PATENT ABSTRACT
The present invention discloses a modified tumor necrosis factor-alpha converting enzyme (TACE) catalytic domain, that unlike the native TACE catalytic domain, is stable at high protein concentrations. The present invention further discloses methods for generating crystals of the modified TACE protein in protein-ligand complexes with a number of inhibitors. In addition, the present invention discloses methods of using the proteins, crystals and/or three-dimensional structures obtained to identify compounds that can modulate the enzymatic activity of TACE.

PATENT DESCRIPTION
CROSS-REFERENCE TO RELATED APPLICATIONS 
     This application is a non-provisional application that claims priority under 35 U.S.C. § 119(e) of provisional application, U.S. Ser. No. 60/383,391 filed May 24, 2002, the contents of which are hereby incorporated by reference in their entireties. 
    
    
     BACKGROUND OF THE INVENTION 
     1. Field of Invention 
     The present invention pertains to a modified tumor necrosis factor-alpha converting enzyme (TACE). The present invention further pertains to generating a crystal of the modified TACE protein in protein-ligand complex with a selected inhibitor for use in structure based rational drug design. In addition, the present invention pertains to methods of using these proteins and crystals to identify compounds that can modulate the enzymatic activity of TACE. 
     2. Background 
     Tumor necrosis factor-alpha (TNF-alpha) plays a major role in the immune and inflammatory responses in mammals [Qi and Pekala,  Proc Soc Exp Biol Med.  223(2):128–135 (2000)]. First isolated from the serum of rabbits that had been treated with endotoxin, TNF-alpha was named for its ability to trigger the hemorrhagic necrosis of specific transplantable tumors [Old,  Science  230:630-633 (1985)]. Subsequently, TNF-alpha was found to be identical to cachetin, a protein that is intimately involved in cachexia, the wasting disease prevalent in AIDS and cancer [Beutler et al.,  J. Exp. Med.,  161:984-995 (1985)]. 
     TNF-alpha can bind to two distinct cell membrane receptors (TNFR1 and TNFR2) to transduce intercellular signals to a variety of different target cells in a number of different tissues [Qi and Pekala,  Proc Soc Exp Biol Med.  223(2):128-135 (2000)]. Though a central participant in several key cellular processes, TNF-alpha also functions deleteriously as a mediator of insulin resistance in diabetes mellitus [Hotamisligil and Spiegelman,  Diabetes  43:1271-1278 (1994)]. In addition, an over-abundance of the active form of TNF-alpha has been linked to adverse symptoms in a number of disease states, including in rheumatoid arthritis, Crohn&#39;s disease, sepsis, and cachexia. Since there are presently no effective treatments for these conditions, there remains a need to find new drugs that can be used to modulate the effective physiological concentration of the active form of TNF-alpha. 
     TNF-alpha is transcribed as a transmembrane protein having a monomeric molecular weight of 26 kilodaltons [Shirai et al.,  Nature  313:803-806 (1985)]. A metalloprotease, tumor necrosis factor-alpha converting enzyme (TACE) cleaves the membrane-associated form of TNF-alpha at a specific site of the protein, converting it to its corresponding soluble form [Black et al.,  Nature  385:729-733 (1997); Moss et al.,  Nature  385:733-736 (1997); U.S. Pat. No. 5,830,742, Issued Nov. 3, 1998; U.S. Pat. No. 6,013,466, Issued Jan. 11, 2000, the contents of which are hereby incorporated by reference in their entireties]. The soluble form of TNF-alpha then associates as a homotrimer of three 17 kilodalton monomers [Kriegler et al.,  Cell,  53:45-53 (1988)]. Although the membrane-associated form of TNF-alpha appears to be active, it is the proteolyzed soluble form that is responsible for the mortality associated with endotoxic shock [Gearing et al.,  Nature  370:555-558 (1994)]. Thus, reducing the circulating concentration of active TNF-alpha appears to be critical to alleviate the harmful side effects caused by this cytokine. One means for achieving this reduction in concentration of soluble TNF-alpha is to inhibit the TACE protease. 
     TACE, also referred to as ADAM 17 and CD156q, is a zinc endopeptidase that is a member of the “A Disintegrin And Metalloprotease” (ADAM) family of metalloproteases [Schlondorff and Blobel,  J. Cell Sci.,  112:3603-3617 (1999); Black,  Intern. J. Biochem. Cell Biol  34:1-5 (2002); U.S. Pat. No. 5,830,742, Issued Nov. 3, 1998, the contents of all of which are hereby incorporated by reference in their entireties]. A type I transmembrane protein, TACE comprises (i) an extracellular region having an N-terminal signal peptide, (ii) a pro domain, (iii) a zinc-dependent catalytic domain, (iv) a disintegrin domain, (v) an EGF-like domain, (vi) a crambin-like domain, (vii) a transmembrane helix and (viii) an intracellular C-terminal tail [see WO9940182, Published Aug. 12, 1999]. More recently, the EGF-like and the crambin-like domains have been grouped together and re-named as a cysteine-rich domain [Black,  Intern. J. Biochem. Cell Biol  34:1-5 (2002)]. 
     Since TACE is a protease, the portion of the enzyme that is critical for drug discovery is its catalytic domain. The catalytic domain (TCD) of TACE comprises 263 amino acid residues preceded by a furin cleavage site (residues 211-214). The pro domain comprises a cysteine that interacts with the zinc molecule at the active-site preventing proteolytic action. Therefore, this cysteine must be displaced in order to generate an active protease [Black,  Intern. J. Biochem. Cell Biol  34:1-5 (2002)]. 
     Zask et al. have prepared a compilation of inhibitors of metalloproteinases [ Curr. Pharm. Des.,  2:624-661 (1996), the contents of which are hereby incorporated by reference in their entireties], and more recently, Letavic et al. has disclosed several specific inhibitors of TACE [ Biorgan . &amp;  Medic. Chem Lett.  12:1387-1390 (2002), the contents of which are hereby incorporated by reference in their entireties]. To date, however, none of these has proven to be useful in the treatment of conditions related to an over-abundance of soluble TNF-alpha. 
     Three-dimensional structures of two different TACE-inhibitor complexes have been obtained via X-ray crystallographic analyses [Letavic et al.,  Biorgan . &amp;  Medic. Chem Lett.  12:1387-1390 (2002); WO9940182, Published Aug. 12, 1999, U.S. application Ser. No. 09/117,476, filed Jan. 27, 1999, the contents of which are all hereby incorporated by reference in their entireties]. Importantly, however, the conditions for preparing the two TACE-inhibitor complexes were significantly different. These results suggest that new crystallization conditions may be required for every different TACE-ligand complex. Determining crystallization conditions, de novo can be extremely time-consuming. Moreover, such a requirement severely hampers progress in identifying new and more potent inhibitors of TACE which are necessary for developing safe and effective drugs to ameliorate the deleterious effects due to an overabundance of the soluble form of TNF-alpha. 
     Therefore, there is need to provide methods for performing X-ray crystallographic structural determinations on multiple TACE protein-ligand complexes without having to determine crystallization conditions, de novo. In addition, there is a need to obtain X-ray diffractable crystals of the TACE catalytic domain that are stable. Furthermore, there is a need to obtain crystals of the TACE catalytic domain that are amenable to ligand exchange. 
     The citation of any reference herein should not be construed as an admission that such reference is available as “prior art” to the instant application. 
     SUMMARY OF THE INVENTION 
     The present invention discloses that the native TACE protein unexpectedly undergoes autoproteolysis at the high protein concentrations required for X-ray crystallography. The present invention further identifies the peptide bond between amino acid residues Tyr352 and Val353 (Y 352 –V 353 ) of SEQ ID NO: 2 as the specific cleavage site. 
     Therefore, the present invention provides a polypeptide comprising a modified TACE catalytic domain that is significantly less susceptible to autoproteolysis than the native TACE. The modified TACE of the present invention imparts improved stability to the protease under the conditions employed to generate TACE crystals. The present invention also uniquely enables X-ray crystallographic structural determinations to be performed on multiple TACE protein-ligand complexes in rapid succession. This ability to rapidly generate three-dimensional structures of TACE protein-ligand complexes is critical for a successful structure based rational drug design program. 
     Indeed, the structural information generated using the compositions and methods of the present invention greatly facilitates the identification of new and more potent inhibitors of the TACE protease. Selected inhibitors, in turn, become lead candidates in the development of drugs that will be useful for counteracting the harmful effects due to an overabundance of the soluble form of TNF-alpha, i.e., drugs that can be used in the treatment of rheumatoid arthritis, Crohn&#39;s disease, sepsis, and/or cachexia. 
     One aspect of the present invention provides a polypeptide comprising the amino acid sequence of SEQ ID NO: 8. In one such embodiment, the polypeptide consists essentially of the amino acid sequence of SEQ ID NO: 8. In a particular embodiment, the amino acid residue at position 139 of SEQ ID NO: 8 is serine. 1  In another embodiment of this type, the amino acid residue at position 139 of SEQ ID NO: 8 is alanine. In a preferred embodiment, the amino acid residue at position 139 of SEQ ID NO: 8 is glycine (denoted as “vgTACE” in the Example below, and has the amino acid sequence of SEQ ID NO: 20). 
       1 The amino acid sequences of the TACE catalytic domain and the modified TACE catalytic domain are SEQ ID NOs: 6 and 8, respectively. Position 139 of SEQ ID NOs: 6 and 8 is equivalent to position 353 of SEQ ID NO: 2, the amino acid sequence of the TACE polypeptide comprising the Pre, Pro and catalytic domains. 
     In a related embodiment, the present invention provides a polypeptide comprising a modified TACE catalytic domain comprising at least 95% identity with the amino acid sequence of SEQ ID NO: 8. Preferably, this polypeptide catalyzes the proteolytic cleavage of SEQ ID NO: 17 and/or binds to N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide and/or binds to N-{3-(hydroxyaminocarbonyl)-1-oxo-(2R)-benzylpropyl}-Ile-Leu-OH. In one such embodiment, the polypeptide consists essentially of a modified TACE catalytic domain having at least 95% identity with the amino acid sequence of SEQ ID NO: 8. In one specific embodiment of this type, the amino acid residue at position 139 of SEQ ID NO: 8 is alanine. In another embodiment, the amino acid residue at position 139 of SEQ ID NO: 8 is glycine. In yet another embodiment, the amino acid residue at position 139 of SEQ ID NO: 8 is serine. 
     The present invention also provides the full-length TACE polypeptide and fragments thereof that comprise the TACE modified catalytic domain. In one such embodiment the TACE protein comprises (i) the pre domain, (ii) the pro domain, and (iii) the modified catalytic domain. In another embodiment, the fragment of the TACE polypeptide comprises the pro domain, and the modified catalytic domain. 
     Chimeric proteins comprising the polypeptides of the present invention are also part of the present invention. In a particular embodiment, the chimeric TACE is a fusion protein comprising (i) the pre domain, (ii) the pro domain, (iii) the modified catalytic domain and (iv) a polyhistidine tag. In another embodiment, the chimeric protein comprises the modified catalytic domain and a polyhistidine tag. In a preferred embodiment, the polyhistidine tag further comprises a glycyl-seryl (i.e., Gly-Ser) linker. 
     The present invention further provides nucleic acids that encode the polypeptides and chimeric proteins of the present invention (see e.g., Table 1 below). In a particular embodiment, the nucleic acid encodes a polypeptide having the amino acid of SEQ ID NO: 8. The present invention further provides expression vectors that comprise the nucleic acids of the present invention and a transcriptional control sequence. Preferably the nucleic acids of the present invention are operatively linked to the transcriptional control sequences in the expression vectors. Host cells comprising the expression vectors are also part of the present invention. 
     In addition, the present invention provides methods for producing the above-mentioned polypeptides. One such embodiment comprises culturing a host cell of the present invention that produces the polypeptides. Methods for purifying the resulting recombinant polypeptides are also included in the present invention, as are the purified recombinant polypeptides. 
     Crystals, each comprising one of the protein-ligand complexes of the present invention, are also contemplated. Preferably, such crystals effectively diffract X-rays for the determination of the atomic coordinates of the protein-ligand complex to a resolution of greater than 5.0 Angstroms. More preferably, a crystal of the present invention effectively diffracts X-rays for the determination of the atomic coordinates to a resolution of greater than 3.5 Angstroms. Even more preferably, a crystal of the present invention effectively diffracts X-rays for the determination of the atomic coordinates equal to or greater than 3.0 Angstroms. Still more preferably, a crystal of the present invention effectively diffracts X-rays for the determination of the atomic coordinates equal to or greater than 2.5 Angstroms, and, yet even more preferably, equal to or greater than 2.0 Angstroms. Most preferably, a crystal of the present invention effectively diffracts X-rays for the determination of the atomic coordinates equal to or greater than 1.5-1.7 Angstroms. 
     In a particular embodiment, the crystal comprises a protein-ligand binding complex in which the polypeptide comprises the amino acid sequence of SEQ ID NO: 8. In another embodiment, the crystal comprises a polypeptide comprising a protein-ligand binding complex in which the polypeptide comprises a modified TACE catalytic domain having at least 95% identity with the amino acid sequence of SEQ ID NO: 8. Preferably this polypeptide catalyzes the proteolytic cleavage of SEQ ID NO: 17, and/or binds to the compound, N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide and/or binds to N-{3-(hydroxyaminocarbonyl)-1-oxo-(2R)-benzylpropyl}-Ile-Leu-OH. In one particular embodiment of this type, the crystal of the present invention has the space group P2 1 2 1 2 1 , with unit cell dimensions of: a=73, b=75, c=103 Angstroms. 
     Another aspect of the present invention provides methods for obtaining a crystal comprising a protein-ligand complex between a substitute ligand and a modified TACE catalytic domain. One such method comprises incubating (e.g., soaking) an excess of a substitute ligand with a crystal comprising a modified TACE catalytic domain and an initial ligand in a protein-ligand binding complex. The incubation is performed under the appropriate conditions and for a sufficient time period for the substitute ligand to replace the initial ligand in the protein-ligand complex. A crystal comprising the protein-ligand complex between the substitute ligand and the modified TACE catalytic domain is thus, obtained. The modified TACE catalytic domain can be part of a larger polypeptide (e.g., the full-length TACE or a chimeric protein). In a preferred embodiment, the modified TACE catalytic domain comprises the amino acid sequence of SEQ ID NO: 8. In a one such embodiment, the modified TACE catalytic domain comprises the amino acid sequence of SEQ ID NO: 20. In a preferred embodiment, the initial ligand is N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide. In a particular embodiment of this type, the substitute ligand is N-{3-(hydroxyaminocarbonyl)-1-oxo-(2R)-benzylpropyl}-Ile-Leu-OH. The present invention further provides the crystals that comprise protein-ligand binding complexes that have had their initial ligand replaced with a substitute ligand. 
     In an alternative embodiment, the present invention provides a method for identifying an agent for use as an inhibitor of TACE. One such embodiment comprises obtaining a set of atomic coordinates that define the three-dimensional structure of the protein-ligand binding complex from a crystal of the present invention. A potential agent is then selected by performing rational drug design with the atomic coordinates obtained. Preferably, the selection is performed in conjunction with computer modeling. The potential agent is contacted with a proteolytic polypeptide that comprises the catalytic domain of TACE, or alternatively, an active fragment thereof. The catalytic activity of the proteolytic polypeptide is then determined in a TACE activity assay. A potential agent is identified as an agent that inhibits TACE when there is a decrease in the activity of the proteolytic polypeptide in the presence of the agent relative to in its absence. 
     In a related embodiment, a method of identifying a compound that is predicted to inhibit TACE is provided. One such embodiment comprises using the atomic coordinates in Table 3 to define the structure of the complex between the modified catalytic domain of TACE and N-{3-(hydroxyaminocarbonyl)-1-oxo-(2R)-benzylpropyl}-Ile-Leu-OH and/or to define the structure of a portion of that complex. The portion of the complex defined is required to comprise sufficient structural information to enable the identification of a given compound as a potential inhibitor. A compound then is identified as one predicted to inhibit TACE through the use of the defined structure. A particular embodiment of this type further comprises contacting the compound with a proteolytic polypeptide comprising the catalytic domain of TACE or an active fragment thereof and determining the catalytic activity of the proteolytic polypeptide in a TACE activity assay. A potential agent is identified as an agent that inhibits TACE when there is a decrease in the activity of the proteolytic polypeptide in the presence of the agent relative to in its absence. 
     The present invention further provides a computer comprising a three-dimensional representation of a protein-ligand complex between a modified TACE catalytic domain and N-{3-(hydroxyaminocarbonyl)-1-oxo-(2R)-benzylpropyl}-Ile-Leu-OH in computer memory. One such embodiment comprises: (i) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data comprising the atomic coordinates of Table 3; (ii) a working memory for storing instructions for processing the machine-readable data; and (iii) a central-processing unit coupled to the working memory and to the machine-readable data storage medium for processing the machine readable data into a three-dimensional representation. Preferably a display is also provided that is coupled to the central-processing unit for visualizing the three-dimensional representation of the protein-ligand complex. 
     Accordingly, it is a principal object of the present invention to provide an active TACE catalytic domain that can form a stable X-ray diffractable crystal. 
     It is a further object of the present invention to provide a way for exchanging ligands of a TACE catalytic domain in a crystal. 
     It is a further object of the present invention to provide multiple crystals of the TACE catalytic domain each comprising a different protein-ligand complex. 
     It is a further object of the present invention to provide an effective way of performing structure based rational drug design with TACE. 
     It is a further object of the present invention to provide drugs to treat conditions due to an overabundance of the soluble form of TNF-alpha. 
     These and other aspects of the present invention will be better appreciated by reference to the following drawing and Detailed Description. 
    
    
     
       BRIEF DESCRIPTION OF THE DRAWING 
         FIG. 1  depicts a schematic of a computer comprising a central processing unit (CPU), a working memory, a mass storage memory, a display terminal, and a keyboard that are interconnected by a conventional bidirectional system bus. The computer can be used to display and manipulate the structural data of the present invention. 
     
    
    
     DETAILED DESCRIPTION OF THE INVENTION 
     Although entirely independent of any particular mechanism, the present invention was conceived following the unexpected discovery by the present inventors that the native TACE protein undergoes autoproteolysis at the high protein concentrations required for X-ray crystallographic analysis. The subsequent identification by the inventors of an autoproteolysis site between Y 352 –V 353  of SEQ ID NO: 2, raised the possibility that the replacement of either one or both of these amino acid residues might lead to a TACE protein that was resistant to autoproteolysis. Insertion(s) or deletion(s) of amino acid residues adjacent to the Y 352 –V 353  cleavage site might also lead to a TACE polypeptide that is resistant to autoproteolyisis. However, inserting or deleting amino acid residues adjacent to the Y 352 –V 353  cleavage site could create conformational changes in the protein that significantly reduce its enzyme activity and/or stability. Similarly, since Tyr352 of SEQ ID NO: 2 is located within a hydrophobic pocket that is close to the active site of the TACE protease, modification of this amino acid residue also might effect the enzymatic activity and/or protein stability. In direct contrast, Val353 of SEQ ID NO: 2 is located on the enzyme surface with its side chain exposed to the solvent, and so modification of the valine side chain might be less traumatic to the enzyme structure. Therefore, modification of Val353 is preferred over either modifying Tyr352, or inserting or deleting amino acid residues adjacent to the Y 352 –V 353  cleavage site. These latter two alternatives, however, remain part of the present invention. 
     Indeed, as disclosed herein, substitution of the hydrophobic valine side chain with either serine or glycine significantly reduces autoproteolysis, and dramatically improved the stability of the protein, without significantly altering the proteolytic activity of the TACE enzyme. In a preferred embodiment, the modified TACE catalytic domain contains an amino acid change at amino acid residue 353 of SEQ ID NO: 2. In one such embodiment, Val353 is replaced with a glycyl residue. In another embodiment, Val353 is replaced with a seryl residue. Substitutions of the nonpolar side chain of valine with alternative non-hydrophobic side chains can also prevent auto-proteolysis, and such substitutions are also part of the present invention. In addition, in order to remove N-glycosylation sites it is preferable as exemplified below, that Ser266 be replaced e.g., with an alanyl residue, and Asp452 be replaced e.g., with a glutaminyl residue. 
     The present invention further provides crystals comprising a protein-ligand complex of a polypeptide that comprises a modified TACE catalytic domain. The three-dimensional structure of a protein-ligand complex comprising a modified TACE catalytic domain bound to N-{3-(hydroxyaminocarbonyl)-1-oxo-(2R)-benzylpropyl}-Ile-Leu-OH is provided in the Example below (see Table 3 which lists the atomic coordinates). 
     N-{3-(hydroxyaminocarbonyl)-1-oxo-(2R)-benzylpropyl}-Ile-Leu-OH which is commercially available, e.g., from Chem-Impex International, Wood Dale Ill., (product code 09538), has the following chemical structure: 
     
       
                 
         
             
             
         
      
     
     Structure based rational drug design is the most efficient method of drug development. In one common paradigm, a three dimensional structure of a protein-ligand complex is determined, and potential antagonists (e.g., inhibitors) of the protein (e.g., potential drugs) are identified and/or designed with the aid of computer modeling [Bugg et al.,  Scientific American, Dec.:  92-98 (1993); West et al.,  TIPS,  16:67-74 (1995); Dunbrack et al.,  Folding  &amp;  Design,  2:27-42 (1997)]. The drug candidates are selected and assayed. The most promising drug candidates are identified, and then incubated in excess with crystals of a protein-ligand complex to replace the initial ligand. The three-dimensional structure of the new protein-ligand complex is then determined, and new potential antagonists of the protein are identified and/or designed with the aid of computer modeling. This process can then be continued in successive iterations until a lead drug candidate is identified. 
     Heretofore, the ability to perform structure based rational drug design with TACE was severely hampered because only two TACE protein-ligands complexes were known to form an X-ray quality crystal, [Maskos et. al.,  Proc. Natl. Acad. Sci. USA  95:3408-3412 (1998); Letavic et al.,  Biorgan . &amp;  Medic. Chem Lett.  12:1387-1390 (2002)], and these crystals were not reported to be capable of ligand exchange. As disclosed herein, the present invention overcomes this problem by providing crystals of the modified TACE catalytic domain that are conducive to ligand exchange. 
     As used herein the following terms shall have the definitions set out below: 
     As used herein the term “polypeptide” is used interchangeably with the term “protein” and is further meant to encompass peptides. Therefore, as used herein, a polypeptide is a polymer of two or more amino acids joined together by peptide linkages. Preferably, a polypeptide is a polymer comprising twenty or more amino acid residues joined together by peptide linkages. 
     As used herein a polypeptide “consisting essentially of” or that “consists essentially of” a specified amino acid sequence is a polypeptide that (i) retains the general characteristics of a polypeptide comprising that amino acid sequence, e.g., the activity of the polypeptide, and (ii) further comprises the identical amino acid sequence, except it consists of plus or minus 10% (or a lower percentage), preferably plus or minus 5% (or a lower percentage), and more preferably plus or minus 2.5% (or a lower percentage) of the amino acid residues. 
     As used herein a “modified TACE catalytic domain” is a TACE catalytic domain that has been modified to resist and/or prevent autocatalysis. Preferably, at least one of the two critical amino acid residues at the autoproteolytic site of TACE, i.e., Tyr352 and Val353 of SEQ ID NO: 2, has been replaced. More preferably, a modified TACE catalytic domain has the Val353 residue replaced with a non-hydrophobic amino acid residue. 
     As used herein a “non-hydrophobic amino acid” is an amino acid that is not hydrophobic. The genus of non-hydrophobic amino acids specifically does not include leucine, isoleucine, valine, methionine, tryptophan, and phenylalanine. 
     As used herein a “polypeptide comprising a modified TACE catalytic domain”, can be (i) the full length TACE protein, (ii) a fragment of the TACE protein that includes the modified TACE catalytic domain e.g., the pro and catalytic domain, (iii) the modified TACE catalytic domain alone, or (iv) a chimeric protein which comprises any of the above. 
     As used herein a “proteolytic polypeptide” of the present invention is a polypeptide that is capable of catalyzing the proteolytic cleavage of a substrate of the native TACE protease. A proteolytic polypeptide of the present invention minimally comprises an active fragment of the TACE catalytic domain that retains proteolytic activity. A proteolytic polypeptide of the present invention can be a chimeric protein. 
     As used herein an “active fragment” of the catalytic domain of TACE” is a fragment of the catalytic domain of TACE and/or modified TACE catalytic domain that retains at least about 10%, preferably at least about 20%, and more preferably at least about 25% of the proteolytic activity of the full-length TACE protease. Preferably, the active fragment retains at least about 25%, more preferably at least about 50%, and even more preferably at least about 75% of the amino acid residues of the catalytic domain of TACE having the amino acid sequence of SEQ ID NO: 6. More preferably, the amino acid sequence of the active fragment of the TACE catalytic domain has at least about 95% identity to the corresponding amino acid residues of SEQ ID NO: 6. 
     As used herein the term “chimeric” protein is meant to include “fusion proteins”. “Chimeric” proteins of the present invention comprise at least a portion of a non-TACE protein joined via a peptide bond to at least a portion of a TACE polypeptide. Chimeric proteins can have additional structural, regulatory, or catalytic properties. In a particular embodiment the chimeric protein functions as a means of detecting and/or isolating the TACE polypeptide or fragment thereof after the recombinant nucleic acid is expressed. Non-TACE amino acid sequences are preferably either amino- or carboxy-terminal to the TACE sequence. 
     As used herein one amino acid sequence is 100% “identical” to a second amino acid sequence when the amino acid residues of both sequences are identical. Accordingly, an amino acid sequence is 50% “identical” to a second amino acid sequence when 50% of the amino acid residues of the two amino acid sequences are identical. The sequence comparison is performed over a contiguous block of amino acid residues comprised by the TACE polypeptide or the portion of the TACE polypeptide being compared, e.g., the modified catalytic domain (SEQ ID NO: 8). In a preferred embodiment, selected deletions or insertions that could otherwise alter the correspondence between the two amino acid sequences are taken into account. 
     As used herein, DNA and protein sequence percent identity can be determined using C, MacVector 6.0.1, Oxford Molecular Group PLC (1996) and the Clustal W algorithm with the alignment default parameters, and default parameters for identity. These commercially available programs can also be used to determine sequence similarity using the same or analogous default parameters. Alternatively, an Advanced Blast search under the default filter conditions can be used, e.g., using the GCG (Genetics Computer Group, Program Manual for the GCG Package, Version 7, Madison, Wis.) pileup program using the default parameters. 
     As used herein a “nucleic acid” refers to the phosphate ester polymeric form of ribonucleosides (adenosine, guanosine, uridine or cytidine; “RNA molecules”) or deoxyribonucleosides (deoxyadenosine, deoxyguanosine, deoxythymidine, or deoxycytidine; “DNA molecules”), or any phosphoester analogs thereof, such as phosphorothioates and thioesters, in either single stranded form, or a double-stranded helix. Double stranded DNA-DNA, DNA-RNA and RNA-RNA helices are possible. When referring to a nucleic acid that is double stranded both the “sense” strand and the complementary “antisense” strand are intended to be included. Thus a nucleic acid that is hybridizable to SEQ ID NO: 1, for example, can be either hybridizable to the “sense” strand of SEQ ID NO: 1, which is particularly listed in the SEQUENCE LISTING, or to the “antisense” strand which can be readily determined from that SEQUENCE LISTING. 
     A DNA “coding sequence” is a double-stranded DNA sequence that is transcribed and translated into a polypeptide in a cell in vitro or in vivo when placed under the control of appropriate regulatory sequences. The boundaries of the coding sequence are determined by a start codon at the 5′ (amino) terminus and a translation stop codon at the 3′ (carboxyl) terminus. A coding sequence can include, but is not limited to, prokaryotic sequences, cDNA from eukaryotic mRNA, genomic DNA sequences from eukaryotic (e.g., mammalian) DNA, and even synthetic DNA sequences. If the coding sequence is intended for expression in a eukaryotic cell, a polyadenylation signal and transcription termination sequence will usually be located 3′ to the coding sequence. 
     Transcriptional and translational control sequences are DNA regulatory sequences, such as promoters, enhancers, terminators, and the like, that provide for the expression of a coding sequence in a host cell. In eukaryotic cells, polyadenylation signals are control sequences. 
     A “promoter sequence” is a DNA regulatory region capable of binding RNA polymerase in a cell and initiating transcription of a downstream (3′ direction) coding sequence. For purposes of defining the present invention, the promoter sequence is bounded at its 3′ terminus by the transcription initiation site and extends upstream (5′ direction) to include the minimum number of bases or elements necessary to initiate transcription at levels detectable above background. Within the promoter sequence will be found a transcription initiation site (conveniently defined for example, by mapping with nuclease SI), as well as protein binding domains (consensus sequences) responsible for the binding of RNA polymerase. 
     A coding sequence is “under the control” of transcriptional and translational control sequences in a cell when RNA polymerase transcribes the coding sequence into mRNA, which can then be trans-RNA spliced and translated into the protein encoded by the coding sequence. 
     A nucleic acid sequence is “operatively linked” to an expression control sequence when the expression control sequence controls or regulates the transcription and translation of that nucleic acid sequence. The term operatively linked includes having an appropriate start signal. 
     A “heterologous nucleotide sequence” as used herein is a nucleotide sequence that is added to a nucleotide sequence of the present invention by recombinant methods to form a nucleic acid that is not naturally formed in nature. Such nucleic acids can encode chimeric proteins. Alternatively, a heterologous nucleotide sequence can contain a nucleic acid regulatory sequence. Thus a heterologous nucleotide sequence can comprise non-coding sequences including restriction sites, regulatory sites, promoters and the like. In still another embodiment the heterologous nucleotide can function as a means of detecting a nucleotide sequence of the present invention. The present invention provides heterologous nucleotide sequences that when combined with nucleotide sequences encoding the TACE proteins, and fragments thereof, are necessary and sufficient to encode all of the chimeric proteins of the present invention. 
     As used herein the phrases “structure based rational drug design”, “structure based drug design”, “structure assisted drug design” and “rational drug design” are used interchangeably. These phrases are meant to convey a particular method of identifying and/or designing a ligand (preferably an inhibitor) for a specific target protein that includes the use of the three-dimensional structure of that protein and/or its corresponding protein-ligand complex. 
     The phrase “binding to” in regard to a ligand binding to a polypeptide is used herein to include any or all such specific interactions that lead to a protein-ligand binding complex. This can include processes such as covalent, ionic, hydrophobic and hydrogen bonding, but does not include non-specific associations such solvent preferences. 
     As used herein a “ligand” of a polypeptide is a compound that binds to the polypeptide in a protein-ligand binding complex. In a specific embodiment of the present invention the polypeptide has an enzymatic activity and the ligand inhibits that activity when bound to the polypeptide in a protein-ligand binding complex. Such a ligand is also termed an “inhibitor”. 
     As used herein the term “initial ligand” denotes a ligand in a protein-ligand complex that is, or can be displaced by a “substitute ligand”. 
     As used herein, a “protein-ligand binding complex” is a specific association between a polypeptide and the compound that binds to it. In a preferred embodiment of the present invention, the ligand is an inhibitor of the polypeptide. In a particular embodiment of this type, the binding of the inhibitor to the polypeptide occurs at the active site of the polypeptide. 
     As used herein “incubating a ligand with a crystal” is used interchangeably with “soaking a crystal with a ligand”. Incubating a ligand with a crystal is the contacting of a ligand with a crystal of a polypeptide under the appropriate conditions and for a sufficient time period (e.g., hours to several days) for the ligand to bind to the crystalline polypeptide and form a crystalline protein-ligand complex. Such incubating can further and/or alternatively, include contacting an excess of a substitute ligand with a crystal of a protein-ligand complex under the appropriate conditions and for a sufficient time period (e.g., hours to several days) for the substitute ligand to replace the initial ligand and form the new crystalline protein-ligand complex. 
     As used herein the terms “displacing”, “replacing”, and “exchanging” are used interchangeably in regard to the substitution of one ligand in a protein-ligand complex for another. 
     As used herein an “excess of a substitute ligand” is an amount of that ligand that is sufficient to replace 80% or more, and preferably 90% or more, of the initial ligand in a protein-ligand complex. In a particular embodiment of this type, the concentration of the substitute ligand is about ten-fold higher than the concentration of the protein-ligand complex. In a preferred embodiment, the concentration of the substitute ligand is about one hundred-fold higher than the concentration of the protein-ligand complex. 
     As used herein the term “X-ray diffractable crystal” is a crystal of a compound that yields a discernable diffraction pattern when subjected to 0.5 to 2.5 Å incident X-ray radiation. 
     As used herein an “X-ray quality crystal” is an X-ray diffractable crystal that can yield meaningful structural data of its crystalline composition when subjected to X-ray crystallographic analysis. 
     As used herein, and unless otherwise specified, the terms “agent”, “potential drug”, “compound”, or “test compound” are used interchangeably, and refer to chemicals that have or potentially have a use as an inhibitor of the proteolytic activity of TACE. Preferably such agents include drugs for the treatment or prevention of a disease and/or condition involving the proteolytic action of TACE. Therefore, such agents may be used, as described herein, in drug assays and drug screens and the like. 
     As used herein a “small organic molecule” is an organic compound [or organic compound complexed with an inorganic compound (e.g., metal)] that has a molecular weight of less than 3 Kd. 
     As used herein the terms “approximately” and “about” are used to signify that a value is within twenty percent of the indicated value i.e., an amino acid sequence containing “approximately” 260 amino acid residues can contain between 208 and 312 amino acid residues. 
     Nucleic Acids Encoding TACE 
     Obtaining and/or constructing a cDNA that encodes a polypeptide comprising a modified TACE facilitates the production of the large quantities of protein required to perform X-ray crystallographic analysis. Since the sequence of the native protein is known [see U.S. Pat. No. 6,013,466, Issued Jan. 11, 2000, the contents of which are hereby incorporated by reference in their entireties], a cDNA encoding the modified protease can be readily obtained. 
     To express a recombinant protein of the present invention in a host cell, an expression vector can be constructed comprising the corresponding cDNA. The present invention therefore, provides expression vectors containing nucleic acids encoding polypeptides comprising the modified TACE catalytic domains of the present invention. Due to the degeneracy of nucleotide coding sequences, other DNA sequences which encode substantially the same amino acid sequence as a nucleic acid encoding a polypeptide comprising the modified TACE catalytic domain of the present invention may be used in the practice of the present invention. These include, but are not limited to, allelic genes, homologous genes from other species, which are altered by the substitution of different codons that encode the same amino acid residue within the sequence, thus producing a silent change. Host cells comprising the expression vectors of the present invention are also provided. 
     Cloning of cDNAs and expression of their corresponding recombinant proteins have become a routine laboratory exercise [see Sambrook and Russell,  Molecular Cloning, A laboratory Manual,  3 rd    edition , Cold Spring Harbor Laboratory Press, Cold Spring Harbor L.I. (2000), the contents of which are hereby incorporated by reference in their entireties]. The use of a Baculovirus recombination system and Sf9 host cells is exemplified below. Purification of recombinant proteins has also become a routine laboratory exercise. In the present case, the modified TACE protein was cloned and expressed as the pro-protein. The pre and pro domains were cleaved during protein expression and secretion by the cells. The catalytic domain was then purified (see Example below). 
     The nucleotide sequence for open reading frame of TACE with a GS linker, a polyHis tag (H6), and stop codon is shown below. The nucleic acid sequence encoding: (i) the pre domain is underlined, (ii) the pro domain is under-dashed, (iii) the catalytic domain is unmarked and (iv) the GS linker and the polyHis tag (H6) are double underlined. The stop codon is underlined with a wavy line. 
     
       
                 
         
             
             
         
      
     
     Any technique for mutagenesis known in the art can be used to convert the native TACE catalytic domain to a modified domain, including but not limited to, ill vitro site-directed mutagenesis [Hutchinson et al.,  J. Biol. Chem.,  253:6551 (1978); Zoller and Smith,  DNA,  3:479-488 (1984); Oliphant et al.,  Gene,  44:177 (1986); Hutchinson et al.,  Proc. Natl. Acad. Sci. U.S.A.,  83:710 (1986)]. The use of TAB@ linkers (Pharmacia), etc. and PCR techniques also can be employed for site directed mutagenesis [see Higuchi, “Using PCR to Engineer DNA”, in PCR Technology: Principles and Applications for DNA Amplification, H. Erlich, ed., Stockton Press, Chapter 6, pp. 61-70 (1989)]. Preferably mutagenesis (i.e., modification) of the TACE catalytic domain is performed in a two step process [Wang, and Malcolm,  BioTechniques  26:680-682 (1999)]. In the Example below, two extension reactions were performed in separate tubes in the first stage: (i) one containing the forward primer, and (ii) the other containing the reverse primer. After two cycles, the two reactions are mixed and the standard QuickChange mutagenisis procedure is carried out for an additional 18 cycles. Following amplification, the parental strand is digested with 1Unit of Dpn1 for 1 hour and an aliquot is transformed into DH5-alpha cells [GeneWiz, New York, N.Y.] 
     The TACE Polypeptide 
     The amino acid sequence for the TACE polypeptide is shown below. (i) The pre domain is underlined, (ii) the pro domain is under-dashed, and (iii) the catalytic domain is unmarked. The GS-linker and polyhistidine tag (H6) are not included. The valine residue that is replaced with a non-hydrophobic amino acid residue in the modified TACE polypeptide is in bold. In addition, serine-266 has been replaced by an alanine, and asparagine-452 has been replaced by a glutamine in order to remove the N-linked glycosylation sites. 
     
       
                 
         
             
             
         
      
     
     The amino acid sequence for the catalytic domain of the modified TACE polypeptide is shown below. Whereas, the native protein comprises VAL 353  (VAL 139  of SEQ ID NO: 6), this amino acid residue is replaced by a non-hydrophobic amino acid residue in a modified TACE catalytic domain. This amino acid position is denoted with an “X” in bold below. Preferably the non-hydrophobic amino acid residue is a glycl, alanyl, or seryl amino acid residue. The GS-linker and Polyhistidine tag (H6) are not included. RADPDPMKNTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTAWDNAGFKG YGIQIEQIRILKSPQEVKPGEKHYNMAKSYPNEEKDAWDVKMLLEQFSFDIAEEASKVCL AHLFTYQDFDMGTLGLAYXGSPRANSHGGVCPKAYYSPVGKKNIYLNSGLTSTKNYGKTI LTKEADLVTTHELGHNFGAEHDPDGLAECAPNEDQGGKYVMYPIAVSGDHENNKMFSQCS KQSIYKTIESKAQECFQERSNKV (SEQ ID NO: 8), where X is a non-hydrophobic amino acid residue, and preferably either alanine, glycine or serine. 
     In a particular embodiment of the present invention, a modified TACE polypeptide or fragment thereof (e.g., the catalytic domain) is at least about 75% identical, more preferably at least about 90% identical, and most preferably at least about 95% identical to the TACE polypeptide or fragment thereof. As indicated above, a modified TACE or fragment thereof has a non-hydrophobic amino acid residue in place of the valine at position 353 (as defined in SEQ ID NO: 2). 
     Polypeptides comprising the modified TACE catalytic domains of the invention include those containing altered sequences in which functionally equivalent amino acid residues are substituted for residues within the sequence resulting in a conservative amino acid substitution. For example, one or more amino acid residues within the sequence can be substituted by another amino acid of a similar polarity, which acts as a functional equivalent, resulting in a silent alteration. Substitutes for an amino acid within the sequence may be selected from other members of the class to which the amino acid belongs. 
     For example, the nonpolar amino acids include alanine, leucine, isoleucine, valine, proline, phenylalanine, tryptophan, and methionine. Amino acids containing aromatic ring structures are phenylalanine, tryptophan, and tyrosine. The polar neutral amino acids include glycine, serine, threonine, cysteine, tyrosine, asparagine, and glutamine. The positively charged (basic) amino acids include arginine and lysine. The negatively charged (acidic) amino acids include aspartic acid and glutamic acid. 
     Particularly preferred conserved amino acid exchanges are: 
     (a) Lys for Arg or vice versa such that a positive charge may be maintained; 
     (b) Glu for Asp or vice versa such that a negative charge may be maintained; 
     (c) Ser for Thr or vice versa such that a free —OH can be maintained; 
     (d) Gln for Asn or vice versa such that a free NH 2  can be maintained; and 
     (e) Ile for Leu or for Val or vice versa as roughly equivalent hydrophobic amino acids. 
     All of the modified TACE catalytic domains of the present invention also can be part of a chimeric protein. In a specific embodiment, a chimeric TACE protein is expressed in a eukaryotic cell. Such a chimeric protein can be a fusion protein used to isolate a modified TACE of the present invention, through the use of an affinity column that is specific for the protein fused to the TACE protein. In one such embodiment, the chimeric TACE is expressed in a eukaryotic cell. Examples of such fusion proteins include: a glutathione-S-transferase (GST) fusion protein, a maltose-binding (MBP) protein fusion protein, a FLAG-tagged fusion protein, or as specifically exemplified below, a poly-histidine-tagged fusion protein. 
     Expression of a chimeric TACE protein, or fragment thereof, as a fusion protein can facilitate stable expression, and/or allow for purification based on the properties of the fusion partner. Thus the purification of the recombinant polypeptides of the present invention can be simplified through the use of fusion proteins having affinity tags. For example, GST binds glutathione conjugated to a solid support matrix, MBP binds to a maltose matrix, and poly-histidine chelates to a NI-chelation support matrix, as specifically exemplified below [see Hochuli et al.,  Biotechnolgy  6:1321-1325 (1998)]. The fusion protein can be eluted from the specific matrix with appropriate buffers, or by treating with a protease that is specific for a cleavage site that has been genetically engineered in between the TACE protein and its fusion partner. Alternatively, a modified TACE catalytic domain can be combined with a marker protein such as green fluorescent protein [Waldo et al.,  Nature Biotech.  17:691-695 (1999); U.S. Pat. No. 5,625,048 filed Apr. 29, 1997 and WO 97/26333, published Jul. 24, 1997, the contents of which are hereby incorporated by reference herein in their entireties]. 
     Alternatively or in addition, other column chromatography steps (e.g., gel filtration, ion exchange, affinity chromatography etc.) can be used to purify the recombinant proteins of the present invention. In many cases, such column chromatography steps employ high performance liquid chromatography or analogous methods in place of the more classical gravity-based procedures. 
     As exemplified below, a recombinant modified TACE catalytic domain was purified with a NiNTA column following routine centrifugation and diafiltration steps. After the purified protein was collected from the NiNTA column, it was placed on a gel filtration column. The resulting eluate was then concentrated and desalted prior to being combined with an inhibitor to form a protein-ligand complex. 
     Alternatively, polypeptides comprising the modified TACE catalytic domains of the present invention can be chemically synthesized [see e.g., Synthetic Peptides:  A User&#39;s Guide , W.H. Freeman &amp; Co., New York, N.Y., pp. 382, Grant, ed. (1992)]. 
     Enzyme Assays 
     The catalytic activity of the TACE protease can be determined in an assay using the synthetic peptide Ac-SPLAQA-VRSSSR-NH 2  (SEQ ID NO: 17) as the substrate. This amino acid sequence corresponds to the cleavage site of TACE on proTNF-alpha, with the sessile bond being between the alanine and the valine. The activity can be measured by incubating 100 nM TACE with 100 micromolar substrate in 25 mM HEPES pH 7.3, 5 mM CaCl 2 , for 1 hour at room temperature. Product formation can be quantified at 214 nm by HPLC using a reverse phase column to separate the substrate from the products. The ability of a given compound added to the reaction to act as an inhibitor of TACE can then be determined. 
     Alternatively, TACE activity can be determined in a fluorescence assay using the synthetic peptide substrate, K(Mca)-SPLAQA-VRSSSRK(Dpn)-NH 2  (SEQ ID NO: 18). K(Mca) is a lysyl residue modified by comprising an epsilonN-methoxycoumarin, whereas K(Dpn)-NH 2  is a lysyl residue modified to comprise an epsilonN 2,4, dinitrophenyl. 2-100 nanomolar TACE protease (or active fragment thereof) is incubated with 25 micromolar peptide substrate in 25 mM HEPES pH 7.3, 5 mM CaCl 2  for 1 hour at room temperature. Product formation is detected by exciting at 340 nm and measuring the fluorescence emission at 380 nm every 30 seconds for about an hour. The initial velocity can be obtained by linear regression. The increase in fluorescence emission can be correlated with the quantity of cleaved product. The ability of a given compound added to the reaction to act as an inhibitor of TACE can then be determined. 
     Crystallization 
     Crystals of the protein-ligand complex comprising a modified TACE catalytic domain of the present invention can be grown by a number of techniques including batch crystallization, vapor diffusion (e.g., by sitting drop or hanging drop) and by microdialysis. In the Example below, the modified TACE catalytic domain was complexed with N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide and crystallized by hanging drop vapor diffusion. Seeding of the crystals in some instances is required to obtain X-ray quality crystals. Standard micro and/or macro seeding of crystals may therefore be used. 
     As exemplified below, the protein-ligand complex comprising the modified TACE catalytic domain V353G (vgTACE) was crystallized under similar conditions to those previously employed for the non-modified TACE [WO9940182, Published Aug. 12, 1999, U.S. application Ser. No. 09/117,476, filed Jan. 27, 1999, the contents of which are both hereby incorporated by reference in its entireties]. 
     A substitute ligand can replace the co-crystallized initial ligand by soaking a crystal of protein-initial ligand complex with the substitute ligand. Thus, one or more crystals of protein-initial ligand complex can be placed in the reservoir solution containing about a 10-fold or greater excess of substitute ligand. The crystal is kept under the appropriate conditions and for a sufficient time period for the substitute ligand to replace the initial ligand and form the new crystalline protein-substitute ligand complex. In the example below, a crystal was kept in the solution containing the substitute ligand for about 72 hours. After the incubation, the crystal of the protein-substitute ligand complex can be frozen in liquid propane, for example and then used for X-ray diffraction. 
     Crystals can be characterized using X-rays produced in a conventional source (such as a sealed tube or a rotating anode) or using a synchrotron source. Methods of characterization include, but are not limited to, precision photography, oscillation photography and diffractometer data collection. As exemplified below, the crystals were flash frozen in liquid propane and X-ray diffraction was collected at 100 degrees Kelvin using conventional or synchrotron sources. 
     In the Example below, the crystal structure of the modified TACE catalytic domain V353G (vgTACE) was solved by molecular replacement and then refined using standard crystallographic programs. The published TACE structure was used as the starting model [PDB code:1BKC; Maskos et. al.,  Proc. Natl. Acad. Sci. USA  95:3408-3412 (1998); WO9940182, Published Aug. 12, 1999, U.S. application Ser. No. 09/117,476, filed Jan. 27, 1999, the contents of which are both hereby incorporated by reference in its entirety]. Replacement of the co-crystallized inhibitor was verified by difference electron density maps. The vgTACE:inhibitor structures were refined using X-PLOR [Brunger et al.,  Acta Crystallogr. A  46:585-593 (1990); Brunger et al.,  Acta Crystallogr. D Biol. Crystallogr.,  54:905-921 (1998)]. 
     Refinement calculations also can be performed using CNS [Adams et al.,  Proc. Natl. Acad. Sci. USA,  94:5018-5023 (1997)]. Map interpretation and model building also can be performed using O [Jones et al.,  Acta Cryst, A  47:110-119 (1991)]. Other computer programs that can be used to solve crystal structures include: QUANTA, CHARMM; INSIGHT; SYBYL; MACROMODE; and ICM. 
     Generally, structure based rational drug design is performed by analyzing the three-dimensional structures of successive protein-ligand complexes. This iterative process requires X-ray quality crystals of numerous protein-ligand complexes. These crystals can be obtained three ways. First, crystals of each protein-ligand complex can be grown de novo. This is the most time-consuming method, and in many instances requires determining a new set of crystallization conditions. The second method is to incubate (e.g., soak) individual crystals of the uncomplexed protein with each different ligand. This method is much faster than growing new crystals, but still requires a relatively large stock of protein to generate all of the new crystals. The third and most expedient method is to incubate a previously formed protein-ligand crystal with a large excess of a substitute ligand, thereby replacing the initial ligand with the substitute ligand in the protein-ligand complex. Heretofore, it was difficult to prepare alternative protein-ligand complexes of TACE since the two available X-ray quality crystals of TACE comprised the unstable, native TACE. The present invention overcomes this problem by providing a modified TACE catalytic domain that forms X-ray quality crystals that are amenable to ligand exchange. 
     Structure Based Rational Drug Design 
     Once three-dimensional structures of crystals comprising modified TACE catalytic domains are determined, a potential inhibitor of TACE can be examined through the use of computer modeling using a docking program such as GRAM, DOCK, or AUTODOCK [Dunbrack et al.,  Folding  &amp;  Design,  2:27-42 (1997)]. This procedure can include computer fitting of potential inhibitors to the modified TACE catalytic domain to ascertain how well the shape and the chemical structure of the potential modulator will interact with the TACE protein [Bugg et al.,  Scientific American, Dec.: 92-98 (1993); West et al.,  TIBS,  16:67-74 (1995)]. Computer programs can also be employed to estimate the attraction, repulsion, and steric hindrance of the modified TACE catalytic domain with an inhibitor. 
     Generally the tighter the fit, the lower the steric hindrances, and the greater the attractive forces, the more potent the inhibitor, since these properties are consistent with a tighter binding constant. Furthermore, the more specificity in the design of a potential drug the more likely that the drug will not interact as well with other proteins. This will minimize potential side-effects due to unwanted interactions with other proteins. 
     Initially compounds known to bind TACE, for example N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide, or a compound that inhibits TACE disclosed by Letavic et al., [ Biorgan . &amp;  Medic. Chem Lett.  12:1387-1390 (2002) the contents of which are hereby incorporated by reference in their entireties], or alternatively, a compound that binds metalloproteases as disclosed as by Zask et al. [ Curr. Pharm. Des.,  2:624-661 (1996), the contents of which are hereby incorporated by reference in their entireties], can be systematically modified by computer modeling programs until one or more promising potential analogs are identified. Such analysis has been shown to be effective in the development of HIV protease inhibitors [Lam et al.,  Science  263:380-384 (1994); Wlodawer et al.,  Ann. Rev. Biochem.  62:543-585 (1993); Appelt,  Perspectives in Drug Discovery and Design  1:23-48 (1993); Erickson,  Perspectives in Drug Discovery and Design  1:109-128 (1993)]. Alternatively, a potential inhibitor initially can be obtained by screening a random peptide library or a chemical library. In the former case, a random peptide library can be produced by recombinant bacteriophage, for example, [Scott and Smith,  Science,  249:386-390 (1990); Cwirla et al.,  Proc. Natl. Acad. Sci.,  87:6378-6382 (1990); Devlin et al.,  Science,  249:404-406 (1990)]. A peptide selected in this manner would then be systematically modified by computer modeling programs, as described above. 
     If a potential inhibitor is a small organic compound, it can be selected from a library of chemicals, including commercially available chemical libraries. Alternatively, the small organic compound may be synthesized de novo. The de novo synthesis of one or even a relatively small group of specific compounds is reasonable in the art of drug design. Once obtained, the potential inhibitor can be further tested in a standard binding and/or catalytic assay with TACE, the TACE catalytic domain, or an active fragment thereof. 
     For example, a binding assay can be performed following the attachment of the TACE catalytic domain to a solid support. Methods for placing the TACE catalytic domain on the solid support are well known in the art and include such things as linking biotin to the TACE catalytic domain and linking avidin to the solid support. The solid support can be washed to remove unbound protein. A solution of a labeled potential inhibitor can be contacted with the solid support. The solid support is washed again to remove the potential inhibitor not bound to the support. The amount of labeled potential inhibitor remaining with the solid support, and thereby bound to the TACE catalytic domain can be determined. Alternatively, or in addition, the dissociation constant between the labeled potential inhibitor and the TACE catalytic domain, for example, can be determined. Suitable labels for either the TACE catalytic domain or the potential inhibitor include, radioactive labels (e.g.,  14 C,  1 H,) and fluorescent labels such as fluorescein isothiocyanate (FITC). 
     In another embodiment, a Biacore machine can be used to determine the binding constant of the TACE catalytic domain with a potential inhibitor [O&#39;Shannessy et al.  Anal. Biochem.  212:457-468 (1993); Schuster et al.,  Nature  365:343-347 (1993)]. In another aspect of the present invention a potential inhibitor is tested for its ability to inhibit the proteolytic activity of TACE or an active fragment thereof. An inhibitor is then selected on the basis of its ability to inhibit the catalytic reaction of the TACE protease. 
     When a promising inhibitor is identified, a crystal comprising a protein-ligand complex of the inhibitor and the modified TACE catalytic domain can be prepared by incubating an excess of the inhibitor (substitute ligand) with a crystal of a modified TACE catalytic domain-ligand complex. The three-dimensional structure of the resulting crystalline protein-substitute ligand complex can then be determined by molecular replacement analysis, for example. 
     Molecular replacement involves using a known three-dimensional structure as a search model to determine the structure of a closely related molecule or protein-ligand complex in a different crystalline form. The measured X-ray diffraction properties of the new crystal are compared with the search model structure to compute the position and orientation of the protein in the new crystal. Computer programs that can be used include: X-PLOR (see above), CNS, (Crystallography and NMR System, a next level of XPLOR), and AMORE [Navaza,  Acta Crystallographics  ASO, 157-163 (1994)]. Once the position and orientation are known, an electron density map can be calculated using the search model to provide X-ray phases. Thereafter, the electron density is inspected for structural differences and the search model is modified to conform to the new structure. Using this approach, it is possible to solve the three-dimensional structures of crystals of any protein-ligand complex of the modified TACE catalytic domain. 
     For all of the drug screening assays described herein, further refinements to the structure of the drug will generally be necessary and can be made by the successive iterations of any and/or all of the steps provided by the particular drug screening assay and/or in combination with other such drug screening assays. 
     A candidate drug selected by performing structure based rational drug design can then be assayed in situ and/or in vivo. A candidate drug can be identified as a drug, for example, if it ameliorates a symptom caused by an overabundance of the soluble form of TNF-alpha in an animal model. Indeed, methods of testing such potential candidate drugs in animal models are well known in the art. The potential drugs can be administered by a variety of ways including topically, orally, subcutaneously, or intraperitoneally depending on the proposed use. Generally, at least two groups of animals are used in the assay, with at least one group being a control group that is administered the administration vehicle without the potential drug. 
     Electronic Representation of the Three Dimensional Structure of TACE 
     The present invention provides the three-dimensional depiction of the TACE catalytic domain in a complex with an inhibitor on an electronic and/or magnetic medium. More specifically, the present invention provides the data comprised in Table 3 on an electronic and/or magnetic medium. In addition, the present invention provides a computer that comprises a representation of the TACE catalytic domain-inhibitor complex in computer memory that can be used to screen for compounds that will inhibit the proteolytic activity of TACE. The computer may comprise portions of, or all of the information contained in Table 3. In a particular embodiment, the computer comprises: (i) a machine-readable data storage material encoded with machine-readable data, (ii) a working memory for storing instructions for processing the machine readable data, (iii) a central processing unit coupled to the working memory and the machine-readable data storage material for processing the machine readable data into a three-dimensional representation, and (iv) a display coupled to the central processing unit for displaying the three-dimensional representation. Thus the machine-readable data storage medium comprises a data storage material encoded with machine readable data which can comprise portions of, or all of the structural information contained in Table 3. 
     One embodiment for manipulating and displaying the structural data provided by the present invention is schematically depicted in  FIG. 1 . As depicted the System  1 , includes a computer  2  comprising a central processing unit (“CPU”)  3 , a working memory  4  which may be random-access memory or “core” memory, mass storage memory  5  (e.g., one or more disk or CD-ROM drives), a display terminal  6  (e.g., a cathoderay tube), one or more keyboards  7 , one or more input lines  10 , and one or more output lines  20 , all of which are interconnected by a conventional bidirectional system bus  30 . 
     Input hardware  12 , coupled to the computer  2  by input lines  10 , may be implemented in a variety of ways. Machine-readable data may be inputted via the use of one or more modems  14  connected by a telephone line or dedicated data line  16 . Alternatively or additionally, the input hardware may comprise CD-ROM or disk drives  5 . In conjunction with the display terminal  6 , the keyboard  7  may also be used as an input device. Output hardware  22 , coupled to computer  2  by output lines  20 , may similarly be implemented by conventional devices. Output hardware  22  may include a display terminal  6  for displaying the three dimensional data. Output hardware might also include a printer  24 , so that a hard copy output may be produced, or a disk drive or CDROM  5 , to store system output for later use, [see also U.S. Pat. No. 5,978,740, Issued Nov. 2, 1999, the contents of which are hereby incorporated by reference in their entireties]. 
     In operation, the CPU  3  (i) coordinates the use of the various input and output devices  12  and  22 ; (ii) coordinates data accesses from mass storage  5  and accesses to and from working memory  4 ; and (iii) determines the sequence of data processing steps. Any of a number of programs may be used to process the machine-readable data of this invention. 
     
       
         
               
             
               
               
               
               
             
           
               
                 TABLE 1 
               
             
             
               
                   
               
               
                 TABLE OF SEQUENCES 
               
             
          
           
               
                   
                 SEQ ID NO: 
                 Type 
                 Description 
               
               
                   
                   
               
               
                   
                  1 
                 N.A. 
                 Pre, Pro, and Catalytic domain 
               
               
                   
                  2 
                 A.A. 
                 Pre, Pro, and Catalytic domain 
               
               
                   
                  3 
                 N.A. 
                 Pro and Catalytic domain 
               
               
                   
                  4 
                 A.A. 
                 Pro, and Catalytic domain 
               
               
                   
                  5 
                 N.A. 
                 Catalytic domain 
               
               
                   
                  6 
                 A.A. 
                 Catalytic domain 
               
               
                   
                  7 
                 N.A. 
                 Catalytic domain (modified) 
               
               
                   
                  8 
                 A.A. 
                 Catalytic domain (modified) 
               
               
                   
                  9 
                 N.A. 
                 open reading frame 
               
               
                   
                 10 
                 N.A. 
                 BamH1f primer 
               
               
                   
                 11 
                 N.A. 
                 Kpn1r primer 
               
               
                   
                 12 
                 N.A. 
                 V353Gf primer 
               
               
                   
                 13 
                 N.A. 
                 V353Gr primer 
               
               
                   
                 14 
                 N.A. 
                 V353Sf primer 
               
               
                   
                 15 
                 N.A. 
                 V353Sr primer 
               
               
                   
                 16 
                 A.A  
                 internal cleave site 
               
               
                   
                 17 
                 A.A  
                 synthetic TACE substrate 
               
               
                   
                 18 
                 A.A  
                 synthetic TACE substrate 
               
               
                   
                 19 
                 N.A. 
                 vgTACE 
               
               
                   
                 20 
                 A.A  
                 vgTACE 
               
               
                   
                   
               
             
          
         
       
     
     The present invention may be better understood by reference to the following non-limiting Example, which is provided as exemplary of the invention. The following example is presented in order to more fully illustrate the preferred embodiments of the invention. It should in no way be construed, however, as limiting the broad scope of the invention. 
     EXAMPLE 
     Material and Methods 
     Cloning of TACE and TACE Mutants: 
     The TACE protein was cloned and expressed as the pro-protein. The pre and pro domains are cleaved during protein expression and secretion by the cells. Only the catalytic domain was purified. 
     Two PCR primers were used to amplify the pre-pro-cat domains of TACE having BamH1 and GS-(His)6-Kpn1 sites at the 5′ and 3′ ends respectively: 
     BamH1f: 5′ cgcggatccatgaggcagtctctcctattcctg 3′ SEQ ID NO: 10 
     Kpn1r: 5′ ccggcctaccttagtgatgqtgatgatggtgggatc 3′ SEQ ID NO: 11 
     The purified PCR fragment was digested with BamH1 and Kpn1 and subcoloned into the pFastBac1 vector provided in the Bac-to-Bac Baculovirus expression system (Invitrogen, Carlsbad, Calif.). The TACE mutants (V353G, V353S) were generated using the QUICKCHANGE kit (Stratagene, La Jolla, Calif., USA) using the native TACE pFastBac1 vector as a template and the following complementary mutagenic primers: 
     V353Gf: SEQ ID NO: 12 
     5′ GGA ACT CTT GGA TTA GCT TAT GGA GGC TCT CCC AGA GCA AAC 3′ 
     V353Gr: SEQ ID NO: 13 
     5′ GTT TGC TCT GGG AGA GCC TCC ATA AGC TAA TCC AAG AGT TCC 3′ 
     V353Sf: SEQ ID NO: 14 
     5′GGA ACT CTT GGA TTA GCT TAT AGC GGC TCT CCC AGA GCA AAC3′ 
     V353Sr: SEQ ID NO: 15 
     5′ GTT TGC TCT GGG AGA GCC GCT ATA AGC TAA TCC AAG AGT TCC3′ 
     The mutagenesis was performed in two steps as previously described [Wang, and Malcolm,  BioTechniques  26:680-682 (1999) the contents of which are hereby incorporated by reference in their entireties]. In the first stage, two extension reactions were performed in separate tubes; one containing the forward primer and the other containing the reverse primer. After two cycles, the two reactions were mixed and the standard QUICKCHANGE mutagenisis procedure was carried out for an additional 18 cycles. Following amplification, the parental strand was digested with 1Unit of Dpn1 for 1 hour and an aliquot was transformed into DH5-alpha cells. The sequences of all of the vectors were confirmed. (GeneWiz, New York, N.Y.) 
     Production of Recombinant Baculovirus. Recombinant baculovirus was produced using the BAC-TO-BAC expression system (Invitrogen, Carlsbad, Calif.) following known protocols for the transposition, isolation and transfection of recombinant bacmid DNA into Sf9 cells for production of viral particles. The virus was amplified to the P2 generation and was titered using the BacPAC Baculovirus Rapid Titer Kit (Clonetech, Palo Alto, Calif.). 
     Expression and Purification of TACE and TACE mutants: Logarithmically growing  Trichoplusia Ni  cells (High-5™ cells, 2×10 6  cells/ml) were infected with amplified baculovirus at a MOI=1.0 (2.5×10 8  pfu/ml) and grown at 27 degrees Celsius for 48-60 hours. Secreted TACE was isolated from the cell culture media after clarification by centrifugation. The pooled supernatants were concentrated 10 fold and the buffer exchanged into 25 mM HEPES, 0.15M NaCl, pH 7.5 by diafiltration. To the desalted supernatant, 4-aminophenyl-mercuric acetate (APMA) was added to 20 μM, lauryl maltoside to 0.05%, and imidazole to 25 mM. The supernatant was then applied to a NiNTA column (Qiagen Hilden, Germany). The NiNTA column was washed with 25 mM imidazole in buffer A (50 mM HEPES, 10% glycerol, 0.3M NaCl, 0.1% m-octyl-Beta-D-glucopyranoside, pH 7.5) until a stable baseline was achieved. The protein was then eluted with 250 mM imidazole in buffer A. The eluted protein was diluted to 0.1 mg/ml and dialyzed overnight against 25 mM Tris pH 7.5, with 20 μM APMA to digest excess pro-domain. The protein was collected and adjusted to 0.15M NaCl, concentrated, and applied to a SUPERDEX-75 gel filtration column (Pharmacia) equilibrated with 25 mM Tris-HCl, 0.2M NaCl pH 7.5 at 4 degrees Celsius. Fractions corresponding to the monomer of TACE were pooled, and stored at 4 degrees Celsius. The pooled TACE enzyme was concentrated to 15 mg/ml, desalted into 25 mM Tris-HCl pH 7.5 using BIO-SPIN 6 columns (Bio-Rad, Hercules, Calif.) and immediately complexed with N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide at a 1:1.5 molar ratio. Using this protocol, total expression levels of 5-10 mg/L were obtained with a final recovery of 0.5–5 mg/L. 
     Crystallization: Crystals were obtained by the hanging drop vapor diffusion method [Ducruix and Giege.  Crystallization of Nucleic Acids and Proteins. A practical approach . Oxford University Press, (1992)]. A small volume (1 to 15 microliters) containing the N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide [commercially available from e.g., CALBIOCHEM, San Diego Calif., Catalogue No. 579052, (TAPI-2)] solution was equilibrated with a larger volume (1 ml) of a reservoir solution. The reservoir solution contains the precipitant that facilitates the crystallization. 
     During equilibration the water content in the hanging drop is reduced and the protein-ligand complex, [i.e., the complex between vgTACE and N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide] forms crystals. To crystallize the protein-ligand complex, one microliter of the protein-ligand complex solution was mixed with one microliter of the reservoir solution, which contains 15% polyethylenglycol 4000, 10% 2-Propanol, and 100 mM Citrate-Buffer pH 5.6. Crystals were observed after one week. 
     The crystals obtained were washed with the reservoir solution. In the next step, a single protein-ligand complex crystal was put into the reservoir solution, which contained in addition, a 10 mM TACE inhibitor to replace the co-crystallized N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide. The crystal is usually kept for 72 hours in the solution containing the inhibitor to allow the ligand replacement. After incubation, the crystal was frozen in liquid propane and used for X-ray diffraction. 
     Results 
     Two distinct structures of TACE:inhibitor complexes have been previously disclosed [Maskos et. al.,  Proc. Natl. Acad. Sci. USA  95:3408–3412 (1998); Letavic et al.  Biorgan . &amp;  Medic. Chem Lett.  12:1387–1390 (2002)]. However, neither crystal appears to be amenable to crystal soaking. As disclosed herein, it has been unexpectedly discovered that the uncomplexed TACE protein (apo-protein) is unstable at the high concentrations required to grow and use crystals for X-ray crystallographic studies. Consistently, the crystal of Maskos et. al. has been found to be resistant to standard inhibitor soaking experiments, severely limiting its value in structure based rational drug design. 
     Stability of TACE: The stability of TACE was examined under several buffer conditions at pH 7.5. Twenty microliter aliquots of TACE at 15 mg/ml were desalted over P-6 spin columns (BioRAD, Hercules, Calif.) that had been equilibrated in: 
     (a) 25 mM Tris, 0.15M NaCl; 
     (b) 25 mM Tris; or 
     (c) 25 mM Tris plus N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide. 
     The stability of the TACE protein was evaluated after storage at 4 degrees Celsius for seven days. After incubating the TACE polypeptide under the three conditions listed above, Sodium Dodecyl Sulfate PolyAcrylamide Gel Electrophoresis (SDS-PAGE) was performed. The results show that only a single band having a molecular weight of 30 Kd was observed when either high salt (0.15 sodium chloride) or an inhibitor [N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide, at a 1:1.5 molar ratio enzyme:inhibitor] was included in the incubation. In direct contrast, two additional fainter bands that ran well ahead of the more significant TACE band were observed in the sample lacking either high salt or the inhibitor. The molecular weights of these two additional fainter bands were 14 Kd and 16 Kd, respectively, which add up to the 30 Kd molecular weight of the TACE polypeptide. N-terminal sequencing of the peptides corresponding to the two additional bands indicated that they were indeed, proteolytic products of the TACE protein. Moreover, the sequencing data indicated the presence of a single cleavage site at 352Y–V353 of SEQ ID NO: 2. 
     Substrate Specificity of TACE: In an effort to understand the role of the different amino-acid residues of TACE regarding substrate specificity, a substitution study was performed at the P′1 position. The catalytic activity of TACE was determined in an assay using the synthetic peptide Ac-SPLAQA-VRSSSR-NH2 (SEQ ID NO: 17) as the substrate. The sequence corresponds to the cleavage site of TACE on proTNF-alpha, with the sessile bond being between the alanine and the valine. Activity was measured by incubating 100 nM TACE with 100 micromolar substrate in 25 mM HEPES pH 7.3, 5 mM CaCl 2 , for 1 hour at room temperature. Product formation was quantified at 214 mm after HPLC separation using a POROS-R1 reverse phase column. Substitution of the P′1 valine (in bold above) with either alanine, glycine or serine decreased activity of TACE to non-detectable levels. Based on this data it was decided to substitute the P′1 position of the internal cleave site [ . . . LGLAY-VGSPR . . . (SEQ ID NO: 16)] with one of these amino acids e.g., either glycine or serine, in an attempt to eliminate the auto-proteolysis of TACE seen in the absence of NaCl. 
     Stability of TACE and TACE mutants: To test for stability under different storage conditions, 20 ul of TACE protein, at 15 mg/ml, was desalted over BIO-RAD P-6 columns equilibrated at pH 7.5 in: 
     (a) 25 mM Tris, 0.15M NaCl; 
     (b) 25 mM Tris+1 mM N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide; or 
     (c) 25 mM Tris. 
     One microliter aliquots were analyzed by SDS-PAGE after storing them for 3 hours, or 17 days at 4 degrees Celsius. In the absence of salt, the native protein exhibits a pattern consistent with substantial proteolysis occurring after only 3 hours, with the protein being completely proteolyzed after 17 days. In direct contrast, all constructs were stable in either 0.15M NaCl, or 1 mM N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide. The 2 loop mutants V353G and V353S showed improved stability, with the V353G (vgTACE) mutant being highly resistant to auto-proteolysis, even after 17 days. 
     Crystallization. The TACE mutant V353G (vgTACE) could be crystallized under similar conditions as the native TACE [WO9940182, Published Aug. 12, 1999, U.S. application Ser. No. 09/117,476, filed Jan. 27, 1999, the contents of which are both hereby incorporated by reference in its entirety]. vgTACE was concentrated to 15 mg/ml in 150 mM NaCl, 25 mM Tris-HCl pH 8. After desalting the vgTACE with Bio-Rad P-6 columns, N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide was added to a molecular ratio of 1:2 (enzyme:inhibitor). The complex was crystallized using the hanging drop vapor diffusion technique. Equal amounts of vgTACE-inhibitor solution were mixed with the reservoir solution, containing 15% Polyethylenglycol 4000, 10% 2-propanol, 100 mM sodium citrate pH 4.6, and equilibrated at 295 degrees Kelvin. Crystals were observed after 7 days. 
     Crystallographic analysis: vgTACE crystals were washed using the reservoir solution. Glycerol was then added to the reservoir solution to a final concentration of 15%, and the crystals were flash frozen in liquid propane. X-ray diffraction data were collected at 100 degrees Kelvin, using a rotating anode generator (Rigaku/MSC) or synchrotron sources. Diffraction was observed up to 1.7 Å. The vgTACE crystals belong to space group P2 1 2 1 2 1  (a=73, b=75, c=103 Å). There are two molecules located within the asymmetric unit. Soaking with the compounds of Table 2 was performed by incubation of the crystals in the reservoir solution in the presence of up to 70 mM of the respective inhibitor. In the V353G mutant crystals, the co-crystallized inhibitor N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide could be replaced during soaking. 
     Model building and refinement: The crystal structure of V353G mutant was solved by molecular replacement and refined using standard crystallographic programs. The published TACE structure was used as the starting model [PDB code:1BKC; Maskos et. al.,  Proc. Natl. Acad. Sci. USA  95:3408–3412 (1998)]. Replacement of the co-crystallized inhibitor was verified by difference electron density maps. The vgTACE:inhibitor structures were refined using X-PLOR(CNS). A list of vgTACE:inhibitor structures that have been solved is shown in Table 2 below. 
     
       
         
               
             
               
               
             
               
               
             
           
               
                 TABLE 2 
               
             
             
               
                   
               
               
                 RESOLUTION OF TACE-INHIBITOR COMPLEXES 
               
             
          
           
               
                   
                 Resolution 
               
               
                 INHIBITOR 
                 (Angstroms) 
               
               
                   
               
             
          
           
               
                 (4-biphenylsulfonyl)amino-propionic acid 
                 1.7 
               
               
                 3,4-dimethyl-2-(N-3&#39;-pyridylmethyl-p- 
                 1.9 
               
               
                 methoxysulfonamido)-benzenehydroxyamic acid 
               
               
                 alpha(R)-[[[4-2-butynyloxy) phenyl]sulfonyl]amino] 
                 1.7 
               
               
                 benzenepropanoic acid 
               
               
                 N-hydroxy-alpha(R),3(S)-dimethyl-3-[4-[(2-methyl-4- 
                 2.1 
               
               
                 quinolinyl)methoxy]phenyl]-2-oxo-1-pyrrolidineacetamide 
               
               
                 N-{3-(hydroxyaminocarbonyl)-1-oxo-(2R)-benzylpropyl}- 
                 2.0 
               
               
                 Ile-Leu-OH 
               
               
                   
               
             
          
         
       
     
     Table 3 below, comprises the coordinate set from the crystal structure of TACE complexed with N-{3-(hydroxyaminocarbonyl)-1-oxo-(2R)-benzylpropyl}-Ile-Leu-OH. To obtain these coordinates a single co-crystal of TACE in complex with N-{D,L-2-(hydroxyaminocarbonyl)methyl-4-methylpentanoyl}-L-3-amino-2-dimethylbutanoyl-L-alanine, 2-(amino)ethyl amide was soaked in 10% polyethylenglycol 8000, 50 mM sodium citrate, 10 mM [N-{3-(hydroxyaminocarbonyl)-1-oxo-(2R)-benzylpropyl}-Ile-Leu-OH] and 10% dimethylsulphoxide (DMSO) for three days. The crystal was transferred into a solution with additional 10% glycerol and flash-frozen in liquid nitrogen. X-ray diffraction data were collected as described above. These data were processed and the structure was refined as described above. 
     The TACE monomer includes amino acid residues 6–259 of the catalytic domain (see SEQ ID NO: 20) and is bound to the inhibitor, N-{3-(hydroxyaminocarbonyl)-1-oxo-(2R)-benzylpropyl}-Ile-Leu-OH which has the number 260 in Table 3. The catalytic zinc ion has the number 261. Amino acid residues Arg 28 , Lys 72 , Glu 81 , Lys 88 , Glu 93 , Glu 94 , Lys 95 , and Arg 143  were modeled as Ala residues since their side chains were disordered. The TACE protein used had the amino acid sequence of SEQ ID NO: 20, i.e., Gly 139  is the single point mutation site replacing Val 139  of the TACE wild-type amino acid sequence. 
     In the data set below, one line contains information per one atom. The seven columns of Table 3 represent respectively: 
     1) residue number, 
     2) one-letter amino acid code, 
     3) atom name, 
     4) x-coordinate, 
     5) y-coordinate, 
     6) z-coordinate, and 
     7) B-factor. 
     
       
         
               
             
               
               
               
               
               
               
               
             
           
               
                 TABLE 3 
               
               
                   
               
               
                 COORDINATES for the COMPLEX of vgTACE with 
               
               
                 N-{3-(Hydroxyaminocarbonyl)-1-Oxo-(2R)-Benzylpropyl}-Ile-Leu-OH 
               
               
                   
               
             
             
               
                   
               
             
          
           
               
                 6 
                 PRO 
                 CB 
                 62.073 
                 53.680 
                 60.089 
                 57.01 
               
               
                 6 
                 PRO 
                 CG 
                 62.468 
                 55.126 
                 60.364 
                 57.06 
               
               
                 6 
                 PRO 
                 C 
                 59.660 
                 54.054 
                 59.521 
                 56.73 
               
               
                 6 
                 PRO 
                 O 
                 59.094 
                 53.151 
                 60.132 
                 56.72 
               
               
                 6 
                 PRO 
                 N 
                 61.472 
                 55.081 
                 58.226 
                 56.90 
               
               
                 6 
                 PRO 
                 CD 
                 62.545 
                 55.773 
                 58.963 
                 57.18 
               
               
                 6 
                 PRO 
                 CA 
                 61.066 
                 53.868 
                 58.966 
                 56.85 
               
               
                 7 
                 MET 
                 N 
                 59.104 
                 55.240 
                 59.307 
                 56.47 
               
               
                 7 
                 MET 
                 CA 
                 57.761 
                 55.534 
                 59.770 
                 56.16 
               
               
                 7 
                 MET 
                 CB 
                 57.653 
                 57.002 
                 60.180 
                 57.02 
               
               
                 7 
                 MET 
                 CG 
                 58.514 
                 57.370 
                 61.375 
                 58.06 
               
               
                 7 
                 MET 
                 SD 
                 58.165 
                 59.050 
                 61.936 
                 59.40 
               
               
                 7 
                 MET 
                 CE 
                 59.102 
                 59.999 
                 60.715 
                 59.24 
               
               
                 7 
                 MET 
                 C 
                 56.780 
                 55.226 
                 58.644 
                 55.35 
               
               
                 7 
                 MET 
                 O 
                 55.612 
                 54.925 
                 58.885 
                 55.64 
               
               
                 8 
                 LYS 
                 N 
                 57.269 
                 55.306 
                 57.411 
                 54.05 
               
               
                 8 
                 LYS 
                 CA 
                 56.458 
                 55.020 
                 56.236 
                 52.67 
               
               
                 8 
                 LYS 
                 CB 
                 56.923 
                 55.885 
                 55.062 
                 53.02 
               
               
                 8 
                 LYS 
                 CG 
                 56.888 
                 57.377 
                 55.362 
                 53.28 
               
               
                 8 
                 LYS 
                 CD 
                 57.228 
                 58.210 
                 54.135 
                 53.51 
               
               
                 8 
                 LYS 
                 CE 
                 57.057 
                 59.698 
                 54.425 
                 53.52 
               
               
                 8 
                 LYS 
                 NZ 
                 57.362 
                 60.531 
                 53.233 
                 53.75 
               
               
                 8 
                 LYS 
                 C 
                 56.625 
                 53.534 
                 55.909 
                 51.45 
               
               
                 8 
                 LYS 
                 O 
                 57.436 
                 53.153 
                 55.066 
                 51.21 
               
               
                 9 
                 ASN 
                 N 
                 55.843 
                 52.701 
                 56.585 
                 49.93 
               
               
                 9 
                 ASN 
                 CA 
                 55.927 
                 51.263 
                 56.398 
                 48.31 
               
               
                 9 
                 ASN 
                 CB 
                 56.409 
                 50.618 
                 57.696 
                 48.36 
               
               
                 9 
                 ASN 
                 CG 
                 55.496 
                 50.928 
                 58.878 
                 48.21 
               
               
                 9 
                 ASN 
                 OD1 
                 55.835 
                 50.643 
                 60.029 
                 48.47 
               
               
                 9 
                 ASN 
                 ND2 
                 54.333 
                 51.504 
                 58.599 
                 48.06 
               
               
                 9 
                 ASN 
                 C 
                 54.610 
                 50.632 
                 55.987 
                 47.19 
               
               
                 9 
                 ASN 
                 O 
                 54.456 
                 49.415 
                 56.074 
                 47.11 
               
               
                 10 
                 THR 
                 N 
                 53.662 
                 51.446 
                 55.540 
                 45.73 
               
               
                 10 
                 THR 
                 CA 
                 52.367 
                 50.913 
                 55.151 
                 44.26 
               
               
                 10 
                 THR 
                 CB 
                 51.264 
                 51.294 
                 56.156 
                 44.15 
               
               
                 10 
                 THR 
                 OG1 
                 51.681 
                 50.975 
                 57.487 
                 44.15 
               
               
                 10 
                 THR 
                 CG2 
                 49.992 
                 50.519 
                 55.834 
                 43.84 
               
               
                 10 
                 THR 
                 C 
                 51.883 
                 51.361 
                 53.787 
                 43.31 
               
               
                 10 
                 THR 
                 O 
                 51.918 
                 52.546 
                 53.454 
                 43.14 
               
               
                 11 
                 CYS 
                 N 
                 51.420 
                 50.393 
                 53.007 
                 42.09 
               
               
                 11 
                 CYS 
                 CA 
                 50.872 
                 50.663 
                 51.693 
                 41.05 
               
               
                 11 
                 CYS 
                 C 
                 49.373 
                 50.626 
                 51.927 
                 40.79 
               
               
                 11 
                 CYS 
                 O 
                 48.813 
                 49.571 
                 52.249 
                 40.43 
               
               
                 11 
                 CYS 
                 CB 
                 51.310 
                 49.574 
                 50.705 
                 40.41 
               
               
                 11 
                 CYS 
                 SG 
                 50.526 
                 49.576 
                 49.063 
                 39.35 
               
               
                 12 
                 LYS 
                 N 
                 48.737 
                 51.792 
                 51.812 
                 40.40 
               
               
                 12 
                 LYS 
                 CA 
                 47.297 
                 51.914 
                 52.011 
                 40.31 
               
               
                 12 
                 LYS 
                 CB 
                 46.926 
                 53.386 
                 52.236 
                 40.50 
               
               
                 12 
                 LYS 
                 CG 
                 47.582 
                 54.002 
                 53.467 
                 40.84 
               
               
                 12 
                 LYS 
                 CD 
                 47.193 
                 53.242 
                 54.728 
                 41.39 
               
               
                 12 
                 LYS 
                 CE 
                 47.795 
                 53.864 
                 55.982 
                 42.05 
               
               
                 12 
                 LYS 
                 NZ 
                 47.309 
                 55.259 
                 56.185 
                 42.58 
               
               
                 12 
                 LYS 
                 C 
                 46.567 
                 51.353 
                 50.793 
                 40.16 
               
               
                 12 
                 LYS 
                 O 
                 46.996 
                 51.573 
                 49.660 
                 39.93 
               
               
                 13 
                 LEU 
                 N 
                 45.467 
                 50.637 
                 51.031 
                 39.94 
               
               
                 13 
                 LEU 
                 CA 
                 44.698 
                 50.015 
                 49.954 
                 39.87 
               
               
                 13 
                 LEU 
                 CB 
                 44.540 
                 48.506 
                 50.189 
                 39.57 
               
               
                 13 
                 LEU 
                 CG 
                 45.817 
                 47.718 
                 50.470 
                 39.45 
               
               
                 13 
                 LEU 
                 CD1 
                 45.455 
                 46.287 
                 50.855 
                 39.64 
               
               
                 13 
                 LEU 
                 CD2 
                 46.742 
                 47.691 
                 49.256 
                 39.49 
               
               
                 13 
                 LEU 
                 C 
                 43.283 
                 50.536 
                 49.735 
                 40.21 
               
               
                 13 
                 LEU 
                 O 
                 42.590 
                 50.941 
                 50.674 
                 40.15 
               
               
                 14 
                 LEU 
                 N 
                 42.861 
                 50.484 
                 48.477 
                 40.14 
               
               
                 14 
                 LEU 
                 CA 
                 41.506 
                 50.825 
                 48.098 
                 40.45 
               
               
                 14 
                 LEU 
                 CB 
                 41.451 
                 51.674 
                 46.823 
                 40.27 
               
               
                 14 
                 LEU 
                 CG 
                 40.026 
                 51.690 
                 46.235 
                 40.37 
               
               
                 14 
                 LEU 
                 CD1 
                 39.053 
                 52.388 
                 47.192 
                 40.36 
               
               
                 14 
                 LEU 
                 CD2 
                 39.992 
                 52.378 
                 44.869 
                 40.24 
               
               
                 14 
                 LEU 
                 C 
                 40.996 
                 49.428 
                 47.775 
                 40.61 
               
               
                 14 
                 LEU 
                 O 
                 41.361 
                 48.859 
                 46.749 
                 40.61 
               
               
                 15 
                 VAL 
                 N 
                 40.186 
                 48.853 
                 48.652 
                 40.60 
               
               
                 15 
                 VAL 
                 CA 
                 39.679 
                 47.518 
                 48.387 
                 40.72 
               
               
                 15 
                 VAL 
                 CB 
                 39.685 
                 46.670 
                 49.668 
                 40.68 
               
               
                 15 
                 VAL 
                 CG1 
                 39.000 
                 45.333 
                 49.416 
                 40.84 
               
               
                 15 
                 VAL 
                 CG2 
                 41.133 
                 46.454 
                 50.110 
                 40.43 
               
               
                 15 
                 VAL 
                 C 
                 38.287 
                 47.606 
                 47.805 
                 40.94 
               
               
                 15 
                 VAL 
                 O 
                 37.403 
                 48.247 
                 48.374 
                 40.84 
               
               
                 16 
                 VAL 
                 N 
                 38.104 
                 46.979 
                 46.648 
                 41.32 
               
               
                 16 
                 VAL 
                 CA 
                 36.813 
                 47.000 
                 45.979 
                 41.65 
               
               
                 16 
                 VAL 
                 CB 
                 36.908 
                 47.619 
                 44.556 
                 41.38 
               
               
                 16 
                 VAL 
                 CG1 
                 35.520 
                 47.653 
                 43.911 
                 41.06 
               
               
                 16 
                 VAL 
                 CG2 
                 37.502 
                 49.030 
                 44.633 
                 41.07 
               
               
                 16 
                 VAL 
                 C 
                 36.218 
                 45.610 
                 45.844 
                 42.07 
               
               
                 16 
                 VAL 
                 O 
                 36.890 
                 44.663 
                 45.430 
                 41.85 
               
               
                 17 
                 ALA 
                 N 
                 34.948 
                 45.509 
                 46.217 
                 42.61 
               
               
                 17 
                 ALA 
                 CA 
                 34.195 
                 44.272 
                 46.124 
                 43.48 
               
               
                 17 
                 ALA 
                 CB 
                 33.525 
                 43.956 
                 47.466 
                 43.31 
               
               
                 17 
                 ALA 
                 C 
                 33.140 
                 44.554 
                 45.062 
                 44.03 
               
               
                 17 
                 ALA 
                 O 
                 32.409 
                 45.543 
                 45.169 
                 44.04 
               
               
                 18 
                 ASP 
                 N 
                 33.073 
                 43.714 
                 44.032 
                 44.77 
               
               
                 18 
                 ASP 
                 CA 
                 32.089 
                 43.916 
                 42.973 
                 45.53 
               
               
                 18 
                 ASP 
                 CB 
                 32.632 
                 43.438 
                 41.611 
                 45.20 
               
               
                 18 
                 ASP 
                 CG 
                 32.781 
                 41.928 
                 41.520 
                 45.15 
               
               
                 18 
                 ASP 
                 OD1 
                 32.552 
                 41.243 
                 42.534 
                 45.18 
               
               
                 18 
                 ASP 
                 OD2 
                 33.134 
                 41.429 
                 40.426 
                 44.69 
               
               
                 18 
                 ASP 
                 C 
                 30.798 
                 43.193 
                 43.329 
                 46.32 
               
               
                 18 
                 ASP 
                 O 
                 30.702 
                 42.584 
                 44.398 
                 46.49 
               
               
                 19 
                 HIS 
                 N 
                 29.811 
                 43.255 
                 42.440 
                 47.07 
               
               
                 19 
                 HIS 
                 CA 
                 28.519 
                 42.626 
                 42.699 
                 47.79 
               
               
                 19 
                 HIS 
                 CB 
                 27.505 
                 43.003 
                 41.603 
                 47.47 
               
               
                 19 
                 HIS 
                 CG 
                 27.776 
                 42.367 
                 40.273 
                 47.28 
               
               
                 19 
                 HIS 
                 CD2 
                 27.273 
                 41.247 
                 39.704 
                 47.04 
               
               
                 19 
                 HIS 
                 ND1 
                 28.654 
                 42.902 
                 39.355 
                 47.15 
               
               
                 19 
                 HIS 
                 CE1 
                 28.677 
                 42.140 
                 38.275 
                 47.10 
               
               
                 19 
                 HIS 
                 NE2 
                 27.848 
                 41.129 
                 38.462 
                 47.20 
               
               
                 19 
                 HIS 
                 C 
                 28.585 
                 41.109 
                 42.835 
                 48.24 
               
               
                 19 
                 HIS 
                 O 
                 27.810 
                 40.514 
                 43.584 
                 48.59 
               
               
                 20 
                 ARG 
                 N 
                 29.496 
                 40.475 
                 42.110 
                 48.97 
               
               
                 20 
                 ARG 
                 CA 
                 29.628 
                 39.028 
                 42.194 
                 49.60 
               
               
                 20 
                 ARG 
                 CB 
                 30.652 
                 38.517 
                 41.180 
                 50.00 
               
               
                 20 
                 ARG 
                 CG 
                 30.268 
                 38.661 
                 39.709 
                 50.36 
               
               
                 20 
                 ARG 
                 CD 
                 31.196 
                 37.786 
                 38.863 
                 50.71 
               
               
                 20 
                 ARG 
                 NE 
                 30.919 
                 37.837 
                 37.428 
                 50.98 
               
               
                 20 
                 ARG 
                 CZ 
                 30.938 
                 38.950 
                 36.705 
                 51.03 
               
               
                 20 
                 ARG 
                 NH1 
                 31.217 
                 40.112 
                 37.282 
                 51.22 
               
               
                 20 
                 ARG 
                 NH2 
                 30.693 
                 38.900 
                 35.404 
                 51.10 
               
               
                 20 
                 ARG 
                 C 
                 30.064 
                 38.606 
                 43.601 
                 49.92 
               
               
                 20 
                 ARG 
                 O 
                 29.445 
                 37.743 
                 44.221 
                 50.02 
               
               
                 21 
                 PHE 
                 N 
                 31.135 
                 39.223 
                 44.093 
                 50.14 
               
               
                 21 
                 PHE 
                 CA 
                 31.680 
                 38.921 
                 45.419 
                 50.40 
               
               
                 21 
                 PHE 
                 CB 
                 32.929 
                 39.773 
                 45.671 
                 49.84 
               
               
                 21 
                 PHE 
                 CG 
                 33.724 
                 39.353 
                 46.875 
                 49.29 
               
               
                 21 
                 PHE 
                 CD1 
                 34.687 
                 38.353 
                 46.773 
                 49.02 
               
               
                 21 
                 PHE 
                 CD2 
                 33.512 
                 39.955 
                 48.113 
                 49.00 
               
               
                 21 
                 PHE 
                 CE1 
                 35.427 
                 37.961 
                 47.885 
                 48.83 
               
               
                 21 
                 PHE 
                 CE2 
                 34.247 
                 39.567 
                 49.227 
                 48.85 
               
               
                 21 
                 PHE 
                 CZ 
                 35.206 
                 38.568 
                 49.112 
                 48.76 
               
               
                 21 
                 PHE 
                 C 
                 30.645 
                 39.223 
                 46.499 
                 50.80 
               
               
                 21 
                 PHE 
                 O 
                 30.398 
                 38.412 
                 47.389 
                 50.79 
               
               
                 22 
                 TYR 
                 N 
                 30.057 
                 40.410 
                 46.406 
                 51.47 
               
               
                 22 
                 TYR 
                 CA 
                 29.044 
                 40.882 
                 47.344 
                 52.08 
               
               
                 22 
                 TYR 
                 CB 
                 28.473 
                 42.208 
                 46.847 
                 52.14 
               
               
                 22 
                 TYR 
                 CG 
                 27.346 
                 42.764 
                 47.688 
                 52.33 
               
               
                 22 
                 TYR 
                 CD1 
                 27.568 
                 43.176 
                 49.002 
                 52.41 
               
               
                 22 
                 TYR 
                 CE1 
                 26.543 
                 43.723 
                 49.768 
                 52.36 
               
               
                 22 
                 TYR 
                 CD2 
                 26.061 
                 42.908 
                 47.159 
                 52.31 
               
               
                 22 
                 TYR 
                 CE2 
                 25.027 
                 43.451 
                 47.915 
                 52.30 
               
               
                 22 
                 TYR 
                 CZ 
                 25.274 
                 43.857 
                 49.219 
                 52.34 
               
               
                 22 
                 TYR 
                 OH 
                 24.260 
                 44.396 
                 49.980 
                 52.15 
               
               
                 22 
                 TYR 
                 C 
                 27.902 
                 39.890 
                 47.527 
                 52.49 
               
               
                 22 
                 TYR 
                 O 
                 27.420 
                 39.678 
                 48.639 
                 52.58 
               
               
                 23 
                 ARG 
                 N 
                 27.478 
                 39.285 
                 46.427 
                 52.99 
               
               
                 23 
                 ARG 
                 CA 
                 26.377 
                 38.337 
                 46.439 
                 53.57 
               
               
                 23 
                 ARG 
                 CB 
                 25.772 
                 38.259 
                 45.032 
                 54.21 
               
               
                 23 
                 ARG 
                 CG 
                 24.670 
                 37.231 
                 44.862 
                 55.41 
               
               
                 23 
                 ARG 
                 CD 
                 24.194 
                 37.165 
                 43.414 
                 56.15 
               
               
                 23 
                 ARG 
                 NE 
                 23.138 
                 36.171 
                 43.243 
                 57.12 
               
               
                 23 
                 ARG 
                 CZ 
                 22.521 
                 35.920 
                 42.092 
                 57.61 
               
               
                 23 
                 ARG 
                 NH1 
                 22.853 
                 36.592 
                 40.993 
                 57.83 
               
               
                 23 
                 ARG 
                 NH2 
                 21.575 
                 34.990 
                 42.037 
                 57.92 
               
               
                 23 
                 ARG 
                 C 
                 26.757 
                 36.936 
                 46.915 
                 53.55 
               
               
                 23 
                 ARG 
                 O 
                 26.147 
                 36.400 
                 47.841 
                 53.56 
               
               
                 24 
                 TYR 
                 N 
                 27.771 
                 36.352 
                 46.288 
                 53.52 
               
               
                 24 
                 TYR 
                 CA 
                 28.201 
                 34.997 
                 46.617 
                 53.49 
               
               
                 24 
                 TYR 
                 CB 
                 28.807 
                 34.357 
                 45.369 
                 54.15 
               
               
                 24 
                 TYR 
                 CG 
                 27.825 
                 34.268 
                 44.218 
                 54.87 
               
               
                 24 
                 TYR 
                 CD1 
                 26.763 
                 33.362 
                 44.252 
                 55.28 
               
               
                 24 
                 TYR 
                 CE1 
                 25.845 
                 33.285 
                 43.202 
                 55.60 
               
               
                 24 
                 TYR 
                 CD2 
                 27.945 
                 35.100 
                 43.103 
                 55.19 
               
               
                 24 
                 TYR 
                 CE2 
                 27.031 
                 35.032 
                 42.046 
                 55.54 
               
               
                 24 
                 TYR 
                 CZ 
                 25.987 
                 34.122 
                 42.103 
                 55.78 
               
               
                 24 
                 TYR 
                 OH 
                 25.096 
                 34.033 
                 41.060 
                 56.16 
               
               
                 24 
                 TYR 
                 C 
                 29.156 
                 34.836 
                 47.799 
                 53.15 
               
               
                 24 
                 TYR 
                 O 
                 29.227 
                 33.763 
                 48.393 
                 53.19 
               
               
                 25 
                 MET 
                 N 
                 29.890 
                 35.889 
                 48.142 
                 52.56 
               
               
                 25 
                 MET 
                 CA 
                 30.820 
                 35.816 
                 49.263 
                 51.92 
               
               
                 25 
                 MET 
                 CB 
                 32.197 
                 36.350 
                 48.850 
                 51.12 
               
               
                 25 
                 MET 
                 CG 
                 32.938 
                 35.473 
                 47.856 
                 50.04 
               
               
                 25 
                 MET 
                 SD 
                 33.311 
                 33.822 
                 48.484 
                 48.61 
               
               
                 25 
                 MET 
                 CE 
                 34.533 
                 34.186 
                 49.697 
                 49.08 
               
               
                 25 
                 MET 
                 C 
                 30.312 
                 36.601 
                 50.468 
                 51.97 
               
               
                 25 
                 MET 
                 O 
                 30.580 
                 36.244 
                 51.610 
                 51.92 
               
               
                 26 
                 GLY 
                 N 
                 29.583 
                 37.677 
                 50.206 
                 52.06 
               
               
                 26 
                 GLY 
                 CA 
                 29.065 
                 38.489 
                 51.289 
                 52.32 
               
               
                 26 
                 GLY 
                 C 
                 27.611 
                 38.186 
                 51.579 
                 52.46 
               
               
                 26 
                 GLY 
                 O 
                 26.975 
                 38.889 
                 52.360 
                 52.49 
               
               
                 27 
                 ARG 
                 N 
                 27.089 
                 37.137 
                 50.949 
                 52.57 
               
               
                 27 
                 ARG 
                 CA 
                 25.698 
                 36.740 
                 51.132 
                 52.75 
               
               
                 27 
                 ARG 
                 CB 
                 25.506 
                 36.116 
                 52.520 
                 52.63 
               
               
                 27 
                 ARG 
                 C 
                 24.799 
                 37.964 
                 50.957 
                 52.81 
               
               
                 27 
                 ARG 
                 O 
                 23.786 
                 38.121 
                 51.642 
                 52.84 
               
               
                 28 
                 GLY 
                 N 
                 25.192 
                 38.831 
                 50.028 
                 52.75 
               
               
                 28 
                 GLY 
                 CA 
                 24.429 
                 40.032 
                 49.748 
                 52.70 
               
               
                 28 
                 GLY 
                 C 
                 24.352 
                 41.002 
                 50.906 
                 52.59 
               
               
                 28 
                 GLY 
                 O 
                 23.514 
                 41.900 
                 50.912 
                 52.70 
               
               
                 29 
                 GLU 
                 N 
                 25.225 
                 40.832 
                 51.890 
                 52.61 
               
               
                 29 
                 GLU 
                 CA 
                 25.226 
                 41.716 
                 53.050 
                 52.45 
               
               
                 29 
                 GLU 
                 CB 
                 25.178 
                 40.900 
                 54.340 
                 52.72 
               
               
                 29 
                 GLU 
                 CG 
                 24.292 
                 39.673 
                 54.284 
                 53.26 
               
               
                 29 
                 GLU 
                 CD 
                 24.218 
                 38.966 
                 55.620 
                 53.50 
               
               
                 29 
                 GLU 
                 OE1 
                 23.661 
                 39.561 
                 56.564 
                 53.95 
               
               
                 29 
                 GLU 
                 OE2 
                 24.721 
                 37.826 
                 55.732 
                 53.73 
               
               
                 29 
                 GLU 
                 C 
                 26.462 
                 42.614 
                 53.079 
                 52.17 
               
               
                 29 
                 GLU 
                 O 
                 27.596 
                 42.152 
                 52.911 
                 52.18 
               
               
                 30 
                 GLU 
                 N 
                 26.237 
                 43.899 
                 53.313 
                 51.57 
               
               
                 30 
                 GLU 
                 CA 
                 27.325 
                 44.854 
                 53.365 
                 51.00 
               
               
                 30 
                 GLU 
                 CB 
                 26.760 
                 46.264 
                 53.525 
                 51.37 
               
               
                 30 
                 GLU 
                 CG 
                 27.780 
                 47.365 
                 53.347 
                 51.94 
               
               
                 30 
                 GLU 
                 CD 
                 27.166 
                 48.747 
                 53.451 
                 52.20 
               
               
                 30 
                 GLU 
                 OE1 
                 26.101 
                 48.968 
                 52.840 
                 52.34 
               
               
                 30 
                 GLU 
                 OE2 
                 27.751 
                 49.614 
                 54.134 
                 52.46 
               
               
                 30 
                 GLU 
                 C 
                 28.278 
                 44.539 
                 54.516 
                 50.33 
               
               
                 30 
                 GLU 
                 O 
                 29.495 
                 44.505 
                 54.338 
                 50.25 
               
               
                 31 
                 SER 
                 N 
                 27.717 
                 44.300 
                 55.697 
                 49.48 
               
               
                 31 
                 SER 
                 CA 
                 28.514 
                 44.005 
                 56.880 
                 48.61 
               
               
                 31 
                 SER 
                 CB 
                 27.603 
                 43.854 
                 58.105 
                 48.80 
               
               
                 31 
                 SER 
                 OG 
                 26.746 
                 42.730 
                 57.967 
                 49.18 
               
               
                 31 
                 SER 
                 C 
                 29.353 
                 42.742 
                 56.714 
                 47.87 
               
               
                 31 
                 SER 
                 O 
                 30.516 
                 42.710 
                 57.105 
                 47.78 
               
               
                 32 
                 THR 
                 N 
                 28.755 
                 41.707 
                 56.134 
                 46.96 
               
               
                 32 
                 THR 
                 CA 
                 29.436 
                 40.435 
                 55.924 
                 46.18 
               
               
                 32 
                 THR 
                 CB 
                 28.456 
                 39.373 
                 55.407 
                 46.10 
               
               
                 32 
                 THR 
                 OG1 
                 27.349 
                 39.281 
                 56.310 
                 46.18 
               
               
                 32 
                 THR 
                 CG2 
                 29.132 
                 38.006 
                 55.321 
                 45.75 
               
               
                 32 
                 THR 
                 C 
                 30.567 
                 40.599 
                 54.919 
                 45.65 
               
               
                 32 
                 THR 
                 O 
                 31.699 
                 40.177 
                 55.165 
                 45.46 
               
               
                 33 
                 THR 
                 N 
                 30.254 
                 41.222 
                 53.788 
                 44.84 
               
               
                 33 
                 THR 
                 CA 
                 31.248 
                 41.451 
                 52.752 
                 44.08 
               
               
                 33 
                 THR 
                 CB 
                 30.637 
                 42.243 
                 51.569 
                 43.91 
               
               
                 33 
                 THR 
                 OG1 
                 29.650 
                 41.432 
                 50.922 
                 43.61 
               
               
                 33 
                 THR 
                 CG2 
                 31.710 
                 42.623 
                 50.550 
                 43.80 
               
               
                 33 
                 THR 
                 C 
                 32.436 
                 42.211 
                 53.333 
                 43.65 
               
               
                 33 
                 THR 
                 O 
                 33.585 
                 41.828 
                 53.124 
                 43.57 
               
               
                 34 
                 THR 
                 N 
                 32.155 
                 43.271 
                 54.086 
                 43.09 
               
               
                 34 
                 THR 
                 CA 
                 33.205 
                 44.091 
                 54.688 
                 42.76 
               
               
                 34 
                 THR 
                 CB 
                 32.614 
                 45.317 
                 55.413 
                 42.93 
               
               
                 34 
                 THR 
                 OG1 
                 31.956 
                 46.158 
                 54.462 
                 43.33 
               
               
                 34 
                 THR 
                 CG2 
                 33.715 
                 46.118 
                 56.100 
                 43.26 
               
               
                 34 
                 THR 
                 C 
                 34.082 
                 43.328 
                 55.676 
                 42.38 
               
               
                 34 
                 THR 
                 O 
                 35.314 
                 43.433 
                 55.631 
                 42.11 
               
               
                 35 
                 ASN 
                 N 
                 33.449 
                 42.566 
                 56.564 
                 41.68 
               
               
                 35 
                 ASN 
                 CA 
                 34.183 
                 41.800 
                 57.564 
                 41.10 
               
               
                 35 
                 ASN 
                 CB 
                 33.216 
                 41.095 
                 58.521 
                 41.84 
               
               
                 35 
                 ASN 
                 CG 
                 32.534 
                 42.065 
                 59.473 
                 42.72 
               
               
                 35 
                 ASN 
                 OD1 
                 33.191 
                 42.905 
                 60.091 
                 43.34 
               
               
                 35 
                 ASN 
                 ND2 
                 31.212 
                 41.952 
                 59.600 
                 43.12 
               
               
                 35 
                 ASN 
                 C 
                 35.126 
                 40.778 
                 56.940 
                 40.39 
               
               
                 35 
                 ASN 
                 O 
                 36.269 
                 40.633 
                 57.380 
                 40.26 
               
               
                 36 
                 TYR 
                 N 
                 34.647 
                 40.075 
                 55.920 
                 39.29 
               
               
                 36 
                 TYR 
                 CA 
                 35.469 
                 39.076 
                 55.255 
                 38.44 
               
               
                 36 
                 TYR 
                 CB 
                 34.702 
                 38.447 
                 54.087 
                 38.50 
               
               
                 36 
                 TYR 
                 CG 
                 35.481 
                 37.381 
                 53.337 
                 38.59 
               
               
                 36 
                 TYR 
                 CD1 
                 36.460 
                 37.729 
                 52.406 
                 38.87 
               
               
                 36 
                 TYR 
                 CE1 
                 37.201 
                 36.751 
                 51.737 
                 38.98 
               
               
                 36 
                 TYR 
                 CD2 
                 35.258 
                 36.028 
                 53.578 
                 38.76 
               
               
                 36 
                 TYR 
                 CE2 
                 35.990 
                 35.042 
                 52.915 
                 38.96 
               
               
                 36 
                 TYR 
                 CZ 
                 36.960 
                 35.412 
                 51.999 
                 39.14 
               
               
                 36 
                 TYR 
                 OH 
                 37.695 
                 34.448 
                 51.351 
                 39.43 
               
               
                 36 
                 TYR 
                 C 
                 36.755 
                 39.728 
                 54.753 
                 37.64 
               
               
                 36 
                 TYR 
                 O 
                 37.852 
                 39.220 
                 54.987 
                 37.54 
               
               
                 37 
                 LEU 
                 N 
                 36.614 
                 40.871 
                 54.089 
                 36.62 
               
               
                 37 
                 LEU 
                 CA 
                 37.764 
                 41.582 
                 53.544 
                 35.66 
               
               
                 37 
                 LEU 
                 CB 
                 37.293 
                 42.678 
                 52.589 
                 35.78 
               
               
                 37 
                 LEU 
                 CG 
                 36.523 
                 42.090 
                 51.409 
                 35.99 
               
               
                 37 
                 LEU 
                 CD1 
                 35.933 
                 43.204 
                 50.540 
                 36.23 
               
               
                 37 
                 LEU 
                 CD2 
                 37.423 
                 41.175 
                 50.572 
                 35.84 
               
               
                 37 
                 LEU 
                 C 
                 38.692 
                 42.170 
                 54.592 
                 34.90 
               
               
                 37 
                 LEU 
                 O 
                 39.908 
                 42.183 
                 54.409 
                 34.78 
               
               
                 38 
                 ILE 
                 N 
                 38.125 
                 42.677 
                 55.681 
                 33.72 
               
               
                 38 
                 ILE 
                 CA 
                 38.931 
                 43.237 
                 56.750 
                 32.55 
               
               
                 38 
                 ILE 
                 CB 
                 38.045 
                 43.881 
                 57.838 
                 32.75 
               
               
                 38 
                 ILE 
                 CG2 
                 38.873 
                 44.133 
                 59.101 
                 32.67 
               
               
                 38 
                 ILE 
                 CG1 
                 37.404 
                 45.158 
                 57.286 
                 32.95 
               
               
                 38 
                 ILE 
                 CD1 
                 36.421 
                 45.792 
                 58.267 
                 33.04 
               
               
                 38 
                 ILE 
                 C 
                 39.764 
                 42.117 
                 57.380 
                 32.11 
               
               
                 38 
                 ILE 
                 O 
                 40.946 
                 42.304 
                 57.672 
                 31.63 
               
               
                 39 
                 GLU 
                 N 
                 39.153 
                 40.951 
                 57.581 
                 31.02 
               
               
                 39 
                 GLU 
                 CA 
                 39.888 
                 39.842 
                 58.173 
                 30.48 
               
               
                 39 
                 GLU 
                 CB 
                 38.920 
                 38.752 
                 58.652 
                 30.75 
               
               
                 39 
                 GLU 
                 CG 
                 38.105 
                 39.226 
                 59.858 
                 30.87 
               
               
                 39 
                 GLU 
                 CD 
                 37.639 
                 38.098 
                 60.759 
                 31.45 
               
               
                 39 
                 GLU 
                 OE1 
                 38.342 
                 37.065 
                 60.853 
                 31.14 
               
               
                 39 
                 GLU 
                 OE2 
                 36.576 
                 38.263 
                 61.402 
                 31.89 
               
               
                 39 
                 GLU 
                 C 
                 40.957 
                 39.272 
                 57.236 
                 29.76 
               
               
                 39 
                 GLU 
                 O 
                 42.059 
                 38.961 
                 57.681 
                 29.28 
               
               
                 40 
                 LEU 
                 N 
                 40.636 
                 39.160 
                 55.948 
                 29.41 
               
               
                 40 
                 LEU 
                 CA 
                 41.580 
                 38.648 
                 54.951 
                 29.09 
               
               
                 40 
                 LEU 
                 CB 
                 40.910 
                 38.551 
                 53.568 
                 28.82 
               
               
                 40 
                 LEU 
                 CG 
                 41.832 
                 38.033 
                 52.437 
                 28.74 
               
               
                 40 
                 LEU 
                 CD1 
                 41.002 
                 37.394 
                 51.318 
                 29.05 
               
               
                 40 
                 LEU 
                 CD2 
                 42.690 
                 39.160 
                 51.834 
                 28.74 
               
               
                 40 
                 LEU 
                 C 
                 42.793 
                 39.581 
                 54.869 
                 29.05 
               
               
                 40 
                 LEU 
                 O 
                 43.928 
                 39.124 
                 54.915 
                 29.32 
               
               
                 41 
                 ILE 
                 N 
                 42.559 
                 40.886 
                 54.760 
                 28.87 
               
               
                 41 
                 ILE 
                 CA 
                 43.666 
                 41.827 
                 54.663 
                 29.03 
               
               
                 41 
                 ILE 
                 CG 
                 43.176 
                 43.251 
                 54.326 
                 29.55 
               
               
                 41 
                 ILE 
                 CG2 
                 44.336 
                 44.248 
                 54.448 
                 29.61 
               
               
                 41 
                 ILE 
                 CG1 
                 42.584 
                 43.247 
                 52.915 
                 29.85 
               
               
                 41 
                 ILE 
                 CD1 
                 43.620 
                 42.893 
                 51.871 
                 30.69 
               
               
                 41 
                 ILE 
                 C 
                 44.505 
                 41.843 
                 55.920 
                 28.81 
               
               
                 41 
                 ILE 
                 O 
                 45.735 
                 41.948 
                 55.843 
                 28.95 
               
               
                 42 
                 ASP 
                 N 
                 43.857 
                 41.712 
                 57.082 
                 28.46 
               
               
                 42 
                 ASP 
                 CA 
                 44.602 
                 41.692 
                 58.334 
                 28.44 
               
               
                 42 
                 ASP 
                 CB 
                 43.642 
                 41.680 
                 59.532 
                 28.61 
               
               
                 42 
                 ASP 
                 CG 
                 44.364 
                 41.535 
                 60.858 
                 28.75 
               
               
                 42 
                 ASP 
                 OD1 
                 45.085 
                 42.463 
                 61.281 
                 29.10 
               
               
                 42 
                 ASP 
                 OD2 
                 44.211 
                 40.477 
                 61.477 
                 29.27 
               
               
                 42 
                 ASP 
                 C 
                 45.538 
                 40.474 
                 58.366 
                 28.03 
               
               
                 42 
                 ASP 
                 O 
                 46.685 
                 40.580 
                 58.796 
                 27.60 
               
               
                 43 
                 ARG 
                 N 
                 45.063 
                 39.324 
                 57.898 
                 28.15 
               
               
                 43 
                 ARG 
                 CA 
                 45.906 
                 38.120 
                 57.885 
                 28.17 
               
               
                 43 
                 ARG 
                 CB 
                 45.062 
                 36.863 
                 57.623 
                 28.15 
               
               
                 43 
                 ARG 
                 CG 
                 44.122 
                 36.454 
                 58.770 
                 27.76 
               
               
                 43 
                 ARG 
                 CD 
                 43.472 
                 35.089 
                 58.475 
                 27.71 
               
               
                 43 
                 ARG 
                 NE 
                 42.820 
                 35.046 
                 57.161 
                 26.80 
               
               
                 43 
                 ARG 
                 CZ 
                 41.529 
                 35.271 
                 56.937 
                 27.38 
               
               
                 43 
                 ARG 
                 NH1 
                 40.709 
                 35.562 
                 57.944 
                 27.15 
               
               
                 43 
                 ARG 
                 NH2 
                 41.048 
                 35.194 
                 55.696 
                 27.00 
               
               
                 43 
                 ARG 
                 C 
                 47.046 
                 38.202 
                 56.857 
                 27.98 
               
               
                 43 
                 ARG 
                 O 
                 48.161 
                 37.749 
                 57.125 
                 28.36 
               
               
                 44 
                 VAL 
                 N 
                 46.785 
                 38.774 
                 55.690 
                 28.21 
               
               
                 44 
                 VAL 
                 CA 
                 47.840 
                 38.909 
                 54.678 
                 28.18 
               
               
                 44 
                 VAL 
                 CB 
                 47.269 
                 39.445 
                 53.341 
                 28.21 
               
               
                 44 
                 VAL 
                 CG1 
                 48.384 
                 39.630 
                 52.308 
                 27.55 
               
               
                 44 
                 VAL 
                 CG2 
                 46.203 
                 38.466 
                 52.821 
                 27.51 
               
               
                 44 
                 VAL 
                 C 
                 48.878 
                 39.877 
                 55.238 
                 28.58 
               
               
                 44 
                 VAL 
                 O 
                 50.096 
                 39.657 
                 55.139 
                 28.66 
               
               
                 45 
                 ASP 
                 N 
                 48.392 
                 40.940 
                 55.865 
                 28.68 
               
               
                 45 
                 ASP 
                 CA 
                 49.279 
                 41.922 
                 56.450 
                 28.96 
               
               
                 45 
                 ASP 
                 CB 
                 48.460 
                 43.038 
                 57.112 
                 29.15 
               
               
                 45 
                 ASP 
                 CG 
                 49.334 
                 44.065 
                 57.813 
                 29.82 
               
               
                 45 
                 ASP 
                 OD1 
                 50.246 
                 44.634 
                 57.167 
                 29.51 
               
               
                 45 
                 ASP 
                 OD2 
                 49.108 
                 44.298 
                 59.017 
                 29.85 
               
               
                 45 
                 ASP 
                 C 
                 50.207 
                 41.239 
                 57.462 
                 29.03 
               
               
                 45 
                 ASP 
                 O 
                 51.412 
                 41.502 
                 57.478 
                 28.77 
               
               
                 46 
                 ASP 
                 N 
                 49.660 
                 40.348 
                 58.292 
                 29.37 
               
               
                 46 
                 ASP 
                 CA 
                 50.483 
                 39.637 
                 59.281 
                 29.71 
               
               
                 46 
                 ASP 
                 CB 
                 49.672 
                 38.556 
                 60.019 
                 29.76 
               
               
                 46 
                 ASP 
                 CG 
                 48.718 
                 39.133 
                 61.080 
                 30.25 
               
               
                 46 
                 ASP 
                 OD1 
                 48.876 
                 40.305 
                 61.490 
                 29.71 
               
               
                 46 
                 ASP 
                 OD2 
                 47.818 
                 38.388 
                 61.509 
                 29.87 
               
               
                 46 
                 ASP 
                 C 
                 51.693 
                 38.982 
                 58.593 
                 29.78 
               
               
                 46 
                 ASP 
                 O 
                 52.816 
                 39.029 
                 59.108 
                 29.62 
               
               
                 47 
                 ILE 
                 N 
                 51.460 
                 38.382 
                 57.427 
                 30.23 
               
               
                 47 
                 ILE 
                 CA 
                 52.538 
                 37.735 
                 56.679 
                 30.67 
               
               
                 47 
                 ILE 
                 CB 
                 51.992 
                 37.002 
                 55.433 
                 31.15 
               
               
                 47 
                 ILE 
                 CG2 
                 53.125 
                 36.727 
                 54.447 
                 30.51 
               
               
                 47 
                 ILE 
                 CG1 
                 51.279 
                 35.721 
                 55.872 
                 31.48 
               
               
                 47 
                 ILE 
                 CD1 
                 50.451 
                 35.132 
                 54.766 
                 32.09 
               
               
                 47 
                 ILE 
                 C 
                 53.593 
                 38.755 
                 56.254 
                 31.14 
               
               
                 47 
                 ILE 
                 O 
                 54.792 
                 38.510 
                 56.405 
                 30.87 
               
               
                 48 
                 TYR 
                 N 
                 53.148 
                 39.896 
                 55.732 
                 31.49 
               
               
                 48 
                 TYR 
                 CA 
                 54.068 
                 40.942 
                 55.309 
                 32.49 
               
               
                 48 
                 TYR 
                 CB 
                 53.319 
                 42.061 
                 54.583 
                 31.94 
               
               
                 48 
                 TYR 
                 CG 
                 53.040 
                 41.766 
                 53.135 
                 31.45 
               
               
                 48 
                 TYR 
                 CD1 
                 51.996 
                 40.921 
                 52.760 
                 31.16 
               
               
                 48 
                 TYR 
                 CE1 
                 51.788 
                 40.592 
                 51.431 
                 31.44 
               
               
                 48 
                 TYR 
                 CD2 
                 53.865 
                 42.281 
                 52.135 
                 31.29 
               
               
                 48 
                 TYR 
                 CE2 
                 53.663 
                 41.959 
                 50.801 
                 31.23 
               
               
                 48 
                 TYR 
                 CZ 
                 52.629 
                 41.113 
                 50.452 
                 31.44 
               
               
                 48 
                 TYR 
                 OH 
                 52.432 
                 40.774 
                 49.131 
                 31.26 
               
               
                 48 
                 TYR 
                 C 
                 54.870 
                 41.543 
                 56.460 
                 33.48 
               
               
                 48 
                 TYR 
                 O 
                 56.089 
                 41.631 
                 56.384 
                 33.46 
               
               
                 49 
                 ARG 
                 N 
                 54.185 
                 41.952 
                 57.526 
                 34.66 
               
               
                 49 
                 ARG 
                 CA 
                 54.857 
                 42.550 
                 58.677 
                 36.02 
               
               
                 49 
                 ARG 
                 CB 
                 53.841 
                 42.907 
                 59.764 
                 36.26 
               
               
                 49 
                 ARG 
                 CG 
                 52.763 
                 43.847 
                 59.289 
                 36.68 
               
               
                 49 
                 ARG 
                 CD 
                 53.292 
                 45.229 
                 58.934 
                 37.07 
               
               
                 49 
                 ARG 
                 NE 
                 52.209 
                 46.034 
                 58.368 
                 37.56 
               
               
                 49 
                 ARG 
                 CZ 
                 52.193 
                 47.364 
                 58.307 
                 37.89 
               
               
                 49 
                 ARG 
                 NH1 
                 53.213 
                 48.077 
                 58.781 
                 37.88 
               
               
                 49 
                 ARG 
                 NH2 
                 51.140 
                 47.983 
                 57.785 
                 37.74 
               
               
                 49 
                 ARG 
                 C 
                 55.942 
                 41.659 
                 59.276 
                 36.73 
               
               
                 49 
                 ARG 
                 O 
                 57.010 
                 42.145 
                 59.643 
                 36.86 
               
               
                 50 
                 ASN 
                 N 
                 55.674 
                 40.359 
                 59.373 
                 37.87 
               
               
                 50 
                 ASN 
                 CA 
                 56.648 
                 39.425 
                 59.938 
                 38.88 
               
               
                 50 
                 ASN 
                 CB 
                 55.960 
                 38.130 
                 60.391 
                 39.28 
               
               
                 50 
                 ASN 
                 CG 
                 55.127 
                 38.313 
                 61.653 
                 40.06 
               
               
                 50 
                 ASN 
                 OD1 
                 55.654 
                 38.613 
                 62.729 
                 40.35 
               
               
                 50 
                 ASN 
                 ND2 
                 53.820 
                 38.128 
                 61.527 
                 40.37 
               
               
                 50 
                 ASN 
                 C 
                 57.785 
                 39.076 
                 58.981 
                 39.41 
               
               
                 50 
                 ASN 
                 O 
                 58.719 
                 38.361 
                 59.355 
                 39.55 
               
               
                 51 
                 THR 
                 N 
                 57.716 
                 39.570 
                 57.748 
                 39.83 
               
               
                 51 
                 THR 
                 CA 
                 58.759 
                 39.273 
                 56.766 
                 40.21 
               
               
                 51 
                 THR 
                 CB 
                 58.193 
                 39.341 
                 55.321 
                 39.71 
               
               
                 51 
                 THR 
                 OG1 
                 57.247 
                 38.284 
                 55.130 
                 39.05 
               
               
                 51 
                 THR 
                 CG2 
                 59.311 
                 39.214 
                 54.289 
                 39.56 
               
               
                 51 
                 THR 
                 C 
                 59.963 
                 40.214 
                 56.884 
                 40.90 
               
               
                 51 
                 THR 
                 O 
                 59.811 
                 41.435 
                 56.898 
                 40.72 
               
               
                 52 
                 ALA 
                 N 
                 61.160 
                 39.637 
                 56.989 
                 41.77 
               
               
                 52 
                 ALA 
                 CA 
                 62.377 
                 40.435 
                 57.081 
                 42.50 
               
               
                 52 
                 ALA 
                 CB 
                 63.324 
                 39.846 
                 58.129 
                 42.80 
               
               
                 52 
                 ALA 
                 C 
                 63.024 
                 40.422 
                 55.702 
                 43.07 
               
               
                 52 
                 ALA 
                 O 
                 63.718 
                 39.478 
                 55.335 
                 43.06 
               
               
                 53 
                 TRP 
                 N 
                 62.779 
                 41.481 
                 54.945 
                 43.91 
               
               
                 53 
                 TRP 
                 CA 
                 63.289 
                 41.612 
                 53.589 
                 45.05 
               
               
                 53 
                 TRP 
                 CB 
                 62.739 
                 42.900 
                 52.974 
                 44.35 
               
               
                 53 
                 TRP 
                 CG 
                 61.263 
                 43.028 
                 53.191 
                 44.14 
               
               
                 53 
                 TRP 
                 CD2 
                 60.237 
                 42.245 
                 52.570 
                 43.92 
               
               
                 53 
                 TRP 
                 CE2 
                 59.009 
                 42.619 
                 53.161 
                 43.92 
               
               
                 53 
                 TRP 
                 CE3 
                 60.236 
                 41.260 
                 51.574 
                 43.79 
               
               
                 53 
                 TRP 
                 CD1 
                 60.631 
                 43.829 
                 54.104 
                 43.91 
               
               
                 53 
                 TRP 
                 NE1 
                 59.280 
                 43.587 
                 54.094 
                 43.79 
               
               
                 53 
                 TRP 
                 CZ2 
                 57.790 
                 42.039 
                 52.790 
                 43.71 
               
               
                 53 
                 TRP 
                 CZ3 
                 59.020 
                 40.681 
                 51.205 
                 43.76 
               
               
                 53 
                 TRP 
                 CH2 
                 57.817 
                 41.076 
                 51.813 
                 43.65 
               
               
                 53 
                 TRP 
                 C 
                 64.812 
                 41.568 
                 53.469 
                 46.12 
               
               
                 53 
                 TRP 
                 O 
                 65.355 
                 41.475 
                 52.366 
                 46.40 
               
               
                 54 
                 ASP 
                 N 
                 65.501 
                 41.633 
                 54.601 
                 47.29 
               
               
                 54 
                 ASP 
                 CA 
                 66.957 
                 41.592 
                 54.597 
                 48.59 
               
               
                 54 
                 ASP 
                 CB 
                 67.516 
                 42.909 
                 55.136 
                 48.87 
               
               
                 54 
                 ASP 
                 CG 
                 67.313 
                 43.057 
                 56.624 
                 49.36 
               
               
                 54 
                 ASP 
                 OD1 
                 66.354 
                 42.460 
                 57.157 
                 49.66 
               
               
                 54 
                 ASP 
                 OD2 
                 68.106 
                 43.777 
                 57.264 
                 49.88 
               
               
                 54 
                 ASP 
                 C 
                 67.405 
                 40.438 
                 55.481 
                 49.24 
               
               
                 54 
                 ASP 
                 O 
                 68.549 
                 40.387 
                 55.914 
                 49.44 
               
               
                 55 
                 ASN 
                 N 
                 66.486 
                 39.514 
                 55.748 
                 50.07 
               
               
                 55 
                 ASN 
                 CA 
                 66.766 
                 38.355 
                 56.590 
                 50.93 
               
               
                 55 
                 ASN 
                 CB 
                 67.749 
                 37.415 
                 55.888 
                 51.38 
               
               
                 55 
                 ASN 
                 CG 
                 67.176 
                 36.824 
                 54.618 
                 51.78 
               
               
                 55 
                 ASN 
                 OD1 
                 66.118 
                 36.188 
                 54.642 
                 52.49 
               
               
                 55 
                 ASN 
                 ND2 
                 67.866 
                 37.028 
                 53.500 
                 51.87 
               
               
                 55 
                 ASN 
                 C 
                 67.325 
                 38.768 
                 57.948 
                 51.31 
               
               
                 55 
                 ASN 
                 O 
                 67.796 
                 37.932 
                 58.719 
                 51.50 
               
               
                 56 
                 ALA 
                 N 
                 67.259 
                 40.062 
                 58.238 
                 51.62 
               
               
                 56 
                 ALA 
                 CA 
                 67.760 
                 40.590 
                 59.497 
                 51.85 
               
               
                 56 
                 ALA 
                 CB 
                 68.875 
                 41.606 
                 59.230 
                 51.88 
               
               
                 56 
                 ALA 
                 C 
                 66.641 
                 41.237 
                 60.306 
                 51.99 
               
               
                 56 
                 ALA 
                 O 
                 65.756 
                 40.550 
                 60.827 
                 52.12 
               
               
                 57 
                 GLY 
                 N 
                 66.683 
                 42.562 
                 60.407 
                 52.02 
               
               
                 57 
                 GLY 
                 CA 
                 65.673 
                 43.273 
                 61.172 
                 51.90 
               
               
                 57 
                 GLY 
                 C 
                 64.834 
                 44.247 
                 60.371 
                 51.78 
               
               
                 57 
                 GLY 
                 O 
                 64.105 
                 45.066 
                 60.941 
                 51.80 
               
               
                 58 
                 PHE 
                 N 
                 64.934 
                 44.170 
                 59.047 
                 51.52 
               
               
                 58 
                 PHE 
                 CA 
                 64.161 
                 45.056 
                 58.192 
                 51.17 
               
               
                 58 
                 PHE 
                 CB 
                 64.863 
                 45.257 
                 56.850 
                 51.44 
               
               
                 58 
                 PHE 
                 CG 
                 64.329 
                 46.414 
                 56.053 
                 51.66 
               
               
                 58 
                 PHE 
                 CD1 
                 64.497 
                 47.719 
                 56.504 
                 51.71 
               
               
                 58 
                 PHE 
                 CD2 
                 63.679 
                 46.201 
                 54.838 
                 51.82 
               
               
                 58 
                 PHE 
                 CE1 
                 64.030 
                 48.797 
                 55.754 
                 51.85 
               
               
                 58 
                 PHE 
                 CE2 
                 63.206 
                 47.273 
                 54.078 
                 51.76 
               
               
                 58 
                 PHE 
                 CZ 
                 63.383 
                 48.573 
                 54.536 
                 51.92 
               
               
                 58 
                 PHE 
                 C 
                 62.791 
                 44.427 
                 57.978 
                 50.89 
               
               
                 58 
                 PHE 
                 O 
                 62.525 
                 43.813 
                 56.945 
                 50.82 
               
               
                 59 
                 LYS 
                 N 
                 61.933 
                 44.565 
                 58.981 
                 50.35 
               
               
                 59 
                 LYS 
                 CA 
                 60.584 
                 44.027 
                 58.924 
                 49.76 
               
               
                 59 
                 LYS 
                 CB 
                 60.455 
                 42.835 
                 59.875 
                 50.20 
               
               
                 59 
                 LYS 
                 CG 
                 60.515 
                 43.213 
                 61.340 
                 50.70 
               
               
                 59 
                 LYS 
                 CD 
                 61.263 
                 42.182 
                 62.176 
                 51.68 
               
               
                 59 
                 LYS 
                 CE 
                 60.698 
                 40.771 
                 62.023 
                 52.16 
               
               
                 59 
                 LYS 
                 NZ 
                 61.171 
                 40.095 
                 60.774 
                 52.55 
               
               
                 59 
                 LYS 
                 C 
                 59.623 
                 45.130 
                 59.342 
                 49.05 
               
               
                 59 
                 LYS 
                 O 
                 60.017 
                 46.292 
                 59.468 
                 49.13 
               
               
                 60 
                 GLY 
                 N 
                 58.366 
                 44.768 
                 59.563 
                 48.23 
               
               
                 60 
                 GLY 
                 CA 
                 57.391 
                 45.757 
                 59.973 
                 47.17 
               
               
                 60 
                 GLY 
                 C 
                 56.658 
                 46.411 
                 58.821 
                 46.43 
               
               
                 60 
                 GLY 
                 O 
                 55.847 
                 47.304 
                 59.041 
                 46.28 
               
               
                 61 
                 TYR 
                 N 
                 56.945 
                 45.979 
                 57.594 
                 45.82 
               
               
                 61 
                 TYR 
                 CA 
                 56.274 
                 46.529 
                 56.421 
                 45.19 
               
               
                 61 
                 TYR 
                 CB 
                 57.231 
                 46.588 
                 55.220 
                 45.23 
               
               
                 61 
                 TYR 
                 CG 
                 58.318 
                 47.628 
                 55.362 
                 45.61 
               
               
                 61 
                 TYR 
                 CD1 
                 59.495 
                 47.344 
                 56.054 
                 45.69 
               
               
                 61 
                 TYR 
                 CE1 
                 60.476 
                 48.310 
                 56.228 
                 46.00 
               
               
                 61 
                 TYR 
                 CD2 
                 58.150 
                 48.913 
                 54.844 
                 45.72 
               
               
                 61 
                 TYR 
                 CE2 
                 59.128 
                 49.891 
                 55.017 
                 46.07 
               
               
                 61 
                 TYR 
                 CZ 
                 60.287 
                 49.579 
                 55.711 
                 46.07 
               
               
                 61 
                 TYR 
                 OH 
                 61.254 
                 50.534 
                 55.898 
                 46.61 
               
               
                 61 
                 TYR 
                 C 
                 55.030 
                 45.713 
                 56.050 
                 44.60 
               
               
                 61 
                 TYR 
                 O 
                 55.018 
                 44.486 
                 56.151 
                 44.29 
               
               
                 62 
                 GLY 
                 N 
                 53.982 
                 46.404 
                 55.617 
                 44.24 
               
               
                 62 
                 GLY 
                 CA 
                 52.764 
                 45.710 
                 55.245 
                 43.54 
               
               
                 62 
                 GLY 
                 C 
                 51.743 
                 46.578 
                 54.547 
                 43.26 
               
               
                 62 
                 GLY 
                 O 
                 52.071 
                 47.584 
                 53.916 
                 43.26 
               
               
                 63 
                 ILE 
                 N 
                 50.486 
                 46.178 
                 54.674 
                 42.96 
               
               
                 63 
                 ILE 
                 CA 
                 49.382 
                 46.884 
                 54.055 
                 42.58 
               
               
                 63 
                 ILE 
                 CB 
                 48.708 
                 45.999 
                 52.994 
                 42.40 
               
               
                 63 
                 ILE 
                 CG2 
                 49.671 
                 45.795 
                 51.825 
                 42.19 
               
               
                 63 
                 ILE 
                 CG1 
                 48.283 
                 44.674 
                 53.628 
                 42.25 
               
               
                 63 
                 ILE 
                 CD1 
                 47.610 
                 43.744 
                 52.647 
                 42.44 
               
               
                 63 
                 ILE 
                 C 
                 48.350 
                 47.298 
                 55.096 
                 42.70 
               
               
                 63 
                 ILE 
                 O 
                 48.451 
                 46.940 
                 56.265 
                 42.36 
               
               
                 64 
                 GLN 
                 N 
                 47.353 
                 48.053 
                 54.655 
                 42.99 
               
               
                 64 
                 GLN 
                 CA 
                 46.312 
                 48.535 
                 55.549 
                 43.58 
               
               
                 64 
                 GLN 
                 CB 
                 46.872 
                 49.646 
                 56.435 
                 43.72 
               
               
                 64 
                 GLN 
                 CG 
                 46.027 
                 49.964 
                 57.643 
                 44.56 
               
               
                 64 
                 GLN 
                 CD 
                 46.544 
                 51.166 
                 58.404 
                 44.90 
               
               
                 64 
                 GLN 
                 OE1 
                 46.220 
                 52.311 
                 58.076 
                 45.06 
               
               
                 64 
                 GLN 
                 NE2 
                 47.369 
                 50.915 
                 59.417 
                 45.02 
               
               
                 64 
                 GLN 
                 C 
                 45.185 
                 49.080 
                 54.692 
                 43.80 
               
               
                 64 
                 GLN 
                 O 
                 45.424 
                 49.864 
                 53.774 
                 43.54 
               
               
                 65 
                 ILE 
                 N 
                 43.960 
                 48.654 
                 54.973 
                 44.15 
               
               
                 65 
                 ILE 
                 CA 
                 42.821 
                 49.133 
                 54.208 
                 44.77 
               
               
                 65 
                 ILE 
                 CB 
                 41.545 
                 48.358 
                 54.549 
                 44.68 
               
               
                 65 
                 ILE 
                 CG2 
                 40.369 
                 48.967 
                 53.790 
                 44.65 
               
               
                 65 
                 ILE 
                 CG1 
                 41.742 
                 46.876 
                 54.225 
                 44.77 
               
               
                 65 
                 ILE 
                 CD1 
                 40.501 
                 46.043 
                 54.484 
                 44.90 
               
               
                 65 
                 ILE 
                 C 
                 42.612 
                 50.611 
                 54.517 
                 45.39 
               
               
                 65 
                 ILE 
                 O 
                 42.644 
                 51.032 
                 55.673 
                 45.02 
               
               
                 66 
                 GLU 
                 N 
                 42.424 
                 51.395 
                 53.466 
                 46.36 
               
               
                 66 
                 GLU 
                 CA 
                 42.217 
                 52.825 
                 53.603 
                 47.29 
               
               
                 66 
                 GLU 
                 CB 
                 43.081 
                 53.570 
                 52.595 
                 47.91 
               
               
                 66 
                 GLU 
                 CG 
                 42.907 
                 55.071 
                 52.625 
                 48.97 
               
               
                 66 
                 GLU 
                 CD 
                 44.110 
                 55.764 
                 53.218 
                 49.62 
               
               
                 66 
                 GLU 
                 OE1 
                 44.403 
                 55.552 
                 54.422 
                 50.07 
               
               
                 66 
                 GLU 
                 OE2 
                 44.774 
                 56.516 
                 52.469 
                 49.95 
               
               
                 66 
                 GLU 
                 C 
                 40.757 
                 53.128 
                 53.336 
                 47.78 
               
               
                 66 
                 GLU 
                 O 
                 40.147 
                 53.964 
                 54.001 
                 47.77 
               
               
                 67 
                 GLN 
                 N 
                 40.211 
                 52.445 
                 52.342 
                 48.29 
               
               
                 67 
                 GLN 
                 CA 
                 38.820 
                 52.613 
                 51.971 
                 49.15 
               
               
                 67 
                 GLN 
                 CB 
                 38.660 
                 53.773 
                 50.981 
                 49.40 
               
               
                 67 
                 GLN 
                 CG 
                 37.210 
                 54.029 
                 50.600 
                 50.14 
               
               
                 67 
                 GLN 
                 CD 
                 37.025 
                 55.165 
                 49.609 
                 50.48 
               
               
                 67 
                 GLN 
                 OE1 
                 35.895 
                 55.527 
                 49.284 
                 50.88 
               
               
                 67 
                 GLN 
                 NE2 
                 38.127 
                 55.729 
                 49.120 
                 50.48 
               
               
                 67 
                 GLN 
                 C 
                 38.304 
                 51.330 
                 51.334 
                 49.40 
               
               
                 67 
                 GLN 
                 O 
                 39.037 
                 50.640 
                 50.621 
                 49.36 
               
               
                 68 
                 ILE 
                 N 
                 37.044 
                 51.010 
                 51.604 
                 49.87 
               
               
                 68 
                 ILE 
                 CA 
                 36.419 
                 49.822 
                 51.042 
                 50.50 
               
               
                 68 
                 ILE 
                 CB 
                 35.922 
                 48.853 
                 52.135 
                 50.51 
               
               
                 68 
                 ILE 
                 CG2 
                 35.176 
                 47.695 
                 51.472 
                 50.47 
               
               
                 68 
                 ILE 
                 CG1 
                 37.096 
                 48.365 
                 52.984 
                 50.62 
               
               
                 68 
                 ILE 
                 CD1 
                 36.657 
                 47.442 
                 54.122 
                 50.63 
               
               
                 68 
                 ILE 
                 C 
                 35.222 
                 50.236 
                 50.203 
                 51.11 
               
               
                 68 
                 ILE 
                 O 
                 34.411 
                 51.054 
                 50.625 
                 51.20 
               
               
                 69 
                 ARG 
                 N 
                 35.115 
                 49.672 
                 49.010 
                 51.81 
               
               
                 69 
                 ARG 
                 CA 
                 34.001 
                 49.973 
                 48.132 
                 52.54 
               
               
                 69 
                 ARG 
                 CB 
                 34.488 
                 50.628 
                 46.840 
                 53.05 
               
               
                 69 
                 ARG 
                 CG 
                 35.030 
                 52.025 
                 47.035 
                 53.82 
               
               
                 69 
                 ARG 
                 CD 
                 34.029 
                 52.901 
                 47.769 
                 54.59 
               
               
                 69 
                 ARG 
                 NE 
                 34.453 
                 54.296 
                 47.791 
                 55.44 
               
               
                 69 
                 ARG 
                 CZ 
                 34.497 
                 55.078 
                 46.715 
                 55.75 
               
               
                 69 
                 ARG 
                 NH1 
                 34.140 
                 54.601 
                 45.528 
                 55.91 
               
               
                 69 
                 ARG 
                 NH2 
                 34.897 
                 56.340 
                 46.823 
                 55.87 
               
               
                 69 
                 ARG 
                 C 
                 33.268 
                 48.694 
                 47.807 
                 52.75 
               
               
                 69 
                 ARG 
                 O 
                 33.845 
                 47.762 
                 47.256 
                 52.71 
               
               
                 70 
                 ILE 
                 N 
                 31.992 
                 48.651 
                 48.162 
                 53.11 
               
               
                 70 
                 ILE 
                 CA 
                 31.177 
                 47.479 
                 47.898 
                 53.49 
               
               
                 70 
                 ILE 
                 CB 
                 30.459 
                 47.005 
                 49.183 
                 53.40 
               
               
                 70 
                 ILE 
                 CG2 
                 29.657 
                 45.738 
                 48.885 
                 53.34 
               
               
                 70 
                 ILE 
                 CG1 
                 31.484 
                 46.782 
                 50.296 
                 53.46 
               
               
                 70 
                 ILE 
                 CD1 
                 30.841 
                 46.428 
                 51.613 
                 53.40 
               
               
                 70 
                 ILE 
                 C 
                 30.138 
                 47.815 
                 46.839 
                 53.85 
               
               
                 70 
                 ILE 
                 O 
                 29.202 
                 48.566 
                 47.099 
                 53.84 
               
               
                 71 
                 LEU 
                 N 
                 30.317 
                 47.271 
                 45.639 
                 54.37 
               
               
                 71 
                 LEU 
                 CA 
                 29.379 
                 47.506 
                 44.549 
                 54.89 
               
               
                 71 
                 LEU 
                 CB 
                 30.055 
                 47.275 
                 43.198 
                 54.74 
               
               
                 71 
                 LEU 
                 CG 
                 31.388 
                 48.015 
                 43.074 
                 54.71 
               
               
                 71 
                 LEU 
                 CD1 
                 32.007 
                 47.768 
                 41.699 
                 54.69 
               
               
                 71 
                 LEU 
                 CD2 
                 31.210 
                 49.515 
                 43.310 
                 54.57 
               
               
                 71 
                 LEU 
                 C 
                 28.229 
                 46.526 
                 44.719 
                 55.34 
               
               
                 71 
                 LEU 
                 O 
                 28.326 
                 45.368 
                 44.307 
                 55.27 
               
               
                 72 
                 LYS 
                 N 
                 27.144 
                 47.002 
                 45.324 
                 55.90 
               
               
                 72 
                 LYS 
                 CA 
                 25.969 
                 46.177 
                 45.587 
                 56.55 
               
               
                 72 
                 LYS 
                 CB 
                 24.938 
                 46.986 
                 46.376 
                 56.47 
               
               
                 72 
                 LYS 
                 C 
                 25.323 
                 45.575 
                 44.343 
                 56.94 
               
               
                 72 
                 LYS 
                 O 
                 24.900 
                 44.421 
                 44.357 
                 56.97 
               
               
                 73 
                 SER 
                 N 
                 25.245 
                 46.346 
                 43.265 
                 57.51 
               
               
                 73 
                 SER 
                 CA 
                 24.637 
                 45.839 
                 42.038 
                 58.13 
               
               
                 73 
                 SER 
                 CB 
                 23.242 
                 46.451 
                 41.846 
                 58.24 
               
               
                 73 
                 SER 
                 OG 
                 23.283 
                 47.867 
                 41.883 
                 58.49 
               
               
                 73 
                 SER 
                 C 
                 25.497 
                 46.099 
                 40.805 
                 58.43 
               
               
                 73 
                 SER 
                 O 
                 26.317 
                 47.018 
                 40.790 
                 58.35 
               
               
                 74 
                 PRO 
                 N 
                 25.313 
                 45.287 
                 39.750 
                 58.80 
               
               
                 74 
                 PRO 
                 CD 
                 24.286 
                 44.237 
                 39.626 
                 58.89 
               
               
                 74 
                 PRO 
                 CA 
                 26.069 
                 45.414 
                 38.501 
                 59.17 
               
               
                 74 
                 PRO 
                 CB 
                 25.339 
                 44.466 
                 37.553 
                 59.11 
               
               
                 74 
                 PRO 
                 CG 
                 24.798 
                 43.424 
                 38.464 
                 58.95 
               
               
                 74 
                 PRO 
                 C 
                 26.069 
                 46.838 
                 37.976 
                 59.58 
               
               
                 74 
                 PRO 
                 O 
                 25.188 
                 47.630 
                 38.310 
                 59.54 
               
               
                 75 
                 GLN 
                 N 
                 27.067 
                 47.157 
                 37.159 
                 60.04 
               
               
                 75 
                 GLN 
                 CA 
                 27.183 
                 48.482 
                 36.565 
                 60.43 
               
               
                 75 
                 GLN 
                 CB 
                 28.652 
                 48.859 
                 36.377 
                 60.42 
               
               
                 75 
                 GLN 
                 CG 
                 28.870 
                 50.163 
                 35.619 
                 60.40 
               
               
                 75 
                 GLN 
                 CD 
                 28.245 
                 51.355 
                 36.315 
                 60.49 
               
               
                 75 
                 GLN 
                 OE1 
                 28.527 
                 51.624 
                 37.480 
                 60.43 
               
               
                 75 
                 GLN 
                 NE2 
                 27.389 
                 52.080 
                 35.599 
                 60.54 
               
               
                 75 
                 GLN 
                 C 
                 26.495 
                 48.464 
                 35.211 
                 60.80 
               
               
                 75 
                 GLN 
                 O 
                 26.787 
                 47.614 
                 34.374 
                 60.79 
               
               
                 76 
                 GLU 
                 N 
                 25.574 
                 49.397 
                 35.001 
                 61.39 
               
               
                 76 
                 GLU 
                 CA 
                 24.859 
                 49.474 
                 33.732 
                 61.84 
               
               
                 76 
                 GLU 
                 CB 
                 23.699 
                 50.466 
                 33.841 
                 62.11 
               
               
                 76 
                 GLU 
                 CG 
                 22.626 
                 50.078 
                 34.855 
                 62.52 
               
               
                 76 
                 GLU 
                 CD 
                 21.468 
                 51.068 
                 34.878 
                 62.88 
               
               
                 76 
                 GLU 
                 OE1 
                 20.799 
                 51.224 
                 33.830 
                 63.21 
               
               
                 76 
                 GLU 
                 OE2 
                 21.227 
                 51.690 
                 35.937 
                 62.90 
               
               
                 76 
                 GLU 
                 C 
                 25.830 
                 49.924 
                 32.643 
                 62.00 
               
               
                 76 
                 GLU 
                 O 
                 26.533 
                 50.918 
                 32.811 
                 62.07 
               
               
                 77 
                 VAL 
                 N 
                 25.871 
                 49.192 
                 31.534 
                 62.20 
               
               
                 77 
                 VAL 
                 CA 
                 26.770 
                 49.531 
                 30.435 
                 62.49 
               
               
                 77 
                 VAL 
                 CB 
                 27.862 
                 48.459 
                 30.257 
                 62.52 
               
               
                 77 
                 VAL 
                 CG1 
                 28.693 
                 48.369 
                 31.537 
                 62.62 
               
               
                 77 
                 VAL 
                 CG2 
                 27.224 
                 47.108 
                 29.924 
                 62.51 
               
               
                 77 
                 VAL 
                 C 
                 26.085 
                 49.736 
                 29.083 
                 62.64 
               
               
                 77 
                 VAL 
                 O 
                 25.424 
                 48.839 
                 28.544 
                 62.75 
               
               
                 78 
                 LYS 
                 N 
                 26.270 
                 50.930 
                 28.535 
                 62.74 
               
               
                 78 
                 LYS 
                 CA 
                 25.698 
                 51.291 
                 27.248 
                 62.72 
               
               
                 78 
                 LYS 
                 CB 
                 26.135 
                 52.715 
                 26.895 
                 62.87 
               
               
                 78 
                 LYS 
                 CG 
                 25.966 
                 53.683 
                 28.068 
                 63.12 
               
               
                 78 
                 LYS 
                 CD 
                 26.509 
                 55.069 
                 27.760 
                 63.35 
               
               
                 78 
                 LYS 
                 CE 
                 25.682 
                 55.757 
                 26.695 
                 63.52 
               
               
                 78 
                 LYS 
                 NZ 
                 26.220 
                 57.097 
                 26.322 
                 63.67 
               
               
                 78 
                 LYS 
                 C 
                 26.164 
                 50.296 
                 26.184 
                 62.54 
               
               
                 78 
                 LYS 
                 O 
                 27.154 
                 49.584 
                 26.382 
                 62.53 
               
               
                 79 
                 PRO 
                 N 
                 25.440 
                 50.216 
                 25.051 
                 62.36 
               
               
                 79 
                 PRO 
                 CD 
                 24.173 
                 50.912 
                 24.749 
                 62.31 
               
               
                 79 
                 PRO 
                 CA 
                 25.796 
                 49.298 
                 23.964 
                 62.20 
               
               
                 79 
                 PRO 
                 CB 
                 24.878 
                 49.745 
                 22.832 
                 62.24 
               
               
                 79 
                 PRO 
                 CG 
                 23.626 
                 50.111 
                 23.578 
                 62.28 
               
               
                 79 
                 PRO 
                 C 
                 27.273 
                 49.375 
                 23.580 
                 61.91 
               
               
                 79 
                 PRO 
                 O 
                 27.788 
                 50.452 
                 23.270 
                 62.02 
               
               
                 80 
                 GLY 
                 N 
                 27.947 
                 48.228 
                 23.605 
                 61.55 
               
               
                 80 
                 GLY 
                 CA 
                 29.356 
                 48.175 
                 23.258 
                 60.89 
               
               
                 80 
                 GLY 
                 C 
                 30.309 
                 48.534 
                 24.385 
                 60.40 
               
               
                 80 
                 GLY 
                 O 
                 31.483 
                 48.166 
                 24.331 
                 60.45 
               
               
                 81 
                 GLU 
                 N 
                 29.819 
                 49.255 
                 25.391 
                 59.82 
               
               
                 81 
                 GLU 
                 CA 
                 30.642 
                 49.675 
                 26.526 
                 59.12 
               
               
                 81 
                 GLU 
                 CB 
                 29.969 
                 50.851 
                 27.250 
                 59.16 
               
               
                 81 
                 GLU 
                 C 
                 30.926 
                 48.540 
                 27.518 
                 58.67 
               
               
                 81 
                 GLU 
                 O 
                 30.174 
                 47.562 
                 27.603 
                 58.69 
               
               
                 82 
                 LYS 
                 N 
                 32.021 
                 48.683 
                 28.262 
                 57.81 
               
               
                 82 
                 LYS 
                 CA 
                 32.429 
                 47.696 
                 29.263 
                 57.01 
               
               
                 82 
                 LYS 
                 CB 
                 33.671 
                 46.933 
                 28.809 
                 57.13 
               
               
                 82 
                 LYS 
                 CG 
                 33.473 
                 46.000 
                 27.637 
                 57.26 
               
               
                 82 
                 LYS 
                 CD 
                 34.827 
                 45.557 
                 27.082 
                 57.37 
               
               
                 82 
                 LYS 
                 CE 
                 35.623 
                 46.743 
                 26.528 
                 57.56 
               
               
                 82 
                 LYS 
                 NZ 
                 36.890 
                 46.328 
                 25.854 
                 57.55 
               
               
                 82 
                 LYS 
                 C 
                 32.756 
                 48.344 
                 30.597 
                 56.39 
               
               
                 82 
                 LYS 
                 O 
                 33.085 
                 49.530 
                 30.678 
                 56.15 
               
               
                 83 
                 HIS 
                 N 
                 32.668 
                 47.535 
                 31.643 
                 55.70 
               
               
                 83 
                 HIS 
                 CA 
                 32.969 
                 47.970 
                 32.999 
                 55.05 
               
               
                 83 
                 HIS 
                 CB 
                 31.767 
                 48.705 
                 33.606 
                 54.78 
               
               
                 83 
                 HIS 
                 CG 
                 32.061 
                 49.374 
                 34.916 
                 54.53 
               
               
                 83 
                 HIS 
                 CD2 
                 32.328 
                 50.664 
                 35.218 
                 54.59 
               
               
                 83 
                 HIS 
                 ND1 
                 32.126 
                 48.682 
                 36.107 
                 54.54 
               
               
                 83 
                 HIS 
                 CE1 
                 32.419 
                 49.520 
                 37.085 
                 54.44 
               
               
                 83 
                 HIS 
                 NE2 
                 32.548 
                 50.730 
                 36.574 
                 54.55 
               
               
                 83 
                 HIS 
                 C 
                 33.291 
                 46.701 
                 33.787 
                 54.71 
               
               
                 83 
                 HIS 
                 O 
                 32.661 
                 45.662 
                 33.575 
                 54.68 
               
               
                 84 
                 TYR 
                 N 
                 34.276 
                 46.768 
                 34.679 
                 54.17 
               
               
                 84 
                 TYR 
                 CA 
                 34.645 
                 45.587 
                 35.455 
                 53.76 
               
               
                 84 
                 TYR 
                 CB 
                 35.851 
                 45.880 
                 36.350 
                 52.91 
               
               
                 84 
                 TYR 
                 CG 
                 35.579 
                 46.812 
                 37.510 
                 52.25 
               
               
                 84 
                 TYR 
                 CD1 
                 35.627 
                 48.199 
                 37.351 
                 51.75 
               
               
                 84 
                 TYR 
                 CE1 
                 35.431 
                 49.059 
                 38.438 
                 51.53 
               
               
                 84 
                 TYR 
                 CD2 
                 35.316 
                 46.303 
                 38.785 
                 51.78 
               
               
                 84 
                 TYR 
                 CE2 
                 35.113 
                 47.150 
                 39.876 
                 51.52 
               
               
                 84 
                 TYR 
                 CZ 
                 35.175 
                 48.522 
                 39.701 
                 51.42 
               
               
                 84 
                 TYR 
                 OH 
                 35.007 
                 49.343 
                 40.789 
                 50.97 
               
               
                 84 
                 TYR 
                 C 
                 33.493 
                 45.059 
                 36.310 
                 53.81 
               
               
                 84 
                 TYR 
                 O 
                 33.437 
                 43.867 
                 36.617 
                 53.72 
               
               
                 85 
                 ASN 
                 N 
                 32.571 
                 45.941 
                 36.680 
                 54.04 
               
               
                 85 
                 ASN 
                 CA 
                 31.437 
                 45.550 
                 37.511 
                 54.28 
               
               
                 85 
                 ASN 
                 CB 
                 31.208 
                 46.599 
                 38.604 
                 54.07 
               
               
                 85 
                 ASN 
                 CG 
                 30.175 
                 46.160 
                 39.630 
                 53.85 
               
               
                 85 
                 ASN 
                 OD1 
                 30.173 
                 45.012 
                 40.072 
                 53.62 
               
               
                 85 
                 ASN 
                 ND2 
                 29.302 
                 47.081 
                 40.026 
                 53.78 
               
               
                 85 
                 ASN 
                 C 
                 30.133 
                 45.308 
                 36.746 
                 54.72 
               
               
                 85 
                 ASN 
                 O 
                 29.061 
                 45.282 
                 37.347 
                 54.66 
               
               
                 86 
                 MET 
                 N 
                 30.222 
                 45.121 
                 35.430 
                 55.28 
               
               
                 86 
                 MET 
                 CA 
                 29.032 
                 44.865 
                 34.622 
                 55.89 
               
               
                 86 
                 MET 
                 CB 
                 29.305 
                 45.136 
                 33.133 
                 56.02 
               
               
                 86 
                 MET 
                 CG 
                 30.326 
                 44.225 
                 32.476 
                 56.14 
               
               
                 86 
                 MET 
                 SD 
                 30.704 
                 44.761 
                 30.775 
                 56.77 
               
               
                 86 
                 MET 
                 CE 
                 30.752 
                 43.196 
                 29.895 
                 56.07 
               
               
                 86 
                 MET 
                 C 
                 28.568 
                 43.425 
                 34.813 
                 56.27 
               
               
                 86 
                 MET 
                 O 
                 29.360 
                 42.545 
                 35.169 
                 56.28 
               
               
                 87 
                 ALA 
                 N 
                 27.283 
                 43.191 
                 34.564 
                 56.60 
               
               
                 87 
                 ALA 
                 CA 
                 26.688 
                 41.871 
                 34.735 
                 56.88 
               
               
                 87 
                 ALA 
                 CB 
                 25.177 
                 41.953 
                 34.505 
                 56.95 
               
               
                 87 
                 ALA 
                 C 
                 27.285 
                 40.784 
                 33.855 
                 57.08 
               
               
                 87 
                 ALA 
                 O 
                 27.508 
                 39.662 
                 34.310 
                 57.04 
               
               
                 88 
                 LYS 
                 N 
                 27.542 
                 41.107 
                 32.595 
                 57.40 
               
               
                 88 
                 LYS 
                 CA 
                 28.097 
                 40.123 
                 31.676 
                 57.94 
               
               
                 88 
                 LYS 
                 CB 
                 27.616 
                 40.413 
                 30.251 
                 57.93 
               
               
                 88 
                 LYS 
                 C 
                 29.621 
                 40.089 
                 31.715 
                 58.25 
               
               
                 88 
                 LYS 
                 O 
                 30.272 
                 41.107 
                 31.956 
                 58.25 
               
               
                 89 
                 SER 
                 N 
                 30.187 
                 38.912 
                 31.489 
                 58.63 
               
               
                 89 
                 SER 
                 CA 
                 31.633 
                 38.785 
                 31.476 
                 59.25 
               
               
                 89 
                 SER 
                 CB 
                 32.059 
                 37.355 
                 31.823 
                 59.17 
               
               
                 89 
                 SER 
                 OG 
                 31.725 
                 36.450 
                 30.787 
                 59.39 
               
               
                 89 
                 SER 
                 C 
                 32.070 
                 39.146 
                 30.062 
                 59.60 
               
               
                 89 
                 SER 
                 O 
                 31.258 
                 39.140 
                 29.136 
                 59.66 
               
               
                 90 
                 TYR 
                 N 
                 33.344 
                 39.475 
                 29.900 
                 59.97 
               
               
                 90 
                 TYR 
                 CA 
                 33.884 
                 39.847 
                 28.597 
                 60.31 
               
               
                 90 
                 TYR 
                 CB 
                 34.038 
                 41.371 
                 28.537 
                 60.49 
               
               
                 90 
                 TYR 
                 CG 
                 34.554 
                 41.917 
                 27.225 
                 60.75 
               
               
                 90 
                 TYR 
                 CD1 
                 35.901 
                 41.812 
                 26.881 
                 60.73 
               
               
                 90 
                 TYR 
                 CE1 
                 36.377 
                 42.321 
                 25.672 
                 60.86 
               
               
                 90 
                 TYR 
                 CD2 
                 33.691 
                 42.545 
                 26.326 
                 60.76 
               
               
                 90 
                 TYR 
                 CE2 
                 34.156 
                 43.056 
                 25.117 
                 60.81 
               
               
                 90 
                 TYR 
                 CZ 
                 35.498 
                 42.942 
                 24.796 
                 60.86 
               
               
                 90 
                 TYR 
                 OH 
                 35.957 
                 43.457 
                 23.604 
                 60.88 
               
               
                 90 
                 TYR 
                 C 
                 35.238 
                 39.163 
                 28.438 
                 60.43 
               
               
                 90 
                 TYR 
                 O 
                 35.975 
                 39.017 
                 29.411 
                 60.46 
               
               
                 91 
                 PRO 
                 N 
                 35.597 
                 38.746 
                 27.209 
                 60.56 
               
               
                 91 
                 PRO 
                 CD 
                 36.958 
                 38.218 
                 27.000 
                 60.61 
               
               
                 91 
                 PRO 
                 CA 
                 34.888 
                 38.845 
                 25.925 
                 60.69 
               
               
                 91 
                 PRO 
                 CB 
                 36.017 
                 38.719 
                 24.915 
                 60.67 
               
               
                 91 
                 PRO 
                 CG 
                 36.899 
                 37.713 
                 25.577 
                 60.65 
               
               
                 91 
                 PRO 
                 C 
                 33.772 
                 37.830 
                 25.645 
                 60.74 
               
               
                 91 
                 PRO 
                 O 
                 32.830 
                 38.138 
                 24.908 
                 60.86 
               
               
                 92 
                 ASN 
                 N 
                 33.877 
                 36.627 
                 26.208 
                 60.72 
               
               
                 92 
                 ASN 
                 CA 
                 32.862 
                 35.594 
                 25.989 
                 60.66 
               
               
                 92 
                 ASN 
                 CB 
                 33.482 
                 34.202 
                 26.115 
                 60.91 
               
               
                 92 
                 ASN 
                 CG 
                 32.607 
                 33.117 
                 25.509 
                 61.25 
               
               
                 92 
                 ASN 
                 OD1 
                 31.443 
                 32.951 
                 25.889 
                 61.45 
               
               
                 92 
                 ASN 
                 ND2 
                 33.164 
                 32.372 
                 24.557 
                 61.35 
               
               
                 92 
                 ASN 
                 C 
                 31.701 
                 35.713 
                 26.970 
                 60.49 
               
               
                 92 
                 ASN 
                 O 
                 31.734 
                 35.126 
                 28.051 
                 60.44 
               
               
                 93 
                 GLU 
                 N 
                 30.674 
                 36.463 
                 26.581 
                 60.23 
               
               
                 93 
                 GLU 
                 CA 
                 29.502 
                 36.672 
                 27.427 
                 59.90 
               
               
                 93 
                 GLU 
                 CB 
                 28.433 
                 37.469 
                 26.667 
                 60.10 
               
               
                 93 
                 GLU 
                 C 
                 28.911 
                 35.362 
                 27.919 
                 59.61 
               
               
                 93 
                 GLU 
                 O 
                 28.273 
                 35.322 
                 28.974 
                 59.58 
               
               
                 94 
                 GLU 
                 N 
                 29.140 
                 34.289 
                 27.166 
                 59.18 
               
               
                 94 
                 GLU 
                 CA 
                 28.603 
                 32.976 
                 27.518 
                 58.67 
               
               
                 94 
                 GLU 
                 CB 
                 28.631 
                 32.061 
                 26.289 
                 58.81 
               
               
                 94 
                 GLU 
                 C 
                 29.302 
                 32.291 
                 28.696 
                 58.28 
               
               
                 94 
                 GLU 
                 O 
                 28.686 
                 31.486 
                 29.405 
                 58.33 
               
               
                 95 
                 LYS 
                 N 
                 30.579 
                 32.604 
                 28.900 
                 57.63 
               
               
                 95 
                 LYS 
                 CA 
                 31.352 
                 32.013 
                 29.986 
                 56.88 
               
               
                 95 
                 LYS 
                 CB 
                 32.843 
                 32.047 
                 29.640 
                 56.89 
               
               
                 95 
                 LYS 
                 C 
                 31.102 
                 32.719 
                 31.323 
                 56.39 
               
               
                 95 
                 LYS 
                 O 
                 30.639 
                 33.863 
                 31.368 
                 56.43 
               
               
                 96 
                 ASP 
                 N 
                 31.415 
                 32.026 
                 32.414 
                 55.64 
               
               
                 96 
                 ASP 
                 CA 
                 31.230 
                 32.568 
                 33.758 
                 54.84 
               
               
                 96 
                 ASP 
                 CB 
                 31.501 
                 31.479 
                 34.805 
                 55.19 
               
               
                 96 
                 ASP 
                 CG 
                 31.613 
                 32.036 
                 36.220 
                 55.58 
               
               
                 96 
                 ASP 
                 OD1 
                 30.665 
                 32.704 
                 36.685 
                 55.84 
               
               
                 96 
                 ASP 
                 OD2 
                 32.650 
                 31.798 
                 36.868 
                 55.61 
               
               
                 96 
                 ASP 
                 C 
                 32.100 
                 33.782 
                 34.073 
                 53.98 
               
               
                 96 
                 ASP 
                 O 
                 31.639 
                 34.734 
                 34.707 
                 53.84 
               
               
                 97 
                 ALA 
                 N 
                 33.348 
                 33.758 
                 33.616 
                 52.96 
               
               
                 97 
                 ALA 
                 CA 
                 34.270 
                 34.845 
                 33.916 
                 51.86 
               
               
                 97 
                 ALA 
                 CB 
                 35.353 
                 34.325 
                 34.866 
                 52.03 
               
               
                 97 
                 ALA 
                 C 
                 34.934 
                 35.558 
                 32.742 
                 51.02 
               
               
                 97 
                 ALA 
                 O 
                 35.056 
                 35.020 
                 31.638 
                 50.90 
               
               
                 98 
                 TRP 
                 N 
                 35.373 
                 36.784 
                 33.014 
                 49.95 
               
               
                 98 
                 TRP 
                 CA 
                 36.080 
                 37.600 
                 32.036 
                 48.91 
               
               
                 98 
                 TRP 
                 CB 
                 36.458 
                 38.962 
                 32.608 
                 48.72 
               
               
                 98 
                 TRP 
                 CG 
                 35.441 
                 40.023 
                 32.645 
                 48.66 
               
               
                 98 
                 TRP 
                 CD2 
                 35.581 
                 41.334 
                 32.094 
                 48.56 
               
               
                 98 
                 TRP 
                 CE2 
                 34.458 
                 42.081 
                 32.503 
                 48.57 
               
               
                 98 
                 TRP 
                 CE3 
                 36.556 
                 41.953 
                 31.296 
                 48.57 
               
               
                 98 
                 TRP 
                 CD1 
                 34.264 
                 40.019 
                 33.335 
                 48.50 
               
               
                 98 
                 TRP 
                 NE1 
                 33.671 
                 41.253 
                 33.260 
                 48.39 
               
               
                 98 
                 TRP 
                 CZ2 
                 34.279 
                 43.421 
                 32.145 
                 48.50 
               
               
                 98 
                 TRP 
                 CZ3 
                 36.379 
                 43.284 
                 30.941 
                 48.55 
               
               
                 98 
                 TRP 
                 CH2 
                 35.248 
                 44.004 
                 31.367 
                 48.57 
               
               
                 98 
                 TRP 
                 C 
                 37.413 
                 36.939 
                 31.772 
                 48.06 
               
               
                 98 
                 TRP 
                 O 
                 37.813 
                 36.005 
                 32.470 
                 47.91 
               
               
                 99 
                 ASP 
                 N 
                 38.104 
                 37.453 
                 30.761 
                 47.24 
               
               
                 99 
                 ASP 
                 CA 
                 39.457 
                 37.013 
                 30.468 
                 46.10 
               
               
                 99 
                 ASP 
                 CB 
                 39.929 
                 37.579 
                 29.137 
                 46.43 
               
               
                 99 
                 ASP 
                 CG 
                 41.427 
                 37.508 
                 28.986 
                 46.46 
               
               
                 99 
                 ASP 
                 OD1 
                 41.941 
                 36.400 
                 28.727 
                 47.06 
               
               
                 99 
                 ASP 
                 OD2 
                 42.092 
                 38.550 
                 29.144 
                 46.60 
               
               
                 99 
                 ASP 
                 C 
                 40.144 
                 37.776 
                 31.600 
                 45.23 
               
               
                 99 
                 ASP 
                 O 
                 40.003 
                 39.002 
                 31.691 
                 44.88 
               
               
                 100 
                 VAL 
                 N 
                 40.867 
                 37.073 
                 32.466 
                 44.29 
               
               
                 100 
                 VAL 
                 CA 
                 41.502 
                 37.725 
                 33.605 
                 43.47 
               
               
                 100 
                 VAL 
                 CB 
                 42.310 
                 36.706 
                 34.465 
                 43.18 
               
               
                 100 
                 VAL 
                 CG1 
                 43.509 
                 36.157 
                 33.689 
                 42.91 
               
               
                 100 
                 VAL 
                 CG2 
                 42.758 
                 37.388 
                 35.760 
                 42.85 
               
               
                 100 
                 VAL 
                 C 
                 42.387 
                 38.923 
                 33.256 
                 43.23 
               
               
                 100 
                 VAL 
                 O 
                 42.304 
                 39.971 
                 33.909 
                 42.97 
               
               
                 101 
                 LYS 
                 N 
                 43.225 
                 38.777 
                 32.233 
                 42.98 
               
               
                 101 
                 LYS 
                 CA 
                 44.107 
                 39.864 
                 31.822 
                 43.00 
               
               
                 101 
                 LYS 
                 CB 
                 45.033 
                 39.393 
                 30.690 
                 43.37 
               
               
                 101 
                 LYS 
                 CG 
                 46.058 
                 40.425 
                 30.248 
                 43.86 
               
               
                 101 
                 LYS 
                 CD 
                 46.966 
                 39.889 
                 29.141 
                 44.34 
               
               
                 101 
                 LYS 
                 CE 
                 47.942 
                 40.968 
                 28.673 
                 44.98 
               
               
                 101 
                 LYS 
                 NZ 
                 49.056 
                 40.417 
                 27.830 
                 44.94 
               
               
                 101 
                 LYS 
                 C 
                 43.281 
                 41.079 
                 31.377 
                 42.76 
               
               
                 101 
                 LYS 
                 O 
                 43.573 
                 42.216 
                 31.754 
                 42.74 
               
               
                 102 
                 MET 
                 N 
                 42.245 
                 40.838 
                 30.579 
                 42.66 
               
               
                 102 
                 MET 
                 CA 
                 41.385 
                 41.924 
                 30.121 
                 42.38 
               
               
                 102 
                 MET 
                 CB 
                 40.387 
                 41.424 
                 29.077 
                 42.94 
               
               
                 102 
                 MET 
                 CG 
                 41.000 
                 41.193 
                 27.696 
                 43.54 
               
               
                 102 
                 MET 
                 SD 
                 39.812 
                 40.663 
                 26.435 
                 44.26 
               
               
                 102 
                 MET 
                 CE 
                 40.520 
                 39.136 
                 25.937 
                 44.13 
               
               
                 102 
                 MET 
                 C 
                 40.632 
                 42.531 
                 31.296 
                 41.87 
               
               
                 102 
                 MET 
                 O 
                 40.461 
                 43.744 
                 31.373 
                 42.04 
               
               
                 103 
                 LEU 
                 N 
                 40.186 
                 41.687 
                 32.220 
                 41.39 
               
               
                 103 
                 LEU 
                 CA 
                 39.457 
                 42.177 
                 33.376 
                 40.80 
               
               
                 103 
                 LEU 
                 CB 
                 38.980 
                 41.007 
                 34.245 
                 40.97 
               
               
                 103 
                 LEU 
                 CG 
                 38.421 
                 41.464 
                 35.605 
                 41.14 
               
               
                 103 
                 LEU 
                 CD1 
                 37.354 
                 42.554 
                 35.429 
                 41.16 
               
               
                 103 
                 LEU 
                 CD2 
                 37.840 
                 40.278 
                 36.376 
                 40.92 
               
               
                 103 
                 LEU 
                 C 
                 40.315 
                 43.124 
                 34.207 
                 40.26 
               
               
                 103 
                 LEU 
                 O 
                 39.854 
                 44.181 
                 34.630 
                 39.94 
               
               
                 104 
                 LEU 
                 N 
                 41.570 
                 42.751 
                 34.432 
                 39.97 
               
               
                 104 
                 LEU 
                 CA 
                 42.457 
                 43.586 
                 35.234 
                 39.64 
               
               
                 104 
                 LEU 
                 CG 
                 43.802 
                 42.873 
                 35.453 
                 39.38 
               
               
                 104 
                 LEU 
                 CG 
                 44.769 
                 43.686 
                 36.322 
                 39.11 
               
               
                 104 
                 LEU 
                 CD1 
                 44.122 
                 44.066 
                 37.656 
                 38.99 
               
               
                 104 
                 LEU 
                 CD2 
                 46.064 
                 42.905 
                 36.567 
                 39.19 
               
               
                 104 
                 LEU 
                 C 
                 42.673 
                 44.958 
                 34.591 
                 39.70 
               
               
                 104 
                 LEU 
                 O 
                 42.686 
                 45.977 
                 35.282 
                 39.74 
               
               
                 105 
                 GLU 
                 N 
                 42.829 
                 44.991 
                 33.270 
                 39.72 
               
               
                 105 
                 GLU 
                 CA 
                 43.038 
                 46.262 
                 32.590 
                 39.81 
               
               
                 105 
                 GLU 
                 CB 
                 43.403 
                 46.048 
                 31.113 
                 39.50 
               
               
                 105 
                 GLU 
                 CG 
                 44.044 
                 47.290 
                 30.505 
                 39.45 
               
               
                 105 
                 GLU 
                 CD 
                 44.533 
                 47.106 
                 29.080 
                 39.30 
               
               
                 105 
                 GLU 
                 OE1 
                 45.020 
                 46.004 
                 28.735 
                 39.29 
               
               
                 105 
                 GLU 
                 OE2 
                 44.446 
                 48.082 
                 28.308 
                 39.37 
               
               
                 105 
                 GLU 
                 C 
                 41.783 
                 47.130 
                 32.701 
                 40.04 
               
               
                 105 
                 GLU 
                 O 
                 41.875 
                 48.339 
                 32.914 
                 39.95 
               
               
                 106 
                 GLN 
                 N 
                 40.611 
                 46.510 
                 32.565 
                 40.23 
               
               
                 106 
                 GLN 
                 CA 
                 39.351 
                 47.246 
                 32.676 
                 40.32 
               
               
                 106 
                 GLN 
                 CB 
                 38.159 
                 46.328 
                 32.436 
                 40.79 
               
               
                 106 
                 GLN 
                 CG 
                 36.847 
                 47.083 
                 32.344 
                 41.31 
               
               
                 106 
                 GLN 
                 CD 
                 36.810 
                 47.977 
                 31.122 
                 41.76 
               
               
                 106 
                 GLN 
                 OE1 
                 36.925 
                 47.497 
                 30.003 
                 42.24 
               
               
                 106 
                 GLN 
                 NE2 
                 36.663 
                 49.282 
                 31.331 
                 41.92 
               
               
                 106 
                 GLN 
                 C 
                 39.214 
                 47.853 
                 34.066 
                 40.23 
               
               
                 106 
                 GLN 
                 O 
                 38.889 
                 49.037 
                 34.225 
                 39.87 
               
               
                 107 
                 PHE 
                 N 
                 39.451 
                 47.030 
                 35.080 
                 39.95 
               
               
                 107 
                 PHE 
                 CA 
                 39.350 
                 47.502 
                 36.448 
                 39.81 
               
               
                 107 
                 PHE 
                 CB 
                 39.753 
                 46.396 
                 37.425 
                 39.46 
               
               
                 107 
                 PHE 
                 CG 
                 39.855 
                 46.859 
                 38.843 
                 39.13 
               
               
                 107 
                 PHE 
                 CD1 
                 38.759 
                 47.434 
                 39.479 
                 38.92 
               
               
                 107 
                 PHE 
                 CD2 
                 41.057 
                 46.745 
                 39.541 
                 39.16 
               
               
                 107 
                 PHE 
                 CE1 
                 38.853 
                 47.892 
                 40.783 
                 38.80 
               
               
                 107 
                 PHE 
                 CE2 
                 41.166 
                 47.200 
                 40.852 
                 38.87 
               
               
                 107 
                 PHE 
                 CZ 
                 40.062 
                 47.777 
                 41.475 
                 39.11 
               
               
                 107 
                 PHE 
                 C 
                 40.249 
                 48.714 
                 36.635 
                 39.97 
               
               
                 107 
                 PHE 
                 O 
                 39.852 
                 49.705 
                 37.249 
                 39.64 
               
               
                 108 
                 SER 
                 N 
                 41.467 
                 48.624 
                 36.100 
                 40.20 
               
               
                 108 
                 SER 
                 CA 
                 42.435 
                 49.708 
                 36.198 
                 40.65 
               
               
                 108 
                 SER 
                 CB 
                 43.764 
                 49.281 
                 35.555 
                 40.75 
               
               
                 108 
                 SER 
                 OG 
                 44.397 
                 48.270 
                 36.326 
                 40.70 
               
               
                 108 
                 SER 
                 C 
                 41.901 
                 50.976 
                 35.525 
                 41.00 
               
               
                 108 
                 SER 
                 O 
                 42.091 
                 52.085 
                 36.023 
                 40.78 
               
               
                 109 
                 PHE 
                 N 
                 41.232 
                 50.796 
                 34.392 
                 41.58 
               
               
                 109 
                 PHE 
                 CA 
                 40.664 
                 51.914 
                 33.647 
                 42.31 
               
               
                 109 
                 PHE 
                 CB 
                 40.138 
                 51.422 
                 32.294 
                 42.55 
               
               
                 109 
                 PHE 
                 CG 
                 39.381 
                 52.468 
                 31.512 
                 43.19 
               
               
                 109 
                 PHE 
                 CD1 
                 40.058 
                 53.489 
                 30.840 
                 43.31 
               
               
                 109 
                 PHE 
                 CD2 
                 37.986 
                 52.444 
                 31.466 
                 43.13 
               
               
                 109 
                 PHE 
                 CE1 
                 39.358 
                 54.472 
                 30.134 
                 43.43 
               
               
                 109 
                 PHE 
                 CE2 
                 37.277 
                 53.421 
                 30.766 
                 43.47 
               
               
                 109 
                 PHE 
                 CZ 
                 37.965 
                 54.440 
                 30.097 
                 43.28 
               
               
                 109 
                 PHE 
                 C 
                 39.530 
                 52.604 
                 34.409 
                 42.61 
               
               
                 109 
                 PHE 
                 O 
                 39.489 
                 53.828 
                 34.504 
                 42.49 
               
               
                 110 
                 ASP 
                 N 
                 38.616 
                 51.810 
                 34.955 
                 43.11 
               
               
                 110 
                 ASP 
                 CA 
                 37.468 
                 52.356 
                 35.672 
                 43.65 
               
               
                 110 
                 ASP 
                 CB 
                 36.394 
                 51.278 
                 35.834 
                 43.73 
               
               
                 110 
                 ASP 
                 CG 
                 35.826 
                 50.827 
                 34.511 
                 43.66 
               
               
                 110 
                 ASP 
                 OD1 
                 35.467 
                 51.703 
                 33.698 
                 44.35 
               
               
                 110 
                 ASP 
                 OD2 
                 35.725 
                 49.605 
                 34.280 
                 43.87 
               
               
                 110 
                 ASP 
                 C 
                 37.756 
                 52.985 
                 37.026 
                 44.03 
               
               
                 110 
                 ASP 
                 O 
                 37.168 
                 54.011 
                 37.367 
                 44.05 
               
               
                 111 
                 ILE 
                 N 
                 38.658 
                 52.384 
                 37.796 
                 44.24 
               
               
                 111 
                 ILE 
                 CA 
                 38.982 
                 52.903 
                 39.118 
                 44.73 
               
               
                 111 
                 ILE 
                 CB 
                 39.388 
                 51.739 
                 40.074 
                 44.96 
               
               
                 111 
                 ILE 
                 CG2 
                 40.899 
                 51.509 
                 40.001 
                 45.08 
               
               
                 111 
                 ILE 
                 CG1 
                 38.920 
                 52.040 
                 41.499 
                 45.06 
               
               
                 111 
                 ILE 
                 CD1 
                 37.407 
                 52.123 
                 41.605 
                 45.37 
               
               
                 111 
                 ILE 
                 C 
                 40.097 
                 53.952 
                 39.091 
                 44.84 
               
               
                 111 
                 ILE 
                 O 
                 40.495 
                 54.472 
                 40.134 
                 44.79 
               
               
                 112 
                 ALA 
                 N 
                 40.581 
                 54.269 
                 37.894 
                 45.28 
               
               
                 112 
                 ALA 
                 CA 
                 41.668 
                 55.234 
                 37.703 
                 45.60 
               
               
                 112 
                 ALA 
                 CB 
                 41.664 
                 55.721 
                 36.251 
                 45.60 
               
               
                 112 
                 ALA 
                 C 
                 41.703 
                 56.437 
                 38.656 
                 46.11 
               
               
                 112 
                 ALA 
                 O 
                 42.695 
                 56.654 
                 39.359 
                 45.85 
               
               
                 113 
                 GLU 
                 N 
                 40.633 
                 57.230 
                 38.672 
                 46.58 
               
               
                 113 
                 GLU 
                 CA 
                 40.579 
                 58.404 
                 39.542 
                 47.25 
               
               
                 113 
                 GLU 
                 CB 
                 39.206 
                 59.003 
                 39.453 
                 48.10 
               
               
                 113 
                 GLU 
                 CG 
                 38.831 
                 59.503 
                 38.044 
                 49.39 
               
               
                 113 
                 GLU 
                 CD 
                 38.447 
                 58.322 
                 37.168 
                 50.14 
               
               
                 113 
                 GLU 
                 OE1 
                 38.460 
                 58.476 
                 35.927 
                 50.83 
               
               
                 113 
                 GLU 
                 OE2 
                 38.124 
                 57.243 
                 37.721 
                 50.63 
               
               
                 113 
                 GLU 
                 C 
                 40.882 
                 58.058 
                 40.996 
                 47.10 
               
               
                 113 
                 GLU 
                 O 
                 41.702 
                 58.714 
                 41.640 
                 46.96 
               
               
                 114 
                 GLU 
                 N 
                 40.223 
                 57.028 
                 41.515 
                 47.26 
               
               
                 114 
                 GLU 
                 CA 
                 40.459 
                 56.624 
                 42.895 
                 47.33 
               
               
                 114 
                 GLU 
                 CB 
                 39.307 
                 55.624 
                 43.339 
                 48.04 
               
               
                 114 
                 GLU 
                 CG 
                 37.978 
                 56.204 
                 43.279 
                 49.07 
               
               
                 114 
                 GLU 
                 CD 
                 36.938 
                 55.295 
                 43.903 
                 49.76 
               
               
                 114 
                 GLU 
                 OE1 
                 37.024 
                 55.045 
                 45.129 
                 50.01 
               
               
                 114 
                 GLU 
                 OE2 
                 36.034 
                 54.831 
                 43.169 
                 50.18 
               
               
                 114 
                 GLU 
                 C 
                 41.859 
                 56.027 
                 43.058 
                 46.96 
               
               
                 114 
                 GLU 
                 O 
                 42.580 
                 56.374 
                 43.990 
                 46.83 
               
               
                 115 
                 ALA 
                 N 
                 42.250 
                 55.155 
                 42.131 
                 46.60 
               
               
                 115 
                 ALA 
                 CA 
                 43.560 
                 54.518 
                 42.188 
                 46.18 
               
               
                 115 
                 ALA 
                 CB 
                 43.763 
                 53.636 
                 40.954 
                 46.08 
               
               
                 115 
                 ALA 
                 C 
                 44.692 
                 55.540 
                 42.296 
                 45.96 
               
               
                 115 
                 ALA 
                 O 
                 45.732 
                 55.261 
                 42.888 
                 45.88 
               
               
                 116 
                 SER 
                 N 
                 44.479 
                 56.726 
                 41.734 
                 45.83 
               
               
                 116 
                 SER 
                 CA 
                 45.491 
                 57.781 
                 41.752 
                 45.45 
               
               
                 116 
                 SER 
                 CB 
                 45.051 
                 58.941 
                 40.857 
                 45.79 
               
               
                 116 
                 SER 
                 OG 
                 43.950 
                 59.637 
                 41.431 
                 46.56 
               
               
                 116 
                 SER 
                 C 
                 45.783 
                 58.321 
                 43.145 
                 45.01 
               
               
                 116 
                 SER 
                 O 
                 46.820 
                 58.942 
                 43.370 
                 44.95 
               
               
                 117 
                 LYS 
                 N 
                 44.877 
                 58.078 
                 44.084 
                 44.49 
               
               
                 117 
                 LYS 
                 CA 
                 45.034 
                 58.592 
                 45.438 
                 43.96 
               
               
                 117 
                 LYS 
                 CB 
                 43.699 
                 59.167 
                 45.916 
                 44.62 
               
               
                 117 
                 LYS 
                 CG 
                 43.180 
                 60.294 
                 45.040 
                 45.26 
               
               
                 117 
                 LYS 
                 CD 
                 41.749 
                 60.682 
                 45.391 
                 45.71 
               
               
                 117 
                 LYS 
                 CE 
                 41.290 
                 61.840 
                 44.512 
                 46.27 
               
               
                 117 
                 LYS 
                 NZ 
                 39.905 
                 62.270 
                 44.841 
                 46.64 
               
               
                 117 
                 LYS 
                 C 
                 45.562 
                 57.617 
                 46.481 
                 43.42 
               
               
                 117 
                 LYS 
                 O 
                 45.813 
                 58.014 
                 47.617 
                 43.44 
               
               
                 118 
                 VAL 
                 N 
                 45.735 
                 56.351 
                 46.111 
                 42.52 
               
               
                 118 
                 VAL 
                 CA 
                 46.239 
                 55.359 
                 47.062 
                 41.47 
               
               
                 118 
                 VAL 
                 CB 
                 45.155 
                 54.330 
                 47.435 
                 41.77 
               
               
                 118 
                 VAL 
                 CG1 
                 44.181 
                 54.939 
                 48.444 
                 41.78 
               
               
                 118 
                 VAL 
                 CG2 
                 44.417 
                 53.882 
                 46.168 
                 41.66 
               
               
                 118 
                 VAL 
                 C 
                 47.457 
                 54.579 
                 46.589 
                 40.74 
               
               
                 118 
                 VAL 
                 O 
                 47.823 
                 54.611 
                 45.416 
                 40.46 
               
               
                 119 
                 CYS 
                 N 
                 48.076 
                 53.867 
                 47.526 
                 39.88 
               
               
                 119 
                 CYS 
                 CA 
                 49.242 
                 53.057 
                 47.226 
                 38.75 
               
               
                 119 
                 CYS 
                 C 
                 48.871 
                 51.928 
                 46.269 
                 38.23 
               
               
                 119 
                 CYS 
                 O 
                 49.550 
                 51.705 
                 45.262 
                 37.93 
               
               
                 119 
                 CYS 
                 CB 
                 49.828 
                 52.489 
                 48.516 
                 38.99 
               
               
                 119 
                 CYS 
                 SG 
                 51.156 
                 51.304 
                 48.189 
                 39.08 
               
               
                 120 
                 LEU 
                 N 
                 47.782 
                 51.232 
                 46.582 
                 37.29 
               
               
                 120 
                 LEU 
                 CA 
                 47.294 
                 50.130 
                 45.758 
                 36.83 
               
               
                 120 
                 LEU 
                 CB 
                 47.825 
                 48.787 
                 46.268 
                 36.78 
               
               
                 120 
                 LEU 
                 CG 
                 49.289 
                 48.477 
                 45.935 
                 36.84 
               
               
                 120 
                 LEU 
                 CD1 
                 49.699 
                 47.143 
                 46.584 
                 36.69 
               
               
                 120 
                 LEU 
                 CD2 
                 49.505 
                 48.411 
                 44.416 
                 36.93 
               
               
                 120 
                 LEU 
                 C 
                 45.776 
                 50.044 
                 45.758 
                 36.55 
               
               
                 120 
                 LEU 
                 O 
                 45.117 
                 50.448 
                 46.712 
                 36.38 
               
               
                 121 
                 ALA 
                 N 
                 45.237 
                 49.498 
                 44.676 
                 36.37 
               
               
                 121 
                 ALA 
                 CA 
                 43.802 
                 49.283 
                 44.539 
                 36.19 
               
               
                 121 
                 ALA 
                 CB 
                 43.233 
                 50.126 
                 43.398 
                 36.11 
               
               
                 121 
                 ALA 
                 C 
                 43.670 
                 47.790 
                 44.225 
                 35.94 
               
               
                 121 
                 ALA 
                 O 
                 44.370 
                 47.278 
                 43.354 
                 35.76 
               
               
                 122 
                 HIS 
                 N 
                 42.789 
                 47.092 
                 44.937 
                 35.85 
               
               
                 122 
                 HIS 
                 CA 
                 42.614 
                 45.661 
                 44.717 
                 35.65 
               
               
                 122 
                 HIS 
                 CB 
                 43.191 
                 44.869 
                 45.903 
                 35.42 
               
               
                 122 
                 HIS 
                 CG 
                 43.523 
                 43.447 
                 45.575 
                 35.09 
               
               
                 122 
                 HIS 
                 CD2 
                 42.833 
                 42.302 
                 45.778 
                 34.99 
               
               
                 122 
                 HIS 
                 ND1 
                 44.674 
                 43.086 
                 44.906 
                 35.06 
               
               
                 122 
                 HIS 
                 CE1 
                 44.675 
                 41.780 
                 44.710 
                 34.72 
               
               
                 122 
                 HIS 
                 NE2 
                 43.571 
                 41.280 
                 45.227 
                 34.70 
               
               
                 122 
                 HIS 
                 C 
                 41.147 
                 45.298 
                 44.532 
                 35.95 
               
               
                 122 
                 HIS 
                 O 
                 40.281 
                 45.718 
                 45.306 
                 35.96 
               
               
                 123 
                 LEU 
                 N 
                 40.882 
                 44.503 
                 43.503 
                 36.17 
               
               
                 123 
                 LEU 
                 CA 
                 39.536 
                 44.053 
                 43.186 
                 36.35 
               
               
                 123 
                 LEU 
                 CB 
                 39.325 
                 44.126 
                 41.676 
                 36.14 
               
               
                 123 
                 LEU 
                 CG 
                 38.054 
                 43.424 
                 41.186 
                 36.51 
               
               
                 123 
                 LEU 
                 CD1 
                 36.797 
                 44.062 
                 41.781 
                 35.94 
               
               
                 123 
                 LEU 
                 CD2 
                 37.995 
                 43.461 
                 39.652 
                 35.81 
               
               
                 123 
                 LEU 
                 C 
                 39.250 
                 42.627 
                 43.668 
                 36.77 
               
               
                 123 
                 LEU 
                 O 
                 39.970 
                 41.685 
                 43.334 
                 36.61 
               
               
                 124 
                 PHE 
                 N 
                 38.204 
                 42.482 
                 44.480 
                 36.97 
               
               
                 124 
                 PHE 
                 CA 
                 37.798 
                 41.166 
                 44.955 
                 37.31 
               
               
                 124 
                 PHE 
                 CB 
                 37.563 
                 41.158 
                 46.470 
                 36.56 
               
               
                 124 
                 PHE 
                 CG 
                 38.827 
                 41.275 
                 47.275 
                 35.87 
               
               
                 124 
                 PHE 
                 CD1 
                 39.350 
                 42.520 
                 47.601 
                 35.46 
               
               
                 124 
                 PHE 
                 CD2 
                 39.510 
                 40.130 
                 47.683 
                 35.68 
               
               
                 124 
                 PHE 
                 CE1 
                 40.536 
                 42.630 
                 48.327 
                 35.35 
               
               
                 124 
                 PHE 
                 CE2 
                 40.701 
                 40.225 
                 48.411 
                 35.04 
               
               
                 124 
                 PHE 
                 CZ 
                 41.211 
                 41.476 
                 48.732 
                 35.19 
               
               
                 124 
                 PHE 
                 C 
                 36.515 
                 40.847 
                 44.222 
                 37.97 
               
               
                 124 
                 PHE 
                 O 
                 35.510 
                 41.533 
                 44.395 
                 37.89 
               
               
                 125 
                 THR 
                 N 
                 36.576 
                 39.819 
                 43.387 
                 38.53 
               
               
                 125 
                 THR 
                 CA 
                 35.442 
                 39.382 
                 42.589 
                 39.62 
               
               
                 125 
                 THR 
                 CB 
                 35.743 
                 39.519 
                 41.082 
                 39.80 
               
               
                 125 
                 THR 
                 OG1 
                 34.580 
                 09.180 
                 40.313 
                 40.27 
               
               
                 125 
                 THR 
                 CG2 
                 36.882 
                 38.572 
                 40.698 
                 40.00 
               
               
                 125 
                 THR 
                 C 
                 35.143 
                 37.914 
                 42.872 
                 40.18 
               
               
                 125 
                 THR 
                 O 
                 35.818 
                 37.267 
                 43.673 
                 39.87 
               
               
                 126 
                 TYR 
                 N 
                 34.129 
                 37.392 
                 42.197 
                 40.95 
               
               
                 126 
                 TYR 
                 CA 
                 33.747 
                 35.998 
                 42.363 
                 41.69 
               
               
                 126 
                 TYR 
                 CB 
                 32.552 
                 35.879 
                 43.318 
                 41.98 
               
               
                 126 
                 TYR 
                 CG 
                 32.259 
                 34.454 
                 43.736 
                 42.49 
               
               
                 126 
                 TYR 
                 CD1 
                 33.053 
                 33.808 
                 44.685 
                 42.57 
               
               
                 126 
                 TYR 
                 CE1 
                 32.818 
                 32.482 
                 45.039 
                 42.99 
               
               
                 126 
                 TYR 
                 CD2 
                 31.218 
                 33.735 
                 43.151 
                 42.74 
               
               
                 126 
                 TYR 
                 CE2 
                 30.973 
                 32.403 
                 43.495 
                 42.81 
               
               
                 126 
                 TYR 
                 CZ 
                 31.777 
                 31.784 
                 44.437 
                 42.91 
               
               
                 126 
                 TYR 
                 OH 
                 31.566 
                 30.465 
                 44.755 
                 43.11 
               
               
                 126 
                 TYR 
                 C 
                 33.394 
                 35.384 
                 41.008 
                 42.12 
               
               
                 126 
                 TYR 
                 O 
                 32.224 
                 35.230 
                 40.670 
                 42.34 
               
               
                 127 
                 GLN 
                 N 
                 34.415 
                 35.065 
                 40.219 
                 42.76 
               
               
                 127 
                 GLN 
                 CA 
                 34.208 
                 34.442 
                 38.915 
                 43.26 
               
               
                 127 
                 GLN 
                 CB 
                 34.217 
                 35.498 
                 37.799 
                 43.14 
               
               
                 127 
                 GLN 
                 CG 
                 35.246 
                 36.612 
                 37.946 
                 42.91 
               
               
                 127 
                 GLN 
                 CD 
                 34.958 
                 37.792 
                 37.024 
                 42.59 
               
               
                 127 
                 GLN 
                 OE1 
                 34.938 
                 37.654 
                 35.803 
                 42.66 
               
               
                 127 
                 GLN 
                 NE2 
                 34.735 
                 38.958 
                 37.610 
                 42.61 
               
               
                 127 
                 GLN 
                 C 
                 35.260 
                 33.360 
                 38.672 
                 43.75 
               
               
                 127 
                 GLN 
                 O 
                 36.400 
                 33.474 
                 39.120 
                 43.51 
               
               
                 128 
                 ASP 
                 N 
                 34.861 
                 32.303 
                 37.973 
                 44.39 
               
               
                 128 
                 ASP 
                 CA 
                 35.745 
                 31.179 
                 37.705 
                 45.26 
               
               
                 128 
                 ASP 
                 CB 
                 34.920 
                 29.893 
                 37.597 
                 46.00 
               
               
                 128 
                 ASP 
                 CG 
                 35.770 
                 28.639 
                 37.682 
                 46.60 
               
               
                 128 
                 ASP 
                 OD1 
                 37.011 
                 28.752 
                 37.811 
                 47.14 
               
               
                 128 
                 ASP 
                 OD2 
                 35.186 
                 27.533 
                 37.626 
                 47.15 
               
               
                 128 
                 ASP 
                 C 
                 36.548 
                 31.386 
                 36.434 
                 45.56 
               
               
                 128 
                 ASP 
                 O 
                 36.023 
                 31.228 
                 35.331 
                 45.53 
               
               
                 129 
                 PHE 
                 N 
                 37.822 
                 31.740 
                 36.602 
                 45.62 
               
               
                 129 
                 PHE 
                 CA 
                 38.719 
                 31.982 
                 35.477 
                 45.80 
               
               
                 129 
                 PHE 
                 CB 
                 39.944 
                 32.797 
                 35.916 
                 45.38 
               
               
                 129 
                 PHE 
                 CG 
                 39.615 
                 34.179 
                 36.412 
                 44.95 
               
               
                 129 
                 PHE 
                 CD1 
                 38.936 
                 35.081 
                 35.599 
                 44.72 
               
               
                 129 
                 PHE 
                 CD2 
                 39.986 
                 34.578 
                 37.690 
                 44.59 
               
               
                 129 
                 PHE 
                 CE1 
                 38.630 
                 36.362 
                 36.057 
                 44.77 
               
               
                 129 
                 PHE 
                 CE2 
                 39.687 
                 35.854 
                 38.158 
                 44.62 
               
               
                 129 
                 PHE 
                 CZ 
                 39.006 
                 36.750 
                 37.342 
                 44.61 
               
               
                 129 
                 PHE 
                 C 
                 39.193 
                 30.673 
                 34.875 
                 46.19 
               
               
                 129 
                 PHE 
                 O 
                 39.149 
                 29.622 
                 35.521 
                 46.15 
               
               
                 130 
                 ASP 
                 N 
                 39.651 
                 30.755 
                 33.630 
                 46.61 
               
               
                 130 
                 ASP 
                 CA 
                 40.154 
                 29.597 
                 32.896 
                 47.04 
               
               
                 130 
                 ASP 
                 CB 
                 40.314 
                 29.949 
                 31.417 
                 47.59 
               
               
                 130 
                 ASP 
                 CG 
                 39.089 
                 29.600 
                 30.604 
                 48.18 
               
               
                 130 
                 ASP 
                 OD1 
                 38.725 
                 28.403 
                 30.574 
                 48.64 
               
               
                 130 
                 ASP 
                 OD2 
                 38.490 
                 30.514 
                 29.994 
                 48.61 
               
               
                 130 
                 ASP 
                 C 
                 41.479 
                 29.056 
                 33.412 
                 46.87 
               
               
                 130 
                 ASP 
                 O 
                 42.295 
                 29.792 
                 33.967 
                 46.99 
               
               
                 131 
                 MET 
                 N 
                 41.682 
                 27.759 
                 33.211 
                 46.72 
               
               
                 131 
                 MET 
                 CA 
                 42.907 
                 27.088 
                 33.618 
                 46.61 
               
               
                 131 
                 MET 
                 CB 
                 44.112 
                 27.686 
                 32.873 
                 47.71 
               
               
                 131 
                 MET 
                 CG 
                 43.962 
                 27.784 
                 31.348 
                 49.21 
               
               
                 131 
                 MET 
                 SD 
                 45.510 
                 28.252 
                 30.493 
                 50.81 
               
               
                 131 
                 MET 
                 CE 
                 45.787 
                 29.965 
                 31.114 
                 50.14 
               
               
                 131 
                 MET 
                 C 
                 43.155 
                 27.148 
                 35.129 
                 45.94 
               
               
                 131 
                 MET 
                 O 
                 44.265 
                 26.870 
                 35.582 
                 45.93 
               
               
                 132 
                 GLY 
                 N 
                 42.132 
                 27.517 
                 35.899 
                 44.94 
               
               
                 132 
                 GLY 
                 CA 
                 42.277 
                 27.580 
                 37.346 
                 44.07 
               
               
                 132 
                 GLY 
                 C 
                 43.000 
                 28.794 
                 37.914 
                 43.19 
               
               
                 132 
                 GLY 
                 O 
                 43.528 
                 28.745 
                 39.033 
                 43.33 
               
               
                 133 
                 THR 
                 N 
                 43.023 
                 29.882 
                 37.150 
                 42.18 
               
               
                 133 
                 THR 
                 CA 
                 43.666 
                 31.121 
                 37.578 
                 40.98 
               
               
                 133 
                 THR 
                 CB 
                 43.808 
                 32.099 
                 36.383 
                 41.19 
               
               
                 133 
                 THR 
                 OG1 
                 44.649 
                 71.515 
                 35.377 
                 41.40 
               
               
                 133 
                 THR 
                 CG2 
                 44.414 
                 33.427 
                 36.842 
                 41.23 
               
               
                 133 
                 THR 
                 C 
                 42.809 
                 31.771 
                 38.674 
                 39.94 
               
               
                 133 
                 THR 
                 O 
                 41.586 
                 31.842 
                 38.546 
                 39.84 
               
               
                 134 
                 LEU 
                 N 
                 43.444 
                 32.239 
                 39.747 
                 38.76 
               
               
                 134 
                 LEU 
                 CA 
                 42.711 
                 32.869 
                 40.845 
                 37.81 
               
               
                 134 
                 LEU 
                 CB 
                 43.042 
                 32.173 
                 42.175 
                 37.94 
               
               
                 134 
                 LEU 
                 CG 
                 42.389 
                 30.789 
                 42.318 
                 37.96 
               
               
                 134 
                 LEU 
                 CD1 
                 42.685 
                 30.206 
                 43.698 
                 37.70 
               
               
                 134 
                 LEU 
                 CD2 
                 40.870 
                 30.873 
                 42.122 
                 37.86 
               
               
                 134 
                 LEU 
                 C 
                 42.927 
                 34.377 
                 41.003 
                 37.01 
               
               
                 134 
                 LEU 
                 O 
                 42.134 
                 35.065 
                 41.650 
                 36.89 
               
               
                 135 
                 GLY 
                 N 
                 43.998 
                 34.902 
                 40.430 
                 36.22 
               
               
                 135 
                 GLY 
                 CA 
                 44.235 
                 36.328 
                 40.559 
                 35.22 
               
               
                 135 
                 GLY 
                 C 
                 45.271 
                 36.830 
                 39.581 
                 34.68 
               
               
                 135 
                 GLY 
                 O 
                 45.902 
                 36.035 
                 38.886 
                 34.19 
               
               
                 136 
                 LEU 
                 N 
                 45.449 
                 38.146 
                 39.530 
                 34.01 
               
               
                 136 
                 LEU 
                 CA 
                 46.423 
                 38.747 
                 38.625 
                 33.85 
               
               
                 136 
                 LEU 
                 CB 
                 45.798 
                 38.886 
                 37.229 
                 33.98 
               
               
                 136 
                 LEU 
                 CG 
                 46.809 
                 39.145 
                 36.108 
                 34.21 
               
               
                 136 
                 LEU 
                 CD1 
                 47.681 
                 37.906 
                 35.869 
                 34.29 
               
               
                 136 
                 LEU 
                 CD2 
                 46.072 
                 39.523 
                 34.814 
                 33.73 
               
               
                 136 
                 LEU 
                 C 
                 46.806 
                 40.120 
                 39.182 
                 33.49 
               
               
                 136 
                 LEU 
                 O 
                 45.999 
                 40.766 
                 39.852 
                 33.44 
               
               
                 137 
                 ALA 
                 N 
                 48.032 
                 40.563 
                 38.912 
                 33.26 
               
               
                 137 
                 ALA 
                 CA 
                 48.501 
                 41.858 
                 39.402 
                 33.14 
               
               
                 137 
                 ALA 
                 CB 
                 48.891 
                 41.743 
                 40.876 
                 32.82 
               
               
                 137 
                 ALA 
                 C 
                 49.691 
                 42.373 
                 38.603 
                 33.33 
               
               
                 137 
                 ALA 
                 O 
                 50.378 
                 41.597 
                 37.942 
                 32.89 
               
               
                 138 
                 TYR 
                 N 
                 49.932 
                 43.679 
                 38.679 
                 33.35 
               
               
                 138 
                 TYR 
                 CA 
                 51.051 
                 44.300 
                 37.967 
                 34.13 
               
               
                 138 
                 TYR 
                 CB 
                 50.633 
                 45.642 
                 37.343 
                 33.72 
               
               
                 138 
                 TYR 
                 CG 
                 49.420 
                 45.578 
                 36.435 
                 34.20 
               
               
                 138 
                 TYR 
                 CD1 
                 49.409 
                 44.750 
                 35.311 
                 34.16 
               
               
                 138 
                 TYR 
                 CE1 
                 48.314 
                 44.718 
                 34.444 
                 34.48 
               
               
                 138 
                 TYR 
                 CD2 
                 48.295 
                 46.380 
                 36.676 
                 34.16 
               
               
                 138 
                 TYR 
                 CE2 
                 47.192 
                 46.359 
                 35.812 
                 34.13 
               
               
                 138 
                 TYR 
                 CZ 
                 47.209 
                 45.526 
                 34.700 
                 34.39 
               
               
                 138 
                 TYR 
                 OH 
                 46.129 
                 45.474 
                 33.843 
                 34.66 
               
               
                 138 
                 TYR 
                 C 
                 52.214 
                 44.554 
                 38.924 
                 34.55 
               
               
                 138 
                 TYR 
                 O 
                 52.031 
                 44.643 
                 40.139 
                 34.22 
               
               
                 139 
                 GLY 
                 N 
                 53.411 
                 44.688 
                 38.360 
                 35.47 
               
               
                 139 
                 GLY 
                 CA 
                 54.582 
                 44.949 
                 39.173 
                 36.62 
               
               
                 139 
                 GLY 
                 C 
                 55.701 
                 43.955 
                 38.966 
                 37.31 
               
               
                 139 
                 GLY 
                 O 
                 56.866 
                 44.278 
                 39.201 
                 37.52 
               
               
                 140 
                 GLY 
                 N 
                 55.364 
                 42.753 
                 38.509 
                 38.05 
               
               
                 140 
                 GLY 
                 CA 
                 56.390 
                 41.745 
                 38.301 
                 39.17 
               
               
                 140 
                 GLY 
                 C 
                 56.480 
                 41.123 
                 36.915 
                 39.93 
               
               
                 140 
                 GLY 
                 O 
                 56.986 
                 40.010 
                 36.772 
                 39.75 
               
               
                 141 
                 SER 
                 N 
                 56.005 
                 41.830 
                 35.892 
                 40.71 
               
               
                 141 
                 SER 
                 CA 
                 56.047 
                 41.310 
                 34.521 
                 41.34 
               
               
                 141 
                 SER 
                 CB 
                 54.726 
                 40.612 
                 34.171 
                 41.61 
               
               
                 141 
                 SER 
                 OG 
                 53.644 
                 41.531 
                 34.107 
                 41.68 
               
               
                 141 
                 SER 
                 C 
                 56.315 
                 42.424 
                 33.510 
                 41.80 
               
               
                 141 
                 SER 
                 O 
                 55.864 
                 43.556 
                 33.690 
                 41.68 
               
               
                 142 
                 PRO 
                 N 
                 57.042 
                 42.112 
                 32.418 
                 42.10 
               
               
                 142 
                 PRO 
                 CD 
                 57.531 
                 43.131 
                 31.468 
                 42.24 
               
               
                 142 
                 PRO 
                 CA 
                 57.606 
                 40.797 
                 32.089 
                 42.58 
               
               
                 142 
                 PRO 
                 CB 
                 58.156 
                 41.011 
                 30.681 
                 42.47 
               
               
                 142 
                 PRO 
                 CG 
                 58.675 
                 42.413 
                 30.770 
                 42.16 
               
               
                 142 
                 PRO 
                 C 
                 58.695 
                 40.313 
                 33.053 
                 42.97 
               
               
                 142 
                 PRO 
                 O 
                 59.102 
                 39.148 
                 33.000 
                 43.23 
               
               
                 143 
                 ARG 
                 N 
                 59.167 
                 41.204 
                 33.922 
                 43.15 
               
               
                 143 
                 ARG 
                 CA 
                 60.210 
                 40.849 
                 34.876 
                 43.34 
               
               
                 143 
                 ARG 
                 CB 
                 61.586 
                 41.240 
                 34.315 
                 43.34 
               
               
                 143 
                 ARG 
                 C 
                 59.975 
                 41.523 
                 36.230 
                 43.27 
               
               
                 143 
                 ARG 
                 O 
                 59.069 
                 42.353 
                 36.380 
                 43.08 
               
               
                 144 
                 ALA 
                 N 
                 60.792 
                 41.161 
                 37.217 
                 43.16 
               
               
                 144 
                 ALA 
                 CA 
                 60.658 
                 41.746 
                 38.540 
                 43.21 
               
               
                 144 
                 ALA 
                 CB 
                 61.685 
                 41.136 
                 39.500 
                 43.24 
               
               
                 144 
                 ALA 
                 C 
                 60.846 
                 43.258 
                 38.457 
                 43.31 
               
               
                 144 
                 ALA 
                 O 
                 61.550 
                 43.759 
                 37.578 
                 43.14 
               
               
                 145 
                 ASN 
                 N 
                 60.197 
                 43.968 
                 39.377 
                 43.45 
               
               
                 145 
                 ASN 
                 CA 
                 60.261 
                 45.422 
                 39.472 
                 43.71 
               
               
                 145 
                 ASN 
                 CB 
                 61.657 
                 45.857 
                 39.936 
                 43.64 
               
               
                 145 
                 ASN 
                 CG 
                 62.076 
                 45.183 
                 41.237 
                 43.64 
               
               
                 145 
                 ASN 
                 OD1 
                 62.790 
                 44.185 
                 41.227 
                 43.65 
               
               
                 145 
                 ASN 
                 ND2 
                 61.616 
                 45.720 
                 42.359 
                 43.62 
               
               
                 145 
                 ASN 
                 C 
                 59.892 
                 46.151 
                 38.183 
                 43.96 
               
               
                 145 
                 ASN 
                 O 
                 60.412 
                 47.228 
                 37.904 
                 44.11 
               
               
                 146 
                 SER 
                 N 
                 58.986 
                 45.568 
                 37.406 
                 44.30 
               
               
                 146 
                 SER 
                 CA 
                 58.561 
                 46.178 
                 36.149 
                 44.53 
               
               
                 146 
                 SER 
                 CB 
                 58.053 
                 45.095 
                 35.194 
                 44.90 
               
               
                 146 
                 SER 
                 OG 
                 57.994 
                 45.580 
                 33.861 
                 45.57 
               
               
                 146 
                 SER 
                 C 
                 57.468 
                 47.231 
                 36.390 
                 44.52 
               
               
                 146 
                 SER 
                 O 
                 57.213 
                 47.616 
                 37.536 
                 44.02 
               
               
                 147 
                 HIS 
                 N 
                 56.838 
                 47.693 
                 35.306 
                 44.59 
               
               
                 147 
                 HIS 
                 CA 
                 55.772 
                 48.698 
                 35.377 
                 44.76 
               
               
                 147 
                 HIS 
                 CB 
                 55.110 
                 48.913 
                 34.014 
                 45.09 
               
               
                 147 
                 HIS 
                 CG 
                 56.026 
                 49.448 
                 32.966 
                 45.61 
               
               
                 147 
                 HIS 
                 CD2 
                 56.441 
                 50.712 
                 32.701 
                 45.76 
               
               
                 147 
                 HIS 
                 ND1 
                 56.620 
                 48.642 
                 32.022 
                 45.97 
               
               
                 147 
                 HIS 
                 CE1 
                 57.360 
                 49.383 
                 31.216 
                 46.05 
               
               
                 147 
                 HIS 
                 NE2 
                 57.266 
                 50.642 
                 31.607 
                 45.97 
               
               
                 147 
                 HIS 
                 C 
                 54.667 
                 48.317 
                 36.349 
                 44.59 
               
               
                 147 
                 HIS 
                 O 
                 54.346 
                 47.137 
                 36.509 
                 44.78 
               
               
                 148 
                 GLY 
                 N 
                 54.072 
                 49.323 
                 36.978 
                 44.20 
               
               
                 148 
                 GLY 
                 CA 
                 52.992 
                 49.056 
                 37.905 
                 43.92 
               
               
                 148 
                 GLY 
                 C 
                 53.439 
                 48.668 
                 39.297 
                 43.71 
               
               
                 148 
                 GLY 
                 O 
                 54.623 
                 48.746 
                 39.643 
                 43.63 
               
               
                 149 
                 GLY 
                 N 
                 52.481 
                 48.226 
                 40.101 
                 43.39 
               
               
                 149 
                 GLY 
                 CA 
                 52.798 
                 47.862 
                 41.461 
                 43.23 
               
               
                 149 
                 GLY 
                 C 
                 52.524 
                 49.052 
                 42.354 
                 43.19 
               
               
                 149 
                 GLY 
                 O 
                 51.878 
                 50.010 
                 41.938 
                 42.72 
               
               
                 150 
                 VAL 
                 N 
                 53.028 
                 48.994 
                 43.576 
                 43.52 
               
               
                 150 
                 VAL 
                 CA 
                 52.813 
                 50.047 
                 44.557 
                 44.13 
               
               
                 150 
                 VAL 
                 CB 
                 53.640 
                 49.776 
                 45.836 
                 43.94 
               
               
                 150 
                 VAL 
                 CG1 
                 53.225 
                 48.426 
                 46.429 
                 43.80 
               
               
                 150 
                 VAL 
                 CG2 
                 55.142 
                 49.794 
                 45.512 
                 43.74 
               
               
                 150 
                 VAL 
                 C 
                 53.109 
                 51.464 
                 44.072 
                 44.80 
               
               
                 150 
                 VAL 
                 O 
                 53.981 
                 51.685 
                 43.233 
                 44.70 
               
               
                 151 
                 CYS 
                 N 
                 52.360 
                 52.416 
                 44.621 
                 45.70 
               
               
                 151 
                 CYS 
                 CA 
                 52.490 
                 53.833 
                 44.301 
                 46.52 
               
               
                 151 
                 CYS 
                 C 
                 51.926 
                 54.161 
                 42.928 
                 46.62 
               
               
                 151 
                 CYS 
                 O 
                 52.421 
                 53.688 
                 41.910 
                 46.64 
               
               
                 151 
                 CYS 
                 CB 
                 53.952 
                 54.272 
                 44.383 
                 47.29 
               
               
                 151 
                 CYS 
                 SG 
                 54.701 
                 54.094 
                 46.035 
                 48.62 
               
               
                 152 
                 PRO 
                 N 
                 50.881 
                 54.996 
                 42.885 
                 46.88 
               
               
                 152 
                 PRO 
                 CD 
                 50.302 
                 55.789 
                 43.988 
                 46.91 
               
               
                 152 
                 PRO 
                 CA 
                 50.275 
                 55.360 
                 41.608 
                 47.02 
               
               
                 152 
                 PRO 
                 CB 
                 49.057 
                 56.178 
                 42.030 
                 47.05 
               
               
                 152 
                 PRO 
                 CG 
                 49.553 
                 56.888 
                 43.248 
                 46.98 
               
               
                 152 
                 PRO 
                 C 
                 51.227 
                 56.152 
                 40.715 
                 47.22 
               
               
                 152 
                 PRO 
                 O 
                 51.923 
                 57.058 
                 41.170 
                 47.34 
               
               
                 153 
                 LYS 
                 N 
                 51.271 
                 55.768 
                 39.449 
                 47.40 
               
               
                 153 
                 LYS 
                 CA 
                 52.083 
                 56.441 
                 38.445 
                 47.63 
               
               
                 153 
                 LYS 
                 CB 
                 53.417 
                 55.730 
                 38.211 
                 48.04 
               
               
                 153 
                 LYS 
                 CG 
                 54.161 
                 56.286 
                 36.997 
                 48.80 
               
               
                 153 
                 LYS 
                 CD 
                 55.514 
                 55.622 
                 36.766 
                 49.22 
               
               
                 153 
                 LYS 
                 CE 
                 56.049 
                 55.963 
                 35.379 
                 49.72 
               
               
                 153 
                 LYS 
                 NZ 
                 56.112 
                 57.435 
                 35.118 
                 49.77 
               
               
                 153 
                 LYS 
                 C 
                 51.225 
                 56.360 
                 37.199 
                 47.58 
               
               
                 153 
                 LYS 
                 O 
                 50.798 
                 55.275 
                 36.804 
                 47.34 
               
               
                 154 
                 ALA 
                 N 
                 50.955 
                 57.506 
                 36.588 
                 47.43 
               
               
                 154 
                 ALA 
                 CA 
                 50.107 
                 57.533 
                 35.411 
                 47.58 
               
               
                 154 
                 ALA 
                 CB 
                 49.631 
                 58.970 
                 35.148 
                 47.52 
               
               
                 154 
                 ALA 
                 C 
                 50.751 
                 56.959 
                 34.156 
                 47.66 
               
               
                 154 
                 ALA 
                 O 
                 51.945 
                 57.135 
                 33.912 
                 47.36 
               
               
                 155 
                 TYR 
                 N 
                 49.935 
                 56.245 
                 33.385 
                 47.93 
               
               
                 155 
                 TYR 
                 CA 
                 50.332 
                 55.663 
                 32.108 
                 48.40 
               
               
                 155 
                 TYR 
                 CB 
                 50.496 
                 54.145 
                 32.178 
                 48.59 
               
               
                 155 
                 TYR 
                 CG 
                 51.659 
                 53.666 
                 33.007 
                 48.89 
               
               
                 155 
                 TYR 
                 CD1 
                 51.577 
                 53.627 
                 34.396 
                 49.04 
               
               
                 155 
                 TYR 
                 CE1 
                 52.648 
                 53.180 
                 35.172 
                 49.22 
               
               
                 155 
                 TYR 
                 CD2 
                 52.846 
                 53.246 
                 32.400 
                 49.00 
               
               
                 155 
                 TYR 
                 CE2 
                 53.923 
                 52.797 
                 33.166 
                 49.11 
               
               
                 155 
                 TYR 
                 CZ 
                 53.815 
                 52.765 
                 34.553 
                 49.11 
               
               
                 155 
                 TYR 
                 OH 
                 54.867 
                 52.313 
                 35.317 
                 48.98 
               
               
                 155 
                 TYR 
                 C 
                 49.156 
                 55.981 
                 31.201 
                 48.65 
               
               
                 155 
                 TYR 
                 O 
                 48.020 
                 55.591 
                 31.489 
                 48.52 
               
               
                 156 
                 TYR 
                 N 
                 49.422 
                 56.695 
                 30.115 
                 48.94 
               
               
                 156 
                 TYR 
                 CA 
                 48.362 
                 57.068 
                 29.196 
                 49.32 
               
               
                 156 
                 TYR 
                 CB 
                 48.830 
                 58.192 
                 28.261 
                 49.84 
               
               
                 156 
                 TYR 
                 CG 
                 47.712 
                 58.733 
                 27.392 
                 50.40 
               
               
                 156 
                 TYR 
                 CD1 
                 46.759 
                 59.608 
                 27.915 
                 50.55 
               
               
                 156 
                 TYR 
                 CE1 
                 45.697 
                 60.059 
                 27.141 
                 50.83 
               
               
                 156 
                 TYR 
                 CD2 
                 47.573 
                 58.322 
                 26.064 
                 50.63 
               
               
                 156 
                 TYR 
                 CE2 
                 46.511 
                 58.763 
                 25.283 
                 50.88 
               
               
                 156 
                 TYR 
                 CZ 
                 45.579 
                 59.629 
                 25.827 
                 50.96 
               
               
                 156 
                 TYR 
                 OH 
                 44.519 
                 60.052 
                 25.059 
                 51.42 
               
               
                 156 
                 TYR 
                 C 
                 47.886 
                 55.884 
                 28.368 
                 49.30 
               
               
                 156 
                 TYR 
                 O 
                 48.671 
                 55.239 
                 27.673 
                 49.46 
               
               
                 157 
                 SER 
                 N 
                 46.595 
                 55.595 
                 28.453 
                 49.12 
               
               
                 157 
                 SER 
                 CA 
                 46.010 
                 54.509 
                 27.688 
                 49.10 
               
               
                 157 
                 SER 
                 CB 
                 44.894 
                 53.839 
                 28.489 
                 48.89 
               
               
                 157 
                 SER 
                 OG 
                 44.305 
                 52.779 
                 27.759 
                 48.59 
               
               
                 157 
                 SER 
                 C 
                 45.448 
                 55.103 
                 26.395 
                 49.27 
               
               
                 157 
                 SER 
                 O 
                 44.431 
                 55.794 
                 26.412 
                 49.40 
               
               
                 158 
                 PRO 
                 N 
                 46.126 
                 54.865 
                 25.259 
                 49.31 
               
               
                 158 
                 PRO 
                 CD 
                 47.451 
                 54.230 
                 25.138 
                 49.24 
               
               
                 158 
                 PRO 
                 CA 
                 45.680 
                 55.382 
                 23.959 
                 49.35 
               
               
                 158 
                 PRO 
                 CB 
                 46.646 
                 54.721 
                 22.986 
                 49.33 
               
               
                 158 
                 PRO 
                 CG 
                 47.923 
                 54.721 
                 23.781 
                 49.38 
               
               
                 158 
                 PRO 
                 C 
                 44.225 
                 55.043 
                 23.668 
                 49.29 
               
               
                 158 
                 PRO 
                 O 
                 43.462 
                 55.901 
                 23.228 
                 49.38 
               
               
                 159 
                 VAL 
                 N 
                 43.841 
                 53.796 
                 23.918 
                 49.12 
               
               
                 159 
                 VAL 
                 CA 
                 42.464 
                 53.380 
                 23.693 
                 49.15 
               
               
                 159 
                 VAL 
                 CB 
                 42.311 
                 51.848 
                 23.780 
                 49.15 
               
               
                 159 
                 VAL 
                 CG1 
                 40.836 
                 51.468 
                 23.636 
                 49.23 
               
               
                 159 
                 VAL 
                 CG2 
                 43.119 
                 51.183 
                 22.673 
                 49.17 
               
               
                 159 
                 VAL 
                 C 
                 41.543 
                 54.018 
                 24.736 
                 49.15 
               
               
                 159 
                 VAL 
                 O 
                 40.398 
                 54.357 
                 24.445 
                 49.18 
               
               
                 160 
                 GLY 
                 N 
                 42.049 
                 54.178 
                 25.953 
                 49.05 
               
               
                 160 
                 GLY 
                 CA 
                 41.242 
                 54.771 
                 27.005 
                 48.98 
               
               
                 160 
                 GLY 
                 C 
                 41.118 
                 56.279 
                 26.901 
                 48.70 
               
               
                 160 
                 GLY 
                 O 
                 40.251 
                 56.880 
                 27.537 
                 48.86 
               
               
                 161 
                 LYS 
                 N 
                 41.979 
                 56.887 
                 26.094 
                 48.39 
               
               
                 161 
                 LYS 
                 CA 
                 41.984 
                 58.331 
                 25.914 
                 48.06 
               
               
                 161 
                 LYS 
                 CB 
                 40.707 
                 58.782 
                 25.197 
                 48.57 
               
               
                 161 
                 LYS 
                 CG 
                 40.574 
                 58.210 
                 23.792 
                 49.22 
               
               
                 161 
                 LYS 
                 CD 
                 39.228 
                 58.548 
                 23.165 
                 49.84 
               
               
                 161 
                 LYS 
                 CE 
                 39.116 
                 57.933 
                 21.776 
                 50.37 
               
               
                 161 
                 LYS 
                 NZ 
                 37.765 
                 58.122 
                 21.153 
                 50.81 
               
               
                 161 
                 LYS 
                 C 
                 42.113 
                 59.041 
                 27.252 
                 47.59 
               
               
                 161 
                 LYS 
                 O 
                 41.632 
                 60.163 
                 27.417 
                 47.67 
               
               
                 162 
                 LYS 
                 N 
                 42.763 
                 58.384 
                 28.210 
                 46.75 
               
               
                 162 
                 LYS 
                 CA 
                 42.962 
                 58.973 
                 29.531 
                 46.11 
               
               
                 162 
                 LYS 
                 CB 
                 41.665 
                 58.937 
                 30.349 
                 46.11 
               
               
                 162 
                 LYS 
                 CG 
                 41.400 
                 57.609 
                 31.058 
                 46.38 
               
               
                 162 
                 LYS 
                 CD 
                 40.277 
                 57.753 
                 32.073 
                 46.41 
               
               
                 162 
                 LYS 
                 CE 
                 40.057 
                 56.480 
                 32.873 
                 46.71 
               
               
                 162 
                 LYS 
                 NZ 
                 38.867 
                 56.602 
                 33.778 
                 46.17 
               
               
                 162 
                 LYS 
                 C 
                 44.042 
                 58.230 
                 30.300 
                 45.48 
               
               
                 162 
                 LYS 
                 O 
                 44.426 
                 57.128 
                 29.929 
                 45.34 
               
               
                 163 
                 ASN 
                 N 
                 44.533 
                 58.839 
                 31.371 
                 44.81 
               
               
                 163 
                 ASN 
                 CA 
                 45.544 
                 58.185 
                 32.184 
                 44.41 
               
               
                 163 
                 ASN 
                 CB 
                 46.232 
                 59.171 
                 33.120 
                 44.52 
               
               
                 163 
                 ASN 
                 CG 
                 47.001 
                 60.220 
                 32.380 
                 44.76 
               
               
                 163 
                 ASN 
                 OD1 
                 47.576 
                 59.951 
                 31.328 
                 45.24 
               
               
                 163 
                 ASN 
                 ND2 
                 47.032 
                 61.425 
                 32.926 
                 44.78 
               
               
                 163 
                 ASN 
                 C 
                 44.912 
                 57.090 
                 33.022 
                 43.96 
               
               
                 163 
                 ASN 
                 O 
                 43.740 
                 57.160 
                 33.399 
                 43.97 
               
               
                 164 
                 ILE 
                 N 
                 45.702 
                 56.066 
                 33.299 
                 43.24 
               
               
                 164 
                 ILE 
                 CA 
                 45.249 
                 54.961 
                 34.114 
                 42.52 
               
               
                 164 
                 ILE 
                 CB 
                 44.841 
                 53.761 
                 33.239 
                 42.41 
               
               
                 164 
                 ILE 
                 CG2 
                 43.707 
                 54.206 
                 32.318 
                 42.46 
               
               
                 164 
                 ILE 
                 CG1 
                 46.040 
                 53.223 
                 32.447 
                 42.23 
               
               
                 164 
                 ILE 
                 CD1 
                 46.908 
                 52.260 
                 33.246 
                 41.87 
               
               
                 164 
                 ILE 
                 C 
                 46.433 
                 54.627 
                 34.999 
                 42.09 
               
               
                 164 
                 ILE 
                 O 
                 47.530 
                 55.157 
                 34.794 
                 41.98 
               
               
                 165 
                 TYR 
                 N 
                 46.216 
                 53.777 
                 35.993 
                 41.37 
               
               
                 165 
                 TYR 
                 CA 
                 47.300 
                 53.410 
                 36.881 
                 40.63 
               
               
                 165 
                 TYR 
                 CB 
                 47.073 
                 54.025 
                 38.268 
                 41.16 
               
               
                 165 
                 TYR 
                 CG 
                 46.943 
                 55.538 
                 38.225 
                 41.76 
               
               
                 165 
                 TYR 
                 CD1 
                 45.740 
                 56.145 
                 37.852 
                 42.03 
               
               
                 165 
                 TYR 
                 CE1 
                 45.632 
                 57.531 
                 37.738 
                 42.27 
               
               
                 165 
                 TYR 
                 CD2 
                 48.040 
                 56.361 
                 38.488 
                 41.97 
               
               
                 165 
                 TYR 
                 CE2 
                 47.946 
                 57.754 
                 38.373 
                 42.23 
               
               
                 165 
                 TYR 
                 CZ 
                 46.735 
                 58.328 
                 37.995 
                 42.58 
               
               
                 165 
                 TYR 
                 OH 
                 46.628 
                 59.693 
                 37.847 
                 42.79 
               
               
                 165 
                 TYR 
                 C 
                 47.439 
                 51.896 
                 36.943 
                 39.77 
               
               
                 165 
                 TYR 
                 O 
                 46.458 
                 51.157 
                 36.790 
                 39.50 
               
               
                 166 
                 LEU 
                 N 
                 48.671 
                 51.442 
                 37.143 
                 38.73 
               
               
                 166 
                 LEU 
                 CA 
                 48.959 
                 50.015 
                 37.202 
                 37.71 
               
               
                 166 
                 LEU 
                 CB 
                 50.128 
                 49.689 
                 36.266 
                 37.45 
               
               
                 166 
                 LEU 
                 CG 
                 49.830 
                 50.047 
                 34.805 
                 37.43 
               
               
                 166 
                 LEU 
                 CD1 
                 51.057 
                 49.796 
                 33.921 
                 37.38 
               
               
                 166 
                 LEU 
                 CD2 
                 48.640 
                 49.243 
                 34.283 
                 37.14 
               
               
                 166 
                 LEU 
                 C 
                 49.286 
                 49.560 
                 38.621 
                 37.06 
               
               
                 166 
                 LEU 
                 O 
                 49.983 
                 48.566 
                 38.819 
                 36.54 
               
               
                 167 
                 ASN 
                 N 
                 48.799 
                 50.312 
                 39.604 
                 36.57 
               
               
                 167 
                 ASN 
                 CA 
                 49.013 
                 49.979 
                 41.005 
                 36.02 
               
               
                 167 
                 ASN 
                 CB 
                 49.129 
                 51.264 
                 41.835 
                 35.90 
               
               
                 167 
                 ASN 
                 CG 
                 47.866 
                 52.122 
                 41.782 
                 35.90 
               
               
                 167 
                 ASN 
                 OD1 
                 47.078 
                 52.047 
                 40.835 
                 35.38 
               
               
                 167 
                 ASN 
                 ND2 
                 47.682 
                 52.952 
                 42.800 
                 35.49 
               
               
                 167 
                 ASN 
                 C 
                 47.783 
                 49.171 
                 41.411 
                 35.89 
               
               
                 167 
                 ASN 
                 O 
                 47.042 
                 49.547 
                 42.314 
                 35.95 
               
               
                 168 
                 SER 
                 N 
                 47.582 
                 48.042 
                 40.742 
                 35.61 
               
               
                 168 
                 SER 
                 CA 
                 46.409 
                 47.231 
                 41.009 
                 35.49 
               
               
                 168 
                 SER 
                 CB 
                 45.273 
                 47.715 
                 40.124 
                 35.83 
               
               
                 168 
                 SER 
                 OG 
                 45.729 
                 47.807 
                 38.786 
                 36.17 
               
               
                 168 
                 SER 
                 C 
                 46.563 
                 45.736 
                 40.813 
                 35.19 
               
               
                 168 
                 SER 
                 O 
                 47.544 
                 45.248 
                 40.247 
                 34.75 
               
               
                 169 
                 GLY 
                 N 
                 45.548 
                 45.023 
                 41.285 
                 34.71 
               
               
                 169 
                 GLY 
                 CA 
                 45.515 
                 43.584 
                 41.179 
                 34.72 
               
               
                 169 
                 GLY 
                 C 
                 44.141 
                 43.073 
                 41.582 
                 34.64 
               
               
                 169 
                 GLY 
                 O 
                 43.335 
                 43.816 
                 42.145 
                 34.48 
               
               
                 170 
                 LEU 
                 N 
                 43.855 
                 41.814 
                 41.281 
                 34.68 
               
               
                 170 
                 LEU 
                 CA 
                 42.561 
                 41.251 
                 41.645 
                 34.73 
               
               
                 170 
                 LEU 
                 CB 
                 41.607 
                 41.284 
                 40.439 
                 34.66 
               
               
                 170 
                 LEU 
                 CG 
                 42.086 
                 40.441 
                 39.249 
                 34.68 
               
               
                 170 
                 LEU 
                 CD1 
                 41.551 
                 39.014 
                 39.336 
                 34.63 
               
               
                 170 
                 LEU 
                 CD2 
                 41.609 
                 41.063 
                 37.932 
                 35.09 
               
               
                 170 
                 LEU 
                 C 
                 42.673 
                 39.833 
                 42.189 
                 34.65 
               
               
                 170 
                 LEU 
                 O 
                 43.635 
                 39.103 
                 41.916 
                 34.21 
               
               
                 171 
                 THR 
                 N 
                 41.668 
                 39.460 
                 42.969 
                 34.78 
               
               
                 171 
                 THR 
                 CA 
                 41.590 
                 38.147 
                 43.579 
                 35.11 
               
               
                 171 
                 THR 
                 CB 
                 41.803 
                 38.211 
                 45.115 
                 34.88 
               
               
                 171 
                 THR 
                 OG1 
                 43.161 
                 38.556 
                 45.414 
                 34.61 
               
               
                 171 
                 THR 
                 CG2 
                 41.444 
                 36.868 
                 45.755 
                 34.57 
               
               
                 171 
                 THR 
                 C 
                 40.192 
                 37.606 
                 43.344 
                 35.57 
               
               
                 171 
                 THR 
                 O 
                 39.211 
                 38.342 
                 43.444 
                 35.84 
               
               
                 172 
                 SER 
                 N 
                 40.101 
                 36.323 
                 43.023 
                 36.15 
               
               
                 172 
                 SER 
                 CA 
                 38.806 
                 35.684 
                 42.821 
                 36.77 
               
               
                 172 
                 SER 
                 CB 
                 38.679 
                 35.115 
                 41.405 
                 36.76 
               
               
                 172 
                 SER 
                 OG 
                 37.490 
                 34.342 
                 41.298 
                 36.64 
               
               
                 172 
                 SER 
                 C 
                 38.729 
                 34.548 
                 43.827 
                 37.20 
               
               
                 172 
                 SER 
                 O 
                 39.711 
                 33.830 
                 44.031 
                 37.07 
               
               
                 173 
                 THR 
                 N 
                 37.578 
                 34.390 
                 44.471 
                 37.77 
               
               
                 173 
                 THR 
                 CA 
                 37.430 
                 33.325 
                 45.448 
                 38.35 
               
               
                 173 
                 THR 
                 CB 
                 36.824 
                 33.867 
                 46.756 
                 38.23 
               
               
                 173 
                 THR 
                 OG1 
                 35.577 
                 34.511 
                 46.480 
                 37.93 
               
               
                 173 
                 THR 
                 CG2 
                 37.787 
                 34.877 
                 47.396 
                 37.78 
               
               
                 173 
                 THR 
                 C 
                 36.581 
                 32.165 
                 44.915 
                 39.17 
               
               
                 173 
                 THR 
                 O 
                 36.047 
                 31.363 
                 45.689 
                 38.97 
               
               
                 174 
                 LYS 
                 N 
                 36.463 
                 32.082 
                 43.590 
                 39.81 
               
               
                 174 
                 LYS 
                 CA 
                 35.717 
                 31.006 
                 42.948 
                 40.76 
               
               
                 174 
                 LYS 
                 CB 
                 34.533 
                 31.558 
                 42.149 
                 40.83 
               
               
                 174 
                 LYS 
                 CG 
                 33.657 
                 30.477 
                 41.497 
                 41.18 
               
               
                 174 
                 LYS 
                 CD 
                 32.508 
                 31.079 
                 40.709 
                 41.38 
               
               
                 174 
                 LYS 
                 CE 
                 31.724 
                 30.009 
                 39.943 
                 41.88 
               
               
                 174 
                 LYS 
                 NZ 
                 30.543 
                 30.600 
                 39.218 
                 42.08 
               
               
                 174 
                 LYS 
                 C 
                 36.664 
                 30.275 
                 42.006 
                 41.39 
               
               
                 174 
                 LYS 
                 O 
                 37.503 
                 30.896 
                 41.359 
                 41.31 
               
               
                 175 
                 ASN 
                 N 
                 36.530 
                 28.957 
                 41.932 
                 42.11 
               
               
                 175 
                 ASN 
                 CA 
                 37.382 
                 28.158 
                 41.059 
                 42.96 
               
               
                 175 
                 ASN 
                 CB 
                 38.770 
                 27.983 
                 41.691 
                 42.77 
               
               
                 175 
                 ASN 
                 CG 
                 39.808 
                 27.479 
                 40.698 
                 42.84 
               
               
                 175 
                 ASN 
                 OD1 
                 39.721 
                 27.752 
                 39.501 
                 42.69 
               
               
                 175 
                 ASN 
                 ND2 
                 40.808 
                 26.759 
                 41.198 
                 42.67 
               
               
                 175 
                 ASN 
                 C 
                 36.711 
                 26.807 
                 40.848 
                 43.46 
               
               
                 175 
                 ASN 
                 O 
                 36.223 
                 26.195 
                 41.801 
                 43.65 
               
               
                 176 
                 TYR 
                 N 
                 36.685 
                 26.353 
                 39.595 
                 44.06 
               
               
                 176 
                 TYR 
                 CA 
                 36.055 
                 25.083 
                 39.245 
                 44.41 
               
               
                 176 
                 TYR 
                 CB 
                 36.945 
                 23.909 
                 39.676 
                 45.08 
               
               
                 176 
                 TYR 
                 CG 
                 38.335 
                 23.920 
                 39.054 
                 45.89 
               
               
                 176 
                 TYR 
                 CD1 
                 38.525 
                 23.666 
                 37.688 
                 46.26 
               
               
                 176 
                 TYR 
                 CE1 
                 39.810 
                 23.693 
                 37.120 
                 46.51 
               
               
                 176 
                 TYR 
                 CD2 
                 39.459 
                 24.199 
                 39.830 
                 46.18 
               
               
                 176 
                 TYR 
                 CE2 
                 40.736 
                 24.229 
                 39.270 
                 46.46 
               
               
                 176 
                 TYR 
                 CZ 
                 40.903 
                 23.978 
                 37.923 
                 46.52 
               
               
                 176 
                 TYR 
                 OH 
                 42.169 
                 24.035 
                 37.392 
                 47.33 
               
               
                 176 
                 TYR 
                 C 
                 34.678 
                 25.000 
                 39.914 
                 44.40 
               
               
                 176 
                 TYR 
                 O 
                 34.361 
                 24.045 
                 40.626 
                 44.47 
               
               
                 177 
                 GLY 
                 N 
                 33.884 
                 26.045 
                 39.704 
                 44.31 
               
               
                 177 
                 GLY 
                 CA 
                 32.536 
                 26.102 
                 40.244 
                 43.91 
               
               
                 177 
                 GLY 
                 C 
                 32.340 
                 26.213 
                 41.750 
                 43.76 
               
               
                 177 
                 GLY 
                 O 
                 31.208 
                 26.389 
                 42.206 
                 43.81 
               
               
                 178 
                 LYS 
                 N 
                 33.415 
                 26.122 
                 42.526 
                 43.32 
               
               
                 178 
                 LYS 
                 CA 
                 33.296 
                 26.194 
                 43.987 
                 42.94 
               
               
                 178 
                 LYS 
                 CB 
                 33.913 
                 24.934 
                 44.617 
                 43.40 
               
               
                 178 
                 LYS 
                 CG 
                 33.138 
                 23.658 
                 44.317 
                 44.05 
               
               
                 178 
                 LYS 
                 CD 
                 33.875 
                 22.393 
                 44.750 
                 44.34 
               
               
                 178 
                 LYS 
                 CE 
                 33.049 
                 21.157 
                 44.389 
                 44.84 
               
               
                 178 
                 LYS 
                 NZ 
                 33.794 
                 19.866 
                 44.501 
                 45.03 
               
               
                 178 
                 LYS 
                 C 
                 33.940 
                 27.427 
                 44.614 
                 42.19 
               
               
                 178 
                 LYS 
                 O 
                 34.745 
                 28.114 
                 43.985 
                 42.28 
               
               
                 179 
                 THR 
                 N 
                 33.548 
                 27.719 
                 45.850 
                 41.39 
               
               
                 179 
                 THR 
                 CA 
                 34.142 
                 28.824 
                 46.584 
                 40.46 
               
               
                 179 
                 THR 
                 CB 
                 33.265 
                 29.251 
                 47.765 
                 40.32 
               
               
                 179 
                 THR 
                 OG1 
                 32.033 
                 29.780 
                 47.269 
                 40.47 
               
               
                 179 
                 THR 
                 CG2 
                 33.972 
                 30.317 
                 48.605 
                 40.08 
               
               
                 179 
                 THR 
                 C 
                 35.431 
                 28.203 
                 47.113 
                 39.85 
               
               
                 179 
                 THR 
                 O 
                 35.396 
                 27.107 
                 47.666 
                 39.95 
               
               
                 180 
                 ILE 
                 N 
                 36.563 
                 28.877 
                 46.929 
                 38.94 
               
               
                 180 
                 ILE 
                 CA 
                 37.839 
                 28.327 
                 47.385 
                 38.10 
               
               
                 180 
                 ILE 
                 CB 
                 39.037 
                 29.046 
                 46.706 
                 37.98 
               
               
                 180 
                 ILE 
                 CG2 
                 38.852 
                 28.980 
                 45.187 
                 37.87 
               
               
                 180 
                 ILE 
                 CG1 
                 39.152 
                 30.489 
                 47.215 
                 37.90 
               
               
                 180 
                 ILE 
                 CD1 
                 40.253 
                 31.299 
                 46.509 
                 37.67 
               
               
                 180 
                 ILE 
                 C 
                 37.952 
                 28.479 
                 48.893 
                 37.44 
               
               
                 180 
                 ILE 
                 O 
                 37.200 
                 29.230 
                 49.495 
                 37.34 
               
               
                 181 
                 LEU 
                 N 
                 38.889 
                 27.763 
                 49.496 
                 36.91 
               
               
                 181 
                 LEU 
                 CA 
                 39.090 
                 27.836 
                 50.940 
                 36.32 
               
               
                 181 
                 LEU 
                 CB 
                 40.127 
                 26.792 
                 51.373 
                 36.29 
               
               
                 181 
                 LEU 
                 CG 
                 39.647 
                 25.347 
                 51.160 
                 36.15 
               
               
                 181 
                 LEU 
                 CD1 
                 40.729 
                 24.351 
                 51.572 
                 36.24 
               
               
                 181 
                 LEU 
                 CD2 
                 38.370 
                 25.075 
                 51.970 
                 36.93 
               
               
                 181 
                 LEU 
                 C 
                 39.559 
                 29.236 
                 51.333 
                 35.93 
               
               
                 181 
                 LEU 
                 O 
                 40.141 
                 29.951 
                 50.519 
                 35.92 
               
               
                 182 
                 THR 
                 N 
                 39.287 
                 29.636 
                 52.572 
                 35.30 
               
               
                 182 
                 THR 
                 CA 
                 39.719 
                 30.939 
                 53.054 
                 34.71 
               
               
                 182 
                 THR 
                 CB 
                 39.209 
                 31.195 
                 54.488 
                 35.13 
               
               
                 182 
                 THR 
                 OG1 
                 37.778 
                 31.307 
                 54.471 
                 35.39 
               
               
                 182 
                 THR 
                 CG2 
                 39.823 
                 32.483 
                 55.047 
                 35.65 
               
               
                 182 
                 THR 
                 C 
                 41.255 
                 90.998 
                 53.045 
                 34.02 
               
               
                 182 
                 THR 
                 O 
                 41.846 
                 32.004 
                 52.650 
                 33.73 
               
               
                 183 
                 LYS 
                 N 
                 41.899 
                 29.917 
                 53.472 
                 33.23 
               
               
                 183 
                 LYS 
                 CA 
                 43.353 
                 29.876 
                 53.497 
                 32.54 
               
               
                 183 
                 LYS 
                 CB 
                 43.843 
                 28.583 
                 54.154 
                 32.61 
               
               
                 183 
                 LYS 
                 CG 
                 43.545 
                 27.315 
                 53.371 
                 32.68 
               
               
                 183 
                 LYS 
                 CD 
                 44.198 
                 26.114 
                 54.023 
                 32.79 
               
               
                 183 
                 LYS 
                 CE 
                 44.147 
                 24.900 
                 53.111 
                 33.20 
               
               
                 183 
                 LYS 
                 NZ 
                 44.906 
                 23.737 
                 53.680 
                 33.32 
               
               
                 183 
                 LYS 
                 C 
                 43.948 
                 30.004 
                 52.089 
                 32.34 
               
               
                 183 
                 LYS 
                 O 
                 45.078 
                 30.476 
                 51.936 
                 31.99 
               
               
                 184 
                 GLU 
                 N 
                 43.198 
                 29.574 
                 51.071 
                 31.88 
               
               
                 184 
                 GLU 
                 CA 
                 43.667 
                 29.676 
                 49.682 
                 31.79 
               
               
                 184 
                 GLU 
                 CB 
                 42.859 
                 28.751 
                 48.753 
                 32.16 
               
               
                 184 
                 GLU 
                 CG 
                 42.872 
                 27.283 
                 49.166 
                 32.95 
               
               
                 184 
                 GLU 
                 CD 
                 41.977 
                 26.407 
                 48.287 
                 33.41 
               
               
                 184 
                 GLU 
                 OE1 
                 40.936 
                 26.893 
                 47.825 
                 33.91 
               
               
                 184 
                 GLU 
                 OE2 
                 42.315 
                 25.233 
                 48.072 
                 34.31 
               
               
                 184 
                 GLU 
                 C 
                 43.503 
                 31.126 
                 49.239 
                 31.34 
               
               
                 184 
                 GLU 
                 O 
                 44.401 
                 31.701 
                 48.610 
                 31.32 
               
               
                 185 
                 ALA 
                 N 
                 42.368 
                 31.723 
                 49.596 
                 30.75 
               
               
                 185 
                 ALA 
                 CA 
                 42.088 
                 33.121 
                 49.249 
                 30.21 
               
               
                 185 
                 ALA 
                 CB 
                 40.708 
                 33.523 
                 49.772 
                 30.06 
               
               
                 185 
                 ALA 
                 C 
                 43.172 
                 34.045 
                 49.830 
                 29.95 
               
               
                 185 
                 ALA 
                 O 
                 43.603 
                 34.997 
                 49.183 
                 29.57 
               
               
                 186 
                 ASP 
                 N 
                 43.598 
                 33.769 
                 51.062 
                 29.71 
               
               
                 186 
                 ASP 
                 CA 
                 44.654 
                 34.553 
                 51.695 
                 29.29 
               
               
                 186 
                 ASP 
                 CB 
                 44.970 
                 34.007 
                 53.092 
                 29.21 
               
               
                 186 
                 ASP 
                 CG 
                 43.869 
                 34.291 
                 54.106 
                 29.44 
               
               
                 186 
                 ASP 
                 OD1 
                 42.860 
                 34.927 
                 53.751 
                 28.72 
               
               
                 186 
                 ASP 
                 OD2 
                 44.029 
                 33.870 
                 55.268 
                 29.64 
               
               
                 186 
                 ASP 
                 C 
                 45.927 
                 34.477 
                 50.856 
                 29.17 
               
               
                 186 
                 ASP 
                 O 
                 46.666 
                 35.455 
                 50.721 
                 28.88 
               
               
                 187 
                 LEU 
                 N 
                 46.192 
                 33.295 
                 50.316 
                 29.08 
               
               
                 187 
                 LEU 
                 CA 
                 47.386 
                 33.079 
                 49.511 
                 29.71 
               
               
                 187 
                 LEU 
                 CB 
                 47.648 
                 31.564 
                 49.358 
                 30.11 
               
               
                 187 
                 LEU 
                 CG 
                 47.946 
                 30.921 
                 50.728 
                 31.10 
               
               
                 187 
                 LEU 
                 CD1 
                 48.287 
                 29.441 
                 50.587 
                 31.30 
               
               
                 187 
                 LEU 
                 CD2 
                 49.106 
                 31.640 
                 51.419 
                 31.18 
               
               
                 187 
                 LEU 
                 C 
                 47.315 
                 33.783 
                 48.150 
                 29.27 
               
               
                 187 
                 LEU 
                 O 
                 48.301 
                 34.350 
                 47.700 
                 29.26 
               
               
                 188 
                 VAL 
                 N 
                 46.151 
                 33.768 
                 47.512 
                 29.33 
               
               
                 188 
                 VAL 
                 CA 
                 45.991 
                 34.438 
                 46.226 
                 28.96 
               
               
                 188 
                 VAL 
                 CB 
                 44.530 
                 34.290 
                 45.694 
                 29.41 
               
               
                 188 
                 VAL 
                 CG1 
                 44.379 
                 35.028 
                 44.356 
                 29.10 
               
               
                 188 
                 VAL 
                 CG2 
                 44.186 
                 32.805 
                 45.503 
                 29.21 
               
               
                 188 
                 VAL 
                 C 
                 46.321 
                 35.929 
                 46.410 
                 28.70 
               
               
                 188 
                 VAL 
                 O 
                 47.158 
                 36.507 
                 45.697 
                 28.11 
               
               
                 189 
                 TSR 
                 N 
                 45.691 
                 36.537 
                 47.404 
                 27.95 
               
               
                 189 
                 THR 
                 CA 
                 45.910 
                 37.949 
                 47.670 
                 27.87 
               
               
                 189 
                 THR 
                 CB 
                 44.899 
                 38.444 
                 48.725 
                 28.07 
               
               
                 189 
                 THR 
                 OG1 
                 43.580 
                 38.244 
                 48.213 
                 27.14 
               
               
                 189 
                 THR 
                 CG2 
                 45.083 
                 39.940 
                 48.998 
                 27.79 
               
               
                 189 
                 TSR 
                 C 
                 47.349 
                 38.302 
                 48.086 
                 27.47 
               
               
                 189 
                 THR 
                 O 
                 47.881 
                 39.326 
                 47.650 
                 27.36 
               
               
                 190 
                 THR 
                 N 
                 47.971 
                 37.473 
                 48.920 
                 27.06 
               
               
                 190 
                 THR 
                 CA 
                 49.349 
                 37.721 
                 49.356 
                 26.95 
               
               
                 190 
                 THR 
                 CB 
                 49.855 
                 36.607 
                 50.310 
                 26.97 
               
               
                 190 
                 THR 
                 OG1 
                 49.024 
                 36.535 
                 51.472 
                 26.25 
               
               
                 190 
                 THR 
                 CG2 
                 51.306 
                 36.879 
                 50.734 
                 26.12 
               
               
                 190 
                 THR 
                 C 
                 50.251 
                 37.709 
                 48.114 
                 27.31 
               
               
                 190 
                 THR 
                 O 
                 51.143 
                 38.541 
                 47.962 
                 27.08 
               
               
                 191 
                 HIS 
                 N 
                 49.988 
                 36.747 
                 47.234 
                 27.47 
               
               
                 191 
                 HIS 
                 CA 
                 50.740 
                 36.558 
                 45.991 
                 27.77 
               
               
                 191 
                 HIS 
                 CB 
                 50.303 
                 35.248 
                 45.326 
                 27.41 
               
               
                 191 
                 HIS 
                 CG 
                 50.934 
                 34.995 
                 43.990 
                 27.50 
               
               
                 191 
                 HIS 
                 CD2 
                 50.646 
                 35.485 
                 42.755 
                 27.59 
               
               
                 191 
                 HIS 
                 ND1 
                 51.950 
                 34.083 
                 43.810 
                 27.34 
               
               
                 191 
                 HIS 
                 CE1 
                 52.259 
                 74.013 
                 42.525 
                 27.71 
               
               
                 191 
                 HIS 
                 NE2 
                 51.479 
                 34.853 
                 41.865 
                 27.92 
               
               
                 191 
                 HIS 
                 C 
                 50.559 
                 37.717 
                 45.002 
                 27.83 
               
               
                 191 
                 HIS 
                 O 
                 51.530 
                 38.199 
                 44.423 
                 28.20 
               
               
                 192 
                 GLU 
                 N 
                 49.322 
                 38.147 
                 44.790 
                 27.77 
               
               
                 192 
                 GLU 
                 CA 
                 49.086 
                 39.251 
                 43.876 
                 27.96 
               
               
                 192 
                 GLU 
                 CB 
                 47.588 
                 39.432 
                 43.627 
                 28.01 
               
               
                 192 
                 GLU 
                 CG 
                 46.898 
                 38.207 
                 43.019 
                 28.59 
               
               
                 192 
                 GLU 
                 CD 
                 47.664 
                 37.557 
                 41.865 
                 29.60 
               
               
                 192 
                 GLU 
                 OE1 
                 48.456 
                 38.259 
                 41.177 
                 29.97 
               
               
                 192 
                 GLU 
                 OE2 
                 47.452 
                 36.337 
                 41.634 
                 29.61 
               
               
                 192 
                 GLU 
                 C 
                 49.723 
                 40.529 
                 44.439 
                 27.98 
               
               
                 192 
                 GLU 
                 O 
                 50.335 
                 41.307 
                 43.687 
                 27.71 
               
               
                 193 
                 LEU 
                 N 
                 49.594 
                 40.742 
                 45.751 
                 27.68 
               
               
                 193 
                 LEU 
                 CA 
                 50.207 
                 41.908 
                 46.376 
                 27.69 
               
               
                 193 
                 LEU 
                 CB 
                 49.813 
                 42.035 
                 47.854 
                 27.93 
               
               
                 193 
                 LEU 
                 CG 
                 48.343 
                 42.445 
                 48.037 
                 28.23 
               
               
                 193 
                 LEU 
                 CD1 
                 47.999 
                 42.597 
                 49.525 
                 28.74 
               
               
                 193 
                 LEU 
                 CD2 
                 48.052 
                 43.752 
                 47.305 
                 28.07 
               
               
                 193 
                 LEU 
                 C 
                 51.721 
                 41.788 
                 46.261 
                 27.81 
               
               
                 193 
                 LEU 
                 O 
                 52.419 
                 42.799 
                 46.182 
                 27.59 
               
               
                 194 
                 GLY 
                 N 
                 52.214 
                 40.548 
                 46.261 
                 27.45 
               
               
                 194 
                 GLY 
                 CA 
                 53.640 
                 40.309 
                 46.127 
                 27.67 
               
               
                 194 
                 GLY 
                 C 
                 54.145 
                 40.860 
                 44.805 
                 27.89 
               
               
                 194 
                 GLY 
                 O 
                 55.214 
                 41.484 
                 44.758 
                 27.74 
               
               
                 195 
                 HIS 
                 N 
                 53.387 
                 40.618 
                 43.730 
                 28.34 
               
               
                 195 
                 HIS 
                 CA 
                 53.728 
                 41.138 
                 42.409 
                 28.91 
               
               
                 195 
                 HIS 
                 CB 
                 52.722 
                 40.684 
                 41.344 
                 28.90 
               
               
                 195 
                 HIS 
                 CG 
                 52.885 
                 39.265 
                 40.904 
                 29.19 
               
               
                 195 
                 HIS 
                 CD2 
                 51.972 
                 38.284 
                 40.707 
                 29.13 
               
               
                 195 
                 HIS 
                 ND1 
                 54.107 
                 38.728 
                 40.555 
                 29.27 
               
               
                 195 
                 HIS 
                 CE1 
                 53.940 
                 37.475 
                 40.167 
                 29.41 
               
               
                 195 
                 HIS 
                 NE2 
                 52.653 
                 37.181 
                 40.252 
                 29.67 
               
               
                 195 
                 HIS 
                 C 
                 53.686 
                 42.668 
                 42.479 
                 29.47 
               
               
                 195 
                 HIS 
                 O 
                 54.517 
                 43.357 
                 41.876 
                 29.42 
               
               
                 196 
                 ASN 
                 N 
                 52.702 
                 43.197 
                 43.201 
                 29.77 
               
               
                 196 
                 ASN 
                 CA 
                 52.554 
                 44.642 
                 43.350 
                 30.47 
               
               
                 196 
                 ASN 
                 CB 
                 51.306 
                 44.963 
                 44.180 
                 30.42 
               
               
                 196 
                 ASN 
                 CG 
                 50.025 
                 44.913 
                 43.364 
                 30.22 
               
               
                 196 
                 ASN 
                 OD1 
                 48.930 
                 44.822 
                 43.919 
                 30.73 
               
               
                 196 
                 ASN 
                 ND2 
                 50.154 
                 44.984 
                 42.047 
                 30.10 
               
               
                 196 
                 ASN 
                 C 
                 53.784 
                 45.215 
                 44.033 
                 30.97 
               
               
                 196 
                 ASN 
                 O 
                 54.210 
                 46.326 
                 43.726 
                 31.07 
               
               
                 197 
                 PHE 
                 N 
                 54.332 
                 44.460 
                 44.983 
                 31.16 
               
               
                 197 
                 PHE 
                 CA 
                 55.527 
                 44.893 
                 45.683 
                 32.11 
               
               
                 197 
                 PHE 
                 CB 
                 55.654 
                 44.211 
                 47.056 
                 32.06 
               
               
                 197 
                 PHE 
                 CG 
                 54.897 
                 44.909 
                 48.160 
                 32.49 
               
               
                 197 
                 PHE 
                 CD1 
                 53.505 
                 44.971 
                 48.142 
                 32.55 
               
               
                 197 
                 PHE 
                 CD2 
                 55.575 
                 45.481 
                 49.233 
                 32.76 
               
               
                 197 
                 PHE 
                 CE1 
                 52.797 
                 45.586 
                 49.173 
                 32.63 
               
               
                 197 
                 PHE 
                 CE2 
                 54.876 
                 46.102 
                 50.275 
                 32.94 
               
               
                 197 
                 PHE 
                 CZ 
                 53.479 
                 46.154 
                 50.243 
                 32.84 
               
               
                 197 
                 PHE 
                 C 
                 56.770 
                 44.604 
                 44.839 
                 32.36 
               
               
                 197 
                 PHE 
                 O 
                 57.880 
                 44.755 
                 45.317 
                 32.90 
               
               
                 198 
                 GLY 
                 N 
                 56.566 
                 44.169 
                 43.597 
                 32.88 
               
               
                 198 
                 GLY 
                 CA 
                 57.672 
                 43.913 
                 42.683 
                 33.15 
               
               
                 198 
                 GLY 
                 C 
                 58.218 
                 42.507 
                 42.461 
                 33.54 
               
               
                 198 
                 GLY 
                 O 
                 59.084 
                 42.313 
                 41.595 
                 33.69 
               
               
                 199 
                 ALA 
                 N 
                 57.752 
                 41.522 
                 43.219 
                 33.46 
               
               
                 199 
                 ALA 
                 CA 
                 58.275 
                 40.172 
                 43.038 
                 33.97 
               
               
                 199 
                 ALA 
                 CB 
                 57.988 
                 39.314 
                 44.278 
                 33.62 
               
               
                 199 
                 ALA 
                 C 
                 57.723 
                 39.486 
                 41.802 
                 34.11 
               
               
                 199 
                 ALA 
                 O 
                 56.575 
                 39.721 
                 41.399 
                 33.95 
               
               
                 200 
                 GLU 
                 N 
                 58.567 
                 38.668 
                 41.173 
                 34.47 
               
               
                 200 
                 GLU 
                 CA 
                 58.142 
                 37.884 
                 40.021 
                 34.84 
               
               
                 200 
                 GLU 
                 CB 
                 59.177 
                 37.931 
                 38.876 
                 36.00 
               
               
                 200 
                 GLU 
                 CG 
                 60.553 
                 37.335 
                 39.156 
                 37.49 
               
               
                 200 
                 GLU 
                 CD 
                 61.565 
                 37.624 
                 38.028 
                 38.44 
               
               
                 200 
                 GLU 
                 OE1 
                 61.245 
                 37.381 
                 36.848 
                 38.87 
               
               
                 200 
                 GLU 
                 OE2 
                 62.680 
                 38.093 
                 38.330 
                 39.55 
               
               
                 200 
                 GLU 
                 C 
                 58.024 
                 36.483 
                 40.626 
                 34.62 
               
               
                 200 
                 GLU 
                 O 
                 58.230 
                 36.312 
                 41.827 
                 33.71 
               
               
                 201 
                 HIS 
                 N 
                 57.687 
                 35.489 
                 39.819 
                 34.34 
               
               
                 201 
                 HIS 
                 CA 
                 57.537 
                 34.142 
                 40.346 
                 34.53 
               
               
                 201 
                 HIS 
                 CB 
                 56.856 
                 33.266 
                 39.299 
                 33.54 
               
               
                 201 
                 HIS 
                 CG 
                 55.433 
                 33.644 
                 39.047 
                 32.67 
               
               
                 201 
                 HIS 
                 CD2 
                 54.541 
                 34.303 
                 39.824 
                 32.28 
               
               
                 201 
                 HIS 
                 ND1 
                 54.770 
                 33.331 
                 37.881 
                 32.61 
               
               
                 201 
                 HIS 
                 CE1 
                 53.530 
                 33.783 
                 37.946 
                 32.40 
               
               
                 201 
                 HIS 
                 NE2 
                 53.366 
                 34.377 
                 39.116 
                 32.32 
               
               
                 201 
                 HIS 
                 C 
                 58.842 
                 33.498 
                 40.796 
                 35.26 
               
               
                 201 
                 HIS 
                 O 
                 59.933 
                 33.867 
                 40.341 
                 35.22 
               
               
                 202 
                 ASP 
                 N 
                 58.727 
                 32.559 
                 41.728 
                 36.11 
               
               
                 202 
                 ASP 
                 CA 
                 59.894 
                 31.828 
                 42.187 
                 36.98 
               
               
                 202 
                 ASP 
                 CB 
                 59.589 
                 31.079 
                 43.488 
                 36.36 
               
               
                 202 
                 ASP 
                 CG 
                 59.438 
                 32.010 
                 44.670 
                 35.88 
               
               
                 202 
                 ASP 
                 OD1 
                 60.198 
                 32.988 
                 44.737 
                 35.54 
               
               
                 202 
                 ASP 
                 OD2 
                 58.575 
                 31.767 
                 45.534 
                 35.71 
               
               
                 202 
                 ASP 
                 C 
                 60.210 
                 30.824 
                 41.076 
                 38.08 
               
               
                 202 
                 ASP 
                 O 
                 59.331 
                 30.459 
                 40.305 
                 37.52 
               
               
                 203 
                 PRO 
                 N 
                 61.473 
                 30.392 
                 40.966 
                 39.66 
               
               
                 203 
                 PRO 
                 CD 
                 62.651 
                 30.883 
                 41.699 
                 40.16 
               
               
                 203 
                 PRO 
                 CA 
                 61.864 
                 29.418 
                 39.934 
                 40.91 
               
               
                 203 
                 PRO 
                 CB 
                 63.353 
                 29.233 
                 40.180 
                 40.99 
               
               
                 203 
                 PRO 
                 CG 
                 63.773 
                 30.564 
                 40.727 
                 40.90 
               
               
                 203 
                 PRO 
                 C 
                 61.101 
                 28.123 
                 40.180 
                 42.10 
               
               
                 203 
                 PRO 
                 O 
                 60.710 
                 27.840 
                 41.313 
                 42.51 
               
               
                 204 
                 ASP 
                 N 
                 60.873 
                 27.334 
                 39.141 
                 43.15 
               
               
                 204 
                 ASP 
                 CA 
                 60.152 
                 26.079 
                 39.338 
                 44.22 
               
               
                 204 
                 ASP 
                 CB 
                 59.428 
                 25.647 
                 38.064 
                 44.53 
               
               
                 204 
                 ASP 
                 CG 
                 60.385 
                 25.360 
                 36.925 
                 44.89 
               
               
                 204 
                 ASP 
                 OD1 
                 61.006 
                 26.325 
                 36.426 
                 45.32 
               
               
                 204 
                 ASP 
                 OD2 
                 60.525 
                 24.179 
                 36.531 
                 45.28 
               
               
                 204 
                 ASP 
                 C 
                 61.085 
                 24.958 
                 39.768 
                 44.93 
               
               
                 204 
                 ASP 
                 O 
                 62.308 
                 25.133 
                 39.868 
                 44.76 
               
               
                 205 
                 GLY 
                 N 
                 60.486 
                 23.798 
                 40.024 
                 45.69 
               
               
                 205 
                 GLY 
                 CA 
                 61.263 
                 22.645 
                 40.432 
                 46.42 
               
               
                 205 
                 GLY 
                 C 
                 61.906 
                 22.881 
                 41.783 
                 46.99 
               
               
                 205 
                 GLY 
                 O 
                 61.328 
                 23.565 
                 42.633 
                 47.23 
               
               
                 206 
                 LEU 
                 N 
                 63.097 
                 22.313 
                 41.980 
                 47.22 
               
               
                 206 
                 LEU 
                 CA 
                 63.837 
                 22.458 
                 43.235 
                 47.38 
               
               
                 206 
                 LEU 
                 CB 
                 64.500 
                 21.129 
                 43.653 
                 47.47 
               
               
                 206 
                 LEU 
                 CG 
                 64.965 
                 21.114 
                 45.126 
                 47.66 
               
               
                 206 
                 LEU 
                 CD1 
                 63.767 
                 21.238 
                 46.078 
                 47.96 
               
               
                 206 
                 LEU 
                 CD2 
                 65.719 
                 19.822 
                 45.451 
                 47.67 
               
               
                 206 
                 LEU 
                 C 
                 64.914 
                 23.540 
                 43.111 
                 47.44 
               
               
                 206 
                 LEU 
                 O 
                 65.730 
                 23.555 
                 42.179 
                 47.57 
               
               
                 207 
                 ALA 
                 N 
                 64.909 
                 24.449 
                 44.070 
                 47.44 
               
               
                 207 
                 ALA 
                 CA 
                 65.863 
                 25.536 
                 44.081 
                 47.34 
               
               
                 207 
                 ALA 
                 CB 
                 65.447 
                 26.596 
                 43.058 
                 47.44 
               
               
                 207 
                 ALA 
                 C 
                 65.849 
                 26.111 
                 45.484 
                 47.38 
               
               
                 207 
                 ALA 
                 O 
                 65.042 
                 25.715 
                 46.322 
                 47.46 
               
               
                 208 
                 GLU 
                 N 
                 66.755 
                 27.037 
                 45.749 
                 47.42 
               
               
                 208 
                 GLU 
                 CA 
                 66.827 
                 27.672 
                 47.056 
                 47.30 
               
               
                 208 
                 GLU 
                 CB 
                 68.024 
                 28.621 
                 47.062 
                 48.01 
               
               
                 208 
                 GLU 
                 CG 
                 68.202 
                 29.500 
                 48.286 
                 49.08 
               
               
                 208 
                 GLU 
                 CD 
                 69.296 
                 30.532 
                 48.053 
                 49.75 
               
               
                 208 
                 GLU 
                 OE1 
                 69.087 
                 31.437 
                 47.209 
                 50.27 
               
               
                 208 
                 GLU 
                 OE2 
                 70.370 
                 30.430 
                 48.693 
                 50.06 
               
               
                 208 
                 GLU 
                 C 
                 65.518 
                 28.437 
                 47.308 
                 46.98 
               
               
                 208 
                 GLU 
                 O 
                 65.086 
                 28.599 
                 48.448 
                 46.85 
               
               
                 209 
                 CYS 
                 N 
                 64.886 
                 28.885 
                 46.225 
                 46.21 
               
               
                 209 
                 CYS 
                 CA 
                 63.641 
                 29.642 
                 46.305 
                 45.87 
               
               
                 209 
                 CYS 
                 C 
                 62.385 
                 28.832 
                 46.015 
                 46.10 
               
               
                 209 
                 CYS 
                 O 
                 61.297 
                 29.393 
                 45.886 
                 45.97 
               
               
                 209 
                 CYS 
                 CB 
                 63.704 
                 30.828 
                 45.344 
                 44.89 
               
               
                 209 
                 CYS 
                 SG 
                 64.959 
                 32.048 
                 45.809 
                 43.60 
               
               
                 210 
                 ALA 
                 N 
                 62.540 
                 27.517 
                 45.908 
                 46.44 
               
               
                 210 
                 ALA 
                 CA 
                 61.421 
                 26.623 
                 45.644 
                 47.08 
               
               
                 210 
                 ALA 
                 CB 
                 61.212 
                 26.467 
                 44.142 
                 47.11 
               
               
                 210 
                 ALA 
                 C 
                 61.720 
                 25.269 
                 46.277 
                 47.86 
               
               
                 210 
                 ALA 
                 O 
                 61.906 
                 24.274 
                 45.581 
                 47.67 
               
               
                 211 
                 PRO 
                 N 
                 61.766 
                 25.219 
                 47.620 
                 48.58 
               
               
                 211 
                 PRO 
                 CD 
                 61.587 
                 26.356 
                 48.540 
                 48.62 
               
               
                 211 
                 PRO 
                 CA 
                 62.048 
                 23.988 
                 48.366 
                 49.20 
               
               
                 211 
                 PRO 
                 CB 
                 61.955 
                 24.439 
                 49.823 
                 49.08 
               
               
                 211 
                 PRO 
                 CG 
                 62.341 
                 25.897 
                 49.760 
                 48.69 
               
               
                 211 
                 PRO 
                 C 
                 61.083 
                 22.849 
                 48.054 
                 50.05 
               
               
                 211 
                 PRO 
                 O 
                 60.004 
                 23.048 
                 47.496 
                 49.93 
               
               
                 212 
                 ASN 
                 N 
                 61.503 
                 21.642 
                 48.407 
                 51.18 
               
               
                 212 
                 ASN 
                 CA 
                 60.706 
                 20.439 
                 48.206 
                 52.30 
               
               
                 212 
                 ASN 
                 CB 
                 61.640 
                 19.224 
                 48.139 
                 52.92 
               
               
                 212 
                 ASN 
                 CG 
                 62.555 
                 19.117 
                 49.364 
                 53.44 
               
               
                 212 
                 ASN 
                 OD1 
                 62.104 
                 18.809 
                 50.471 
                 54.23 
               
               
                 212 
                 ASN 
                 ND2 
                 63.844 
                 19.382 
                 49.169 
                 53.84 
               
               
                 212 
                 ASN 
                 C 
                 59.773 
                 20.312 
                 49.416 
                 52.71 
               
               
                 212 
                 ASN 
                 O 
                 59.964 
                 20.993 
                 50.424 
                 52.73 
               
               
                 213 
                 GLU 
                 N 
                 58.783 
                 19.432 
                 49.328 
                 53.24 
               
               
                 213 
                 GLU 
                 CA 
                 57.855 
                 19.238 
                 50.442 
                 53.82 
               
               
                 213 
                 GLU 
                 CB 
                 56.958 
                 18.033 
                 50.171 
                 54.25 
               
               
                 213 
                 GLU 
                 CG 
                 55.856 
                 18.290 
                 49.155 
                 54.86 
               
               
                 213 
                 GLU 
                 CD 
                 54.935 
                 17.087 
                 40.983 
                 55.49 
               
               
                 213 
                 GLU 
                 OE1 
                 55.417 
                 16.037 
                 48.489 
                 55.75 
               
               
                 213 
                 GLU 
                 OE2 
                 53.735 
                 17.182 
                 49.344 
                 55.69 
               
               
                 213 
                 GLU 
                 C 
                 58.534 
                 19.065 
                 51.813 
                 53.91 
               
               
                 213 
                 GLU 
                 O 
                 58.130 
                 19.704 
                 52.798 
                 54.01 
               
               
                 214 
                 ASP 
                 N 
                 59.551 
                 18.202 
                 51.889 
                 53.72 
               
               
                 214 
                 ASP 
                 CA 
                 60.255 
                 17.960 
                 53.159 
                 53.41 
               
               
                 214 
                 ASP 
                 CB 
                 61.297 
                 16.847 
                 53.000 
                 54.15 
               
               
                 214 
                 ASP 
                 CG 
                 62.163 
                 16.644 
                 54.235 
                 54.73 
               
               
                 214 
                 ASP 
                 OD1 
                 61.678 
                 16.044 
                 55.225 
                 55.16 
               
               
                 214 
                 ASP 
                 OD2 
                 63.341 
                 17.071 
                 54.202 
                 55.21 
               
               
                 214 
                 ASP 
                 C 
                 60.936 
                 19.189 
                 53.736 
                 52.79 
               
               
                 214 
                 ASP 
                 O 
                 61.118 
                 19.282 
                 54.953 
                 52.99 
               
               
                 215 
                 GLN 
                 N 
                 61.335 
                 20.122 
                 52.880 
                 51.88 
               
               
                 215 
                 GLN 
                 CA 
                 61.974 
                 21.331 
                 53.383 
                 50.96 
               
               
                 215 
                 GLN 
                 CB 
                 62.968 
                 21.910 
                 52.366 
                 51.60 
               
               
                 215 
                 GLN 
                 CG 
                 63.931 
                 22.928 
                 52.975 
                 52.22 
               
               
                 215 
                 GLN 
                 CD 
                 65.005 
                 22.267 
                 53.828 
                 52.81 
               
               
                 215 
                 GLN 
                 OE1 
                 64.703 
                 21.457 
                 54.714 
                 53.24 
               
               
                 215 
                 GLN 
                 NE2 
                 66.268 
                 22.605 
                 53.563 
                 52.88 
               
               
                 215 
                 GLN 
                 C 
                 60.888 
                 22.363 
                 53.685 
                 49.85 
               
               
                 215 
                 GLN 
                 O 
                 61.183 
                 23.472 
                 54.140 
                 49.74 
               
               
                 216 
                 GLY 
                 N 
                 59.635 
                 21.989 
                 53.414 
                 48.46 
               
               
                 216 
                 GLY 
                 CA 
                 58.515 
                 22.880 
                 53.679 
                 46.62 
               
               
                 216 
                 GLY 
                 C 
                 57.625 
                 23.281 
                 52.506 
                 45.32 
               
               
                 216 
                 GLY 
                 O 
                 56.666 
                 24.037 
                 52.692 
                 44.87 
               
               
                 217 
                 GLY 
                 N 
                 57.928 
                 22.793 
                 51.303 
                 43.79 
               
               
                 217 
                 GLY 
                 CA 
                 57.107 
                 23.139 
                 50.151 
                 42.16 
               
               
                 217 
                 GLY 
                 C 
                 57.490 
                 24.463 
                 49.506 
                 40.85 
               
               
                 217 
                 GLY 
                 O 
                 58.503 
                 25.064 
                 49.856 
                 40.57 
               
               
                 218 
                 LYS 
                 N 
                 56.675 
                 24.928 
                 48.566 
                 39.66 
               
               
                 218 
                 LYS 
                 CA 
                 56.962 
                 26.180 
                 47.869 
                 38.74 
               
               
                 218 
                 LYS 
                 CB 
                 56.289 
                 26.165 
                 46.488 
                 38.96 
               
               
                 218 
                 LYS 
                 CG 
                 56.559 
                 24.907 
                 45.658 
                 39.24 
               
               
                 218 
                 LYS 
                 CD 
                 58.053 
                 24.587 
                 45.548 
                 39.71 
               
               
                 218 
                 LYS 
                 CE 
                 58.283 
                 23.288 
                 44.756 
                 39.75 
               
               
                 218 
                 LYS 
                 NZ 
                 59.659 
                 22.715 
                 44.945 
                 40.80 
               
               
                 218 
                 LYS 
                 C 
                 56.540 
                 27.456 
                 48.627 
                 37.69 
               
               
                 218 
                 LYS 
                 O 
                 55.681 
                 27.412 
                 49.504 
                 37.33 
               
               
                 219 
                 TYR 
                 N 
                 57.171 
                 28.579 
                 48.280 
                 36.44 
               
               
                 219 
                 TYR 
                 CA 
                 56.861 
                 29.880 
                 48.871 
                 35.08 
               
               
                 219 
                 TYR 
                 CB 
                 58.081 
                 30.790 
                 48.826 
                 35.14 
               
               
                 219 
                 TYR 
                 CG 
                 59.141 
                 30.373 
                 49.811 
                 35.36 
               
               
                 219 
                 TYR 
                 CD1 
                 58.947 
                 30.542 
                 51.184 
                 35.32 
               
               
                 219 
                 TYR 
                 CE1 
                 59.897 
                 30.095 
                 52.111 
                 35.38 
               
               
                 219 
                 TYR 
                 CD2 
                 60.314 
                 29.749 
                 49.380 
                 35.55 
               
               
                 219 
                 TYR 
                 CE2 
                 61.269 
                 29.299 
                 50.294 
                 35.73 
               
               
                 219 
                 TYR 
                 CZ 
                 61.055 
                 29.475 
                 51.655 
                 35.85 
               
               
                 219 
                 TYR 
                 OH 
                 62.012 
                 29.037 
                 52.552 
                 35.93 
               
               
                 219 
                 TYR 
                 C 
                 55.687 
                 30.502 
                 48.117 
                 34.52 
               
               
                 219 
                 TYR 
                 O 
                 55.322 
                 30.036 
                 47.035 
                 33.65 
               
               
                 220 
                 VAL 
                 N 
                 55.103 
                 31.552 
                 48.689 
                 33.96 
               
               
                 220 
                 VAL 
                 CA 
                 53.916 
                 32.183 
                 48.114 
                 33.59 
               
               
                 220 
                 VAL 
                 CB 
                 53.419 
                 33.356 
                 49.003 
                 33.34 
               
               
                 220 
                 VAL 
                 CG1 
                 54.312 
                 34.585 
                 48.815 
                 32.91 
               
               
                 220 
                 VAL 
                 CG2 
                 51.963 
                 33.673 
                 48.659 
                 32.96 
               
               
                 220 
                 VAL 
                 C 
                 53.999 
                 32.657 
                 46.665 
                 33.69 
               
               
                 220 
                 VAL 
                 O 
                 52.982 
                 32.665 
                 45.961 
                 33.62 
               
               
                 221 
                 MET 
                 N 
                 55.189 
                 33.045 
                 46.211 
                 33.66 
               
               
                 221 
                 MET 
                 CA 
                 55.338 
                 33.499 
                 44.827 
                 34.39 
               
               
                 221 
                 MET 
                 CB 
                 56.464 
                 34.536 
                 44.698 
                 33.60 
               
               
                 221 
                 MET 
                 CG 
                 56.167 
                 35.877 
                 45.391 
                 33.08 
               
               
                 221 
                 MET 
                 SD 
                 54.466 
                 36.501 
                 45.157 
                 32.05 
               
               
                 221 
                 MET 
                 CE 
                 54.422 
                 36.801 
                 43.385 
                 32.38 
               
               
                 221 
                 MET 
                 C 
                 55.548 
                 32.371 
                 43.811 
                 35.23 
               
               
                 221 
                 MET 
                 O 
                 55.907 
                 32.626 
                 42.659 
                 35.28 
               
               
                 222 
                 TYR 
                 N 
                 55.345 
                 31.126 
                 44.232 
                 35.97 
               
               
                 222 
                 TYR 
                 CA 
                 55.463 
                 30.014 
                 43.298 
                 36.93 
               
               
                 222 
                 TYR 
                 CB 
                 55.432 
                 28.673 
                 44.027 
                 37.59 
               
               
                 222 
                 TYR 
                 CG 
                 55.974 
                 27.540 
                 43.187 
                 38.08 
               
               
                 222 
                 TYR 
                 CD1 
                 57.327 
                 27.478 
                 42.866 
                 38.44 
               
               
                 222 
                 TYR 
                 CE1 
                 57.832 
                 26.463 
                 42.052 
                 38.71 
               
               
                 222 
                 TYR 
                 CD2 
                 55.129 
                 26.554 
                 42.678 
                 38.39 
               
               
                 222 
                 TYR 
                 CE2 
                 55.621 
                 25.533 
                 41.868 
                 38.73 
               
               
                 222 
                 TYR 
                 CZ 
                 56.976 
                 25.498 
                 41.559 
                 39.11 
               
               
                 222 
                 TYR 
                 OH 
                 57.471 
                 24.499 
                 40.746 
                 40.00 
               
               
                 222 
                 TYR 
                 C 
                 54.219 
                 30.169 
                 42.414 
                 37.37 
               
               
                 222 
                 TYR 
                 O 
                 53.140 
                 30.513 
                 42.902 
                 37.08 
               
               
                 223 
                 PRO 
                 N 
                 54.354 
                 29.920 
                 41.103 
                 38.04 
               
               
                 223 
                 PRO 
                 CD 
                 55.614 
                 29.594 
                 40.418 
                 38.08 
               
               
                 223 
                 PRO 
                 CA 
                 53.256 
                 30.042 
                 40.135 
                 38.39 
               
               
                 223 
                 PRO 
                 CB 
                 53.979 
                 29.955 
                 38.796 
                 38.48 
               
               
                 223 
                 PRO 
                 CG 
                 55.112 
                 29.055 
                 39.095 
                 38.40 
               
               
                 223 
                 PRO 
                 C 
                 52.079 
                 29.077 
                 40.200 
                 38.94 
               
               
                 223 
                 PRO 
                 O 
                 50.947 
                 29.448 
                 39.890 
                 38.98 
               
               
                 224 
                 ILE 
                 N 
                 52.323 
                 27.847 
                 40.618 
                 39.26 
               
               
                 224 
                 ILE 
                 CA 
                 51.244 
                 26.886 
                 40.628 
                 40.09 
               
               
                 224 
                 ILE 
                 CB 
                 51.400 
                 25.917 
                 39.451 
                 40.48 
               
               
                 224 
                 ILE 
                 CG2 
                 50.837 
                 26.567 
                 38.185 
                 40.60 
               
               
                 224 
                 ILE 
                 CG1 
                 52.880 
                 25.526 
                 39.317 
                 40.80 
               
               
                 224 
                 ILE 
                 CD1 
                 53.147 
                 24.535 
                 38.211 
                 41.41 
               
               
                 224 
                 ILE 
                 C 
                 51.056 
                 26.058 
                 41.873 
                 40.24 
               
               
                 224 
                 ILE 
                 O 
                 51.989 
                 25.821 
                 42.638 
                 40.30 
               
               
                 225 
                 ALA 
                 N 
                 49.816 
                 25.614 
                 42.034 
                 40.58 
               
               
                 225 
                 ALA 
                 CA 
                 49.380 
                 24.764 
                 43.127 
                 40.97 
               
               
                 225 
                 ALA 
                 CB 
                 49.722 
                 23.308 
                 42.795 
                 41.20 
               
               
                 225 
                 ALA 
                 C 
                 49.825 
                 25.070 
                 44.556 
                 41.21 
               
               
                 225 
                 ALA 
                 O 
                 49.990 
                 24.139 
                 45.343 
                 41.39 
               
               
                 226 
                 VAL 
                 N 
                 50.037 
                 26.330 
                 44.920 
                 41.25 
               
               
                 226 
                 VAL 
                 CA 
                 50.394 
                 26.568 
                 46.314 
                 41.45 
               
               
                 226 
                 VAL 
                 CB 
                 51.272 
                 27.840 
                 46.493 
                 41.51 
               
               
                 226 
                 VAL 
                 CG1 
                 51.068 
                 28.797 
                 45.334 
                 41.64 
               
               
                 226 
                 VAL 
                 CG2 
                 50.969 
                 28.515 
                 47.827 
                 41.44 
               
               
                 226 
                 VAL 
                 C 
                 49.057 
                 26.630 
                 47.072 
                 41.43 
               
               
                 226 
                 VAL 
                 O 
                 48.406 
                 27.668 
                 47.171 
                 41.19 
               
               
                 227 
                 SER 
                 N 
                 48.652 
                 25.460 
                 47.564 
                 41.45 
               
               
                 227 
                 SER 
                 CA 
                 47.397 
                 25.236 
                 48.289 
                 41.89 
               
               
                 227 
                 SER 
                 CB 
                 47.132 
                 23.736 
                 48.353 
                 41.88 
               
               
                 227 
                 SER 
                 OG 
                 48.230 
                 23.085 
                 48.982 
                 41.75 
               
               
                 227 
                 SER 
                 C 
                 47.298 
                 25.775 
                 49.708 
                 41.96 
               
               
                 227 
                 SER 
                 O 
                 46.190 
                 25.967 
                 50.228 
                 42.00 
               
               
                 228 
                 GLY 
                 N 
                 48.447 
                 25.990 
                 50.337 
                 41.99 
               
               
                 228 
                 GLY 
                 CA 
                 48.466 
                 26.463 
                 51.709 
                 42.37 
               
               
                 228 
                 GLY 
                 C 
                 48.642 
                 25.275 
                 52.635 
                 42.72 
               
               
                 228 
                 GLY 
                 O 
                 48.721 
                 25.426 
                 53.853 
                 42.58 
               
               
                 229 
                 ASP 
                 N 
                 48.710 
                 24.087 
                 52.037 
                 43.09 
               
               
                 229 
                 ASP 
                 CA 
                 48.874 
                 22.835 
                 52.772 
                 43.59 
               
               
                 229 
                 ASP 
                 CB 
                 48.539 
                 21.636 
                 51.884 
                 44.44 
               
               
                 229 
                 ASP 
                 CG 
                 47.071 
                 21.558 
                 51.518 
                 45.07 
               
               
                 229 
                 ASP 
                 OD1 
                 46.698 
                 20.559 
                 50.865 
                 46.12 
               
               
                 229 
                 ASP 
                 OD2 
                 46.294 
                 22.472 
                 51.863 
                 45.27 
               
               
                 229 
                 ASP 
                 C 
                 50.287 
                 22.645 
                 53.291 
                 43.55 
               
               
                 229 
                 ASP 
                 O 
                 50.550 
                 21.722 
                 54.060 
                 43.45 
               
               
                 230 
                 HIS 
                 N 
                 51.197 
                 23.512 
                 52.865 
                 43.38 
               
               
                 230 
                 HIS 
                 CA 
                 52.586 
                 23.411 
                 53.287 
                 43.24 
               
               
                 230 
                 HIS 
                 CB 
                 53.455 
                 23.095 
                 52.076 
                 43.74 
               
               
                 230 
                 HIS 
                 CG 
                 53.018 
                 21.863 
                 51.355 
                 44.30 
               
               
                 230 
                 HIS 
                 CD2 
                 52.116 
                 21.690 
                 50.357 
                 44.53 
               
               
                 230 
                 HIS 
                 ND1 
                 53.423 
                 20.601 
                 51.728 
                 44.35 
               
               
                 230 
                 HIS 
                 CE1 
                 52.787 
                 19.703 
                 50.997 
                 44.69 
               
               
                 230 
                 HIS 
                 NE2 
                 51.988 
                 20.339 
                 50.158 
                 44.94 
               
               
                 230 
                 HIS 
                 C 
                 53.064 
                 24.673 
                 53.975 
                 42.89 
               
               
                 230 
                 HIS 
                 O 
                 52.631 
                 25.780 
                 53.637 
                 42.41 
               
               
                 231 
                 GLU 
                 N 
                 53.963 
                 24.484 
                 54.939 
                 42.49 
               
               
                 231 
                 GLU 
                 CA 
                 54.511 
                 25.574 
                 55.735 
                 42.28 
               
               
                 231 
                 GLU 
                 CB 
                 55.656 
                 25.064 
                 56.625 
                 43.29 
               
               
                 231 
                 GLU 
                 CG 
                 56.270 
                 26.150 
                 57.523 
                 44.54 
               
               
                 231 
                 GLU 
                 CD 
                 57.300 
                 25.603 
                 58.521 
                 45.36 
               
               
                 231 
                 GLU 
                 OE1 
                 57.909 
                 26.418 
                 59.265 
                 45.54 
               
               
                 231 
                 GLU 
                 OE2 
                 57.492 
                 24.365 
                 58.558 
                 45.66 
               
               
                 231 
                 GLU 
                 C 
                 55.001 
                 26.786 
                 54.957 
                 41.71 
               
               
                 231 
                 GLU 
                 O 
                 54.627 
                 27.915 
                 55.277 
                 41.40 
               
               
                 232 
                 ASN 
                 N 
                 55.833 
                 26.563 
                 53.941 
                 40.80 
               
               
                 232 
                 ASN 
                 CA 
                 56.381 
                 27.684 
                 53.184 
                 40.30 
               
               
                 232 
                 ASN 
                 CB 
                 57.548 
                 27.228 
                 52.289 
                 40.22 
               
               
                 232 
                 ASN 
                 CG 
                 58.721 
                 26.673 
                 53.086 
                 40.58 
               
               
                 232 
                 ASN 
                 OD1 
                 59.053 
                 27.175 
                 54.157 
                 40.38 
               
               
                 232 
                 ASN 
                 ND2 
                 59.364 
                 25.642 
                 52.550 
                 40.48 
               
               
                 232 
                 ASN 
                 C 
                 55.359 
                 28.434 
                 52.336 
                 39.58 
               
               
                 232 
                 ASN 
                 O 
                 55.616 
                 29.562 
                 51.928 
                 39.26 
               
               
                 233 
                 ASN 
                 N 
                 54.215 
                 27.815 
                 52.073 
                 39.33 
               
               
                 233 
                 ASN 
                 CA 
                 53.182 
                 28.447 
                 51.252 
                 39.40 
               
               
                 233 
                 ASN 
                 CB 
                 51.904 
                 27.605 
                 51.239 
                 39.00 
               
               
                 233 
                 ASN 
                 CG 
                 52.081 
                 26.256 
                 50.543 
                 38.74 
               
               
                 233 
                 ASN 
                 OD1 
                 51.163 
                 25.441 
                 50.523 
                 38.17 
               
               
                 233 
                 ASN 
                 ND2 
                 53.259 
                 26.021 
                 49.973 
                 38.66 
               
               
                 233 
                 ASN 
                 C 
                 52.832 
                 29.863 
                 51.702 
                 39.53 
               
               
                 233 
                 ASN 
                 O 
                 52.547 
                 30.719 
                 50.871 
                 39.63 
               
               
                 234 
                 LYS 
                 N 
                 52.867 
                 30.101 
                 53.012 
                 39.81 
               
               
                 234 
                 LYS 
                 CA 
                 52.532 
                 31.403 
                 53.594 
                 40.33 
               
               
                 234 
                 LYS 
                 CB 
                 51.901 
                 31.226 
                 54.978 
                 40.90 
               
               
                 234 
                 LYS 
                 CG 
                 50.714 
                 30.297 
                 55.069 
                 41.90 
               
               
                 234 
                 LYS 
                 CD 
                 50.448 
                 30.006 
                 56.544 
                 42.73 
               
               
                 234 
                 LYS 
                 CE 
                 49.282 
                 29.054 
                 56.742 
                 43.39 
               
               
                 234 
                 LYS 
                 NZ 
                 49.502 
                 27.769 
                 56.016 
                 44.13 
               
               
                 234 
                 LYS 
                 C 
                 53.708 
                 32.361 
                 53.772 
                 40.21 
               
               
                 234 
                 LYS 
                 O 
                 53.569 
                 33.363 
                 54.484 
                 40.40 
               
               
                 235 
                 MET 
                 N 
                 54.860 
                 32.066 
                 53.173 
                 39.47 
               
               
                 235 
                 MET 
                 CA 
                 56.014 
                 32.946 
                 53.333 
                 39.09 
               
               
                 235 
                 MET 
                 CB 
                 57.052 
                 32.289 
                 54.244 
                 40.17 
               
               
                 235 
                 MET 
                 CG 
                 56.465 
                 31.689 
                 55.512 
                 41.84 
               
               
                 235 
                 MET 
                 SD 
                 57.740 
                 30.990 
                 56.579 
                 44.64 
               
               
                 235 
                 MET 
                 CE 
                 58.083 
                 29.387 
                 55.761 
                 43.33 
               
               
                 235 
                 MET 
                 C 
                 56.674 
                 33.312 
                 52.013 
                 38.33 
               
               
                 235 
                 MET 
                 O 
                 56.446 
                 32.657 
                 50.988 
                 37.96 
               
               
                 236 
                 PHE 
                 N 
                 57.490 
                 34.360 
                 52.046 
                 37.26 
               
               
                 236 
                 PHE 
                 CA 
                 58.204 
                 34.808 
                 50.859 
                 37.15 
               
               
                 236 
                 PHE 
                 CB 
                 58.372 
                 36.326 
                 50.881 
                 36.44 
               
               
                 236 
                 PHE 
                 CG 
                 57.125 
                 37.077 
                 50.504 
                 35.82 
               
               
                 236 
                 PHE 
                 CD1 
                 56.721 
                 37.153 
                 49.172 
                 35.71 
               
               
                 236 
                 PHE 
                 CD2 
                 56.344 
                 37.686 
                 51.477 
                 35.44 
               
               
                 236 
                 PHE 
                 CE1 
                 55.554 
                 37.832 
                 48.816 
                 35.24 
               
               
                 236 
                 PHE 
                 CE2 
                 55.174 
                 38.367 
                 51.132 
                 35.20 
               
               
                 236 
                 PHE 
                 CZ 
                 54.777 
                 38.439 
                 49.800 
                 35.07 
               
               
                 236 
                 PHE 
                 C 
                 59.577 
                 34.146 
                 50.763 
                 37.28 
               
               
                 236 
                 PHE 
                 O 
                 60.243 
                 33.922 
                 51.770 
                 36.90 
               
               
                 237 
                 SER 
                 N 
                 59.987 
                 33.823 
                 49.541 
                 37.66 
               
               
                 237 
                 SER 
                 CA 
                 61.284 
                 33.205 
                 49.312 
                 38.05 
               
               
                 237 
                 SER 
                 CB 
                 61.321 
                 32.542 
                 47.935 
                 38.00 
               
               
                 237 
                 SER 
                 OG 
                 61.120 
                 33.505 
                 46.917 
                 37.41 
               
               
                 237 
                 SER 
                 C 
                 62.342 
                 34.293 
                 49.357 
                 38.70 
               
               
                 237 
                 SER 
                 O 
                 62.024 
                 35.486 
                 49.375 
                 38.35 
               
               
                 238 
                 GLN 
                 N 
                 63.601 
                 33.869 
                 49.379 
                 39.50 
               
               
                 238 
                 GLN 
                 CA 
                 64.726 
                 34.790 
                 49.380 
                 40.45 
               
               
                 238 
                 GLN 
                 CB 
                 66.048 
                 24.010 
                 49.458 
                 41.34 
               
               
                 238 
                 GLN 
                 CG 
                 66.243 
                 33.277 
                 50.783 
                 42.67 
               
               
                 238 
                 GLN 
                 CD 
                 66.412 
                 34.242 
                 51.951 
                 43.54 
               
               
                 238 
                 GLN 
                 OE1 
                 66.160 
                 33.891 
                 53.111 
                 44.24 
               
               
                 238 
                 GLN 
                 NE2 
                 66.849 
                 35.468 
                 51.649 
                 43.86 
               
               
                 238 
                 GLN 
                 C 
                 64.671 
                 35.590 
                 48.085 
                 40.43 
               
               
                 238 
                 GLN 
                 O 
                 65.017 
                 36.769 
                 48.059 
                 40.66 
               
               
                 239 
                 CYS 
                 N 
                 64.225 
                 34.939 
                 47.013 
                 40.63 
               
               
                 239 
                 CYS 
                 CA 
                 64.120 
                 35.586 
                 45.703 
                 40.74 
               
               
                 239 
                 CYS 
                 C 
                 63.102 
                 36.727 
                 45.725 
                 40.41 
               
               
                 239 
                 CYS 
                 O 
                 63.356 
                 37.808 
                 45.184 
                 40.04 
               
               
                 239 
                 CYS 
                 CB 
                 63.739 
                 34.559 
                 44.628 
                 41.45 
               
               
                 239 
                 CYS 
                 SG 
                 65.042 
                 33.335 
                 44.236 
                 42.69 
               
               
                 240 
                 SER 
                 N 
                 61.954 
                 36.479 
                 46.349 
                 40.19 
               
               
                 240 
                 SER 
                 CA 
                 60.910 
                 37.493 
                 46.462 
                 40.29 
               
               
                 240 
                 SER 
                 CB 
                 59.643 
                 36.882 
                 47.071 
                 40.08 
               
               
                 240 
                 SER 
                 OG 
                 59.074 
                 35.910 
                 46.215 
                 39.76 
               
               
                 240 
                 SER 
                 C 
                 61.383 
                 38.659 
                 47.335 
                 40.40 
               
               
                 240 
                 SER 
                 O 
                 61.078 
                 39.823 
                 47.053 
                 40.33 
               
               
                 241 
                 LYS 
                 N 
                 62.127 
                 38.339 
                 48.391 
                 40.50 
               
               
                 241 
                 LYS 
                 CA 
                 62.637 
                 39.354 
                 49.308 
                 41.10 
               
               
                 241 
                 LYS 
                 CB 
                 63.365 
                 38.698 
                 50.481 
                 40.76 
               
               
                 241 
                 LYS 
                 CG 
                 62.460 
                 38.012 
                 51.491 
                 40.60 
               
               
                 241 
                 LYS 
                 CD 
                 63.282 
                 37.429 
                 52.628 
                 40.39 
               
               
                 241 
                 LYS 
                 CE 
                 62.395 
                 36.840 
                 53.707 
                 40.49 
               
               
                 241 
                 LYS 
                 NZ 
                 63.204 
                 36.274 
                 54.818 
                 40.45 
               
               
                 241 
                 LYS 
                 C 
                 63.586 
                 40.329 
                 48.620 
                 41.77 
               
               
                 241 
                 LYS 
                 O 
                 63.494 
                 41.544 
                 48.810 
                 41.57 
               
               
                 242 
                 GLN 
                 N 
                 64.505 
                 39.788 
                 47.826 
                 42.60 
               
               
                 242 
                 GLN 
                 CA 
                 65.470 
                 40.613 
                 47.113 
                 43.55 
               
               
                 242 
                 GLN 
                 CB 
                 66.398 
                 39.712 
                 46.281 
                 44.45 
               
               
                 242 
                 GLN 
                 CG 
                 67.611 
                 40.417 
                 45.716 
                 45.86 
               
               
                 242 
                 GLN 
                 CD 
                 68.577 
                 39.463 
                 45.038 
                 46.74 
               
               
                 242 
                 GLN 
                 OE1 
                 68.199 
                 38.719 
                 44.133 
                 47.71 
               
               
                 242 
                 GLN 
                 NE2 
                 69.834 
                 39.486 
                 45.467 
                 47.24 
               
               
                 242 
                 GLN 
                 C 
                 64.731 
                 41.607 
                 46.209 
                 43.65 
               
               
                 242 
                 GLN 
                 O 
                 65.047 
                 42.797 
                 46.170 
                 43.59 
               
               
                 243 
                 SER 
                 N 
                 63.734 
                 41.113 
                 45.485 
                 43.77 
               
               
                 243 
                 SER 
                 CA 
                 62.961 
                 41.959 
                 44.588 
                 43.87 
               
               
                 243 
                 SER 
                 CB 
                 62.028 
                 41.092 
                 43.740 
                 43.76 
               
               
                 243 
                 SER 
                 OG 
                 62.771 
                 40.173 
                 42.961 
                 43.31 
               
               
                 243 
                 SER 
                 C 
                 62.145 
                 43.006 
                 45.337 
                 44.23 
               
               
                 243 
                 SER 
                 O 
                 62.098 
                 44.171 
                 44.940 
                 44.17 
               
               
                 244 
                 ILE 
                 N 
                 61.510 
                 42.588 
                 46.427 
                 44.68 
               
               
                 244 
                 ILE 
                 CA 
                 60.668 
                 43.480 
                 47.218 
                 45.21 
               
               
                 244 
                 ILE 
                 CB 
                 59.730 
                 42.656 
                 48.137 
                 44.81 
               
               
                 244 
                 ILE 
                 CG2 
                 59.051 
                 43.562 
                 49.171 
                 44.62 
               
               
                 244 
                 ILE 
                 CG1 
                 58.717 
                 41.909 
                 47.258 
                 44.59 
               
               
                 244 
                 ILE 
                 CD1 
                 57.892 
                 40.891 
                 48.014 
                 44.05 
               
               
                 244 
                 ILE 
                 C 
                 61.467 
                 44.499 
                 48.025 
                 46.05 
               
               
                 244 
                 ILE 
                 O 
                 61.017 
                 45.627 
                 48.224 
                 45.65 
               
               
                 245 
                 TYR 
                 N 
                 62.651 
                 44.102 
                 48.481 
                 47.25 
               
               
                 245 
                 TYR 
                 CA 
                 63.511 
                 45.006 
                 49.233 
                 48.50 
               
               
                 245 
                 TYR 
                 CB 
                 64.825 
                 44.320 
                 49.611 
                 49.13 
               
               
                 245 
                 TYR 
                 CG 
                 65.755 
                 45.191 
                 50.434 
                 49.90 
               
               
                 245 
                 TYR 
                 CD1 
                 65.463 
                 45.497 
                 51.766 
                 50.03 
               
               
                 245 
                 TYR 
                 CE1 
                 66.312 
                 46.302 
                 52.526 
                 50.40 
               
               
                 245 
                 TYR 
                 CD2 
                 66.922 
                 45.715 
                 49.878 
                 50.27 
               
               
                 245 
                 TYR 
                 CE2 
                 67.781 
                 46.527 
                 50.630 
                 50.62 
               
               
                 245 
                 TYR 
                 CZ 
                 67.471 
                 46.815 
                 51.952 
                 50.61 
               
               
                 245 
                 TYR 
                 OH 
                 68.321 
                 47.612 
                 52.693 
                 50.69 
               
               
                 245 
                 TYR 
                 C 
                 63.799 
                 46.187 
                 48.315 
                 49.10 
               
               
                 245 
                 TYR 
                 O 
                 63.675 
                 47.341 
                 48.716 
                 49.04 
               
               
                 246 
                 LYS 
                 N 
                 64.174 
                 45.887 
                 47.074 
                 49.81 
               
               
                 246 
                 LYS 
                 CA 
                 64.452 
                 46.927 
                 46.090 
                 50.75 
               
               
                 246 
                 LYS 
                 CB 
                 64.673 
                 46.323 
                 44.695 
                 51.00 
               
               
                 246 
                 LYS 
                 CG 
                 65.982 
                 45.571 
                 44.502 
                 51.59 
               
               
                 246 
                 LYS 
                 CD 
                 66.129 
                 45.125 
                 43.052 
                 51.90 
               
               
                 246 
                 LYS 
                 CE 
                 67.416 
                 44.357 
                 42.830 
                 52.28 
               
               
                 246 
                 LYS 
                 NZ 
                 67.560 
                 43.948 
                 41.403 
                 52.33 
               
               
                 246 
                 LYS 
                 C 
                 63.273 
                 47.890 
                 46.023 
                 51.14 
               
               
                 246 
                 LYS 
                 O 
                 63.440 
                 49.103 
                 46.118 
                 51.15 
               
               
                 247 
                 THR 
                 N 
                 62.078 
                 47.336 
                 45.855 
                 51.80 
               
               
                 247 
                 THR 
                 CA 
                 60.866 
                 48.139 
                 45.773 
                 52.40 
               
               
                 247 
                 THR 
                 CB 
                 59.614 
                 47.248 
                 45.651 
                 52.30 
               
               
                 247 
                 THR 
                 OG1 
                 59.664 
                 46.514 
                 44.420 
                 52.09 
               
               
                 247 
                 THR 
                 CG2 
                 58.346 
                 48.107 
                 45.684 
                 52.13 
               
               
                 247 
                 THR 
                 C 
                 60.702 
                 49.033 
                 46.998 
                 53.14 
               
               
                 247 
                 THR 
                 O 
                 60.542 
                 50.246 
                 46.877 
                 53.08 
               
               
                 248 
                 ILE 
                 N 
                 60.750 
                 48.428 
                 48.176 
                 53.94 
               
               
                 248 
                 ILE 
                 CA 
                 60.583 
                 49.178 
                 49.408 
                 54.96 
               
               
                 248 
                 ILE 
                 CB 
                 60.655 
                 48.240 
                 50.637 
                 54.88 
               
               
                 248 
                 ILE 
                 CG2 
                 60.528 
                 49.057 
                 51.925 
                 54.90 
               
               
                 248 
                 ILE 
                 CG1 
                 59.562 
                 47.177 
                 50.526 
                 54.89 
               
               
                 248 
                 ILE 
                 CD1 
                 59.554 
                 46.217 
                 51.686 
                 54.95 
               
               
                 248 
                 ILE 
                 C 
                 61.593 
                 50.314 
                 49.570 
                 55.69 
               
               
                 248 
                 ILE 
                 O 
                 61.207 
                 51.454 
                 49.833 
                 55.77 
               
               
                 249 
                 GLU 
                 N 
                 62.877 
                 50.027 
                 49.393 
                 56.54 
               
               
                 249 
                 GLU 
                 CA 
                 63.878 
                 51.071 
                 49.578 
                 57.48 
               
               
                 249 
                 GLU 
                 CB 
                 65.289 
                 50.469 
                 49.652 
                 58.05 
               
               
                 249 
                 GLU 
                 CG 
                 65.828 
                 49.905 
                 48.351 
                 59.02 
               
               
                 249 
                 GLU 
                 CD 
                 67.257 
                 49.398 
                 48.493 
                 59.54 
               
               
                 249 
                 GLU 
                 OE1 
                 68.160 
                 50.222 
                 48.760 
                 59.84 
               
               
                 249 
                 GLU 
                 OE2 
                 67.476 
                 48.175 
                 48.345 
                 60.02 
               
               
                 249 
                 GLU 
                 C 
                 63.843 
                 52.193 
                 48.543 
                 57.80 
               
               
                 249 
                 GLU 
                 O 
                 64.546 
                 53.192 
                 48.693 
                 57.86 
               
               
                 250 
                 SER 
                 N 
                 63.025 
                 52.055 
                 47.505 
                 58.16 
               
               
                 250 
                 SER 
                 CA 
                 62.953 
                 53.105 
                 46.494 
                 58.45 
               
               
                 250 
                 SER 
                 CB 
                 63.514 
                 52.598 
                 45.165 
                 58.61 
               
               
                 250 
                 SER 
                 OG 
                 62.729 
                 51.541 
                 44.647 
                 58.94 
               
               
                 250 
                 SER 
                 C 
                 61.554 
                 53.672 
                 46.269 
                 58.59 
               
               
                 250 
                 SER 
                 O 
                 61.387 
                 54.623 
                 45.506 
                 58.57 
               
               
                 251 
                 LYS 
                 N 
                 60.554 
                 53.098 
                 46.935 
                 58.76 
               
               
                 251 
                 LYS 
                 CA 
                 59.172 
                 53.554 
                 46.781 
                 58.85 
               
               
                 251 
                 LYS 
                 CB 
                 58.351 
                 52.516 
                 46.017 
                 58.99 
               
               
                 251 
                 LYS 
                 CG 
                 58.596 
                 52.438 
                 44.520 
                 59.31 
               
               
                 251 
                 LYS 
                 CD 
                 57.673 
                 51.377 
                 43.940 
                 59.49 
               
               
                 251 
                 LYS 
                 CE 
                 57.609 
                 51.388 
                 42.423 
                 59.66 
               
               
                 251 
                 LYS 
                 NZ 
                 56.579 
                 50.404 
                 41.938 
                 59.42 
               
               
                 251 
                 LYS 
                 C 
                 58.474 
                 53.839 
                 48.106 
                 58.77 
               
               
                 251 
                 LYS 
                 O 
                 57.508 
                 54.597 
                 48.152 
                 58.81 
               
               
                 252 
                 ALA 
                 N 
                 58.945 
                 53.217 
                 49.179 
                 58.69 
               
               
                 252 
                 ALA 
                 CA 
                 58.339 
                 53.429 
                 50.489 
                 58.69 
               
               
                 252 
                 ALA 
                 CB 
                 59.160 
                 52.721 
                 51.573 
                 58.66 
               
               
                 252 
                 ALA 
                 C 
                 58.273 
                 54.926 
                 50.772 
                 58.54 
               
               
                 252 
                 ALA 
                 O 
                 57.297 
                 55.431 
                 51.331 
                 58.67 
               
               
                 253 
                 GLN 
                 N 
                 59.320 
                 55.635 
                 50.364 
                 58.33 
               
               
                 253 
                 GLN 
                 CA 
                 59.396 
                 57.071 
                 50.575 
                 57.97 
               
               
                 253 
                 GLN 
                 CB 
                 60.815 
                 57.559 
                 50.278 
                 58.55 
               
               
                 253 
                 GLN 
                 CG 
                 61.072 
                 59.009 
                 50.627 
                 59.13 
               
               
                 253 
                 GLN 
                 CD 
                 60.856 
                 59.299 
                 52.101 
                 59.51 
               
               
                 253 
                 GLN 
                 OE1 
                 59.718 
                 59.354 
                 52.577 
                 59.79 
               
               
                 253 
                 GLN 
                 NE2 
                 61.952 
                 59.480 
                 52.835 
                 59.76 
               
               
                 253 
                 GLN 
                 C 
                 58.399 
                 57.788 
                 49.676 
                 57.38 
               
               
                 253 
                 GLN 
                 O 
                 57.889 
                 58.856 
                 50.024 
                 57.51 
               
               
                 254 
                 GLU 
                 N 
                 58.114 
                 57.180 
                 48.528 
                 56.50 
               
               
                 254 
                 GLU 
                 CA 
                 57.193 
                 57.747 
                 47.551 
                 55.63 
               
               
                 254 
                 GLU 
                 CB 
                 57.363 
                 57.039 
                 46.204 
                 56.07 
               
               
                 254 
                 GLU 
                 CG 
                 56.591 
                 57.692 
                 45.060 
                 56.47 
               
               
                 254 
                 GLU 
                 CD 
                 56.739 
                 56.943 
                 43.746 
                 56.78 
               
               
                 254 
                 GLU 
                 OE1 
                 57.891 
                 56.701 
                 43.318 
                 57.11 
               
               
                 254 
                 GLU 
                 OE2 
                 55.702 
                 56.602 
                 43.139 
                 56.77 
               
               
                 254 
                 GLU 
                 C 
                 55.709 
                 57.735 
                 47.941 
                 54.80 
               
               
                 254 
                 GLU 
                 O 
                 55.030 
                 58.753 
                 47.801 
                 54.58 
               
               
                 255 
                 CYS 
                 N 
                 55.195 
                 56.602 
                 48.422 
                 53.66 
               
               
                 255 
                 CYS 
                 CA 
                 53.778 
                 56.547 
                 48.783 
                 52.59 
               
               
                 255 
                 CYS 
                 C 
                 53.410 
                 55.742 
                 50.023 
                 52.52 
               
               
                 255 
                 CYS 
                 O 
                 52.231 
                 55.633 
                 50.345 
                 52.30 
               
               
                 255 
                 CYS 
                 CB 
                 52.954 
                 56.028 
                 47.603 
                 51.44 
               
               
                 255 
                 CYS 
                 SG 
                 53.117 
                 54.239 
                 47.304 
                 49.73 
               
               
                 256 
                 PHE 
                 N 
                 54.393 
                 55.171 
                 50.712 
                 52.58 
               
               
                 256 
                 PHE 
                 CA 
                 54.095 
                 54.408 
                 51.922 
                 52.90 
               
               
                 256 
                 PHE 
                 CB 
                 55.255 
                 53.479 
                 52.288 
                 52.57 
               
               
                 256 
                 PHE 
                 CG 
                 55.233 
                 52.163 
                 51.570 
                 52.17 
               
               
                 256 
                 PHE 
                 CD1 
                 54.791 
                 52.079 
                 50.252 
                 52.00 
               
               
                 256 
                 PHE 
                 CD2 
                 55.701 
                 51.013 
                 52.194 
                 51.99 
               
               
                 256 
                 PHE 
                 CE1 
                 54.819 
                 50.872 
                 49.566 
                 51.86 
               
               
                 256 
                 PHE 
                 CE2 
                 55.733 
                 49.797 
                 51.512 
                 51.86 
               
               
                 256 
                 PHE 
                 CZ 
                 55.291 
                 49.728 
                 50.196 
                 51.82 
               
               
                 256 
                 PHE 
                 C 
                 53.832 
                 55.376 
                 53.066 
                 53.32 
               
               
                 256 
                 PHE 
                 O 
                 54.473 
                 56.421 
                 53.164 
                 53.19 
               
               
                 257 
                 GLN 
                 N 
                 52.888 
                 55.022 
                 53.930 
                 53.81 
               
               
                 257 
                 GLN 
                 CA 
                 52.529 
                 55.874 
                 55.057 
                 54.49 
               
               
                 257 
                 GLN 
                 CB 
                 51.075 
                 56.327 
                 54.924 
                 54.41 
               
               
                 257 
                 GLN 
                 CG 
                 50.729 
                 56.968 
                 53.593 
                 54.72 
               
               
                 257 
                 GLN 
                 CD 
                 49.269 
                 57.361 
                 53.509 
                 54.80 
               
               
                 257 
                 GLN 
                 OE1 
                 48.826 
                 57.946 
                 52.521 
                 55.05 
               
               
                 257 
                 GLN 
                 NE2 
                 48.510 
                 57.038 
                 54.549 
                 54.80 
               
               
                 257 
                 GLN 
                 C 
                 52.683 
                 55.125 
                 56.369 
                 54.95 
               
               
                 257 
                 GLN 
                 O 
                 53.133 
                 53.981 
                 56.396 
                 55.09 
               
               
                 258 
                 GLU 
                 N 
                 52.309 
                 55.788 
                 57.458 
                 55.42 
               
               
                 258 
                 GLU 
                 CA 
                 52.353 
                 55.184 
                 58.781 
                 55.77 
               
               
                 258 
                 GLU 
                 CB 
                 52.566 
                 56.261 
                 59.851 
                 56.14 
               
               
                 258 
                 GLU 
                 CG 
                 53.849 
                 57.070 
                 59.678 
                 56.74 
               
               
                 258 
                 GLU 
                 CD 
                 54.055 
                 58.095 
                 60.779 
                 57.19 
               
               
                 258 
                 GLU 
                 OE1 
                 55.140 
                 58.729 
                 60.819 
                 57.35 
               
               
                 258 
                 GLU 
                 OE2 
                 53.129 
                 58.270 
                 61.606 
                 57.42 
               
               
                 258 
                 GLU 
                 C 
                 50.973 
                 54.554 
                 58.949 
                 55.81 
               
               
                 258 
                 GLU 
                 O 
                 50.057 
                 54.864 
                 58.185 
                 55.77 
               
               
                 259 
                 ARG 
                 N 
                 50.814 
                 53.664 
                 59.921 
                 55.84 
               
               
                 259 
                 ARG 
                 CA 
                 49.506 
                 53.058 
                 60.133 
                 55.95 
               
               
                 259 
                 ARG 
                 CB 
                 49.577 
                 51.980 
                 61.212 
                 55.87 
               
               
                 259 
                 ARG 
                 CG 
                 50.094 
                 50.635 
                 60.726 
                 55.84 
               
               
                 259 
                 ARG 
                 CD 
                 50.023 
                 49.614 
                 61.849 
                 55.69 
               
               
                 259 
                 ARG 
                 NE 
                 50.405 
                 40.261 
                 61.442 
                 55.63 
               
               
                 259 
                 ARG 
                 CZ 
                 49.673 
                 47.461 
                 60.670 
                 55.58 
               
               
                 259 
                 ARG 
                 NH1 
                 48.498 
                 47.860 
                 60.196 
                 55.45 
               
               
                 259 
                 ARG 
                 NH2 
                 50.113 
                 46.245 
                 60.387 
                 55.58 
               
               
                 259 
                 ARG 
                 C 
                 48.504 
                 54.143 
                 60.542 
                 56.13 
               
               
                 259 
                 ARG 
                 O 
                 47.427 
                 54.231 
                 59.911 
                 56.19 
               
               
                 259 
                 ARG 
                 OXT 
                 48.802 
                 54.904 
                 61.491 
                 56.12 
               
               
                 260 
                 007 
                 N3 
                 47.727 
                 29.829 
                 39.980 
                 39.58 
               
               
                 260 
                 007 
                 O6 
                 47.576 
                 27.266 
                 41.351 
                 41.05 
               
               
                 260 
                 007 
                 O1 
                 44.788 
                 23.897 
                 40.843 
                 43.59 
               
               
                 260 
                 007 
                 C5 
                 47.174 
                 31.040 
                 40.173 
                 38.64 
               
               
                 260 
                 007 
                 O2 
                 49.740 
                 36.283 
                 39.759 
                 35.36 
               
               
                 260 
                 007 
                 C1 
                 46.829 
                 28.736 
                 39.597 
                 40.68 
               
               
                 260 
                 007 
                 C2 
                 47.378 
                 28.034 
                 38.342 
                 40.79 
               
               
                 260 
                 007 
                 C3 
                 47.601 
                 29.053 
                 37.224 
                 40.76 
               
               
                 260 
                 007 
                 C4 
                 48.428 
                 28.495 
                 36.081 
                 40.93 
               
               
                 260 
                 007 
                 C6 
                 46.620 
                 27.701 
                 40.709 
                 41.02 
               
               
                 260 
                 007 
                 C7 
                 45.036 
                 26.131 
                 41.645 
                 42.36 
               
               
                 260 
                 007 
                 C8 
                 44.100 
                 26.443 
                 42.823 
                 42.38 
               
               
                 260 
                 007 
                 C13 
                 44.799 
                 27.056 
                 44.045 
                 42.39 
               
               
                 260 
                 007 
                 C20 
                 46.068 
                 26.282 
                 44.406 
                 42.54 
               
               
                 260 
                 007 
                 C21 
                 43.850 
                 27.067 
                 45.249 
                 42.60 
               
               
                 260 
                 007 
                 N1 
                 48.734 
                 35.382 
                 39.482 
                 36.20 
               
               
                 260 
                 007 
                 C9 
                 49.235 
                 34.151 
                 39.306 
                 36.48 
               
               
                 260 
                 007 
                 O3 
                 50.444 
                 33.937 
                 39.245 
                 35.65 
               
               
                 260 
                 007 
                 C10 
                 48.255 
                 33.016 
                 39.175 
                 37.20 
               
               
                 260 
                 007 
                 C22 
                 48.177 
                 32.158 
                 40.439 
                 38.16 
               
               
                 260 
                 007 
                 C23 
                 47.749 
                 32.989 
                 41.665 
                 37.95 
               
               
                 260 
                 007 
                 O4 
                 45.975 
                 31.286 
                 40.126 
                 38.63 
               
               
                 260 
                 007 
                 N2 
                 45.330 
                 27.355 
                 40.904 
                 41.60 
               
               
                 260 
                 007 
                 C11 
                 44.380 
                 25.075 
                 40.766 
                 42.75 
               
               
                 260 
                 007 
                 O5 
                 43.453 
                 25.430 
                 40.003 
                 43.03 
               
               
                 260 
                 007 
                 C14 
                 47.884 
                 32.183 
                 42.942 
                 38.16 
               
               
                 260 
                 007 
                 C15 
                 49.090 
                 32.237 
                 43.694 
                 38.38 
               
               
                 260 
                 007 
                 C16 
                 49.209 
                 31.514 
                 44.917 
                 38.20 
               
               
                 260 
                 007 
                 C17 
                 48.120 
                 30.724 
                 45.385 
                 38.22 
               
               
                 260 
                 007 
                 C18 
                 46.921 
                 30.645 
                 44.623 
                 38.22 
               
               
                 260 
                 007 
                 C19 
                 46.801 
                 31.375 
                 43.401 
                 38.18 
               
               
                 260 
                 007 
                 C12 
                 46.392 
                 26.942 
                 37.907 
                 41.12 
               
               
                 261 
                 ZN2 
                 ZN + 2 
                 51.599 
                 35.407 
                 39.845 
                 36.08 
               
               
                   
               
             
          
         
       
     
     The present invention is not to be limited in scope by the specific embodiments described herein. Indeed, various modifications of the invention in addition to those described herein will become apparent to those skilled in the art from the foregoing description. Such modifications are intended to fall within the scope of the appended claims. 
     It is further to be understood that all base sizes or amino acid sizes, and all molecular weight or molecular mass values, given for nucleic acids or polypeptides are approximate, and are provided for description. 
     Various publications are cited herein, the disclosures of which are hereby incorporated by reference in their entireties.