Patent Publication Number: US-2005131209-A1

Title: Crystallized hnf4 gamma ligand binding domain polypeptide and screening methods employing same

Description:
TECHNICAL FIELD  
      The present invention relates generally to the structure of the ligand binding domain of HNF4γ, and more particularly to the crystalline structure of the ligand binding domain of HNF4γ. The invention further relates to methods by which modulators and ligands of HNF4γ, and HNF4α, can be identified.  
                               Abbreviations                                                ATP   adenosine triphosphate           ADP   adenosine diphosphate           APS   Advanced Photon Source           BSA   bovine serum albumin           CBP   CREB-binding protein           cDNA   complementary DNA           CI   chemical ionization           DBD   DNA binding domain           DMSO   dimethyl sulfoxide           DNA   deoxyribonucleic acid           DTT   dithiothreitol           EDTA   ethylenediaminetetraacetic acid           EI   electron impact ionization           ER   estrogen receptor           FAME   fatty acid methyl ester           FRET   fluorescent resonance energy transfer           GC   gas chromatography           GC/MS   gas chromatography/mass spectrometry           HEPES   N-2-Hydroxyethylpiperazine-N′-2-ethanesulfonic               acid           HNF   hepatocyte nuclear factor           HNF1   hepatocyte nuclear factor 1           HNF4α   hepatocyte nuclear factor 4 α           HNF4γ   hepatocyte nuclear factor 4 γ           HRE   hormone response element           kDa   kilodalton(s)           LBD   ligand binding domain           MODY   mature onset diabetes of the young           MS   mass spectrometry           m/z   mass to charge ratio           NDP   nucleotide diphosphate           nt   nucleotide           NTP   nucleotide triphosphate           PAGE   polyacrylamide gel electrophoresis           PCR   polymerase chain reaction           pI   isoelectric point           PR   progesterone receptor           RAR   retinoic acid receptor           RXR   retinoid X receptor           SDS   sodium dodecyl sulfate           SDS-PAGE   sodium dodecyl sulfate polyacrylamide gel               electrophoresis           SIRAS   single isomorphous replacement anomalous               scattering           TIC   total ion chromatogram           TR   thyroid hormone receptor           TTR   plasma transthyretin           vHNF   variant hepatocyte nuclear factor                      
 
     
       
         
           
               
            
               
                   
               
               
                   
               
               
                 Amino Acid Abbreviations 
               
            
           
           
               
               
               
            
               
                 Single-Letter Code 
                 Three-Letter Code 
                 Name 
               
               
                   
               
            
           
           
               
               
               
               
            
               
                 A 
                 Ala 
                 Alanine 
                   
               
               
                   
               
               
                 V 
                 Val 
                 Valine 
               
               
                   
               
               
                 L 
                 Leu 
                 Leucine 
               
               
                   
               
               
                 I 
                 Ile 
                 Isoleucine 
               
               
                   
               
               
                 P 
                 Pro 
                 Proline 
               
               
                   
               
               
                 F 
                 Phe 
                 Phenylalanine 
               
               
                   
               
               
                 W 
                 Trp 
                 Tryptophan 
               
               
                   
               
               
                 M 
                 Met 
                 Methionine 
               
               
                   
               
               
                 G 
                 Gly 
                 Glycine 
               
               
                   
               
               
                 S 
                 Ser 
                 Serine 
               
               
                   
               
               
                 T 
                 Thr 
                 Threonine 
               
               
                   
               
               
                 C 
                 Cys 
                 Cysteine 
               
               
                   
               
               
                 Y 
                 Tyr 
                 Tyrosine 
               
               
                   
               
               
                 N 
                 Asn 
                 Asparagine 
               
               
                   
               
               
                 Q 
                 Gln 
                 Glutamine 
               
               
                   
               
               
                 D 
                 Asp 
                 Aspartic Acid 
               
               
                   
               
               
                 E 
                 Glu 
                 Glutamic Acid 
               
               
                   
               
               
                 K 
                 Lys 
                 Lysine 
               
               
                   
               
               
                 R 
                 Arg 
                 Arginine 
               
               
                   
               
               
                 H 
                 His 
                 Histidine 
               
               
                   
               
            
           
         
       
     
     
       
         
           
               
            
               
                   
               
               
                   
               
               
                 Functionally Equivalent Codons 
               
            
           
           
               
               
               
            
               
                   
                 Amino Acid 
                 Codons 
               
               
                   
                   
               
            
           
           
               
               
               
               
               
               
            
               
                   
                 Alanine 
                 Ala 
                 A 
                 GCA GCC GCG GCU 
                   
               
               
                   
                   
               
               
                   
                 Cysteine 
                 Cys 
                 C 
                 UGC UGU 
               
               
                   
                   
               
               
                   
                 Aspartic Acid 
                 Asp 
                 D 
                 GAC GAU 
               
               
                   
                   
               
               
                   
                 Glumatic acid 
                 Glu 
                 E 
                 GAA GAG 
               
               
                   
                   
               
               
                   
                 Phenylalanine 
                 Phe 
                 F 
                 UUC UUU 
               
               
                   
                   
               
               
                   
                 Glycine 
                 Gly 
                 G 
                 GGA GGC GGG GGU 
               
               
                   
                   
               
               
                   
                 Histidine 
                 His 
                 H 
                 CAC CAU 
               
               
                   
                   
               
               
                   
                 Isoleucine 
                 Ile 
                 I 
                 AUA AUC AUU 
               
               
                   
                   
               
               
                   
                 Lysine 
                 Lys 
                 K 
                 AAA AAG 
               
               
                   
                   
               
               
                   
                 Methionine 
                 Met 
                 M 
                 AUG 
               
               
                   
                   
               
               
                   
                 Asparagine 
                 Asn 
                 N 
                 AAC AAU 
               
               
                   
                   
               
               
                   
                 Proline 
                 Pro 
                 P 
                 CCA CCC CCG CCU 
               
               
                   
                   
               
               
                   
                 Glutamine 
                 Gln 
                 Q 
                 CAA CAG 
               
               
                   
                   
               
               
                   
                 Threonine 
                 Thr 
                 T 
                 ACA ACC ACG ACU 
               
               
                   
                   
               
               
                   
                 Valine 
                 Val 
                 V 
                 GUA GUC GUG GUU 
               
               
                   
                   
               
               
                   
                 Tryptophan 
                 Trp 
                 W 
                 UGG 
               
               
                   
                   
               
               
                   
                 Tyrosine 
                 Tyr 
                 Y 
                 UAC UAU 
               
               
                   
                   
               
               
                   
                 Leucine 
                 Leu 
                 L 
                 UUA UUG CUA CUC 
               
               
                   
                   
               
               
                   
                   
                   
                   
                 CUG CUU 
               
               
                   
                   
               
               
                   
                 Arginine 
                 Arg 
                 R 
                 AGA AGG CGA CGC 
               
               
                   
                   
               
               
                   
                   
                   
                   
                 CGG CGU 
               
               
                   
                   
               
               
                   
                 Serine 
                 Ser 
                 S 
                 ACG AGU UCA UCC 
               
               
                   
                   
               
               
                   
                   
                   
                   
                 UCG UCU 
               
               
                   
                   
               
            
           
         
       
     
     BACKGROUND ART  
      Nuclear receptors represent a superfamily of proteins that specifically bind a physiologically relevant small molecule, such as a hormone or vitamin. As a result of a molecule binding to a nuclear receptor, the nuclear receptor changes the ability of a cell to transcribe DNA, i.e. nuclear receptors modulate the transcription of DNA. However they can also have transcription independent actions.  
      Unlike integral membrane receptors and membrane-associated receptors, nuclear receptors reside in either the cytoplasm or nucleus of eukaryotic cells. Thus nuclear receptors comprise a class of intracellular, soluble ligand-regulated transcription factors. Nuclear receptors include but are not limited to receptors for glucocorticoids, androgens, mineralcorticoids, progestins, estrogens, thyroid hormones, vitamin D retinoids, icosanoids and peroxisomes. Many nuclear receptors, identified by either sequence homology to known receptors (See, Drewes et al., (1996)  Mol. Cell. Biol.  16:925-31) or based on their affinity for specific DNA binding sites in gene promoters (See, Sladek et al.,  Genes Dev.  4:2353-65), have unascertained ligands and are therefore termed “orphan receptors”.  
      Hepatocyte Nuclear Factor 4 (HNF4) is an orphan nuclear receptor and two isoforms, HNF4α and HNF4γ, have currently been identified. HNF4α was originally identified based on its ability to bind promoter regions in the plasma transthyretin (TTR) and apoCIII genes. Sladek et al.,  Genes Dev.  4:2353-65. HNF4γ was identified based on its known homology to HNF4α. Drewes et al., (1996)  Mol. Cell. Biol.  16:925-31. Nuclear receptors activate or repress transcription through partner proteins called co-activators or co-repressors, respectively. CREB-binding protein, or CBP, is a known co-activator for HNF4α (Wang et al., (1998)  J. Biol. Chem.  273: 30847-50; Dell &amp; Hadzopoulou-Cladaras, (1999)  J. Biol. Chem.  274: 9013-21). Mutations in HNF4α have been linked to the metabolic disorder Mature Onset of Diabetes of the Young (MODY), type 1. Yamagata et al., (1996)  Nature  384:458-60. HNF4α +/−  subjects experience reduced serum levels of apolipoprotein AII, apolipoprotein CIII and lipoproitein(a), leading to reduced triglycerides. Shih et al., (2000)  Diabetes  49:832-37. HNF4α regulation had previously been identified for these apolipoprotien genes (Mietus-Snyder et al., (1992)  Mol. Cell. Biol.  12:1708-18; Chan et al., (1993)  Nucleic Acid Res.  21:1205-11), as well as regulation of other factors involved in glucose metabolism and insulin secretion. Diaz Guerra et al., (1993)  Mol. Cell. Biol.  13:7725-33; Miguerol et al., (1994)  J. Biol. Chem.  269:8944-51; Stoffel &amp; Duncan, (1997)  Proc. Natl. Acad. Sci. U.S.A.  94:13209-14; Wang et al., (1998)  J. Biol. Chem.  273:30847-50.  
      Structurally, the HNF4 family of nuclear receptors, including HNF4α and HNF4γ, are generally characterized by two distinct structural elements. First, nuclear receptors comprise a central DNA binding domain which targets the receptor to specific DNA sequences, which are known as hormone response elements (HREs). The DNA binding domains of these receptors are related in structure and sequence, and are located within the middle of the receptor. Second, the C-terminal region of the HNF4 family of nuclear receptors encompasses the ligand binding domain (LBD). Upon binding a ligand, the receptor shifts to a transcriptionally active state.  
      Almost all nuclear hormone receptors bind DNA, and the physiologically active complex of many is as a heterodimer with the retinoid X receptor (RXR). The HNF4 isoforms are unusual in that they are obligate homodimers and cannot dimerize with any other nuclear receptors. In fact, retinoid X receptor (RXR) heterodimer formation is actually prevented by LBD interactions. Jiang &amp; Sladek, (1997) J. Biol. Chem. 272:1218-25.  
      Polypeptides, including the ligand binding domain of HNF4γ, have a three-dimensional structure determined by the primary amino acid sequence and the environment surrounding the polypeptide. This three-dimensional structure establishes the polypeptide&#39;s activity, stability, binding affinity, binding specificity, and other biochemical attributes. Thus, knowledge of a protein&#39;s three-dimensional structure can provide much guidance in designing agents that mimic, inhibit, or improve its biological activity in soluble or membrane bound forms.  
      The three-dimensional structure of a polypeptide can be determined in a number of ways. Many of the most precise methods employ X-ray crystallography (See, e.g., Van Holde, (1971)  Physical Biochemistry , Prentice-Hall, N.J., 221-39). This technique relies on the ability of crystalline lattices to diffract X-rays or other forms of radiation. Diffraction experiments suitable for determining the three-dimensional structure of macromolecules typically require high-quality crystals. Unfortunately, such crystals have been unavailable for the ligand binding domain of HNF4γ, as well as many other proteins of interest. Thus, high-quality diffracting crystals of the ligand binding domain of HNF4γ would greatly assist in the elucidation of HNF4γ&#39;s three-dimensional structure, and would provide insight into the ligand binding properties of HNF4γ.  
      Clearly, the solved crystal structure of the HNF4γ ligand binding domain would be useful in the design of modulators of activity mediated by all HNF4 isoforms. Evaluation of the available sequence data has made it clear that HNF4α shares significant sequence homology with HNF4γ. Further, HNF4γ shows structural homology with the three-dimensional fold of other proteins.  
      The solved HNF4γ-ligand crystal structure would provide structural details and insights necessary to design a modulator of HNF4γ that maximizes preferred requirements for any modulator, i.e. potency and specificity. By exploiting the structural details obtained from an HNF4γ-ligand crystal structure, it would be possible to design an HNF4 modulator that, despite HNF4γ&#39;s similarity with other proteins, exploits the unique structural features of HNF4γ. An HNF4 modulator developed using structure-assisted design would take advantage of heretofore unknown HNF4 structural considerations and thus be more effective than a modulator developed using homology-based design. Potential or existent homology models cannot provide the necessary degree of specificity. An HNF4γ modulator designed using the structural coordinates of a crystalline form of HNF4γ would also provide a starting point for the development of modulators of other HNF4s.  
      What is needed, therefore, is a crystallized form of an HNF4γ LBD polypeptide, preferably in complex with a ligand. Acquisition of crystals of the HNF4γ LBD polypeptide will permit the three dimensional structure of the HNF4γ LBD to be determined. Knowledge of this three dimensional structure will facilitate the design of modulators of HNF4γ activity. Such modulators can lead to therapeutic compounds to treat a wide range of conditions, including lipid homeostasis disorders and glucose homeostasis disorders.  
     SUMMARY OF THE INVENTION  
      A substantially pure HNF4γ ligand binding domain polypeptide in crystalline form is disclosed. Preferably, the crystalline form has lattice constants of a=152.71 Å, b=152.71 Å, c=93.42 Å, α=90°, β=90°, γ=90°. More preferably, the crystalline form is a tetragonal crystalline form. Even more preferably, the crystalline form has a space group of 14 1 22. Still more preferably, the HNF4γ ligand binding domain polypeptide has the amino acid sequence shown in SEQ ID NO:4.  
      In a preferred embodiment, the HNF4γ ligand binding domain polypeptide is in complex with a ligand. More preferably, the ligand is a fatty acid.  
      A method for determining the three-dimensional structure of a crystallized HNF4γ ligand binding domain polypeptide to a resolution of about 3.0 Å or better is also disclosed. The method comprises (a) crystallizing an HNF4γ ligand binding domain polypeptide; and (b) analyzing the HNF4γ ligand binding domain polypeptide to determine the three-dimensional structure of the crystallized HNF4γ ligand binding domain polypeptide, whereby the three-dimensional structure of a crystallized HNF4γ ligand binding domain polypeptide is determined to a resolution of about 3.0 Å or better.  
      A method of designing a modulator of an HNF4 polypeptide is also disclosed. The method comprises (a) designing a potential modulator of an HNF4 polypeptide that will form bonds with amino acids in a substrate binding site based upon a crystalline structure of an HNF4γ ligand binding domain polypeptide; (b) synthesizing the modulator; and (c) determining whether the potential modulator modulates the activity of the HNF4 polypeptide, whereby a modulator of an HNF4 polypeptide is designed.  
      In an alternative embodiment, a method of designing a modulator that selectively modulates the activity of an HNF4 polypeptide in accordance with the present invention comprises: (a) obtaining a crystalline form of an HNF4γ ligand binding domain polypeptide; (b) evaluating the three-dimensional structure of the crystallized HNF4γ ligand binding domain polypeptide; and (c) synthesizing a potential modulator based on the three-dimensional crystal structure of the crystallized HNF4γ ligand binding domain polypeptide, whereby a modulator that selectively modulates the activity of an HNF4 polypeptide is designed. Preferably, the method further comprises contacting an HNF4γ ligand binding domain polypeptide with the potential modulator; and assaying the HNF4γ ligand binding domain polypeptide for binding of the potential modulator, for a change in activity of the HNF4γ ligand binding domain polypeptide, or both. More preferably, the crystalline form is such that the three-dimensional structure of the crystallized HNF4γ ligand binding domain polypeptide can be determined to a resolution of about 3.0 Å or better.  
      In yet another embodiment, a method of designing a modulator of an HNF4 polypeptide in accordance with the present invention comprises: (a) selecting a candidate HNF4 ligand; (b) determining which amino acid or amino acids of an HNF4 polypeptide interact with the ligand using a three-dimensional model of a crystallized protein comprising an HNF4γ LBD; (c) identifying in a biological assay for HNF4 activity a degree to which the ligand modulates the activity of the HNF4 polypeptide; (d) selecting a chemical modification of the ligand wherein the interaction between the amino acids of the HNF4 polypeptide and the ligand is predicted to be modulated by the chemical modification; (e) performing the chemical modification on the ligand to form a modified ligand; (f) contacting the modified ligand with the HNF4 polypeptide; (g) identifying in a biological assay for HNF4 activity a degree to which the modified ligand modulates the biological activity of the HNF4 polypeptide; and (h) comparing the biological activity of the HNF4 polypeptide in the presence of modified ligand with the biological activity of the HNF4 polypeptide in the presence of the unmodified ligand, whereby a modulator of an HNF4 polypeptide is designed. Preferably, the HNF4 polypeptide is an HNF4γ polypeptide. More preferably, the three-dimensional model of a crystallized protein is an HNF4γ LBD polypeptide with a bound ligand. Even more preferably, the method further comprises repeating steps (a) through (f), if the biological activity of the HNF4 polypeptide in the presence of the modified ligand varies from the biological activity of the HNF4 polypeptide in the presence of the unmodified ligand.  
      A method for identifying an HNF4 modulator is also disclosed. The method comprises (a) providing atomic coordinates of an HNF4γ ligand binding domain to a computerized modeling system; and (b) modeling ligands that fit spatially into the binding pocket of the HNF4γ ligand binding domain to thereby identify an HNF4 modulator. Preferably, the method further comprises identifying in an assay for HNF4-mediated activity a modeled ligand that increases or decreases the activity of the HNF4.  
      A method of identifying an HNF4γ modulator that selectively modulates the activity of an HNF4γ polypeptide compared to other polypeptides is disclosed. The method comprises (a) providing atomic coordinates of an HNF4γ ligand binding domain to a computerized modeling system; and (b) modeling a ligand that fits into the binding pocket of an HNF4γ ligand binding domain and that interacts with conformationally constrained residues of an HNF4γ that are conserved among HNF4 isoforms to thereby identify an HNF4γ modulator. Preferably, the method further comprises identifying in a biological assay for HNF4γ-mediated activity a modeled ligand that selectively binds to the HNF4γ ligand binding domain and increases or decreases the activity of the HNF4γ.  
      An assay method for identifying a compound that inhibits binding of a ligand to an HNF4 polypeptide is disclosed. The assay method comprises (a) incubating an HNF4 polypeptide with a ligand in the presence of a test inhibitor compound; (b) determining an amount of ligand that is bound to the HNF4 polypeptide, wherein decreased binding of ligand to the HNF4 protein in the presence of the test inhibitor compound relative to binding of ligand in the absence of the test inhibitor compound is indicative of inhibition; and (c) identifying the test compound as an inhibitor of ligand binding if decreased ligand binding is observed. Preferably, the ligand is a fatty acid.  
      Accordingly, it is an object of the present invention to provide a three dimensional structure of the ligand binding domain of HNF4γ. The object is achieved in whole or in part by the present invention.  
      An object of the invention having been stated hereinabove, other objects will be evident as the description proceeds, when taken in connection with the accompanying Drawings and Laboratory Examples as best described hereinbelow. 
    
    
     BRIEF DESCRIPTION OF THE DRAWINGS  
       FIG. 1A  is a ribbon diagram depicting the structure of the HNF4γ LBD complexed with a natural ligand, palmitic acid. The palmitic acid is depicted in space-filling form. The protein is in gray and palmitic acid is in black, with the oxygen atoms in white.  
       FIG. 1B  is a composite-omit electron density map of the binding pocket of HNF4γ contoured at 1.2σ showing electron density from bound ligand. HNF4γ atoms are shown as a gray ball-and-stick figure.  
       FIG. 2  is a diagram depicting the binding pocket of the HNF4γ LBD. Palmitic acid, a natural ligand of HNF4γ, is depicted space filling form. Side chains of residues R186, Q145, 1202, A215, V214, M301, M142 and 1305 are involved in ligand binding and are depicted in ball-and-stick form. The protein is in gray and palmitic acid is in black, with the oxygen atoms in white.  
       FIG. 3  is a bar graph depicting the results of FRET assays performed to detect CBP peptide recruitment.  
       FIG. 4  is a GC/MS chromatogram of the HNF4γ extract obtained by employing chemical ionization.  
       FIG. 5  is a chemical ionization mass spectrum for peak g, depicted in  FIG. 4 . The protonated ion at m/z 271 was subsequently identified as the methyl ester of palmitic acid.  
       FIG. 6  is a GC/MS chromatogram of the HNF4γ extract obtained by employing electron impact ionization.  
       FIG. 7  is an electron impact ionization mass spectrum for peak c, depicted in  FIG. 6 . The molecular ion at m/z 270 was subsequently identified as the methyl ester of palmitic acid.  
    
    
     DETAILED DESCRIPTION OF THE INVENTION  
      Until disclosure of the present invention presented herein, the ability to obtain crystalline forms of an HNF4γ LBD has not been realized. And until disclosure of the present invention presented herein, a detailed three-dimensional crystal structure of an HNF4γ polypeptide has not been solved.  
      In addition to providing structural information, crystalline polypeptides provide other advantages. For example, the crystallization process itself further purifies the polypeptide, and satisfies one of the classical criteria for homogeneity. In fact, crystallization frequently provides unparalleled purification quality, removing impurities that are not removed by other purification methods such as HPLC, dialysis, conventional column chromatography, etc. Moreover, crystalline polypeptides are often stable at ambient temperatures and free of protease contamination and other degradation associated with solution storage. Crystalline polypeptides can also be useful as pharmaceutical preparations. Finally, crystallization techniques in general are largely free of problems such as denaturation associated with other stabilization methods (e.g., lyophilization). Once crystallization has been accomplished, crystallographic data provides useful structural information that can assist the design of compounds that can serve as agonists or antagonists, as described herein below. In addition, the crystal structure provides information useful to map a receptor binding domain, which could then be mimicked by a small non-peptide molecule that would serve as an antagonist or agonist.  
      I. Definitions  
      Following long-standing patent law convention, the terms “a” and “an” mean “one or more” when used in this application, including the claims.  
      As used herein, the term “mutation” carries its traditional connotation and means a change, inherited, naturally occurring or introduced, in a nucleic acid or polypeptide sequence, and is used in its sense as generally known to those of skill in the art.  
      As used herein, the term “labeled” means the attachment of a moiety, capable of detection by spectroscopic, radiologic or other methods, to a probe molecule.  
      As used herein, the term “target cell” refers to a cell, into which it is desired to insert a nucleic acid sequence or polypeptide, or to otherwise effect a modification from conditions known to be standard in the unmodified cell. A nucleic acid sequence introduced into a target cell can be of variable length. Additionally, a nucleic acid sequence can enter a target cell as a component of a plasmid or other vector or as a naked sequence.  
      As used herein, the term “transcription” means a cellular process involving the interaction of an RNA polymerase with a gene that directs the expression as RNA of the structural information present in the coding sequences of the gene. The process includes, but is not limited to the following steps: (a) the transcription initiation, (b) transcript elongation, (c) transcript splicing, (d) transcript capping, (e) transcript termination, (f) transcript polyadenylation, (g) nuclear export of the transcript, (h) transcript editing, and (i) stabilizing the transcript.  
      As used herein, the term “expression” generally refers to the cellular processes by which a polypeptide is produced from RNA.  
      As used herein, the term “transcription factor” means a cytoplasmic or nuclear protein which binds to a gene, or binds to an RNA transcript of a gene, or binds to another protein which binds to a gene or an RNA transcript or another protein which in turn binds to a gene or an RNA transcript, so as to thereby modulate expression of the gene. Such modulation can additionally be achieved by other mechanisms; the essence of “transcription factor for a gene” is that the level of transcription of the gene is altered in some way.  
      As used herein, the term “hybridization” means the binding of a probe molecule, a molecule to which a detectable moiety has been bound, to a target sample.  
      As used herein, the term “detecting” means confirming the presence of a target entity by observing the occurrence of a detectable signal, such as a radiologic or spectroscopic signal that will appear exclusively in the presence of the target entity.  
      As used herein, the term “sequencing” means determining the ordered linear sequence of nucleic acids or amino acids of a DNA or protein target sample, using conventional manual or automated laboratory techniques.  
      As used herein, the term “isolated” means oligonucleotides substantially free of other nucleic acids, proteins, lipids, carbohydrates or other materials with which they can be associated, such association being either in cellular material or in a synthesis medium. The term can also be applied to polypeptides, in which case the polypeptide will be substantially free of nucleic acids, carbohydrates, lipids and other undesired polypeptides.  
      As used herein, the term “substantially pure” means that the polynucleotide or polypeptide is substantially free of the sequences and molecules with which it is associated in its natural state, and those molecules used in the isolation procedure. The term “substantially free” means that the sample is at least 50%, preferably at least 70%, more preferably 80% and most preferably 90% free of the materials and compounds with which is it associated in nature.  
      As used herein, the term “primer” means a sequence comprising two or more deoxyribonucleotides or ribonucleotides, preferably more than three, and more preferably more than eight and most preferably at least about 20 nucleotides of an exonic or intronic region. Such oligonucleotides are preferably between ten and thirty bases in length.  
      As used herein, the term “DNA segment” means a DNA molecule that has been isolated free of total genomic DNA of a particular species. In a preferred embodiment, a DNA segment encoding an HNF4 polypeptide refers to a DNA segment that contains SEQ ID NO:1, but can optionally comprise fewer or additional nucleic acids, yet is isolated away from, or purified free from, total genomic DNA of a source species, such as  Homo sapiens . Included within the term “DNA segment” are DNA segments and smaller fragments of such segments, and also recombinant vectors, including, for example, plasmids, cosmids, phages, viruses, and the like.  
      As used herein, the phrase “enhancer-promoter” means a composite unit that contains both enhancer and promoter elements. An enhancer-promoter is operatively linked to a coding sequence that encodes at least one gene product.  
      As used herein, the phrase “operatively linked” means that an enhancer-promoter is connected to a coding sequence in such a way that the transcription of that coding sequence is controlled and regulated by that enhancer-promoter. Techniques for operatively linking an enhancer-promoter to a coding sequence are well known in the art; the precise orientation and location relative to a coding sequence of interest is dependent, inter alia, upon the specific nature of the enhancer-promoter.  
      As used herein, the terms “candidate substance” and “candidate compound” are used interchangeably and refer to a substance that is believed to interact with another moiety, for example a given ligand that is believed to interact with a complete, or a fragment of, an HNF4 polypeptide, and which can be subsequently evaluated for such an interaction. Representative candidate substances or compounds include xenobiotics such as drugs and other therapeutic agents, carcinogens and environmental pollutants, natural products and extracts, as well as endobiotics such as steroids, fatty acids and prostaglandins. Other examples of candidate compounds that can be investigated using the methods of the present invention include, but are not restricted to, agonists and antagonists of an HNF4 polypeptide, toxins and venoms, viral epitopes, hormones (e.g., opioid peptides, steroids, etc.), hormone receptors, peptides, enzymes, enzyme substrates, co-factors, lectins, sugars, oligonucleotides or nucleic acids, oligosaccharides, proteins, small molecules and monoclonal antibodies.  
      As used herein, the term “biological activity” means any observable effect flowing from interaction between an HNF4 polypeptide and a ligand. Representative, but non-limiting, examples of biological activity in the context of the present invention include homodimerization of an HNF4, lipid binding by HNF4 and association of an HNF4 with DNA.  
      As used herein, the term “modified” means an alteration from an entity&#39;s normally occurring state. An entity can be modified by removing discrete chemical units or by adding discrete chemical units. The term “modified” encompasses detectable labels as well as those entities added as aids in purification.  
      As used herein, the terms “structure coordinates” and “structural coordinates” mean mathematical coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of a molecule in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are used to establish the positions of the individual atoms within the unit cell of the crystal.  
      Those of skill in the art understand that a set of structure coordinates determined by X-ray crystallography is not without standard error. For the purpose of this invention, any set of structure coordinates for HNF4γ or an HNF4γ mutant that have a root mean square (RMS) deviation from ideal of no more than 0.5 Å when superimposed, using the polypeptide backbone atoms, on the structure coordinates listed in Table 2 shall be considered identical.  
      As used herein, the term “space group” means the arrangement of symmetry elements of a crystal.  
      As used herein, the term “molecular replacement” means a method that involves generating a preliminary model of the wild-type HNF4γ ligand binding domain, or an HNF4γ mutant crystal whose structure coordinates are unknown, by orienting and positioning a molecule whose structure coordinates are known within the unit cell of the unknown crystal so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. This, in turn, can be subject to any of the several forms of refinement to provide a final, accurate structure of the unknown crystal. See, e.g., Lattman, (1985)  Method Enzymol.,  115: 55-77; Rossmann, ed, (1972)  The Molecular Replacement Method , Gordon &amp; Breach, New York.) Using the structure coordinates of the ligand binding domain of HNF4γ provided by this invention, molecular replacement can be used to determine the structure coordinates of a crystalline mutant or homologue of the HNF4γ ligand binding domain, or of a different crystal form of the HNF4γ ligand binding domain.  
      As used herein, the term “isomorphous replacement” means a method of using heavy atom derivative crystals to obtain the phase information necessary to elucidate the three-dimensional structure of a native crystal (Blundell et al., (1976)  Protein Crystallography , Academic Press; Otwinowski, (1991), in  Isomorphous Replacement and Anomalous Scattering , (Evans &amp; Leslie, eds.), pp. 80-86, Daresbury Laboratory, Daresbury, United Kingdom). The phrase “heavy-atom derivatization” is synonymous with the term “isomorphous replacement”.  
      As used herein, the terms “β-sheet” and “beta-sheet” mean the conformation of a polypeptide chain stretched into an extended zig-zig conformation. Portions of polypeptide chains that run “parallel” all run in the same direction. Polypeptide chains that are “antiparallel” run in the opposite direction from the parallel chains.  
      As used herein, the terms “α-helix” and “alpha-helix” mean the conformation of a polypeptide chain wherein the polypeptide backbone is wound around the long axis of the molecule in a left-handed or right-handed direction, and the R groups of the amino acids protrude outward from the helical backbone, wherein the repeating unit of the structure is a single turnoff the helix, which extends about 0.56 nm along the long axis.  
      As used herein, the term “unit cell” means a basic parallelepiped shaped block. The entire volume of a crystal can be constructed by regular assembly of such blocks. Each unit cell comprises a complete representation of the unit of pattern, the repetition of which builds up the crystal. Thus, the term “unit cell” means the fundamental portion of a crystal structure that is repeated infinitely by translation in three dimensions. A unit cell is characterized by three vectors a, b, and c, not located in one plane, which form the edges of a parallelepiped. Angles α, β and γ define the angles between the vectors: angle α is the angle between vectors b and c; angle β is the angle between vectors a and c; and angle γ is the angle between vectors a and b. The entire volume of a crystal can be constructed by regular assembly of unit cells; each unit cell comprises a complete representation of the unit of pattern, the repetition of which builds up the crystal.  
      As used herein, the term “tetragonal unit cell” means a unit cell wherein a=b≠c; and α=β=γ=90°. The vectors a, b and c describe the unit cell edges and the angles α, β, and γ describe the unit cell angles.  
      As used herein, the term “crystal lattice” means the array of points defined by the vertices of packed unit cells.  
      As used herein, the term “active site” means that site in a polypeptide where substrate binding occurs. For HNF4γ, the active site comprises the residues Ile135, Val138, Cys139, Ser141, Met142, Gln145, Leu179, Leu180, Gly182, Ala183, Arg186, Leu194, Leu196, Gly197, Ile202, Glu210, Ile211, Val214, Ala215, Val218, Met301, Gln304, Ile305, Val308, Val314, Ile316 and Leu320.  
      As used herein, the term “HNF4” means nucleic acids encoding a hepatocyte nuclear factor 4 (HNF4) nuclear receptor polypeptide that can bind DNA and/or one or more ligands and/or has the ability to form multimers. The term “HNF4” encompasses at least the HNF4α and HNF4γ isoforms. The term “HNF4” includes invertebrate homologs; however, preferably, HNF4 nucleic acids and polypeptides are isolated from vertebrate sources. “HNF4” further includes vertebrate homologs of HNF4 family members, including, but not limited to, mammalian and avian homologs. Representative mammalian homologs of HNF4 family members include, but are not limited to, murine and human homologs.  
      As used herein, the terms “HNF4 gene product”, “HNF4 protein”, “HNF4 polypeptide”, and “HNF4 peptide” are used interchangeably and mean peptides having amino acid sequences which are substantially identical to native amino acid sequences from an organism of interest and which are biologically active in that they comprise all or a part of the amino acid sequence of an HNF4 polypeptide, or cross-react with antibodies raised against an HNF4 polypeptide, or retain all or some of the biological activity (e.g., DNA or ligand binding ability and/or dimerization ability) of the native amino acid sequence or protein. Such biological activity can include immunogenicity.  
      As used herein, the terms “HNF4 gene product”, “HNF4 protein”, “HNF4 polypeptide”, and “HNF4 peptide” also include analogs of an HNF4 polypeptide. By “analog” is intended that a DNA or peptide sequence can contain alterations relative to the sequences disclosed herein, yet retain all or some of the biological activity of those sequences. Analogs can be derived from genomic nucleotide sequences as are disclosed herein or from other organisms, or can be created synthetically. Those skilled in the art will appreciate that other analogs, as yet undisclosed or undiscovered, can be used to design and/or construct HNF4 analogs. There is no need for an “HNF4 gene product”, “HNF4 protein”, “HNF4 polypeptide”, or “HNF4 peptide” to comprise all or substantially all of the amino acid sequence of an HNF4 polypeptide gene product. Shorter or longer sequences are anticipated to be of use in the invention; shorter sequences are herein referred to as “segments”. Thus, the terms “HNF4 gene product”, “HNF4 protein”, “HNF4 polypeptide”, and “HNF4 peptide” also include fusion, chimeric or recombinant HNF4 polypeptides and proteins comprising sequences of the present invention. Methods of preparing such proteins are disclosed herein and are known in the art.  
      In the present invention, the terms “HNF4γ gene product”, “HNF4γ protein”, “HNF4γ polypeptide”, and “HNF4γ peptide” are used interchangeably and mean to a preferred isoform of an HNF4 polypeptide family, namely HNF4γ. A more preferred embodiment of an HNF4γ polypeptide comprises the amino acid sequence of SEQ ID NO:2.  
      As used herein, the term “polypeptide” means any polymer comprising any of the 20 protein amino acids, regardless of its size. Although “protein” is often used in reference to relatively large polypeptides, and “peptide” is often used in reference to small polypeptides, usage of these terms in the art overlaps and varies. The term “polypeptide” as used herein refers to peptides, polypeptides and proteins, unless otherwise noted. As used herein, the terms “protein”, “polypeptide” and “peptide” are used interchangeably herein when referring to a gene product.  
      As used herein, the term “modulate” means an increase, decrease, or other alteration of any or all chemical and biological activities or properties of a wild-type or mutant HNF4 polypeptide, preferably a wild-type or mutant HNF4γ polypeptide. The term “modulation” as used herein refers to both upregulation (i.e., activation or stimulation) and downregulation (i.e. inhibition or suppression) of a response.  
      As used herein, the term “diabetes” means disorders related to alterations in glucose homeostasis. In the mildest forms of diabetes, this alteration is detected only after challenge with a carbohydrate load, while in moderate to severe forms of disease, hyperglycemia is present. Type I diabetes, insulin dependent diabetes mellitus or IDDM, is the result of a progressive autoimmune destruction of the pancreatic β-cells with subsequent insulin deficiency. The more prevalent Type II, non-insulin dependent diabetes mellitus or NIDDM, is associated with peripheral insulin resistance, elevated hepatic glucose production, and inappropriate insulin secretion. Type II diabetes that develops during the age of 20-30 years old and is associated with chronic hyperglycemia and monogenic inheritance is referred to as maturity onset diabetes of the young (MODY, Type II). Other forms of Type II diabetes develop in an individual sometime after 20-30 years of age, for example, late-onset NIDDM. HNF4α is linked to MODY I.  
      As used herein, the terms “HNF4 gene” and “recombinant HNF4 gene” mean a nucleic acid molecule comprising an open reading frame encoding an HNF4 polypeptide of the present invention, including both exon and (optionally) intron sequences.  
      As used herein, the term “gene” is used for simplicity to refer to a functional protein, polypeptide or peptide encoding unit. As will be understood by those in the art, this functional term includes both genomic sequences and cDNA sequences. Preferred embodiments of genomic and cDNA sequences are disclosed herein.  
      As used herein, the term “DNA sequence encoding an HNF4 polypeptide” can refer to one or more coding sequences within a particular individual. Moreover, certain differences in nucleotide sequences can exist between individual organisms, which are called alleles. It is possible that such allelic differences might or might not result in differences in amino acid sequence of the encoded polypeptide yet still encode a protein with the same biological activity. As is well known, genes for a particular polypeptide can exist in single or multiple copies within the genome of an individual. Such duplicate genes can be identical or can have certain modifications, including nucleotide substitutions, additions or deletions, all of which still code for polypeptides having substantially the same activity.  
      As used herein, the term “intron” means a DNA sequence present in a given gene which is not translated into protein.  
      As used herein, the term “interact” means detectable interactions between molecules, such as can be detected using, for example, a yeast two hybrid assay. The term “interact” is also meant to include “binding” interactions between molecules. Interactions can, for example, be protein-protein or protein-nucleic acid in nature.  
      As used herein, the terms “cells,” “host cells” or “recombinant host cells” are used interchangeably and mean not only to the particular subject cell, but also to the progeny or potential progeny of such a cell. Because certain modifications can occur in succeeding generations due to either mutation or environmental influences, such progeny might not, in fact, be identical to the parent cell, but are still included within the scope of the term as used herein.  
      As used herein, the term “agonist” means an agent that supplements or potentiates the bioactivity of a functional HNF4 gene or protein or of a polypeptide encoded by a gene that is up- or down-regulated by an HNF4 polypeptide and/or a polypeptide encoded by a gene that contains an HNF4 binding site in its promoter region.  
      As used herein, the term “antagonist” means an agent that decreases or inhibits the bioactivity of a functional HNF4 gene or protein, or that supplements or potentiates the bioactivity of a naturally occurring or engineered non-functional HNF4 gene or protein. Alternatively, an antagonist can decrease or inhibit the bioactivity of a functional gene or polypeptide encoded by a gene that is up- or down-regulated by an HNF4 polypeptide and/or contains an HNF4 binding site in its promoter region. An antagonist can also supplement or potentiate the bioactivity of a naturally occurring or engineered non-functional gene or polypeptide encoded by a gene that is up- or down-regulated by an HNF4 polypeptide, and/or contains an HNF4 binding site in its promoter region.  
      As used herein, the terms “chimeric protein” or “fusion protein” are used interchangeably and mean a fusion of a first amino acid sequence encoding an HNF4 polypeptide with a second amino acid sequence defining a polypeptide domain foreign to, and not homologous with, any domain of one of an HNF4 polypeptide. A chimeric protein can present a foreign domain which is found in an organism which also expresses the first protein, or it can be an “interspecies” or “intergenic” fusion of protein structures expressed by different kinds of organisms. In general, a fusion protein can be represented by the general formula X—HNF4—Y, wherein HNF4 represents a portion of the protein which is derived from an HNF4 polypeptide, and X and Y are independently absent or represent amino acid sequences which are not related to an HNF4 sequence in an organism, which includes naturally occurring mutants.  
      II. Description of Tables  
      Table 1 is a table summarizing the crystal and data statistics obtained from the crystallized ligand binding domain of HNF4γ. Data on the unit cell are presented, including data on the crystal space group, unit cell dimensions, molecules per asymmetric cell and crystal resolution.  
      Table 2 is a table of the atomic structure coordinate data obtained from X-ray diffraction from the ligand binding domain of HNF4γ in complex with a ligand.  
      Table 3 is a table depicting a sequence alignment comparing HNF4γ and HNF4α. Boxed HNF4γ residues are in alpha helices, shaded HNF4γ residues are in beta strands. Bold HNF4γ residues are thoser residues that have the potential to form Van der Waals&#39;s contacts (5Å) with palmitic acid; bold and underlined HNF4γ residues form hydrogen bonds to palmitic acid. Underlined HNF4α residues are mutations associated with the disease MODY 1.  
      Table 4 is a table summarizing data obtained from analytes detected by GC/MS using chemical ionization  
      III. General Considerations  
      Hepatocyte nuclear factor cDNAs code for several different genes and map to different chromosomes. HNF1 maps to chromosome 12, vHNF1 maps to chromosome 17, HNF4α maps to chromosome 20 and HNF4γ maps to chromosome 8. HNF1 and vHNF1 are homologous to each other, regulate several of the same genes and have similar tissues expression patterns. HNF4α and HNF4γ are also homologous to each other. Additionally, HNF4α and HNF4γ have an overlapping, but not identical expression pattern. The existence of multiple isoforms of the HNF4 polypeptide could explain the complex forms of regulation controlled by these transcription factors in different tissues. The redundancy of these transcription factors suggests the possibility of biological complementation by these genes, with respect to each other; when one isoform is defective, for example in a subject afflicted with diabetes, the other isoform could compensate.  
      The present invention will usually be applicable mutatis mutandis to all HNF4 polypeptides, as discussed herein based, in part, on the patterns of HNF4 structure and modulation that have emerged as a consequence of determining the three dimensional structure of HNF4γ in complex with a ligand. Generally, the HNF4s display substantial regions of amino acid homology. Additionally, the HNF4s display an overall structural motif comprising three modular domains: 
          1) a variable amino-terminal domain;     2) a highly conserved DNA-binding domain (DBD); and     3) a less conserved carboxy-terminal ligand binding domain (LBD). 
 
 The modularity of the HNF4s permits different domains of each protein to separately accomplish different functions, although the domains can influence each other. The separate function of a domain is usually preserved when a particular domain is isolated from the remainder of the protein. Using conventional protein chemistry techniques, a modular domain can sometimes be separated from the parent protein. Using conventional molecular biology techniques, each domain can usually be separately expressed with its original function intact or, as discussed herein below, chimeric proteins comprising two different proteins can be constructed, wherein the chimeric proteins retain the properties of the individual functional domains of the respective polypeptides from which the chimeric proteins were generated. 
       

      The amino terminal domain of the HNF4 isoforms is the least conserved of the three domains. This domain is involved in transcriptional activation and, in some cases, its uniqueness can dictate selective receptor-DNA binding and activation of target genes by HNF4 isoforms.  
      The DNA binding domain is the most conserved structure amongst the HNF4s. It typically contains about 70 amino acids that fold into two zinc finger motifs, wherein a zinc ion coordinates four cysteines. The DBD contains two perpendicularly oriented α-helices that extend from the base of the first and second zinc fingers. The two zinc fingers function in concert along with non-zinc finger residues to direct the HNF4s to specific target sites on DNA. Various amino acids in the DBD influence spacing between two half-sites (which usually comprises six nucleotides) for receptor homodimerization. The optimal spacings facilitate cooperative interactions between DBDs, and D box residues are part of the dimerization interface. Other regions of the DBD facilitate DNA-protein and protein-protein interactions required for HNF4 homodimerization.  
      The LBD is the second most highly conserved domain in these receptors. Whereas the integrity of several different LBD sub-domains is important for ligand binding, truncated molecules containing only the LBD can retain normal ligand binding activity. This domain also participates in other functions, including dimerization, nuclear translocation and transcriptional regulation activities. Importantly, this domain can bind a ligand and can undergo ligand-induced conformational changes. Ligand binding allows the activation domain to serve as an interaction site for essential co-activator proteins that function to stimulate or inhibit transcription.  
      The carboxy-terminal activation subdomain is in close three-dimensional proximity in the LBD to the ligand, so as to allow for ligands bound to the LBD to coordinate (or interact) with amino acid(s) in the activation subdomain. As disclosed herein, the LBD of an HNF4 is expressed, crystallized and its three dimensional structure determined. Computational and other methods for the design of ligands to the LBD are also disclosed.  
      IV. Production of HNF4 Polypeptides  
      The native and mutated HNF4 polypeptides, and fragments thereof, of the present invention can be chemically synthesized in whole or part using techniques that are well-known in the art (See, e.g., Creighton, (1983)  Proteins: Structures and Molecular Principles , W.H. Freeman &amp; Co., New York, incorporated herein in its entirety). Alternatively, methods which are well known to those skilled in the art can be used to construct expression vectors containing a partial or the entire native or mutated HNF4 polypeptide coding sequence and appropriate transcriptional/translational control signals. These methods include in vitro recombinant DNA techniques, synthetic techniques and in vivo recombination/genetic recombination. See, for example, the techniques described in Sambrook et al., (1989)  Molecular Cloning: A Laboratory Manual , Cold Spring Harbor Laboratory, New York, and Ausubel et al., (1989)  Current Protocols in Molecular Biology , Greene Publishing Associates and Wiley Interscience, New York, both incorporated herein in their entirety.  
      A variety of host-expression vector systems can be utilized to express an HNF4 coding sequence. These include but are not limited to microorganisms such as bacteria transformed with recombinant bacteriophage DNA, plasmid DNA or cosmid DNA expression vectors containing an HNF4 coding sequence; yeast transformed with recombinant yeast expression vectors containing an HNF4 coding sequence; insect cell systems infected with recombinant virus expression vectors (e.g., baculovirus) containing an HNF4 coding sequence; plant cell systems infected with recombinant virus expression vectors (e.g., cauliflower mosaic virus, CaMV; tobacco mosaic virus, TMV) or transformed with recombinant plasmid expression vectors (e.g., Ti plasmid) containing an HNF4 coding sequence; or animal cell systems. The expression elements of these systems vary in their strength and specificities.  
      Depending on the host/vector system utilized, any of a number of suitable transcription and translation elements, including constitutive and inducible promoters, can be used in the expression vector. For example, when cloning in bacterial systems, inducible promoters such as pL of bacteriophage λ, plac, ptrp, ptac (ptrp-lac hybrid promoter) and the like can be used. When cloning in insect cell systems, promoters such as the baculovirus polyhedrin promoter can be used. When cloning in plant cell systems, promoters derived from the genome of plant cells, such as heat shock promoters; the promoter for the small subunit of RUBISCO; the promoter for the chlorophyll a/b binding protein) or from plant viruses (e.g., the  35 S RNA promoter of CaMV; the coat protein promoter of TMV) can be used. When cloning in mammalian cell systems, promoters derived from the genome of mammalian cells (e.g., metallothionein promoter) or from mammalian viruses (e.g., the adenovirus late promoter; the vaccinia virus 7.5 K promoter) can be used. When generating cell lines that contain multiple copies of the tyrosine kinase domain DNA, SV40-, BPV- and EBV-based vectors can be used with an appropriate selectable marker.  
      V. Formation of HNF4γ Ligand Binding Domain Crystals  
      In one embodiment, the present invention provides crystals of HNF4γ. The crystals were obtained using the methodology disclosed in the Examples. The HNF4γ crystals, which can be native crystals, derivative crystals or co-crystals, have tetragonal unit cells (a tetragonal unit cell is a unit cell wherein a=b≠c, and wherein α=β=γ=90°) and space group symmetry 14 1 22. There is one HNF4γ molecule in the asymmetric unit. In the HNF4γ crystalline form, the unit cell has dimensions of a=b=152.71 c=93.42, and α=β=γ=90°.  
      The HNF4γ LBD-ligand structure was solved using single isomorphous replacement anomalous scattering (SIRAS) techniques. In the SIRAS method of solving protein crystals, a derivative crystal is prepared that contains an atom that is heavier than the other atoms of the sample. One representative heavy atom that can be incorporated into the derivative crystal is mercury. A mercury-based heavy atom derivative crystal was used to solve the structure of the HNF4γ ligand binding domain of the present invention. Heavy atom derivative crystals can be prepared by soaking a crystal in a solution containing a selected heavy atom salt. In the present invention, heavy atom derivative crystals were prepared by soaking a crystalline form of the HNF4γ LBD in methyl mercury chloride (MeHgCl).  
      Symmetry-related reflections in the X-ray diffraction pattern, usually identical, are altered by the anomalous scattering contribution of the heavy atoms. The measured differences in symmetry-related reflections are used to determine the position of the heavy atoms, leading to an initial estimation of the diffraction phases, and subsequently, an electron density map is prepared. The prepared electron density map is then used to identify the position of the other atoms in the sample.  
      V.A. Preparation of HNF4 Crystals  
      The native and derivative co-crystals, and fragments thereof, disclosed in the present invention can be obtained by a variety of techniques, including batch, liquid bridge, dialysis, vapor diffusion and hanging drop methods (See, e.g., McPherson, (1982)  Preparation and Analysis of Protein Crystals , John Wiley, New York.; McPherson, (1990)  Eur. J. Biochem.  189:1-23.; Weber, (1991)  Adv. Protein Chem.  41:1-36). In a preferred embodiment, the vapor diffusion and hanging drop methods are used for the crystallization of HNF4 polypeptides and fragments thereof.  
      In general, native crystals of the present invention are grown by dissolving substantially pure HNF4 polypeptide or a fragment thereof in an aqueous buffer containing a precipitant at a concentration just below that necessary to precipitate the protein. Water is removed by controlled evaporation to produce precipitating conditions, which are maintained until crystal growth ceases.  
      In a preferred embodiment of the invention, native crystals are grown by vapor diffusion (See, e.g., McPherson, (1982)  Preparation and Analysis of Protein Crystals , John Wiley, New York.; McPherson, (1990)  Eur. J. Biochem.  189:1-23). In this method, the polypeptide/precipitant solution is allowed to equilibrate in a closed container with a larger aqueous reservoir having a precipitant concentration optimal for producing crystals. Generally, less than about 25 μL of HNF4 polypeptide solution is mixed with an equal volume of reservoir solution, giving a precipitant concentration about half that required for crystallization. This solution is suspended as a droplet underneath a coverslip, which is sealed onto the top of the reservoir. The sealed container is allowed to stand, until crystals grow. Crystals generally form within two to six weeks, and are suitable for data collection within approximately seven to ten weeks. Of course, those of skill in the art will recognize that the above-described crystallization procedures and conditions can be varied.  
      V.B. Preparation of Derivative Crystals  
      Derivative crystals of the present invention, e.g. heavy atom derivative crystals, can be obtained by soaking native crystals in mother liquor containing salts of heavy metal atoms. Such derivative crystals are useful for phase analysis in the solution of crystals of the present invention. In a preferred embodiment of the present invention, for example, soaking a native crystal in a solution containing methyl-mercury chloride provides derivative crystals suitable for use as isomorphous replacements in determining the X-ray crystal structure of an HNF4 polypeptide. Additional reagents useful for the preparation of the derivative crystals of the present invention will be apparent to those of skill in the art after review of the disclosure of the present invention presented herein.  
      V.C. Preparation of Co-Crystals  
      Co-crystals of the present invention can be obtained by soaking a native crystal in mother liquor containing compounds known or predicted to bind the LBD of an HNF4, or a fragment thereof. Alternatively, co-crystals can be obtained by co-crystallizing an HNF4 LBD polypeptide or a fragment thereof in the presence of one or more compounds known or predicted to bind the polypeptide. In a preferred embodiment, such a compound is a fatty acid of variable length.  
      V.D. Solving a Crystal Structure of the Present Invention  
      Crystal structures of the present invention can be solved using a variety of techniques including, but not limited to, isomorphous replacement anomalous scattering or molecular replacement methods. Computer software packages will also be helpful in solving a crystal structure of the present invention. Applicable software packages include but are not limited to X-PLOR™ program (Brünger, (1992)  X - PLOR, Version  3.1 . A System for X - ray Crystallography and NMR , Yale University Press, New Haven, Conn.; X-PLOR is available from Molecular Simulations, Inc., San Diego, Calif.), Xtal View (McRee, (1992)  J. Mol. Graphics  10: 44-47; X-tal View is available from the San Diego Supercomputer Center), SHELXS 97 (Sheldrick (1990)  Acta Cryst. A 46: 467; SHELX 97 is available from the Institute of Inorganic Chemistry, Georg-August-Universitat, Göttingen, Germany), HEAVY (Terwilliger, Los Alamos National Laboratory) can be used and SHAKE-AND-BAKE (Hauptman, (1997)  Curr. Opin. Struct. Biol.  7: 672-80; Weeks et al., (1993)  Acta Cryst . D49: 179; available from the Hauptman-Woodward Medical Research Institute, Buffalo, N.Y.). See also, Ducruix &amp; Geige, (1992)  Crystallization of Nucleic Acids and Proteins: A Practical Approach , IRL Press, Oxford, England, and references cited therein.  
      VI. Summary of Results for the HNF4γ Ligand Binding Domain  
      The three-dimensional structure of the HNF4γ LBD has been solved by X-ray crystallography and is depicted in  FIG. 1A . The structure of HNF4γ is shown to contain the characteristic ligand binding pocket observed for “classic” nuclear receptors. The ligand binding pocket is depicted in  FIG. 2 . The long HNF4γ F-domain was present in the crystals but was disordered, suggesting that it did not make strong interactions with the core residues of the LBD. The HNF4γ LBD induces obligate homodimerization due to deviations from the conserved heterodimer motif. The structure of HNF4γ revealed a bound ligand. The identity of this ligand was determined to be the fatty acids palmitic acid and stearic acid by GC/EI/MS. The saturated fatty acids palmitic acid and stearic acid were shown to be functional activators for two HNF4 isoforms, HNF4α and HNF4γ, using a FRET assay to detect CBP peptide recruitment.  FIG. 3  depicts the results of the FRET assay. Shorter fatty acids had no effect on CBP peptide recruitment. Fatty acyl CoA derivatives of palmitic acid and stearic acid had a small negative effect on CBP recruitment, suggesting that they were not activators for HNF4α or HNF4γ.  
      VI.A. Overall Structure of the HNF41 LBD  
      The overall fold of the HNF4γ LBD of the present invention is an “α-helical sandwich”, is depicted in  FIG. 1A , is similar to that observed in other nuclear receptor LBDs, and is most similar to holo-RXRα (Bourguet et al., (2000)  Mol. Cell  5: 289-98; Gampe, Jr. et al., (2000) Mol. Cell 5: 545-55). Although mass spectrometry confirmed that crystals contained full length HNF4γ LBD (amino acids 102408), only amino acids 102-118 and 123-327 are visible in the electron density map. These residues comprise the “core” LBD, and contain the conserved structural motifs observed in other nuclear receptor LBD&#39;s. The observation that the HNF4γ C-terminal tail is disordered suggests that the strong interactions between the “core” LBD and the C-terminal tail seen in PR and AR are absent in HNF4. The AF2 helix of HNF4γ (amino acids 316-325) is in the “active” conformation, characteristic of other agonist-bound nuclear receptors.  
      VI.B. Structural Features of the Dimerization Site  
      The HNF4γ homodimer interface is composed of residues in helices 7, 9 and 10, and is the same interface seen in other nuclear receptor homo- and heterodimers (Bourguet et al., (1995)  Nature  375: 377-82; Brzozowski et al., (1997)  Nature  (London) 389: 753-58; Nolte et al., (1998)  Nature  (London) 395: 1374, (Bourguet et al., (2000)  Mol. Cell  5: 289-98; Gampe, Jr. et al., (2000)  Mol. Cell  5: 545-55). Of the 22 residues involved in HNF4γ dimerization, 20 are conserved in HNF4α, and all charged residues in the HNF4γ dimer interface are identical in HNF4α. This homodimer interface exemplifies themes seen in other nuclear receptor dimers, buried hydrophobic surface for stability, with hydrogen bonds and charge-pairing for specificity. As a dimer HNF4γ buries 1320 Å 2  of accessible surface per monomer, between the 1266 Å 2  and 1632 Å 2  observed for RXRα and ERα homodimers, respectively. The HNF4γ homodimer interface includes specific side-chain/side-chain interactions, with hydrogen bonds between Q266Nε-E2860ε and Q295Oε-Q295Nε and salt bridges between E228Oε-K259Nζand possibly D271Oδ-R281Nε, and R281NH. HNF4/RXR heterodimer formation is prevented by LBD interactions (Jiang &amp; Sladek, (1997)  J. Biol. Chem.  272: 1218-25), and LBD heterodimer formation is precluded because not all salt-bridges will form. The RXR equivalent to HNF4γ E228 and K259 are D359 and E390, respectively, so a heterodimer will create one salt bridge and one potentially unfavorable pairing. HNF4γ D271 and R281 are equivalent to RXRα A402 and P412, respectively, and no charge-pairing is possible. Also, the critical heterodimer salt bridge observed between RXRα R393 and PPARγ D441 cannot be made to HNF4, where the equivalent residue is a Thr. Our observation that the E228-K259 salt bridge is important for homodimer formation agrees with the work of Bogan et al. (Bogan et al., (2000)  J. Mol. Biol.  302: 831-851). Their results showed that wild-type HNF4α cannot form heterodimers with HNF4α mutants where residues E327 (γE286) and K300 (γK259) are changed to their RXR equivalents. The conservation of the interface residues between HNF4γ and HNF4α suggests that the HNF4α homodimer interface is similar to HNF4γ&#39;s. In fact, HNF4α/HNF4γ heterodimers could possibly exist in tissues where both are present.  
      VI.C. Structural Features of the HNF4γ Binding Pocket  
      The HNF4γ LBD has a well-defined ligand binding pocket, which is similar to the nuclear receptors RXR (Bourguet et al., (1995)  Nature  375: 377-82) and RAR (Renaud et al., (1995)  Nature  378: 681-89). The pocket volume, 476 Å 3 , is consistent with binding a small molecule ligand, and is hydrophobic over 76% of the pocket surface. Arginine 186, which is conserved among a number of nuclear receptors, occupies the same pocket position seen in retinoid X receptor (RXR), retinoic acid receptor (RAR), thyroid hormone receptor (TR), estrogen receptor (ER) and progesterone receptor (PR). In all previous structures, this binding-pocket arginine makes hydrogen bonds to oxygen atoms of bound ligands. HNF4γ&#39;s pocket is too narrow to accommodate steroids. Another prominent feature of the pocket is a direct contact between M142 in helix 3 and M301 in helix 11. This contact bridges the binding pocket, and effectively blocks direct ligand access to residues 318-325 in helix 12.  
      Palmitic acid forms hydrogen bonds with the side chain of arginine 186, and with the backbone nitrogen of glycine 197 (not shown). Alanine 215 corresponds to serine 256 in HNF4α. Because serine can form hydrogen bonds to the ligand, the specificity is different for the two receptor subtypes. GC/MS analyses of receptor extracts indicates that although HNF4α also binds palmitic and stearic acid, it preferentially binds different fatty acids. Valine 214 corresponds to valine 255 in HNF4α, and is one of the mutations associated with MODY, Type 1.  
      VI.D. Identification and Characterization of an HNF4α Binding Pocket Ligand  
      Electron density was observed in the HNF4γ binding pocket in the first solvent-flattened SIRAS map. During the course of refinement, the pocket density improved and appeared consistent with a thin curved ligand, depicted in  FIG. 1B . The ligand density starts adjacent to residue R186, curves around the M142-M301 bridge and proceeds towards HNF4γ residue V314.  
      The description of the bound ligand from the structural data led to the belief that the compound was a fatty acid. Analytical methods were used to obtain a definitive identification of the ligand. First, bound ligand(s) was separated from a purified preparation of HNF4γ LBD by liquid-liquid extraction (Folch et al., (1957) J. Biol. Chem. 226: 497-509). The extract was then treated with 3% (v/v) acetyl chloride in methanol. This reagent converts fatty acids to their corresponding fatty acid methyl esters (FAME). The derivatized sample was then analyzed by gas chromatography/mass spectrometry (GC/MS) using both electron impact ionization (EI) and chemical ionization (CI) in separate analyses. The constituents of the extract were identified by comparing the GC/MS data for the extract with data for standard fatty acids, acquired likewise.  
       FIG. 4  shows the total ion current (TIC) chromatogram from the analysis of the derivatized extract by GCMS with CI. A similar TIC chromatogram was obtained from the EI analysis as shown in  FIG. 6 . The CI mass spectra for peaks a through g all show a protonated molecular ion ([M+H] + ) along with a fragment ion at a mass-to-charge (m/z) value 32 Da below the protonated molecular ion. This fragmentation is common in CI mass spectra for FAME and represents the loss of methanol from the protonated methyl ester. The CI mass spectrum for peak c is shown in  FIG. 6 . It was identified as the methyl ester of palmitic acid.  
      A comparison of  FIG. 4  and  FIG. 6 , reveals that peaks a-g that were present in the TIC from the CI analysis were also present in the TIC from the EI analysis. The EI spectrum for peak c is shown in  FIG. 7  and shows the molecular ion for methyl palmitate at m/z 270. The 14 Da mass difference observed for the fragment ions in this spectrum is characteristic of EI mass spectra of long chain aliphatic compounds such as fatty acids. A similar fragmentation pattern was observed in the EI spectrum for all of peaks a through g.  
      Results of the GC/MS analyses show that the HNF4γ extract consisted of a mixture of fatty acids with palmitic acid as the most abundant component. Data from the CI analysis are summarized in Table 4. The second column lists the protonated molecular ion detected of each labeled peak in  FIG. 4 . The third column gives the predicted molecular weight of the free acid form for each component in the extract.  
      VI.E. Confirmation of the Functionality of the HNF4 Ligand by FRET Assay  
      To confirm that fatty acids were functional HNF4 ligands, HNF4α and HNF4γ were tested for their ability to recruit the nuclear receptor co-activator CREB binding protein, a known activation partner (Wang et al., (1998)  J. Biol. Chem.  273: 30847-50; Dell &amp; Hadzopoulou-Cladaras, (1999)  J. Biol. Chem.  274: 9013-21). A FRET (fluorescent resonance energy transfer) assay was employed using purified recombinant CREB-binding protein (CBP) and HNF4 LBD (Zhou et al., (1998)  Mol. Endocrinol.  12: 1594-1604). Long-chain fatty acids (LCFA) with increasing carbon lengths from 12 to 18 carbon methylene units were tested for their ability to modulate the association between HNF4 and CBP in a dose dependent manner. Saturated fatty acids with chains smaller than 16 carbons did not affect basal CBP association. Palmitic and stearic acids increased the allosteric interaction between CBP and HNF4, with apparent binding constants of 1 μM.  
      The reported ligands for HNF4α are fatty acyl-CoA thioesters (Hertz et al., (1998)  Nature  (London) 392: 512-16), which are much larger than other nuclear receptor ligands (Bogan et al., (1998)  Nat. Struct. Biol.  5: 679-81). When tested in the FRET assay, palmitoyl-CoA and steroyl-CoA decreased the basal level of CBP recruitment to both HNF4α and HNF4γ. Shorter fatty acyl-CoAs had no effect on CBP association. This behavior indicates that longer chain fatty-acyl CoA derivatives are not HNF4 agonists.  
      HNF4α is primarily expressed in the liver and pancreas and is regulated by fatty acids, indicating a link between fatty acid and glucose metabolism. There are known effects of free fatty acids on glucose-stimulated insulin secretion (GSIS), including an initial stimulatory effect (Stein et al., (1997)  J. Clin. Invest  100:398403; Dobbins et al., (1998a)  Diabetes  47:1613-18; Dobbins et al., (1998b)  J. Clin. Invest.  101:2370-76), followed by a decrease after long term exposure (Zhou &amp; Grill, (1994)  J. Clin. Invest.  93:870-76; Zhou &amp; Grill, (1995)  J. Clin. Endocrinol. Metab.  80:1584-90; Boliheimer et al., (1998)  J. Clin. Invest.  101:1094-1101; Biorklund &amp; Grill (1999)  Diabetes  48:1409-14; Jacqueminet et al., (2000)  Metab. Clin. Exp.  49:532-36). The observed negative effects of long term fatty acid exposure on pancreatic islet function (Zhou &amp; Grill, (1995)  J. Clin. Endocrinol Metab.  80:1584-90) are likely to be partially mediated by HNF4.  
      VI.F. Analysis of the HNF4α Ligand Binding Mode  
      Although fatty acids are ligands for both PPARs and HNF4s, the proposed binding mode and specificity are significantly different. The structure of EPA bound to PPARδ (Xu et al., (1999) MOL Cell 3: 397-403) showed that the acid head group hydrogen bonds to PPARδ residues H323, H449 and Y43 in the AF2 helix. In HNF4γ, the fatty acid head group most likely hydrogen bonds to residue R185 in helix 5, and possibly to G197, much like the acid-protein interactions observed in retinoid binding nuclear receptors (Bourguet et al., (2000) Mol. Cell  5: 289-98; Gampe, Jr. et al., (2000)  Mol. Cell  5: 545-55; Renaud et al., (1995) Nature 378: 681-89). The hydrophobic tail in the PPARδ/EPA complex can adopt two bent conformations, with the tail-up conformation pointing towards helix 5. In contrast, the hydrophobic tail in HNF4γ curves around the M142-M301 salt bridge and points towards the loop between helix 11 and the AF2 helix. Thus, the fatty acid in PPARδ binds in essentially the reverse orientation to that in HNF4γ.  
      The substrate specificity of the HNF4s is also markedly different from PPARs. The PPARs accept a wide range of fatty acids, but C18-20 mono- and poly-unsaturated fatty acids bind most tightly. Both HNF4s bind a much smaller range of substrates, with 16-18 carbon saturated fatty acids highly preferred. Thus, all HNF4 substrates are also bound by PPARα and PPARδ, but the converse is not true. The greater substrate specificity of HNF4 indicates a more specific role in the regulation of biological pathways.  
      VI.G Unique Structural Differences Between HNF4, and HNF4α 
      Without an atomic structure for HNF4α, the structure of HNF4γ can be considered in order to speculate on the design of isoform specific compounds. The solved structure of HNF4γ suggests that there is a potential for isoform specific ligand recognition based on amino acid differences between HNF4α and HNF4γ. Of the 26 amino acids in the binding pocket, 6 are different between HNF4γ and HNF4α. The substitution that can be directly exploited for designing isoform specific ligands is Ala215γ-Ser256α. This substitution adds a hydrogen bond donor near the C 8 -C 9  of palmitic acid, and represents a substantial change to the chemical character of the binding pocket. Compounds that make this hydrogen bond will preferentially bind to HNF4α. Alternatively, compounds with a bulky hydrophobic group in that position may clash sterically with the hydroxyl of serine, and would preferentially bind HNF4γ. Thus, the HNF4γ structure provides a roadmap for the design of isoform specific compounds.  
      Most of the substitutions between HNF4α and HNF4γ are conservative, exchanging one hydrophobic residue for another. These are Ile202γ-Val242α, Ile211γ-Met252α, Val218γ-Ile259α, Val308γ-Ile349α, and Val314γ-Ala355α. These substitutions have the effect of changing the shape of the binding pocket without altering its chemical characteristics greatly. Two of the substitutions that add mass to the binding pocket residues (Ile211γ-Met252α, Val218γ-Ile259α) occur along the curve of palmitic acid, and have the effect of restricting the pocket. This is partially offset by the substitution Ile202γ-Val242α near palmitic acid C 6 -C 8 , which enlarges a cavity in the binding pocket. The pair of substitutions Val308γ-Ile349α, and Val314γ-Ala355α occur near the paimitic acid tail, and direct the fatty acid tail more towards the loop connecting helix 11 and helix 12 (the AF2 helix), while expanding the pocket there. These shape changes to the binding pocket can also be exploited in the design of isoform specific compounds.  
      One other difference between HNF4γ and HNF4α that could change the characteristics of the binding pocket is that HNF4α has an extra residue, Ala250, in the loop between the beta turn and helix 7. This extra residue could slightly shift the positions of the residues in helix 7, i.e. Glu251, Met252, Val255, Ser256, and Ile259. However, modeling amino acid shifts caused by extra loop residues is more speculative than substitutions.  
      VI.H. Generation of Easily-Solved HNF4 Crystals  
      The present invention discloses a substantially pure HNF4 LBD polypeptide in crystalline form. In a preferred embodiment, exemplified in the Figures and Laboratory Examples, HNF4γ is crystallized with bound ligand. Crystals are formed from HNF4 LBD polypeptides that are usually expressed by a cell culture, such as  E. coli . Bromo-, iodo- and substitutions can be included during the preparation of crystal forms and can act as heavy atom substitutions in HNF4 ligands and crystals of HNF4s. This method can be advantageous for the phasing of the crystal, which is a crucial, and sometimes limiting, step in solving the three-dimensional structure of a crystallized entity. Thus, the need for generating the heavy metal derivatives traditionally employed in crystallography can be eliminated. After the three-dimensional structure of an HNF4 or HNF4 LBD with or without a ligand bound is determined, the resultant three-dimensional structure can be used in computational methods to design synthetic ligands for HNF4γ and other HNF4 polypeptides. Further activity structure relationships can be determined through routine testing, using assays disclosed herein and known in the art.  
      VII. Uses of HNF4γ Crystals and the Three-Dimensional Structure of the Ligand Bindina Domain of HNF4γ 
      VII.A. Design and Development of HNF4 Modulators  
      The knowledge of the structure of the HNF4γ ligand binding domain (LBD), an aspect of the present invention, provides a tool for investigating the mechanism of action of HNF4γ and other HNF4 polypeptides in a subject. For example, various computer models, as described herein, can predict the binding of various substrate molecules to the LBD of HNF4γ. Upon discovering that such binding in fact takes place, knowledge of the protein structure then allows design and synthesis of small molecules that mimic the functional binding of the substrate to the LBD of HNF4γ, and to the LBDs of other HNF4 polypeptides. This is the method of “rational” drug design, further described herein.  
      Use of the isolated and purified HNF4γ crystalline structure of the present invention in rational drug design is thus provided in accordance with the present invention. Additional rational drug design techniques are described in U.S. Pat. Nos. 5,834,228 and 5,872,011, incorporated herein in their entirety.  
      Thus, in addition to the compounds described herein, other sterically similar compounds can be formulated to mimic the key structural regions of an HNF4 in general, or of HNF4γ in particular. The generation of a structural functional equivalent can be achieved by the techniques of modeling and chemical design known to those of skill in the art and described herein. It will be understood that all such sterically similar constructs fall within the scope of the present invention.  
      VII.A.1. Rational Drug Design  
      The three-dimensional structure of the ligand binding domain of HNF4γ is unprecedented and will greatly aid in the development of new synthetic ligands for an HNF4 polypeptide, such as HNF4 agonists and antagonists, including those that bind exclusively to any one of the HNF4 isoforms. In addition, the HNF4s are well suited to modern methods, including three-dimensional structure elucidation and combinatorial chemistry, such as those disclosed in U.S. Pat. No. 5,463,564, incorporated herein by reference. Structure determination using X-ray crystallography is possible because of the solubility properties of the HNF4s. Computer programs that use crystallography data when practicing the present invention will enable the rational design of ligands to these receptors. Programs such as RASMOL (Biomolecular Structures Group, Glaxo Wellcome Research &amp; Development Stevenage, Hertfordshire, UK Version 2.6, August 1995, Version 2.6.4, December 1998, Copyright © Roger Sayle 1992-1999) can be used with the atomic structural coordinates from crystals generate by practicing the invention or used to practice the invention by generating three-dimensional models and/or determining the structures involved in ligand binding. Computer programs such as those sold under the registered trademark INSIGHT II® and such as GRASP (Nicholls et al., (1991)  Proteins  11: 282) allow for further manipulations and the ability to introduce new structures. In addition, high throughput binding and bioactivity assays can be devised using purified recombinant protein and modern reporter gene transcription assays known to those of skill in the art in order to refine the activity of a designed ligand.  
      A method of identifying modulators of the activity of an HNF4 polypeptide using rational drug design is thus provided in accordance with the present invention. The method comprises designing a potential modulator for an HNF4 polypeptide of the present invention that will form non-covalent bonds with amino acids in the ligand binding pocket based upon the crystalline structure of the HNF4γ LBD polypeptide; synthesizing the modulator; and determining whether the potential modulator modulates the activity of the HNF4 polypeptide. In a preferred embodiment, the modulator is designed for an HNF4γ polypeptide. Preferably, the HNF4γ polypeptide comprises the nucleic acid sequence of SEQ ID NO:1, and the HNF4γ LBD comprises the nucleic acid sequence SEQ ID NO:3. The determination of whether the modulator modulates the biological activity of an HNF4 polypeptide is made in accordance with the screening methods disclosed herein, or by other screening methods known to those of skill in the art. Modulators can be synthesized using techniques known to those of ordinary skill in the art.  
      In an alternative embodiment, a method of designing a modulator of an HNF4 polypeptide in accordance with the present invention is disclosed comprising: (a) selecting a candidate HNF4 ligand; (b) determining which amino acid or amino acids of an HNF4 polypeptide interact with the ligand using a three-dimensional model of a crystallized HNF4γ LBD; (c) identifying in a biological assay for HNF4 activity a degree to which the ligand modulates the activity of the HNF4 polypeptide; (d) selecting a chemical modification of the ligand wherein the interaction between the amino acids of the HNF4 polypeptide and the ligand is predicted to be modulated by the chemical modification; (e) performing the chemical modification on the ligand to form a modified ligand; (f) contacting the modified ligand with the HNF4 polypeptide; (g) identifying in a biological assay for HNF4 activity a degree to which the modified ligand modulates the biological activity of the HNF4 polypeptide; and (h) comparing the biological activity of the HNF4 polypeptide in the presence of modified ligand with the biological activity of the HNF4 polypeptide in the presence of the unmodified ligand, whereby a modulator of an HNF4 polypeptide is designed. present invention. The method comprises designing a potential modulator for an HNF4 polypeptide of the present invention that will form non-covalent bonds with amino acids in the ligand binding pocket based upon the crystalline structure of the HNF4γ LBD polypeptide; synthesizing the modulator; and determining whether the potential modulator modulates the activity of the HNF4 polypeptide. In a preferred embodiment, the modulator is designed for an HNF4γ polypeptide. Preferably, the HNF4γ polypeptide comprises the nucleic acid sequence of SEQ ID NO:1, and the HNF4γ LBD comprises the nucleic acid sequence SEQ ID NO:3. The determination of whether the modulator modulates the biological activity of an HNF4 polypeptide is made in accordance with the screening methods disclosed herein, or by other screening methods known to those of skill in the art. Modulators can be synthesized using techniques known to those of ordinary skill in the art.  
      In an alternative embodiment, a method of designing a modulator of an HNF4 polypeptide in accordance with the present invention is disclosed comprising: (a) selecting a candidate HNF4 ligand; (b) determining which amino acid or amino acids of an HNF4 polypeptide interact with the ligand using a three-dimensional model of a crystallized HNF4γ LBD; (c) identifying in a biological assay for HNF4 activity a degree to which the ligand modulates the activity of the HNF4 polypeptide; (d) selecting a chemical modification of the ligand wherein the interaction between the amino acids of the HNF4 polypeptide and the ligand is predicted to be modulated by the chemical modification; (e) performing the chemical modification on the ligand to form a modified ligand; (f) contacting the modified ligand with the HNF4 polypeptide; (g) identifying in a biological assay for HNF4 activity a degree to which the modified ligand modulates the biological activity of the HNF4 polypeptide; and (h) comparing the biological activity of the HNF4 polypeptide in the presence of modified ligand with the biological activity of the HNF4 polypeptide in the presence of the unmodified ligand, whereby a modulator of an HNF4 polypeptide is designed.  
      VII.A.2. Methods for Using the HNF4γ LBD Structural Coordinates for Molecular Design  
      For the first time, the present invention permits the use of molecular design techniques to design, select and synthesize chemical entities and compounds, including modulatory compounds, capable of binding to the ligand binding pocket or an accessory binding site of HNF4γ and the HNF4γ LBD, in whole or in part. Correspondingly, the present invention also provides for the application of similar techniques in the design of modulators of any HNF4 polypeptide.  
      In accordance with a preferred embodiment of the present invention, the structure coordinates of a crystalline HNF4γ LBD can be used to design compounds that bind to an HNF4 LBD (more preferably an HNF4γ LBD) and alter the properties of an HNF4 LBD (for example, the dimerization or ligand binding ability) in different ways. One aspect of the present invention provides for the design of compounds that act as competitive inhibitors of an HNF4 polypeptide by binding to all, or a portion of, the binding sites on an HNF4 LBD. The present invention also provides for the design of compounds that can act as uncompetitive inhibitors of an HNF4 LBD. These compounds can bind to all, or a portion of, an accessory binding site of an HNF4 that is already binding its ligand and can, therefore, be more potent and less non-specific than known competitive inhibitors that compete only for the HNF4 ligand binding pocket. Similarly, non-competitive inhibitors that bind to and inhibit HNF4 LBD activity, whether or not it is bound to another chemical entity, can be designed using the HNF4 LBD structure coordinates of this invention.  
      A second design approach is to probe an HNF4 or HNF4 LBD (preferably an HNF4γ or HNFγ LBD) crystal with molecules comprising a variety of different chemical entities to determine optimal sites for interaction between candidate HNF4 or HNF4 LBD modulators and the polypeptide. For example, high resolution X-ray diffraction data collected from crystals saturated with solvent allows the determination of the site where each type of solvent molecule adheres. Small molecules that bind tightly to those sites can then be designed and synthesized and tested for their HNF4γ modulator activity.  
      Once a computationally-designed ligand is synthesized using the methods of the present invention or other methods known to those of skill in the art, assays can be used to establish its efficacy of the ligand as a modulator of HNF4 (preferably HNF4γ) activity. After such assays, the ligands can be further refined by generating intact HNF4, or HNF4 LBD, crystals with a ligand bound to the LBD. The structure of the ligand can then be further refined using the chemical modification methods described herein and known to those of skill in the art, in order to improve the modulation activity or the binding affinity of the ligand. This process can lead to second generation ligands with improved properties.  
      Ligands also can be selected that modulate HNF4 responsive gene transcription by the method of altering the interaction of co-activators and co-repressors with their cognate HNF4. For example, agonistic ligands can be selected that block or dissociate a co-repressor from interacting with the HNF4, and/or that promote binding or association of a co-activator. Antagonistic ligands can be selected that block co-activator interaction and/or promote co-repressor interaction with a target receptor. Selection can be done via binding assays that screen for designed ligands having the desired modulatory properties. Preferably, interactions of an HNF4γ polypeptide are targeted. Suitable assays for screening that can be employed, mutatis mutandis in the present invention, are described in published PCT international applications WO 00/037,077 and WO 00/025,134, which are incorporated herein in their entirety by reference.  
      VII.A.3. Methods of Designing HNF4 LBD Modulator Compounds  
      The design of candidate substances, also referred to as “compounds” or “candidate compounds”, that bind to or inhibit HNF4 LBD-mediated activity according to the present invention generally involves consideration of two factors. First, the compound must be capable of physically and structurally associating with an HNF4 LBD. Non-covalent molecular interactions important in the association of an HNF4 LBD with its substrate include hydrogen bonding, van der Waals interactions and hydrophobic interactions.  
      Second, the compound must be able to assume a conformation that allows it to associate with an HNF4 LBD. Although certain portions of the compound will not directly participate in this association with an HNF4 LBD, those portions can still influence the overall conformation of the molecule. This, in turn, can have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity or compound in relation to all or a portion of the binding site, e.g., the ligand binding pocket or an accessory binding site of an HNF4 LBD, or the spacing between functional groups of a compound comprising several chemical entities that directly interact with an HNF4 LBD.  
      The potential modulatory or binding effect of a chemical compound on an HNF4 LBD can be analyzed prior to its actual synthesis and testing by the use of computer modeling techniques that employ the coordinates of a crystalline HNF4γ LBD polypeptide of the present invention. If the theoretical structure of the given compound suggests insufficient interaction and association between it and an HNF4 LBD, synthesis and testing of the compound is obviated. However, if computer modeling indicates a strong interaction, the molecule can then be synthesized and tested for its ability to bind and modulate the activity of an HNF4 LBD. In this manner, synthesis of unproductive or inoperative compounds can be avoided.  
      A modulatory or other binding compound of an HNF4 LBD polypeptide (preferably an HNF4γ LBD) can be computationally evaluated and designed via a series of steps in which chemical entities or fragments are screened and selected for their ability to associate with the individual binding sites or other areas of a crystalline HNF4γ LBD polypeptide of the present invention.  
      One of several methods can be used to screen chemical entities or fragments for their ability to associate with an HNF4 LBD and, more particularly, with the individual binding sites of an HNF4 LBD, such as ligand binding pocket or an accessory binding site. This process can begin by visual inspection of, for example, the ligand binding pocket on a computer screen based on the HNF4γ LBD atomic coordinates in Table 2. Selected fragments or chemical entities can then be positioned in a variety of orientations, or docked, within an individual binding site of an HNF4γ LBD as defined herein above. Docking can be accomplished using software programs such as those available under the tradenames QUANTA™ (Molecular Simulations Inc., San Diego, Calif.) and SYBYL™ (Tripos, Inc., St. Louis, Mo.), followed by energy minimization and molecular dynamics with standard molecular mechanics forcefields, such as CHARM (Brooks et al., (1983)  J. Comp. Chem.,  8: 132) and AMBER 5 (Case et al., (1997), AMBER 5, University of California, San Francisco; Pearlman et al., (1995)  Comput. Phys. Commun.  91: 1-41).  
      Specialized computer programs can also assist in the process of selecting fragments or chemical entities. These include: 
          1. GRID™ program, version 17 (Goodford, (1985)  J. Med. Chem.  28: 849-57), which is available from Molecular Discovery Ltd., Oxford, UK;     2. MCSS™ program (Miranker &amp; Karplus, (1991) Proteins 11: 29-34), which is available from Molecular Simulations, Inc., San Diego, Calif.;     3. AUTODOCK™ 3.0 program (Goodsell &amp; Olsen, (1990) Proteins 8: 195-202), which is available from the Scripps Research Institute, La Jolla, Calif.;     4. DOCK™ 4.0 program (Kuntz et al., (1992) J. Mol. Biol. 161: 269-88), which is available from the University of California, San Francisco, Calif.;     5. FLEX-X™ program (See, Rarey et al., (1996)  J. Comput Aid. Mol Des.  10:41-54), which is available from Tripos, Inc., St. Louis, Mo.;     6. MVP program (Lambert, (1997) in Practical Application of Computer-Aided Drug Design, (Charifson, ed.) Marcel-Dekker, New York, pp. 243-303); and     7. LUDI™ program (Bohm, (1992)  J. Comput Aid. Mol. Des.,  6: 61-78), which is available from Molecular Simulations, Inc., San Diego, Calif.        

      Once suitable chemical entities or fragments have been selected, they can be assembled into a single compound or modulator. Assembly can proceed by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of an HNF4γ LBD. Manual model building using software such as QUANTA™ or SYBYL™ typically follows.  
      Useful programs to aid one of ordinary skill in the art in connecting the individual chemical entities or fragments include: 
          1. CAVEAT™ program (Bartlett et al., (1989) Special Pub.,  Royal Chem. Soc.  78: 182-96), which is available from the University of California, Berkeley, Calif.;     2. 3D Database systems, such as MACCS-3D™ system program, which is available from MDL Information Systems, San Leandro, Calif.. This area is reviewed in Martin, (1992)  J. Med. Chem.  35: 2145-54; and     3. HOOK™ program (Eisen et al., (1994). Proteins 19: 199-221), which is available from Molecular Simulations, Inc., San Diego, Calif.        

      Instead of proceeding to build an HNF4 LBD modulator (preferably an HNF4γ LBD modulator) in a step-wise fashion one fragment or chemical entity at a time as described above, modulatory or other binding compounds can be designed as a whole or de novo using the structural coordinates of a crystalline HNF4γ LBD polypeptide of the present invention and either an empty binding site or optionally including some portion(s) of a known modulator(s). Applicable methods can employ the following software programs: 
          1. LUDI™ program (Bohm, (1992)  J. Comput. Aid. Mol. Des.,  6: 61-78), which is available from Molecular Simulations, Inc., San Diego, Calif.;     2. LEGEND™ program (Nishibata &amp; ltai, (1991)  Tetrahedron  47: 8985); and     3. LEAPFROG™, which is available from Tripos Associates, St. Louis, Mo.        

      Other molecular modeling techniques can also be employed in accordance with this invention. See, e.g., Cohen et al., (1990)  J. Med. Chem.  33: 883-94. See also, Navia &amp; Murcko, (1992)  Curr. Opin. Struc. Biol.  2: 202-10; U.S. Pat. No. 6,008,033, herein incorporated by reference.  
      Once a compound has been designed or selected by the above methods, the efficiency with which that compound can bind to an HNF4γ LBD can be tested and optimized by computational evaluation. By way of particular example, a compound that has been designed or selected to function as an HNF4γ LBD modulator should also preferably traverse a volume not overlapping that occupied by the binding site when it is bound to its native ligand. Additionally, an effective HNF4 LBD modulator should preferably demonstrate a relatively small difference in energy between its bound and free states (i.e., a small deformation energy of binding). Thus, the most efficient HNF4 LBD modulators should preferably be designed with a deformation energy of binding of not greater than about 10 kcal/mole, and preferably, not greater than 7 kcal/mole. It is possible for HNF4 LBD modulators to interact with the polypeptide in more than one conformation that is similar in overall binding energy. In those cases, the deformation energy of binding is taken to be the difference between the energy of the free compound and the average energy of the conformations observed when the modulator binds to the polypeptide.  
      A compound designed or selected as binding to an HNF4 polypeptide (preferably an HNF4γ LBD polypeptide) can be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the target polypeptide. Such non-complementary (e.g., electrostatic) interactions include repulsive charge-charge, dipole-dipole and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the modulator and the polypeptide when the modulator is bound to an HNF4 LBD preferably make a neutral or favorable contribution to the enthalpy of binding.  
      Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include: 
          1. Gaussian 98™, which is available from Gaussian, Inc., Pittsburgh, Pa.;     2. AMBER™ program, version 6.0, which is available from the University of California at San Francisco;     3. QUANTA™ program, which is available from Molecular Simulations, Inc., San Diego, Calif.;     4. CHARMm® program, which is available from Molecular Simulations, Inc., San Diego, Calif.; and     4. Insight II® program, which is available from Molecular Simulations, Inc., San Diego, Calif.        

      These programs can be implemented using a suitable computer system. Other hardware systems and software packages will be apparent to those skilled in the art after review of the disclosure of the present invention presented herein.  
      Once an HNF4 LBD modulating compound has been optimally selected or designed, as described above, substitutions can then be made in some of its atoms or side groups in order to improve or modify its binding properties. Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. It should, of course, be understood that components known in the art to alter conformation should be avoided. Such substituted chemical compounds can then be analyzed for efficiency of fit to an HNF4 LBD binding site using the same computer-based approaches described in detail above.  
      VII.B. Distinguishing Between HNF4 Isoforms  
      The present invention discloses the ability to generate new synthetic ligands to distinguish between HNF4 isoforms. As described herein, computer-designed ligands can be generated that distinguish between binding isoforms, thereby allowing the generation of either tissue specific or function specific ligands. The atomic structural coordinates disclosed in the present invention reveal structural details unique to HNF4γ. These structural details can be exploited when a novel ligand is designed using the methods of the present invention or other ligand design methods known in the art. The structural features that differentiate an HNF4γ from an HNF4α can be targeted in ligand design. Thus, for example, a ligand can be designed that will recognize HNF4γ, while not interacting with other HNF4s or even with moieties having similar structural features. Prior to the disclosure of the present invention, the ability to target an HNF4 isoform was unattainable.  
      VII.C. Method of Screening for Chemical and Biological Modulators of the Biological Activity of HNF4γ 
      A candidate substance identified according to a screening assay of the present invention has an ability to modulate the biological activity of an HNF4 polypeptide or an HNF4 LBD polypeptide. In a preferred embodiment, such a candidate compound can have utility in the treatment of disorders and conditions associated with the biological activity of an HNF4γ or an HNF4γ LBD polypeptide, including diabetes, glucose homeostasis and lipid homeostasis.  
      In a cell-free system, the method comprises the steps of establishing a control system comprising an HNF4γ polypeptide and a ligand which is capable of binding to the polypeptide; establishing a test system comprising an HNF4γ polypeptide, the ligand, and a candidate compound; and determining whether the candidate compound modulates the activity of the polypeptide by comparison of the test and control systems. A representative ligand comprises a fatty acid or other small molecule, and in this embodiment, the biological activity or property screened includes binding affinity.  
      In another embodiment of the invention, a form of an HNF4γ polypeptide or a catalytic or immunogenic fragment or oligopeptide thereof, can be used for screening libraries of compounds in any of a variety of drug screening techniques. The fragment employed in such a screening can be affixed to a solid support. The formation of binding complexes, between an HNF4γ polypeptide and the agent being tested, will be detected. In a preferred embodiment, the HNF4γ polypeptide has an amino acid sequence of SEQ ID NO:2. When an HNF4γ LBD polypeptide is employed, a preferred embodiment will include an HNF4γ polypeptide having the amino acid sequence of SEQ ID NO:4.  
      Another technique for drug screening which can be used provides for high throughput screening of compounds having suitable binding affinity to the protein of interest as described in published PCT application WO 84/03564, herein incorporated by reference. In this method, as applied to a polypeptide of the present invention, large numbers of different small test compounds are synthesized on a solid substrate, such as plastic pins or some other surface. The test compounds are reacted with the polypeptide, or fragments thereof. Bound polypeptide is then detected by methods well known to those of skill in the art. The polypeptide can also be placed directly onto plates for use in the aforementioned drug screening techniques.  
      In yet another embodiment, a method of screening for a modulator of an HNF4γ polypeptide or an HNF4γ LBD polypeptide comprises: providing a library of test samples; contacting an HNF4γ polypeptide or an HNF4γ LBD polypeptide with each test sample; detecting an interaction between a test sample and a an HNF4γ polypeptide or an HNF4γ LBD polypeptide; identifying a test sample that interacts with an HNF4γ polypeptide or an HNF4γ LBD polypeptide; and isolating a test sample that interacts with an HNF4γ polypeptide or an HNF4γ LBD polypeptide.  
      In each of the foregoing embodiments, an interaction can be detected spectrophotometrically, radiologically or immunologically. An interaction between an HNF4γ polypeptide or an HNF4γ LBD polypeptide and a test sample can also be quantified using methodology known to those of skill in the art. In another embodiment, the HNF4γ polypeptide and the HNF4γ LBD is in crystalline form.  
      In accordance with the present invention there is also provided a rapid and high throughput screening method that relies on the methods described above. This screening method comprises separately contacting each of a plurality of substantially identical samples with an HNF4γ polypeptide or an HNF4γ LBD and detecting a resulting binding complex. In such a screening method the plurality of samples preferably comprises more than about 10 4  samples, or more preferably comprises more than about 5×10 4  samples.  
      VII.D. Method of Identifying Compounds Which Inhibit Ligand Binding  
      Until disclosure of the present invention, the natural ligand of HNF4γ was unknown. Various hypotheses predicted the general properties an HNF4γ ligand might exhibit, but no ligand was conclusively identified. The present invention solves this problem by conclusively identifying a natural ligand of HNF4γ, the fatty acid palmitic acid. Using the identity of HNF4γ&#39;s natural ligand, disclosed for the first time herein, it is possible to design test compounds that inhibit binding of ligands normally bound by an HNF4 polypeptide.  
      In one aspect of the present invention, an assay method for identifying a compound that inhibits binding of a ligand to an HNF4 polypeptide is disclosed. A natural ligand of HNF4γ, such as a fatty acid can be used in the assay method as the ligand against which the inhibition by a test compound is gauged. Palmitic acid is a preferred fatty acid in the assay method. The method comprises (a) incubating an HNF4 polypeptide with a ligand in the presence of a test inhibitor compound; (b) determining an amount of ligand that is bound to the HNF4 polypeptide, wherein decreased binding of ligand to the HNF4 polypeptide in the presence of the test inhibitor compound relative to binding in the absence of the test inhibitor compound is indicative of inhibition; and (c) identifying the test compound as an inhibitor of ligand binding if decreased ligand binding is observed. Preferably, the ligand is a fatty acid and even more preferably, the fatty acid is palmitic acid.  
      In another aspect of the present invention, the disclosed assay method can be used in the structural refinement of candidate HNF4 inhibitors. For example, multiple rounds of optimization can be followed by gradual structural changes in a strategy of inhibitor design. A strategy such as this is made possible by the disclosure of the coordinates of the HNF4γ LBD and the disclosure of a natural ligand of HNF4, the fatty acid, palmitic acid.  
      VII.E. Design of HNF4 Isoform Modulators  
      The HNF4γ crystal structure of the present invention can be used to generate modulators of other HNF4 isoforms, such as HNF4α. Analysis of the disclosed crystal structure can provide a guide for designing HNF4α modulators. Absent the crystal structure of the present invention, researches would be required to design HNF4α modulators de novo. The present invention, however, addresses this problem by providing insights into the binding pocket of HNF4γ which can be extended, due to significant structural similarity, to the binding pocket of HNF4α. An evaluation of the binding pocket of HNF4γ indicates that a potential HNF4α modulator would meet a broad set of general criteria. Broadly, it can be stated that, based on the crystal structure of HNF4γ, a potent HNF4α ligand would require several general features including: (a) a carboxylic acid or equivalent isosteric “head group” to interact with the amino acids R186 and G197 to form a strong polar hydrogen bonding interaction; (b) a lipophilic non-head group region of the molecule, which could possibly consist of aromatic rings, aliphatic carbon atoms, ether oxygens atoms, etc.; and (c) the ability to adopt a conformation that is complementary to the shape of the binding pocket.  
      Using the discerned structural similarities and differences between HNF4 isoforms, as represented and predicted based on the crystal structure of the present invention and homology models, an HNF4α modulator can be designed. For example, based on an evaluation of a homology model of HNF4α, which is derived from the HNF4γ crystal structure, it is expected that a potent ligand would need similar characteristics as listed above for a compound recognized by HNF4γ. Additional modifications can be included, based on the disclosed structure, which are predicted to further define a modulator specific for HNF4α over other isoforms. For example, if amino acid A215 (using HNF4γ numbering scheme) is mutated to a serine residue, a group capable of hydrogen bonding (which could be either donating or accepting) placed within 3 angstroms of the serine residue (distance of OG of the serine residue to the “heavy atom” of the hydrogen bonding group) would increase both the potency and selectivity of the compounds for HNF4α. Thus, the disclosed crystal structure of HNF4γ can be useful when designing modulators of HNF4α and other isoforms.  
      VII. Design. Preparation and Structural Analysis of HNF4γ and HNF4γ LBD Mutants and Structural Equivalents  
      The present invention provides for the generation of HNF4 and HNF4 mutants (preferably HNF4γ and HNF4γ LBD mutants), and the ability to solve the crystal structures of those that crystallize. More particularly, through the provision of the three-dimensional structure of an HNF4γ LBD, desirable sites for mutation can be identified.  
      The structure coordinates of an HNF4γ LBD provided in accordance with the present invention also facilitate the identification of related proteins or enzymes analogous to HNF4γ in function, structure or both, (for example, an HNF4α), which can lead to novel therapeutic modes for treating or preventing a range of disease states.  
      VIII.A. Sterically Similar Compounds  
      A further aspect of the present invention is that sterically similar compounds can be formulated to mimic the key portions of an HNF4 LBD structure. Such compounds are functional equivalents. The generation of a structural functional equivalent can be achieved by the techniques of modeling and chemical design known to those of skill in the art and described herein. Modeling and chemical design of HNF4 and HNF4 LBD structural equivalents can be based on the structure coordinates of a crystalline HNF4γ LBD polypeptide of the present invention. It will be understood that all such sterically similar constructs fall within the scope of the present invention.  
      VIII.B. HNF4 Polypeptides  
      The generation of chimeric HNF4 polypeptides is also an aspect of the present invention. Such a chimeric polypeptide can comprise an HNF4 LBD polypeptide or a portion of an HNF4 LBD, (e.g. an HNF4γ LBD) that is fused to a candidate polypeptide or a suitable region of the candidate polypeptide, for example HNF4α. Throughout the present disclosure it is intended that the term “mutant” encompass not only mutants of an HNF4 LBD polypeptide but chimeric proteins generated using an HNF4 LBD as well. It is thus intended that the following discussion of mutant HNF4 LBDs apply mutatis mutandis to chimeric HNF4 and HNF4 LBD polypeptides and to structural equivalents thereof.  
      In accordance with the present invention, a mutation can be directed to a particular site or combination of sites of a wild-type HNF4 LBD. For example, an accessory binding site or the binding pocket can be chosen for mutagenesis. Similarly, a residue having a location on, at or near the surface of the polypeptide can be replaced, resulting in an altered surface charge of one or more charge units, as compared to the wild-type HNF4 and HNF4 LBD. Alternatively, an amino acid residue in an HNF4 or an HNF4 LBD can be chosen for replacement based on its hydrophilic or hydrophobic characteristics.  
      Such mutants can be characterized by any one of several different properties as compared with the wild-type HNF4 LBD. For example, such mutants can have an altered surface charge of one or more charge units, or can have an increase in overall stability. Other mutants can have altered substrate specificity in comparison with, or a higher specific activity than, a wild-type HNF4 or HNF4 LBD.  
      HNF4 and HNF4 LBD mutants of the present invention can be generated in a number of ways. For example, the wild-type sequence of an HNF4 or an HNF4 LBD can be mutated at those sites identified using this invention as desirable for mutation, by means of oligonucleotide-directed mutagenesis or other conventional methods, such as deletion. Alternatively, mutants of an HNF4 or an HNF4 LBD can be generated by the site-specific replacement of a particular amino acid with an unnaturally occurring amino acid. In addition, HNF4 or HNF4 LBD mutants can be generated through replacement of an amino acid residue, for example, a particular cysteine or methionine residue, with selenocysteine or selenomethionine. This can be achieved by growing a host organism capable of expressing either the wild-type or mutant polypeptide on a growth medium depleted of either natural cysteine or methionine (or both) but enriched in selenocysteine or selenomethionine (or both).  
      Mutations can be introduced into a DNA sequence coding for an HNF4 or an HNF4 LBD using synthetic oligonucleotides. These oligonucleotides contain nucleotide sequences flanking the desired mutation sites. Mutations can be generated in the full-length DNA sequence of an HNF4 or an HNF4 LBD or in any sequence coding for polypeptide fragments of an HNF4 or an HNF4 LBD.  
      According to the present invention, a mutated HNF4 or HNF4 LBD DNA sequence produced by the methods described above, or any alternative methods known in the art, can be expressed using an expression vector. An expression vector, as is well known to those of skill in the art, typically includes elements that permit autonomous replication in a host cell independent of the host genome, and one or more phenotypic markers for selection purposes. Either prior to or after insertion of the DNA sequences surrounding the desired HNF4 or HNF4 LBD mutant coding sequence, an expression vector also will include control sequences encoding a promoter, operator, ribosome binding site, translation initiation signal, and, optionally, a repressor gene or various activator genes and a signal for termination. In some embodiments, where secretion of the produced mutant is desired, nucleotides encoding a “signal sequence” can be inserted prior to an HNF4 or an HNF4 LBD mutant coding sequence. For expression under the direction of the control sequences, a desired DNA sequence must be operatively linked to the control sequences; that is, the sequence must have an appropriate start signal in front of the DNA sequence encoding the HNF4 or HNF4 LBD mutant, and the correct reading frame to permit expression of that sequence under the control of the control sequences and production of the desired product encoded by that HNF4 or HNF4 LBD sequence must be maintained.  
      Any of a wide variety of well-known available expression vectors can be useful to express a mutated HNF4 or HNF4 LBD coding sequences of this invention. These include for example, vectors consisting of segments of chromosomal, non-chromosomal and synthetic DNA sequences, such as various known derivatives of SV40, known bacterial plasmids, e.g., plasmids from  E. coli  including col E1, pCR1, pBR322, pMB9 and their derivatives, wider host range plasmids, e.g., RP4, phage DNAs, e.g., the numerous derivatives of phage X, e.g., NM 989, and other DNA phages, e.g., M13 and filamentous single stranded DNA phages, yeast plasmids and vectors derived from combinations of plasmids and phage DNAs, such as plasmids which have been modified to employ phage DNA or other expression control sequences. In a preferred embodiment of this invention, the  E. coli  vector pRSET A, including a T7-based expression system, is employed.  
      In addition, any of a wide variety of expression control sequences-sequences that control the expression of a DNA sequence when operatively linked to it—can be used in these vectors to express the mutated DNA sequences according to this invention. Such useful expression control sequences, include, for example, the early and late promoters of SV40 for animal cells, the lac system, the trp system the TAC or TRC system, the major operator and promoter regions of phage X, the control regions of fd coat protein, all for  E. coli , the promoter for 3-phosphoglycerate kinase or other glycolytic enzymes, the promoters of acid phosphatase, e.g., Pho5, the promoters of the yeast α-mating factors for yeast, and other sequences known to control the expression of genes of prokaryotic or eukaryotic cells or their viruses, and various combinations thereof.  
      A wide variety of hosts are also useful for producing mutated HNF4γ and HNF4γ LBD polypeptides according to this invention. These hosts include, for example, bacteria, such as  E. coli, Bacillus  and  Streptomyces , fungi, such as yeasts, and animal cells, such as CHO and COS-1 cells, plant cells, insect cells, such as Sfg cells, and transgenic host cells.  
      It should be understood that not all expression vectors and expression systems function in the same way to express mutated DNA sequences of this invention, and to produce modified HNF4 and HNF4 LBD polypeptides or HNF4 or HNF4 LBD mutants. Neither do all hosts function equally well with the same expression system. One of skill in the art can, however, make a selection among these vectors, expression control sequences and hosts without undue experimentation and without departing from the scope of this invention. For example, an important consideration in selecting a vector will be the ability of the vector to replicate in a given host. The copy number of the vector, the ability to control that copy number, and the expression of any other proteins encoded by the vector, such as antibiotic markers, should also be considered.  
      In selecting an expression control sequence, a variety of factors should also be considered. These include, for example, the relative strength of the system, its controllability and its compatibility with the DNA sequence encoding a modified HNF4 or HNF4 LBD polypeptide of this invention, with particular regard to the formation of potential secondary and tertiary structures.  
      Hosts should be selected by consideration of their compatibility with the chosen vector, the toxicity of a modified HNF4 or HNF4 LBD to them, their ability to express mature products, their ability to fold proteins correctly, their fermentation requirements, the ease of purification of a modified HNF4 or HNF4 LBD and safety. Within these parameters, one of skill in the art can select various vector/expression control system/host combinations that will produce useful amounts of a mutant HNF4 or HNF4 LBD. A mutant HNF4 or HNF4 LBD produced in these systems can be purified by a variety of conventional steps and strategies, including those used to purify the wild-type HNF4 or HNF4 LBD.  
      Once an HNF4 LBD mutation(s) has been generated in the desired location, such as an active site or dimerization site, the mutants can be tested for any one of several properties of interest. For example, mutants can be screened for an altered charge at physiological pH. This is determined by measuring the mutant HNF4 or HNF4 LBD isoelectric point (pI) and comparing the observed value with that of the wild-type parent. Isoelectric point can be measured by gel-electrophoresis according to the method of Wellner (Wellner, (1971)  Anal. Chem.  43: 597). A mutant HNF4 or HNF4 LBD polypeptide containing a replacement amino acid located at the surface of the enzyme, as provided by the structural information of this invention, can lead to an altered surface charge and an altered pl.  
      VIII.C. Generation of an Engineered HNF4 or HNF4 LBD Mutant  
      In another aspect of the present invention, a unique HNF4 or HNF4 LBD polypeptide can be generated. Such a mutant can facilitate purification and the study of the ligand-binding abilities of an HNF4 polypeptide.  
      As used in the following discussion, the terms “engineered HNF4”, “engineered HNF4 LDB”, “HNF4 mutant”, and “HNF4 LBD mutant” refers to polypeptides having amino acid sequences which contain at least one mutation in the wild-type sequence. The terms also refer to HNF4 and HNF4 LBD polypeptides which are capable of exerting a biological effect in that they comprise all or a part of the amino acid sequence of an engineered HNF4 or HNF4 LBD mutant polypeptide of the present invention, or cross-react with antibodies raised against an engineered HNF4 or HNF4 LBD mutant polypeptide, or retain all or some or an enhanced degree of the biological activity of the engineered HNF4 or HNF4 LBD mutant amino acid sequence or protein. Such biological activity can include lipid binding in general, and fatty acid binding in particular.  
      The terms “engineered HNF4 LBD” and “HNF4 LBD mutant” also includes analogs of an engineered HNF4 LBD or HNF4 LBD mutant polypeptide. By “analog” is intended that a DNA or polypeptide sequence can contain alterations relative to the sequences disclosed herein, yet retain all or some or an enhanced degree of the biological activity of those sequences. Analogs can be derived from genomic nucleotide sequences or from other organisms, or can be created synthetically. Those of skill in the art will appreciate that other analogs, as yet undisclosed or undiscovered, can be used to design and/or construct HNF4 LBD or HNF4 LBD mutant analogs. There is no need for an engineered HNF4 LBD or HNF4 LBD mutant polypeptide to comprise all or substantially all of the amino acid sequence of SEQ ID NOs:2 or 4. Shorter or longer sequences are anticipated to be of use in the invention; shorter sequences are herein referred to as “segments”. Thus, the terms “engineered HNF4 LBD” and “HNF4 LBD mutant” also includes fusion, chimeric or recombinant engineered HNF4 LBD or HNF4 LBD mutant polypeptides and proteins comprising sequences of the present invention. Methods of preparing such proteins are disclosed herein above and are known in the art.  
      VIII.D. Sequence Similarity and Identity  
      As used herein, the term “substantially similar” means that a particular sequence varies from nucleic acid sequence of SEQ ID NOs:1 or 3, or the amino acid sequence of SEQ ID NOs:2 or 4 by one or more deletions, substitutions, or additions, the net effect of which is to retain at least some of biological activity of the natural gene, gene product, or sequence. Such sequences include “mutant” or “polymorphic” sequences, or sequences in which the biological activity and/or the physical properties are altered to some degree but retains at least some or an enhanced degree of the original biological activity and/or physical properties. In determining nucleic acid sequences, all subject nucleic acid sequences capable of encoding substantially similar amino acid sequences are considered to be substantially similar to a reference nucleic acid sequence, regardless of differences in codon sequences or substitution of equivalent amino acids to create biologically functional equivalents.  
      VIII.D.1. Sequences that are Substantially Identical to an Engineered HNF4 or HNF4 LBD Mutant Sequence of the Present Invention  
      Nucleic acids that are substantially identical to a nucleic acid sequence of an engineered HNF4 or HNF4 LBD mutant of the present invention, e.g. allelic variants, genetically altered versions of the gene, etc., bind to an engineered HNF4 or HNF4 LBD mutant sequence under stringent hybridization conditions. By using probes, particularly labeled probes of DNA sequences, one can isolate homologous or related genes. The source of homologous genes can be any species, e.g. primate species; rodents, such as rats and mice, canines, felines, bovines, equines, yeast, nematodes, etc.  
      Between mammalian species, e.g. human and mouse, homologs have substantial sequence similarity, i.e. at least 75% sequence identity between nucleotide sequences. Sequence similarity is calculated based on a reference sequence, which can be a subset of a larger sequence, such as a conserved motif, coding region, flanking region, etc. A reference sequence will usually be at least about 18 nt long, more usually at least about 30 nt long, and can extend to the complete sequence that is being compared. Algorithms for sequence analysis are known in the art, such as BLAST, described in Altschul et al., (1990)  J. Mol. Biol.  215: 403-10.  
      Percent identity or percent similarity of a DNA or peptide sequence can be determined, for example, by comparing sequence information using the GAP computer program, available from the University of Wisconsin Geneticist Computer Group. The GAP program utilizes the alignment method of Needleman et al., (1970)  J. Mol. Biol.  48: 443, as revised by Smith et al., (1981)  Adv. Appl. Math.  2:482. Briefly, the GAP program defines similarity as the number of aligned symbols (i.e., nucleotides or amino acids) which are similar, divided by the total number of symbols in the shorter of the two sequences. The preferred parameters for the GAP program are the default parameters, which do not impose a penalty for end gaps. See, e.g., Schwartz et al., eds., (1979),  Atlas of Protein Sequence and Structure, National Biomedical Research Foundation , pp. 357-358, and Gribskov et al., (1986)  Nucl. Acids. Res.  14: 6745.  
      The term “similarity” is contrasted with the term “identity”. Similarity is defined as above; “identity”, however, means a nucleic acid or amino acid sequence having the same amino acid at the same relative position in a given family member of a gene family. Homology and similarity are generally viewed as broader terms than the term identity. Biochemically similar amino acids, for example leucine/isoleucine or glutamate/aspartate, can be present at the same position-these are not identical per se, but are biochemically “similar.” As disclosed herein, these are referred to as conservative differences or conservative substitutions. This differs from a conservative mutation at the DNA level, which changes the nucleotide sequence without making a change in the encoded amino acid, e.g. TCC to TCA, both of which encode serine.  
      As used herein, DNA analog sequences are “substantially identical” to specific DNA sequences disclosed herein if: (a) the DNA analog sequence is derived from coding regions of the nucleic acid sequence shown in SEQ ID NOs:1 or 3; or (b) the DNA analog sequence is capable of hybridization with DNA sequences of (a) under stringent conditions and which encode a biologically active HNF4γ or HNF4γ LBD gene product; or (c) the DNA sequences are degenerate as a result of alternative genetic code to the DNA analog sequences defined in (a) and/or (b). Substantially identical analog proteins and nucleic acids will have between about 70% and 80%, preferably between about 81% to about 90% or even more preferably between about 91% and 99% sequence identity with the corresponding sequence of the native protein or nucleic acid. Sequences having lesser degrees of identity but comparable biological activity are considered to be equivalents.  
      As used herein, “stringent conditions” means conditions of high stringency, for example 6×SSC, 0.2% polyvinylpyrrolidone, 0.2% Ficoll, 0.2% bovine serum albumin, 0.1% sodium dodecyl sulfate, 100 μg/ml salmon sperm DNA and 15% formamide at 68° C. For the purposes of specifying additional conditions of high stringency, preferred conditions are salt concentration of about 200 mM and temperature of about 45° C. One example of such stringent conditions is hybridization at 4×SSC, at 65° C., followed by a washing in 0.1×SSC at 65° C. for one hour. Another exemplary stringent hybridization scheme uses 50% formamide, 4×SSC at 42° C.  
      In contrast, nucleic acids having sequence similarity are detected by hybridization under lower stringency conditions. Thus, sequence identity can be determined by hybridization under lower stringency conditions, for example, at 50° C. or higher and 0.1×SSC (9 mM NaCl/0.9 mM sodium citrate) and the sequences will remain bound when subjected to washing at 55° C. in 1×SSC.  
      VIII.D.2. Complementarity and Hybridization to an Engineered HNF4 or HNF4 LBD Mutant Sequence  
      As used herein, the term “complementary sequences” means nucleic acid sequences which are base-paired according to the standard Watson-Crick complementarity rules. The present invention also encompasses the use of nucleotide segments that are complementary to the sequences of the present invention.  
      Hybridization can also be used for assessing complementary sequences and/or isolating complementary nucleotide sequences. As discussed above, nucleic acid hybridization will be affected by such conditions as salt concentration, temperature, or organic solvents, in addition to the base composition, length of the complementary strands, and the number of nucleotide base mismatches between the hybridizing nucleic acids, as will be readily appreciated by those skilled in the art. Stringent temperature conditions will generally include temperatures in excess of about 30° C., typically in excess of about 37° C., and preferably in excess of about 45° C. Stringent salt conditions will ordinarily be less than about 1,000 mM, typically less than about 500 mM, and preferably less than about 200 mM. However, the combination of parameters is much more important than the measure of any single parameter. See, e.g., Wetmur &amp; Davidson, (1968)  J. Mol. Biol.  31: 349-70. Determining appropriate hybridization conditions to identify and/or isolate sequences containing high levels of homology is well known in the art. See, e.g., Sambrook et al., (1989)  Molecular Cloning: A Laboratory Manual , Cold Spring Harbor, N.Y.  
      VIII.D.3. Functional Equivalents of an Engineered HNF4 or HNF4 LBD Mutant Nucleic Acid Sequence of the Present Invention  
      As used herein, the term “functionally equivalent codon” is used to refer to codons that encode the same amino acid, such as the ACG and AGU codons for serine. HNF4γ or HNF4γ LBD-encoding nucleic acid sequences comprising SEQ ID NOs:1 and 3 which have functionally equivalent codons are covered by the present invention. Thus, when referring to the sequence example presented in SEQ ID NOs:1 and 3, applicants contemplate substitution of functionally equivalent codons into the sequence example of SEQ ID NOs:1 and 3. Thus, applicants are in possession of amino acid and nucleic acids sequences which include such substitutions but which are not set forth herein in their entirety for convenience.  
      It will also be understood by those of skill in the art that amino acid and nucleic acid sequences can include additional residues, such as additional N- or C-terminal amino acids or 5′ or 3′ nucleic acid sequences, and yet still be essentially as set forth in one of the sequences disclosed herein, so long as the sequence retains biological protein activity where polypeptide expression is concerned. The addition of terminal sequences particularly applies to nucleic acid sequences which can, for example, include various non-coding sequences flanking either of the 5′ or 3′ portions of the coding region or can include various internal sequences, i.e., introns, which are known to occur within genes.  
      VIII.D.4. Biological Equivalents  
      The present invention envisions and includes biological equivalents of an engineered HNF4 or HNF4 LBD mutant polypeptide of the present invention. The term “biological equivalent” refers to proteins having amino acid sequences which are substantially identical to the amino acid sequence of an engineered HNF4 LBD mutant of the present invention and which are capable of exerting a biological effect in that they are capable of binding lipid moieties or cross-reacting with anti-HNF4 or HNF4 LBD mutant antibodies raised against an engineered mutant HNF4 or HNF4 LBD polypeptide of the present invention.  
      For example, certain amino acids can be substituted for other amino acids in a protein structure without appreciable loss of interactive capacity with, for example, structures in the nucleus of a cell. Since it is the interactive capacity and nature of a protein that defines that protein&#39;s biological functional activity, certain amino acid sequence substitutions can be made in a protein sequence (or the nucleic acid sequence encoding it) to obtain a protein with the same, enhanced, or antagonistic properties. Such properties can be achieved by interaction with the normal targets of the protein, but this need not be the case, and the biological activity of the invention is not limited to a particular mechanism of action. It is thus in accordance with the present invention that various changes can be made in the amino acid sequence of an engineered HNF4 or HNF4 LBD mutant polypeptide of the present invention or its underlying nucleic acid sequence without appreciable loss of biological utility or activity.  
      Biologically equivalent polypeptides, as used herein, are polypeptides in which certain, but not most or all, of the amino acids can be substituted. Thus, when referring to the sequence examples presented in SEQ ID NOs:1 and 3, applicants envision substitution of codons that encode biologically equivalent amino acids, as described herein, into the sequence example of SEQ ID NOs:2 and 4, respectively. Thus, applicants are in possession of amino acid and nucleic acids sequences which include such substitutions but which are not set forth herein in their entirety for convenience.  
      Alternatively, functionally equivalent proteins or peptides can be created via the application of recombinant DNA technology, in which changes in the protein structure can be engineered, based on considerations of the properties of the amino acids being exchanged, e.g. substitution of lie for Leu. Changes designed by man can be introduced through the application of site-directed mutagenesis techniques, e.g., to introduce improvements to the antigenicity of the protein or to test an engineered HNF4 or HNF4 LBD mutant polypeptide of the present invention in order to modulate lipid-binding or other activity, at the molecular level.  
      Amino acid substitutions, such as those which might be employed in modifying an engineered HNF4 or HNF4 LBD mutant polypeptide of the present invention are generally, but not necessarily, based on the relative similarity of the amino acid side-chain substituents, for example, their hydrophobicity, hydrophilicity, charge, size, and the like. An analysis of the size, shape and type of the amino acid side-chain substituents reveals that arginine, lysine and histidine are all positively charged residues; that alanine, glycine and serine are all of similar size; and that phenylalanine, tryptophan and tyrosine all have a generally similar shape. Therefore, based upon these considerations, arginine, lysine and histidine; alanine, glycine and serine; and phenylalanine, tryptophan and tyrosine; are defined herein as biologically functional equivalents. Other biologically functionally equivalent changes will be appreciated by those of skill in the art. It is implicit in the above discussion, however, that one of skill in the art can appreciate that a radical, rather than a conservative substitution is warranted in a given situation. Non-conservative substitutions in engineered mutant HNF4 or HNF4 LBD polypeptides of the present invention are also an aspect of the present invention.  
      In making biologically functional equivalent amino acid substitutions, the hydropathic index of amino acids can be considered. Each amino acid has been assigned a hydropathic index on the basis of their hydrophobicity and charge characteristics, these are: isoleucine (+4.5); valine (+4.2); leucine (+3.8); phenylalanine (+2.8); cysteine (+2.5); methionine (+1.9); alanine (+1.8); glycine (−0.4); threonine (−0.7); serine (−0.8); tryptophan (−0.9); tyrosine (−1.3); proline (−1.6); histidine (−3.2); glutamate (−3.5); glutamine (−3.5); aspartate (−3.5); asparagine (−3.5); lysine (−3.9); and arginine (−4.5).  
      The importance of the hydropathic amino acid index in conferring interactive biological function on a protein is generally understood in the art (Kyte &amp; Doolittle, (1982),  J. Mol. Biol.  157: 105-132, incorporated herein by reference). It is known that certain amino acids can be substituted for other amino acids having a similar hydropathic index or score and still retain a similar biological activity. In making changes based upon the hydropathic index, the substitution of amino acids whose hydropathic indices are within +2 of the original value is preferred, those which are within +1 of the original value are particularly preferred, and those within ±0.5 of the original value are even more particularly preferred.  
      It is also understood in the art that the substitution of like amino acids can be made effectively on the basis of hydrophilicity. U.S. Pat. No. 4,554,101, incorporated herein by reference, states that the greatest local average hydrophilicity of a protein, as governed by the hydrophilicity of its adjacent amino acids, correlates with its immunogenicity and antigenicity, i.e. with a biological property of the protein. It is understood that an amino acid can be substituted for another having a similar hydrophilicity value and still obtain a biologically equivalent protein.  
      As detailed in U.S. Pat. No. 4,554,101, the following hydrophilicity values have been assigned to amino acid residues: arginine (+3.0); lysine (+3.0); aspartate (+3.0±1); glutamate (+3.0±1); serine (+0.3); asparagine (+0.2); glutamine (+0.2); glycine (0); threonine (−0.4); proline (−0.5±1); alanine (−0.5); histidine (−0.5); cysteine (−1.0); methionine (−1.3); valine (−1.5); leucine (−1.8); isoleucine (−1.8); tyrosine (−2.3); phenylalanine (−2.5); tryptophan (−3.4).  
      In making changes based upon similar hydrophilicity values, the substitution of amino acids whose hydrophilicity values are within ±2 of the original value is preferred, those which are within ±1 of the original value are particularly preferred, and those within +0.5 of the original value are even more particularly preferred.  
      While discussion has focused on functionally equivalent polypeptides arising from amino acid changes, it will be appreciated that these changes can be effected by alteration of the encoding DNA, taking into consideration also that the genetic code is degenerate and that two or more codons can code for the same amino acid.  
      Thus, it will also be understood that this invention is not limited to the particular amino acid and nucleic acid sequences of SEQ ID NOs:1-4. Recombinant vectors and isolated DNA segments can therefore variously include an engineered HNF4γ or HNF4γ LBD mutant polypeptide-encoding region itself, include coding regions bearing selected alterations or modifications in the basic coding region, or include larger polypeptides which nevertheless comprise an HNF4γ or HNF4γ LBD mutant polypeptide-encoding regions or can encode biologically functional equivalent proteins or polypeptides which have variant amino acid sequences. Biological activity of an engineered HNF4γ or HNF4γ LBD mutant polypeptide can be determined, for example, by lipid-binding assays known to those of skill in the art.  
      The nucleic acid segments of the present invention, regardless of the length of the coding sequence itself, can be combined with other DNA sequences, such as promoters, enhancers, polyadenylation signals, additional restriction enzyme sites, multiple cloning sites, other coding segments, and the like, such that their overall length can vary considerably. It is therefore contemplated that a nucleic acid fragment of almost any length can be employed, with the total length preferably being limited by the ease of preparation and use in the intended recombinant DNA protocol. For example, nucleic acid fragments can be prepared which include a short stretch complementary to a nucleic acid sequence set forth in SEQ ID NOs:1 and 3, such as about 10 nucleotides, and which are up to 10,000 or 5,000 base pairs in length. DNA segments with total lengths of about 4,000, 3,000, 2,000, 1,000, 500, 200, 100, and about 50 base pairs in length are also useful.  
      The DNA segments of the present invention encompass biologically functional equivalents of engineered HNF4 or HNF4 LBD mutant polypeptides. Such sequences can rise as a consequence of codon redundancy and functional equivalency that are known to occur naturally within nucleic acid sequences and the proteins thus encoded. Alternatively, functionally equivalent proteins or polypeptides can be created via the application of recombinant DNA technology, in which changes in the protein structure can be engineered, based on considerations of the properties of the amino acids being exchanged. Changes can be introduced through the application of site-directed mutagenesis techniques, e.g., to introduce improvements to the antigenicity of the protein or to test variants of an engineered HNF4 or HNF4 LBD mutant of the present invention in order to examine the degree of lipid-binding activity, or other activity at the molecular level. Various site-directed mutagenesis techniques are known to those of skill in the art and can be employed in the present invention.  
      The invention further encompasses fusion proteins and peptides wherein an engineered HNF4 or HNF4 LBD mutant coding region of the present invention is aligned within the same expression unit with other proteins or peptides having desired functions, such as for purification or immunodetection purposes.  
      Recombinant vectors form important further aspects of the present invention. Particularly useful vectors are those in which the coding portion of the DNA segment is positioned under the control of a promoter. The promoter can be that naturally associated with an HNF4 gene, as can be obtained by isolating the 5′ non-coding sequences located upstream of the coding segment or exon, for example, using recombinant cloning and/or PCR technology and/or other methods known in the art, in conjunction with the compositions disclosed herein.  
      In other embodiments, certain advantages will be gained by positioning the coding DNA segment under the control of a recombinant, or heterologous, promoter. As used herein, a recombinant or heterologous promoter is a promoter that is not normally associated with an HNF4 gene in its natural environment. Such promoters can include promoters isolated from bacterial, viral, eukaryotic, or mammalian cells. Naturally, it will be important to employ a promoter that effectively directs the expression of the DNA segment in the cell type chosen for expression. The use of promoter and cell type combinations for protein expression is generally known to those of skill in the art of molecular biology (See, e.g., Sambrook et al., (1989)  Molecular Cloning: A Laboratory Manual , Cold Spring Harbor Laboratory, New York, specifically incorporated herein by reference). The promoters employed can be constitutive or inducible and can be used under the appropriate conditions to direct high level expression of the introduced DNA segment, such as is advantageous in the large-scale production of recombinant proteins or peptides. One preferred promoter system contemplated for use in high-level expression is a T7 promoter-based system.  
      IX. The Role of the Three-Dimensional Structure of the HNF4γ LDB in Solving Additional HNF4 Crystals  
      Because polypeptides can crystallize in more than one crystal form, the structural coordinates of an HNF4γ LBD, or portions thereof, as provided by the present invention, are particularly useful in solving the structure of other crystal forms of HNF4γ and the crystalline forms of other HNF4s. The coordinates provided in the present invention can also be used to solve the structure of HNF4 or HNF4 LBD mutants (such as those described in Section VIII above), HNF4 LDB co-complexes, or of the crystalline form of any other protein with significant amino acid sequence homology to any functional domain of HNF4.  
      IX.A. Determining the Three-Dimensional Structure of a Polypeptide Using the Three-Dimensional Structure of the HNF4γ LBD as a Template in Molecular Replacement  
      One method that can be employed for the purpose of solving additional HNF4 crystal structures is molecular replacement. See generally, Rossmann, ed, (1972)  The Molecular Replacement Method , Gordon &amp; Breach, New York. In the molecular replacement method, the unknown crystal structure, whether it is another crystal form of an HNF4γ or an HNF4γ LBD, (i.e. an HNF4γ or an HNF4γ LBD mutant), or an HNF4γ or an HNF4γ LBD polypeptide complexed with another compound (a “co-complex”), or the crystal of some other protein with significant amino acid sequence homology to any functional region of the HNF4γ LBD, can be determined using the HNF4γ LBD structure coordinates provided in Table 2. This method provides an accurate structural form for the unknown crystal more quickly and efficiently than attempting to determine such information ab initio.  
      In addition, in accordance with this invention, HNF4γ or HNF4γ LBD mutants can be crystallized in complex with known modulators. The crystal structures of a series of such complexes can then be solved by molecular replacement and compared with that of wild-type HNF4γ or the wild-type HNF4γ LBD. Potential sites for modification within the various binding sites of the enzyme can thus be identified. This information provides an additional tool for determining the most efficient binding interactions, for example, increased hydrophobic interactions, between the HNF4γ LBD and a chemical entity or compound.  
      All of the complexes referred to in the present disclosure can be studied using X-ray diffraction techniques (See, e.g., Blundell &amp; Johnson (1985)  Method.Enzymol.,  114A &amp; 115B, (Wyckoff et al., eds.), Academic Press) and can be refined using computer software, such as the X-PLOR™ program (Brünger, (1992)  X - PLOR, Version  3.1 . A System for X - ray Crystallography and NMR , Yale University Press, New Haven, Conn.; X-PLOR is available from Molecular Simulations, Inc., San Diego, Calif.). This information can thus be used to optimize known classes of HNF4 and HNF4 LBD modulators, and more importantly, to design and synthesize novel classes of HNF4 and HNF4 LBD modulators.  
     Laboratory Examples  
      The following Laboratory Examples have been included to illustrate preferred modes of the invention. Certain aspects of the following Laboratory Examples are described in terms of techniques and procedures found or contemplated by the present inventors to work well in the practice of the invention. These Laboratory Examples are exemplified through the use of standard laboratory practices of the inventors. In light of the present disclosure and the general level of skill in the art, those of skill will appreciate that the following Laboratory Examples are intended to be exemplary only and that numerous changes, modifications and alterations can be employed without departing from the spirit and scope of the invention.  
     Laboratory Example 1  
     Sub-Cloning and Protein Purification  
      Amino acids 102408 of the HNF4γ LDB (SEQ ID NO:3) were expressed by subcloning Into a T7  E. coli  expression vector, pRSETa (Invitrogen, Carlsbad, Calif.). A histidine tag, sequence MKKGHHHHHHG (SEQ ID NO:5), was engineered at the N-terminus of the HNF4γ protein using a 5′ oligo. The plasmid was transformed into BL21 (DE3) cells which were grown at 22° C. overnight and were then harvested. The soluble protein was purified with an affinity column of Ni+2-NTA coupled agarose (Qiagen, Valencia, Calif.) (25 mM Tris pH=8.0, 50 mM imidazole pH=8.0, 150 mM NaCl). A 50-500 mM imidazole gradient was used for elution. HNF4γ eluted at 100 mM imidazole. The protein was diluted to 25 mM salt and further purified using a POROS™ 50HQ column (PerSeptive Biosystems, Foster City, Calif.) (25 mM Tris pH 8.0, 0.5 mM EDTA, 25 mM NaCl, 5 mM DTT, 5% Propane-diol) eluting with a 25 to 500 mM NaCl gradient. Two peaks were isolated, one representing homodimers of full-length HNF4γ LBD, the other containing heterodimers of full-length and C-terminally truncated HNF4γ. The homodimer peak was concentrated to 20 mg/ml and further purified by gel filtration chromatography (10 mM Tris pH 8.0, 0.1 mM EDTA, 150 mM NaCl, 10 mM DTT, 5% Propane-diol) using a Superdex 75 column (AP Biotech, Piscataway, N.J.). Protein sequence and purity were confirmed by N-terminal sequencing and mass spectrometry to greater than 95% homogeneity.  
     Laboratory Example 2  
     Crystallization  
      Crystallization trials were initially conducted with both the homogenous purified protein and the heterogeneous mixture. Crystals were obtained from both; however, the heterogeneous crystals were of poor diffraction quality. The purified protein was concentrated to 30 mg/ml (10 mM Tris pH 8.0, 0.1 mM EDTA, 150 mM NaCl, 10 mM DTT, 5% propane-diol) and crystallized using the vapor diffusion method by adding equal volume amounts of concentrated protein and a crystallization buffer of 0.75M ammonium di-hydrogen phosphate/di-ammonium hydrogen phosphate pH=5.0, 10 mM DTT. Crystals formed within 2-3 weeks and were suitable for data collection in 7 to 10 weeks.  
     Laboratory Example 3  
     Structure Determination and Refinement  
      HNF4γ LBD crystallized in the space group 14 1 22 with a unit cell of dimensions a=b=152.71 Å, c=93.42 Å, α=β=γ=90°, and one molecule in the asymmetric unit. The structure was solved using single isomorphous replacement anomalous scattering (SIRAS) from a methyl-mercury derivative collected at beam line 171D at the Advanced Photon Source (located at the Argonne National Lab, Argonne, Ill.). Mercury sites were found using the software package Shake-and-Bake (Hauptman, (1997) Curr. Opin. Struct Biol. 7: 672-80; Weeks et al., (1993) Acta Cryst. D49: 179; available from the Hauptman-Woodward Medical Research Institute, Buffalo, N.Y.), and phases were improved by solvent flipping (Abrahams &amp; Leslie, (1996) Acta Cryst. D52: 3042), which produced traceable electron density. Models were built using QUANTA™ (Molecular Simulations Inc., San Diego, Calif.), and refined using CNX™ (Molecular Simulations Inc., San Diego, Calif.).  
     Laboratory Example 4  
     GC/MS  
      Lipids were extracted from an aliquot of HNF4γ LBD with chloroform/methanol 2:1 (v/v). The extract was dried under argon and then dissolved in a small volume of organic solvent. The extract was then treated with an aliquot of 3% (v/v) acetyl chloride in methanol for 30 min at room temperature to produce the methyl ester of the predicted fatty acid. After the reaction, the sample was dried again under argon. The derivatized sample was then analyzed by GC/MS on a Shimadzu GC-17A QP-5050A instrument. Analytes were eluted from a 25 meter DB5 column by increasing the column temperature from 100-280° C. at 120° C. per minute. Ionization of analytes was achieved by either EI or CI. Mass spectra were acquired using a scan range of 70-500 Da in 0.5 seconds. Representative data are depicted in  FIGS. 4-7 .  
     Laboratory Example 5  
     FRET Assay  
      A cell-free fluorescent resonance energy transfer (FRET) assay was used to measure the association between the amino portion of CBP (CREB-binding protein) (residues 54-457) and the HNF4 LBD (HNF4α amino acids 141465 and HNF4γ amino acids 102-408) (Zhou et al., (1998) Mol. Endocrinol 12: 1594-1604). Proteins were expressed in  E. coli , purified to homogeneity, and biotinylated. CBP, the fluorescence donor, was labeled with a europium chelate, and HNF4 LBD was labeled with the streptavidin-conjugated fluorophore allophycocyanin (Molecular Probes, Eugene, Oreg.). Labeled HNF4 LBD and CBP were incubated together with ligands for 15 minutes at 21° C. before assaying. A small basal level was observed, as depicted in  FIG. 3 .  
     Laboratory Example 6  
     Computational Studies  
      The crystal structure of HNF4γ was subjected to hydrogen addition and subsequent minimization holding all heavy atoms fixed using the DISCOVER™ CVFF™ force field (Molecular Simulations, San Diego, Calif.). The model of palmitic acid was generated using the above-described HNF4γ protein and docking calculations using the program MVP (Lambert, (1997) in  Practical Application of Computer - Aided Drug Design , (Charifson, ed.) Marcel-Dekker, New York, pp. 243-303). Crystallographically determined atoms were used as a template and the corresponding atoms in palmitic acid were constrained to within 0.5 Å of the template.  
     REFERENCES  
      The references listed below as well as all references cited in the specification are incorporated herein by reference to the extent that they supplement, explain, provide a background for or teach methodology, techniques and/or compositions employed herein. 
      Abrahams &amp; Leslie, (1996)  Acta Cryst . D52: 30-42     Altschul et al., (1990)  J. Mol. Biol.  215: 403-10     Ausubel et al., (1989)  Current Protocols in Molecular Biology , Greene Publishing Associates and Wiley Interscience, New York     Bartlett et al., (1989) Special Pub.,  Royal Chem. Soc.  78: 182-96     Bjorklund &amp; Grill (1999)  Diabetes  48:1409-14     Blundell et al., (1976)  Protein Crystallography, Academic Press       Blundell &amp; Johnson, (1985)  Method.Enzymol.,  114A &amp; 115B, (Wyckoff et al., eds.), Academic Press     Bogan et al., (1998)  Nat. Struct. Biol.  5: 679-81     Bohm, (1992)  J. Comput. Aid. Mol. Des.,  6: 61-78     Bollheimer et al., (1998)  J. Clin. Invest.  101:1094-1101     Bourguet et al., (1995)  Nature  375: 377-82     Bourguet et al., (2000)  Mol. Cell  5: 289-98     Brooks et al., (1983)  J. Comp. Chem.,  8: 132     Brünger, (1992)  X - PLOR, Version  3.1 . A System for X - ray Crystallography and NMR , Yale University Press, New Haven, Conn.     Brzozowski et al., (1997)  Nature  (London) 389: 753-58     Case et al., (1997), AMBER 5, University of California, San Francisco     Chan et al., (1993)  Nucleic Acid Res.  21:1205-11     Cohen et al., (1990)  J. Med. Chem.  33: 883-94     Creighton, (1983)  Proteins: Structures and Molecular Principles , W.H. Freeman &amp; Co., N.Y.     Dell &amp; Hadzopoulou-Cladaras, (1999)  J. Biol. Chem.  274: 9013-21     Diaz Guerra et al., (1993)  Mol. Cell. Biol.  13:7725-33     Dobbins et al., (1998a)  Diabetes  47:1613-18     Dobbins et al., (1998b)  J. Clin. Invest.  101:2370-76     Drewes et al., (1996)  Mol. Cell. Biol.  16:925-31     Ducruix &amp; Geige, (1992)  Crystallization of Nucleic Acids and Proteins: A Practical Approach , IRL Press, Oxford, England     Eisen et al., (1994)  Proteins  19: 199-221     Folch et al., (1957)  J. Biol. Chem.  226: 497-509     Gampe, Jr. et al., (2000)  Mol. Cell  5: 545-55     Goodford, (1985)  J. Med. Chem.  28: 849-57     Goodsell &amp; Olsen, (1990)  Proteins  8: 195-202     Gribskov et al., (1986)  Nucl. Acids. Res.  14: 6745     Hauptman, (1997)  Curr. Opin. Struct. Biol.  7: 672-80     Hertz et al., (1998)  Nature  (London) 392: 512-16     Jacqueminet et al., (2000)  Metab. Clin. Exp.  49: 532-36     Jiang &amp; Sladek, (1997)  J. Biol. Chem.  272: 1218-25     Jiang et al., (1995)  Mol. Cell. Biol.  15: 5131-43     Kuntz et al., (1992)  J. Mol. Biol.  161: 269-88     Kyte &amp; Doolittle, (1982),  J. Mol. Biol.  157: 105-132     Lambert, (1997) in  Practical Application of Computer - Aided Drug Design , (Charifson, ed.) Marcel-Dekker, New York, pp. 243-303     Lattman, (1985)  Method Enzymol.,  115: 55-77     Martin, (1992)  J. Med. Chem.  35: 2145-54     McPherson, (1982)  Preparation and Analysis of Protein Crystals , John Wiley, New York     McPherson, (1990)  Eur. J. Biochem.  189:1-23     McPherson et al., (1989)  Preparation and Analysis of Protein Crystals , Robert E. Krieger Publishing Company, Malabar, Fla.     McRee, (1992)  J. Mol. Graphics  10: 44-47     Meng et al., (1992)  J. Comput. Chem.  13: 505-24     Mietus-Snyder et al., (1992)  Mol. Cell. Biol.  12:1708-18     Miquerol et al., (1994)  J. Biol. Chem.  269:8944-51     Miranker &amp; Karplus, (1991)  Proteins  11: 29-34     Navia &amp; Murcko, (1992)  Curr. Opin. Struc. Biol.  2: 202-10     Needleman et al., (1970)  J. Mol. Biol.  48: 443     Nicholls et al., (1991)  Proteins  11: 282     Nishibata &amp; Ital, (1991)  Tetrahedron  47: 8985     Nolte et al., (1998)  Nature  (London) 395: 137-43     Otwinowski, (1991), in  Isomorphous Replacement and Anomalous Scattering , (Evans &amp; Leslie, eds.), pp. 80-86, Daresbury Laboratory, Daresbury, United Kingdom     Pearlman et al., (1995)  Comput. Phys. Commun.  91: 1-41     Renaud et al., (1995)  Nature  378: 681-89     Rossmann, ed, (1972)  The Molecular Replacement Method , Gordon &amp; Breach, New York     Sambrook et al., (1989)  Molecular Cloning: A Laboratory Manual , Cold Spring Harbor Laboratory, New York     Schwartz et al., eds., (1979),  Atlas of Protein Sequence and Structure , National Biomedical Research Foundation, pp. 357-358     Sheldrick (1990)  Acta Cryst . A46: 467     Shih et al., (2000)  Diabetes  49: 832-37     Sladek et al.,  Genes Dev.  4: 2353-65     Smith et al., (1981)  Adv. Appl. Math . 2: 482     Stein et al., (1997)  J. Clin. Invest.  100: 398-403     Stoffel &amp; Duncan, (1997)  Proc. Natl. Acad. Sci. U.S.A.  94: 13209-14     Van Holde, (1971)  Physical Biochemistry , Prentice-Hall, N.J., 221-39     Wang et al., (1998)  J. Biol. Chem.  273: 30847-50     Weber, (1991)  Adv. Protein Chem.  41:1-36     Weeks et al., (1993)  Acta Cryst. D 49: 179     Wellner, (1971)  Anal. Chem.  43: 597     Wetmur &amp; Davidson, (1968)  J. Mol. Biol.  31: 349-70     Xu et al., (1999)  Mol. Cell  3: 397-403     Yamagata et al., (1996)  Nature  384: 458-60     Zhou et al., (1998)  Mol. Endocrinol  12: 1594-1604     Zhou &amp; Grill, (1994)  J. Clin. Invest.  93: 870-76     Zhou &amp; Grill, (1995)  J. Clin. Endocrinol Metab.  80: 1584-90     U.S. Pat. No. 4,554,101     U.S. Pat. No. 4,672,108     U.S. Pat. No. 4,833,233     U.S. Pat. No. 5,463,564     U.S. Pat. No. 6,008,033     WO 84/03564     WO 2000/037,077    

      WO 2000/025,134  
               TABLE 1                          CRYSTALLOGRAPHIC DATA AND REFINEMENT                                     MeHgCl   Native                       Crystal                   Resolution Range   40.-3.0   50.0-2.7           Observations (Unique)   413191 (10558)   1308098 (18866)           Completeness   99.6 (100)   98.4 (93.7)           I/s   36.3 (3.3)   35.8 (3.5)           Rmerge %   7.8 (44)   4.8 (32)           Refinement Statistics           Resolution Range       50.0-2.7           % Rfree       7           Rcryst Rfree       24.8 (26.8)           Protein atoms       1774           Ligand atoms       18           Water Molecules       15           Rmsd bonds/angles       0.0085/1.675           Average Protein B factor       70.1                      
 
     
       
         
           
               
             
               
                 TABLE 2 
               
             
            
               
                   
               
               
                   
               
               
                 ATOMIC STRUCTURE COORDINATE DATA OBTAINED FROM X-RAY 
               
               
                 DIFFRACTION FROM THE LIGAND BINDING DOMAIN OF HNF4γ 
               
               
                 COMPLEXED WITH PALMITIC ACID 
               
            
           
           
               
               
               
               
               
               
               
               
               
               
            
               
                   
                 ATOM 
                   
                 PROTEIN 
                   
                   
                   
                   
                   
                   
               
               
                 ATOM 
                 TYPE 
                 RESIDUE 
                 # 
                 # 
                 X 
                 Y 
                 Z 
                 OCC 
                 B 
               
               
                   
               
            
           
           
               
               
               
               
               
               
               
               
               
               
            
               
                 1 
                 CB 
                 ALA 
                 A 
                 99 
                 45.376 
                 107.876 
                 27.936 
                 1.00 
                 95.38 
               
               
                 2 
                 C 
                 ALA 
                 A 
                 99 
                 44.561 
                 106.474 
                 29.858 
                 1.00 
                 94.20 
               
               
                 3 
                 O 
                 ALA 
                 A 
                 99 
                 45.642 
                 106.159 
                 30.365 
                 1.00 
                 94.42 
               
               
                 4 
                 N 
                 ALA 
                 A 
                 99 
                 44.646 
                 108.963 
                 30.044 
                 1.00 
                 95.61 
               
               
                 5 
                 CA 
                 ALA 
                 A 
                 99 
                 44.403 
                 107.809 
                 29.123 
                 1.00 
                 95.37 
               
               
                 6 
                 N 
                 ALA 
                 A 
                 100 
                 43.481 
                 105.696 
                 29.923 
                 1.00 
                 90.76 
               
               
                 7 
                 CA 
                 ALA 
                 A 
                 100 
                 43.519 
                 104.399 
                 30.596 
                 1.00 
                 87.68 
               
               
                 8 
                 CB 
                 ALA 
                 A 
                 100 
                 42.243 
                 104.199 
                 31.414 
                 1.00 
                 86.59 
               
               
                 9 
                 C 
                 ALA 
                 A 
                 100 
                 43.675 
                 103.281 
                 29.560 
                 1.00 
                 85.41 
               
               
                 10 
                 O 
                 ALA 
                 A 
                 100 
                 44.307 
                 103.477 
                 28.519 
                 1.00 
                 85.92 
               
               
                 11 
                 N 
                 GLY 
                 A 
                 101 
                 43.117 
                 102.105 
                 29.853 
                 1.00 
                 81.95 
               
               
                 12 
                 CA 
                 GLY 
                 A 
                 101 
                 43.187 
                 101.004 
                 28.907 
                 1.00 
                 75.36 
               
               
                 13 
                 C 
                 GLY 
                 A 
                 101 
                 44.054 
                 99.816 
                 29.268 
                 1.00 
                 71.65 
               
               
                 14 
                 O 
                 GLY 
                 A 
                 101 
                 44.002 
                 98.788 
                 28.592 
                 1.00 
                 71.37 
               
               
                 15 
                 N 
                 SER 
                 A 
                 102 
                 44.852 
                 99.934 
                 30.321 
                 1.00 
                 67.35 
               
               
                 16 
                 CA 
                 SER 
                 A 
                 102 
                 45.726 
                 98.831 
                 30.719 
                 1.00 
                 63.45 
               
               
                 17 
                 CB 
                 SER 
                 A 
                 102 
                 46.647 
                 99.261 
                 31.858 
                 1.00 
                 62.72 
               
               
                 18 
                 OG 
                 SER 
                 A 
                 102 
                 46.395 
                 100.605 
                 32.201 
                 1.00 
                 69.29 
               
               
                 19 
                 C 
                 SER 
                 A 
                 102 
                 44.919 
                 97.623 
                 31.154 
                 1.00 
                 60.14 
               
               
                 20 
                 O 
                 SER 
                 A 
                 102 
                 45.222 
                 96.483 
                 30.790 
                 1.00 
                 58.87 
               
               
                 21 
                 N 
                 ILE 
                 A 
                 103 
                 43.879 
                 97.878 
                 31.936 
                 1.00 
                 56.58 
               
               
                 22 
                 CA 
                 ILE 
                 A 
                 103 
                 43.040 
                 96.809 
                 32.429 
                 1.00 
                 54.03 
               
               
                 23 
                 CB 
                 ILE 
                 A 
                 103 
                 42.020 
                 97.377 
                 33.423 
                 1.00 
                 51.99 
               
               
                 24 
                 CG2 
                 ILE 
                 A 
                 103 
                 40.987 
                 96.312 
                 33.822 
                 1.00 
                 46.51 
               
               
                 25 
                 CG1 
                 ILE 
                 A 
                 103 
                 42.799 
                 97.970 
                 34.604 
                 1.00 
                 50.00 
               
               
                 26 
                 CD1 
                 ILE 
                 A 
                 103 
                 42.480 
                 97.390 
                 35.953 
                 1.00 
                 48.75 
               
               
                 27 
                 C 
                 ILE 
                 A 
                 103 
                 42.349 
                 96.067 
                 31.291 
                 1.00 
                 54.95 
               
               
                 28 
                 O 
                 ILE 
                 A 
                 103 
                 42.157 
                 94.847 
                 31.366 
                 1.00 
                 55.77 
               
               
                 29 
                 N 
                 ASN 
                 A 
                 104 
                 41.997 
                 96.791 
                 30.232 
                 1.00 
                 54.74 
               
               
                 30 
                 CA 
                 ASN 
                 A 
                 104 
                 41.326 
                 96.184 
                 29.086 
                 1.00 
                 55.19 
               
               
                 31 
                 CB 
                 ASN 
                 A 
                 104 
                 40.777 
                 97.257 
                 28.143 
                 1.00 
                 55.87 
               
               
                 32 
                 CG 
                 ASN 
                 A 
                 104 
                 39.813 
                 98.196 
                 28.827 
                 1.00 
                 57.61 
               
               
                 33 
                 OD1 
                 ASN 
                 A 
                 104 
                 40.169 
                 98.892 
                 29.787 
                 1.00 
                 59.08 
               
               
                 34 
                 ND2 
                 ASN 
                 A 
                 104 
                 38.579 
                 98.229 
                 28.335 
                 1.00 
                 57.32 
               
               
                 35 
                 C 
                 ASN 
                 A 
                 104 
                 42.291 
                 95.288 
                 28.318 
                 1.00 
                 54.92 
               
               
                 36 
                 O 
                 ASN 
                 A 
                 104 
                 41.961 
                 94.153 
                 27.977 
                 1.00 
                 55.16 
               
               
                 37 
                 N 
                 THR 
                 A 
                 105 
                 43.486 
                 95.804 
                 28.047 
                 1.00 
                 54.02 
               
               
                 38 
                 CA 
                 THR 
                 A 
                 105 
                 44.488 
                 95.039 
                 27.319 
                 1.00 
                 53.20 
               
               
                 39 
                 CB 
                 THR 
                 A 
                 105 
                 45.788 
                 95.819 
                 27.171 
                 1.00 
                 55.37 
               
               
                 40 
                 OG1 
                 THR 
                 A 
                 105 
                 45.532 
                 97.048 
                 26.481 
                 1.00 
                 57.24 
               
               
                 41 
                 CG2 
                 THR 
                 A 
                 105 
                 46.807 
                 94.989 
                 26.403 
                 1.00 
                 54.39 
               
               
                 42 
                 C 
                 THR 
                 A 
                 105 
                 44.818 
                 93.756 
                 28.050 
                 1.00 
                 52.82 
               
               
                 43 
                 O 
                 THR 
                 A 
                 105 
                 44.861 
                 92.687 
                 27.451 
                 1.00 
                 53.56 
               
               
                 44 
                 N 
                 LEU 
                 A 
                 106 
                 45.062 
                 93.862 
                 29.349 
                 1.00 
                 50.68 
               
               
                 45 
                 CA 
                 LEU 
                 A 
                 106 
                 45.389 
                 92.690 
                 30.125 
                 1.00 
                 48.81 
               
               
                 46 
                 CB 
                 LEU 
                 A 
                 106 
                 45.758 
                 93.100 
                 31.557 
                 1.00 
                 47.15 
               
               
                 47 
                 CG 
                 LEU 
                 A 
                 106 
                 46.988 
                 94.031 
                 31.627 
                 1.00 
                 47.77 
               
               
                 48 
                 CD1 
                 LEU 
                 A 
                 106 
                 47.315 
                 94.387 
                 33.071 
                 1.00 
                 47.75 
               
               
                 49 
                 CD2 
                 LEU 
                 A 
                 106 
                 48.188 
                 93.358 
                 30.962 
                 1.00 
                 42.84 
               
               
                 50 
                 C 
                 LEU 
                 A 
                 106 
                 44.234 
                 91.695 
                 30.110 
                 1.00 
                 49.48 
               
               
                 51 
                 O 
                 LEU 
                 A 
                 106 
                 44.450 
                 90.484 
                 30.028 
                 1.00 
                 50.59 
               
               
                 52 
                 N 
                 ALA 
                 A 
                 107 
                 43.005 
                 92.193 
                 30.166 
                 1.00 
                 49.70 
               
               
                 53 
                 CA 
                 ALA 
                 A 
                 107 
                 41.846 
                 91.303 
                 30.176 
                 1.00 
                 50.54 
               
               
                 54 
                 CB 
                 ALA 
                 A 
                 107 
                 40.580 
                 92.089 
                 30.508 
                 1.00 
                 48.64 
               
               
                 55 
                 C 
                 ALA 
                 A 
                 107 
                 41.682 
                 90.570 
                 28.850 
                 1.00 
                 51.75 
               
               
                 56 
                 O 
                 ALA 
                 A 
                 107 
                 41.228 
                 89.426 
                 28.814 
                 1.00 
                 49.39 
               
               
                 57 
                 N 
                 GLN 
                 A 
                 108 
                 42.046 
                 91.229 
                 27.756 
                 1.00 
                 54.62 
               
               
                 58 
                 CA 
                 GLN 
                 A 
                 108 
                 41.921 
                 90.600 
                 26.457 
                 1.00 
                 57.26 
               
               
                 59 
                 CB 
                 GLN 
                 A 
                 108 
                 42.074 
                 91.622 
                 25.333 
                 1.00 
                 61.54 
               
               
                 60 
                 CG 
                 GLN 
                 A 
                 108 
                 41.327 
                 91.193 
                 24.084 
                 1.00 
                 71.90 
               
               
                 61 
                 CD 
                 GLN 
                 A 
                 108 
                 41.464 
                 92.167 
                 22.932 
                 1.00 
                 77.98 
               
               
                 62 
                 OE1 
                 GLN 
                 A 
                 108 
                 40.643 
                 92.175 
                 22.001 
                 1.00 
                 82.40 
               
               
                 63 
                 NE2 
                 GLN 
                 A 
                 108 
                 42.510 
                 92.989 
                 22.973 
                 1.00 
                 78.49 
               
               
                 64 
                 C 
                 GLN 
                 A 
                 108 
                 42.976 
                 89.509 
                 26.337 
                 1.00 
                 55.58 
               
               
                 65 
                 O 
                 GLN 
                 A 
                 108 
                 42.688 
                 88.415 
                 25.856 
                 1.00 
                 56.07 
               
               
                 66 
                 N 
                 ALA 
                 A 
                 109 
                 44.190 
                 89.804 
                 26.784 
                 1.00 
                 53.19 
               
               
                 67 
                 CA 
                 ALA 
                 A 
                 109 
                 45.266 
                 88.831 
                 26.742 
                 1.00 
                 52.55 
               
               
                 68 
                 CB 
                 ALA 
                 A 
                 109 
                 46.516 
                 89.435 
                 27.296 
                 1.00 
                 49.96 
               
               
                 69 
                 C 
                 ALA 
                 A 
                 109 
                 44.851 
                 87.611 
                 27.561 
                 1.00 
                 54.91 
               
               
                 70 
                 O 
                 ALA 
                 A 
                 109 
                 45.232 
                 86.476 
                 27.253 
                 1.00 
                 54.72 
               
               
                 71 
                 N 
                 GLU 
                 A 
                 110 
                 44.054 
                 87.845 
                 28.600 
                 1.00 
                 58.11 
               
               
                 72 
                 CA 
                 GLU 
                 A 
                 110 
                 43.568 
                 86.755 
                 29.450 
                 1.00 
                 62.24 
               
               
                 73 
                 CB 
                 GLU 
                 A 
                 110 
                 42.999 
                 87.308 
                 30.763 
                 1.00 
                 62.93 
               
               
                 74 
                 CG 
                 GLU 
                 A 
                 110 
                 44.052 
                 87.811 
                 31.732 
                 1.00 
                 68.89 
               
               
                 75 
                 CD 
                 GLU 
                 A 
                 110 
                 44.691 
                 86.694 
                 32.543 
                 1.00 
                 71.43 
               
               
                 76 
                 OE1 
                 GLU 
                 A 
                 110 
                 45.754 
                 86.942 
                 33.152 
                 1.00 
                 72.25 
               
               
                 77 
                 OE2 
                 GLU 
                 A 
                 110 
                 44.126 
                 85.575 
                 32.580 
                 1.00 
                 73.64 
               
               
                 78 
                 C 
                 GLU 
                 A 
                 110 
                 42.492 
                 85.933 
                 28.734 
                 1.00 
                 63.15 
               
               
                 79 
                 O 
                 GLU 
                 A 
                 110 
                 42.199 
                 84.816 
                 29.135 
                 1.00 
                 64.60 
               
               
                 80 
                 N 
                 VAL 
                 A 
                 111 
                 41.898 
                 86.496 
                 27.690 
                 1.00 
                 64.29 
               
               
                 81 
                 CA 
                 VAL 
                 A 
                 111 
                 40.870 
                 85.798 
                 26.930 
                 1.00 
                 66.07 
               
               
                 82 
                 CB 
                 VAL 
                 A 
                 111 
                 39.952 
                 86.795 
                 26.174 
                 1.00 
                 64.79 
               
               
                 83 
                 CG1 
                 VAL 
                 A 
                 111 
                 39.009 
                 86.050 
                 25.248 
                 1.00 
                 62.48 
               
               
                 84 
                 CG2 
                 VAL 
                 A 
                 111 
                 39.156 
                 87.611 
                 27.162 
                 1.00 
                 64.93 
               
               
                 85 
                 C 
                 VAL 
                 A 
                 111 
                 41.552 
                 84.890 
                 25.916 
                 1.00 
                 69.12 
               
               
                 86 
                 O 
                 VAL 
                 A 
                 111 
                 41.266 
                 83.692 
                 25.843 
                 1.00 
                 68.18 
               
               
                 87 
                 N 
                 ARG 
                 A 
                 112 
                 42.461 
                 85.479 
                 25.146 
                 1.00 
                 73.10 
               
               
                 88 
                 CA 
                 ARG 
                 A 
                 112 
                 43.204 
                 84.762 
                 24.122 
                 1.00 
                 76.92 
               
               
                 89 
                 CB 
                 ARG 
                 A 
                 112 
                 44.060 
                 85.745 
                 23.318 
                 1.00 
                 79.90 
               
               
                 90 
                 CG 
                 ARG 
                 A 
                 112 
                 43.264 
                 86.903 
                 22.704 
                 1.00 
                 84.65 
               
               
                 91 
                 CD 
                 ARG 
                 A 
                 112 
                 43.423 
                 86.958 
                 21.189 
                 1.00 
                 88.42 
               
               
                 92 
                 NE 
                 ARG 
                 A 
                 112 
                 44.657 
                 87.616 
                 20.762 
                 1.00 
                 91.17 
               
               
                 93 
                 CZ 
                 ARG 
                 A 
                 112 
                 45.423 
                 87.189 
                 19.759 
                 1.00 
                 93.20 
               
               
                 94 
                 NH1 
                 ARG 
                 A 
                 112 
                 45.092 
                 86.093 
                 19.082 
                 1.00 
                 93.43 
               
               
                 95 
                 NH2 
                 ARG 
                 A 
                 112 
                 46.509 
                 87.871 
                 19.422 
                 1.00 
                 94.12 
               
               
                 96 
                 C 
                 ARG 
                 A 
                 112 
                 44.079 
                 83.667 
                 24.725 
                 1.00 
                 78.59 
               
               
                 97 
                 O 
                 ARG 
                 A 
                 112 
                 44.341 
                 82.654 
                 24.077 
                 1.00 
                 79.07 
               
               
                 98 
                 N 
                 SER 
                 A 
                 113 
                 44.526 
                 83.862 
                 25.966 
                 1.00 
                 80.11 
               
               
                 99 
                 CA 
                 SER 
                 A 
                 113 
                 45.361 
                 82.858 
                 26.627 
                 1.00 
                 80.28 
               
               
                 100 
                 CB 
                 SER 
                 A 
                 113 
                 46.081 
                 83.456 
                 27.838 
                 1.00 
                 78.76 
               
               
                 101 
                 OG 
                 SER 
                 A 
                 113 
                 45.178 
                 83.675 
                 28.901 
                 1.00 
                 78.74 
               
               
                 102 
                 C 
                 SER 
                 A 
                 113 
                 44.524 
                 81.660 
                 27.077 
                 1.00 
                 80.80 
               
               
                 103 
                 O 
                 SER 
                 A 
                 113 
                 45.067 
                 80.598 
                 27.370 
                 1.00 
                 82.91 
               
               
                 104 
                 N 
                 ARG 
                 A 
                 114 
                 43.204 
                 81.831 
                 27.131 
                 1.00 
                 80.42 
               
               
                 105 
                 CA 
                 ARG 
                 A 
                 114 
                 42.308 
                 80.751 
                 27.532 
                 1.00 
                 80.13 
               
               
                 106 
                 CB 
                 ARG 
                 A 
                 114 
                 40.966 
                 81.303 
                 27.997 
                 1.00 
                 79.19 
               
               
                 107 
                 CG 
                 ARG 
                 A 
                 114 
                 40.966 
                 81.970 
                 29.349 
                 1.00 
                 78.23 
               
               
                 108 
                 CD 
                 ARG 
                 A 
                 114 
                 39.536 
                 82.002 
                 29.864 
                 1.00 
                 78.83 
               
               
                 109 
                 NE 
                 ARG 
                 A 
                 114 
                 39.356 
                 82.815 
                 31.061 
                 1.00 
                 79.39 
               
               
                 110 
                 CZ 
                 ARG 
                 A 
                 114 
                 39.216 
                 84.137 
                 31.054 
                 1.00 
                 79.53 
               
               
                 111 
                 NH1 
                 ARG 
                 A 
                 114 
                 39.056 
                 84.787 
                 32.197 
                 1.00 
                 81.50 
               
               
                 112 
                 NH2 
                 ARG 
                 A 
                 114 
                 39.226 
                 84.810 
                 29.913 
                 1.00 
                 78.80 
               
               
                 113 
                 C 
                 ARG 
                 A 
                 114 
                 42.058 
                 79.742 
                 26.407 
                 1.00 
                 81.14 
               
               
                 114 
                 O 
                 ARG 
                 A 
                 114 
                 41.591 
                 78.634 
                 26.655 
                 1.00 
                 79.80 
               
               
                 115 
                 N 
                 GLN 
                 A 
                 115 
                 42.335 
                 80.137 
                 25.170 
                 1.00 
                 83.68 
               
               
                 116 
                 CA 
                 GLN 
                 A 
                 115 
                 42.170 
                 79.228 
                 24.039 
                 1.00 
                 86.76 
               
               
                 117 
                 CB 
                 GLN 
                 A 
                 115 
                 41.785 
                 79.987 
                 22.768 
                 1.00 
                 86.56 
               
               
                 118 
                 CG 
                 GLN 
                 A 
                 115 
                 41.691 
                 81.489 
                 22.925 
                 1.00 
                 86.49 
               
               
                 119 
                 CD 
                 GLN 
                 A 
                 115 
                 41.601 
                 82.202 
                 21.588 
                 1.00 
                 86.47 
               
               
                 120 
                 OE1 
                 GLN 
                 A 
                 115 
                 42.576 
                 82.789 
                 21.106 
                 1.00 
                 86.58 
               
               
                 121 
                 NE2 
                 GLN 
                 A 
                 115 
                 40.429 
                 82.143 
                 20.973 
                 1.00 
                 85.92 
               
               
                 122 
                 C 
                 GLN 
                 A 
                 115 
                 43.540 
                 78.595 
                 23.855 
                 1.00 
                 88.96 
               
               
                 123 
                 O 
                 GLN 
                 A 
                 115 
                 44.478 
                 79.252 
                 23.397 
                 1.00 
                 89.14 
               
               
                 124 
                 N 
                 ILE 
                 A 
                 116 
                 43.664 
                 77.322 
                 24.214 
                 1.00 
                 91.44 
               
               
                 125 
                 CA 
                 ILE 
                 A 
                 116 
                 44.961 
                 76.663 
                 24.114 
                 1.00 
                 93.24 
               
               
                 126 
                 CB 
                 ILE 
                 A 
                 116 
                 45.815 
                 77.000 
                 25.352 
                 1.00 
                 92.35 
               
               
                 127 
                 CG2 
                 ILE 
                 A 
                 116 
                 46.407 
                 78.408 
                 25.215 
                 1.00 
                 91.76 
               
               
                 128 
                 CG1 
                 ILE 
                 A 
                 116 
                 44.958 
                 76.822 
                 26.614 
                 1.00 
                 90.28 
               
               
                 129 
                 CD1 
                 ILE 
                 A 
                 116 
                 45.614 
                 77.276 
                 27.899 
                 1.00 
                 88.50 
               
               
                 130 
                 C 
                 ILE 
                 A 
                 116 
                 44.953 
                 75.142 
                 23.950 
                 1.00 
                 94.87 
               
               
                 131 
                 O 
                 ILE 
                 A 
                 116 
                 44.137 
                 74.566 
                 23.231 
                 1.00 
                 95.95 
               
               
                 132 
                 N 
                 SER 
                 A 
                 117 
                 45.893 
                 74.511 
                 24.638 
                 1.00 
                 95.66 
               
               
                 133 
                 CA 
                 SER 
                 A 
                 117 
                 46.062 
                 73.071 
                 24.596 
                 1.00 
                 95.95 
               
               
                 134 
                 CB 
                 SER 
                 A 
                 117 
                 47.294 
                 72.737 
                 23.747 
                 1.00 
                 95.95 
               
               
                 135 
                 OG 
                 SER 
                 A 
                 117 
                 48.419 
                 73.495 
                 24.172 
                 1.00 
                 95.95 
               
               
                 136 
                 C 
                 SER 
                 A 
                 117 
                 46.248 
                 72.554 
                 26.023 
                 1.00 
                 95.95 
               
               
                 137 
                 O 
                 SER 
                 A 
                 117 
                 45.361 
                 72.706 
                 26.865 
                 1.00 
                 95.95 
               
               
                 138 
                 N 
                 VAL 
                 A 
                 118 
                 47.412 
                 71.954 
                 26.270 
                 1.00 
                 95.90 
               
               
                 139 
                 CA 
                 VAL 
                 A 
                 118 
                 47.792 
                 71.389 
                 27.565 
                 1.00 
                 95.32 
               
               
                 140 
                 CB 
                 VAL 
                 A 
                 118 
                 47.852 
                 72.499 
                 28.672 
                 1.00 
                 94.33 
               
               
                 141 
                 CG1 
                 VAL 
                 A 
                 118 
                 48.328 
                 73.813 
                 28.064 
                 1.00 
                 91.45 
               
               
                 142 
                 CG2 
                 VAL 
                 A 
                 118 
                 46.502 
                 72.652 
                 29.373 
                 1.00 
                 93.04 
               
               
                 143 
                 C 
                 VAL 
                 A 
                 118 
                 46.901 
                 70.223 
                 28.043 
                 1.00 
                 95.95 
               
               
                 144 
                 O 
                 VAL 
                 A 
                 118 
                 45.680 
                 70.206 
                 27.752 
                 1.00 
                 95.95 
               
               
                 145 
                 OXT 
                 VAL 
                 A 
                 118 
                 47.452 
                 69.328 
                 28.728 
                 1.00 
                 95.95 
               
               
                 146 
                   
                 VAL 
                 A 
                 118 
               
               
                 147 
                 CB 
                 ALA 
                 A 
                 123 
                 32.298 
                 61.127 
                 43.467 
                 1.00 
                 95.95 
               
               
                 148 
                 C 
                 ALA 
                 A 
                 123 
                 33.448 
                 62.457 
                 41.672 
                 1.00 
                 95.95 
               
               
                 149 
                 O 
                 ALA 
                 A 
                 123 
                 33.788 
                 61.585 
                 40.873 
                 1.00 
                 95.95 
               
               
                 150 
                 N 
                 ALA 
                 A 
                 123 
                 33.099 
                 63.412 
                 43.950 
                 1.00 
                 95.08 
               
               
                 151 
                 CA 
                 ALA 
                 A 
                 123 
                 33.385 
                 62.169 
                 43.180 
                 1.00 
                 95.95 
               
               
                 152 
                 TF 
                 SER 
                 A 
                 124 
                 33.172 
                 63.699 
                 41.296 
                 1.00 
                 95.95 
               
               
                 153 
                 CA 
                 SER 
                 A 
                 124 
                 33.119 
                 64.108 
                 39.891 
                 1.00 
                 95.75 
               
               
                 154 
                 CB 
                 SER 
                 A 
                 124 
                 31.683 
                 64.531 
                 39.618 
                 1.00 
                 95.95 
               
               
                 155 
                 OG 
                 SER 
                 A 
                 124 
                 31.143 
                 65.129 
                 40.796 
                 1.00 
                 95.95 
               
               
                 156 
                 C 
                 SER 
                 A 
                 124 
                 34.073 
                 65.234 
                 39.462 
                 1.00 
                 95.95 
               
               
                 157 
                 O 
                 SER 
                 A 
                 124 
                 35.130 
                 64.999 
                 38.866 
                 1.00 
                 95.95 
               
               
                 158 
                 N 
                 ALA 
                 A 
                 125 
                 33.629 
                 66.462 
                 39.727 
                 1.00 
                 95.95 
               
               
                 159 
                 CA 
                 ALA 
                 A 
                 125 
                 34.359 
                 67.697 
                 39.457 
                 1.00 
                 95.91 
               
               
                 160 
                 CB 
                 ALA 
                 A 
                 125 
                 33.465 
                 68.685 
                 38.715 
                 1.00 
                 95.50 
               
               
                 161 
                 C 
                 ALA 
                 A 
                 125 
                 34.581 
                 68.142 
                 40.896 
                 1.00 
                 95.95 
               
               
                 162 
                 O 
                 ALA 
                 A 
                 125 
                 34.035 
                 69.145 
                 41.371 
                 1.00 
                 95.06 
               
               
                 163 
                 N 
                 ASP 
                 A 
                 126 
                 35.368 
                 67.317 
                 41.584 
                 1.00 
                 95.95 
               
               
                 164 
                 CA 
                 ASP 
                 A 
                 126 
                 35.699 
                 67.474 
                 42.991 
                 1.00 
                 95.81 
               
               
                 165 
                 CB 
                 ASP 
                 A 
                 126 
                 35.100 
                 66.296 
                 43.759 
                 1.00 
                 95.13 
               
               
                 166 
                 CG 
                 ASP 
                 A 
                 126 
                 35.470 
                 66.293 
                 45.225 
                 1.00 
                 95.95 
               
               
                 167 
                 OD1 
                 ASP 
                 A 
                 126 
                 36.511 
                 66.878 
                 45.601 
                 1.00 
                 95.95 
               
               
                 168 
                 OD2 
                 ASP 
                 A 
                 126 
                 34.720 
                 65.678 
                 46.008 
                 1.00 
                 95.95 
               
               
                 169 
                 C 
                 ASP 
                 A 
                 126 
                 37.215 
                 67.491 
                 43.167 
                 1.00 
                 95.56 
               
               
                 170 
                 O 
                 ASP 
                 A 
                 126 
                 37.935 
                 66.729 
                 42.515 
                 1.00 
                 94.70 
               
               
                 171 
                 N 
                 ILE 
                 A 
                 127 
                 37.683 
                 68.351 
                 44.067 
                 1.00 
                 95.46 
               
               
                 172 
                 CA 
                 ILE 
                 A 
                 127 
                 39.107 
                 68.493 
                 44.333 
                 1.00 
                 95.63 
               
               
                 173 
                 CB 
                 ILE 
                 A 
                 127 
                 39.402 
                 69.858 
                 45.055 
                 1.00 
                 94.48 
               
               
                 174 
                 CG2 
                 ILE 
                 A 
                 127 
                 39.107 
                 69.765 
                 46.548 
                 1.00 
                 93.67 
               
               
                 175 
                 CG1 
                 ILE 
                 A 
                 127 
                 40.851 
                 70.282 
                 44.802 
                 1.00 
                 93.58 
               
               
                 176 
                 CD1 
                 ILE 
                 A 
                 127 
                 41.086 
                 70.811 
                 43.398 
                 1.00 
                 91.76 
               
               
                 177 
                 C 
                 ILE 
                 A 
                 127 
                 39.686 
                 67.330 
                 45.149 
                 1.00 
                 95.95 
               
               
                 178 
                 O 
                 ILE 
                 A 
                 127 
                 40.595 
                 66.642 
                 44.691 
                 1.00 
                 95.95 
               
               
                 179 
                 N 
                 ASN 
                 A 
                 128 
                 39.144 
                 67.091 
                 46.339 
                 1.00 
                 95.95 
               
               
                 180 
                 CA 
                 ASN 
                 A 
                 128 
                 39.645 
                 66.035 
                 47.213 
                 1.00 
                 95.82 
               
               
                 181 
                 CB 
                 ASN 
                 A 
                 128 
                 38.997 
                 66.187 
                 48.592 
                 1.00 
                 95.95 
               
               
                 182 
                 CG 
                 ASN 
                 A 
                 128 
                 39.344 
                 67.520 
                 49.246 
                 1.00 
                 95.95 
               
               
                 183 
                 OD1 
                 ASN 
                 A 
                 128 
                 38.486 
                 68.396 
                 49.404 
                 1.00 
                 95.95 
               
               
                 184 
                 ND2 
                 ASN 
                 A 
                 128 
                 40.619 
                 67.685 
                 49.617 
                 1.00 
                 95.95 
               
               
                 185 
                 C 
                 ASN 
                 A 
                 128 
                 39.497 
                 64.601 
                 46.683 
                 1.00 
                 94.84 
               
               
                 186 
                 O 
                 ASN 
                 A 
                 128 
                 39.398 
                 63.648 
                 47.453 
                 1.00 
                 95.23 
               
               
                 187 
                 N 
                 VAL 
                 A 
                 129 
                 39.516 
                 64.472 
                 45.359 
                 1.00 
                 93.62 
               
               
                 188 
                 CA 
                 VAL 
                 A 
                 129 
                 39.396 
                 63.200 
                 44.638 
                 1.00 
                 92.16 
               
               
                 189 
                 CB 
                 VAL 
                 A 
                 129 
                 37.917 
                 62.998 
                 44.111 
                 1.00 
                 92.64 
               
               
                 190 
                 CG1 
                 VAL 
                 A 
                 129 
                 37.872 
                 62.181 
                 42.829 
                 1.00 
                 91.97 
               
               
                 191 
                 CG2 
                 VAL 
                 A 
                 129 
                 37.093 
                 62.283 
                 45.151 
                 1.00 
                 92.68 
               
               
                 192 
                 C 
                 VAL 
                 A 
                 129 
                 40.364 
                 63.296 
                 43.451 
                 1.00 
                 91.17 
               
               
                 193 
                 O 
                 VAL 
                 A 
                 129 
                 40.031 
                 62.936 
                 42.324 
                 1.00 
                 90.51 
               
               
                 194 
                 N 
                 LYS 
                 A 
                 130 
                 41.581 
                 63.771 
                 43.672 
                 1.00 
                 89.45 
               
               
                 195 
                 CA 
                 LYS 
                 A 
                 130 
                 42.430 
                 63.896 
                 42.500 
                 1.00 
                 87.77 
               
               
                 196 
                 CB 
                 LYS 
                 A 
                 130 
                 42.509 
                 65.362 
                 42.085 
                 1.00 
                 86.37 
               
               
                 197 
                 CG 
                 LYS 
                 A 
                 130 
                 41.177 
                 66.057 
                 42.202 
                 1.00 
                 82.54 
               
               
                 198 
                 CD 
                 LYS 
                 A 
                 130 
                 41.136 
                 67.350 
                 41.452 
                 1.00 
                 79.99 
               
               
                 199 
                 CE 
                 LYS 
                 A 
                 130 
                 40.993 
                 67.065 
                 39.984 
                 1.00 
                 78.70 
               
               
                 200 
                 NZ 
                 LYS 
                 A 
                 130 
                 40.183 
                 68.120 
                 39.330 
                 1.00 
                 77.13 
               
               
                 201 
                 C 
                 LYS 
                 A 
                 130 
                 43.814 
                 63.299 
                 42.488 
                 1.00 
                 87.56 
               
               
                 202 
                 O 
                 LYS 
                 A 
                 130 
                 44.472 
                 63.142 
                 43.518 
                 1.00 
                 87.42 
               
               
                 203 
                 N 
                 ALA 
                 A 
                 131 
                 44.232 
                 62.968 
                 41.273 
                 1.00 
                 87.33 
               
               
                 204 
                 CA 
                 ALA 
                 A 
                 131 
                 45.529 
                 62.384 
                 41.027 
                 1.00 
                 87.17 
               
               
                 205 
                 CB 
                 ALA 
                 A 
                 131 
                 45.812 
                 62.359 
                 39.525 
                 1.00 
                 86.74 
               
               
                 206 
                 C 
                 ALA 
                 A 
                 131 
                 46.549 
                 63.244 
                 41.751 
                 1.00 
                 86.91 
               
               
                 207 
                 O 
                 ALA 
                 A 
                 131 
                 46.804 
                 64.381 
                 41.358 
                 1.00 
                 87.23 
               
               
                 208 
                 N 
                 ILE 
                 A 
                 132 
                 47.103 
                 62.708 
                 42.834 
                 1.00 
                 86.12 
               
               
                 209 
                 CA 
                 ILE 
                 A 
                 132 
                 48.105 
                 63.431 
                 43.596 
                 1.00 
                 84.31 
               
               
                 210 
                 CB 
                 ILE 
                 A 
                 132 
                 48.341 
                 62.773 
                 44.960 
                 1.00 
                 82.19 
               
               
                 211 
                 CG2 
                 ILE 
                 A 
                 132 
                 49.592 
                 63.329 
                 45.591 
                 1.00 
                 80.93 
               
               
                 212 
                 CG1 
                 ILE 
                 A 
                 132 
                 47.116 
                 63.017 
                 45.849 
                 1.00 
                 81.34 
               
               
                 213 
                 CD1 
                 ILE 
                 A 
                 132 
                 47.295 
                 62.619 
                 47.293 
                 1.00 
                 79.69 
               
               
                 214 
                 C 
                 ILE 
                 A 
                 132 
                 49.388 
                 63.480 
                 42.773 
                 1.00 
                 85.57 
               
               
                 215 
                 O 
                 ILE 
                 A 
                 132 
                 49.859 
                 62.467 
                 42.256 
                 1.00 
                 85.67 
               
               
                 216 
                 N 
                 ALA 
                 A 
                 133 
                 49.934 
                 64.684 
                 42.656 
                 1.00 
                 86.78 
               
               
                 217 
                 CA 
                 ALA 
                 A 
                 133 
                 51.124 
                 64.955 
                 41.859 
                 1.00 
                 86.55 
               
               
                 218 
                 CB 
                 ALA 
                 A 
                 133 
                 51.216 
                 66.455 
                 41.596 
                 1.00 
                 87.10 
               
               
                 219 
                 C 
                 ALA 
                 A 
                 133 
                 52.480 
                 64.446 
                 42.322 
                 1.00 
                 86.05 
               
               
                 220 
                 O 
                 ALA 
                 A 
                 133 
                 52.785 
                 64.360 
                 43.514 
                 1.00 
                 85.49 
               
               
                 221 
                 N 
                 SER 
                 A 
                 134 
                 53.294 
                 64.141 
                 41.319 
                 1.00 
                 85.85 
               
               
                 222 
                 CA 
                 SER 
                 A 
                 134 
                 54.651 
                 63.648 
                 41.480 
                 1.00 
                 85.47 
               
               
                 223 
                 CB 
                 SER 
                 A 
                 134 
                 54.836 
                 62.369 
                 40.667 
                 1.00 
                 86.54 
               
               
                 224 
                 OG 
                 SER 
                 A 
                 134 
                 54.405 
                 62.563 
                 39.326 
                 1.00 
                 85.37 
               
               
                 225 
                 C 
                 SER 
                 A 
                 134 
                 55.569 
                 64.723 
                 40.930 
                 1.00 
                 84.17 
               
               
                 226 
                 O 
                 SER 
                 A 
                 134 
                 55.111 
                 65.648 
                 40.265 
                 1.00 
                 84.65 
               
               
                 227 
                 N 
                 ILE 
                 A 
                 135 
                 56.861 
                 64.591 
                 41.192 
                 1.00 
                 82.68 
               
               
                 228 
                 CA 
                 ILE 
                 A 
                 135 
                 57.822 
                 65.569 
                 40.714 
                 1.00 
                 81.44 
               
               
                 229 
                 CB 
                 ILE 
                 A 
                 135 
                 59.241 
                 65.123 
                 41.049 
                 1.00 
                 81.17 
               
               
                 230 
                 CG2 
                 ILE 
                 A 
                 135 
                 60.237 
                 66.153 
                 40.560 
                 1.00 
                 81.24 
               
               
                 231 
                 CG1 
                 ILE 
                 A 
                 135 
                 59.360 
                 64.918 
                 42.559 
                 1.00 
                 81.55 
               
               
                 232 
                 CD1 
                 ILE 
                 A 
                 135 
                 60.675 
                 64.319 
                 42.990 
                 1.00 
                 81.94 
               
               
                 233 
                 C 
                 ILE 
                 A 
                 135 
                 57.694 
                 65.765 
                 39.205 
                 1.00 
                 81.19 
               
               
                 234 
                 O 
                 ILE 
                 A 
                 135 
                 57.644 
                 66.897 
                 38.717 
                 1.00 
                 81.57 
               
               
                 235 
                 N 
                 GLY 
                 A 
                 136 
                 57.632 
                 64.651 
                 38.480 
                 1.00 
                 79.98 
               
               
                 236 
                 CA 
                 GLY 
                 A 
                 136 
                 57.515 
                 64.697 
                 37.032 
                 1.00 
                 78.08 
               
               
                 237 
                 C 
                 GLY 
                 A 
                 136 
                 56.169 
                 65.234 
                 36.607 
                 1.00 
                 77.36 
               
               
                 238 
                 O 
                 GLY 
                 A 
                 136 
                 56.030 
                 65.806 
                 35.523 
                 1.00 
                 77.19 
               
               
                 239 
                 N 
                 ASP 
                 A 
                 137 
                 55.160 
                 65.030 
                 37.446 
                 1.00 
                 77.11 
               
               
                 240 
                 CA 
                 ASP 
                 A 
                 137 
                 53.834 
                 65.552 
                 37.142 
                 1.00 
                 77.27 
               
               
                 241 
                 CB 
                 ASP 
                 A 
                 137 
                 52.807 
                 65.111 
                 38.190 
                 1.00 
                 78.06 
               
               
                 242 
                 CG 
                 ASP 
                 A 
                 137 
                 52.206 
                 63.747 
                 37.885 
                 1.00 
                 79.23 
               
               
                 243 
                 OD1 
                 ASP 
                 A 
                 137 
                 52.224 
                 63.351 
                 36.700 
                 1.00 
                 79.32 
               
               
                 244 
                 OD2 
                 ASP 
                 A 
                 137 
                 51.700 
                 63.084 
                 38.820 
                 1.00 
                 78.62 
               
               
                 245 
                 C 
                 ASP 
                 A 
                 137 
                 53.959 
                 67.072 
                 37.157 
                 1.00 
                 76.82 
               
               
                 246 
                 O 
                 ASP 
                 A 
                 137 
                 53.535 
                 67.755 
                 36.225 
                 1.00 
                 77.73 
               
               
                 247 
                 N 
                 VAL 
                 A 
                 138 
                 54.566 
                 67.583 
                 38.227 
                 1.00 
                 74.98 
               
               
                 248 
                 CA 
                 VAL 
                 A 
                 138 
                 54.790 
                 69.011 
                 38.407 
                 1.00 
                 72.09 
               
               
                 249 
                 CB 
                 VAL 
                 A 
                 138 
                 55.500 
                 69.275 
                 39.758 
                 1.00 
                 69.50 
               
               
                 250 
                 CG1 
                 VAL 
                 A 
                 138 
                 56.007 
                 70.698 
                 39.823 
                 1.00 
                 68.92 
               
               
                 251 
                 CG2 
                 VAL 
                 A 
                 138 
                 54.532 
                 69.030 
                 40.902 
                 1.00 
                 68.43 
               
               
                 252 
                 C 
                 VAL 
                 A 
                 138 
                 55.620 
                 69.607 
                 37.264 
                 1.00 
                 73.00 
               
               
                 253 
                 O 
                 VAL 
                 A 
                 138 
                 55.225 
                 70.598 
                 36.650 
                 1.00 
                 73.94 
               
               
                 254 
                 N 
                 CYS 
                 A 
                 139 
                 56.764 
                 68.998 
                 36.970 
                 1.00 
                 73.34 
               
               
                 255 
                 CA 
                 CYS 
                 A 
                 139 
                 57.640 
                 69.487 
                 35.910 
                 1.00 
                 73.46 
               
               
                 256 
                 CB 
                 CYS 
                 A 
                 139 
                 58.912 
                 68.646 
                 35.844 
                 1.00 
                 73.03 
               
               
                 257 
                 SG 
                 CYS 
                 A 
                 139 
                 59.882 
                 68.672 
                 37.361 
                 1.00 
                 75.79 
               
               
                 258 
                 C 
                 CYS 
                 A 
                 139 
                 56.991 
                 69.518 
                 34.534 
                 1.00 
                 73.93 
               
               
                 259 
                 O 
                 CYS 
                 A 
                 139 
                 57.506 
                 70.158 
                 33.622 
                 1.00 
                 73.62 
               
               
                 260 
                 N 
                 GLU 
                 A 
                 140 
                 55.878 
                 68.821 
                 34.367 
                 1.00 
                 75.40 
               
               
                 261 
                 CA 
                 GLU 
                 A 
                 140 
                 55.211 
                 68.835 
                 33.072 
                 1.00 
                 78.36 
               
               
                 262 
                 CB 
                 GLU 
                 A 
                 140 
                 54.348 
                 67.585 
                 32.881 
                 1.00 
                 82.20 
               
               
                 263 
                 CG 
                 GLU 
                 A 
                 140 
                 54.283 
                 67.089 
                 31.432 
                 1.00 
                 88.31 
               
               
                 264 
                 CD 
                 GLU 
                 A 
                 140 
                 55.670 
                 66.768 
                 30.843 
                 1.00 
                 93.87 
               
               
                 265 
                 OE1 
                 GLU 
                 A 
                 140 
                 56.531 
                 66.209 
                 31.572 
                 1.00 
                 95.48 
               
               
                 266 
                 OE2 
                 GLU 
                 A 
                 140 
                 55.893 
                 67.063 
                 29.643 
                 1.00 
                 95.89 
               
               
                 267 
                 C 
                 GLU 
                 A 
                 140 
                 54.347 
                 70.090 
                 33.021 
                 1.00 
                 77.74 
               
               
                 268 
                 O 
                 GLU 
                 A 
                 140 
                 54.432 
                 70.866 
                 32.062 
                 1.00 
                 78.09 
               
               
                 269 
                 N 
                 SER 
                 A 
                 141 
                 53.527 
                 70.285 
                 34.057 
                 1.00 
                 75.94 
               
               
                 270 
                 CA 
                 SER 
                 A 
                 141 
                 52.673 
                 71.469 
                 34.152 
                 1.00 
                 73.84 
               
               
                 271 
                 CB 
                 SER 
                 A 
                 141 
                 52.051 
                 71.599 
                 35.541 
                 1.00 
                 72.73 
               
               
                 272 
                 OG 
                 SER 
                 A 
                 141 
                 50.862 
                 70.852 
                 35.654 
                 1.00 
                 73.73 
               
               
                 273 
                 C 
                 SER 
                 A 
                 141 
                 53.536 
                 72.689 
                 33.910 
                 1.00 
                 73.29 
               
               
                 274 
                 O 
                 SER 
                 A 
                 141 
                 53.152 
                 73.587 
                 33.169 
                 1.00 
                 73.32 
               
               
                 275 
                 N 
                 MET 
                 A 
                 142 
                 54.707 
                 72.710 
                 34.538 
                 1.00 
                 71.76 
               
               
                 276 
                 CA 
                 MET 
                 A 
                 142 
                 55.613 
                 73.829 
                 34.382 
                 1.00 
                 71.52 
               
               
                 277 
                 CB 
                 MET 
                 A 
                 142 
                 56.916 
                 73.573 
                 35.136 
                 1.00 
                 69.70 
               
               
                 278 
                 CG 
                 MET 
                 A 
                 142 
                 56.762 
                 73.592 
                 36.651 
                 1.00 
                 70.49 
               
               
                 279 
                 SD 
                 MET 
                 A 
                 142 
                 58.341 
                 73.522 
                 37.548 
                 1.00 
                 71.68 
               
               
                 280 
                 CE 
                 MET 
                 A 
                 142 
                 57.787 
                 73.490 
                 39.227 
                 1.00 
                 72.18 
               
               
                 281 
                 C 
                 MET 
                 A 
                 142 
                 55.901 
                 74.123 
                 32.917 
                 1.00 
                 72.98 
               
               
                 282 
                 O 
                 MET 
                 A 
                 142 
                 55.819 
                 75.280 
                 32.488 
                 1.00 
                 74.62 
               
               
                 283 
                 N 
                 ALA 
                 A 
                 143 
                 56.223 
                 73.091 
                 32.140 
                 1.00 
                 73.11 
               
               
                 284 
                 CA 
                 ALA 
                 A 
                 143 
                 56.524 
                 73.283 
                 30.719 
                 1.00 
                 73.25 
               
               
                 285 
                 CB 
                 ALA 
                 A 
                 143 
                 57.026 
                 71.985 
                 30.098 
                 1.00 
                 72.62 
               
               
                 286 
                 C 
                 ALA 
                 A 
                 143 
                 55.298 
                 73.781 
                 29.966 
                 1.00 
                 73.43 
               
               
                 287 
                 O 
                 ALA 
                 A 
                 143 
                 55.389 
                 74.701 
                 29.147 
                 1.00 
                 73.18 
               
               
                 288 
                 N 
                 GLN 
                 A 
                 144 
                 54.154 
                 73.158 
                 30.238 
                 1.00 
                 73.15 
               
               
                 289 
                 CA 
                 GLN 
                 A 
                 144 
                 52.901 
                 73.553 
                 29.604 
                 1.00 
                 73.54 
               
               
                 290 
                 CB 
                 GLN 
                 A 
                 144 
                 51.719 
                 72.800 
                 30.234 
                 1.00 
                 75.06 
               
               
                 291 
                 CG 
                 GLN 
                 A 
                 144 
                 51.543 
                 71.338 
                 29.826 
                 1.00 
                 77.70 
               
               
                 292 
                 CD 
                 GLN 
                 A 
                 144 
                 50.398 
                 70.643 
                 30.581 
                 1.00 
                 79.20 
               
               
                 293 
                 OE1 
                 GLN 
                 A 
                 144 
                 49.310 
                 71.195 
                 30.741 
                 1.00 
                 80.93 
               
               
                 294 
                 NE2 
                 GLN 
                 A 
                 144 
                 50.648 
                 69.424 
                 31.037 
                 1.00 
                 80.45 
               
               
                 295 
                 C 
                 GLN 
                 A 
                 144 
                 52.705 
                 75.052 
                 29.838 
                 1.00 
                 72.67 
               
               
                 296 
                 O 
                 GLN 
                 A 
                 144 
                 52.608 
                 75.848 
                 28.901 
                 1.00 
                 73.16 
               
               
                 297 
                 N 
                 GLN 
                 A 
                 145 
                 52.670 
                 75.415 
                 31.117 
                 1.00 
                 70.73 
               
               
                 298 
                 CA 
                 GLN 
                 A 
                 145 
                 52.454 
                 76.781 
                 31.560 
                 1.00 
                 67.58 
               
               
                 299 
                 CB 
                 GLN 
                 A 
                 145 
                 52.344 
                 76.797 
                 33.077 
                 1.00 
                 65.85 
               
               
                 300 
                 CG 
                 GLN 
                 A 
                 145 
                 51.157 
                 76.015 
                 33.569 
                 1.00 
                 64.88 
               
               
                 301 
                 CD 
                 GLN 
                 A 
                 145 
                 49.858 
                 76.610 
                 33.090 
                 1.00 
                 66.60 
               
               
                 302 
                 OE1 
                 GLN 
                 A 
                 145 
                 48.841 
                 75.922 
                 32.999 
                 1.00 
                 69.03 
               
               
                 303 
                 NE2 
                 GLN 
                 A 
                 145 
                 49.876 
                 77.906 
                 32.793 
                 1.00 
                 66.18 
               
               
                 304 
                 C 
                 GLN 
                 A 
                 145 
                 53.480 
                 77.792 
                 31.101 
                 1.00 
                 67.27 
               
               
                 305 
                 O 
                 GLN 
                 A 
                 145 
                 53.203 
                 78.990 
                 31.096 
                 1.00 
                 67.02 
               
               
                 306 
                 N 
                 LEU 
                 A 
                 146 
                 54.664 
                 77.325 
                 30.721 
                 1.00 
                 67.13 
               
               
                 307 
                 CA 
                 LEU 
                 A 
                 146 
                 55.699 
                 78.233 
                 30.243 
                 1.00 
                 68.36 
               
               
                 308 
                 CB 
                 LEU 
                 A 
                 146 
                 57.086 
                 77.617 
                 30.419 
                 1.00 
                 68.70 
               
               
                 309 
                 CG 
                 LEU 
                 A 
                 146 
                 57.663 
                 77.717 
                 31.834 
                 1.00 
                 70.98 
               
               
                 310 
                 CD1 
                 LEU 
                 A 
                 146 
                 58.943 
                 76.891 
                 31.938 
                 1.00 
                 69.66 
               
               
                 311 
                 CD2 
                 LEU 
                 A 
                 146 
                 57.933 
                 79.189 
                 32.168 
                 1.00 
                 69.79 
               
               
                 312 
                 C 
                 LEU 
                 A 
                 146 
                 55.448 
                 78.550 
                 28.777 
                 1.00 
                 70.12 
               
               
                 313 
                 O 
                 LEU 
                 A 
                 146 
                 55.967 
                 79.534 
                 28.240 
                 1.00 
                 72.20 
               
               
                 314 
                 N 
                 LEU 
                 A 
                 147 
                 54.653 
                 77.706 
                 28.125 
                 1.00 
                 70.46 
               
               
                 315 
                 CA 
                 LEU 
                 A 
                 147 
                 54.309 
                 77.928 
                 26.728 
                 1.00 
                 70.71 
               
               
                 316 
                 CB 
                 LEU 
                 A 
                 147 
                 53.993 
                 76.599 
                 26.036 
                 1.00 
                 71.32 
               
               
                 317 
                 CG 
                 LEU 
                 A 
                 147 
                 55.209 
                 75.680 
                 25.849 
                 1.00 
                 72.36 
               
               
                 318 
                 CD1 
                 LEU 
                 A 
                 147 
                 54.753 
                 74.329 
                 25.364 
                 1.00 
                 71.57 
               
               
                 319 
                 CD2 
                 LEU 
                 A 
                 147 
                 56.196 
                 76.295 
                 24.860 
                 1.00 
                 72.32 
               
               
                 320 
                 C 
                 LEU 
                 A 
                 147 
                 53.100 
                 78.857 
                 26.729 
                 1.00 
                 69.91 
               
               
                 321 
                 O 
                 LEU 
                 A 
                 147 
                 52.978 
                 79.734 
                 25.870 
                 1.00 
                 71.07 
               
               
                 322 
                 N 
                 VAL 
                 A 
                 148 
                 52.217 
                 78.669 
                 27.708 
                 1.00 
                 67.53 
               
               
                 323 
                 CA 
                 VAL 
                 A 
                 148 
                 51.046 
                 79.526 
                 27.858 
                 1.00 
                 65.43 
               
               
                 324 
                 CB 
                 VAL 
                 A 
                 148 
                 50.229 
                 79.165 
                 29.114 
                 1.00 
                 64.44 
               
               
                 325 
                 CG1 
                 VAL 
                 A 
                 148 
                 49.128 
                 80.189 
                 29.328 
                 1.00 
                 61.99 
               
               
                 326 
                 CG2 
                 VAL 
                 A 
                 148 
                 49.634 
                 77.780 
                 28.972 
                 1.00 
                 64.58 
               
               
                 327 
                 C 
                 VAL 
                 A 
                 148 
                 51.591 
                 80.937 
                 28.040 
                 1.00 
                 65.14 
               
               
                 328 
                 O 
                 VAL 
                 A 
                 148 
                 51.013 
                 81.911 
                 27.563 
                 1.00 
                 65.26 
               
               
                 329 
                 N 
                 LEU 
                 A 
                 149 
                 52.721 
                 81.020 
                 28.736 
                 1.00 
                 64.53 
               
               
                 330 
                 CA 
                 LEU 
                 A 
                 149 
                 53.397 
                 82.279 
                 29.004 
                 1.00 
                 64.62 
               
               
                 331 
                 CB 
                 LEU 
                 A 
                 149 
                 54.642 
                 82.029 
                 29.860 
                 1.00 
                 62.67 
               
               
                 332 
                 CO 
                 LEU 
                 A 
                 149 
                 55.497 
                 83.261 
                 30.169 
                 1.00 
                 63.20 
               
               
                 333 
                 CD1 
                 LEU 
                 A 
                 149 
                 54.716 
                 84.234 
                 31.040 
                 1.00 
                 64.08 
               
               
                 334 
                 CD2 
                 LEU 
                 A 
                 149 
                 56.761 
                 82.834 
                 30.866 
                 1.00 
                 62.00 
               
               
                 335 
                 C 
                 LEU 
                 A 
                 149 
                 53.801 
                 82.990 
                 27.715 
                 1.00 
                 65.16 
               
               
                 336 
                 O 
                 LEU 
                 A 
                 149 
                 53.492 
                 84.164 
                 27.525 
                 1.00 
                 66.07 
               
               
                 337 
                 N 
                 VAL 
                 A 
                 150 
                 54.497 
                 82.280 
                 26.833 
                 1.00 
                 65.72 
               
               
                 338 
                 CA 
                 VAL 
                 A 
                 150 
                 54.941 
                 82.859 
                 25.568 
                 1.00 
                 65.84 
               
               
                 339 
                 CB 
                 VAL 
                 A 
                 150 
                 55.743 
                 81.833 
                 24.732 
                 1.00 
                 65.71 
               
               
                 340 
                 CG1 
                 VAL 
                 A 
                 150 
                 56.208 
                 82.473 
                 23.443 
                 1.00 
                 64.98 
               
               
                 341 
                 CG2 
                 VAL 
                 A 
                 150 
                 56.940 
                 81.330 
                 25.522 
                 1.00 
                 63.28 
               
               
                 342 
                 C 
                 VAL 
                 A 
                 150 
                 53.758 
                 83.360 
                 24.737 
                 1.00 
                 67.17 
               
               
                 343 
                 O 
                 VAL 
                 A 
                 150 
                 53.846 
                 84.394 
                 24.075 
                 1.00 
                 66.64 
               
               
                 344 
                 N 
                 GLU 
                 A 
                 151 
                 52.651 
                 82.629 
                 24.771 
                 1.00 
                 68.10 
               
               
                 345 
                 CA 
                 GLU 
                 A 
                 151 
                 51.477 
                 83.040 
                 24.021 
                 1.00 
                 70.10 
               
               
                 346 
                 CB 
                 GLU 
                 A 
                 151 
                 50.471 
                 81.891 
                 23.919 
                 1.00 
                 73.89 
               
               
                 347 
                 CG 
                 GLU 
                 A 
                 151 
                 50.815 
                 80.889 
                 22.807 
                 1.00 
                 80.45 
               
               
                 348 
                 CD 
                 GLU 
                 A 
                 151 
                 51.083 
                 81.575 
                 21.457 
                 1.00 
                 84.36 
               
               
                 349 
                 OE1 
                 GLU 
                 A 
                 151 
                 50.187 
                 82.3a5 
                 20.960 
                 1.00 
                 85.05 
               
               
                 350 
                 OE2 
                 GLU 
                 A 
                 151 
                 52.192 
                 81.388 
                 20.896 
                 1.00 
                 84.09 
               
               
                 351 
                 C 
                 GLU 
                 A 
                 151 
                 50.829 
                 84.257 
                 24.658 
                 1.00 
                 69.69 
               
               
                 352 
                 O 
                 GLU 
                 A 
                 151 
                 50.457 
                 85.199 
                 23.962 
                 1.00 
                 71.57 
               
               
                 353 
                 N 
                 TRP 
                 A 
                 152 
                 50.702 
                 84.232 
                 25.981 
                 1.00 
                 67.95 
               
               
                 354 
                 CA 
                 TRP 
                 A 
                 152 
                 50.113 
                 85.336 
                 26.735 
                 1.00 
                 65.17 
               
               
                 355 
                 CB 
                 TRP 
                 A 
                 152 
                 50.254 
                 85.073 
                 28.235 
                 1.00 
                 64.16 
               
               
                 356 
                 CG 
                 TRP 
                 A 
                 152 
                 49.864 
                 86.229 
                 29.117 
                 1.00 
                 63.25 
               
               
                 357 
                 CD2 
                 TRP 
                 A 
                 152 
                 50.753 
                 87.169 
                 29.740 
                 1.00 
                 62.56 
               
               
                 358 
                 CE2 
                 TRP 
                 A 
                 152 
                 49.957 
                 88.053 
                 30.496 
                 1.00 
                 62.55 
               
               
                 359 
                 CE3 
                 TRP 
                 A 
                 152 
                 52.146 
                 87.315 
                 29.767 
                 1.00 
                 60.84 
               
               
                 360 
                 CD1 
                 TRP 
                 A 
                 152 
                 48.602 
                 86.596 
                 29.484 
                 1.00 
                 62.18 
               
               
                 361 
                 NE1 
                 TRP 
                 A 
                 152 
                 48.649 
                 87.693 
                 30.309 
                 1.00 
                 61.89 
               
               
                 362 
                 CZ2 
                 TRP 
                 A 
                 152 
                 50.508 
                 89.115 
                 31.230 
                 1.00 
                 63.00 
               
               
                 363 
                 CZ3 
                 TRP 
                 A 
                 152 
                 52.691 
                 88.363 
                 30.497 
                 1.00 
                 61.77 
               
               
                 364 
                 CH2 
                 TRP 
                 A 
                 152 
                 51.873 
                 89.238 
                 31.235 
                 1.00 
                 62.39 
               
               
                 365 
                 C 
                 TRP 
                 A 
                 152 
                 50.807 
                 86.647 
                 26.394 
                 1.00 
                 64.30 
               
               
                 366 
                 O 
                 TRP 
                 A 
                 152 
                 50.153 
                 87.631 
                 26.066 
                 1.00 
                 63.52 
               
               
                 367 
                 N 
                 ALA 
                 A 
                 153 
                 52.133 
                 86.648 
                 26.481 
                 1.00 
                 63.82 
               
               
                 368 
                 CA 
                 ALA 
                 A 
                 153 
                 52.932 
                 87.834 
                 26.193 
                 1.00 
                 64.71 
               
               
                 369 
                 CB 
                 ALA 
                 A 
                 153 
                 54.420 
                 87.512 
                 26.341 
                 1.00 
                 61.96 
               
               
                 370 
                 C 
                 ALA 
                 A 
                 153 
                 52.651 
                 88.383 
                 24.801 
                 1.00 
                 66.54 
               
               
                 371 
                 O 
                 ALA 
                 A 
                 153 
                 52.554 
                 89.590 
                 24.618 
                 1.00 
                 65.93 
               
               
                 372 
                 N 
                 LYS 
                 A 
                 154 
                 52.523 
                 87.488 
                 23.823 
                 1.00 
                 70.74 
               
               
                 373 
                 CA 
                 LYS 
                 A 
                 154 
                 52.258 
                 87.879 
                 22.442 
                 1.00 
                 74.19 
               
               
                 374 
                 CB 
                 LYS 
                 A 
                 154 
                 52.267 
                 86.652 
                 21.536 
                 1.00 
                 76.20 
               
               
                 375 
                 CG 
                 LYS 
                 A 
                 154 
                 53.642 
                 86.226 
                 21.068 
                 1.00 
                 79.72 
               
               
                 376 
                 CD 
                 LYS 
                 A 
                 154 
                 53.520 
                 85.062 
                 20.095 
                 1.00 
                 83.94 
               
               
                 377 
                 CE 
                 LYS 
                 A 
                 154 
                 54.804 
                 84.847 
                 19.311 
                 1.00 
                 86.83 
               
               
                 378 
                 NZ 
                 LYS 
                 A 
                 154 
                 54.625 
                 83.810 
                 18.253 
                 1.00 
                 89.17 
               
               
                 379 
                 C 
                 LYS 
                 A 
                 154 
                 50.941 
                 88.625 
                 22.245 
                 1.00 
                 75.81 
               
               
                 380 
                 O 
                 LYS 
                 A 
                 154 
                 50.834 
                 89.476 
                 21.358 
                 1.00 
                 76.31 
               
               
                 381 
                 N 
                 TYR 
                 A 
                 155 
                 49.940 
                 88.305 
                 23.063 
                 1.00 
                 76.01 
               
               
                 382 
                 CA 
                 TYR 
                 A 
                 155 
                 48.645 
                 88.957 
                 22.952 
                 1.00 
                 76.70 
               
               
                 383 
                 CB 
                 TYR 
                 A 
                 155 
                 47.555 
                 88.091 
                 23.580 
                 1.00 
                 81.46 
               
               
                 384 
                 CG 
                 TYR 
                 A 
                 155 
                 47.524 
                 86.668 
                 23.057 
                 1.00 
                 87.69 
               
               
                 385 
                 CD1 
                 TYR 
                 A 
                 155 
                 47.884 
                 86.376 
                 21.738 
                 1.00 
                 90.53 
               
               
                 386 
                 CE1 
                 TYR 
                 A 
                 155 
                 47.817 
                 85.067 
                 21.240 
                 1.00 
                 93.30 
               
               
                 387 
                 CD2 
                 TYR 
                 A 
                 155 
                 47.095 
                 85.617 
                 23.868 
                 1.00 
                 90.10 
               
               
                 388 
                 CE2 
                 TYR 
                 A 
                 155 
                 47.020 
                 84.309 
                 23.381 
                 1.00 
                 92.95 
               
               
                 389 
                 CZ 
                 TYR 
                 A 
                 155 
                 47.379 
                 84.041 
                 22.067 
                 1.00 
                 93.86 
               
               
                 390 
                 OH 
                 TYR 
                 A 
                 155 
                 47.282 
                 82.753 
                 21.582 
                 1.00 
                 94.60 
               
               
                 391 
                 C 
                 TYR 
                 A 
                 155 
                 48.646 
                 90.336 
                 23.593 
                 1.00 
                 75.45 
               
               
                 392 
                 O 
                 TYR 
                 A 
                 155 
                 47.600 
                 90.961 
                 23.741 
                 1.00 
                 76.85 
               
               
                 393 
                 N 
                 ILE 
                 A 
                 156 
                 49.825 
                 90.800 
                 23.986 
                 1.00 
                 72.89 
               
               
                 394 
                 CA 
                 ILE 
                 A 
                 156 
                 49.976 
                 92.123 
                 24.571 
                 1.00 
                 71.65 
               
               
                 395 
                 CB 
                 ILE 
                 A 
                 156 
                 50.731 
                 92.076 
                 25.911 
                 1.00 
                 68.23 
               
               
                 396 
                 CG2 
                 ILE 
                 A 
                 156 
                 51.109 
                 93.481 
                 26.331 
                 1.00 
                 66.06 
               
               
                 397 
                 CG1 
                 ILE 
                 A 
                 156 
                 49.864 
                 91.404 
                 26.981 
                 1.00 
                 65.29 
               
               
                 398 
                 CD1 
                 ILE 
                 A 
                 156 
                 50.620 
                 90.992 
                 28.221 
                 1.00 
                 59.40 
               
               
                 399 
                 C 
                 ILE 
                 A 
                 156 
                 50.807 
                 92.906 
                 23.562 
                 1.00 
                 75.04 
               
               
                 400 
                 O 
                 ILE 
                 A 
                 156 
                 52.015 
                 92.690 
                 23.443 
                 1.00 
                 75.84 
               
               
                 401 
                 N 
                 PRO 
                 A 
                 157 
                 50.166 
                 93.826 
                 22.820 
                 1.00 
                 76.73 
               
               
                 402 
                 CD 
                 PRO 
                 A 
                 157 
                 48.825 
                 94.320 
                 23.163 
                 1.00 
                 77.28 
               
               
                 403 
                 CA 
                 PRO 
                 A 
                 157 
                 50.767 
                 94.682 
                 21.787 
                 1.00 
                 78.12 
               
               
                 404 
                 CG 
                 PRO 
                 A 
                 157 
                 49.688 
                 95.739 
                 21.546 
                 1.00 
                 78.74 
               
               
                 405 
                 CG 
                 PRO 
                 A 
                 157 
                 48.957 
                 95.784 
                 22.854 
                 1.00 
                 78.01 
               
               
                 406 
                 C 
                 PRO 
                 A 
                 157 
                 52.116 
                 95.307 
                 22.120 
                 1.00 
                 78.74 
               
               
                 407 
                 O 
                 PRO 
                 A 
                 157 
                 53.092 
                 95.130 
                 21.385 
                 1.00 
                 78.83 
               
               
                 408 
                 N 
                 ALA 
                 A 
                 158 
                 52.167 
                 96.048 
                 23.221 
                 1.00 
                 79.14 
               
               
                 409 
                 CA 
                 ALA 
                 A 
                 158 
                 53.402 
                 96.696 
                 23.645 
                 1.00 
                 79.39 
               
               
                 410 
                 CG 
                 ALA 
                 A 
                 158 
                 53.204 
                 97.311 
                 25.027 
                 1.00 
                 78.10 
               
               
                 411 
                 C 
                 ALA 
                 A 
                 158 
                 54.593 
                 95.716 
                 23.647 
                 1.00 
                 79.63 
               
               
                 412 
                 O 
                 ALA 
                 A 
                 158 
                 55.737 
                 96.111 
                 23.416 
                 1.00 
                 81.18 
               
               
                 413 
                 N 
                 PHE 
                 A 
                 159 
                 54.320 
                 94.440 
                 23.897 
                 1.00 
                 78.10 
               
               
                 414 
                 CA 
                 PHE 
                 A 
                 159 
                 55.361 
                 93.417 
                 23.914 
                 1.00 
                 77.04 
               
               
                 415 
                 CG 
                 PHE 
                 A 
                 159 
                 54.830 
                 92.149 
                 24.589 
                 1.00 
                 74.93 
               
               
                 416 
                 CG 
                 PHE 
                 A 
                 159 
                 55.767 
                 90.974 
                 24.519 
                 1.00 
                 70.81 
               
               
                 417 
                 CD1 
                 PHE 
                 A 
                 159 
                 56.866 
                 90.892 
                 25.365 
                 1.00 
                 70.05 
               
               
                 418 
                 CD2 
                 PHE 
                 A 
                 159 
                 55.536 
                 89.938 
                 23.620 
                 1.00 
                 68.83 
               
               
                 419 
                 CE1 
                 PHE 
                 A 
                 159 
                 57.718 
                 89.789 
                 25.320 
                 1.00 
                 69.21 
               
               
                 420 
                 CE2 
                 PHE 
                 A 
                 159 
                 56.382 
                 88.834 
                 23.567 
                 1.00 
                 68.27 
               
               
                 421 
                 CZ 
                 PHE 
                 A 
                 159 
                 57.474 
                 88.757 
                 24.418 
                 1.00 
                 67.85 
               
               
                 422 
                 C 
                 PHE 
                 A 
                 159 
                 55.810 
                 93.079 
                 22.493 
                 1.00 
                 77.93 
               
               
                 423 
                 O 
                 PHE 
                 A 
                 159 
                 57.003 
                 92.913 
                 22.232 
                 1.00 
                 77.40 
               
               
                 424 
                 N 
                 CYS 
                 A 
                 160 
                 54.841 
                 92.973 
                 21.586 
                 1.00 
                 78.83 
               
               
                 425 
                 CA 
                 CYS 
                 A 
                 160 
                 55.103 
                 92.640 
                 20.189 
                 1.00 
                 80.28 
               
               
                 426 
                 CB 
                 CYS 
                 A 
                 160 
                 53.786 
                 92.394 
                 19.462 
                 1.00 
                 79.59 
               
               
                 427 
                 SG 
                 CYS 
                 A 
                 160 
                 52.902 
                 90.944 
                 20.065 
                 1.00 
                 82.03 
               
               
                 428 
                 C 
                 CYS 
                 A 
                 160 
                 55.902 
                 93.694 
                 19.443 
                 1.00 
                 81.71 
               
               
                 429 
                 O 
                 GYS 
                 A 
                 160 
                 56.650 
                 93.372 
                 18.522 
                 1.00 
                 81.61 
               
               
                 430 
                 N 
                 GLU 
                 A 
                 161 
                 55.744 
                 94.949 
                 19.848 
                 1.00 
                 83.80 
               
               
                 431 
                 CA 
                 GLU 
                 A 
                 161 
                 56.443 
                 96.066 
                 19.222 
                 1.00 
                 85.81 
               
               
                 432 
                 CG 
                 GLU 
                 A 
                 161 
                 55.666 
                 97.355 
                 19.484 
                 1.00 
                 87.23 
               
               
                 433 
                 CG 
                 GLU 
                 A 
                 161 
                 54.265 
                 97.337 
                 18.880 
                 1.00 
                 89.73 
               
               
                 434 
                 CD 
                 GLU 
                 A 
                 161 
                 53.343 
                 98.367 
                 19.511 
                 1.00 
                 91.91 
               
               
                 435 
                 OE1 
                 GLU 
                 A 
                 161 
                 53.841 
                 99.241 
                 20.263 
                 1.00 
                 91.31 
               
               
                 436 
                 OE2 
                 GLU 
                 A 
                 161 
                 52.121 
                 98.301 
                 19.252 
                 1.00 
                 92.34 
               
               
                 437 
                 C 
                 GLU 
                 A 
                 161 
                 57.881 
                 96.206 
                 19.713 
                 1.00 
                 86.38 
               
               
                 438 
                 O 
                 GLU 
                 A 
                 161 
                 58.630 
                 97.075 
                 19.251 
                 1.00 
                 86.35 
               
               
                 439 
                 N 
                 LEU 
                 A 
                 162 
                 58.259 
                 95.347 
                 20.656 
                 1.00 
                 86.57 
               
               
                 440 
                 CA 
                 LEU 
                 A 
                 162 
                 59.610 
                 95.351 
                 21.206 
                 1.00 
                 86.05 
               
               
                 441 
                 CB 
                 LEU 
                 A 
                 162 
                 59.651 
                 94.677 
                 22.579 
                 1.00 
                 84.95 
               
               
                 442 
                 CG 
                 LEU 
                 A 
                 162 
                 59.076 
                 95.368 
                 23.810 
                 1.00 
                 85.09 
               
               
                 443 
                 CD1 
                 LEU 
                 A 
                 162 
                 59.210 
                 94.427 
                 24.993 
                 1.00 
                 84.65 
               
               
                 444 
                 CD2 
                 LEU 
                 A 
                 162 
                 59.809 
                 96.672 
                 24.077 
                 1.00 
                 84.78 
               
               
                 445 
                 C 
                 LEU 
                 A 
                 162 
                 60.510 
                 94.560 
                 20.279 
                 1.00 
                 86.36 
               
               
                 446 
                 O 
                 LEU 
                 A 
                 162 
                 60.063 
                 93.605 
                 19.640 
                 1.00 
                 85.97 
               
               
                 447 
                 N 
                 PRO 
                 A 
                 163 
                 61.791 
                 94.948 
                 20.183 
                 1.00 
                 86.60 
               
               
                 448 
                 CD 
                 PRO 
                 A 
                 163 
                 62.516 
                 96.098 
                 20.745 
                 1.00 
                 86.06 
               
               
                 449 
                 CA 
                 PRO 
                 A 
                 163 
                 62.655 
                 94.171 
                 19.298 
                 1.00 
                 87.01 
               
               
                 450 
                 CB 
                 PRO 
                 A 
                 163 
                 64.000 
                 94.896 
                 19.389 
                 1.00 
                 85.41 
               
               
                 451 
                 CG 
                 PRO 
                 A 
                 163 
                 63.937 
                 95.613 
                 20.690 
                 1.00 
                 85.73 
               
               
                 452 
                 C 
                 PRO 
                 A 
                 163 
                 62.719 
                 92.706 
                 19.736 
                 1.00 
                 88.45 
               
               
                 453 
                 O 
                 PRO 
                 A 
                 163 
                 62.696 
                 92.379 
                 20.921 
                 1.00 
                 89.25 
               
               
                 454 
                 N 
                 LEU 
                 A 
                 164 
                 62.778 
                 91.839 
                 18.740 
                 1.00 
                 90.01 
               
               
                 455 
                 CA 
                 LEU 
                 A 
                 164 
                 62.826 
                 90.391 
                 18.887 
                 1.00 
                 91.31 
               
               
                 456 
                 CB 
                 LEU 
                 A 
                 164 
                 63.233 
                 89.820 
                 17.525 
                 1.00 
                 93.70 
               
               
                 457 
                 CG 
                 LEU 
                 A 
                 164 
                 62.566 
                 90.662 
                 16.414 
                 1.00 
                 95.67 
               
               
                 458 
                 CD1 
                 LEU 
                 A 
                 164 
                 63.570 
                 90.984 
                 15.315 
                 1.00 
                 94.00 
               
               
                 459 
                 CD2 
                 LEU 
                 A 
                 164 
                 61.322 
                 89.942 
                 15.873 
                 1.00 
                 95.69 
               
               
                 460 
                 C 
                 LEU 
                 A 
                 164 
                 63.711 
                 89.815 
                 20.007 
                 1.00 
                 91.13 
               
               
                 461 
                 O 
                 LEU 
                 A 
                 164 
                 63.551 
                 88.657 
                 20.386 
                 1.00 
                 91.42 
               
               
                 462 
                 N 
                 ASP 
                 A 
                 165 
                 64.632 
                 90.613 
                 20.539 
                 1.00 
                 90.81 
               
               
                 463 
                 CA 
                 ASP 
                 A 
                 165 
                 65.533 
                 90.152 
                 21.597 
                 1.00 
                 89.80 
               
               
                 464 
                 CB 
                 ASP 
                 A 
                 165 
                 66.941 
                 90.690 
                 21.359 
                 1.00 
                 92.39 
               
               
                 465 
                 CG 
                 ASP 
                 A 
                 165 
                 67.734 
                 89.826 
                 20.399 
                 1.00 
                 95.54 
               
               
                 466 
                 OD1 
                 ASP 
                 A 
                 165 
                 67.104 
                 89.026 
                 19.667 
                 1.00 
                 95.95 
               
               
                 467 
                 OD2 
                 ASP 
                 A 
                 165 
                 68.981 
                 89.948 
                 20.373 
                 1.00 
                 95.95 
               
               
                 468 
                 C 
                 ASP 
                 A 
                 165 
                 65.094 
                 90.517 
                 23.002 
                 1.00 
                 88.43 
               
               
                 469 
                 O 
                 ASP 
                 A 
                 165 
                 65.323 
                 89.753 
                 23.942 
                 1.00 
                 88.39 
               
               
                 470 
                 N 
                 ASP 
                 A 
                 166 
                 64.486 
                 91.690 
                 23.146 
                 1.00 
                 86.37 
               
               
                 471 
                 CA 
                 ASP 
                 A 
                 166 
                 64.001 
                 92.144 
                 24.443 
                 1.00 
                 83.98 
               
               
                 472 
                 CB 
                 ASP 
                 A 
                 166 
                 63.536 
                 93.590 
                 24.353 
                 1.00 
                 85.58 
               
               
                 473 
                 CG 
                 ASP 
                 A 
                 166 
                 64.673 
                 94.543 
                 24.086 
                 1.00 
                 86.69 
               
               
                 474 
                 OD1 
                 ASP 
                 A 
                 166 
                 65.782 
                 94.302 
                 24.608 
                 1.00 
                 87.53 
               
               
                 475 
                 OD2 
                 ASP 
                 A 
                 166 
                 64.456 
                 95.541 
                 23.372 
                 1.00 
                 87.88 
               
               
                 476 
                 C 
                 ASP 
                 A 
                 166 
                 62.845 
                 91.255 
                 24.873 
                 1.00 
                 81.98 
               
               
                 477 
                 O 
                 ASP 
                 A 
                 166 
                 62.640 
                 90.997 
                 26.063 
                 1.00 
                 81.09 
               
               
                 478 
                 N 
                 GLN 
                 A 
                 167 
                 62.091 
                 90.796 
                 23.883 
                 1.00 
                 79.33 
               
               
                 479 
                 CA 
                 GLN 
                 A 
                 167 
                 60.970 
                 89.907 
                 24.114 
                 1.00 
                 78.44 
               
               
                 480 
                 CB 
                 GLN 
                 A 
                 167 
                 60.374 
                 89.465 
                 22.784 
                 1.00 
                 78.73 
               
               
                 481 
                 CG 
                 GLN 
                 A 
                 167 
                 59.383 
                 90.423 
                 22.175 
                 1.00 
                 80.96 
               
               
                 482 
                 CD 
                 GLN 
                 A 
                 167 
                 58.908 
                 89.948 
                 20.816 
                 1.00 
                 81.58 
               
               
                 483 
                 OE1 
                 GLN 
                 A 
                 167 
                 58.712 
                 88.748 
                 20.592 
                 1.00 
                 79.69 
               
               
                 484 
                 NE2 
                 GLN 
                 A 
                 167 
                 58.711 
                 90.890 
                 19.900 
                 1.00 
                 82.38 
               
               
                 485 
                 C 
                 GLN 
                 A 
                 167 
                 61.468 
                 88.670 
                 24.844 
                 1.00 
                 77.98 
               
               
                 486 
                 O 
                 GLN 
                 A 
                 167 
                 60.789 
                 88.122 
                 25.715 
                 1.00 
                 78.61 
               
               
                 487 
                 N 
                 VAL 
                 A 
                 168 
                 62.662 
                 88.237 
                 24.470 
                 1.00 
                 76.37 
               
               
                 488 
                 CA 
                 VAL 
                 A 
                 168 
                 63.269 
                 87.046 
                 25.045 
                 1.00 
                 74.15 
               
               
                 489 
                 CB 
                 VAL 
                 A 
                 168 
                 64.367 
                 86.498 
                 24.106 
                 1.00 
                 75.65 
               
               
                 490 
                 CG1 
                 VAL 
                 A 
                 168 
                 64.806 
                 85.109 
                 24.557 
                 1.00 
                 74.83 
               
               
                 491 
                 CG2 
                 VAL 
                 A 
                 168 
                 63.837 
                 86.456 
                 22.673 
                 1.00 
                 76.04 
               
               
                 492 
                 C 
                 VAL 
                 A 
                 168 
                 63.855 
                 87.274 
                 26.432 
                 1.00 
                 71.12 
               
               
                 493 
                 O 
                 VAL 
                 A 
                 168 
                 63.831 
                 86.375 
                 27.269 
                 1.00 
                 70.68 
               
               
                 494 
                 N 
                 ALA 
                 A 
                 169 
                 64.377 
                 88.468 
                 26.676 
                 1.00 
                 68.41 
               
               
                 495 
                 CA 
                 ALA 
                 A 
                 169 
                 64.954 
                 88.775 
                 27.977 
                 1.00 
                 66.77 
               
               
                 496 
                 CB 
                 ALA 
                 A 
                 169 
                 65.694 
                 90.092 
                 27.925 
                 1.00 
                 64.43 
               
               
                 497 
                 C 
                 ALA 
                 A 
                 169 
                 63.855 
                 88.829 
                 29.026 
                 1.00 
                 66.98 
               
               
                 498 
                 O 
                 ALA 
                 A 
                 169 
                 64.006 
                 88.277 
                 30.116 
                 1.00 
                 67.68 
               
               
                 499 
                 N 
                 LEU 
                 A 
                 170 
                 62.744 
                 89.485 
                 28.694 
                 1.00 
                 66.54 
               
               
                 500 
                 CA 
                 LEU 
                 A 
                 170 
                 61.620 
                 89.602 
                 29.624 
                 1.00 
                 65.31 
               
               
                 501 
                 CB 
                 LEU 
                 A 
                 170 
                 60.506 
                 90.466 
                 29.026 
                 1.00 
                 62.20 
               
               
                 502 
                 CG 
                 LEU 
                 A 
                 170 
                 60.820 
                 91.951 
                 28.827 
                 1.00 
                 62.51 
               
               
                 503 
                 CD1 
                 LEU 
                 A 
                 170 
                 59.628 
                 92.632 
                 28.170 
                 1.00 
                 61.74 
               
               
                 504 
                 CD2 
                 LEU 
                 A 
                 170 
                 61.145 
                 92.610 
                 30.164 
                 1.00 
                 59.41 
               
               
                 505 
                 C 
                 LEU 
                 A 
                 170 
                 61.064 
                 88.230 
                 29.979 
                 1.00 
                 65.02 
               
               
                 506 
                 O 
                 LEU 
                 A 
                 170 
                 60.822 
                 87.930 
                 31.146 
                 1.00 
                 65.89 
               
               
                 507 
                 N 
                 LEU 
                 A 
                 171 
                 60.868 
                 87.405 
                 28.957 
                 1.00 
                 64.59 
               
               
                 508 
                 CA 
                 LEU 
                 A 
                 171 
                 60.344 
                 86.060 
                 29.124 
                 1.00 
                 64.70 
               
               
                 509 
                 CB 
                 LEU 
                 A 
                 171 
                 60.218 
                 85.390 
                 27.757 
                 1.00 
                 64.46 
               
               
                 510 
                 CG 
                 LEU 
                 A 
                 171 
                 59.102 
                 85.867 
                 26.824 
                 1.00 
                 64.80 
               
               
                 511 
                 CD1 
                 LEU 
                 A 
                 171 
                 59.390 
                 85.417 
                 25.396 
                 1.00 
                 62.26 
               
               
                 512 
                 CD2 
                 LEU 
                 A 
                 171 
                 57.765 
                 85.319 
                 27.314 
                 1.00 
                 62.74 
               
               
                 513 
                 C 
                 LEU 
                 A 
                 171 
                 61.217 
                 85.191 
                 30.029 
                 1.00 
                 66.21 
               
               
                 514 
                 O 
                 LEU 
                 A 
                 171 
                 60.713 
                 84.389 
                 30.811 
                 1.00 
                 65.95 
               
               
                 515 
                 N 
                 ARG 
                 A 
                 172 
                 62.530 
                 85.355 
                 29.923 
                 1.00 
                 67.44 
               
               
                 516 
                 CA 
                 ARG 
                 A 
                 172 
                 63.466 
                 84.563 
                 30.713 
                 1.00 
                 67.95 
               
               
                 517 
                 CB 
                 ARG 
                 A 
                 172 
                 64.790 
                 84.415 
                 29.950 
                 1.00 
                 73.51 
               
               
                 518 
                 CG 
                 ARG 
                 A 
                 172 
                 64.735 
                 83.518 
                 28.712 
                 1.00 
                 80.88 
               
               
                 519 
                 CD 
                 ARG 
                 A 
                 172 
                 66.080 
                 83.504 
                 27.971 
                 1.00 
                 86.71 
               
               
                 520 
                 NE 
                 ARG 
                 A 
                 172 
                 66.123 
                 82.488 
                 26.914 
                 1.00 
                 92.46 
               
               
                 521 
                 CZ 
                 ARG 
                 A 
                 172 
                 67.118 
                 82.338 
                 26.039 
                 1.00 
                 94.34 
               
               
                 522 
                 NH1 
                 ARG 
                 A 
                 172 
                 68.179 
                 83.142 
                 26.075 
                 1.00 
                 93.95 
               
               
                 523 
                 NH2 
                 ARG 
                 A 
                 172 
                 67.060 
                 81.372 
                 25.128 
                 1.00 
                 94.24 
               
               
                 524 
                 C 
                 ARG 
                 A 
                 172 
                 63.773 
                 85.107 
                 32.110 
                 1.00 
                 65.79 
               
               
                 525 
                 O 
                 ARG 
                 A 
                 172 
                 64.293 
                 84.381 
                 32.952 
                 1.00 
                 64.93 
               
               
                 526 
                 N 
                 ALA 
                 A 
                 173 
                 63.442 
                 86.369 
                 32.361 
                 1.00 
                 63.58 
               
               
                 527 
                 CA 
                 ALA 
                 A 
                 173 
                 63.750 
                 86.997 
                 33.643 
                 1.00 
                 61.78 
               
               
                 528 
                 CB 
                 ALA 
                 A 
                 173 
                 63.717 
                 88.507 
                 33.483 
                 1.00 
                 61.72 
               
               
                 529 
                 C 
                 ALA 
                 A 
                 173 
                 62.932 
                 86.598 
                 34.866 
                 1.00 
                 62.00 
               
               
                 530 
                 O 
                 ALA 
                 A 
                 173 
                 63.492 
                 86.387 
                 35.939 
                 1.00 
                 61.86 
               
               
                 531 
                 N 
                 HIS 
                 A 
                 174 
                 61.614 
                 86.507 
                 34.738 
                 1.00 
                 61.78 
               
               
                 532 
                 CA 
                 HIS 
                 A 
                 174 
                 60.821 
                 86.150 
                 35.902 
                 1.00 
                 60.73 
               
               
                 533 
                 CB 
                 HIS 
                 A 
                 174 
                 60.188 
                 87.411 
                 36.509 
                 1.00 
                 62.68 
               
               
                 534 
                 CG 
                 HIS 
                 A 
                 174 
                 61.172 
                 88.510 
                 36.771 
                 1.00 
                 62.85 
               
               
                 535 
                 CD2 
                 HIS 
                 A 
                 174 
                 61.911 
                 88.804 
                 37.869 
                 1.00 
                 63.15 
               
               
                 536 
                 ND1 
                 HIS 
                 A 
                 174 
                 61.523 
                 89.443 
                 35.815 
                 1.00 
                 63.25 
               
               
                 537 
                 CE1 
                 HIS 
                 A 
                 174 
                 62.434 
                 90.263 
                 36.316 
                 1.00 
                 62.46 
               
               
                 538 
                 NE2 
                 HIS 
                 A 
                 174 
                 62.686 
                 89.896 
                 37.556 
                 1.00 
                 63.69 
               
               
                 539 
                 C 
                 HIS 
                 A 
                 174 
                 59.760 
                 85.101 
                 35.619 
                 1.00 
                 60.12 
               
               
                 540 
                 O 
                 HIS 
                 A 
                 174 
                 58.695 
                 85.086 
                 36.241 
                 1.00 
                 60.90 
               
               
                 541 
                 N 
                 ALA 
                 A 
                 175 
                 60.062 
                 84.213 
                 34.678 
                 1.00 
                 59.27 
               
               
                 542 
                 CA 
                 ALA 
                 A 
                 175 
                 59.148 
                 83.134 
                 34.328 
                 1.00 
                 58.49 
               
               
                 543 
                 CB 
                 ALA 
                 A 
                 175 
                 59.810 
                 82.201 
                 33.327 
                 1.00 
                 57.98 
               
               
                 544 
                 C 
                 ALA 
                 A 
                 175 
                 58.757 
                 82.361 
                 35.590 
                 1.00 
                 58.48 
               
               
                 545 
                 O 
                 ALA 
                 A 
                 175 
                 57.643 
                 81.846 
                 35.690 
                 1.00 
                 57.69 
               
               
                 546 
                 N 
                 GLY 
                 A 
                 176 
                 59.682 
                 82.290 
                 36.550 
                 1.00 
                 59.08 
               
               
                 547 
                 CA 
                 GLY 
                 A 
                 176 
                 59.429 
                 81.588 
                 37.798 
                 1.00 
                 58.18 
               
               
                 548 
                 C 
                 GLY 
                 A 
                 176 
                 58.279 
                 82.172 
                 38.597 
                 1.00 
                 58.64 
               
               
                 549 
                 O 
                 GLY 
                 A 
                 176 
                 57.382 
                 81.446 
                 39.040 
                 1.00 
                 58.62 
               
               
                 550 
                 N 
                 GLU 
                 A 
                 177 
                 58.296 
                 83.490 
                 38.792 
                 1.00 
                 59.58 
               
               
                 551 
                 CA 
                 GLU 
                 A 
                 177 
                 57.234 
                 84.153 
                 39.538 
                 1.00 
                 60.16 
               
               
                 552 
                 CB 
                 GLU 
                 A 
                 177 
                 57.551 
                 85.637 
                 39.750 
                 1.00 
                 61.50 
               
               
                 553 
                 CG 
                 GLU 
                 A 
                 177 
                 58.622 
                 85.903 
                 40.794 
                 1.00 
                 63.08 
               
               
                 554 
                 CD 
                 GLU 
                 A 
                 177 
                 60.005 
                 86.044 
                 40.193 
                 1.00 
                 65.42 
               
               
                 555 
                 OE1 
                 GLU 
                 A 
                 177 
                 60.336 
                 85.293 
                 39.249 
                 1.00 
                 65.86 
               
               
                 556 
                 OE2 
                 GLU 
                 A 
                 177 
                 60.771 
                 86.905 
                 40.675 
                 1.00 
                 67.01 
               
               
                 557 
                 C 
                 GLU 
                 A 
                 177 
                 55.902 
                 84.026 
                 38.821 
                 1.00 
                 59.91 
               
               
                 558 
                 O 
                 GLU 
                 A 
                 177 
                 54.847 
                 84.024 
                 39.459 
                 1.00 
                 61.25 
               
               
                 559 
                 N 
                 HIS 
                 A 
                 178 
                 55.950 
                 83.916 
                 37.496 
                 1.00 
                 58.62 
               
               
                 560 
                 CA 
                 HIS 
                 A 
                 178 
                 54.734 
                 83.785 
                 36.693 
                 1.00 
                 57.01 
               
               
                 561 
                 CB 
                 HIS 
                 A 
                 178 
                 55.095 
                 83.868 
                 35.212 
                 1.00 
                 58.34 
               
               
                 562 
                 CG 
                 HIS 
                 A 
                 178 
                 53.994 
                 84.387 
                 34.350 
                 1.00 
                 63.30 
               
               
                 563 
                 CD2 
                 HIS 
                 A 
                 178 
                 53.766 
                 85.625 
                 33.840 
                 1.00 
                 64.60 
               
               
                 564 
                 ND1 
                 HIS 
                 A 
                 178 
                 52.947 
                 83.601 
                 33.909 
                 1.00 
                 64.96 
               
               
                 565 
                 CE1 
                 HIS 
                 A 
                 178 
                 52.132 
                 84.322 
                 33.169 
                 1.00 
                 64.34 
               
               
                 566 
                 NE2 
                 HIS 
                 A 
                 178 
                 52.605 
                 85.556 
                 33.110 
                 1.00 
                 66.45 
               
               
                 567 
                 C 
                 HIS 
                 A 
                 178 
                 54.030 
                 82.458 
                 37.007 
                 1.00 
                 55.43 
               
               
                 568 
                 O 
                 HIS 
                 A 
                 178 
                 52.809 
                 82.399 
                 37.192 
                 1.00 
                 54.25 
               
               
                 569 
                 N 
                 LEU 
                 A 
                 179 
                 54.810 
                 81.391 
                 37.080 
                 1.00 
                 52.78 
               
               
                 570 
                 CA 
                 LEU 
                 A 
                 179 
                 54.258 
                 80.093 
                 37.390 
                 1.00 
                 52.79 
               
               
                 571 
                 CB 
                 LEU 
                 A 
                 179 
                 55.351 
                 79.022 
                 37.278 
                 1.00 
                 52.58 
               
               
                 572 
                 CG 
                 LEU 
                 A 
                 179 
                 56.047 
                 78.908 
                 35.916 
                 1.00 
                 52.20 
               
               
                 573 
                 CD1 
                 LEU 
                 A 
                 179 
                 57.180 
                 77.879 
                 35.988 
                 1.00 
                 49.88 
               
               
                 574 
                 CD2 
                 LEU 
                 A 
                 179 
                 55.033 
                 78.513 
                 34.856 
                 1.00 
                 48.69 
               
               
                 575 
                 C 
                 LEU 
                 A 
                 179 
                 53.656 
                 80.097 
                 38.802 
                 1.00 
                 52.79 
               
               
                 576 
                 O 
                 LEU 
                 A 
                 179 
                 52.578 
                 79.546 
                 39.011 
                 1.00 
                 52.68 
               
               
                 577 
                 N 
                 LEU 
                 A 
                 180 
                 54.342 
                 80.708 
                 39.772 
                 1.00 
                 52.49 
               
               
                 578 
                 CA 
                 LEU 
                 A 
                 180 
                 53.815 
                 80.744 
                 41.141 
                 1.00 
                 50.34 
               
               
                 579 
                 CB 
                 LEU 
                 A 
                 180 
                 54.882 
                 81.244 
                 42.118 
                 1.00 
                 52.64 
               
               
                 580 
                 CG 
                 LEU 
                 A 
                 180 
                 56.040 
                 80.271 
                 42.413 
                 1.00 
                 54.04 
               
               
                 581 
                 CD1 
                 LEU 
                 A 
                 180 
                 57.006 
                 80.904 
                 43.394 
                 1.00 
                 56.51 
               
               
                 582 
                 CD2 
                 LEU 
                 A 
                 180 
                 55.515 
                 78.973 
                 42.992 
                 1.00 
                 53.85 
               
               
                 583 
                 C 
                 LEU 
                 A 
                 180 
                 52.531 
                 81.581 
                 41.248 
                 1.00 
                 47.53 
               
               
                 584 
                 O 
                 LEU 
                 A 
                 180 
                 51.591 
                 81.195 
                 41.938 
                 1.00 
                 45.44 
               
               
                 585 
                 N 
                 LEU 
                 A 
                 181 
                 52.476 
                 82.716 
                 40.565 
                 1.00 
                 45.83 
               
               
                 586 
                 CA 
                 LEU 
                 A 
                 181 
                 51.254 
                 83.513 
                 40.585 
                 1.00 
                 46.59 
               
               
                 587 
                 CB 
                 LEU 
                 A 
                 181 
                 51.415 
                 84.767 
                 39.732 
                 1.00 
                 45.48 
               
               
                 588 
                 CG 
                 LEU 
                 A 
                 181 
                 52.179 
                 85.937 
                 40.364 
                 1.00 
                 48.20 
               
               
                 589 
                 CD1 
                 LEU 
                 A 
                 181 
                 52.559 
                 86.933 
                 39.290 
                 1.00 
                 46.83 
               
               
                 590 
                 CD2 
                 LEU 
                 A 
                 181 
                 51.329 
                 86.593 
                 41.455 
                 1.00 
                 45.79 
               
               
                 591 
                 C 
                 LEU 
                 A 
                 181 
                 50.138 
                 82.642 
                 40.008 
                 1.00 
                 48.38 
               
               
                 592 
                 O 
                 LEU 
                 A 
                 181 
                 49.043 
                 82.541 
                 40.574 
                 1.00 
                 48.52 
               
               
                 593 
                 N 
                 GLY 
                 A 
                 182 
                 50.435 
                 81.995 
                 38.883 
                 1.00 
                 49.14 
               
               
                 594 
                 CA 
                 GLY 
                 A 
                 182 
                 49.460 
                 81.132 
                 38.236 
                 1.00 
                 47.78 
               
               
                 595 
                 C 
                 GLY 
                 A 
                 182 
                 48.912 
                 80.020 
                 39.110 
                 1.00 
                 48.81 
               
               
                 596 
                 O 
                 GLY 
                 A 
                 182 
                 47.704 
                 79.822 
                 39.184 
                 1.00 
                 51.08 
               
               
                 597 
                 N 
                 ALA 
                 A 
                 183 
                 49.790 
                 79.283 
                 39.778 
                 1.00 
                 49.60 
               
               
                 598 
                 CA 
                 ALA 
                 A 
                 183 
                 49.351 
                 78.193 
                 40.636 
                 1.00 
                 48.71 
               
               
                 599 
                 CB 
                 ALA 
                 A 
                 183 
                 50.542 
                 77.366 
                 41.066 
                 1.00 
                 47.94 
               
               
                 600 
                 C 
                 ALA 
                 A 
                 183 
                 48.599 
                 78.719 
                 41.854 
                 1.00 
                 49.37 
               
               
                 601 
                 O 
                 ALA 
                 A 
                 183 
                 47.647 
                 78.086 
                 42.323 
                 1.00 
                 49.24 
               
               
                 602 
                 N 
                 THR 
                 A 
                 184 
                 49.021 
                 79.874 
                 42.362 
                 1.00 
                 49.27 
               
               
                 603 
                 CA 
                 THR 
                 A 
                 184 
                 48.364 
                 80.471 
                 43.524 
                 1.00 
                 50.02 
               
               
                 604 
                 CB 
                 THR 
                 A 
                 184 
                 49.127 
                 81.738 
                 44.046 
                 1.00 
                 48.92 
               
               
                 605 
                 OG1 
                 THR 
                 A 
                 184 
                 50.450 
                 81.378 
                 44.453 
                 1.00 
                 49.72 
               
               
                 606 
                 CG2 
                 THR 
                 A 
                 184 
                 48.416 
                 82.344 
                 45.237 
                 1.00 
                 44.67 
               
               
                 607 
                 C 
                 THR 
                 A 
                 184 
                 46.949 
                 80.889 
                 43.136 
                 1.00 
                 51.11 
               
               
                 608 
                 O 
                 THR 
                 A 
                 184 
                 46.000 
                 80.650 
                 43.873 
                 1.00 
                 51.52 
               
               
                 609 
                 N 
                 LYS 
                 A 
                 185 
                 46.821 
                 81.507 
                 41.966 
                 1.00 
                 52.71 
               
               
                 610 
                 CA 
                 LYS 
                 A 
                 185 
                 45.535 
                 81.994 
                 41.476 
                 1.00 
                 55.79 
               
               
                 611 
                 CB 
                 LYS 
                 A 
                 185 
                 45.737 
                 82.744 
                 40.162 
                 1.00 
                 54.28 
               
               
                 612 
                 CG 
                 LYS 
                 A 
                 185 
                 44.877 
                 83.970 
                 40.004 
                 1.00 
                 57.75 
               
               
                 613 
                 CD 
                 LYS 
                 A 
                 185 
                 43.448 
                 83.637 
                 39.692 
                 1.00 
                 61.27 
               
               
                 614 
                 CE 
                 LYS 
                 A 
                 185 
                 42.624 
                 84.908 
                 39.558 
                 1.00 
                 60.47 
               
               
                 615 
                 NZ 
                 LYS 
                 A 
                 185 
                 41.268 
                 84.579 
                 39.044 
                 1.00 
                 61.67 
               
               
                 616 
                 C 
                 LYS 
                 A 
                 185 
                 44.539 
                 80.862 
                 41.262 
                 1.00 
                 57.83 
               
               
                 617 
                 O 
                 LYS 
                 A 
                 185 
                 43.353 
                 80.984 
                 41.595 
                 1.00 
                 59.99 
               
               
                 618 
                 N 
                 ARG 
                 A 
                 186 
                 45.038 
                 79.763 
                 40.714 
                 1.00 
                 57.58 
               
               
                 619 
                 CA 
                 ARG 
                 A 
                 186 
                 44.225 
                 78.592 
                 40.416 
                 1.00 
                 57.92 
               
               
                 620 
                 CB 
                 ARG 
                 A 
                 186 
                 45.022 
                 77.691 
                 39.465 
                 1.00 
                 57.27 
               
               
                 621 
                 CG 
                 ARG 
                 A 
                 186 
                 44.254 
                 76.573 
                 38.766 
                 1.00 
                 55.10 
               
               
                 622 
                 CD 
                 ARG 
                 A 
                 186 
                 45.059 
                 76.144 
                 37.553 
                 1.00 
                 54.62 
               
               
                 623 
                 NE 
                 ARG 
                 A 
                 186 
                 46.433 
                 75.922 
                 37.964 
                 1.00 
                 59.54 
               
               
                 624 
                 CZ 
                 ARG 
                 A 
                 186 
                 47.508 
                 76.342 
                 37.305 
                 1.00 
                 61.35 
               
               
                 625 
                 NH1 
                 ARG 
                 A 
                 186 
                 47.381 
                 77.022 
                 36.173 
                 1.00 
                 59.99 
               
               
                 626 
                 NH2 
                 ARG 
                 A 
                 186 
                 48.714 
                 76.077 
                 37.795 
                 1.00 
                 63.48 
               
               
                 627 
                 C 
                 ARG 
                 A 
                 186 
                 43.777 
                 77.809 
                 41.661 
                 1.00 
                 59.29 
               
               
                 628 
                 O 
                 ARG 
                 A 
                 186 
                 42.721 
                 77.176 
                 41.647 
                 1.00 
                 58.66 
               
               
                 629 
                 N 
                 SER 
                 A 
                 187 
                 44.565 
                 77.870 
                 42.736 
                 1.00 
                 59.78 
               
               
                 630 
                 CA 
                 SER 
                 A 
                 187 
                 44.264 
                 77.144 
                 43.970 
                 1.00 
                 60.64 
               
               
                 631 
                 CB 
                 SER 
                 A 
                 187 
                 45.562 
                 76.650 
                 44.593 
                 1.00 
                 60.64 
               
               
                 632 
                 OG 
                 SER 
                 A 
                 187 
                 46.368 
                 76.015 
                 43.621 
                 1.00 
                 60.45 
               
               
                 633 
                 C 
                 SER 
                 A 
                 187 
                 43.524 
                 77.999 
                 44.986 
                 1.00 
                 62.49 
               
               
                 634 
                 O 
                 SER 
                 A 
                 187 
                 42.971 
                 77.506 
                 45.965 
                 1.00 
                 63.57 
               
               
                 635 
                 N 
                 MET 
                 A 
                 188 
                 43.542 
                 79.294 
                 44.741 
                 1.00 
                 65.32 
               
               
                 636 
                 CA 
                 MET 
                 A 
                 186 
                 42.910 
                 80.301 
                 45.586 
                 1.00 
                 68.54 
               
               
                 637 
                 CB 
                 MET 
                 A 
                 188 
                 42.833 
                 81.574 
                 44.760 
                 1.00 
                 66.44 
               
               
                 638 
                 CG 
                 MET 
                 A 
                 188 
                 42.403 
                 82.771 
                 45.502 
                 1.00 
                 65.27 
               
               
                 639 
                 SD 
                 MET 
                 A 
                 188 
                 42.229 
                 84.057 
                 44.321 
                 1.00 
                 62.32 
               
               
                 640 
                 CE 
                 MET 
                 A 
                 188 
                 41.180 
                 85.106 
                 45.251 
                 1.00 
                 59.32 
               
               
                 641 
                 C 
                 MET 
                 A 
                 188 
                 41.508 
                 79.955 
                 46.139 
                 1.00 
                 71.36 
               
               
                 642 
                 O 
                 MET 
                 A 
                 188 
                 41.099 
                 80.431 
                 47.211 
                 1.00 
                 69.47 
               
               
                 643 
                 N 
                 MET 
                 A 
                 189 
                 40.785 
                 79.134 
                 45.383 
                 1.00 
                 74.71 
               
               
                 644 
                 CA 
                 MET 
                 A 
                 189 
                 39.420 
                 78.720 
                 45.703 
                 1.00 
                 76.70 
               
               
                 645 
                 CB 
                 MET 
                 A 
                 189 
                 38.694 
                 78.441 
                 44.398 
                 1.00 
                 77.78 
               
               
                 646 
                 CG 
                 MET 
                 A 
                 189 
                 39.637 
                 77.947 
                 43.327 
                 1.00 
                 81.52 
               
               
                 647 
                 SD 
                 MET 
                 A 
                 189 
                 39.408 
                 78.872 
                 41.822 
                 1.00 
                 91.12 
               
               
                 648 
                 CE 
                 MET 
                 A 
                 189 
                 40.266 
                 77.807 
                 40.590 
                 1.00 
                 87.46 
               
               
                 649 
                 C 
                 MET 
                 A 
                 189 
                 39.265 
                 77.521 
                 46.635 
                 1.00 
                 77.26 
               
               
                 650 
                 O 
                 MET 
                 A 
                 189 
                 38.156 
                 77.238 
                 47.090 
                 1.00 
                 77.40 
               
               
                 651 
                 N 
                 TYR 
                 A 
                 190 
                 40.361 
                 76.823 
                 46.926 
                 1.00 
                 77.11 
               
               
                 652 
                 CA 
                 TYR 
                 A 
                 190 
                 40.303 
                 75.656 
                 47.799 
                 1.00 
                 76.17 
               
               
                 653 
                 CB 
                 TYR 
                 A 
                 190 
                 41.098 
                 74.521 
                 47.173 
                 1.00 
                 74.05 
               
               
                 654 
                 CG 
                 TYR 
                 A 
                 190 
                 40.581 
                 74.251 
                 45.786 
                 1.00 
                 73.12 
               
               
                 655 
                 CD1 
                 TYR 
                 A 
                 190 
                 39.311 
                 73.715 
                 45.593 
                 1.00 
                 73.09 
               
               
                 656 
                 CE1 
                 TYR 
                 A 
                 190 
                 38.778 
                 73.572 
                 44.320 
                 1.00 
                 73.17 
               
               
                 657 
                 CD2 
                 TYR 
                 A 
                 190 
                 41.313 
                 74.628 
                 44.663 
                 1.00 
                 71.70 
               
               
                 658 
                 CE2 
                 TYR 
                 A 
                 190 
                 40.792 
                 74.489 
                 43.388 
                 1.00 
                 71.27 
               
               
                 659 
                 CZ 
                 TYR 
                 A 
                 190 
                 39.527 
                 73.959 
                 43.221 
                 1.00 
                 73.00 
               
               
                 660 
                 OH 
                 TYR 
                 A 
                 190 
                 39.006 
                 73.831 
                 41.954 
                 1.00 
                 75.02 
               
               
                 661 
                 C 
                 TYR 
                 A 
                 190 
                 40.765 
                 75.967 
                 49.205 
                 1.00 
                 77.18 
               
               
                 662 
                 O 
                 TYR 
                 A 
                 190 
                 41.391 
                 76.993 
                 49.445 
                 1.00 
                 75.10 
               
               
                 663 
                 N 
                 LYS 
                 A 
                 191 
                 40.459 
                 75.072 
                 50.136 
                 1.00 
                 80.68 
               
               
                 664 
                 CA 
                 LYS 
                 A 
                 191 
                 40.776 
                 75.325 
                 51.530 
                 1.00 
                 83.42 
               
               
                 665 
                 CB 
                 LYS 
                 A 
                 191 
                 39.512 
                 75.083 
                 52.376 
                 1.00 
                 87.13 
               
               
                 666 
                 CG 
                 LYS 
                 A 
                 191 
                 38.307 
                 75.968 
                 51.936 
                 1.00 
                 91.60 
               
               
                 667 
                 CD 
                 LYS 
                 A 
                 191 
                 38.669 
                 77.476 
                 51.979 
                 1.00 
                 92.10 
               
               
                 668 
                 CE 
                 LYS 
                 A 
                 191 
                 37.646 
                 78.371 
                 51.279 
                 1.00 
                 89.87 
               
               
                 669 
                 NZ 
                 LYS 
                 A 
                 191 
                 38.016 
                 79.813 
                 51.420 
                 1.00 
                 87.76 
               
               
                 670 
                 C 
                 LYS 
                 A 
                 191 
                 41.980 
                 74.641 
                 52.149 
                 1.00 
                 83.37 
               
               
                 671 
                 O 
                 LYS 
                 A 
                 191 
                 41.964 
                 74.329 
                 53.338 
                 1.00 
                 84.58 
               
               
                 672 
                 N 
                 ASP 
                 A 
                 192 
                 43.016 
                 74.439 
                 51.331 
                 1.00 
                 83.34 
               
               
                 673 
                 CA 
                 ASP 
                 A 
                 192 
                 44.312 
                 73.858 
                 51.726 
                 1.00 
                 82.85 
               
               
                 674 
                 CB 
                 ASP 
                 A 
                 192 
                 44.224 
                 73.101 
                 53.049 
                 1.00 
                 85.81 
               
               
                 675 
                 CG 
                 ASP 
                 A 
                 192 
                 45.302 
                 73.527 
                 54.024 
                 1.00 
                 88.14 
               
               
                 676 
                 OD1 
                 ASP 
                 A 
                 192 
                 46.164 
                 74.343 
                 53.623 
                 1.00 
                 89.00 
               
               
                 677 
                 OD2 
                 ASP 
                 A 
                 192 
                 45.291 
                 73.054 
                 55.182 
                 1.00 
                 89.49 
               
               
                 678 
                 C 
                 ASP 
                 A 
                 192 
                 44.938 
                 72.947 
                 50.678 
                 1.00 
                 81.27 
               
               
                 679 
                 O 
                 ASP 
                 A 
                 192 
                 45.730 
                 72.057 
                 50.995 
                 1.00 
                 79.20 
               
               
                 680 
                 N 
                 ILE 
                 A 
                 193 
                 44.597 
                 73.197 
                 49.420 
                 1.00 
                 80.44 
               
               
                 681 
                 CA 
                 ILE 
                 A 
                 193 
                 45.100 
                 72.402 
                 48.309 
                 1.00 
                 77.82 
               
               
                 682 
                 CB 
                 ILE 
                 A 
                 193 
                 43.944 
                 71.677 
                 47.563 
                 1.00 
                 78.91 
               
               
                 683 
                 CG2 
                 ILE 
                 A 
                 193 
                 44.453 
                 70.383 
                 46.943 
                 1.00 
                 77.91 
               
               
                 684 
                 CG1 
                 ILE 
                 A 
                 193 
                 42.766 
                 71.420 
                 48.515 
                 1.00 
                 80.16 
               
               
                 685 
                 CD1 
                 ILE 
                 A 
                 193 
                 43.063 
                 70.491 
                 49.678 
                 1.00 
                 80.71 
               
               
                 686 
                 C 
                 ILE 
                 A 
                 193 
                 45.787 
                 73.314 
                 47.301 
                 1.00 
                 75.18 
               
               
                 687 
                 O 
                 ILE 
                 A 
                 193 
                 45.621 
                 74.535 
                 47.335 
                 1.00 
                 75.04 
               
               
                 688 
                 N 
                 LEU 
                 A 
                 194 
                 46.547 
                 72.701 
                 46.401 
                 1.00 
                 71.75 
               
               
                 689 
                 CA 
                 LEU 
                 A 
                 194 
                 47.250 
                 73.415 
                 45.351 
                 1.00 
                 68.94 
               
               
                 690 
                 CB 
                 LEU 
                 A 
                 194 
                 48.754 
                 73.424 
                 45.642 
                 1.00 
                 68.41 
               
               
                 691 
                 CG 
                 LEU 
                 A 
                 194 
                 49.481 
                 74.774 
                 45.610 
                 1.00 
                 67.08 
               
               
                 692 
                 CD1 
                 LEU 
                 A 
                 194 
                 48.845 
                 75.728 
                 46.608 
                 1.00 
                 64.34 
               
               
                 693 
                 CD2 
                 LEU 
                 A 
                 194 
                 50.958 
                 74.577 
                 45.927 
                 1.00 
                 65.33 
               
               
                 694 
                 C 
                 LEU 
                 A 
                 194 
                 46.950 
                 72.668 
                 44.049 
                 1.00 
                 68.41 
               
               
                 695 
                 O 
                 LEU 
                 A 
                 194 
                 47.372 
                 71.531 
                 43.860 
                 1.00 
                 67.07 
               
               
                 696 
                 N 
                 LEU 
                 A 
                 195 
                 46.203 
                 73.312 
                 43.158 
                 1.00 
                 67.56 
               
               
                 697 
                 CA 
                 LEU 
                 A 
                 195 
                 45.820 
                 72.713 
                 41.887 
                 1.00 
                 67.21 
               
               
                 698 
                 CB 
                 LEU 
                 A 
                 195 
                 44.372 
                 73.097 
                 41.577 
                 1.00 
                 67.35 
               
               
                 699 
                 CG 
                 LEU 
                 A 
                 195 
                 43.691 
                 72.529 
                 40.331 
                 1.00 
                 67.81 
               
               
                 700 
                 CD1 
                 LEU 
                 A 
                 195 
                 43.537 
                 71.022 
                 40.453 
                 1.00 
                 68.28 
               
               
                 701 
                 CD2 
                 LEU 
                 A 
                 195 
                 42.328 
                 73.179 
                 40.179 
                 1.00 
                 67.92 
               
               
                 702 
                 C 
                 LEU 
                 A 
                 195 
                 46.730 
                 73.119 
                 40.721 
                 1.00 
                 67.73 
               
               
                 703 
                 O 
                 LEU 
                 A 
                 195 
                 46.959 
                 74.306 
                 40.484 
                 1.00 
                 67.24 
               
               
                 704 
                 N 
                 LEU 
                 A 
                 196 
                 47.237 
                 72.133 
                 39.987 
                 1.00 
                 69.14 
               
               
                 705 
                 CA 
                 LEU 
                 A 
                 196 
                 48.115 
                 72.402 
                 38.851 
                 1.00 
                 70.88 
               
               
                 706 
                 CB 
                 LEU 
                 A 
                 196 
                 49.135 
                 71.273 
                 38.692 
                 1.00 
                 70.98 
               
               
                 707 
                 CG 
                 LEU 
                 A 
                 196 
                 49.964 
                 70.916 
                 39.928 
                 1.00 
                 71.86 
               
               
                 708 
                 CD1 
                 LEU 
                 A 
                 196 
                 51.095 
                 69.990 
                 39.518 
                 1.00 
                 71.83 
               
               
                 709 
                 CD2 
                 LEU 
                 A 
                 196 
                 50.529 
                 72.178 
                 40.565 
                 1.00 
                 71.12 
               
               
                 710 
                 C 
                 LEU 
                 A 
                 196 
                 47.342 
                 72.584 
                 37.541 
                 1.00 
                 72.68 
               
               
                 711 
                 O 
                 LEU 
                 A 
                 196 
                 46.141 
                 72.305 
                 37.466 
                 1.00 
                 72.73 
               
               
                 712 
                 N 
                 GLY 
                 A 
                 197 
                 48.044 
                 73.052 
                 36.509 
                 1.00 
                 74.33 
               
               
                 713 
                 CA 
                 GLY 
                 A 
                 197 
                 47.419 
                 73.274 
                 35.214 
                 1.00 
                 76.76 
               
               
                 714 
                 C 
                 GLY 
                 A 
                 197 
                 47.019 
                 72.015 
                 34.460 
                 1.00 
                 78.16 
               
               
                 715 
                 O 
                 GLY 
                 A 
                 197 
                 46.090 
                 72.038 
                 33.651 
                 1.00 
                 79.00 
               
               
                 716 
                 N 
                 ASN 
                 A 
                 198 
                 47.727 
                 70.920 
                 34.719 
                 1.00 
                 78.95 
               
               
                 717 
                 CA 
                 ASN 
                 A 
                 198 
                 47.452 
                 69.634 
                 34.081 
                 1.00 
                 77.71 
               
               
                 718 
                 CB 
                 ASN 
                 A 
                 198 
                 48.747 
                 68.843 
                 33.916 
                 1.00 
                 75.34 
               
               
                 719 
                 CG 
                 ASN 
                 A 
                 198 
                 49.438 
                 68.590 
                 35.235 
                 1.00 
                 73.85 
               
               
                 720 
                 OD1 
                 ASN 
                 A 
                 198 
                 48.836 
                 68.701 
                 36.303 
                 1.00 
                 73.15 
               
               
                 721 
                 ND2 
                 ASN 
                 A 
                 198 
                 50.709 
                 68.236 
                 35.166 
                 1.00 
                 74.53 
               
               
                 722 
                 C 
                 ASN 
                 A 
                 198 
                 46.462 
                 68.823 
                 34.917 
                 1.00 
                 78.19 
               
               
                 723 
                 O 
                 ASN 
                 A 
                 198 
                 46.275 
                 67.630 
                 34.697 
                 1.00 
                 78.86 
               
               
                 724 
                 N 
                 ASN 
                 A 
                 199 
                 45.861 
                 69.481 
                 35.899 
                 1.00 
                 78.85 
               
               
                 725 
                 CA 
                 ASN 
                 A 
                 199 
                 44.863 
                 68.875 
                 36.765 
                 1.00 
                 80.52 
               
               
                 726 
                 CB 
                 ASN 
                 A 
                 199 
                 43.827 
                 68.149 
                 35.907 
                 1.00 
                 81.74 
               
               
                 727 
                 CG 
                 ASN 
                 A 
                 199 
                 42.413 
                 68.404 
                 36.377 
                 1.00 
                 84.00 
               
               
                 728 
                 OD1 
                 ASN 
                 A 
                 199 
                 41.994 
                 67.924 
                 37.430 
                 1.00 
                 85.46 
               
               
                 729 
                 ND2 
                 ASN 
                 A 
                 199 
                 41.666 
                 69.182 
                 35.603 
                 1.00 
                 85.67 
               
               
                 730 
                 C 
                 ASN 
                 A 
                 199 
                 45.325 
                 67.968 
                 37.917 
                 1.00 
                 81.59 
               
               
                 731 
                 O 
                 ASN 
                 A 
                 199 
                 44.501 
                 67.297 
                 38.546 
                 1.00 
                 82.30 
               
               
                 732 
                 N 
                 TYR 
                 A 
                 200 
                 46.621 
                 67.932 
                 38.208 
                 1.00 
                 82.32 
               
               
                 733 
                 CA 
                 TYR 
                 A 
                 200 
                 47.085 
                 67.127 
                 39.340 
                 1.00 
                 82.86 
               
               
                 734 
                 CB 
                 TYR 
                 A 
                 200 
                 48.497 
                 66.600 
                 39.108 
                 1.00 
                 86.02 
               
               
                 735 
                 CG 
                 TYR 
                 A 
                 200 
                 48.553 
                 65.434 
                 38.148 
                 1.00 
                 90.33 
               
               
                 736 
                 CD1 
                 TYR 
                 A 
                 200 
                 48.531 
                 65.635 
                 36.767 
                 1.00 
                 90.78 
               
               
                 737 
                 CE1 
                 TYR 
                 A 
                 200 
                 48.591 
                 64.563 
                 35.880 
                 1.00 
                 91.68 
               
               
                 738 
                 CD2 
                 TYR 
                 A 
                 200 
                 48.639 
                 64.123 
                 38.621 
                 1.00 
                 91.79 
               
               
                 739 
                 CE2 
                 TYR 
                 A 
                 200 
                 48.697 
                 63.044 
                 37.743 
                 1.00 
                 92.89 
               
               
                 740 
                 CZ 
                 TYR 
                 A 
                 200 
                 48.677 
                 63.273 
                 36.371 
                 1.00 
                 92.47 
               
               
                 741 
                 OH 
                 TYR 
                 A 
                 200 
                 48.757 
                 62.217 
                 35.486 
                 1.00 
                 93.63 
               
               
                 742 
                 C 
                 TYR 
                 A 
                 200 
                 47.043 
                 67.990 
                 40.607 
                 1.00 
                 81.66 
               
               
                 743 
                 O 
                 TYR 
                 A 
                 200 
                 46.936 
                 69.211 
                 40.528 
                 1.00 
                 82.15 
               
               
                 744 
                 N 
                 VAL 
                 A 
                 201 
                 47.144 
                 67.364 
                 41.774 
                 1.00 
                 79.68 
               
               
                 745 
                 CA 
                 VAL 
                 A 
                 201 
                 47.057 
                 68.101 
                 43.035 
                 1.00 
                 76.53 
               
               
                 746 
                 CB 
                 VAL 
                 A 
                 201 
                 45.721 
                 67.716 
                 43.740 
                 1.00 
                 75.45 
               
               
                 747 
                 CG1 
                 VAL 
                 A 
                 201 
                 45.860 
                 67.737 
                 45.248 
                 1.00 
                 75.91 
               
               
                 748 
                 CG2 
                 VAL 
                 A 
                 201 
                 44.634 
                 68.679 
                 43.305 
                 1.00 
                 75.08 
               
               
                 749 
                 C 
                 VAL 
                 A 
                 201 
                 48.250 
                 67.952 
                 43.998 
                 1.00 
                 74.98 
               
               
                 750 
                 O 
                 VAL 
                 A 
                 201 
                 49.067 
                 67.047 
                 43.852 
                 1.00 
                 74.91 
               
               
                 751 
                 N 
                 ILE 
                 A 
                 202 
                 48.344 
                 68.870 
                 44.964 
                 1.00 
                 73.09 
               
               
                 752 
                 CA 
                 ILE 
                 A 
                 202 
                 49.408 
                 68.883 
                 45.972 
                 1.00 
                 71.49 
               
               
                 753 
                 CB 
                 ILE 
                 A 
                 202 
                 50.528 
                 69.879 
                 45.601 
                 1.00 
                 68.60 
               
               
                 754 
                 CG2 
                 ILE 
                 A 
                 202 
                 51.565 
                 69.925 
                 46.706 
                 1.00 
                 67.15 
               
               
                 755 
                 CG1 
                 ILE 
                 A 
                 202 
                 51.179 
                 69.478 
                 44.275 
                 1.00 
                 66.77 
               
               
                 756 
                 CD1 
                 ILE 
                 A 
                 202 
                 52.307 
                 70.397 
                 43.834 
                 1.00 
                 60.49 
               
               
                 757 
                 C 
                 ILE 
                 A 
                 202 
                 48.838 
                 69.323 
                 47.322 
                 1.00 
                 73.37 
               
               
                 758 
                 O 
                 ILE 
                 A 
                 202 
                 48.490 
                 70.490 
                 47.489 
                 1.00 
                 73.27 
               
               
                 759 
                 N 
                 HIS 
                 A 
                 203 
                 48.754 
                 68.404 
                 48.286 
                 1.00 
                 75.88 
               
               
                 760 
                 CA 
                 HIS 
                 A 
                 203 
                 48.207 
                 68.738 
                 49.605 
                 1.00 
                 77.79 
               
               
                 761 
                 CB 
                 HIS 
                 A 
                 203 
                 47.600 
                 67.498 
                 50.289 
                 1.00 
                 80.65 
               
               
                 762 
                 CG 
                 HIS 
                 A 
                 203 
                 46.388 
                 66.946 
                 49.599 
                 1.00 
                 84.74 
               
               
                 763 
                 CD2 
                 HIS 
                 A 
                 203 
                 45.068 
                 67.069 
                 49.875 
                 1.00 
                 86.58 
               
               
                 764 
                 ND1 
                 HIS 
                 A 
                 203 
                 46.467 
                 66.166 
                 48.458 
                 1.00 
                 87.32 
               
               
                 765 
                 CE1 
                 HIS 
                 A 
                 203 
                 45.247 
                 65.837 
                 48.068 
                 1.00 
                 87.56 
               
               
                 766 
                 NE2 
                 HIS 
                 A 
                 203 
                 44.382 
                 66.370 
                 48.907 
                 1.00 
                 88.31 
               
               
                 767 
                 C 
                 HIS 
                 A 
                 203 
                 49.252 
                 69.357 
                 50.525 
                 1.00 
                 76.72 
               
               
                 768 
                 O 
                 HIS 
                 A 
                 203 
                 50.442 
                 69.318 
                 50.234 
                 1.00 
                 74.93 
               
               
                 769 
                 N 
                 ARG 
                 A 
                 204 
                 48.795 
                 69.939 
                 51.628 
                 1.00 
                 78.09 
               
               
                 770 
                 CA 
                 ARG 
                 A 
                 204 
                 49.699 
                 70.560 
                 52.590 
                 1.00 
                 80.70 
               
               
                 771 
                 CB 
                 ARG 
                 A 
                 204 
                 48.912 
                 71.337 
                 53.650 
                 1.00 
                 80.75 
               
               
                 772 
                 CG 
                 ARG 
                 A 
                 204 
                 49.775 
                 72.295 
                 54.466 
                 1.00 
                 81.75 
               
               
                 773 
                 CD 
                 ARG 
                 A 
                 204 
                 49.047 
                 72.772 
                 55.700 
                 1.00 
                 82.91 
               
               
                 774 
                 NE 
                 ARG 
                 A 
                 204 
                 48.520 
                 74.129 
                 55.589 
                 1.00 
                 86.56 
               
               
                 775 
                 CZ 
                 ARG 
                 A 
                 204 
                 49.238 
                 75.231 
                 55.780 
                 1.00 
                 88.77 
               
               
                 776 
                 NH1 
                 ARG 
                 A 
                 204 
                 50.529 
                 75.140 
                 56.091 
                 1.00 
                 88.77 
               
               
                 777 
                 NH2 
                 ARG 
                 A 
                 204 
                 48.659 
                 76.424 
                 55.685 
                 1.00 
                 89.41 
               
               
                 778 
                 C 
                 ARG 
                 A 
                 204 
                 50.531 
                 69.471 
                 53.264 
                 1.00 
                 82.55 
               
               
                 779 
                 O 
                 ARG 
                 A 
                 204 
                 50.037 
                 68.360 
                 53.501 
                 1.00 
                 83.37 
               
               
                 780 
                 N 
                 ASN 
                 A 
                 205 
                 51.789 
                 69.787 
                 53.576 
                 1.00 
                 83.50 
               
               
                 781 
                 CA 
                 ASN 
                 A 
                 205 
                 52.683 
                 68.812 
                 54.199 
                 1.00 
                 83.06 
               
               
                 782 
                 CB 
                 ASN 
                 A 
                 205 
                 52.220 
                 68.507 
                 55.624 
                 1.00 
                 81.52 
               
               
                 783 
                 CG 
                 ASN 
                 A 
                 205 
                 52.491 
                 69.652 
                 56.571 
                 1.00 
                 81.76 
               
               
                 784 
                 OD1 
                 ASN 
                 A 
                 205 
                 51.885 
                 69.757 
                 57.632 
                 1.00 
                 82.84 
               
               
                 785 
                 ND2 
                 ASN 
                 A 
                 205 
                 53.420 
                 70.515 
                 56.194 
                 1.00 
                 81.81 
               
               
                 786 
                 C 
                 ASN 
                 A 
                 205 
                 52.652 
                 67.552 
                 53.350 
                 1.00 
                 83.55 
               
               
                 787 
                 O 
                 ASN 
                 A 
                 205 
                 52.437 
                 66.449 
                 53.842 
                 1.00 
                 83.67 
               
               
                 788 
                 N 
                 SER 
                 A 
                 206 
                 52.860 
                 67.739 
                 52.054 
                 1.00 
                 84.99 
               
               
                 789 
                 CA 
                 SER 
                 A 
                 206 
                 52.835 
                 66.635 
                 51.118 
                 1.00 
                 87.22 
               
               
                 790 
                 CB 
                 SER 
                 A 
                 206 
                 53.233 
                 67.124 
                 49.724 
                 1.00 
                 87.83 
               
               
                 791 
                 OG 
                 SER 
                 A 
                 206 
                 53.159 
                 66.072 
                 48.776 
                 1.00 
                 90.49 
               
               
                 792 
                 C 
                 SER 
                 A 
                 206 
                 53.760 
                 65.513 
                 51.552 
                 1.00 
                 88.48 
               
               
                 793 
                 O 
                 SER 
                 A 
                 206 
                 54.777 
                 65.744 
                 52.206 
                 1.00 
                 88.05 
               
               
                 794 
                 N 
                 CYS 
                 A 
                 207 
                 53.383 
                 64.289 
                 51.198 
                 1.00 
                 90.80 
               
               
                 795 
                 CA 
                 CYS 
                 A 
                 207 
                 54.190 
                 63.120 
                 51.517 
                 1.00 
                 93.18 
               
               
                 796 
                 CB 
                 CYS 
                 A 
                 207 
                 53.380 
                 61.838 
                 51.291 
                 1.00 
                 93.25 
               
               
                 797 
                 SG 
                 CYS 
                 A 
                 207 
                 52.513 
                 61.781 
                 49.696 
                 1.00 
                 95.95 
               
               
                 798 
                 C 
                 CYS 
                 A 
                 207 
                 55.400 
                 63.168 
                 50.584 
                 1.00 
                 93.76 
               
               
                 799 
                 O 
                 CYS 
                 A 
                 207 
                 56.419 
                 62.529 
                 50.834 
                 1.00 
                 94.36 
               
               
                 800 
                 N 
                 GLU 
                 A 
                 208 
                 55.263 
                 63.937 
                 49.505 
                 1.00 
                 93.72 
               
               
                 801 
                 CA 
                 GLU 
                 A 
                 208 
                 56.324 
                 64.129 
                 48.520 
                 1.00 
                 93.46 
               
               
                 802 
                 CB 
                 GLU 
                 A 
                 208 
                 55.721 
                 64.587 
                 47.193 
                 1.00 
                 92.84 
               
               
                 803 
                 CG 
                 GLU 
                 A 
                 208 
                 55.415 
                 63.488 
                 46.208 
                 1.00 
                 94.58 
               
               
                 804 
                 CD 
                 GLU 
                 A 
                 208 
                 56.673 
                 62.794 
                 45.706 
                 1.00 
                 95.95 
               
               
                 805 
                 OE1 
                 GLU 
                 A 
                 208 
                 57.752 
                 63.439 
                 45.705 
                 1.00 
                 95.95 
               
               
                 806 
                 OE2 
                 GLU 
                 A 
                 208 
                 56.581 
                 61.609 
                 45.299 
                 1.00 
                 95.95 
               
               
                 807 
                 C 
                 GLU 
                 A 
                 208 
                 57.233 
                 65.229 
                 49.055 
                 1.00 
                 93.74 
               
               
                 808 
                 O 
                 GLU 
                 A 
                 208 
                 57.347 
                 66.292 
                 48.444 
                 1.00 
                 94.45 
               
               
                 809 
                 N 
                 VAL 
                 A 
                 209 
                 57.881 
                 64.975 
                 50.189 
                 1.00 
                 93.41 
               
               
                 810 
                 CA 
                 VAL 
                 A 
                 209 
                 58.737 
                 65.978 
                 50.823 
                 1.00 
                 93.12 
               
               
                 811 
                 CB 
                 VAL 
                 A 
                 209 
                 59.421 
                 65.401 
                 52.105 
                 1.00 
                 94.77 
               
               
                 812 
                 CG1 
                 VAL 
                 A 
                 209 
                 58.356 
                 64.842 
                 53.057 
                 1.00 
                 93.37 
               
               
                 813 
                 CG2 
                 VAL 
                 A 
                 209 
                 60.442 
                 64.326 
                 51.734 
                 1.00 
                 95.25 
               
               
                 814 
                 C 
                 VAL 
                 A 
                 209 
                 59.781 
                 66.632 
                 49.911 
                 1.00 
                 91.19 
               
               
                 815 
                 O 
                 VAL 
                 A 
                 209 
                 60.526 
                 67.516 
                 50.336 
                 1.00 
                 91.21 
               
               
                 816 
                 N 
                 GLU 
                 A 
                 210 
                 59.821 
                 66.209 
                 48.653 
                 1.00 
                 89.40 
               
               
                 817 
                 CA 
                 GLU 
                 A 
                 210 
                 60.740 
                 66.780 
                 47.676 
                 1.00 
                 88.37 
               
               
                 818 
                 CB 
                 GLU 
                 A 
                 210 
                 60.913 
                 65.806 
                 46.505 
                 1.00 
                 90.60 
               
               
                 819 
                 CG 
                 GLU 
                 A 
                 210 
                 61.879 
                 66.250 
                 45.407 
                 1.00 
                 93.35 
               
               
                 820 
                 CD 
                 GLU 
                 A 
                 210 
                 63.334 
                 66.201 
                 45.844 
                 1.00 
                 95.95 
               
               
                 821 
                 OE1 
                 GLU 
                 A 
                 210 
                 63.653 
                 65.418 
                 46.767 
                 1.00 
                 95.95 
               
               
                 822 
                 OE2 
                 GLU 
                 A 
                 210 
                 64.163 
                 66.933 
                 45.255 
                 1.00 
                 95.95 
               
               
                 823 
                 C 
                 GLU 
                 A 
                 210 
                 60.145 
                 68.110 
                 47.173 
                 1.00 
                 86.57 
               
               
                 824 
                 O 
                 GLU 
                 A 
                 210 
                 60.837 
                 68.922 
                 46.558 
                 1.00 
                 86.69 
               
               
                 825 
                 N 
                 ILE 
                 A 
                 211 
                 58.857 
                 68.317 
                 47.441 
                 1.00 
                 83.24 
               
               
                 826 
                 CA 
                 ILE 
                 A 
                 211 
                 58.150 
                 69.529 
                 47.025 
                 1.00 
                 79.90 
               
               
                 827 
                 CB 
                 ILE 
                 A 
                 211 
                 57.220 
                 69.244 
                 45.833 
                 1.00 
                 78.92 
               
               
                 828 
                 CG2 
                 ILE 
                 A 
                 211 
                 57.991 
                 68.533 
                 44.734 
                 1.00 
                 78.06 
               
               
                 829 
                 CG1 
                 ILE 
                 A 
                 211 
                 56.028 
                 68.396 
                 46.297 
                 1.00 
                 78.68 
               
               
                 830 
                 CD1 
                 ILE 
                 A 
                 211 
                 55.086 
                 67.974 
                 45.184 
                 1.00 
                 75.93 
               
               
                 831 
                 C 
                 ILE 
                 A 
                 211 
                 57.296 
                 70.095 
                 48.168 
                 1.00 
                 78.80 
               
               
                 832 
                 O 
                 ILE 
                 A 
                 211 
                 56.613 
                 71.107 
                 48.012 
                 1.00 
                 78.27 
               
               
                 833 
                 N 
                 SER 
                 A 
                 212 
                 57.344 
                 69.428 
                 49.311 
                 1.00 
                 76.20 
               
               
                 834 
                 CA 
                 SER 
                 A 
                 212 
                 56.592 
                 69.824 
                 50.487 
                 1.00 
                 74.47 
               
               
                 835 
                 CB 
                 SER 
                 A 
                 212 
                 56.821 
                 68.790 
                 51.590 
                 1.00 
                 75.30 
               
               
                 836 
                 OG 
                 SER 
                 A 
                 212 
                 56.691 
                 69.362 
                 52.878 
                 1.00 
                 77.57 
               
               
                 837 
                 C 
                 SER 
                 A 
                 212 
                 56.908 
                 71.216 
                 51.024 
                 1.00 
                 73.37 
               
               
                 838 
                 O 
                 SER 
                 A 
                 212 
                 56.008 
                 71.958 
                 51.407 
                 1.00 
                 74.09 
               
               
                 839 
                 N 
                 ARG 
                 A 
                 213 
                 58.185 
                 71.572 
                 51.051 
                 1.00 
                 71.87 
               
               
                 840 
                 CA 
                 ARG 
                 A 
                 213 
                 58.609 
                 72.863 
                 51.587 
                 1.00 
                 70.38 
               
               
                 841 
                 CB 
                 ARG 
                 A 
                 213 
                 60.131 
                 72.858 
                 51.742 
                 1.00 
                 73.94 
               
               
                 842 
                 CG 
                 ARG 
                 A 
                 213 
                 60.639 
                 73.470 
                 53.022 
                 1.00 
                 78.32 
               
               
                 843 
                 CD 
                 ARG 
                 A 
                 213 
                 60.340 
                 72.599 
                 54.231 
                 1.00 
                 83.04 
               
               
                 844 
                 NE 
                 ARG 
                 A 
                 213 
                 61.155 
                 73.026 
                 55.369 
                 1.00 
                 89.48 
               
               
                 845 
                 CZ 
                 ARG 
                 A 
                 213 
                 60.955 
                 72.653 
                 56.629 
                 1.00 
                 91.42 
               
               
                 846 
                 NH1 
                 ARG 
                 A 
                 213 
                 59.952 
                 71.834 
                 56.930 
                 1.00 
                 91.45 
               
               
                 847 
                 NH2 
                 ARG 
                 A 
                 213 
                 61.759 
                 73.108 
                 57.589 
                 1.00 
                 91.27 
               
               
                 848 
                 C 
                 ARG 
                 A 
                 213 
                 58.168 
                 74.081 
                 50.762 
                 1.00 
                 67.58 
               
               
                 849 
                 O 
                 ARG 
                 A 
                 213 
                 57.608 
                 75.032 
                 51.302 
                 1.00 
                 67.01 
               
               
                 850 
                 N 
                 VAL 
                 A 
                 214 
                 58.427 
                 74.061 
                 49.460 
                 1.00 
                 64.81 
               
               
                 851 
                 CA 
                 VAL 
                 A 
                 214 
                 58.044 
                 75.173 
                 48.606 
                 1.00 
                 62.04 
               
               
                 852 
                 CB 
                 VAL 
                 A 
                 214 
                 58.607 
                 74.996 
                 47.184 
                 1.00 
                 58.84 
               
               
                 853 
                 CG1 
                 VAL 
                 A 
                 214 
                 57.959 
                 75.986 
                 46.234 
                 1.00 
                 56.68 
               
               
                 854 
                 CG2 
                 VAL 
                 A 
                 214 
                 60.102 
                 75.220 
                 47.207 
                 1.00 
                 57.41 
               
               
                 855 
                 C 
                 VAL 
                 A 
                 214 
                 56.525 
                 75.307 
                 48.546 
                 1.00 
                 63.00 
               
               
                 856 
                 O 
                 VAL 
                 A 
                 214 
                 55.985 
                 76.408 
                 48.678 
                 1.00 
                 63.30 
               
               
                 857 
                 N 
                 ALA 
                 A 
                 215 
                 55.835 
                 74.184 
                 48.362 
                 1.00 
                 62.03 
               
               
                 858 
                 CA 
                 ALA 
                 A 
                 215 
                 54.380 
                 74.192 
                 48.286 
                 1.00 
                 60.88 
               
               
                 859 
                 CB 
                 ALA 
                 A 
                 215 
                 53.871 
                 72.800 
                 47.981 
                 1.00 
                 59.03 
               
               
                 860 
                 C 
                 ALA 
                 A 
                 215 
                 53.726 
                 74.723 
                 49.564 
                 1.00 
                 61.63 
               
               
                 861 
                 O 
                 ALA 
                 A 
                 215 
                 52.703 
                 75.414 
                 49.504 
                 1.00 
                 61.65 
               
               
                 862 
                 N 
                 ASN 
                 A 
                 216 
                 54.301 
                 74.399 
                 50.721 
                 1.00 
                 60.68 
               
               
                 863 
                 CA 
                 ASN 
                 A 
                 216 
                 53.738 
                 74.879 
                 51.976 
                 1.00 
                 60.28 
               
               
                 864 
                 CB 
                 ASN 
                 A 
                 216 
                 54.419 
                 74.228 
                 53.184 
                 1.00 
                 61.56 
               
               
                 865 
                 CG 
                 ASN 
                 A 
                 216 
                 53.898 
                 72.819 
                 53.485 
                 1.00 
                 62.19 
               
               
                 866 
                 OD1 
                 ASN 
                 A 
                 216 
                 54.265 
                 72.236 
                 54.497 
                 1.00 
                 63.73 
               
               
                 867 
                 ND2 
                 ASN 
                 A 
                 216 
                 53.056 
                 72.273 
                 52.612 
                 1.00 
                 61.04 
               
               
                 868 
                 C 
                 ASN 
                 A 
                 216 
                 53.898 
                 76.387 
                 52.067 
                 1.00 
                 60.33 
               
               
                 869 
                 O 
                 ASN 
                 A 
                 216 
                 53.048 
                 77.065 
                 52.635 
                 1.00 
                 63.02 
               
               
                 870 
                 N 
                 ARG 
                 A 
                 217 
                 54.985 
                 76.922 
                 51.517 
                 1.00 
                 59.23 
               
               
                 871 
                 CA 
                 ARG 
                 A 
                 217 
                 55.192 
                 78.370 
                 51.558 
                 1.00 
                 58.81 
               
               
                 872 
                 CB 
                 ARG 
                 A 
                 217 
                 56.594 
                 78.764 
                 51.073 
                 1.00 
                 57.83 
               
               
                 873 
                 CG 
                 ARG 
                 A 
                 217 
                 57.714 
                 78.526 
                 52.077 
                 1.00 
                 57.69 
               
               
                 874 
                 CD 
                 ARG 
                 A 
                 217 
                 58.981 
                 79.310 
                 51.708 
                 1.00 
                 58.09 
               
               
                 875 
                 NE 
                 ARG 
                 A 
                 217 
                 58.831 
                 80.753 
                 51.908 
                 1.00 
                 55.60 
               
               
                 876 
                 CZ 
                 ARG 
                 A 
                 217 
                 59.725 
                 81.659 
                 51.515 
                 1.00 
                 55.82 
               
               
                 877 
                 NH1 
                 ARG 
                 A 
                 217 
                 60.835 
                 81.276 
                 50.900 
                 1.00 
                 53.67 
               
               
                 878 
                 NH2 
                 ARG 
                 A 
                 217 
                 59.512 
                 82.955 
                 51.738 
                 1.00 
                 55.80 
               
               
                 879 
                 C 
                 ARG 
                 A 
                 217 
                 54.163 
                 79.035 
                 50.670 
                 1.00 
                 59.19 
               
               
                 880 
                 O 
                 ARG 
                 A 
                 217 
                 53.542 
                 80.020 
                 51.064 
                 1.00 
                 60.54 
               
               
                 881 
                 N 
                 VAL 
                 A 
                 218 
                 53.994 
                 78.491 
                 49.467 
                 1.00 
                 58.88 
               
               
                 882 
                 CA 
                 VAL 
                 A 
                 218 
                 53.030 
                 79.013 
                 48.508 
                 1.00 
                 57.71 
               
               
                 883 
                 CB 
                 VAL 
                 A 
                 218 
                 52.951 
                 78.117 
                 47.259 
                 1.00 
                 57.51 
               
               
                 884 
                 CG1 
                 VAL 
                 A 
                 218 
                 51.759 
                 78.511 
                 46.417 
                 1.00 
                 56.31 
               
               
                 885 
                 CG2 
                 VAL 
                 A 
                 218 
                 54.254 
                 78.234 
                 46.444 
                 1.00 
                 56.52 
               
               
                 886 
                 C 
                 VAL 
                 A 
                 218 
                 51.663 
                 79.081 
                 49.165 
                 1.00 
                 58.31 
               
               
                 887 
                 O 
                 VAL 
                 A 
                 218 
                 50.958 
                 80.079 
                 49.045 
                 1.00 
                 59.36 
               
               
                 888 
                 N 
                 LEU 
                 A 
                 219 
                 51.301 
                 78.019 
                 49.874 
                 1.00 
                 59.03 
               
               
                 889 
                 CA 
                 LEU 
                 A 
                 219 
                 50.024 
                 77.961 
                 50.583 
                 1.00 
                 59.79 
               
               
                 890 
                 CB 
                 LEU 
                 A 
                 219 
                 49.804 
                 76.566 
                 51.169 
                 1.00 
                 58.97 
               
               
                 891 
                 CG 
                 LEU 
                 A 
                 219 
                 49.421 
                 75.426 
                 50.227 
                 1.00 
                 58.75 
               
               
                 892 
                 CD1 
                 LEU 
                 A 
                 219 
                 49.467 
                 74.100 
                 50.964 
                 1.00 
                 58.97 
               
               
                 893 
                 CD2 
                 LEU 
                 A 
                 219 
                 48.038 
                 75.669 
                 49.699 
                 1.00 
                 57.39 
               
               
                 894 
                 C 
                 LEU 
                 A 
                 219 
                 49.894 
                 78.986 
                 51.715 
                 1.00 
                 60.43 
               
               
                 895 
                 O 
                 LEU 
                 A 
                 219 
                 48.860 
                 79.634 
                 51.842 
                 1.00 
                 62.13 
               
               
                 896 
                 N 
                 ASP 
                 A 
                 220 
                 50.939 
                 79.129 
                 52.528 
                 1.00 
                 60.61 
               
               
                 897 
                 CA 
                 ASP 
                 A 
                 220 
                 50.930 
                 80.046 
                 53.673 
                 1.00 
                 60.83 
               
               
                 898 
                 CB 
                 ASP 
                 A 
                 220 
                 51.949 
                 79.587 
                 54.724 
                 1.00 
                 62.46 
               
               
                 899 
                 CG 
                 ASP 
                 A 
                 220 
                 51.589 
                 78.255 
                 55.345 
                 1.00 
                 66.34 
               
               
                 900 
                 OD1 
                 ASP 
                 A 
                 220 
                 52.388 
                 77.736 
                 56.156 
                 1.00 
                 67.10 
               
               
                 901 
                 OD2 
                 ASP 
                 A 
                 220 
                 50.509 
                 77.724 
                 55.026 
                 1.00 
                 70.35 
               
               
                 902 
                 C 
                 ASP 
                 A 
                 220 
                 51.213 
                 81.515 
                 53.383 
                 1.00 
                 60.01 
               
               
                 903 
                 O 
                 ASP 
                 A 
                 220 
                 50.628 
                 82.410 
                 54.006 
                 1.00 
                 59.81 
               
               
                 904 
                 N 
                 GLU 
                 A 
                 221 
                 52.117 
                 81.762 
                 52.443 
                 1.00 
                 57.85 
               
               
                 905 
                 CA 
                 GLU 
                 A 
                 221 
                 52.515 
                 83.119 
                 52.130 
                 1.00 
                 55.38 
               
               
                 906 
                 CB 
                 GLU 
                 A 
                 221 
                 54.038 
                 83.176 
                 52.087 
                 1.00 
                 55.40 
               
               
                 907 
                 CG 
                 GLU 
                 A 
                 221 
                 54.670 
                 82.658 
                 53.366 
                 1.00 
                 56.29 
               
               
                 908 
                 CD 
                 GLU 
                 A 
                 221 
                 56.173 
                 82.532 
                 53.269 
                 1.00 
                 59.30 
               
               
                 909 
                 OE1 
                 GLU 
                 A 
                 221 
                 56.831 
                 83.521 
                 52.889 
                 1.00 
                 59.21 
               
               
                 910 
                 OE2 
                 GLU 
                 A 
                 221 
                 56.704 
                 81.443 
                 53.575 
                 1.00 
                 61.34 
               
               
                 911 
                 C 
                 GLU 
                 A 
                 221 
                 51.930 
                 83.725 
                 50.871 
                 1.00 
                 53.92 
               
               
                 912 
                 O 
                 GLU 
                 A 
                 221 
                 52.113 
                 84.910 
                 50.629 
                 1.00 
                 52.66 
               
               
                 913 
                 N 
                 LEU 
                 A 
                 222 
                 51.228 
                 82.933 
                 50.069 
                 1.00 
                 53.81 
               
               
                 914 
                 CA 
                 LEU 
                 A 
                 222 
                 50.636 
                 83.470 
                 48.844 
                 1.00 
                 53.71 
               
               
                 915 
                 CB 
                 LEU 
                 A 
                 222 
                 51.347 
                 82.888 
                 47.616 
                 1.00 
                 51.30 
               
               
                 916 
                 CG 
                 LEU 
                 A 
                 222 
                 52.810 
                 83.349 
                 47.484 
                 1.00 
                 49.50 
               
               
                 917 
                 CD1 
                 LEU 
                 A 
                 222 
                 53.461 
                 82.687 
                 46.285 
                 1.00 
                 47.29 
               
               
                 918 
                 CD2 
                 LEU 
                 A 
                 222 
                 52.873 
                 84.874 
                 47.363 
                 1.00 
                 46.58 
               
               
                 919 
                 C 
                 LEU 
                 A 
                 222 
                 49.124 
                 83.254 
                 48.755 
                 1.00 
                 54.64 
               
               
                 920 
                 O 
                 LEU 
                 A 
                 222 
                 48.372 
                 84.201 
                 48.521 
                 1.00 
                 54.36 
               
               
                 921 
                 N 
                 VAL 
                 A 
                 223 
                 48.679 
                 82.020 
                 48.963 
                 1.00 
                 56.15 
               
               
                 922 
                 CA 
                 VAL 
                 A 
                 223 
                 47.254 
                 81.713 
                 48.908 
                 1.00 
                 57.59 
               
               
                 923 
                 CB 
                 VAL 
                 A 
                 223 
                 47.004 
                 80.188 
                 48.949 
                 1.00 
                 56.81 
               
               
                 924 
                 CG1 
                 VAL 
                 A 
                 223 
                 45.518 
                 79.914 
                 49.038 
                 1.00 
                 54.89 
               
               
                 925 
                 CG2 
                 VAL 
                 A 
                 223 
                 47.584 
                 79.532 
                 47.700 
                 1.00 
                 56.20 
               
               
                 926 
                 C 
                 VAL 
                 A 
                 223 
                 46.483 
                 82.376 
                 50.050 
                 1.00 
                 59.29 
               
               
                 927 
                 O 
                 VAL 
                 A 
                 223 
                 45.496 
                 83.071 
                 49.821 
                 1.00 
                 59.52 
               
               
                 928 
                 N 
                 ARG 
                 A 
                 224 
                 46.928 
                 82.161 
                 51.280 
                 1.00 
                 61.19 
               
               
                 929 
                 CA 
                 ARG 
                 A 
                 224 
                 46.263 
                 82.761 
                 52.426 
                 1.00 
                 62.98 
               
               
                 930 
                 CB 
                 ARG 
                 A 
                 224 
                 47.125 
                 82.580 
                 53.676 
                 1.00 
                 69.48 
               
               
                 931 
                 CG 
                 ARG 
                 A 
                 224 
                 46.506 
                 83.093 
                 54.965 
                 1.00 
                 77.90 
               
               
                 932 
                 CD 
                 ARG 
                 A 
                 224 
                 46.879 
                 82.149 
                 56.095 
                 1.00 
                 84.73 
               
               
                 933 
                 NE 
                 ARG 
                 A 
                 224 
                 46.527 
                 80.776 
                 55.724 
                 1.00 
                 90.58 
               
               
                 934 
                 CZ 
                 ARG 
                 A 
                 224 
                 46.763 
                 79.698 
                 56.466 
                 1.00 
                 92.62 
               
               
                 935 
                 NH1 
                 ARG 
                 A 
                 224 
                 47.366 
                 79.808 
                 57.647 
                 1.00 
                 92.56 
               
               
                 936 
                 NH2 
                 ARG 
                 A 
                 224 
                 46.388 
                 78.501 
                 56.024 
                 1.00 
                 92.21 
               
               
                 937 
                 C 
                 ARG 
                 A 
                 224 
                 46.015 
                 84.246 
                 52.156 
                 1.00 
                 60.60 
               
               
                 938 
                 O 
                 ARG 
                 A 
                 224 
                 44.877 
                 84.707 
                 52.194 
                 1.00 
                 60.88 
               
               
                 939 
                 N 
                 PRO 
                 A 
                 225 
                 47.079 
                 85.011 
                 51.866 
                 1.00 
                 58.53 
               
               
                 940 
                 CD 
                 PRO 
                 A 
                 225 
                 48.499 
                 84.619 
                 51.859 
                 1.00 
                 57.70 
               
               
                 941 
                 CA 
                 PRO 
                 A 
                 225 
                 46.942 
                 86.444 
                 51.586 
                 1.00 
                 57.18 
               
               
                 942 
                 CB 
                 PRO 
                 A 
                 225 
                 48.366 
                 86.864 
                 51.252 
                 1.00 
                 56.90 
               
               
                 943 
                 CG 
                 PRO 
                 A 
                 225 
                 49.192 
                 85.936 
                 52.074 
                 1.00 
                 56.41 
               
               
                 944 
                 C 
                 PRO 
                 A 
                 225 
                 45.983 
                 86.726 
                 50.432 
                 1.00 
                 57.76 
               
               
                 945 
                 O 
                 PRO 
                 A 
                 225 
                 45.213 
                 87.694 
                 50.479 
                 1.00 
                 57.84 
               
               
                 946 
                 N 
                 PHE 
                 A 
                 226 
                 46.047 
                 85.891 
                 49.389 
                 1.00 
                 56.60 
               
               
                 947 
                 CA 
                 PHE 
                 A 
                 226 
                 45.171 
                 86.036 
                 48.224 
                 1.00 
                 55.32 
               
               
                 948 
                 CB 
                 PHE 
                 A 
                 226 
                 45.503 
                 84.973 
                 47.159 
                 1.00 
                 53.08 
               
               
                 949 
                 CG 
                 PHE 
                 A 
                 226 
                 46.409 
                 85.462 
                 46.047 
                 1.00 
                 50.84 
               
               
                 950 
                 CD1 
                 PHE 
                 A 
                 226 
                 47.580 
                 86.162 
                 46.328 
                 1.00 
                 49.31 
               
               
                 951 
                 CD2 
                 PHE 
                 A 
                 226 
                 46.101 
                 85.182 
                 44.713 
                 1.00 
                 50.54 
               
               
                 952 
                 CE1 
                 PHE 
                 A 
                 226 
                 48.436 
                 86.575 
                 45.298 
                 1.00 
                 49.01 
               
               
                 953 
                 CE2 
                 PHE 
                 A 
                 226 
                 46.948 
                 85.589 
                 43.670 
                 1.00 
                 49.21 
               
               
                 954 
                 CZ 
                 PHE 
                 A 
                 226 
                 48.117 
                 86.286 
                 43.962 
                 1.00 
                 48.92 
               
               
                 955 
                 C 
                 PHE 
                 A 
                 226 
                 43.721 
                 85.866 
                 48.688 
                 1.00 
                 55.94 
               
               
                 956 
                 O 
                 PHE 
                 A 
                 226 
                 42.811 
                 86.546 
                 48.207 
                 1.00 
                 55.32 
               
               
                 957 
                 N 
                 GLN 
                 A 
                 227 
                 43.515 
                 84.962 
                 49.637 
                 1.00 
                 56.87 
               
               
                 958 
                 CA 
                 GLN 
                 A 
                 227 
                 42.184 
                 84.710 
                 50.162 
                 1.00 
                 58.58 
               
               
                 959 
                 CB 
                 GLN 
                 A 
                 227 
                 42.141 
                 83.366 
                 50.882 
                 1.00 
                 56.62 
               
               
                 960 
                 CG 
                 GLN 
                 A 
                 227 
                 42.638 
                 82.221 
                 50.040 
                 1.00 
                 59.05 
               
               
                 961 
                 CD 
                 GLN 
                 A 
                 227 
                 42.460 
                 80.882 
                 50.710 
                 1.00 
                 60.02 
               
               
                 962 
                 OE1 
                 GLN 
                 A 
                 227 
                 42.872 
                 80.680 
                 51.855 
                 1.00 
                 61.01 
               
               
                 963 
                 NE2 
                 GLN 
                 A 
                 227 
                 41.846 
                 79.950 
                 49.993 
                 1.00 
                 62.09 
               
               
                 964 
                 C 
                 GLN 
                 A 
                 227 
                 41.778 
                 85.816 
                 51.122 
                 1.00 
                 60.63 
               
               
                 965 
                 O 
                 GLN 
                 A 
                 227 
                 40.644 
                 86.291 
                 51.083 
                 1.00 
                 62.38 
               
               
                 966 
                 N 
                 GLU 
                 A 
                 228 
                 42.706 
                 86.228 
                 51.981 
                 1.00 
                 61.78 
               
               
                 967 
                 CA 
                 GLU 
                 A 
                 228 
                 42.416 
                 87.277 
                 52.946 
                 1.00 
                 63.03 
               
               
                 968 
                 CB 
                 GLU 
                 A 
                 228 
                 43.639 
                 87.558 
                 53.819 
                 1.00 
                 67.62 
               
               
                 969 
                 CG 
                 GLU 
                 A 
                 228 
                 44.010 
                 86.404 
                 54.747 
                 1.00 
                 76.28 
               
               
                 970 
                 CD 
                 GLU 
                 A 
                 228 
                 45.236 
                 86.693 
                 55.607 
                 1.00 
                 81.36 
               
               
                 971 
                 OE1 
                 GLU 
                 A 
                 228 
                 46.328 
                 86.972 
                 55.045 
                 1.00 
                 84.37 
               
               
                 972 
                 OE2 
                 GLU 
                 A 
                 228 
                 45.104 
                 86.633 
                 56.850 
                 1.00 
                 83.53 
               
               
                 973 
                 C 
                 GLU 
                 A 
                 228 
                 41.950 
                 88.567 
                 52.289 
                 1.00 
                 61.96 
               
               
                 974 
                 O 
                 GLU 
                 A 
                 228 
                 40.870 
                 89.060 
                 52.602 
                 1.00 
                 59.80 
               
               
                 975 
                 N 
                 ILE 
                 A 
                 229 
                 42.751 
                 89.111 
                 51.373 
                 1.00 
                 61.04 
               
               
                 976 
                 CA 
                 ILE 
                 A 
                 229 
                 42.384 
                 90.357 
                 50.706 
                 1.00 
                 61.78 
               
               
                 977 
                 CG 
                 ILE 
                 A 
                 229 
                 43.601 
                 91.058 
                 50.081 
                 1.00 
                 65.16 
               
               
                 978 
                 CG2 
                 ILE 
                 A 
                 229 
                 44.834 
                 90.889 
                 50.961 
                 1.00 
                 67.55 
               
               
                 979 
                 CG1 
                 ILE 
                 A 
                 229 
                 43.895 
                 90.440 
                 48.724 
                 1.00 
                 69.34 
               
               
                 980 
                 CD1 
                 ILE 
                 A 
                 229 
                 44.960 
                 91.157 
                 47.982 
                 1.00 
                 72.97 
               
               
                 981 
                 C 
                 ILE 
                 A 
                 229 
                 41.370 
                 90.174 
                 49.584 
                 1.00 
                 60.67 
               
               
                 982 
                 O 
                 ILE 
                 A 
                 229 
                 40.820 
                 91.156 
                 49.077 
                 1.00 
                 59.92 
               
               
                 983 
                 N 
                 GLN 
                 A 
                 230 
                 41.146 
                 88.924 
                 49.182 
                 1.00 
                 59.30 
               
               
                 984 
                 CA 
                 GLN 
                 A 
                 230 
                 40.210 
                 88.607 
                 48.105 
                 1.00 
                 59.64 
               
               
                 985 
                 CG 
                 GLN 
                 A 
                 230 
                 38.769 
                 88.908 
                 48.550 
                 1.00 
                 61.87 
               
               
                 986 
                 CG 
                 GLN 
                 A 
                 230 
                 38.115 
                 87.759 
                 49.324 
                 1.00 
                 67.60 
               
               
                 987 
                 CD 
                 GLN 
                 A 
                 230 
                 36.654 
                 88.032 
                 49.684 
                 1.00 
                 72.09 
               
               
                 988 
                 OE1 
                 GLN 
                 A 
                 230 
                 35.951 
                 87.150 
                 50.187 
                 1.00 
                 74.46 
               
               
                 989 
                 NE2 
                 GLN 
                 A 
                 230 
                 36.195 
                 89.256 
                 49.429 
                 1.00 
                 71.65 
               
               
                 990 
                 C 
                 GLN 
                 A 
                 230 
                 40.529 
                 89.334 
                 46.789 
                 1.00 
                 57.13 
               
               
                 991 
                 O 
                 GLN 
                 A 
                 230 
                 39.721 
                 90.095 
                 46.264 
                 1.00 
                 56.69 
               
               
                 992 
                 N 
                 ILE 
                 A 
                 231 
                 41.713 
                 89.073 
                 46.251 
                 1.00 
                 54.06 
               
               
                 993 
                 CA 
                 ILE 
                 A 
                 231 
                 42.160 
                 89.707 
                 45.013 
                 1.00 
                 52.71 
               
               
                 994 
                 CB 
                 ILE 
                 A 
                 231 
                 43.662 
                 89.394 
                 44.795 
                 1.00 
                 50.87 
               
               
                 995 
                 CG2 
                 ILE 
                 A 
                 231 
                 43.873 
                 87.898 
                 44.727 
                 1.00 
                 51.30 
               
               
                 996 
                 CG1 
                 ILE 
                 A 
                 231 
                 44.162 
                 90.048 
                 43.513 
                 1.00 
                 51.63 
               
               
                 997 
                 CD1 
                 ILE 
                 A 
                 231 
                 45.615 
                 89.747 
                 43.218 
                 1.00 
                 51.05 
               
               
                 998 
                 C 
                 ILE 
                 A 
                 231 
                 41.340 
                 89.281 
                 43.770 
                 1.00 
                 51.08 
               
               
                 999 
                 O 
                 ILE 
                 A 
                 231 
                 41.137 
                 88.088 
                 43.536 
                 1.00 
                 50.68 
               
               
                 1000 
                 N 
                 ASP 
                 A 
                 232 
                 40.863 
                 90.240 
                 42.974 
                 1.00 
                 48.64 
               
               
                 1001 
                 CA 
                 ASP 
                 A 
                 232 
                 40.086 
                 89.859 
                 41.797 
                 1.00 
                 47.47 
               
               
                 1002 
                 CB 
                 ASP 
                 A 
                 232 
                 38.904 
                 90.821 
                 41.525 
                 1.00 
                 46.95 
               
               
                 1003 
                 CG 
                 ASP 
                 A 
                 232 
                 39.332 
                 92.238 
                 41.133 
                 1.00 
                 48.77 
               
               
                 1004 
                 OD1 
                 ASP 
                 A 
                 232 
                 40.277 
                 92.405 
                 40.322 
                 1.00 
                 48.21 
               
               
                 1005 
                 OD2 
                 ASP 
                 A 
                 232 
                 38.683 
                 93.194 
                 41.624 
                 1.00 
                 45.17 
               
               
                 1006 
                 C 
                 ASP 
                 A 
                 232 
                 40.942 
                 89.690 
                 40.556 
                 1.00 
                 46.62 
               
               
                 1007 
                 O 
                 ASP 
                 A 
                 232 
                 42.154 
                 89.914 
                 40.596 
                 1.00 
                 46.42 
               
               
                 1008 
                 N 
                 ASP 
                 A 
                 233 
                 40.304 
                 89.265 
                 39.467 
                 1.00 
                 46.49 
               
               
                 1009 
                 CA 
                 ASP 
                 A 
                 233 
                 40.982 
                 89.013 
                 38.199 
                 1.00 
                 48.18 
               
               
                 1010 
                 CB 
                 ASP 
                 A 
                 233 
                 39.965 
                 88.575 
                 37.151 
                 1.00 
                 52.12 
               
               
                 1011 
                 CG 
                 ASP 
                 A 
                 233 
                 39.694 
                 87.069 
                 37.177 
                 1.00 
                 57.52 
               
               
                 1012 
                 OD1 
                 ASP 
                 A 
                 233 
                 39.562 
                 86.489 
                 38.285 
                 1.00 
                 56.60 
               
               
                 1013 
                 OD2 
                 ASP 
                 A 
                 233 
                 39.596 
                 86.474 
                 36.074 
                 1.00 
                 59.38 
               
               
                 1014 
                 C 
                 ASP 
                 A 
                 233 
                 41.777 
                 90.190 
                 37.668 
                 1.00 
                 47.78 
               
               
                 1015 
                 O 
                 ASP 
                 A 
                 233 
                 42.889 
                 90.016 
                 37.175 
                 1.00 
                 47.91 
               
               
                 1016 
                 N 
                 ASN 
                 A 
                 234 
                 41.211 
                 91.389 
                 37.764 
                 1.00 
                 45.75 
               
               
                 1017 
                 CA 
                 ASN 
                 A 
                 234 
                 41.891 
                 92.580 
                 37.281 
                 1.00 
                 45.96 
               
               
                 1018 
                 CB 
                 ASN 
                 A 
                 234 
                 40.943 
                 93.765 
                 37.316 
                 1.00 
                 45.13 
               
               
                 1019 
                 CG 
                 ASN 
                 A 
                 234 
                 39.780 
                 93.581 
                 36.396 
                 1.00 
                 46.35 
               
               
                 1020 
                 OD1 
                 ASN 
                 A 
                 234 
                 39.960 
                 93.329 
                 35.203 
                 1.00 
                 49.07 
               
               
                 1021 
                 ND2 
                 ASN 
                 A 
                 234 
                 38.571 
                 93.699 
                 36.932 
                 1.00 
                 43.71 
               
               
                 1022 
                 C 
                 ASN 
                 A 
                 234 
                 43.143 
                 92.912 
                 38.066 
                 1.00 
                 46.24 
               
               
                 1023 
                 O 
                 ASN 
                 A 
                 234 
                 44.174 
                 93.234 
                 37.488 
                 1.00 
                 46.25 
               
               
                 1024 
                 N 
                 GLU 
                 A 
                 235 
                 43.049 
                 92.834 
                 39.388 
                 1.00 
                 47.76 
               
               
                 1025 
                 CA 
                 GLU 
                 A 
                 235 
                 44.182 
                 93.128 
                 40.253 
                 1.00 
                 48.46 
               
               
                 1026 
                 CB 
                 GLU 
                 A 
                 235 
                 43.724 
                 93.106 
                 41.711 
                 1.00 
                 49.43 
               
               
                 1027 
                 CG 
                 GLU 
                 A 
                 235 
                 42.606 
                 94.125 
                 41.978 
                 1.00 
                 50.73 
               
               
                 1028 
                 CD 
                 GLU 
                 A 
                 235 
                 41.942 
                 93.956 
                 43.338 
                 1.00 
                 53.14 
               
               
                 1029 
                 OE1 
                 GLU 
                 A 
                 235 
                 41.787 
                 92.805 
                 43.807 
                 1.00 
                 52.31 
               
               
                 1030 
                 OE2 
                 GLU 
                 A 
                 235 
                 41.551 
                 94.979 
                 43.934 
                 1.00 
                 55.18 
               
               
                 1031 
                 C 
                 GLU 
                 A 
                 235 
                 45.289 
                 92.111 
                 39.992 
                 1.00 
                 48.60 
               
               
                 1032 
                 O 
                 GLU 
                 A 
                 235 
                 46.459 
                 92.474 
                 39.843 
                 1.00 
                 48.72 
               
               
                 1033 
                 N 
                 TYR 
                 A 
                 236 
                 44.912 
                 90.839 
                 39.903 
                 1.00 
                 48.87 
               
               
                 1034 
                 CA 
                 TYR 
                 A 
                 236 
                 45.870 
                 89.770 
                 39.630 
                 1.00 
                 48.41 
               
               
                 1035 
                 CB 
                 TYR 
                 A 
                 236 
                 45.154 
                 88.422 
                 39.678 
                 1.00 
                 49.95 
               
               
                 1036 
                 CG 
                 TYR 
                 A 
                 236 
                 45.920 
                 87.283 
                 39.051 
                 1.00 
                 53.44 
               
               
                 1037 
                 CD1 
                 TYR 
                 A 
                 236 
                 45.651 
                 86.886 
                 37.747 
                 1.00 
                 55.68 
               
               
                 1038 
                 CE1 
                 TYR 
                 A 
                 236 
                 46.344 
                 85.841 
                 37.155 
                 1.00 
                 57.29 
               
               
                 1039 
                 CD2 
                 TYR 
                 A 
                 236 
                 46.901 
                 86.592 
                 39.760 
                 1.00 
                 52.47 
               
               
                 1040 
                 CE2 
                 TYR 
                 A 
                 236 
                 47.606 
                 85.542 
                 39.172 
                 1.00 
                 53.08 
               
               
                 1041 
                 CZ 
                 TYR 
                 A 
                 236 
                 47.315 
                 85.167 
                 37.870 
                 1.00 
                 56.41 
               
               
                 1042 
                 OH 
                 TYR 
                 A 
                 236 
                 47.994 
                 84.134 
                 37.252 
                 1.00 
                 56.73 
               
               
                 1043 
                 C 
                 TYR 
                 A 
                 236 
                 46.577 
                 89.962 
                 38.282 
                 1.00 
                 48.08 
               
               
                 1044 
                 O 
                 TYR 
                 A 
                 236 
                 47.791 
                 89.781 
                 38.175 
                 1.00 
                 48.08 
               
               
                 1045 
                 N 
                 ALA 
                 A 
                 237 
                 45.823 
                 90.338 
                 37.254 
                 1.00 
                 48.09 
               
               
                 1046 
                 CA 
                 ALA 
                 A 
                 237 
                 46.412 
                 90.556 
                 35.939 
                 1.00 
                 46.29 
               
               
                 1047 
                 CB 
                 ALA 
                 A 
                 237 
                 45.337 
                 90.916 
                 34.935 
                 1.00 
                 46.10 
               
               
                 1048 
                 C 
                 ALA 
                 A 
                 237 
                 47.452 
                 91.668 
                 36.022 
                 1.00 
                 46.46 
               
               
                 1049 
                 O 
                 ALA 
                 A 
                 237 
                 48.490 
                 91.599 
                 35.376 
                 1.00 
                 45.66 
               
               
                 1050 
                 N 
                 CYS 
                 A 
                 238 
                 47.170 
                 92.699 
                 36.816 
                 1.00 
                 46.82 
               
               
                 1051 
                 CA 
                 CYS 
                 A 
                 238 
                 48.115 
                 93.802 
                 36.976 
                 1.00 
                 48.15 
               
               
                 1052 
                 CB 
                 CYS 
                 A 
                 238 
                 47.458 
                 94.968 
                 37.732 
                 1.00 
                 49.33 
               
               
                 1053 
                 SG 
                 CYS 
                 A 
                 238 
                 46.241 
                 95.936 
                 36.761 
                 1.00 
                 51.88 
               
               
                 1054 
                 C 
                 CYS 
                 A 
                 238 
                 49.411 
                 93.348 
                 37.686 
                 1.00 
                 47.77 
               
               
                 1055 
                 O 
                 CYS 
                 A 
                 238 
                 50.506 
                 93.701 
                 37.245 
                 1.00 
                 47.67 
               
               
                 1056 
                 N 
                 LEU 
                 A 
                 239 
                 49.303 
                 92.568 
                 38.766 
                 1.00 
                 46.50 
               
               
                 1057 
                 CA 
                 LEU 
                 A 
                 239 
                 50.503 
                 92.073 
                 39.459 
                 1.00 
                 48.00 
               
               
                 1058 
                 CB 
                 LEU 
                 A 
                 239 
                 50.146 
                 91.171 
                 40.635 
                 1.00 
                 46.75 
               
               
                 1059 
                 CG 
                 LEU 
                 A 
                 239 
                 49.706 
                 91.835 
                 41.927 
                 1.00 
                 48.33 
               
               
                 1060 
                 CD1 
                 LEU 
                 A 
                 239 
                 49.595 
                 90.778 
                 43.008 
                 1.00 
                 47.55 
               
               
                 1061 
                 CD2 
                 LEU 
                 A 
                 239 
                 50.721 
                 92.893 
                 42.324 
                 1.00 
                 49.61 
               
               
                 1062 
                 C 
                 LEU 
                 A 
                 239 
                 51.333 
                 91.245 
                 38.497 
                 1.00 
                 49.12 
               
               
                 1063 
                 O 
                 LEU 
                 A 
                 239 
                 52.558 
                 91.302 
                 38.477 
                 1.00 
                 49.41 
               
               
                 1064 
                 N 
                 LYS 
                 A 
                 240 
                 50.633 
                 90.448 
                 37.710 
                 1.00 
                 50.71 
               
               
                 1065 
                 CA 
                 LYS 
                 A 
                 240 
                 51.252 
                 89.589 
                 36.728 
                 1.00 
                 50.49 
               
               
                 1066 
                 CB 
                 LYS 
                 A 
                 240 
                 50.126 
                 88.828 
                 36.053 
                 1.00 
                 54.00 
               
               
                 1067 
                 CG 
                 LYS 
                 A 
                 240 
                 50.485 
                 87.682 
                 35.157 
                 1.00 
                 57.50 
               
               
                 1068 
                 CD 
                 LYS 
                 A 
                 240 
                 49.187 
                 86.963 
                 34.799 
                 1.00 
                 56.35 
               
               
                 1069 
                 CE 
                 LYS 
                 A 
                 240 
                 49.320 
                 86.109 
                 33.558 
                 1.00 
                 59.43 
               
               
                 1070 
                 NZ 
                 LYS 
                 A 
                 240 
                 48.042 
                 85.379 
                 33.300 
                 1.00 
                 59.29 
               
               
                 1071 
                 C 
                 LYS 
                 A 
                 240 
                 52.062 
                 90.443 
                 35.739 
                 1.00 
                 50.77 
               
               
                 1072 
                 O 
                 LYS 
                 A 
                 240 
                 53.230 
                 90.156 
                 35.473 
                 1.00 
                 52.17 
               
               
                 1073 
                 N 
                 ALA 
                 A 
                 241 
                 51.457 
                 91.516 
                 35.225 
                 1.00 
                 49.05 
               
               
                 1074 
                 CA 
                 ALA 
                 A 
                 241 
                 52.139 
                 92.392 
                 34.264 
                 1.00 
                 47.99 
               
               
                 1075 
                 CB 
                 ALA 
                 A 
                 241 
                 51.125 
                 93.306 
                 33.569 
                 1.00 
                 45.58 
               
               
                 1076 
                 C 
                 ALA 
                 A 
                 241 
                 53.254 
                 93.235 
                 34.892 
                 1.00 
                 48.74 
               
               
                 1077 
                 O 
                 ALA 
                 A 
                 241 
                 54.284 
                 93.473 
                 34.257 
                 1.00 
                 47.88 
               
               
                 1078 
                 N 
                 ILE 
                 A 
                 242 
                 53.042 
                 93.704 
                 36.121 
                 1.00 
                 49.21 
               
               
                 1079 
                 CA 
                 ILE 
                 A 
                 242 
                 54.052 
                 94.502 
                 36.818 
                 1.00 
                 48.58 
               
               
                 1080 
                 CB 
                 ILE 
                 A 
                 242 
                 53.546 
                 94.949 
                 38.211 
                 1.00 
                 46.80 
               
               
                 1081 
                 CG2 
                 ILE 
                 A 
                 242 
                 54.710 
                 95.441 
                 39.065 
                 1.00 
                 44.00 
               
               
                 1082 
                 CG1 
                 ILE 
                 A 
                 242 
                 52.483 
                 96.042 
                 38.048 
                 1.00 
                 46.90 
               
               
                 1083 
                 CD1 
                 ILE 
                 A 
                 242 
                 51.708 
                 96.362 
                 39.343 
                 1.00 
                 44.31 
               
               
                 1084 
                 C 
                 ILE 
                 A 
                 242 
                 55.330 
                 93.663 
                 36.985 
                 1.00 
                 49.40 
               
               
                 1085 
                 O 
                 ILE 
                 A 
                 242 
                 56.447 
                 94.154 
                 36.818 
                 1.00 
                 50.74 
               
               
                 1086 
                 N 
                 VAL 
                 A 
                 243 
                 55.155 
                 92.390 
                 37.301 
                 1.00 
                 48.19 
               
               
                 1087 
                 CA 
                 VAL 
                 A 
                 243 
                 56.279 
                 91.485 
                 37.478 
                 1.00 
                 48.24 
               
               
                 1088 
                 CB 
                 VAL 
                 A 
                 243 
                 55.783 
                 90.154 
                 38.104 
                 1.00 
                 45.34 
               
               
                 1089 
                 CG1 
                 VAL 
                 A 
                 243 
                 56.826 
                 89.096 
                 38.006 
                 1.00 
                 38.32 
               
               
                 1090 
                 CG2 
                 VAL 
                 A 
                 243 
                 55.409 
                 90.390 
                 39.558 
                 1.00 
                 45.18 
               
               
                 1091 
                 C 
                 VAL 
                 A 
                 243 
                 56.984 
                 91.218 
                 36.142 
                 1.00 
                 51.49 
               
               
                 1092 
                 O 
                 VAL 
                 A 
                 243 
                 58.213 
                 91.145 
                 36.082 
                 1.00 
                 52.53 
               
               
                 1093 
                 N 
                 PHE 
                 A 
                 244 
                 56.201 
                 91.095 
                 35.073 
                 1.00 
                 54.83 
               
               
                 1094 
                 CA 
                 PHE 
                 A 
                 244 
                 56.728 
                 90.814 
                 33.732 
                 1.00 
                 55.59 
               
               
                 1095 
                 CB 
                 PHE 
                 A 
                 244 
                 55.575 
                 90.453 
                 32.796 
                 1.00 
                 54.57 
               
               
                 1096 
                 CG 
                 PHE 
                 A 
                 244 
                 56.013 
                 89.938 
                 31.460 
                 1.00 
                 53.37 
               
               
                 1097 
                 CD1 
                 PHE 
                 A 
                 244 
                 56.555 
                 88.670 
                 31.337 
                 1.00 
                 52.35 
               
               
                 1098 
                 CD2 
                 PHE 
                 A 
                 244 
                 55.864 
                 90.718 
                 30.319 
                 1.00 
                 55.39 
               
               
                 1099 
                 CE1 
                 PHE 
                 A 
                 244 
                 56.943 
                 88.175 
                 30.102 
                 1.00 
                 53.54 
               
               
                 1100 
                 CE2 
                 PHE 
                 A 
                 244 
                 56.248 
                 90.234 
                 29.069 
                 1.00 
                 56.32 
               
               
                 1101 
                 CZ 
                 PHE 
                 A 
                 244 
                 56.789 
                 88.959 
                 28.959 
                 1.00 
                 56.06 
               
               
                 1102 
                 C 
                 PHE 
                 A 
                 244 
                 57.514 
                 91.979 
                 33.133 
                 1.00 
                 57.68 
               
               
                 1103 
                 O 
                 PHE 
                 A 
                 244 
                 58.623 
                 91.799 
                 32.623 
                 1.00 
                 58.70 
               
               
                 1104 
                 N 
                 PHE 
                 A 
                 245 
                 56.935 
                 93.172 
                 33.187 
                 1.00 
                 58.41 
               
               
                 1105 
                 CA 
                 PHE 
                 A 
                 245 
                 57.591 
                 94.347 
                 32.635 
                 1.00 
                 59.59 
               
               
                 1106 
                 CB 
                 PHE 
                 A 
                 245 
                 56.538 
                 95.388 
                 32.225 
                 1.00 
                 58.77 
               
               
                 1107 
                 CG 
                 PHE 
                 A 
                 245 
                 55.705 
                 94.962 
                 31.037 
                 1.00 
                 58.78 
               
               
                 1108 
                 CD1 
                 PHE 
                 A 
                 245 
                 56.298 
                 94.780 
                 29.787 
                 1.00 
                 58.21 
               
               
                 1109 
                 CD2 
                 PHE 
                 A 
                 245 
                 54.343 
                 94.684 
                 31.176 
                 1.00 
                 58.58 
               
               
                 1110 
                 CE1 
                 PHE 
                 A 
                 245 
                 55.550 
                 94.325 
                 28.692 
                 1.00 
                 57.32 
               
               
                 1111 
                 CE2 
                 PHE 
                 A 
                 245 
                 53.585 
                 94.225 
                 30.082 
                 1.00 
                 57.14 
               
               
                 1112 
                 CZ 
                 PHE 
                 A 
                 245 
                 54.193 
                 94.046 
                 28.840 
                 1.00 
                 56.15 
               
               
                 1113 
                 C 
                 PHE 
                 A 
                 245 
                 58.600 
                 94.931 
                 33.614 
                 1.00 
                 61.09 
               
               
                 1114 
                 O 
                 PHE 
                 A 
                 245 
                 58.423 
                 96.030 
                 34.132 
                 1.00 
                 60.20 
               
               
                 1115 
                 N 
                 ASP 
                 A 
                 246 
                 59.668 
                 94.172 
                 33.854 
                 1.00 
                 63.54 
               
               
                 1116 
                 CA 
                 ASP 
                 A 
                 246 
                 60.731 
                 94.582 
                 34.762 
                 1.00 
                 65.15 
               
               
                 1117 
                 CB 
                 ASP 
                 A 
                 246 
                 61.227 
                 93.397 
                 35.578 
                 1.00 
                 64.55 
               
               
                 1118 
                 CG 
                 ASP 
                 A 
                 246 
                 61.961 
                 93.827 
                 36.837 
                 1.00 
                 67.76 
               
               
                 1119 
                 OD1 
                 ASP 
                 A 
                 246 
                 62.644 
                 94.880 
                 36.805 
                 1.00 
                 65.16 
               
               
                 1120 
                 OD2 
                 ASP 
                 A 
                 246 
                 61.857 
                 93.109 
                 37.860 
                 1.00 
                 69.69 
               
               
                 1121 
                 C 
                 ASP 
                 A 
                 246 
                 61.911 
                 95.159 
                 33.993 
                 1.00 
                 66.87 
               
               
                 1122 
                 O 
                 ASP 
                 A 
                 246 
                 62.597 
                 94.438 
                 33.268 
                 1.00 
                 66.84 
               
               
                 1123 
                 N 
                 PRO 
                 A 
                 247 
                 62.177 
                 96.466 
                 34.157 
                 1.00 
                 68.77 
               
               
                 1124 
                 CD 
                 PRO 
                 A 
                 247 
                 61.425 
                 97.421 
                 34.991 
                 1.00 
                 67.95 
               
               
                 1125 
                 CA 
                 PRO 
                 A 
                 247 
                 63.285 
                 97.135 
                 33.469 
                 1.00 
                 70.71 
               
               
                 1126 
                 CB 
                 PRO 
                 A 
                 247 
                 63.047 
                 98.611 
                 33.789 
                 1.00 
                 67.96 
               
               
                 1127 
                 CG 
                 PRO 
                 A 
                 247 
                 62.398 
                 98.564 
                 35.121 
                 1.00 
                 66.76 
               
               
                 1128 
                 C 
                 PRO 
                 A 
                 247 
                 64.670 
                 96.652 
                 33.898 
                 1.00 
                 74.75 
               
               
                 1129 
                 O 
                 PRO 
                 A 
                 247 
                 65.679 
                 96.999 
                 33.277 
                 1.00 
                 76.67 
               
               
                 1130 
                 N 
                 ASP 
                 A 
                 248 
                 64.716 
                 95.833 
                 34.948 
                 1.00 
                 77.65 
               
               
                 1131 
                 CA 
                 ASP 
                 A 
                 248 
                 65.979 
                 95.309 
                 35.464 
                 1.00 
                 79.51 
               
               
                 1132 
                 CB 
                 ASP 
                 A 
                 248 
                 65.835 
                 94.974 
                 36.953 
                 1.00 
                 83.13 
               
               
                 1133 
                 CG 
                 ASP 
                 A 
                 248 
                 65.384 
                 93.526 
                 37.197 
                 1.00 
                 86.52 
               
               
                 1134 
                 OD1 
                 ASP 
                 A 
                 248 
                 64.692 
                 92.949 
                 36.325 
                 1.00 
                 88.52 
               
               
                 1135 
                 OD2 
                 ASP 
                 A 
                 248 
                 65.710 
                 92.966 
                 38.271 
                 1.00 
                 87.60 
               
               
                 1136 
                 C 
                 ASP 
                 A 
                 248 
                 66.436 
                 94.055 
                 34.718 
                 1.00 
                 79.83 
               
               
                 1137 
                 O 
                 ASP 
                 A 
                 248 
                 67.458 
                 93.466 
                 35.057 
                 1.00 
                 79.98 
               
               
                 1138 
                 N 
                 ALA 
                 A 
                 249 
                 65.683 
                 93.647 
                 33.705 
                 1.00 
                 80.13 
               
               
                 1139 
                 CA 
                 ALA 
                 A 
                 249 
                 66.023 
                 92.445 
                 32.955 
                 1.00 
                 81.61 
               
               
                 1140 
                 CB 
                 ALA 
                 A 
                 249 
                 64.879 
                 92.080 
                 32.037 
                 1.00 
                 81.13 
               
               
                 1141 
                 C 
                 ALA 
                 A 
                 249 
                 67.338 
                 92.471 
                 32.168 
                 1.00 
                 83.45 
               
               
                 1142 
                 O 
                 ALA 
                 A 
                 249 
                 67.683 
                 93.452 
                 31.497 
                 1.00 
                 83.67 
               
               
                 1143 
                 N 
                 LYS 
                 A 
                 250 
                 68.038 
                 91.345 
                 32.263 
                 1.00 
                 85.37 
               
               
                 1144 
                 CA 
                 LYS 
                 A 
                 250 
                 69.329 
                 91.074 
                 31.632 
                 1.00 
                 86.69 
               
               
                 1145 
                 CB 
                 LYS 
                 A 
                 250 
                 69.781 
                 89.672 
                 32.069 
                 1.00 
                 89.66 
               
               
                 1146 
                 CG 
                 LYS 
                 A 
                 250 
                 71.047 
                 89.105 
                 31.432 
                 1.00 
                 92.26 
               
               
                 1147 
                 CD 
                 LYS 
                 A 
                 250 
                 71.188 
                 87.630 
                 31.834 
                 1.00 
                 94.47 
               
               
                 1148 
                 CE 
                 LYS 
                 A 
                 250 
                 72.461 
                 86.972 
                 31.300 
                 1.00 
                 95.75 
               
               
                 1149 
                 NZ 
                 LYS 
                 A 
                 250 
                 72.507 
                 85.516 
                 31.655 
                 1.00 
                 95.95 
               
               
                 1150 
                 C 
                 LYS 
                 A 
                 250 
                 69.332 
                 91.163 
                 30.104 
                 1.00 
                 86.09 
               
               
                 1151 
                 O 
                 LYS 
                 A 
                 250 
                 68.820 
                 90.275 
                 29.419 
                 1.00 
                 84.97 
               
               
                 1152 
                 N 
                 GLY 
                 A 
                 251 
                 69.914 
                 92.237 
                 29.578 
                 1.00 
                 85.72 
               
               
                 1153 
                 CA 
                 GLY 
                 A 
                 251 
                 70.001 
                 92.387 
                 28.137 
                 1.00 
                 84.58 
               
               
                 1154 
                 C 
                 GLY 
                 A 
                 251 
                 68.959 
                 93.239 
                 27.440 
                 1.00 
                 83.64 
               
               
                 1155 
                 O 
                 GLY 
                 A 
                 251 
                 68.885 
                 93.227 
                 26.210 
                 1.00 
                 83.59 
               
               
                 1156 
                 N 
                 LEU 
                 A 
                 252 
                 68.146 
                 93.968 
                 28.194 
                 1.00 
                 82.40 
               
               
                 1157 
                 CA 
                 LEU 
                 A 
                 252 
                 67.148 
                 94.812 
                 27.556 
                 1.00 
                 81.56 
               
               
                 1158 
                 CB 
                 LEU 
                 A 
                 252 
                 66.201 
                 95.415 
                 28.599 
                 1.00 
                 79.55 
               
               
                 1159 
                 CG 
                 LEU 
                 A 
                 252 
                 65.150 
                 94.466 
                 29.166 
                 1.00 
                 76.78 
               
               
                 1160 
                 CD1 
                 LEU 
                 A 
                 252 
                 64.349 
                 95.187 
                 30.222 
                 1.00 
                 76.49 
               
               
                 1161 
                 CD2 
                 LEU 
                 A 
                 252 
                 64.237 
                 93.979 
                 28.048 
                 1.00 
                 76.00 
               
               
                 1162 
                 C 
                 LEU 
                 A 
                 252 
                 67.878 
                 95.917 
                 26.795 
                 1.00 
                 81.16 
               
               
                 1163 
                 O 
                 LEU 
                 A 
                 252 
                 68.650 
                 96.674 
                 27.382 
                 1.00 
                 79.97 
               
               
                 1164 
                 N 
                 SER 
                 A 
                 253 
                 67.657 
                 95.989 
                 25.487 
                 1.00 
                 81.23 
               
               
                 1165 
                 CA 
                 SER 
                 A 
                 253 
                 68.306 
                 97.012 
                 24.685 
                 1.00 
                 81.61 
               
               
                 1166 
                 CB 
                 SER 
                 A 
                 253 
                 67.995 
                 96.824 
                 23.197 
                 1.00 
                 81.75 
               
               
                 1167 
                 OG 
                 SER 
                 A 
                 253 
                 66.691 
                 96.323 
                 22.990 
                 1.00 
                 82.66 
               
               
                 1168 
                 C 
                 SER 
                 A 
                 253 
                 67.863 
                 98.383 
                 25.153 
                 1.00 
                 82.13 
               
               
                 1169 
                 O 
                 SER 
                 A 
                 253 
                 68.637 
                 99.332 
                 25.109 
                 1.00 
                 82.65 
               
               
                 1170 
                 N 
                 ASP 
                 A 
                 254 
                 66.621 
                 98.492 
                 25.614 
                 1.00 
                 83.11 
               
               
                 1171 
                 CA 
                 ASP 
                 A 
                 254 
                 66.127 
                 99.772 
                 26.110 
                 1.00 
                 82.79 
               
               
                 1172 
                 CB 
                 ASP 
                 A 
                 254 
                 65.424 
                 100.547 
                 24.991 
                 1.00 
                 82.13 
               
               
                 1173 
                 CG 
                 ASP 
                 A 
                 254 
                 64.827 
                 101.859 
                 25.479 
                 1.00 
                 82.66 
               
               
                 1174 
                 OD1 
                 ASP 
                 A 
                 254 
                 65.492 
                 102.585 
                 26.255 
                 1.00 
                 81.63 
               
               
                 1175 
                 OD2 
                 ASP 
                 A 
                 254 
                 63.688 
                 102.168 
                 25.076 
                 1.00 
                 82.97 
               
               
                 1176 
                 C 
                 ASP 
                 A 
                 254 
                 65.200 
                 99.626 
                 27.317 
                 1.00 
                 82.18 
               
               
                 1177 
                 O 
                 ASP 
                 A 
                 254 
                 63.978 
                 99.548 
                 27.179 
                 1.00 
                 82.68 
               
               
                 1178 
                 N 
                 PRO 
                 A 
                 255 
                 65.788 
                 99.578 
                 28.521 
                 1.00 
                 81.01 
               
               
                 1179 
                 CD 
                 PRO 
                 A 
                 255 
                 67.236 
                 99.400 
                 28.707 
                 1.00 
                 80.96 
               
               
                 1180 
                 CA 
                 PRO 
                 A 
                 255 
                 65.089 
                 99.444 
                 29.803 
                 1.00 
                 80.76 
               
               
                 1181 
                 CB 
                 PRO 
                 A 
                 255 
                 66.236 
                 99.331 
                 30.817 
                 1.00 
                 81.56 
               
               
                 1182 
                 CG 
                 PRO 
                 A 
                 255 
                 67.427 
                 99.910 
                 30.096 
                 1.00 
                 81.32 
               
               
                 1183 
                 C 
                 PRO 
                 A 
                 255 
                 64.097 
                 100.545 
                 30.169 
                 1.00 
                 79.69 
               
               
                 1184 
                 O 
                 PRO 
                 A 
                 255 
                 63.122 
                 100.288 
                 30.865 
                 1.00 
                 80.91 
               
               
                 1185 
                 N 
                 VAL 
                 A 
                 256 
                 64.336 
                 101.769 
                 29.711 
                 1.00 
                 78.91 
               
               
                 1186 
                 CA 
                 VAL 
                 A 
                 256 
                 63.429 
                 102.869 
                 30.030 
                 1.00 
                 77.27 
               
               
                 1187 
                 CB 
                 VAL 
                 A 
                 256 
                 63.992 
                 104.232 
                 29.550 
                 1.00 
                 78.23 
               
               
                 1188 
                 CG1 
                 VAL 
                 A 
                 256 
                 62.983 
                 105.341 
                 29.832 
                 1.00 
                 77.91 
               
               
                 1189 
                 CG2 
                 VAL 
                 A 
                 256 
                 65.308 
                 104.533 
                 30.257 
                 1.00 
                 76.94 
               
               
                 1190 
                 C 
                 VAL 
                 A 
                 256 
                 62.058 
                 102.663 
                 29.403 
                 1.00 
                 75.83 
               
               
                 1191 
                 O 
                 VAL 
                 A 
                 256 
                 61.032 
                 102.881 
                 30.044 
                 1.00 
                 75.15 
               
               
                 1192 
                 N 
                 LYS 
                 A 
                 257 
                 62.046 
                 102.243 
                 28.145 
                 1.00 
                 75.65 
               
               
                 1193 
                 CA 
                 LYS 
                 A 
                 257 
                 60.796 
                 102.002 
                 27.434 
                 1.00 
                 75.92 
               
               
                 1194 
                 CB 
                 LYS 
                 A 
                 257 
                 61.088 
                 101.424 
                 26.043 
                 1.00 
                 79.24 
               
               
                 1195 
                 CG 
                 LYS 
                 A 
                 257 
                 59.871 
                 101.320 
                 25.137 
                 1.00 
                 83.31 
               
               
                 1196 
                 CD 
                 LYS 
                 A 
                 257 
                 60.245 
                 100.876 
                 23.722 
                 1.00 
                 86.30 
               
               
                 1197 
                 CE 
                 LYS 
                 A 
                 257 
                 59.025 
                 100.944 
                 22.802 
                 1.00 
                 88.69 
               
               
                 1198 
                 NZ 
                 LYS 
                 A 
                 257 
                 59.298 
                 100.474 
                 21.417 
                 1.00 
                 89.02 
               
               
                 1199 
                 C 
                 LYS 
                 A 
                 257 
                 59.941 
                 101.024 
                 28.236 
                 1.00 
                 74.13 
               
               
                 1200 
                 O 
                 LYS 
                 A 
                 257 
                 58.718 
                 101.142 
                 28.277 
                 1.00 
                 73.74 
               
               
                 1201 
                 N 
                 ILE 
                 A 
                 258 
                 60.605 
                 100.066 
                 28.876 
                 1.00 
                 72.04 
               
               
                 1202 
                 CA 
                 ILE 
                 A 
                 258 
                 59.942 
                 99.052 
                 29.689 
                 1.00 
                 70.80 
               
               
                 1203 
                 CB 
                 ILE 
                 A 
                 258 
                 60.887 
                 97.861 
                 29.955 
                 1.00 
                 69.63 
               
               
                 1204 
                 CG2 
                 ILE 
                 A 
                 258 
                 60.220 
                 96.857 
                 30.881 
                 1.00 
                 66.22 
               
               
                 1205 
                 CG1 
                 ILE 
                 A 
                 258 
                 61.305 
                 97.221 
                 28.630 
                 1.00 
                 68.99 
               
               
                 1206 
                 CD1 
                 ILE 
                 A 
                 258 
                 60.186 
                 96.543 
                 27.878 
                 1.00 
                 68.59 
               
               
                 1207 
                 C 
                 ILE 
                 A 
                 258 
                 59.480 
                 99.608 
                 31.039 
                 1.00 
                 71.95 
               
               
                 1208 
                 O 
                 ILE 
                 A 
                 258 
                 58.402 
                 99.258 
                 31.524 
                 1.00 
                 71.82 
               
               
                 1209 
                 N 
                 LYS 
                 A 
                 259 
                 60.302 
                 100.465 
                 31.646 
                 1.00 
                 71.81 
               
               
                 1210 
                 CA 
                 LYS 
                 A 
                 259 
                 59.971 
                 101.056 
                 32.935 
                 1.00 
                 71.37 
               
               
                 1211 
                 CB 
                 LYS 
                 A 
                 259 
                 61.122 
                 101.934 
                 33.428 
                 1.00 
                 71.91 
               
               
                 1212 
                 CG 
                 LYS 
                 A 
                 259 
                 60.824 
                 102.721 
                 34.696 
                 1.00 
                 74.08 
               
               
                 1213 
                 CD 
                 LYS 
                 A 
                 259 
                 62.072 
                 103.445 
                 35.170 
                 1.00 
                 77.52 
               
               
                 1214 
                 CE 
                 LYS 
                 A 
                 259 
                 61.741 
                 104.697 
                 35.960 
                 1.00 
                 80.33 
               
               
                 1215 
                 NZ 
                 LYS 
                 A 
                 259 
                 62.972 
                 105.515 
                 36.186 
                 1.00 
                 84.19 
               
               
                 1216 
                 C 
                 LYS 
                 A 
                 259 
                 58.700 
                 101.874 
                 32.817 
                 1.00 
                 70.78 
               
               
                 1217 
                 O 
                 LYS 
                 A 
                 259 
                 57.927 
                 101.974 
                 33.764 
                 1.00 
                 72.63 
               
               
                 1218 
                 N 
                 ASN 
                 A 
                 260 
                 58.472 
                 102.446 
                 31.641 
                 1.00 
                 70.19 
               
               
                 1219 
                 CA 
                 ASN 
                 A 
                 260 
                 57.273 
                 103.244 
                 31.415 
                 1.00 
                 69.79 
               
               
                 1220 
                 CB 
                 ASN 
                 A 
                 260 
                 57.490 
                 104.188 
                 30.236 
                 1.00 
                 71.17 
               
               
                 1221 
                 CG 
                 ASN 
                 A 
                 260 
                 58.720 
                 105.052 
                 30.419 
                 1.00 
                 74.72 
               
               
                 1222 
                 OD1 
                 ASN 
                 A 
                 260 
                 58.922 
                 105.657 
                 31.479 
                 1.00 
                 74.47 
               
               
                 1223 
                 ND2 
                 ASN 
                 A 
                 260 
                 59.556 
                 105.115 
                 29.390 
                 1.00 
                 77.15 
               
               
                 1224 
                 C 
                 ASN 
                 A 
                 260 
                 56.058 
                 102.361 
                 31.172 
                 1.00 
                 68.04 
               
               
                 1225 
                 O 
                 ASN 
                 A 
                 260 
                 54.949 
                 102.676 
                 31.614 
                 1.00 
                 67.39 
               
               
                 1226 
                 N 
                 MET 
                 A 
                 261 
                 56.266 
                 101.257 
                 30.468 
                 1.00 
                 65.33 
               
               
                 1227 
                 CA 
                 MET 
                 A 
                 261 
                 55.180 
                 100.333 
                 30.209 
                 1.00 
                 64.61 
               
               
                 1228 
                 CB 
                 MET 
                 A 
                 261 
                 55.686 
                 99.163 
                 29.367 
                 1.00 
                 65.40 
               
               
                 1229 
                 CG 
                 MET 
                 A 
                 261 
                 56.114 
                 99.580 
                 27.962 
                 1.00 
                 69.44 
               
               
                 1230 
                 SD 
                 MET 
                 A 
                 261 
                 57.072 
                 98.352 
                 27.012 
                 1.00 
                 72.90 
               
               
                 1231 
                 CE 
                 MET 
                 A 
                 261 
                 55.831 
                 97.294 
                 26.447 
                 1.00 
                 69.88 
               
               
                 1232 
                 C 
                 MET 
                 A 
                 261 
                 54.674 
                 99.841 
                 31.561 
                 1.00 
                 63.57 
               
               
                 1233 
                 O 
                 MET 
                 A 
                 261 
                 53.469 
                 99.731 
                 31.793 
                 1.00 
                 63.29 
               
               
                 1234 
                 N 
                 ARG 
                 A 
                 262 
                 55.606 
                 99.566 
                 32.464 
                 1.00 
                 62.82 
               
               
                 1235 
                 CA 
                 ARG 
                 A 
                 262 
                 55.241 
                 99.089 
                 33.783 
                 1.00 
                 61.09 
               
               
                 1236 
                 CB 
                 ARG 
                 A 
                 262 
                 56.466 
                 98.585 
                 34.546 
                 1.00 
                 60.78 
               
               
                 1237 
                 CG 
                 ARG 
                 A 
                 262 
                 56.132 
                 98.203 
                 35.970 
                 1.00 
                 62.33 
               
               
                 1238 
                 CD 
                 ARG 
                 A 
                 262 
                 56.995 
                 97.086 
                 36.488 
                 1.00 
                 64.80 
               
               
                 1239 
                 NE 
                 ARG 
                 A 
                 262 
                 58.042 
                 97.559 
                 37.384 
                 1.00 
                 67.91 
               
               
                 1240 
                 CZ 
                 ARG 
                 A 
                 262 
                 58.792 
                 96.759 
                 38.139 
                 1.00 
                 71.63 
               
               
                 1241 
                 NH1 
                 ARG 
                 A 
                 262 
                 58.616 
                 95.434 
                 38.112 
                 1.00 
                 67.64 
               
               
                 1242 
                 NH2 
                 ARG 
                 A 
                 262 
                 59.721 
                 97.288 
                 38.925 
                 1.00 
                 74.13 
               
               
                 1243 
                 C 
                 ARG 
                 A 
                 262 
                 54.552 
                 100.174 
                 34.584 
                 1.00 
                 60.74 
               
               
                 1244 
                 O 
                 ARG 
                 A 
                 262 
                 53.684 
                 99.881 
                 35.402 
                 1.00 
                 61.57 
               
               
                 1245 
                 N 
                 PHE 
                 A 
                 263 
                 54.925 
                 101.428 
                 34.350 
                 1.00 
                 60.30 
               
               
                 1246 
                 CA 
                 PHE 
                 A 
                 263 
                 54.308 
                 102.523 
                 35.088 
                 1.00 
                 59.97 
               
               
                 1247 
                 CB 
                 PHE 
                 A 
                 263 
                 54.998 
                 103.853 
                 34.783 
                 1.00 
                 58.85 
               
               
                 1248 
                 CG 
                 PHE 
                 A 
                 263 
                 54.642 
                 104.952 
                 35.754 
                 1.00 
                 59.22 
               
               
                 1249 
                 CD1 
                 PHE 
                 A 
                 263 
                 55.188 
                 104.970 
                 37.039 
                 1.00 
                 59.56 
               
               
                 1250 
                 CD2 
                 PHE 
                 A 
                 263 
                 53.740 
                 105.950 
                 35.397 
                 1.00 
                 57.08 
               
               
                 1251 
                 CE1 
                 PHE 
                 A 
                 263 
                 54.838 
                 105.970 
                 37.952 
                 1.00 
                 59.73 
               
               
                 1252 
                 CE2 
                 PHE 
                 A 
                 263 
                 53.383 
                 106.952 
                 36.298 
                 1.00 
                 57.13 
               
               
                 1253 
                 CZ 
                 PHE 
                 A 
                 263 
                 53.931 
                 106.966 
                 37.576 
                 1.00 
                 59.03 
               
               
                 1254 
                 C 
                 PHE 
                 A 
                 263 
                 52.817 
                 102.631 
                 34.769 
                 1.00 
                 59.75 
               
               
                 1255 
                 O 
                 PHE 
                 A 
                 263 
                 52.004 
                 102.908 
                 35.655 
                 1.00 
                 59.30 
               
               
                 1256 
                 N 
                 GLN 
                 A 
                 264 
                 52.462 
                 102.409 
                 33.506 
                 1.00 
                 60.29 
               
               
                 1257 
                 CA 
                 GLN 
                 A 
                 264 
                 51.062 
                 102.468 
                 33.087 
                 1.00 
                 61.03 
               
               
                 1258 
                 CG 
                 GLN 
                 A 
                 264 
                 50.933 
                 102.224 
                 31.581 
                 1.00 
                 64.07 
               
               
                 1259 
                 CG 
                 GLN 
                 A 
                 264 
                 51.512 
                 103.315 
                 30.681 
                 1.00 
                 70.10 
               
               
                 1260 
                 CD 
                 GLN 
                 A 
                 264 
                 51.228 
                 103.055 
                 29.194 
                 1.00 
                 74.41 
               
               
                 1261 
                 OE1 
                 GLN 
                 A 
                 264 
                 50.095 
                 103.229 
                 28.718 
                 1.00 
                 77.09 
               
               
                 1262 
                 NE2 
                 GLN 
                 A 
                 264 
                 52.257 
                 102.624 
                 28.457 
                 1.00 
                 74.80 
               
               
                 1263 
                 C 
                 GLN 
                 A 
                 264 
                 50.234 
                 101.425 
                 33.836 
                 1.00 
                 59.01 
               
               
                 1264 
                 O 
                 GLN 
                 A 
                 264 
                 49.139 
                 101.722 
                 34.323 
                 1.00 
                 58.30 
               
               
                 1265 
                 N 
                 VAL 
                 A 
                 265 
                 50.758 
                 100.205 
                 33.920 
                 1.00 
                 56.49 
               
               
                 1266 
                 CA 
                 VAL 
                 A 
                 265 
                 50.072 
                 99.125 
                 34.619 
                 1.00 
                 55.96 
               
               
                 1267 
                 CG 
                 VAL 
                 A 
                 265 
                 50.846 
                 97.795 
                 34.478 
                 1.00 
                 55.22 
               
               
                 1268 
                 CG1 
                 VAL 
                 A 
                 265 
                 50.087 
                 96.663 
                 35.161 
                 1.00 
                 54.32 
               
               
                 1269 
                 CG2 
                 VAL 
                 A 
                 265 
                 51.068 
                 97.482 
                 33.008 
                 1.00 
                 53.47 
               
               
                 1270 
                 C 
                 VAL 
                 A 
                 265 
                 49.968 
                 99.499 
                 36.097 
                 1.00 
                 55.96 
               
               
                 1271 
                 O 
                 VAL 
                 A 
                 265 
                 48.944 
                 99.279 
                 36.751 
                 1.00 
                 53.81 
               
               
                 1272 
                 N 
                 GLN 
                 A 
                 266 
                 51.047 
                 100.080 
                 36.605 
                 1.00 
                 57.55 
               
               
                 1273 
                 CA 
                 GLN 
                 A 
                 266 
                 51.141 
                 100.528 
                 37.990 
                 1.00 
                 59.27 
               
               
                 1274 
                 CG 
                 GLN 
                 A 
                 266 
                 52.459 
                 101.251 
                 38.171 
                 1.00 
                 62.94 
               
               
                 1275 
                 CG 
                 GLN 
                 A 
                 266 
                 53.283 
                 100.820 
                 39.343 
                 1.00 
                 68.25 
               
               
                 1276 
                 CD 
                 GLN 
                 A 
                 266 
                 54.415 
                 101.793 
                 39.579 
                 1.00 
                 71.68 
               
               
                 1277 
                 OE1 
                 GLN 
                 A 
                 266 
                 54.258 
                 102.784 
                 40.310 
                 1.00 
                 72.80 
               
               
                 1278 
                 NE2 
                 GLN 
                 A 
                 266 
                 55.559 
                 101.539 
                 38.936 
                 1.00 
                 69.00 
               
               
                 1279 
                 C 
                 GLN 
                 A 
                 266 
                 50.001 
                 101.502 
                 38.305 
                 1.00 
                 59.03 
               
               
                 1280 
                 O 
                 GLN 
                 A 
                 266 
                 49.240 
                 101.319 
                 39.267 
                 1.00 
                 58.11 
               
               
                 1281 
                 N 
                 ILE 
                 A 
                 267 
                 49.920 
                 102.555 
                 37.494 
                 1.00 
                 57.81 
               
               
                 1282 
                 CA 
                 ILE 
                 A 
                 267 
                 48.884 
                 103.580 
                 37.626 
                 1.00 
                 55.82 
               
               
                 1283 
                 CG 
                 ILE 
                 A 
                 267 
                 49.075 
                 104.704 
                 36.569 
                 1.00 
                 53.53 
               
               
                 1284 
                 CG2 
                 ILE 
                 A 
                 267 
                 47.859 
                 105.604 
                 36.531 
                 1.00 
                 53.33 
               
               
                 1285 
                 CG1 
                 ILE 
                 A 
                 267 
                 50.312 
                 105.538 
                 36.906 
                 1.00 
                 53.35 
               
               
                 1286 
                 CD1 
                 ILE 
                 A 
                 267 
                 50.162 
                 106.379 
                 38.167 
                 1.00 
                 50.08 
               
               
                 1287 
                 C 
                 ILE 
                 A 
                 267 
                 47.516 
                 102.928 
                 37.435 
                 1.00 
                 55.66 
               
               
                 1288 
                 O 
                 ILE 
                 A 
                 267 
                 46.602 
                 103.132 
                 38.245 
                 1.00 
                 56.39 
               
               
                 1289 
                 N 
                 GLY 
                 A 
                 268 
                 47.387 
                 102.145 
                 36.360 
                 1.00 
                 53.70 
               
               
                 1290 
                 CA 
                 GLY 
                 A 
                 268 
                 46.145 
                 101.450 
                 36.085 
                 1.00 
                 51.40 
               
               
                 1291 
                 C 
                 GLY 
                 A 
                 268 
                 45.630 
                 100.727 
                 37.319 
                 1.00 
                 49.74 
               
               
                 1292 
                 O 
                 GLY 
                 A 
                 268 
                 44.478 
                 100.895 
                 37.711 
                 1.00 
                 49.92 
               
               
                 1293 
                 N 
                 LEU 
                 A 
                 269 
                 46.488 
                 99.933 
                 37.946 
                 1.00 
                 48.32 
               
               
                 1294 
                 CA 
                 LEU 
                 A 
                 269 
                 46.096 
                 99.188 
                 39.133 
                 1.00 
                 48.09 
               
               
                 1295 
                 CB 
                 LEU 
                 A 
                 269 
                 47.249 
                 98.302 
                 39.605 
                 1.00 
                 45.26 
               
               
                 1296 
                 CG 
                 LEU 
                 A 
                 269 
                 46.975 
                 97.534 
                 40.902 
                 1.00 
                 44.87 
               
               
                 1297 
                 CD1 
                 LEU 
                 A 
                 269 
                 45.757 
                 96.639 
                 40.733 
                 1.00 
                 45.06 
               
               
                 1298 
                 CD2 
                 LEU 
                 A 
                 269 
                 48.188 
                 96.715 
                 41.280 
                 1.00 
                 43.07 
               
               
                 1299 
                 C 
                 LEU 
                 A 
                 269 
                 45.629 
                 100.077 
                 40.288 
                 1.00 
                 49.72 
               
               
                 1300 
                 O 
                 LEU 
                 A 
                 269 
                 44.596 
                 99.815 
                 40.909 
                 1.00 
                 49.03 
               
               
                 1301 
                 N 
                 GLU 
                 A 
                 270 
                 46.383 
                 101.127 
                 40.586 
                 1.00 
                 53.23 
               
               
                 1302 
                 CA 
                 GLU 
                 A 
                 270 
                 46.005 
                 102.005 
                 41.687 
                 1.00 
                 55.47 
               
               
                 1303 
                 CB 
                 GLU 
                 A 
                 270 
                 47.109 
                 103.020 
                 41.975 
                 1.00 
                 56.29 
               
               
                 1304 
                 CG 
                 GLU 
                 A 
                 270 
                 46.764 
                 103.939 
                 43.120 
                 1.00 
                 59.90 
               
               
                 1305 
                 CD 
                 GLU 
                 A 
                 270 
                 47.932 
                 104.789 
                 43.581 
                 1.00 
                 61.37 
               
               
                 1306 
                 OE1 
                 GLU 
                 A 
                 270 
                 48.821 
                 105.088 
                 42.756 
                 1.00 
                 61.19 
               
               
                 1307 
                 OE2 
                 GLU 
                 A 
                 270 
                 47.946 
                 105.171 
                 44.774 
                 1.00 
                 64.89 
               
               
                 1308 
                 C 
                 GLU 
                 A 
                 270 
                 44.688 
                 102.713 
                 41.384 
                 1.00 
                 56.76 
               
               
                 1309 
                 O 
                 GLU 
                 A 
                 270 
                 43.803 
                 102.786 
                 42.252 
                 1.00 
                 56.84 
               
               
                 1310 
                 N 
                 ASP 
                 A 
                 271 
                 44.546 
                 103.229 
                 40.164 
                 1.00 
                 55.55 
               
               
                 1311 
                 CA 
                 ASP 
                 A 
                 271 
                 43.300 
                 103.885 
                 39.809 
                 1.00 
                 56.54 
               
               
                 1312 
                 CB 
                 ASP 
                 A 
                 271 
                 43.313 
                 104.357 
                 38.352 
                 1.00 
                 57.29 
               
               
                 1313 
                 CG 
                 ASP 
                 A 
                 271 
                 v.189 
                 105.586 
                 38.130 
                 1.00 
                 58.73 
               
               
                 1314 
                 OD1 
                 ASP 
                 A 
                 271 
                 44.418 
                 106.366 
                 39.088 
                 1.00 
                 57.46 
               
               
                 1315 
                 OD2 
                 ASP 
                 A 
                 271 
                 44.633 
                 105.778 
                 36.974 
                 1.00 
                 59.16 
               
               
                 1316 
                 C 
                 ASP 
                 A 
                 271 
                 42.151 
                 102.890 
                 40.017 
                 1.00 
                 58.03 
               
               
                 1317 
                 O 
                 ASP 
                 A 
                 271 
                 41.209 
                 103.168 
                 40.763 
                 1.00 
                 59.82 
               
               
                 1318 
                 N 
                 TYR 
                 A 
                 272 
                 42.245 
                 101.725 
                 39.377 
                 1.00 
                 57.20 
               
               
                 1319 
                 CA 
                 TYR 
                 A 
                 272 
                 41.213 
                 100.696 
                 39.482 
                 1.00 
                 55.43 
               
               
                 1320 
                 CB 
                 TYR 
                 A 
                 272 
                 41.687 
                 99.400 
                 38.784 
                 1.00 
                 53.36 
               
               
                 1321 
                 CG 
                 TYR 
                 A 
                 272 
                 40.780 
                 98.182 
                 38.971 
                 1.00 
                 51.32 
               
               
                 1322 
                 CD1 
                 TYR 
                 A 
                 272 
                 41.003 
                 97.264 
                 40.012 
                 1.00 
                 48.86 
               
               
                 1323 
                 CE1 
                 TYR 
                 A 
                 272 
                 40.155 
                 96.165 
                 40.217 
                 1.00 
                 47.73 
               
               
                 1324 
                 CD2 
                 TYR 
                 A 
                 272 
                 39.679 
                 97.968 
                 38.134 
                 1.00 
                 49.11 
               
               
                 1325 
                 CE2 
                 TYR 
                 A 
                 272 
                 38.824 
                 96.877 
                 38.327 
                 1.00 
                 48.47 
               
               
                 1326 
                 CZ 
                 TYR 
                 A 
                 272 
                 39.065 
                 95.982 
                 39.371 
                 1.00 
                 49.81 
               
               
                 1327 
                 OH 
                 TYR 
                 A 
                 272 
                 38.216 
                 94.913 
                 39.568 
                 1.00 
                 48.08 
               
               
                 1328 
                 C 
                 TYR 
                 A 
                 272 
                 40.813 
                 100.425 
                 40.933 
                 1.00 
                 57.13 
               
               
                 1329 
                 O 
                 TYR 
                 A 
                 272 
                 39.630 
                 100.323 
                 41.247 
                 1.00 
                 55.46 
               
               
                 1330 
                 N 
                 ILE 
                 A 
                 273 
                 41.796 
                 100.325 
                 41.823 
                 1.00 
                 60.05 
               
               
                 1331 
                 CA 
                 ILE 
                 A 
                 273 
                 41.501 
                 100.061 
                 43.227 
                 1.00 
                 61.62 
               
               
                 1332 
                 CB 
                 ILE 
                 A 
                 273 
                 42.785 
                 99.830 
                 44.057 
                 1.00 
                 61.50 
               
               
                 1333 
                 CG2 
                 ILE 
                 A 
                 273 
                 42.435 
                 99.656 
                 45.527 
                 1.00 
                 60.45 
               
               
                 1334 
                 CG1 
                 ILE 
                 A 
                 273 
                 43.506 
                 98.574 
                 43.574 
                 1.00 
                 62.84 
               
               
                 1335 
                 CD1 
                 ILE 
                 A 
                 273 
                 44.812 
                 98.314 
                 44.310 
                 1.00 
                 62.28 
               
               
                 1336 
                 C 
                 ILE 
                 A 
                 273 
                 40.722 
                 101.190 
                 43.882 
                 1.00 
                 62.81 
               
               
                 1337 
                 O 
                 ILE 
                 A 
                 273 
                 39.798 
                 100.937 
                 44.648 
                 1.00 
                 63.09 
               
               
                 1338 
                 N 
                 ASN 
                 A 
                 274 
                 41.078 
                 102.433 
                 43.586 
                 1.00 
                 64.16 
               
               
                 1339 
                 CA 
                 ASN 
                 A 
                 274 
                 40.380 
                 103.545 
                 44.218 
                 1.00 
                 67.47 
               
               
                 1340 
                 CB 
                 ASN 
                 A 
                 274 
                 41.128 
                 104.861 
                 43.983 
                 1.00 
                 65.58 
               
               
                 1341 
                 CG 
                 ASN 
                 A 
                 274 
                 42.460 
                 104.918 
                 44.726 
                 1.00 
                 64.81 
               
               
                 1342 
                 OD1 
                 ASN 
                 A 
                 274 
                 42.589 
                 104.407 
                 45.846 
                 1.00 
                 63.28 
               
               
                 1343 
                 ND2 
                 ASN 
                 A 
                 274 
                 43.450 
                 105.556 
                 44.113 
                 1.00 
                 63.86 
               
               
                 1344 
                 C 
                 ASN 
                 A 
                 274 
                 38.902 
                 103.701 
                 43.860 
                 1.00 
                 70.39 
               
               
                 1345 
                 O 
                 ASN 
                 A 
                 274 
                 38.155 
                 104.333 
                 44.607 
                 1.00 
                 70.27 
               
               
                 1346 
                 N 
                 ASP 
                 A 
                 275 
                 38.476 
                 103.120 
                 42.738 
                 1.00 
                 74.20 
               
               
                 1347 
                 CA 
                 ASP 
                 A 
                 275 
                 37.068 
                 103.179 
                 42.316 
                 1.00 
                 77.09 
               
               
                 1348 
                 CB 
                 ASP 
                 A 
                 275 
                 36.889 
                 102.586 
                 40.914 
                 1.00 
                 77.74 
               
               
                 1349 
                 CG 
                 ASP 
                 A 
                 275 
                 37.568 
                 103.392 
                 39.827 
                 1.00 
                 79.45 
               
               
                 1350 
                 OD1 
                 ASP 
                 A 
                 275 
                 37.578 
                 104.633 
                 39.930 
                 1.00 
                 80.80 
               
               
                 1351 
                 OD2 
                 ASP 
                 A 
                 275 
                 38.069 
                 102.787 
                 38.851 
                 1.00 
                 79.73 
               
               
                 1352 
                 C 
                 ASP 
                 A 
                 275 
                 36.207 
                 102.333 
                 43.261 
                 1.00 
                 80.11 
               
               
                 1353 
                 O 
                 ASP 
                 A 
                 275 
                 35.038 
                 102.097 
                 43.001 
                 1.00 
                 81.46 
               
               
                 1354 
                 N 
                 ARG 
                 A 
                 276 
                 36.789 
                 101.912 
                 44.371 
                 1.00 
                 83.09 
               
               
                 1355 
                 CA 
                 ARG 
                 A 
                 276 
                 36.149 
                 101.012 
                 45.321 
                 1.00 
                 86.28 
               
               
                 1356 
                 CB 
                 ARG 
                 A 
                 276 
                 37.199 
                 99.960 
                 45.606 
                 1.00 
                 86.11 
               
               
                 1357 
                 CG 
                 ARG 
                 A 
                 276 
                 36.773 
                 98.630 
                 46.075 
                 1.00 
                 85.26 
               
               
                 1358 
                 CD 
                 ARG 
                 A 
                 276 
                 38.053 
                 97.830 
                 46.220 
                 1.00 
                 82.02 
               
               
                 1359 
                 NE 
                 ARG 
                 A 
                 276 
                 38.049 
                 97.031 
                 47.431 
                 1.00 
                 80.67 
               
               
                 1360 
                 CZ 
                 ARG 
                 A 
                 276 
                 37.729 
                 95.747 
                 47.463 
                 1.00 
                 81.52 
               
               
                 1361 
                 NH1 
                 ARG 
                 A 
                 276 
                 37.398 
                 95.129 
                 46.340 
                 1.00 
                 83.68 
               
               
                 1362 
                 NH2 
                 ARG 
                 A 
                 276 
                 37.734 
                 95.081 
                 48.609 
                 1.00 
                 81.37 
               
               
                 1363 
                 C 
                 ARG 
                 A 
                 276 
                 35.637 
                 101.613 
                 46.646 
                 1.00 
                 90.21 
               
               
                 1364 
                 O 
                 ARG 
                 A 
                 276 
                 36.183 
                 102.610 
                 47.132 
                 1.00 
                 91.64 
               
               
                 1365 
                 N 
                 GLN 
                 A 
                 277 
                 34.603 
                 100.994 
                 47.229 
                 1.00 
                 93.27 
               
               
                 1366 
                 CA 
                 GLN 
                 A 
                 277 
                 34.048 
                 101.441 
                 48.521 
                 1.00 
                 94.84 
               
               
                 1367 
                 CB 
                 GLN 
                 A 
                 277 
                 32.518 
                 101.440 
                 48.513 
                 1.00 
                 95.71 
               
               
                 1368 
                 CG 
                 GLN 
                 A 
                 277 
                 31.886 
                 100.885 
                 47.262 
                 1.00 
                 95.87 
               
               
                 1369 
                 CD 
                 GLN 
                 A 
                 277 
                 30.567 
                 100.203 
                 47.557 
                 1.00 
                 95.95 
               
               
                 1370 
                 OE1 
                 GLN 
                 A 
                 277 
                 29.933 
                 99.648 
                 46.663 
                 1.00 
                 95.95 
               
               
                 1371 
                 NE2 
                 GLN 
                 A 
                 277 
                 30.150 
                 100.232 
                 48.824 
                 1.00 
                 95.95 
               
               
                 1372 
                 C 
                 GLN 
                 A 
                 277 
                 34.568 
                 100.555 
                 49.671 
                 1.00 
                 95.30 
               
               
                 1373 
                 O 
                 GLN 
                 A 
                 277 
                 33.853 
                 99.756 
                 50.284 
                 1.00 
                 94.08 
               
               
                 1374 
                 N 
                 TYR 
                 A 
                 278 
                 35.860 
                 100.755 
                 49.893 
                 1.00 
                 95.95 
               
               
                 1375 
                 CA 
                 TYR 
                 A 
                 278 
                 36.742 
                 100.143 
                 50.880 
                 1.00 
                 95.95 
               
               
                 1376 
                 CB 
                 TYR 
                 A 
                 278 
                 36.084 
                 99.872 
                 52.239 
                 1.00 
                 95.95 
               
               
                 1377 
                 CG 
                 TYR 
                 A 
                 278 
                 36.872 
                 100.634 
                 53.307 
                 1.00 
                 95.95 
               
               
                 1378 
                 CD1 
                 TYR 
                 A 
                 278 
                 36.560 
                 101.966 
                 53.613 
                 1.00 
                 95.95 
               
               
                 1379 
                 CE1 
                 TYR 
                 A 
                 278 
                 37.383 
                 102.736 
                 54.450 
                 1.00 
                 95.95 
               
               
                 1380 
                 CD2 
                 TYR 
                 A 
                 278 
                 38.037 
                 100.086 
                 53.877 
                 1.00 
                 95.95 
               
               
                 1381 
                 CE2 
                 TYR 
                 A 
                 278 
                 38.865 
                 100.850 
                 54.713 
                 1.00 
                 95.95 
               
               
                 1382 
                 CZ 
                 TYR 
                 A 
                 278 
                 38.531 
                 102.175 
                 54.990 
                 1.00 
                 95.95 
               
               
                 1383 
                 OH 
                 TYR 
                 A 
                 278 
                 39.350 
                 102.952 
                 55.783 
                 1.00 
                 95.95 
               
               
                 1384 
                 C 
                 TYR 
                 A 
                 278 
                 37.653 
                 98.997 
                 50.484 
                 1.00 
                 95.95 
               
               
                 1385 
                 O 
                 TYR 
                 A 
                 278 
                 37.482 
                 98.330 
                 49.457 
                 1.00 
                 95.95 
               
               
                 1386 
                 N 
                 ASP 
                 A 
                 279 
                 38.616 
                 98.801 
                 51.380 
                 1.00 
                 95.73 
               
               
                 1387 
                 CA 
                 ASP 
                 A 
                 279 
                 39.777 
                 97.942 
                 51.242 
                 1.00 
                 95.32 
               
               
                 1388 
                 CB 
                 ASP 
                 A 
                 279 
                 39.602 
                 96.502 
                 50.779 
                 1.00 
                 95.95 
               
               
                 1389 
                 CG 
                 ASP 
                 A 
                 279 
                 40.972 
                 95.795 
                 50.617 
                 1.00 
                 95.95 
               
               
                 1390 
                 OD1 
                 ASP 
                 A 
                 279 
                 41.982 
                 96.501 
                 50.378 
                 1.00 
                 95.95 
               
               
                 1391 
                 OD2 
                 ASP 
                 A 
                 279 
                 41.062 
                 94.560 
                 50.730 
                 1.00 
                 95.95 
               
               
                 1392 
                 C 
                 ASP 
                 A 
                 279 
                 40.318 
                 98.726 
                 50.070 
                 1.00 
                 94.82 
               
               
                 1393 
                 O 
                 ASP 
                 A 
                 279 
                 40.751 
                 98.186 
                 49.056 
                 1.00 
                 95.95 
               
               
                 1394 
                 N 
                 SER 
                 A 
                 280 
                 40.164 
                 100.026 
                 50.201 
                 1.00 
                 91.60 
               
               
                 1395 
                 CA 
                 SER 
                 A 
                 280 
                 40.665 
                 100.929 
                 49.210 
                 1.00 
                 87.92 
               
               
                 1396 
                 CB 
                 SER 
                 A 
                 280 
                 39.609 
                 101.974 
                 48.882 
                 1.00 
                 87.31 
               
               
                 1397 
                 OG 
                 SER 
                 A 
                 280 
                 39.990 
                 102.694 
                 47.730 
                 1.00 
                 87.85 
               
               
                 1398 
                 C 
                 SER 
                 A 
                 280 
                 41.799 
                 101.516 
                 50.026 
                 1.00 
                 86.39 
               
               
                 1399 
                 O 
                 SER 
                 A 
                 280 
                 42.824 
                 101.934 
                 49.493 
                 1.00 
                 87.98 
               
               
                 1400 
                 N 
                 ARG 
                 A 
                 281 
                 41.610 
                 101.492 
                 51.343 
                 1.00 
                 83.31 
               
               
                 1401 
                 CA 
                 ARG 
                 A 
                 281 
                 42.584 
                 102.015 
                 52.278 
                 1.00 
                 80.17 
               
               
                 1402 
                 CG 
                 ARG 
                 A 
                 281 
                 41.892 
                 102.434 
                 53.588 
                 1.00 
                 81.27 
               
               
                 1403 
                 CG 
                 ARG 
                 A 
                 281 
                 42.763 
                 103.216 
                 54.584 
                 1.00 
                 84.29 
               
               
                 1404 
                 CD 
                 ARG 
                 A 
                 281 
                 42.521 
                 104.729 
                 54.557 
                 1.00 
                 86.17 
               
               
                 1405 
                 NE 
                 ARG 
                 A 
                 281 
                 43.256 
                 105.407 
                 55.629 
                 1.00 
                 88.14 
               
               
                 1406 
                 CZ 
                 ARG 
                 A 
                 281 
                 43.245 
                 105.022 
                 56.905 
                 1.00 
                 89.51 
               
               
                 1407 
                 NH1 
                 ARG 
                 A 
                 281 
                 42.542 
                 103.959 
                 57.288 
                 1.00 
                 89.09 
               
               
                 1408 
                 NH2 
                 ARG 
                 A 
                 281 
                 43.941 
                 105.705 
                 57.808 
                 1.00 
                 89.59 
               
               
                 1409 
                 C 
                 ARG 
                 A 
                 281 
                 43.608 
                 100.920 
                 52.531 
                 1.00 
                 77.05 
               
               
                 1410 
                 O 
                 ARG 
                 A 
                 281 
                 43.334 
                 99.936 
                 53.224 
                 1.00 
                 77.26 
               
               
                 1411 
                 N 
                 GLY 
                 A 
                 282 
                 44.784 
                 101.084 
                 51.932 
                 1.00 
                 72.58 
               
               
                 1412 
                 CA 
                 GLY 
                 A 
                 282 
                 45.856 
                 100.134 
                 52.116 
                 1.00 
                 67.41 
               
               
                 1413 
                 C 
                 GLY 
                 A 
                 282 
                 45.928 
                 98.955 
                 51.168 
                 1.00 
                 64.88 
               
               
                 1414 
                 O 
                 GLY 
                 A 
                 282 
                 46.907 
                 98.217 
                 51.208 
                 1.00 
                 65.99 
               
               
                 1415 
                 N 
                 ARG 
                 A 
                 283 
                 44.917 
                 98.780 
                 50.321 
                 1.00 
                 60.78 
               
               
                 1416 
                 CA 
                 ARG 
                 A 
                 283 
                 44.864 
                 97.668 
                 49.374 
                 1.00 
                 55.84 
               
               
                 1417 
                 CG 
                 ARG 
                 A 
                 283 
                 43.542 
                 97.708 
                 48.605 
                 1.00 
                 54.52 
               
               
                 1418 
                 CG 
                 ARG 
                 A 
                 283 
                 43.178 
                 96.402 
                 47.906 
                 1.00 
                 51.88 
               
               
                 1419 
                 CD 
                 ARG 
                 A 
                 283 
                 41.756 
                 96.413 
                 47.337 
                 1.00 
                 49.72 
               
               
                 1420 
                 NE 
                 ARG 
                 A 
                 283 
                 41.498 
                 95.221 
                 46.541 
                 1.00 
                 48.92 
               
               
                 1421 
                 CZ 
                 ARG 
                 A 
                 283 
                 41.090 
                 94.048 
                 47.018 
                 1.00 
                 51.55 
               
               
                 1422 
                 NH1 
                 ARG 
                 A 
                 283 
                 40.859 
                 93.877 
                 48.316 
                 1.00 
                 47.52 
               
               
                 1423 
                 NH2 
                 ARG 
                 A 
                 283 
                 40.959 
                 93.016 
                 46.191 
                 1.00 
                 52.92 
               
               
                 1424 
                 C 
                 ARG 
                 A 
                 283 
                 46.028 
                 97.630 
                 48.380 
                 1.00 
                 55.27 
               
               
                 1425 
                 O 
                 ARG 
                 A 
                 283 
                 46.725 
                 96.621 
                 48.266 
                 1.00 
                 56.54 
               
               
                 1426 
                 N 
                 PHE 
                 A 
                 284 
                 46.229 
                 98.722 
                 47.653 
                 1.00 
                 53.35 
               
               
                 1427 
                 CA 
                 PHE 
                 A 
                 284 
                 47.300 
                 98.807 
                 46.663 
                 1.00 
                 52.84 
               
               
                 1428 
                 CB 
                 PHE 
                 A 
                 284 
                 47.365 
                 100.234 
                 46.131 
                 1.00 
                 50.60 
               
               
                 1429 
                 CG 
                 PHE 
                 A 
                 284 
                 48.427 
                 100.461 
                 45.099 
                 1.00 
                 50.49 
               
               
                 1430 
                 CD1 
                 PHE 
                 A 
                 284 
                 48.534 
                 99.633 
                 43.988 
                 1.00 
                 51.41 
               
               
                 1431 
                 CD2 
                 PHE 
                 A 
                 284 
                 49.271 
                 101.565 
                 45.194 
                 1.00 
                 50.80 
               
               
                 1432 
                 CE1 
                 PHE 
                 A 
                 284 
                 49.465 
                 99.904 
                 42.977 
                 1.00 
                 52.26 
               
               
                 1433 
                 CE2 
                 PHE 
                 A 
                 284 
                 50.201 
                 101.845 
                 44.198 
                 1.00 
                 51.08 
               
               
                 1434 
                 CZ 
                 PHE 
                 A 
                 284 
                 50.300 
                 101.015 
                 43.083 
                 1.00 
                 51.50 
               
               
                 1435 
                 C 
                 PHE 
                 A 
                 284 
                 48.649 
                 98.407 
                 47.253 
                 1.00 
                 54.00 
               
               
                 1436 
                 O 
                 PHE 
                 A 
                 284 
                 49.451 
                 97.724 
                 46.606 
                 1.00 
                 53.98 
               
               
                 1437 
                 N 
                 GLY 
                 A 
                 285 
                 48.886 
                 98.842 
                 48.488 
                 1.00 
                 54.59 
               
               
                 1438 
                 CA 
                 GLY 
                 A 
                 285 
                 50.127 
                 98.544 
                 49.173 
                 1.00 
                 52.37 
               
               
                 1439 
                 C 
                 GLY 
                 A 
                 285 
                 50.201 
                 97.111 
                 49.637 
                 1.00 
                 53.62 
               
               
                 1440 
                 O 
                 GLY 
                 A 
                 285 
                 51.255 
                 96.492 
                 49.508 
                 1.00 
                 53.97 
               
               
                 1441 
                 N 
                 GLU 
                 A 
                 286 
                 49.107 
                 96.579 
                 50.187 
                 1.00 
                 54.24 
               
               
                 1442 
                 CA 
                 GLU 
                 A 
                 286 
                 49.105 
                 95.195 
                 50.640 
                 1.00 
                 55.89 
               
               
                 1443 
                 CB 
                 GLU 
                 A 
                 286 
                 47.748 
                 94.801 
                 51.243 
                 1.00 
                 59.00 
               
               
                 1444 
                 CG 
                 GLU 
                 A 
                 286 
                 47.543 
                 95.261 
                 52.689 
                 1.00 
                 73.48 
               
               
                 1445 
                 CD 
                 GLU 
                 A 
                 286 
                 48.488 
                 94.578 
                 53.691 
                 1.00 
                 82.58 
               
               
                 1446 
                 OE1 
                 GLU 
                 A 
                 286 
                 49.660 
                 94.314 
                 53.333 
                 1.00 
                 87.77 
               
               
                 1447 
                 OE2 
                 GLU 
                 A 
                 286 
                 48.057 
                 94.316 
                 54.847 
                 1.00 
                 87.95 
               
               
                 1448 
                 C 
                 GLU 
                 A 
                 286 
                 49.444 
                 94.305 
                 49.449 
                 1.00 
                 54.80 
               
               
                 1449 
                 O 
                 GLU 
                 A 
                 286 
                 50.154 
                 93.317 
                 49.585 
                 1.00 
                 55.24 
               
               
                 1450 
                 N 
                 LEU 
                 A 
                 287 
                 48.957 
                 94.674 
                 48.272 
                 1.00 
                 54.63 
               
               
                 1451 
                 CA 
                 LEU 
                 A 
                 287 
                 49.220 
                 93.904 
                 47.062 
                 1.00 
                 53.07 
               
               
                 1452 
                 CG 
                 LEU 
                 A 
                 287 
                 48.328 
                 94.385 
                 45.911 
                 1.00 
                 53.27 
               
               
                 1453 
                 CG 
                 LEU 
                 A 
                 287 
                 46.847 
                 94.013 
                 45.994 
                 1.00 
                 53.62 
               
               
                 1454 
                 CD1 
                 LEU 
                 A 
                 287 
                 46.093 
                 94.548 
                 44.798 
                 1.00 
                 53.04 
               
               
                 1455 
                 CD2 
                 LEU 
                 A 
                 287 
                 46.733 
                 92.522 
                 46.044 
                 1.00 
                 52.80 
               
               
                 1456 
                 C 
                 LEU 
                 A 
                 287 
                 50.681 
                 93.963 
                 46.626 
                 1.00 
                 53.32 
               
               
                 1457 
                 O 
                 LEU 
                 A 
                 287 
                 51.277 
                 92.934 
                 46.326 
                 1.00 
                 54.68 
               
               
                 1458 
                 N 
                 LEU 
                 A 
                 288 
                 51.265 
                 95.160 
                 46.576 
                 1.00 
                 52.06 
               
               
                 1459 
                 CA 
                 LEU 
                 A 
                 288 
                 52.661 
                 95.281 
                 46.168 
                 1.00 
                 49.18 
               
               
                 1460 
                 CG 
                 LEU 
                 A 
                 288 
                 53.051 
                 96.744 
                 45.984 
                 1.00 
                 45.85 
               
               
                 1461 
                 CG 
                 LEU 
                 A 
                 288 
                 52.358 
                 97.509 
                 44.851 
                 1.00 
                 46.91 
               
               
                 1462 
                 CD1 
                 LEU 
                 A 
                 288 
                 52.994 
                 98.880 
                 44.753 
                 1.00 
                 43.72 
               
               
                 1463 
                 CD2 
                 LEU 
                 A 
                 288 
                 52.488 
                 96.772 
                 43.516 
                 1.00 
                 45.08 
               
               
                 1464 
                 C 
                 LEU 
                 A 
                 288 
                 53.617 
                 94.615 
                 47.151 
                 1.00 
                 48.19 
               
               
                 1465 
                 O 
                 LEU 
                 A 
                 288 
                 54.652 
                 94.087 
                 46.746 
                 1.00 
                 48.43 
               
               
                 1466 
                 N 
                 LEU 
                 A 
                 289 
                 53.278 
                 94.627 
                 48.435 
                 1.00 
                 46.56 
               
               
                 1467 
                 CA 
                 LEU 
                 A 
                 289 
                 54.141 
                 94.004 
                 49.430 
                 1.00 
                 47.53 
               
               
                 1468 
                 CB 
                 LEU 
                 A 
                 289 
                 53.735 
                 94.425 
                 50.842 
                 1.00 
                 47.91 
               
               
                 1469 
                 CG 
                 LEU 
                 A 
                 289 
                 54.173 
                 95.850 
                 51.191 
                 1.00 
                 48.14 
               
               
                 1470 
                 CD1 
                 LEU 
                 A 
                 289 
                 53.703 
                 96.203 
                 52.590 
                 1.00 
                 45.88 
               
               
                 1471 
                 CD2 
                 LEU 
                 A 
                 289 
                 55.686 
                 95.954 
                 51.071 
                 1.00 
                 42.68 
               
               
                 1472 
                 C 
                 LEU 
                 A 
                 289 
                 54.129 
                 92.495 
                 49.321 
                 1.00 
                 48.39 
               
               
                 1473 
                 O 
                 LEU 
                 A 
                 289 
                 54.729 
                 91.794 
                 50.136 
                 1.00 
                 49.06 
               
               
                 1474 
                 N 
                 LEU 
                 A 
                 290 
                 53.443 
                 92.005 
                 48.301 
                 1.00 
                 49.93 
               
               
                 1475 
                 CA 
                 LEU 
                 A 
                 290 
                 53.335 
                 90.573 
                 48.049 
                 1.00 
                 50.20 
               
               
                 1476 
                 CB 
                 LEU 
                 A 
                 290 
                 52.000 
                 90.286 
                 47.362 
                 1.00 
                 50.79 
               
               
                 1477 
                 CG 
                 LEU 
                 A 
                 290 
                 50.955 
                 89.327 
                 47.947 
                 1.00 
                 53.52 
               
               
                 1478 
                 CD1 
                 LEU 
                 A 
                 290 
                 50.772 
                 89.553 
                 49.436 
                 1.00 
                 49.98 
               
               
                 1479 
                 CD2 
                 LEU 
                 A 
                 290 
                 49.634 
                 89.525 
                 47.182 
                 1.00 
                 49.11 
               
               
                 1480 
                 C 
                 LEU 
                 A 
                 290 
                 54.492 
                 90.142 
                 47.144 
                 1.00 
                 48.95 
               
               
                 1481 
                 O 
                 LEU 
                 A 
                 290 
                 54.855 
                 88.975 
                 47.098 
                 1.00 
                 49.77 
               
               
                 1482 
                 N 
                 LEU 
                 A 
                 291 
                 55.084 
                 91.109 
                 46.449 
                 1.00 
                 48.49 
               
               
                 1483 
                 CA 
                 LEU 
                 A 
                 291 
                 56.172 
                 90.847 
                 45.517 
                 1.00 
                 48.02 
               
               
                 1484 
                 CB 
                 LEU 
                 A 
                 291 
                 56.376 
                 92.076 
                 44.611 
                 1.00 
                 45.04 
               
               
                 1485 
                 CG 
                 LEU 
                 A 
                 291 
                 55.123 
                 92.577 
                 43.861 
                 1.00 
                 42.75 
               
               
                 1486 
                 CD1 
                 LEU 
                 A 
                 291 
                 55.475 
                 93.803 
                 43.053 
                 1.00 
                 42.83 
               
               
                 1487 
                 CD2 
                 LEU 
                 A 
                 291 
                 54.572 
                 91.512 
                 42.937 
                 1.00 
                 41.80 
               
               
                 1488 
                 C 
                 LEU 
                 A 
                 291 
                 57.504 
                 90.402 
                 46.124 
                 1.00 
                 49.56 
               
               
                 1489 
                 O 
                 LEU 
                 A 
                 291 
                 58.227 
                 89.611 
                 45.522 
                 1.00 
                 51.70 
               
               
                 1490 
                 N 
                 PRO 
                 A 
                 292 
                 57.874 
                 90.916 
                 47.308 
                 1.00 
                 50.50 
               
               
                 1491 
                 CD 
                 PRO 
                 A 
                 292 
                 57.456 
                 92.140 
                 48.012 
                 1.00 
                 51.22 
               
               
                 1492 
                 CA 
                 PRO 
                 A 
                 292 
                 59.160 
                 90.434 
                 47.826 
                 1.00 
                 50.24 
               
               
                 1493 
                 CB 
                 PRO 
                 A 
                 292 
                 59.450 
                 91.388 
                 48.988 
                 1.00 
                 48.90 
               
               
                 1494 
                 CG 
                 PRO 
                 A 
                 292 
                 58.786 
                 92.659 
                 48.549 
                 1.00 
                 49.56 
               
               
                 1495 
                 C 
                 PRO 
                 A 
                 292 
                 59.023 
                 88.984 
                 48.282 
                 1.00 
                 50.05 
               
               
                 1496 
                 O 
                 PRO 
                 A 
                 292 
                 59.977 
                 88.208 
                 48.253 
                 1.00 
                 52.57 
               
               
                 1497 
                 N 
                 THR 
                 A 
                 293 
                 57.820 
                 88.636 
                 48.710 
                 1.00 
                 48.75 
               
               
                 1498 
                 CA 
                 THR 
                 A 
                 293 
                 57.508 
                 87.289 
                 49.159 
                 1.00 
                 49.98 
               
               
                 1499 
                 CB 
                 THR 
                 A 
                 293 
                 56.091 
                 87.240 
                 49.777 
                 1.00 
                 49.37 
               
               
                 1500 
                 OG1 
                 THR 
                 A 
                 293 
                 56.059 
                 88.045 
                 50.959 
                 1.00 
                 49.17 
               
               
                 1501 
                 CG2 
                 THR 
                 A 
                 293 
                 55.716 
                 85.829 
                 50.136 
                 1.00 
                 50.42 
               
               
                 1502 
                 C 
                 THR 
                 A 
                 293 
                 57.557 
                 86.342 
                 47.958 
                 1.00 
                 50.49 
               
               
                 1503 
                 O 
                 THR 
                 A 
                 293 
                 58.160 
                 85.268 
                 48.012 
                 1.00 
                 50.26 
               
               
                 1504 
                 N 
                 LEU 
                 A 
                 294 
                 56.904 
                 86.754 
                 46.880 
                 1.00 
                 50.54 
               
               
                 1505 
                 CA 
                 LEU 
                 A 
                 294 
                 56.858 
                 85.980 
                 45.653 
                 1.00 
                 50.07 
               
               
                 1506 
                 CB 
                 LEU 
                 A 
                 294 
                 56.065 
                 86.760 
                 44.588 
                 1.00 
                 50.37 
               
               
                 1507 
                 CG 
                 LEU 
                 A 
                 294 
                 55.887 
                 86.255 
                 43.147 
                 1.00 
                 50.02 
               
               
                 1508 
                 CD1 
                 LEU 
                 A 
                 294 
                 55.294 
                 84.862 
                 43.141 
                 1.00 
                 49.21 
               
               
                 1509 
                 CD2 
                 LEU 
                 A 
                 294 
                 54.967 
                 87.204 
                 42.393 
                 1.00 
                 50.16 
               
               
                 1510 
                 C 
                 LEU 
                 A 
                 294 
                 58.281 
                 85.716 
                 45.177 
                 1.00 
                 50.36 
               
               
                 1511 
                 O 
                 LEU 
                 A 
                 294 
                 58.593 
                 84.627 
                 44.711 
                 1.00 
                 51.04 
               
               
                 1512 
                 N 
                 GLN 
                 A 
                 295 
                 59.144 
                 86.719 
                 45.315 
                 1.00 
                 51.63 
               
               
                 1513 
                 CA 
                 GLN 
                 A 
                 295 
                 60.540 
                 86.623 
                 44.882 
                 1.00 
                 53.37 
               
               
                 1514 
                 CB 
                 GLN 
                 A 
                 295 
                 61.218 
                 87.983 
                 45.041 
                 1.00 
                 54.61 
               
               
                 1515 
                 CG 
                 GLN 
                 A 
                 295 
                 62.405 
                 88.225 
                 44.137 
                 1.00 
                 59.44 
               
               
                 1516 
                 CD 
                 GLN 
                 A 
                 295 
                 63.079 
                 89.575 
                 44.404 
                 1.00 
                 63.10 
               
               
                 1517 
                 OE1 
                 GLN 
                 A 
                 295 
                 63.698 
                 90.162 
                 43.514 
                 1.00 
                 66.10 
               
               
                 1518 
                 NE2 
                 GLN 
                 A 
                 295 
                 62.971 
                 90.061 
                 45.637 
                 1.00 
                 63.79 
               
               
                 1519 
                 C 
                 GLN 
                 A 
                 295 
                 61.266 
                 85.585 
                 45.723 
                 1.00 
                 53.60 
               
               
                 1520 
                 O 
                 GLN 
                 A 
                 295 
                 61.934 
                 84.699 
                 45.197 
                 1.00 
                 53.68 
               
               
                 1521 
                 N 
                 SER 
                 A 
                 296 
                 61.116 
                 85.706 
                 47.036 
                 1.00 
                 53.49 
               
               
                 1522 
                 CA 
                 SER 
                 A 
                 296 
                 61.740 
                 84.795 
                 47.981 
                 1.00 
                 52.16 
               
               
                 1523 
                 CB 
                 SER 
                 A 
                 296 
                 61.284 
                 85.146 
                 49.398 
                 1.00 
                 52.03 
               
               
                 1524 
                 OG 
                 SER 
                 A 
                 296 
                 61.652 
                 84.137 
                 50.317 
                 1.00 
                 53.93 
               
               
                 1525 
                 C 
                 SER 
                 A 
                 296 
                 61.411 
                 83.333 
                 47.666 
                 1.00 
                 51.43 
               
               
                 1526 
                 O 
                 SER 
                 A 
                 296 
                 62.308 
                 82.511 
                 47.490 
                 1.00 
                 49.71 
               
               
                 1527 
                 N 
                 ILE 
                 A 
                 297 
                 60.128 
                 83.003 
                 47.588 
                 1.00 
                 50.05 
               
               
                 1528 
                 CA 
                 ILE 
                 A 
                 297 
                 59.748 
                 81.628 
                 47.305 
                 1.00 
                 49.62 
               
               
                 1529 
                 CB 
                 ILE 
                 A 
                 297 
                 58.226 
                 81.434 
                 47.398 
                 1.00 
                 45.90 
               
               
                 1530 
                 CG2 
                 ILE 
                 A 
                 297 
                 57.895 
                 79.967 
                 47.361 
                 1.00 
                 44.96 
               
               
                 1531 
                 CG1 
                 ILE 
                 A 
                 297 
                 57.710 
                 81.997 
                 48.720 
                 1.00 
                 44.15 
               
               
                 1532 
                 CD1 
                 ILE 
                 A 
                 297 
                 56.204 
                 82.079 
                 48.800 
                 1.00 
                 42.04 
               
               
                 1533 
                 C 
                 ILE 
                 A 
                 297 
                 60.233 
                 81.165 
                 45.931 
                 1.00 
                 51.40 
               
               
                 1534 
                 O 
                 ILE 
                 A 
                 297 
                 60.556 
                 79.996 
                 45.755 
                 1.00 
                 52.67 
               
               
                 1535 
                 N 
                 THR 
                 A 
                 298 
                 60.302 
                 82.076 
                 44.967 
                 1.00 
                 53.15 
               
               
                 1536 
                 CA 
                 THR 
                 A 
                 298 
                 60.749 
                 81.721 
                 43.615 
                 1.00 
                 54.69 
               
               
                 1537 
                 CB 
                 THR 
                 A 
                 298 
                 60.502 
                 82.879 
                 42.601 
                 1.00 
                 52.86 
               
               
                 1538 
                 OG1 
                 THR 
                 A 
                 298 
                 59.101 
                 83.164 
                 42.524 
                 1.00 
                 50.37 
               
               
                 1539 
                 CG2 
                 THR 
                 A 
                 298 
                 61.007 
                 82.499 
                 41.223 
                 1.00 
                 48.43 
               
               
                 1540 
                 C 
                 THR 
                 A 
                 298 
                 62.234 
                 81.355 
                 43.589 
                 1.00 
                 56.55 
               
               
                 1541 
                 O 
                 THR 
                 A 
                 298 
                 62.640 
                 80.417 
                 42.901 
                 1.00 
                 57.43 
               
               
                 1542 
                 N 
                 TRP 
                 A 
                 299 
                 63.047 
                 82.101 
                 44.327 
                 1.00 
                 59.09 
               
               
                 1543 
                 CA 
                 TRP 
                 A 
                 299 
                 64.475 
                 81.818 
                 44.376 
                 1.00 
                 62.16 
               
               
                 1544 
                 CB 
                 TRP 
                 A 
                 299 
                 65.216 
                 82.913 
                 45.151 
                 1.00 
                 67.64 
               
               
                 1545 
                 CG 
                 TRP 
                 A 
                 299 
                 65.532 
                 84.128 
                 44.315 
                 1.00 
                 76.18 
               
               
                 1546 
                 CD2 
                 TRP 
                 A 
                 299 
                 66.778 
                 84.841 
                 44.261 
                 1.00 
                 81.84 
               
               
                 1547 
                 CE2 
                 TRP 
                 A 
                 299 
                 66.622 
                 85.888 
                 43.320 
                 1.00 
                 82.99 
               
               
                 1548 
                 CE3 
                 TRP 
                 A 
                 299 
                 68.027 
                 84.672 
                 44.891 
                 1.00 
                 84.69 
               
               
                 1549 
                 CD1 
                 TRP 
                 A 
                 299 
                 64.689 
                 84.771 
                 43.450 
                 1.00 
                 77.11 
               
               
                 1550 
                 NE1 
                 TRP 
                 A 
                 299 
                 65.335 
                 85.828 
                 42.851 
                 1.00 
                 80.02 
               
               
                 1551 
                 CZ2 
                 TRP 
                 A 
                 299 
                 67.659 
                 86.798 
                 43.017 
                 1.00 
                 85.95 
               
               
                 1552 
                 CZ3 
                 TRP 
                 A 
                 299 
                 69.064 
                 85.579 
                 44.589 
                 1.00 
                 86.00 
               
               
                 1553 
                 CH2 
                 TRP 
                 A 
                 299 
                 68.874 
                 86.618 
                 43.648 
                 1.00 
                 85.57 
               
               
                 1554 
                 C 
                 TRP 
                 A 
                 299 
                 64.700 
                 80.462 
                 45.031 
                 1.00 
                 61.65 
               
               
                 1555 
                 O 
                 TRP 
                 A 
                 299 
                 65.591 
                 79.714 
                 44.629 
                 1.00 
                 63.42 
               
               
                 1556 
                 N 
                 GLN 
                 A 
                 300 
                 63.884 
                 80.138 
                 46.028 
                 1.00 
                 59.32 
               
               
                 1557 
                 CA 
                 GLN 
                 A 
                 300 
                 64.001 
                 78.861 
                 46.718 
                 1.00 
                 58.51 
               
               
                 1558 
                 CG 
                 GLN 
                 A 
                 300 
                 63.068 
                 78.828 
                 47.926 
                 1.00 
                 56.83 
               
               
                 1559 
                 CG 
                 GLN 
                 A 
                 300 
                 63.482 
                 77.805 
                 48.962 
                 1.00 
                 57.88 
               
               
                 1560 
                 CD 
                 GLN 
                 A 
                 300 
                 62.511 
                 77.692 
                 50.122 
                 1.00 
                 59.40 
               
               
                 1561 
                 OE1 
                 GLN 
                 A 
                 300 
                 62.034 
                 78.697 
                 50.646 
                 1.00 
                 58.26 
               
               
                 1562 
                 NE2 
                 GLN 
                 A 
                 300 
                 62.224 
                 76.459 
                 50.539 
                 1.00 
                 59.18 
               
               
                 1563 
                 C 
                 GLN 
                 A 
                 300 
                 63.665 
                 77.701 
                 45.766 
                 1.00 
                 59.30 
               
               
                 1564 
                 O 
                 GLN 
                 A 
                 300 
                 64.366 
                 76.691 
                 45.727 
                 1.00 
                 60.14 
               
               
                 1565 
                 N 
                 MET 
                 A 
                 301 
                 62.591 
                 77.863 
                 44.999 
                 1.00 
                 58.87 
               
               
                 1566 
                 CA 
                 MET 
                 A 
                 301 
                 62.158 
                 76.860 
                 44.039 
                 1.00 
                 57.31 
               
               
                 1567 
                 CB 
                 MET 
                 A 
                 301 
                 60.825 
                 77.287 
                 43.413 
                 1.00 
                 58.61 
               
               
                 1568 
                 CG 
                 MET 
                 A 
                 301 
                 60.389 
                 76.450 
                 42.204 
                 1.00 
                 59.91 
               
               
                 1569 
                 SD 
                 MET 
                 A 
                 301 
                 58.776 
                 76.899 
                 41.540 
                 1.00 
                 59.27 
               
               
                 1570 
                 CE 
                 MET 
                 A 
                 301 
                 59.226 
                 78.115 
                 40.338 
                 1.00 
                 56.06 
               
               
                 1571 
                 C 
                 MET 
                 A 
                 301 
                 63.197 
                 76.641 
                 42.942 
                 1.00 
                 57.88 
               
               
                 1572 
                 O 
                 MET 
                 A 
                 301 
                 63.482 
                 75.505 
                 42.572 
                 1.00 
                 57.16 
               
               
                 1573 
                 N 
                 ILE 
                 A 
                 302 
                 63.754 
                 77.726 
                 42.408 
                 1.00 
                 58.60 
               
               
                 1574 
                 CA 
                 ILE 
                 A 
                 302 
                 64.751 
                 77.605 
                 41.349 
                 1.00 
                 60.24 
               
               
                 1575 
                 CG 
                 ILE 
                 A 
                 302 
                 65.049 
                 78.969 
                 40.690 
                 1.00 
                 59.46 
               
               
                 1576 
                 CG2 
                 ILE 
                 A 
                 302 
                 66.269 
                 78.864 
                 39.791 
                 1.00 
                 58.10 
               
               
                 1577 
                 CG1 
                 ILE 
                 A 
                 302 
                 63.840 
                 79.414 
                 39.868 
                 1.00 
                 60.85 
               
               
                 1578 
                 CD1 
                 ILE 
                 A 
                 302 
                 64.092 
                 80.665 
                 39.058 
                 1.00 
                 63.07 
               
               
                 1579 
                 C 
                 ILE 
                 A 
                 302 
                 66.050 
                 76.995 
                 41.853 
                 1.00 
                 61.33 
               
               
                 1580 
                 O 
                 ILE 
                 A 
                 302 
                 66.632 
                 76.145 
                 41.191 
                 1.00 
                 62.22 
               
               
                 1581 
                 N 
                 GLU 
                 A 
                 303 
                 66.509 
                 77.440 
                 43.016 
                 1.00 
                 63.68 
               
               
                 1582 
                 CA 
                 GLU 
                 A 
                 303 
                 67.727 
                 76.903 
                 43.595 
                 1.00 
                 66.07 
               
               
                 1583 
                 CB 
                 GLU 
                 A 
                 303 
                 67.994 
                 77.538 
                 44.956 
                 1.00 
                 70.83 
               
               
                 1584 
                 CG 
                 GLU 
                 A 
                 303 
                 68.698 
                 78.887 
                 44.896 
                 1.00 
                 77.80 
               
               
                 1585 
                 CD 
                 GLU 
                 A 
                 303 
                 68.865 
                 79.503 
                 46.276 
                 1.00 
                 82.92 
               
               
                 1586 
                 OE1 
                 GLU 
                 A 
                 303 
                 68.894 
                 78.730 
                 47.260 
                 1.00 
                 86.16 
               
               
                 1587 
                 OE2 
                 GLU 
                 A 
                 303 
                 68.975 
                 80.749 
                 46.379 
                 1.00 
                 86.20 
               
               
                 1588 
                 C 
                 GLU 
                 A 
                 303 
                 67.516 
                 75.414 
                 43.762 
                 1.00 
                 66.02 
               
               
                 1589 
                 O 
                 GLU 
                 A 
                 303 
                 68.409 
                 74.613 
                 43.493 
                 1.00 
                 66.48 
               
               
                 1590 
                 N 
                 GLN 
                 A 
                 304 
                 66.318 
                 75.046 
                 44.199 
                 1.00 
                 65.78 
               
               
                 1591 
                 CA 
                 GLN 
                 A 
                 304 
                 65.975 
                 73.645 
                 44.390 
                 1.00 
                 66.11 
               
               
                 1592 
                 CB 
                 GLN 
                 A 
                 304 
                 64.619 
                 73.529 
                 45.076 
                 1.00 
                 64.66 
               
               
                 1593 
                 CG 
                 GLN 
                 A 
                 304 
                 64.242 
                 72.117 
                 45.419 
                 1.00 
                 66.16 
               
               
                 1594 
                 CD 
                 GLN 
                 A 
                 304 
                 63.078 
                 72.066 
                 46.362 
                 1.00 
                 67.71 
               
               
                 1595 
                 OE1 
                 GLN 
                 A 
                 304 
                 62.889 
                 72.975 
                 47.169 
                 1.00 
                 69.18 
               
               
                 1596 
                 NE2 
                 GLN 
                 A 
                 304 
                 62.295 
                 70.996 
                 46.286 
                 1.00 
                 68.50 
               
               
                 1597 
                 C 
                 GLN 
                 A 
                 304 
                 65.963 
                 72.884 
                 43.058 
                 1.00 
                 66.79 
               
               
                 1598 
                 O 
                 GLN 
                 A 
                 304 
                 66.448 
                 71.766 
                 42.973 
                 1.00 
                 68.04 
               
               
                 1599 
                 N 
                 ILE 
                 A 
                 305 
                 65.402 
                 73.481 
                 42.017 
                 1.00 
                 67.53 
               
               
                 1600 
                 CA 
                 ILE 
                 A 
                 305 
                 65.389 
                 72.832 
                 40.716 
                 1.00 
                 68.72 
               
               
                 1601 
                 CB 
                 ILE 
                 A 
                 305 
                 64.563 
                 73.652 
                 39.692 
                 1.00 
                 68.43 
               
               
                 1602 
                 CG2 
                 ILE 
                 A 
                 305 
                 64.756 
                 73.104 
                 38.290 
                 1.00 
                 67.26 
               
               
                 1603 
                 CG1 
                 ILE 
                 A 
                 305 
                 63.084 
                 73.613 
                 40.070 
                 1.00 
                 67.67 
               
               
                 1604 
                 CD1 
                 ILE 
                 A 
                 305 
                 62.201 
                 74.462 
                 39.183 
                 1.00 
                 66.18 
               
               
                 1605 
                 C 
                 ILE 
                 A 
                 305 
                 66.838 
                 72.736 
                 40.227 
                 1.00 
                 70.29 
               
               
                 1606 
                 O 
                 ILE 
                 A 
                 305 
                 67.240 
                 71.762 
                 39.602 
                 1.00 
                 68.88 
               
               
                 1607 
                 N 
                 GLN 
                 A 
                 306 
                 67.628 
                 73.754 
                 40.533 
                 1.00 
                 73.16 
               
               
                 1608 
                 CA 
                 GLN 
                 A 
                 306 
                 69.010 
                 73.768 
                 40.099 
                 1.00 
                 77.84 
               
               
                 1609 
                 CB 
                 GLN 
                 A 
                 306 
                 69.626 
                 75.150 
                 40.346 
                 1.00 
                 79.91 
               
               
                 1610 
                 CG 
                 GLN 
                 A 
                 306 
                 70.999 
                 75.385 
                 39.704 
                 1.00 
                 85.69 
               
               
                 1611 
                 CD 
                 GLN 
                 A 
                 306 
                 71.185 
                 74.731 
                 38.320 
                 1.00 
                 90.51 
               
               
                 1612 
                 OE1 
                 GLN 
                 A 
                 306 
                 71.815 
                 75.310 
                 37.431 
                 1.00 
                 91.97 
               
               
                 1613 
                 NE2 
                 GLN 
                 A 
                 306 
                 70.668 
                 73.514 
                 38.147 
                 1.00 
                 92.14 
               
               
                 1614 
                 C 
                 GLN 
                 A 
                 306 
                 69.844 
                 72.681 
                 40.761 
                 1.00 
                 79.80 
               
               
                 1615 
                 O 
                 GLN 
                 A 
                 306 
                 70.781 
                 72.150 
                 40.168 
                 1.00 
                 80.34 
               
               
                 1616 
                 N 
                 PHE 
                 A 
                 307 
                 69.506 
                 72.333 
                 41.991 
                 1.00 
                 81.72 
               
               
                 1617 
                 CA 
                 PHE 
                 A 
                 307 
                 70.260 
                 71.299 
                 42.659 
                 1.00 
                 83.32 
               
               
                 1618 
                 CB 
                 PHE 
                 A 
                 307 
                 70.065 
                 71.414 
                 44.175 
                 1.00 
                 87.37 
               
               
                 1619 
                 CG 
                 PHE 
                 A 
                 307 
                 69.411 
                 70.232 
                 44.765 
                 1.00 
                 92.13 
               
               
                 1620 
                 CD1 
                 PHE 
                 A 
                 307 
                 70.160 
                 69.108 
                 45.078 
                 1.00 
                 94.03 
               
               
                 1621 
                 CD2 
                 PHE 
                 A 
                 307 
                 68.024 
                 70.161 
                 44.823 
                 1.00 
                 94.32 
               
               
                 1622 
                 CE1 
                 PHE 
                 A 
                 307 
                 69.542 
                 67.932 
                 45.415 
                 1.00 
                 95.95 
               
               
                 1623 
                 CE2 
                 PHE 
                 A 
                 307 
                 67.390 
                 68.988 
                 45.157 
                 1.00 
                 95.95 
               
               
                 1624 
                 CZ 
                 PHE 
                 A 
                 307 
                 68.145 
                 67.863 
                 45.452 
                 1.00 
                 95.95 
               
               
                 1625 
                 C 
                 PHE 
                 A 
                 307 
                 69.773 
                 69.940 
                 42.124 
                 1.00 
                 83.33 
               
               
                 1626 
                 O 
                 PHE 
                 A 
                 307 
                 70.576 
                 69.128 
                 41.669 
                 1.00 
                 83.75 
               
               
                 1627 
                 N 
                 VAL 
                 A 
                 308 
                 68.461 
                 69.711 
                 42.153 
                 1.00 
                 83.05 
               
               
                 1628 
                 CA 
                 VAL 
                 A 
                 308 
                 67.874 
                 68.454 
                 41.686 
                 1.00 
                 83.61 
               
               
                 1629 
                 CB 
                 VAL 
                 A 
                 308 
                 66.317 
                 68.526 
                 41.663 
                 1.00 
                 83.31 
               
               
                 1630 
                 CG1 
                 VAL 
                 A 
                 308 
                 65.766 
                 67.751 
                 40.492 
                 1.00 
                 85.10 
               
               
                 1631 
                 CG2 
                 VAL 
                 A 
                 308 
                 65.747 
                 67.935 
                 42.934 
                 1.00 
                 81.91 
               
               
                 1632 
                 C 
                 VAL 
                 A 
                 308 
                 68.373 
                 68.077 
                 40.300 
                 1.00 
                 84.94 
               
               
                 1633 
                 O 
                 VAL 
                 A 
                 308 
                 68.405 
                 66.900 
                 39.942 
                 1.00 
                 85.00 
               
               
                 1634 
                 N 
                 LYS 
                 A 
                 309 
                 68.764 
                 69.074 
                 39.517 
                 1.00 
                 86.39 
               
               
                 1635 
                 CA 
                 LYS 
                 A 
                 309 
                 69.260 
                 68.804 
                 38.178 
                 1.00 
                 88.28 
               
               
                 1636 
                 CB 
                 LYS 
                 A 
                 309 
                 69.170 
                 70.042 
                 37.293 
                 1.00 
                 87.33 
               
               
                 1637 
                 CG 
                 LYS 
                 A 
                 309 
                 69.751 
                 69.807 
                 35.918 
                 1.00 
                 85.44 
               
               
                 1638 
                 CD 
                 LYS 
                 A 
                 309 
                 69.948 
                 71.095 
                 35.174 
                 1.00 
                 85.63 
               
               
                 1639 
                 CE 
                 LYS 
                 A 
                 309 
                 70.436 
                 70.826 
                 33.765 
                 1.00 
                 87.76 
               
               
                 1640 
                 NZ 
                 LYS 
                 A 
                 309 
                 70.538 
                 72.085 
                 32.963 
                 1.00 
                 90.34 
               
               
                 1641 
                 C 
                 LYS 
                 A 
                 309 
                 70.705 
                 68.327 
                 38.182 
                 1.00 
                 90.63 
               
               
                 1642 
                 O 
                 LYS 
                 A 
                 309 
                 71.014 
                 67.288 
                 37.593 
                 1.00 
                 92.50 
               
               
                 1643 
                 N 
                 LEU 
                 A 
                 3iW 
                 71.587 
                 69.085 
                 38.833 
                 1.00 
                 91.71 
               
               
                 1644 
                 CA 
                 LEU 
                 A 
                 310 
                 72.998 
                 68.725 
                 38.877 
                 1.00 
                 92.34 
               
               
                 1645 
                 CB 
                 LEU 
                 A 
                 310 
                 73.850 
                 69.920 
                 39.299 
                 1.00 
                 93.54 
               
               
                 1646 
                 CG 
                 LEU 
                 A 
                 310 
                 74.249 
                 70.728 
                 38.056 
                 1.00 
                 95.95 
               
               
                 1647 
                 CD1 
                 LEU 
                 A 
                 310 
                 75.178 
                 71.870 
                 38.440 
                 1.00 
                 95.95 
               
               
                 1648 
                 CD2 
                 LEU 
                 A 
                 310 
                 74.941 
                 69.794 
                 37.042 
                 1.00 
                 95.95 
               
               
                 1649 
                 C 
                 LEU 
                 A 
                 310 
                 73.338 
                 67.509 
                 39.720 
                 1.00 
                 92.16 
               
               
                 1650 
                 O 
                 LEU 
                 A 
                 310 
                 74.417 
                 66.941 
                 39.576 
                 1.00 
                 91.31 
               
               
                 1651 
                 N 
                 PHE 
                 A 
                 311 
                 72.426 
                 67.109 
                 40.597 
                 1.00 
                 92.42 
               
               
                 1652 
                 CA 
                 PHE 
                 A 
                 311 
                 72.649 
                 65.913 
                 41.398 
                 1.00 
                 92.90 
               
               
                 1653 
                 CB 
                 PHE 
                 A 
                 311 
                 72.229 
                 66.141 
                 42.851 
                 1.00 
                 91.58 
               
               
                 1654 
                 CG 
                 PHE 
                 A 
                 311 
                 73.263 
                 66.877 
                 43.652 
                 1.00 
                 92.43 
               
               
                 1655 
                 CD1 
                 PHE 
                 A 
                 311 
                 73.737 
                 68.114 
                 43.220 
                 1.00 
                 93.18 
               
               
                 1656 
                 CD2 
                 PHE 
                 A 
                 311 
                 73.808 
                 66.319 
                 44.801 
                 1.00 
                 92.88 
               
               
                 1657 
                 CE1 
                 PHE 
                 A 
                 311 
                 74.743 
                 68.783 
                 43.920 
                 1.00 
                 93.14 
               
               
                 1658 
                 CE2 
                 PHE 
                 A 
                 311 
                 74.818 
                 66.982 
                 45.510 
                 1.00 
                 93.31 
               
               
                 1659 
                 CZ 
                 PHE 
                 A 
                 311 
                 75.286 
                 68.215 
                 45.066 
                 1.00 
                 92.91 
               
               
                 1660 
                 C 
                 PHE 
                 A 
                 311 
                 71.869 
                 64.774 
                 40.750 
                 1.00 
                 93.93 
               
               
                 1661 
                 O 
                 PHE 
                 A 
                 311 
                 71.419 
                 63.837 
                 41.414 
                 1.00 
                 94.85 
               
               
                 1662 
                 N 
                 GLY 
                 A 
                 312 
                 71.727 
                 64.897 
                 39.428 
                 1.00 
                 94.22 
               
               
                 1663 
                 CA 
                 GLY 
                 A 
                 312 
                 71.044 
                 63.919 
                 38.600 
                 1.00 
                 93.73 
               
               
                 1664 
                 C 
                 GLY 
                 A 
                 312 
                 69.678 
                 63.410 
                 39.011 
                 1.00 
                 94.03 
               
               
                 1665 
                 O 
                 GLY 
                 A 
                 312 
                 69.062 
                 62.664 
                 38.253 
                 1.00 
                 94.80 
               
               
                 1666 
                 N 
                 MET 
                 A 
                 313 
                 69.200 
                 63.800 
                 40.191 
                 1.00 
                 94.19 
               
               
                 1667 
                 CA 
                 MET 
                 A 
                 313 
                 67.898 
                 63.346 
                 40.679 
                 1.00 
                 94.78 
               
               
                 1668 
                 CB 
                 MET 
                 A 
                 313 
                 67.451 
                 64.214 
                 41.856 
                 1.00 
                 94.23 
               
               
                 1669 
                 CG 
                 MET 
                 A 
                 313 
                 67.888 
                 63.660 
                 43.194 
                 1.00 
                 95.95 
               
               
                 1670 
                 SD 
                 MET 
                 A 
                 313 
                 67.866 
                 64.835 
                 44.561 
                 1.00 
                 95.95 
               
               
                 1671 
                 CE 
                 MET 
                 A 
                 313 
                 69.656 
                 64.990 
                 44.848 
                 1.00 
                 95.71 
               
               
                 1672 
                 C 
                 MET 
                 A 
                 313 
                 66.792 
                 63.304 
                 39.626 
                 1.00 
                 95.63 
               
               
                 1673 
                 O 
                 MET 
                 A 
                 313 
                 66.192 
                 62.251 
                 39.389 
                 1.00 
                 95.95 
               
               
                 1674 
                 N 
                 VAL 
                 A 
                 314 
                 66.524 
                 64.444 
                 38.993 
                 1.00 
                 94.89 
               
               
                 1675 
                 CA 
                 VAL 
                 A 
                 314 
                 65.482 
                 64.517 
                 37.976 
                 1.00 
                 93.46 
               
               
                 1676 
                 CB 
                 VAL 
                 A 
                 314 
                 64.325 
                 65.435 
                 38.441 
                 1.00 
                 93.61 
               
               
                 1677 
                 CG1 
                 VAL 
                 A 
                 314 
                 63.173 
                 65.379 
                 37.441 
                 1.00 
                 93.50 
               
               
                 1678 
                 CG2 
                 VAL 
                 A 
                 314 
                 63.863 
                 65.026 
                 39.838 
                 1.00 
                 91.98 
               
               
                 1679 
                 C 
                 VAL 
                 A 
                 314 
                 66.012 
                 65.044 
                 36.643 
                 1.00 
                 92.87 
               
               
                 1680 
                 O 
                 VAL 
                 A 
                 314 
                 67.050 
                 65.708 
                 36.590 
                 1.00 
                 91.94 
               
               
                 1681 
                 N 
                 ALA 
                 A 
                 315 
                 65.298 
                 64.725 
                 35.566 
                 1.00 
                 92.16 
               
               
                 1682 
                 CA 
                 ALA 
                 A 
                 315 
                 65.664 
                 65.185 
                 34.231 
                 1.00 
                 91.57 
               
               
                 1683 
                 CB 
                 ALA 
                 A 
                 315 
                 65.191 
                 64.187 
                 33.174 
                 1.00 
                 90.93 
               
               
                 1684 
                 C 
                 ALA 
                 A 
                 315 
                 64.936 
                 66.511 
                 34.068 
                 1.00 
                 91.09 
               
               
                 1685 
                 O 
                 ALA 
                 A 
                 315 
                 63.792 
                 66.643 
                 34.508 
                 1.00 
                 91.28 
               
               
                 1686 
                 N 
                 ILE 
                 A 
                 316 
                 65.576 
                 67.496 
                 33.449 
                 1.00 
                 89.78 
               
               
                 1687 
                 CA 
                 ILE 
                 A 
                 316 
                 64.913 
                 68.777 
                 33.301 
                 1.00 
                 88.77 
               
               
                 1688 
                 CB 
                 ILE 
                 A 
                 316 
                 65.621 
                 69.837 
                 34.156 
                 1.00 
                 88.28 
               
               
                 1689 
                 CG2 
                 ILE 
                 A 
                 316 
                 65.300 
                 71.241 
                 33.673 
                 1.00 
                 88.35 
               
               
                 1690 
                 CG1 
                 ILE 
                 A 
                 316 
                 65.157 
                 69.656 
                 35.601 
                 1.00 
                 86.07 
               
               
                 1691 
                 CD1 
                 ILE 
                 A 
                 316 
                 65.941 
                 70.428 
                 36.591 
                 1.00 
                 87.92 
               
               
                 1692 
                 C 
                 ILE 
                 A 
                 316 
                 64.634 
                 69.261 
                 31.884 
                 1.00 
                 89.20 
               
               
                 1693 
                 O 
                 ILE 
                 A 
                 316 
                 65.495 
                 69.749 
                 31.150 
                 1.00 
                 88.66 
               
               
                 1694 
                 N 
                 ASP 
                 A 
                 317 
                 63.357 
                 69.078 
                 31.568 
                 1.00 
                 89.57 
               
               
                 1695 
                 CA 
                 ASP 
                 A 
                 317 
                 62.634 
                 69.372 
                 30.335 
                 1.00 
                 90.01 
               
               
                 1696 
                 CB 
                 ASP 
                 A 
                 317 
                 61.193 
                 69.645 
                 30.754 
                 1.00 
                 92.59 
               
               
                 1697 
                 CG 
                 ASP 
                 A 
                 317 
                 60.810 
                 68.877 
                 32.032 
                 1.00 
                 95.95 
               
               
                 1698 
                 CD1 
                 ASP 
                 A 
                 317 
                 60.123 
                 67.834 
                 31.927 
                 1.00 
                 95.95 
               
               
                 1699 
                 OD2 
                 ASP 
                 A 
                 317 
                 61.219 
                 69.301 
                 33.144 
                 1.00 
                 95.95 
               
               
                 1700 
                 C 
                 ASP 
                 A 
                 317 
                 63.099 
                 70.421 
                 29.320 
                 1.00 
                 89.07 
               
               
                 1701 
                 O 
                 ASP 
                 A 
                 317 
                 62.320 
                 70.811 
                 28.446 
                 1.00 
                 88.70 
               
               
                 1702 
                 N 
                 ASN 
                 A 
                 318 
                 64.347 
                 70.864 
                 29.435 
                 1.00 
                 87.57 
               
               
                 1703 
                 CA 
                 ASN 
                 A 
                 318 
                 64.963 
                 71.831 
                 28.520 
                 1.00 
                 87.04 
               
               
                 1704 
                 CB 
                 ASN 
                 A 
                 318 
                 65.213 
                 71.178 
                 27.155 
                 1.00 
                 88.75 
               
               
                 1705 
                 CG 
                 ASN 
                 A 
                 318 
                 66.631 
                 71.413 
                 26.650 
                 1.00 
                 90.71 
               
               
                 1706 
                 OD1 
                 ASN 
                 A 
                 318 
                 67.060 
                 72.557 
                 26.474 
                 1.00 
                 91.48 
               
               
                 1707 
                 ND2 
                 ASN 
                 A 
                 318 
                 67.369 
                 70.328 
                 26.423 
                 1.00 
                 89.69 
               
               
                 1708 
                 C 
                 ASN 
                 A 
                 318 
                 64.292 
                 73.185 
                 28.309 
                 1.00 
                 86.45 
               
               
                 1709 
                 O 
                 ASN 
                 A 
                 318 
                 64.977 
                 74.169 
                 28.009 
                 1.00 
                 86.63 
               
               
                 1710 
                 N 
                 LEU 
                 A 
                 319 
                 62.970 
                 73.259 
                 28.415 
                 1.00 
                 85.40 
               
               
                 1711 
                 CA 
                 LEU 
                 A 
                 319 
                 62.333 
                 74.562 
                 28.272 
                 1.00 
                 84.07 
               
               
                 1712 
                 CB 
                 LEU 
                 A 
                 319 
                 60.829 
                 74.444 
                 27.984 
                 1.00 
                 83.22 
               
               
                 1713 
                 CG 
                 LEU 
                 A 
                 319 
                 60.122 
                 75.778 
                 27.676 
                 1.00 
                 81.79 
               
               
                 1714 
                 CD1 
                 LEU 
                 A 
                 319 
                 60.798 
                 76.470 
                 26.497 
                 1.00 
                 80.23 
               
               
                 1715 
                 CD2 
                 LEU 
                 A 
                 319 
                 58.650 
                 75.534 
                 27.378 
                 1.00 
                 80.40 
               
               
                 1716 
                 C 
                 LEU 
                 A 
                 319 
                 62.566 
                 75.201 
                 29.637 
                 1.00 
                 83.18 
               
               
                 1717 
                 O 
                 LEU 
                 A 
                 319 
                 62.877 
                 76.391 
                 29.743 
                 1.00 
                 82.68 
               
               
                 1718 
                 N 
                 LEU 
                 A 
                 320 
                 62.449 
                 74.379 
                 30.681 
                 1.00 
                 81.52 
               
               
                 1719 
                 CA 
                 LEU 
                 A 
                 320 
                 62.655 
                 74.846 
                 32.042 
                 1.00 
                 81.00 
               
               
                 1720 
                 CB 
                 LEU 
                 A 
                 320 
                 62.433 
                 73.713 
                 33.050 
                 1.00 
                 77.38 
               
               
                 1721 
                 CG 
                 LEU 
                 A 
                 320 
                 61.195 
                 72.812 
                 32.990 
                 1.00 
                 74.93 
               
               
                 1722 
                 CD1 
                 LEU 
                 A 
                 320 
                 60.811 
                 72.470 
                 34.414 
                 1.00 
                 71.44 
               
               
                 1723 
                 CD2 
                 LEU 
                 A 
                 320 
                 60.029 
                 73.483 
                 32.286 
                 1.00 
                 74.69 
               
               
                 1724 
                 C 
                 LEU 
                 A 
                 320 
                 64.070 
                 75.396 
                 32.200 
                 1.00 
                 82.36 
               
               
                 1725 
                 O 
                 LEU 
                 A 
                 320 
                 64.288 
                 76.350 
                 32.940 
                 1.00 
                 83.83 
               
               
                 1726 
                 N 
                 GLN 
                 A 
                 321 
                 65.032 
                 74.795 
                 31.511 
                 1.00 
                 83.98 
               
               
                 1727 
                 CA 
                 GLN 
                 A 
                 321 
                 66.411 
                 75.259 
                 31.591 
                 1.00 
                 85.38 
               
               
                 1728 
                 CB 
                 GLN 
                 A 
                 321 
                 67.355 
                 74.283 
                 30.905 
                 1.00 
                 89.31 
               
               
                 1729 
                 CG 
                 GLN 
                 A 
                 321 
                 67.435 
                 72.913 
                 31.535 
                 1.00 
                 93.36 
               
               
                 1730 
                 CD 
                 GLN 
                 A 
                 321 
                 68.209 
                 71.941 
                 30.660 
                 1.00 
                 95.80 
               
               
                 1731 
                 OE1 
                 GLN 
                 A 
                 321 
                 68.845 
                 71.016 
                 31.158 
                 1.00 
                 95.95 
               
               
                 1732 
                 NE2 
                 GLN 
                 A 
                 321 
                 68.147 
                 72.145 
                 29.343 
                 1.00 
                 95.95 
               
               
                 1733 
                 C 
                 GLN 
                 A 
                 321 
                 66.537 
                 76.602 
                 30.903 
                 1.00 
                 85.17 
               
               
                 1734 
                 O 
                 GLN 
                 A 
                 321 
                 67.101 
                 77.537 
                 31.457 
                 1.00 
                 84.45 
               
               
                 1735 
                 N 
                 GLU 
                 A 
                 322 
                 66.018 
                 76.692 
                 29.683 
                 1.00 
                 85.66 
               
               
                 1736 
                 CA 
                 GLU 
                 A 
                 322 
                 66.088 
                 77.939 
                 28.930 
                 1.00 
                 86.89 
               
               
                 1737 
                 CB 
                 GLU 
                 A 
                 322 
                 65.425 
                 77.788 
                 27.558 
                 1.00 
                 89.68 
               
               
                 1738 
                 CG 
                 GLU 
                 A 
                 322 
                 66.068 
                 76.760 
                 26.635 
                 1.00 
                 94.53 
               
               
                 1739 
                 CD 
                 GLU 
                 A 
                 322 
                 65.478 
                 76.793 
                 25.224 
                 1.00 
                 95.95 
               
               
                 1740 
                 OE1 
                 GLU 
                 A 
                 322 
                 64.294 
                 77.187 
                 25.088 
                 1.00 
                 95.95 
               
               
                 1741 
                 OE2 
                 GLU 
                 A 
                 322 
                 66.189 
                 76.414 
                 24.258 
                 1.00 
                 95.95 
               
               
                 1742 
                 C 
                 GLU 
                 A 
                 322 
                 65.423 
                 79.100 
                 29.666 
                 1.00 
                 85.42 
               
               
                 1743 
                 O 
                 GLU 
                 A 
                 322 
                 65.972 
                 80.204 
                 29.715 
                 1.00 
                 84.52 
               
               
                 1744 
                 N 
                 MET 
                 A 
                 323 
                 64.250 
                 78.845 
                 30.245 
                 1.00 
                 83.85 
               
               
                 1745 
                 CA 
                 MET 
                 A 
                 323 
                 63.505 
                 79.889 
                 30.941 
                 1.00 
                 82.06 
               
               
                 1746 
                 CB 
                 MET 
                 A 
                 323 
                 62.025 
                 79.778 
                 30.586 
                 1.00 
                 83.70 
               
               
                 1747 
                 CG 
                 MET 
                 A 
                 323 
                 61.752 
                 80.018 
                 29.119 
                 1.00 
                 86.33 
               
               
                 1748 
                 SD 
                 MET 
                 A 
                 323 
                 60.007 
                 80.113 
                 28.772 
                 1.00 
                 92.36 
               
               
                 1749 
                 CE 
                 MET 
                 A 
                 323 
                 60.024 
                 80.880 
                 27.173 
                 1.00 
                 93.45 
               
               
                 1750 
                 C 
                 MET 
                 A 
                 323 
                 63.650 
                 80.017 
                 32.457 
                 1.00 
                 79.66 
               
               
                 1751 
                 O 
                 MET 
                 A 
                 323 
                 63.590 
                 81.124 
                 32.980 
                 1.00 
                 79.03 
               
               
                 1752 
                 N 
                 LEU 
                 A 
                 324 
                 63.834 
                 78.912 
                 33.168 
                 1.00 
                 77.18 
               
               
                 1753 
                 CA 
                 LEU 
                 A 
                 324 
                 63.969 
                 78.993 
                 34.620 
                 1.00 
                 75.17 
               
               
                 1754 
                 CB 
                 LEU 
                 A 
                 324 
                 63.250 
                 77.816 
                 35.295 
                 1.00 
                 70.52 
               
               
                 1755 
                 CG 
                 LEU 
                 A 
                 324 
                 61.731 
                 77.702 
                 35.180 
                 1.00 
                 65.13 
               
               
                 1756 
                 CD1 
                 LEU 
                 A 
                 324 
                 61.252 
                 76.517 
                 35.992 
                 1.00 
                 61.92 
               
               
                 1757 
                 CD2 
                 LEU 
                 A 
                 324 
                 61.085 
                 78.971 
                 35.674 
                 1.00 
                 64.50 
               
               
                 1758 
                 C 
                 LEU 
                 A 
                 324 
                 65.413 
                 79.042 
                 35.123 
                 1.00 
                 76.78 
               
               
                 1759 
                 O 
                 LEU 
                 A 
                 324 
                 65.693 
                 79.663 
                 36.152 
                 1.00 
                 75.06 
               
               
                 1760 
                 N 
                 LEU 
                 A 
                 325 
                 66.329 
                 78.401 
                 34.399 
                 1.00 
                 79.20 
               
               
                 1761 
                 CA 
                 LEU 
                 A 
                 325 
                 67.733 
                 78.344 
                 34.815 
                 1.00 
                 81.55 
               
               
                 1762 
                 CB 
                 LEU 
                 A 
                 325 
                 68.185 
                 76.881 
                 34.833 
                 1.00 
                 78.53 
               
               
                 1763 
                 CG 
                 LEU 
                 A 
                 325 
                 67.215 
                 75.944 
                 35.564 
                 1.00 
                 76.77 
               
               
                 1764 
                 CD1 
                 LEU 
                 A 
                 325 
                 67.669 
                 74.506 
                 35.413 
                 1.00 
                 76.38 
               
               
                 1765 
                 CD2 
                 LEU 
                 A 
                 325 
                 67.127 
                 76.332 
                 37.031 
                 1.00 
                 75.85 
               
               
                 1766 
                 C 
                 LEU 
                 A 
                 325 
                 68.710 
                 79.191 
                 33.983 
                 1.00 
                 85.38 
               
               
                 1767 
                 O 
                 LEU 
                 A 
                 325 
                 69.290 
                 80.151 
                 34.489 
                 1.00 
                 85.61 
               
               
                 1768 
                 N 
                 GLY 
                 A 
                 326 
                 68.903 
                 78.832 
                 32.717 
                 1.00 
                 89.93 
               
               
                 1769 
                 CA 
                 GLY 
                 A 
                 326 
                 69.809 
                 79.591 
                 31.862 
                 1.00 
                 92.77 
               
               
                 1770 
                 C 
                 GLY 
                 A 
                 326 
                 70.395 
                 78.763 
                 30.729 
                 1.00 
                 94.69 
               
               
                 1771 
                 O 
                 GLY 
                 A 
                 326 
                 71.369 
                 78.037 
                 30.927 
                 1.00 
                 95.95 
               
               
                 1772 
                 N 
                 GLY 
                 A 
                 327 
                 69.812 
                 78.872 
                 29.538 
                 1.00 
                 95.44 
               
               
                 1773 
                 CA 
                 GLY 
                 A 
                 327 
                 70.304 
                 78.104 
                 28.404 
                 1.00 
                 95.95 
               
               
                 1774 
                 C 
                 GLY 
                 A 
                 327 
                 69.866 
                 78.638 
                 27.048 
                 1.00 
                 95.95 
               
               
                 1775 
                 O 
                 GLY 
                 A 
                 327 
                 69.493 
                 79.830 
                 26.957 
                 1.00 
                 95.95 
               
               
                 1776 
                 OXT 
                 GLY 
                 A 
                 327 
                 69.907 
                 77.866 
                 26.063 
                 1.00 
                 95.95 
               
               
                 1777 
                   
                 GLY 
                 A 
                 327 
               
               
                 1778 
                 O 
                 HOH 
                 W 
                 1 
                 45.353 
                 102.993 
                 32.467 
                 1.00 
                 50.15 
               
               
                 1779 
                 O 
                 HOH 
                 W 
                 2 
                 47.316 
                 82.519 
                 34.627 
                 1.00 
                 57.09 
               
               
                 1780 
                 O 
                 HOH 
                 W 
                 3 
                 31.392 
                 64.065 
                 45.689 
                 1.00 
                 60.13 
               
               
                 1781 
                 O 
                 HOH 
                 W 
                 4 
                 46.892 
                 91.480 
                 19.212 
                 1.00 
                 66.69 
               
               
                 1782 
                 O 
                 HOH 
                 W 
                 5 
                 64.831 
                 89.601 
                 40.555 
                 1.00 
                 46.68 
               
               
                 1783 
                 O 
                 HOH 
                 W 
                 6 
                 45.378 
                 77.628 
                 33.925 
                 1.00 
                 63.84 
               
               
                 1784 
                 O 
                 HOH 
                 W 
                 7 
                 48.658 
                 89.782 
                 54.328 
                 1.00 
                 74.42 
               
               
                 1785 
                 O 
                 HOH 
                 W 
                 8 
                 38.225 
                 90.198 
                 35.001 
                 1.00 
                 94.21 
               
               
                 1786 
                 O 
                 HOH 
                 W 
                 9 
                 67.358 
                 103.472 
                 22.826 
                 1.00 
                 65.96 
               
               
                 1787 
                 O 
                 HOH 
                 W 
                 10 
                 40.781 
                 105.542 
                 59.632 
                 1.00 
                 57.47 
               
               
                 1788 
                 O 
                 HOH 
                 W 
                 11 
                 64.373 
                 76.920 
                 22.211 
                 1.00 
                 90.22 
               
               
                 1789 
                 O 
                 HOH 
                 W 
                 12 
                 65.998 
                 86.720 
                 46.709 
                 1.00 
                 59.52 
               
               
                 1790 
                 O 
                 HOH 
                 W 
                 13 
                 37.481 
                 88.829 
                 39.254 
                 1.00 
                 52.14 
               
               
                 1791 
                 O 
                 HOH 
                 W 
                 14 
                 63.610 
                 91.916 
                 41.126 
                 1.00 
                 57.56 
               
               
                 1792 
                 O 
                 HOH 
                 W 
                 15 
                 38.719 
                 91.362 
                 23.684 
                 1.00 
                 64.77 
               
               
                 1793 
                   
                 HOH 
                 W 
                 15 
               
               
                 1794 
                 C1 
                 PLM 
                 A 
                 328 
                 51.604 
                 75.192 
                 37.410 
                 1.00 
                 85.43 
               
               
                 1795 
                 O1 
                 PLM 
                 A 
                 328 
                 50.976 
                 74.110 
                 37.329 
                 1.00 
                 84.59 
               
               
                 1796 
                 O2 
                 PLM 
                 A 
                 328 
                 51.199 
                 76.231 
                 36.857 
                 1.00 
                 86.9S 
               
               
                 1797 
                 C2 
                 PLM 
                 A 
                 328 
                 52.897 
                 75.263 
                 38.236 
                 1.00 
                 84.45 
               
               
                 1798 
                 C3 
                 PLM 
                 A 
                 328 
                 52.585 
                 75.314 
                 39.72S 
                 1.00 
                 81.28 
               
               
                 1799 
                 C4 
                 PLM 
                 A 
                 328 
                 53.818 
                 75.421 
                 40.617 
                 1.00 
                 82.41 
               
               
                 1800 
                 C5 
                 PLM 
                 A 
                 328 
                 53.431 
                 75.459 
                 42.122 
                 1.00 
                 80.70 
               
               
                 1801 
                 C6 
                 PLM 
                 A 
                 328 
                 53.881 
                 74.176 
                 42.753 
                 1.00 
                 80.20 
               
               
                 1802 
                 C7 
                 PLM 
                 A 
                 328 
                 55.285 
                 74.378 
                 43.205 
                 1.00 
                 81.28 
               
               
                 1803 
                 C8 
                 PLM 
                 A 
                 328 
                 55.933 
                 73.139 
                 43.737 
                 1.00 
                 82.12 
               
               
                 1804 
                 C9 
                 PLM 
                 A 
                 328 
                 57.331 
                 73.563 
                 44.086 
                 1.00 
                 83.S6 
               
               
                 1805 
                 CA 
                 PLM 
                 A 
                 328 
                 58.225 
                 72.448 
                 44.493 
                 1.00 
                 84.66 
               
               
                 1806 
                 CB 
                 PLM 
                 A 
                 328 
                 59.214 
                 72.437 
                 43.346 
                 1.00 
                 86.04 
               
               
                 1807 
                 CC 
                 PLM 
                 A 
                 328 
                 60.264 
                 71.394 
                 43.405 
                 1.00 
                 86.77 
               
               
                 1808 
                 CD 
                 PLM 
                 A 
                 328 
                 61.123 
                 71.558 
                 42.177 
                 1.00 
                 90.12 
               
               
                 1809 
                 CE 
                 PLM 
                 A 
                 328 
                 62.197 
                 70.505 
                 42.125 
                 1.00 
                 92.94 
               
               
                 1810 
                 CF 
                 PLM 
                 A 
                 328 
                 61.694 
                 69.314 
                 41.329 
                 1.00 
                 95.95 
               
               
                 1811 
                 CG 
                 PLM 
                 A 
                 328 
                 62.733 
                 68.218 
                 41.256 
                 1.00 
                 95.95 
               
               
                   
               
            
           
         
       
     
     
       
         
           
               
             
               
                 TABLE 4 
               
             
            
               
                   
               
               
                   
               
               
                 Data Summary Of Analytes Detected By 
               
               
                 GC/MS Using Chemical Ionization 
               
            
           
           
               
               
               
               
            
               
                   
                   
                 Predicted Mass Of 
                   
               
               
                 Peak 
                 [M + H]+ 
                 Free Acid (Da) 
                 Identification/Comments 
               
               
                   
               
               
                 a 
                 243 
                 228 
                 myristic acid 
               
               
                 b 
                 269 
                 254 
                 likely mono-unsaturated palmitic 
               
               
                   
                   
                   
                 acid 
               
               
                 c 
                 271 
                 256 
                 palmitic acid 
               
               
                 d 
                 283 
                 268 
                 idenfication pending 
               
               
                 e 
                 297 
                 282 
                 likely mono-unsaturated stearic 
               
               
                   
                   
                   
                 acid 
               
               
                 f 
                 299 
                 284 
                 stearic acid 
               
               
                 g 
                 311 
                 296 
                 identification pending 
               
               
                   
               
            
           
         
       
     
      It will be understood that various details of the invention can be changed without departing from the scope of the invention. Furthermore, the foregoing description is for the purpose of illustration only, and not for the purpose of limitation—the invention being defined by the claims.