHE388 
                 CA 
                 −9.775 
                 −8.145 
                 9.012 
               
               
                 2946 
                 PHE388 
                 C 
                 −10.688 
                 −7.79 
                 10.176 
               
               
                 2947 
                 PHE388 
                 O 
                 −11.522 
                 −8.597 
                 10.603 
               
               
                 2948 
                 PHE388 
                 CB 
                 −10.558 
                 −7.999 
                 7.709 
               
               
                 2949 
                 PHE388 
                 CG 
                 −9.785 
                 −8.343 
                 6.437 
               
               
                 2950 
                 PHE388 
                 CD1 
                 −8.78 
                 −7.498 
                 5.987 
               
               
                 2951 
                 PHE388 
                 CD2 
                 −10.097 
                 −9.492 
                 5.721 
               
               
                 2952 
                 PHE388 
                 CE1 
                 −8.076 
                 −7.809 
                 4.831 
               
               
                 2953 
                 PHE388 
                 CE2 
                 −9.393 
                 −9.804 
                 4.565 
               
               
                 2954 
                 PHE388 
                 CZ 
                 −8.381 
                 −8.963 
                 4.121 
               
               
                 2955 
                 LYS389 
                 N 
                 −10.5 
                 −6.599 
                 10.707 
               
               
                 2956 
                 LYS389 
                 CA 
                 −11.364 
                 −6.141 
                 11.792 
               
               
                 2957 
                 LYS389 
                 C 
                 −12.626 
                 −5.52 
                 11.203 
               
               
                 2958 
                 LYS389 
                 O 
                 −12.542 
                 −4.581 
                 10.4 
               
               
                 2959 
                 LYS389 
                 CB 
                 −10.611 
                 −5.115 
                 12.633 
               
               
                 2960 
                 LYS389 
                 CG 
                 −11.439 
                 −4.708 
                 13.847 
               
               
                 2961 
                 LYS389 
                 CD 
                 −10.677 
                 −3.763 
                 14.767 
               
               
                 2962 
                 LYS389 
                 CE 
                 −11.487 
                 −3.466 
                 16.023 
               
               
                 2963 
                 LYS389 
                 NZ 
                 −10.719 
                 −2.637 
                 16.96 
               
               
                 2964 
                 HIS390 
                 N 
                 −13.775 
                 −6.068 
                 11.571 
               
               
                 2965 
                 HIS390 
                 CA 
                 −15.055 
                 −5.523 
                 11.102 
               
               
                 2966 
                 HIS390 
                 C 
                 −15.385 
                 −4.226 
                 11.836 
               
               
                 2967 
                 HIS390 
                 O 
                 −15.845 
                 −4.213 
                 12.983 
               
               
                 2968 
                 HIS390 
                 CB 
                 −16.162 
                 −6.548 
                 11.316 
               
               
                 2969 
                 HIS390 
                 CG 
                 −17.525 
                 −6.094 
                 10.826 
               
               
                 2970 
                 HIS390 
                 ND1 
                 −17.895 
                 −5.893 
                 9.545 
               
               
                 2971 
                 HIS390 
                 CD2 
                 −18.62 
                 −5.81 
                 11.607 
               
               
                 2972 
                 HIS390 
                 CE1 
                 −19.181 
                 −5.487 
                 9.511 
               
               
                 2973 
                 HIS390 
                 NE2 
                 −19.629 
                 −5.437 
                 10.786 
               
               
                 2974 
                 ASP391 
                 N 
                 −15.053 
                 −3.138 
                 11.167 
               
               
                 2975 
                 ASP391 
                 CA 
                 −15.269 
                 −1.789 
                 11.683 
               
               
                 2976 
                 ASP391 
                 C 
                 −15.392 
                 −0.871 
                 10.48 
               
               
                 2977 
                 ASP391 
                 O 
                 −14.395 
                 −0.539 
                 9.835 
               
               
                 2978 
                 ASP391 
                 CB 
                 −14.068 
                 −1.414 
                 12.553 
               
               
                 2979 
                 ASP391 
                 CG 
                 −14.172 
                 −0.02 
                 13.18 
               
               
                 2980 
                 ASP391 
                 OD1 
                 −14.984 
                 0.771 
                 12.707 
               
               
                 2981 
                 ASP391 
                 OD2 
                 −13.241 
                 0.324 
                 13.884 
               
               
                 2982 
                 SER392 
                 N 
                 −16.582 
                 −0.335 
                 10.283 
               
               
                 2983 
                 SER392 
                 CA 
                 −16.835 
                 0.448 
                 9.075 
               
               
                 2984 
                 SER392 
                 C 
                 −16.261 
                 1.863 
                 9.129 
               
               
                 2985 
                 SER392 
                 O 
                 −15.99 
                 2.431 
                 8.07 
               
               
                 2986 
                 SER392 
                 CB 
                 −18.342 
                 0.537 
                 8.868 
               
               
                 2987 
                 SER392 
                 OG 
                 −18.876 
                 1.383 
                 9.878 
               
               
                 2988 
                 THR393 
                 N 
                 −15.944 
                 2.392 
                 10.297 
               
               
                 2989 
                 THR393 
                 CA 
                 −15.451 
                 3.768 
                 10.313 
               
               
                 2990 
                 THR393 
                 C 
                 −13.931 
                 3.822 
                 10.468 
               
               
                 2991 
                 THR393 
                 O 
                 −13.294 
                 4.722 
                 9.909 
               
               
                 2992 
                 THR393 
                 CB 
                 −16.183 
                 4.53 
                 11.411 
               
               
                 2993 
                 THR393 
                 OG1 
                 −17.557 
                 4.561 
                 11.04 
               
               
                 2994 
                 THR393 
                 CG2 
                 −15.703 
                 5.972 
                 11.528 
               
               
                 2995 
                 ILE394 
                 N 
                 −13.365 
                 2.816 
                 11.118 
               
               
                 2996 
                 ILE394 
                 CA 
                 −11.899 
                 2.665 
                 11.203 
               
               
                 2997 
                 ILE394 
                 C 
                 −11.525 
                 1.204 
                 10.92 
               
               
                 2998 
                 ILE394 
                 O 
                 −11.205 
                 0.419 
                 11.824 
               
               
                 2999 
                 ILE394 
                 CB 
                 −11.37 
                 3.095 
                 12.577 
               
               
                 3000 
                 ILE394 
                 CG1 
                 −11.744 
                 4.533 
                 12.921 
               
               
                 3001 
                 ILE394 
                 CG2 
                 −9.847 
                 2.978 
                 12.624 
               
               
                 3002 
                 ILE394 
                 CD1 
                 −10.977 
                 5.529 
                 12.055 
               
               
                 3003 
                 TYR395 
                 N 
                 −11.59 
                 0.854 
                 9.649 
               
               
                 3004 
                 TYR395 
                 CA 
                 −11.29 
                 −0.503 
                 9.179 
               
               
                 3005 
                 TYR395 
                 C 
                 −9.792 
                 −0.786 
                 9.302 
               
               
                 3006 
                 TYR395 
                 O 
                 −8.997 
                 0.149 
                 9.447 
               
               
                 3007 
                 TYR395 
                 CB 
                 −11.747 
                 −0.572 
                 7.721 
               
               
                 3008 
                 TYR395 
                 CG 
                 −11.784 
                 −1.967 
                 7.101 
               
               
                 3009 
                 TYR395 
                 CD1 
                 −10.958 
                 −2.272 
                 6.026 
               
               
                 3010 
                 TYR395 
                 CD2 
                 −12.648 
                 −2.927 
                 7.612 
               
               
                 3011 
                 TYR395 
                 CE1 
                 −10.991 
                 −3.543 
                 5.465 
               
               
                 3012 
                 TYR395 
                 CE2 
                 −12.682 
                 −4.199 
                 7.052 
               
               
                 3013 
                 TYR395 
                 CZ 
                 −11.852 
                 −4.502 
                 5.982 
               
               
                 3014 
                 TYR395 
                 OH 
                 −11.882 
                 −5.763 
                 5.427 
               
               
                 3015 
                 GLY396 
                 N 
                 −9.433 
                 −2.053 
                 9.421 
               
               
                 3016 
                 GLY396 
                 CA 
                 −8.007 
                 −2.401 
                 9.468 
               
               
                 3017 
                 GLY396 
                 C 
                 −7.732 
                 −3.871 
                 9.759 
               
               
                 3018 
                 GLY396 
                 O 
                 −8.601 
                 −4.74 
                 9.609 
               
               
                 3019 
                 LEU397 
                 N 
                 −6.493 
                 −4.132 
                 10.134 
               
               
                 3020 
                 LEU397 
                 CA 
                 −6.031 
                 −5.497 
                 10.406 
               
               
                 3021 
                 LEU397 
                 C 
                 −5.334 
                 −5.577 
                 11.751 
               
               
                 3022 
                 LEU397 
                 O 
                 −4.297 
                 −4.938 
                 11.961 
               
               
                 3023 
                 LEU397 
                 CB 
                 −5.051 
                 −5.894 
                 9.311 
               
               
                 3024 
                 LEU397 
                 CG 
                 −5.773 
                 −6.502 
                 8.12 
               
               
                 3025 
                 LEU397 
                 CD1 
                 −5.037 
                 −6.225 
                 6.822 
               
               
                 3026 
                 LEU397 
                 CD2 
                 −5.979 
                 −7.996 
                 8.325 
               
               
                 3027 
                 HIS398 
                 N 
                 −5.87 
                 −6.402 
                 12.634 
               
               
                 3028 
                 HIS398 
                 CA 
                 −5.274 
                 −6.514 
                 13.967 
               
               
                 3029 
                 HIS398 
                 C 
                 −4.348 
                 −7.718 
                 14.107 
               
               
                 3030 
                 HIS398 
                 O 
                 −3.651 
                 −7.848 
                 15.12 
               
               
                 3031 
                 HIS398 
                 CB 
                 −6.363 
                 −6.528 
                 15.033 
               
               
                 3032 
                 HIS398 
                 CG 
                 −6.737 
                 −5.14 
                 15.525 
               
               
                 3033 
                 HIS398 
                 ND1 
                 −7.052 
                 −4.804 
                 16.79 
               
               
                 3034 
                 HIS398 
                 CD2 
                 −6.795 
                 −3.984 
                 14.781 
               
               
                 3035 
                 HIS398 
                 CE1 
                 −7.311 
                 −3.482 
                 16.851 
               
               
                 3036 
                 HIS398 
                 NE2 
                 −7.152 
                 −2.975 
                 15.607 
               
               
                 3037 
                 ALA399 
                 N 
                 −4.306 
                 −8.567 
                 13.094 
               
               
                 3038 
                 ALA399 
                 CA 
                 −3.343 
                 −9.671 
                 13.12 
               
               
                 3039 
                 ALA399 
                 C 
                 −2.7 
                 −9.903 
                 11.756 
               
               
                 3040 
                 ALA399 
                 O 
                 −3.373 
                 −10.014 
                 10.724 
               
               
                 3041 
                 ALA399 
                 CB 
                 −4.014 
                 −10.936 
                 13.633 
               
               
                 3042 
                 LEU400 
                 N 
                 −1.383 
                 −10.004 
                 11.794 
               
               
                 3043 
                 LEU400 
                 CA 
                 −0.567 
                 −10.204 
                 10.589 
               
               
                 3044 
                 LEU400 
                 C 
                 0.772 
                 −10.856 
                 10.935 
               
               
                 3045 
                 LEU400 
                 O 
                 1.712 
                 −10.165 
                 11.35 
               
               
                 3046 
                 LEU400 
                 CB 
                 −0.307 
                 −8.845 
                 9.946 
               
               
                 3047 
                 LEU400 
                 CG 
                 0.615 
                 −8.952 
                 8.736 
               
               
                 3048 
                 LEU400 
                 CD1 
                 0.005 
                 −9.826 
                 7.644 
               
               
                 3049 
                 LEU400 
                 CD2 
                 0.973 
                 −7.572 
                 8.197 
               
               
                 3050 
                 PRO401 
                 N 
                 0.815 
                 −12.178 
                 10.881 
               
               
                 3051 
                 PRO401 
                 CA 
                 2.084 
                 −12.9 
                 10.974 
               
               
                 3052 
                 PRO401 
                 C 
                 2.88 
                 −12.822 
                 9.671 
               
               
                 3053 
                 PRO401 
                 O 
                 2.413 
                 −13.242 
                 8.602 
               
               
                 3054 
                 PRO401 
                 CB 
                 1.686 
                 −14.312 
                 11.269 
               
               
                 3055 
                 PRO401 
                 CG 
                 0.197 
                 −14.466 
                 10.993 
               
               
                 3056 
                 PRO401 
                 CD 
                 −0.308 
                 −13.08 
                 10.625 
               
               
                 3057 
                 VAL402 
                 N 
                 4.074 
                 −12.267 
                 9.78 
               
               
                 3058 
                 VAL402 
                 CA 
                 5.008 
                 −12.183 
                 8.653 
               
               
                 3059 
                 VAL402 
                 C 
                 6.358 
                 −12.814 
                 8.998 
               
               
                 3060 
                 VAL402 
                 O 
                 7.008 
                 −12.485 
                 9.998 
               
               
                 3061 
                 VAL402 
                 CB 
                 5.194 
                 −10.723 
                 8.25 
               
               
                 3062 
                 VAL402 
                 CG1 
                 3.968 
                 −10.185 
                 7.523 
               
               
                 3063 
                 VAL402 
                 CG2 
                 5.553 
                 −9.84 
                 9.44 
               
               
                 3064 
                 THR403 
                 N 
                 6.772 
                 −13.729 
                 8.146 
               
               
                 3065 
                 THR403 
                 CA 
                 8.039 
                 −14.428 
                 8.342 
               
               
                 3066 
                 THR403 
                 C 
                 9.135 
                 −13.709 
                 7.571 
               
               
                 3067 
                 THR403 
                 O 
                 9.102 
                 −13.66 
                 6.335 
               
               
                 3068 
                 THR403 
                 CB 
                 7.888 
                 −15.853 
                 7.827 
               
               
                 3069 
                 THR403 
                 OG1 
                 6.715 
                 −16.403 
                 8.406 
               
               
                 3070 
                 THR403 
                 CG2 
                 9.077 
                 −16.723 
                 8.22 
               
               
                 3071 
                 TRP404 
                 N 
                 10.089 
                 −13.156 
                 8.298 
               
               
                 3072 
                 TRP404 
                 CA 
                 11.177 
                 −12.406 
                 7.66 
               
               
                 3073 
                 TRP404 
                 C 
                 12.136 
                 −13.344 
                 6.931 
               
               
                 3074 
                 TRP404 
                 O 
                 12.984 
                 −12.835 
                 6.21 
               
               
                 3075 
                 TRP404 
                 CB 
                 11.969 
                 −11.654 
                 8.719 
               
               
                 3076 
                 TRP404 
                 CG 
                 11.163 
                 −10.949 
                 9.79 
               
               
                 3077 
                 TRP404 
                 CD1 
                 10.886 
                 −11.444 
                 11.043 
               
               
                 3078 
                 TRP404 
                 CD2 
                 10.559 
                 −9.637 
                 9.729 
               
               
                 3079 
                 TRP404 
                 NE1 
                 10.155 
                 −10.524 
                 11.721 
               
               
                 3080 
                 TRP404 
                 CE2 
                 9.943 
                 −9.428 
                 10.972 
               
               
                 3081 
                 TRP404 
                 CE3 
                 10.506 
                 −8.656 
                 8.749 
               
               
                 3082 
                 TRP404 
                 CZ2 
                 9.278 
                 −8.237 
                 11.225 
               
               
                 3083 
                 TRP404 
                 CZ3 
                 9.838 
                 −7.468 
                 9.009 
               
               
                 3084 
                 TRP404 
                 CH2 
                 9.226 
                 −7.257 
                 10.239 
               
               
                 3085 
                 TRP404 
                 OXT 
                 12.117 
                 −14.53 
                 7.239 
               
               
                 3086 
                 HEM1 
                 FE 
                 −8.08 
                 12.05 
                 10.226 
               
               
                 3087 
                 HEM1 
                 NA 
                 −9.653 
                 12.085 
                 9.078 
               
               
                 3088 
                 HEM1 
                 C1A 
                 −10.7 
                 13.004 
                 9.077 
               
               
                 3089 
                 HEM1 
                 C2A 
                 −11.687 
                 12.681 
                 8.118 
               
               
                 3090 
                 HEM1 
                 C3A 
                 −11.292 
                 11.525 
                 7.568 
               
               
                 3091 
                 HEM1 
                 C4A 
                 −10.019 
                 11.174 
                 8.129 
               
               
                 3092 
                 HEM1 
                 CHB 
                 −9.224 
                 10.115 
                 7.699 
               
               
                 3093 
                 HEM1 
                 C1B 
                 −7.931 
                 9.83 
                 8.181 
               
               
                 3094 
                 HEM1 
                 NB 
                 −7.308 
                 10.582 
                 9.182 
               
               
                 3095 
                 HEM1 
                 C4B 
                 −6.086 
                 9.964 
                 9.364 
               
               
                 3096 
                 HEM1 
                 C3B 
                 −5.946 
                 8.85 
                 8.506 
               
               
                 3097 
                 HEM1 
                 C2B 
                 −7.068 
                 8.771 
                 7.746 
               
               
                 3098 
                 HEM1 
                 CMB 
                 −7.416 
                 7.755 
                 6.682 
               
               
                 3099 
                 HEM1 
                 CAB 
                 −4.833 
                 8.031 
                 8.591 
               
               
                 3100 
                 HEM1 
                 CBB 
                 −4.44 
                 7.051 
                 7.74 
               
               
                 3101 
                 HEM1 
                 CHC 
                 −5.212 
                 10.298 
                 10.374 
               
               
                 3102 
                 HEM1 
                 C1C 
                 −5.439 
                 11.223 
                 11.336 
               
               
                 3103 
                 HEM1 
                 NC 
                 −6.519 
                 12.039 
                 11.384 
               
               
                 3104 
                 HEM1 
                 C4C 
                 −6.227 
                 12.887 
                 12.426 
               
               
                 3105 
                 HEM1 
                 C3C 
                 −4.926 
                 12.636 
                 13.002 
               
               
                 3106 
                 HEM1 
                 C2C 
                 −4.491 
                 11.556 
                 12.313 
               
               
                 3107 
                 HEM1 
                 CMC 
                 −3.265 
                 10.712 
                 12.532 
               
               
                 3108 
                 HEM1 
                 CAC 
                 −4.462 
                 13.435 
                 14.055 
               
               
                 3109 
                 HEM1 
                 CBC 
                 −3.452 
                 13.231 
                 14.936 
               
               
                 3110 
                 HEM1 
                 CHD 
                 −7.061 
                 13.855 
                 12.91 
               
               
                 3111 
                 HEM1 
                 C1D 
                 −8.237 
                 14.203 
                 12.292 
               
               
                 3112 
                 HEM1 
                 ND 
                 −8.777 
                 13.572 
                 11.18 
               
               
                 3113 
                 HEM1 
                 C4D 
                 −9.915 
                 14.313 
                 10.916 
               
               
                 3114 
                 HEM1 
                 C3D 
                 −10.045 
                 15.413 
                 11.808 
               
               
                 3115 
                 HEM1 
                 C2D 
                 −9.006 
                 15.334 
                 12.673 
               
               
                 3116 
                 HEM1 
                 CMD 
                 −8.71 
                 16.241 
                 13.844 
               
               
                 3117 
                 HEM1 
                 CAD 
                 −11.178 
                 16.421 
                 11.802 
               
               
                 3118 
                 HEM1 
                 CBD 
                 −10.91 
                 17.624 
                 10.918 
               
               
                 3119 
                 HEM1 
                 CGD 
                 −12.079 
                 18.574 
                 10.862 
               
               
                 3120 
                 HEM1 
                 O1D 
                 −13.198 
                 18.167 
                 11.204 
               
               
                 3121 
                 HEM1 
                 O2D 
                 −11.889 
                 19.736 
                 10.477 
               
               
                 3122 
                 HEM1 
                 CHA 
                 −10.849 
                 14.026 
                 9.961 
               
               
                 3123 
                 HEM1 
                 CMA 
                 −12.005 
                 10.703 
                 6.498 
               
               
                 3124 
                 HEM1 
                 CAA 
                 −12.907 
                 13.51 
                 7.748 
               
               
                 3125 
                 HEM1 
                 CBA 
                 −14.087 
                 13.112 
                 8.645 
               
               
                 3126 
                 HEM1 
                 CGA 
                 −15.442 
                 13.596 
                 8.14 
               
               
                 3127 
                 HEM1 
                 O1A 
                 −15.522 
                 14.131 
                 7.009 
               
               
                 3128 
                 HEM1 
                 O2A 
                 −16.439 
                 13.4 
                 8.866