# Patent

## Title
Three-dimensional structure of polyketide synthases

## Abstract

The present invention comprises crystalline polyketide synthases, isolated non-native polyketide synthases having the structural coordinates of said crystalline polyketide synthases, and nucleic acids encoding such non-native polyketide synthases. Also disclosed are methods of predicting the activity and/or substrate specificity of putative polyketide synthase, methods of identifying potential polyketide synthase substrates, and methods of identifying potential polyketide synthase inhibitors.

## Background
RELATED APPLICATIONS
This application is a national stage entry of PCT/US00/20674 filed on Jul. 27, 2000, which claims priority from Provisional Application No. 60/145,898 filed on Jul. 27, 1999, each of which is hereby incorporated by reference herein in its entirety.


ACKNOWLEDGMENT
This invention was made with government support under Grant No. MCB9982586 by the National Science Foundation. The government has certain rights in the invention.


FIELD OF THE INVENTION
The present invention relates to methods for designing mutant polyketide synthases, and to predicting the activity and/or substrate specificity of putative native and mutant polyketide synthases. The present invention further relates to methods for identifying polyketide synthase substrates and/or inhibitors.
BACKGROUND
Advances in molecular biology have allowed the development of biological agents useful in modulating protein or nucleic acid activity or expression, respectively. Many of these advances are based on identifying the primary sequence of the molecule to be modulated. For example, determining the nucleic acid sequence of DNA or RNA allows the development of antisense or ribozyme molecules. Similarly, identifying the primary sequence allows for the identification of sequences that may be useful in creating monoclonal antibodies. However, often the primary sequence of a protein is insufficient to develop therapeutic or diagnostic molecules due to the secondary, tertiary or quartenary structure of the protein from which the primary sequence is obtained. The process of designing potent and specific inhibitors or activators has improved with the arrival of techniques for determining the three-dimensional structure of an enzyme or polypeptide to be modulated.
The phenylpropanoid synthetic pathway in plants produces a class of compounds know as anthocyanins, which are used for a variety of applications. Anthocyanins are involved in pigmentation and protection against UV photodamage, synthesis of anti-microbial phytoalexins, and are flavonoid inducers of Rhizobium modulation genes 1–4. As medicinal natural products, the phenylpropanoids exhibit cancer chemopreventive activity, as well as anti-mitotic, estrogenic, anti-malarial, anti-oxidant, and antiasthmatic activities. The benefits of consuming red wine, which contains significant amounts of 3,4′,5-trihydroxystilbene (resveratrol) and other phenylpropanoids, highlight the dietary importance of these compounds. Chalcone synthase (CHS), a polyketide synthase, plays an essential role in the biosynthesis of plant phenylpropanoids.
An improvement in the understanding of the structure/function of these enzymes would allow for the exploitation of the synthetic capabilities of known enzymes for production of useful new chemical compounds, or allow for the creation of novel non-native enzymes having new synthetic capabilities. A need exists, therefore, for a detailed understanding of the molecular basis of the chemical reactions involved in polyketide synthesis. The present invention addresses this and related needs.
SUMMARY OF THE INVENTION
In accordance with the present invention there are presented crystalline polyketide synthases and the three-dimensional coordinates derived therefrom. Three-dimensional coordinates have been obtained for an active form of chalcone synthase and several inactive mutants thereof, both with and without substrate or substrate analog. Similar results have been obtained for the polyketide synthases stilbene synthase and pyrone synthase.
One aspect of the present invention that is made possible by results described herein is that the three-dimensional properties of polyketide synthase proteins are determined, in particular the three-dimensional properties of the active site. The invention features specific coordinates of at least fourteen α carbon atoms defined for the active site in three-dimensional space. R-groups attached to said α-carbons are defined such that mutants can be made by changing at least one R-group found in the synthase active site. Such mutants may have unique and useful properties. Thus, in another embodiment of the invention, there are provided isolated non-native (e.g., mutant) synthase(s) having at least fourteen active site α-carbons having the structural coordinates disclosed herein and one or more R-groups other than those found in native chalcone synthase(s).
The three-dimensional coordinates disclosed herein can be employed in a variety of methods. The polyketide synthase used in the crystallization studies disclosed herein is a chalcone synthase derived from Medicago sataiva (alfalfa). A large number of proteins have been isolated and sequenced which have primary amino acid sequence similar to that of chalcone synthase, but for which substrate specificity and/or product is unknown. Thus, in another embodiment of the present invention, there are provided methods for predicting the activity and/or substrate specificity of a putative polyketide synthase. There are further provided methods for identifying potential substrates for a polyketide synthase, as well as inhibitors thereof.
Other aspects, embodiments, advantages, and features of the present invention will become apparent from the following specification.



BRIEF DESCRIPTION OF FIGURES
FIG. 1A presents the chemical structures of chalcone, naringenin, resveratrol, and cerulenin. FIG. 1B presents final SIGMAA-weighted 2Fo-Fc electron density map of the CHS-resveratrol complex in the vicinity of the resveratrol binding site. The map is contoured at 1σ.
FIG. 2A shows a ribbon representation of the CHS homodimer. The approximate alpha carbon positions of Met 137 from each of the monomers are labeled accordingly. Naringenin completely fills the coumaroyl-binding and cyclization pockets while the CoA binding tunnels are highlighted by black arrows. Produced with MOLSCRIPT and rendered with POV-Ray. FIG. 2B presents a stereoview of the monomer's alpha carbon backbone. The orientation of the left-hand monomer is exactly the same as in FIG. 2A. Every twenty residues are numbered starting with residue 3 and include the C-terminal residue, 389.
FIG. 3 shows a comparison of chalcone synthase and 3-ketoacyl-CoA thiolase. Ribbon view of the CHS monomer is oriented perpendicular to the dimer interface. The active site cysteine (Cys 164) and the location of bound CoA are rendered as ball and stick models. In addition, strands β1d and β2d of the cyclization pocket are noted. The reaction catalyzed by CHS is illustrated with the coumaroyl- and malonyl-derived portions of chalcone, respectively. The thiolase monomer is depicted in the same orientation as CHS with the Active site cysteine (Cys 125) modeled and the reaction of thiolase as indicated. Figure prepared with MOLSCRIPT and rendered with POV-Ray.
FIG. 4 collectively shows structures of CHS-Acyl-CoA complexes. The ribbon diagram in panel FIG. 4A (on the top left) is the same as FIG. 2A. The CoA binding region depicted in stereo is bounded by a black box in the upper ribbon diagram. Close-up stereoviews of the C164S mutant CoA binding region for the malonyl- and hexanoyl-CoA complexes are depicted in FIGS. 4B and 4C, respectively. This mutant retains decarboxylation activity and an acetyl-CoA complex is observed crystallographically for the malonyl-CoA complex. In each complex, placement of the Met 137 loop originating from the dyad-related molecule spatially defines one wall of the cyclization pocket. Hydrogen bonds are depicted as spheres. Figure prepared with MOLSCRIPT and rendered with POV-Ray.
FIG. 5A shows the CHS-naringenin complex viewed down the CoA-binding tunnel. The ribbon diagram at the top left has been rotated 90 degrees around the y-axis from the orientation shown in FIG. 2A. This view approximates the global orientation of the CHS dimer used for the close-up view of the naringenin binding site depicted in stereo. Again, the black box highlights the region of CHS shown in stereo close-up. Hydrogen bonds are depicted as dashed cylinders. FIG. 5B illustrates a comparison of the CHS apoenzyme, CHS-naringenin, and CHS-resveratrol structures. Protein backbone atoms for the three refined structures (apoenzyme, naringenin, and resveratrol) were superimposed by least squares fit in O. The position of bound naringenin and resveratrol are shown. For reference, a modeled low energy conformation of chalcone is indicated by dashed cylinders. Strands β1d and β2d for each complex are also depicted (see FIG. 3). β2d does not change in all the complexes examined, but β1d moves in the CHS-resveratrol complex. FIG. 5C presents representative sequence alignment of the β1d–β2d region is given with positions 255, 266, and 268 (SEQ ID NO:1) highlighted. The first three sequences (SEQ ID NOs:2–4) follow a CHS-like cyclization pathway, while the last three (SEQ ID NOs:5–7) use the STS-cyclization pathway. Figure prepared with MOLSCRIPT and rendered with POV-Ray.
FIG. 6 presents the proposed reaction mechanism for chalcone synthesis. The three boxed regions labeled 1, 2, and 3 depict the addition of acetate units derived from malonyl-CoA during the elongation of polyketide intermediates. Box I is depicted in expanded fashion to illustrate the mechanistic details governing the decarboxylation, enolization, and condensation phase of ketide elongation. Smaller black arrows depict the flow of electrons. Each acetate unit of the malonyl-CoA thioesters is coded to emphasize the portions of chalcone derived from each of three elongation reactions using malonyl-CoA. Cyclization and aromatization of the enzyme bound tetraketide leads to formation of chalcone. Hydrogen bonds are shown as dashed lines. Coenzyme A is symbolized as a circle.
FIG. 7 collectively presents three-dimensional models of the elongation and cyclization reaction in CHS and STS. Views are shown in stereo. FIG. 7A illustrates the elongation of the triketide covalently attached to Cys 164 by the acetyl-CoA carbanion produces the tetraketide CoA thioester reaction intermediate that subsequently reattaches to Cys 164. FIG. 7B illustrates the folding of the tetraketide intermediate in CHS positions the oxygen of C1 near the hydrogen of C6 facilitating internal proton transfer and expulsion of chalcone upon cyclization. FIG. 7C illustrates alternate folding of the tetraketide intermediate and positioning of the oxygen of C7 near the hydrogen of C2 in STS allows formation of resveratrol using an internal proton transfer followed by hydrolysis and decarboxylation. Rendered and dashed lines illustrate potential hydrogen bonding interactions. Figure prepared with MOLSCREPIT and rendered with POV-Ray.
FIG. 8 presents a comparison of the active site volumes of CHS and GCHS2. The active site volumes available for binding ketide intermediates were calculated with VOID00 for the CHS-COA complex and for a homology model of GCHS2 with CoA. The cavities are shown as a wire mesh. The homology model of GCHS2 was generated using MODELER and the volume calculated and displayed as for CHS. The numbering scheme is for alfalfa CHS homodimer. Figure prepared with MOLSCRIPT and rendered with POV-Ray.
FIG. 9 shows an example of a computer system in block diagram form.



DETAILED DESCRIPTION OF THE INVENTION
The phenylpropanoid synthetic pathway in plants produces a class of compounds know as anthocyanins, which are used for a variety of applications. Anthocyanins are involved in pigmentation and protection against UV photodamage, synthesis of anti-microbial phytoalexins, and are flavonoid inducers of Rhizobium modulation genes 1–4. As medicinal natural products, the phenylpropanoids exhibit cancer chemopreventive activity, as well as anti-mitotic, estrogenic, anti-malarial, anti-oxidant, and antiasthmatic activities. The benefits of consuming red wine, which contains significant amounts of 3,4′,5-trihydroxystilbene (resveratrol) and other phenylpropanoids, highlight the dietary importance of these compounds.
Polyketides are a large class of compounds and include a broad range of antibiotics, immunosuppressants and anticancer agents which together account for sales of over $5 billion per year. Polyketides are molecules which are an extremely rich source of bioactivities, including antibiotics (e.g., tetracyclines and erythromycin), anti-cancer agents (e.g., daunomycin), immunosuppressants (e.g., FK506 and rapamycin), and veterinary products (e.g., monensin) and the like. Many polyketides (produced by polyketide synthases) are valuable as therapeutic agents. Polyketide synthases are multifunctional enzymes that catalyze the biosynthesis of a huge variety of carbon chains differing in length and patterns of functionality and cyclization.
Chalcone synthase (CHS), a polyketide synthase, plays an essential role in the biosynthesis of plant phenylpropanoids. CHS supplies 4,2′,4′,6′-tetrahydroxychalcone (chalcone) to downstream enzymes that synthesize a diverse set of flavonoid phytoalexins and anthocyanin pigments. Synthesis of chalcone by CHS involves the sequential condensation of one p-coumaroyl- and three malonyl-Coenzyme-A (CoA) molecules (Kreuzaler and Hahlbrock, Eur. J. Biochem. 56:205–213, 1975). After initial capture of the p-coumaroyl moiety, each subsequent condensation step begins with decarboxylation of malonyl-CoA at the CHS active site; the resulting acetyl-CoA carbanion then serves as the nucleophile for chain elongation.
Ultimately, these reactions generate a tetraketide intermediate that cyclizes by a Claisen condensation into a hydroxylated aromatic ring system. This mechanism mirrors those of the fatty acid and polyketide synthases but with significant differences. CHS uses CoA-thioesters for shuttling substrates and intermediate polyketides instead of the acyl carrier proteins used by the fatty acid synthases. Also, unlike these enzymes, which function as either multichain or multimodular enzyme complexes catalyzing distinct reactions at different active sites, CHS functions as a unimodular polyketide synthase and carries out a series of decarboxylation, condensation, cyclization, and aromatization reactions at a single active site.
A number of plant polyketide synthases related to CHS by sequence identity, including stilbene synthase (STS), bibenzyl synthase (BBS), and acridone synthase (ACS), share a common chemical mechanism, but differ from CHS in their substrate specificity and/or in the stereochemistry of the polyketide cyclization reaction. For example, STS condenses one coumaroyl- and three malonyl-CoA molecules, like CHS, but synthesizes resveratrol (resveratrol) through a structurally distinct cyclization intermediate.
While the cloning of nearly 150 CHS-related genes, and characterization of some of these proteins, provides insight into their biological function, it remains unclear how these enzymes perform multiple decarboxylation and condensation reactions and how they dictate the stereochemistry of the final polyketide cyclization reaction. Furthermore, despite significant advances in the biosynthetic manipulation of structurally complex and biologically important natural products, there remains a lack of structural information on polyketide synthases from any source.
As used herein, “naturally occurring amino acid” and “naturally occurring R-group” includes L-isomers of the twenty amino acids naturally occurring in proteins. Naturally occurring amino acids are glycine, alanine, valine, leucine, isoleucine, serine, methionine, threonine, phenylalanine, tyrosine, tryptophan, cysteine, proline, histidine, aspartic acid, asparagine, glutamic acid, glutamine, arginine, and lysine. Unless specially indicated, all amino acids referred to in this application are in the L-form.
“Unnatural amino acid” and “unnatural R-group” includes amino acids that are not naturally found in proteins. Examples of unnatural amino acids included herein are racemic mixtures of selenocysteine and selenomethionine. In addition, unnatural amino acids include the D or L forms of, for example, nor-leucine, para-nitrophenylalanine, homophenylalanine, para-fluorophenylalanine, 3-amino-2-benzylpropionic acid, homoarginines, D-phenylalanine, and the like.
“R-group” refers to the substituent attached to the α-carbon of an amino acid residue. An R-group is an important determinant of the overall chemical character of an amino acid. There are twenty natural R-groups found in proteins, which make up the twenty naturally occurring amino acids.
“α-carbon” refers to the chiral carbon atom found in an amino acid residue. Typically, four substituents will be covalently bound to said α-carbon including an amine group, a carboxylic acid group, a hydrogen atom, and an R-group.
“Positively charged amino acid” and “positively charged R-group” includes any naturally occurring or unnatural amino acid having a positively charged side chain under normal physiological conditions. Examples of positively charged, naturally occurring amino acids include arginine, lysine, histidine, and the like.
“Negatively charged amino acid” and “negatively charged R-group” includes any naturally occurring or unnatural amino acid having a negatively charged side chain under normal physiological conditions. Examples of negatively charged, naturally occurring amino acids include aspartic acid, glutamic acid, and the like.
“Hydrophobic amino acid” and “hydrophobic R-group” includes any naturally occurring or unnatural amino acid having an uncharged, nonpolar side chain that is relatively insoluble in water. Examples of naturally occurring hydrophobic amino acids are alanine, leucine, isoleucine, valine, proline, phenylalanine, tryptophan, methionine, and the like.
“Hydrophilic amino acid” and “hydrophilic R-group” includes any naturally occurring or unnatural amino acid having a charged polar side chain that is relatively soluble in water. Examples of naturally occurring hydrophilic amino acids include serine, threonine, tyrosine, asparagine, glutamine, cysteine, and the like.
“Mutant” or “mutated synthase” refers to a polyketide synthase polypeptide, having the three-dimensional coordinates as set forth in Protein Data Bank (PDB) Accession No. 1BI5 (Table 5), and having R-groups on each α-carbon other than the prescribed arrangements of R-groups associated with each α-carbon of a known isolated polyketide synthase (Accession No. 1BI5, Table 5). Examples of mutant or mutated synthase polypeptides include those having Protein Data Base Accession No. 1D6F, 1D6I and 1D6H (Tables 6–8, respectively).
The R-groups of known isolated polyketide synthases can be readily determined by consulting sequence databases well known in the art, such as, for example, Genbank. Additional R-groups found inside and/or outside of the active site may or may not be the same. R-groups may be a natural R-group, unnatural R-group, hydrophobic R-group, hydrophilic R-group, positively charged R-group, negatively charged R-group, and the like. The term “mutant” only refers to the configuration of R-groups within the active site; therefore, mutations outside of the residues found in the active site are not considered to be mutants in light of the present invention.
“Nonmutated synthase” includes a synthase wherein no R-group(s) are changed relative to the active site of CHS (see, for example, PDB Accession No. 1BI5). A nonmutated synthase according to the present invention may or may not have amino acid residues outside of the active site that are the same as those taught for native CHS (SEQ ID NO:1). In addition, a nonmutated synthase is a synthase having an active site comprising α-carbons having the coordinates as given in Table 1 and having the arrangements of R-groups associated with □-carbons as given in Table 1.







TABLE 1







Structural Cartesian coordinates of α-carbons found in the


active site of a polyketide synthase of the present invention.















Amino Acid


Active Site-Carbon



residue


Number
X Position
Y Position
Z Position
(SEQ ID NO:1)














1
25.378
49.320
57.979
Thr 132


2
26.089
45.704
56.981
Ser 133


3
35.423
42.296
66.622
Met 137*


4
25.212
49.977
62.196
Gln 161


5
22.745
44.120
51.193
Thr 194


6
19.022
42.892
54.600
Thr 197


7
13.850
48.144
50.791
Gly 211


8
22.118
48.048
46.357
Gly 216


9
13.001
54.666
59.688
Ile 254


10
16.434
48.819
61.334
Gly 256


11
18.715
43.328
59.526
Leu 263


12
13.943
47.516
57.567
Phe 265


13
9.252
52.715
57.456
Leu 267


14
23.141
53.552
52.148
Ser 338





*Met 137 from the second monomer






“Non-native” or “non-native synthase” refers to synthase proteins that are not found in nature, whether isolated or not. A non-native synthase may, for example, be a mutated synthase (see, for example, PDB Accession No. 1D6F, 1D6I and 1D6H).
“Native” or “native synthase” refers to synthase proteins that are produced in nature, e.g., are not mutants (see, for example, PDB Accession No. 1BI5).
“Isolated” refers to a protein or nucleic acid that has been identified and separated from its natural environment. Contaminant components of its natural environment may include enzymes, hormones, and other proteinaceous or non-proteinaceous solutes. In one embodiment, the isolated molecule, in the case of a protein, will be purified to a degree sufficient to obtain at least 15 residues of N-terminal or internal amino acid sequence or to homogeneity by SDS-PAGE under reducing or non-reducing conditions using Coomassie blue or silver stain. In the case of a nucleic acid the isolated molecule will preferably be purified to a degree sufficient to obtain a nucleic acid sequence using standard sequencing methods.
“Degenerate variations thereof” refers to changing a gene sequence using the degenerate nature of the genetic code to encode proteins having the same amino acid sequence yet having a different gene sequence. For example, polyketide synthases of the present invention are based on amino acid sequences. Degenerate gene variations thereof can be made encoding the same protein due to the plasticity of the genetic code, as described herein.
“Expression” refers to transcription of a gene or nucleic acid sequence, stable accumulation of nucleic acid, and the translation of that nucleic acid to a polypeptide sequence. Expression of genes also involves transcription of the gene to make RNA, processing of RNA into mRNA in eukaryotic systems, and translation of mRNA into proteins. It is not necessary for the genes to integrate into the genome of a cell in order to achieve expression. This definition in no way limits expression to a particular system or to being confined to cells or a particular cell type and is meant to include cellular, transient, in vitro, in vivo, and viral expression systems in both prokaryotic, eukaryotic cells, and the like.
“Foreign” or “heterologous” genes refers to a gene encoding a protein whose exact amino acid sequence is not normally found in the host cell.
“Promoter” and “promoter regulatory element”, and the like, refers to a nucleotide sequence element within a nucleic acid fragment or gene that controls the expression of that gene. These can also include expression control sequences. Promoter regulatory elements, and the like, from a variety of sources can be used efficiently to promote gene expression. Promoter regulatory elements are meant to include constitutive, tissue-specific, developmental-specific, inducible, subgenomic promoters, and the like. Promoter regulatory elements may also include certain enhancer elements or silencing elements that improve or regulate transcriptional efficiency. Promoter regulatory elements are recognized by RNA polymerases, promote the binding thereof, and facilitate RNA transcription.
A polypeptide is a chain of amino acids, regardless of length or post-translational modification (e.g., glycosylation or phosphorylation). A polypeptide or protein refers to a polymer in which the monomers are amino acid residues, which are joined together through amide bonds. When the amino acids are alpha-amino acids, either the L-optical isomer or the D-optical isomer can be used, the L-isomers being typical. A synthase polypeptide of the invention is intended to encompass an amino acid sequence as set forth in SEQ ID NO:1 (see, Table 2) or SEQ ID NO:1 having one or more of the following mutations: C164A, H303Q, and N336A, mutants, variants and conservative substitutions thereof comprising L- or D-amino acids and include modified sequences such as glycoproteins.







TABLE 2







(SEQ ID NO:1)







MVSVSEIRKA QRAEGPATIL AIGTANPANC VEQSTYPDFY FKITNSEHKT ELKEKFQRMC


 


DKSMIKRRYM YLTEEILKEN PNVCEYMAPS LDARQDMVVV EVPRLGKEAA VKAIKEWGQP


 


KSKITHLIVC TTSGVDMPGA DYQLTKLLGL RPYVKRYMMY QQGXFAGGTV LRLAKDLAEN


 


NKGARVLVVC SEVTAVTFRG PSDTHLDSLV GQALFGDGAA ALIVGSDPVP EIEKPIFEMV


 


WTAQTIAPDS EGAIDGHLRE AGLTFHLLKD VPGIVSKNIT KALVEAFEPL GISDYNSIFW


 


IAHPGGPAIL DQVEQKLALK PEKMNATREV LSEYGNMSSA CVLFILDEMR KKSTQNGLKT


 


TGEGLEWGVL FGFGPGLTIE TVVLRSVAI









Accordingly, the polypeptides of the invention are intended to cover naturally occurring proteins, as well as those which are recombinantly or synthetically synthesized. Polypeptide or protein fragments are also encompassed by the invention. Fragments can have the same or substantially the same amino acid sequence as the naturally occurring protein. A polypeptide or peptide having substantially the same sequence means that an amino acid sequence is largely, but not entirely, the same, but retains a functional activity of the sequence to which it is related. In general polypeptides of the invention include peptides, or full-length protein, that contains substitutions, deletions, or insertions into the protein backbone, that would still have an approximately 70%–90% homology to the original protein over the corresponding portion. A yet greater degree of departure from homology is allowed if like-amino acids, i.e. conservative amino acid substitutions, do not count as a change in the sequence.
A polypeptide may be substantially related but for a conservative variation, such polypeptides being encompassed by the invention. A conservative variation denotes the replacement of an amino acid residue by another, biologically similar residue. Examples of conservative variations include the substitution of one hydrophobic residue such as isoleucine, valine, leucine or methionine for another, or the substitution of one polar residue for another, such as the substitution of arginine for lysine, glutamic for aspartic acids, or glutamine for asparagine, and the like. Other illustrative examples of conservative substitutions include the changes of: alanine to serine; arginine to lysine; asparagine to glutamine or histidine; aspartate to glutamate; cysteine to serine; glutamine to asparagine; glutamate to aspartate; glycine to proline; histidine to asparagine or glutamine; isoleucine to leucine or valine; leucine to valine or isoleucine; lysine to arginine, glutamine, or glutamate; methionine to leucine or isoleucine; phenylalanine to tyrosine, leucine or methionine; serine to threonine; threonine to serine; tryptophan to tyrosine; tyrosine to tryptophan or phenylalanine; valine to isoleucine or leucine, and the like. The term “conservative variation” also includes the use of a substituted amino acid in place of an unsubstituted parent amino acid provided that antibodies raised to the substituted polypeptide also immunoreact with the unsubstituted polypeptide.
Modifications and substitutions are not limited to replacement of amino acids. For a variety of purposes, such as increased stability, solubility, or configuration concerns, one skilled in the art will recognize the need to introduce, (by deletion, replacement, or addition) other modifications. Examples of such other modifications include incorporation of rare amino acids, dextra-amino acids, glycosylation sites, cytosine for specific disulfide bridge formation. The modified peptides can be chemically synthesized, or the isolated gene can be site-directed mutagenized, or a synthetic gene can be synthesized and expressed in bacteria, yeast, baculovirus, tissue culture and so on.
Chalcone synthase polypeptides of the invention include synthase polypeptides from plants, prokaryotes, eukaryotes, including, for example, invertebrates, mammals and humans and include sequences as set forth in SEQ ID NO:1, as well as sequences that have at least 70% homology to the sequence of SEQ ID NO:1, fragments, variants, or conservative substitutions of any of the foregoing sequences.
The term “variant” refers to polypeptides modified at one or more amino acid residues yet still retain the biological activity of a synthase polypeptide. Variants can be produced by any number of means known in the art, including, for example, methods such as, for example, error-prone PCR, shuffling, oligonucleotide-directed mutagenesis, assembly PCR, sexual PCR mutagenesis, and the like, as well as any combination thereof.
By “substantially identical” is meant a polypeptide or nucleic acid exhibiting at least 50%, preferably 85%, more preferably 90%, and most preferably 95% homology to a reference amino acid or nucleic acid sequence.
Homology or identity is often measured using sequence analysis software (e.g., Sequence Analysis Software Package of the Genetics Computer Group, University of Wisconsin Biotechnology Center, 1710 University Avenue, Madison, Wis. 53705). Such software matches similar sequences by assigning degrees of homology to various deletions, substitutions and other modifications. The terms “homology” and “identity” in the context of two or more nucleic acids or polypeptide sequences, refer to two or more sequences or subsequences that are the same or have a specified percentage of amino acid residues or nucleotides that are the same when compared and aligned for maximum correspondence over a comparison window or designated region as measured using any number of sequence comparison algorithms or by manual alignment and visual inspection.
For sequence comparison, typically one sequence acts as a reference sequence, to which test sequences are compared. When using a sequence comparison algorithm, test and reference sequences are entered into a computer, subsequence coordinates are designated, if necessary, and sequence algorithm program parameters are designated. Default program parameters can be used, or alternative parameters can be designated. The sequence comparison algorithm then calculates the percent sequence identities for the test sequences relative to the reference sequence, based on the program parameters.
A “comparison window”, as used herein, includes reference to a segment of any one of the number of contiguous positions selected from the group consisting of from 20 to 600, usually about 50 to about 200, more usually about 100 to about 150 in which a sequence may be compared to a reference sequence of the same number of contiguous positions after the two sequences are optimally aligned. Methods of alignment of sequence for comparison are well-known in the art. Optimal alignment of sequences for comparison can be conducted, e.g., by the local homology algorithm of Smith & Waterman, Adv. Appl. Math. 2:482, 1981, by the homology alignment algorithm of Needleman & Wunsch, J. Mol. Biol. 48:443, 1970, by the search for similarity method of Person & Lipman, Proc. Nat'l. Acad. Sci. USA 85:2444, 1988, by computerized implementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group, 575 Science Dr., Madison, Wis.), or by manual alignment and visual inspection. Other algorithms for determining homology or identity include, for example, in addition to a BLAST program (Basic Local Alignment Search Tool at the National Center for Biological Information), ALIGN, AMAS (Analysis of Multiply Aligned Sequences), AMPS (Protein Multiple Sequence Alignment), ASSET (Aligned Segment Statistical Evaluation Tool), BANDS, BESTSCOR, BIOSCAN (Biological Sequence Comparative Analysis Node), BLIMPS (BLocks IMProved Searcher), FASTA, Intervals & Points, BMB, CLUSTAL V, CLUSTAL W, CONSENSUS, LCONSENSUS, WCONSENSUS, Smith-Waterman algorithm, DARWIN, Las Vegas algorithm, FNAT (Forced Nucleotide Alignment Tool), Framealign, Framesearch, DYNAMIC, FILTER, FSAP (Fristensky Sequence Analysis Package), GAP (Global Alignment Program), GENAL, GIBBS, GenQuest, ISSC (Sensitive Sequence Comparison), LALIGN (Local Sequence Alignment), LCP (Local Content Program), MACAW (Multiple Alignment Construction & Analysis Workbench), MAP (Multiple Alignment Program), MBLKP, MBLKN, PIMA (Pattern-Induced Multisequence Alignment), SAGA (Sequence Alignment by Genetic Algorithm) and WHAT-IF. Such alignment programs can also be used to screen genome databases to identify polynucleotide sequences having substantially identical sequences. A number of genome databases are available, for example, a substantial portion of the human genome is available as part of the Human Genome Sequencing Project (J. Roach,—available on the world wide web at weber.u.Washington.edu/ ̃roach/human_genome_progress—2.html) (Gibbs, 1995). At least twenty-one other genomes have already been sequenced, including, for example, M. genitalium (Fraser et al., 1995), M. jannaschii (Bult et al., 1996), H. influenzae (Fleischmann et al., 1995), E. coli (Blattner et al., 1997), and yeast (S. cerevisiae) (Mewes et al., 1997), and D. melanogaster (Adams et al., 2000). Significant progress has also been made in sequencing the genomes of model organism, such as mouse, C. elegans, and Arabadopsis sp. Several databases containing genomic information annotated with some functional information are maintained by different organizations, and are accessible on the world wide web, for example, at tigr.org/tdb; genetics.wisc.edu; genome-www.stanford.edu/-ball; hivweb.lanl.gov; ncbi.nlm.nih.gov; ebi.ac.uk; Pasteur.fr/other/biology; and genome.wi.mit.edu.
One example of a useful algorithm is BLAST and BLAST 2.0 algorithms, which are described in Altschul et al., Nuc. Acids Res. 25: 3389–3402, 1977, and Altschul et al., J. Mol. Biol. 215: 403–410, 1990, respectively. Software for performing BLAST analyses is publicly available through the National Center for Biotechnology Information (available on the world wide web at ncbi.nlm.nih.gov). This algorithm involves first identifying high scoring sequence pairs (HSPs) by identifying short words of length W in the query sequence, which either match or satisfy some positive-valued threshold score T when aligned with a word of the same length in a database sequence. T is referred to as the neighborhood word score threshold (Altschul et al., supra). These initial neighborhood word hits act as seeds for initiating searches to find longer HSPs containing them. The word hits are extended in both directions along each sequence for as far as the cumulative alignment score can be increased. Cumulative scores are calculated using, for nucleotide sequences, the parameters M (reward score for a pair of matching residues; always >0). For amino acid sequences, a scoring matrix is used to calculate the cumulative score. Extension of the word hits in each direction are halted when: the cumulative alignment score falls off by the quantity X from its maximum achieved value; the cumulative score goes to zero or below, due to the accumulation of one or more negative-scoring residue alignments; or the end of either sequence is reached. The BLAST algorithm parameters W, T, and X determine the sensitivity and speed of the alignment. The BLASTN program (for nucleotide sequences) uses as defaults a wordlength (W) of 11, an expectation (E) of 10, M=5, N=−4 and a comparison of both strands. For amino acid sequences, the BLASTP program uses as defaults a wordlength of 3, and expectations (E) of 10, and the BLOSUM62 scoring matrix (see Henikoff & Henikoff, Proc. Natl. Acad. Sci. USA 89: 10915, 1989) alignments (B) of 50, expectation (E) of 10, M=5, N=−4, and a comparison of both strands.
The BLAST algorithm also performs a statistical analysis of the similarity between two sequences (see, e.g., Karlin & Altschul, Proc. Natl. Acad. Sci. USA 90:5873, 1993). One measure of similarity provided by BLAST algorithm is the smallest sum probability (P(N)), which provides an indication of the probability by which a match between two nucleotide or amino acid sequences would occur by chance. For example, a nucleic acid is considered similar to a references sequence if the smallest sum probability in a comparison of the test nucleic acid to the reference nucleic acid is less than about 0.2, more preferably less than about 0.01, and most preferably less than about 0.001.
In one embodiment, protein and nucleic acid sequence homologies are evaluated using the Basic Local Alignment Search Tool (“BLAST”) In particular, five specific BLAST programs are used to perform the following task:

    
    
        (1) BLASTP and BLAST3 compare an amino acid query sequence against a protein sequence database;
        (2) BLASTN compares a nucleotide query sequence against a nucleotide sequence database;
        (3) BLASTX compares the six-frame conceptual translation products of a query nucleotide sequence (both strands) against a protein sequence database;
        (4) TBLASTN compares a query protein sequence against a nucleotide sequence database translated in all six reading frames (both strands); and
        (5) TBLASTX compares the six-frame translations of a nucleotide query sequence against the six-frame translations of a nucleotide sequence database.
    
    


The BLAST programs identify homologous sequences by identifying similar segments, which are referred to herein as “high-scoring segment pairs,” between a query amino or nucleic acid sequence and a test sequence which is preferably obtained from a protein or nucleic acid sequence database. High-scoring segment pairs are preferably identified (i.e., aligned) by means of a scoring matrix, many of which are known in the art. Preferably, the scoring matrix used is the BLOSUM62 matrix (Gonnet et al., Science 256: 1443–1445, 1992; Henikoff and Henikoff, Proteins 17:49–61, 1993). Less preferably, the PAM or PAM250 matrices may also be used (see, e.g., Schwartz and Dayhoff, eds., 1978, Matrices for Detecting Distance Relationships: Atlas of Protein Sequence and Structure, Washington: National Biomedical Research Foundation). BLAST programs are accessible through the U.S. National Library of Medicine, e.g., on the world wide web at ncbi.nlm.nih.gov.
The parameters used with the above algorithms may be adapted depending on the sequence length and degree of homology studied. In some embodiments, the parameters may be the default parameters used by the algorithms in the absence of instructions from the user.
By a “substantially pure polypeptide” is meant a synthase polypeptide (e.g., a chalcone synthase) which has been separated from components which naturally accompany it. Typically, the polypeptide is substantially pure when it is at least 60%, by weight, free from the proteins and naturally-occurring organic molecules with which it is naturally associated. Preferably, the preparation is at least 75%, more preferably at least 90%, and most preferably at least 99%, by weight, synthase polypeptide. A substantially pure synthase polypeptide may be obtained, for example, by extraction from a natural source; by expression of a recombinant nucleic acid encoding an synthase polypeptide; or by chemically synthesizing the protein. Purity can be measured by any appropriate method (e.g., column chromatography, polyacrylamide gel electrophoresis, or by HPLC analysis).
One aspect of the invention resides in obtaining crystals of the synthase polypeptide chalcone synthase of sufficient quality to determine the three dimensional (tertiary) structure of the protein by X-ray diffraction methods. The knowledge obtained concerning the three-dimensional structure of chalcone synthase can be used in the determination of the three dimensional structure of other synthase polypeptides in the polyketide synthesis pathway. The structural coordinates of chalcone synthase can be used to develop new polyketide synthesis enzymes or synthase inhibitors using various computer models. Based on the structural coordinates of the chalcone synthase polypeptide (e.g., the three dimensional protein structure), as described herein, novel polyketide synthases can be engineered. In addition, small molecules which mimic or are capable of interacting with a functional domain of a synthase molecule, can be designed and synthesized to modulate chalcone synthase, pyrone synthase, and other polyketide synthase biological functions as well as the biological functions of other polyketide synthases. Accordingly, in one embodiment, the invention provides a method of “rational” enzyme or drug design. Another approach to “rational” enzyme or drug design is based on a lead compound that is discovered using high throughput screens; the lead compound is further modified based on a crystal structure of the binding regions of the molecule in question. Accordingly, another aspect of the invention is to provide related protein sequences or material which is a starting material in the rational design of new synthases or drugs which lead to the synthesis of new polyketides or modify the polyketide synthesis pathway.
“Active Site” refers to a site in a synthase defined by amino acid residues that interact with substrate and facilitate a biosynthetic reaction that allows one or more products to be produced. An active site is comprised of α-carbon atoms that are indirectly linked via peptide bonds and have the structural coordinates disclosed in Table 1±2.3 angstroms. Other active site amino acids for chalcone synthase include C164, H303, and N336. The position in three-dimensional space of an α-carbon at the active site of a synthase and of R-groups associated therewith can be determined using techniques such as three-dimensional modeling, X-ray crystallography, and/or techniques associated therewith.
“Altered substrate specificity” includes a change in the ability of a mutant synthase to produce a polyketide product as compared to a non-mutated synthase. Altered substrate specificity may include the ability of a synthase to exhibit different enzymatic parameters relative to a non-mutated synthase (Km, Vmax. etc), use different substrates, and/or produce products that are different from those of known non-native synthases.
“Structure coordinates” refers to Cartesian coordinates (x, y, and z positions) derived from mathematical equations involving Fourier synthesis as determined from patterns obtained via diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of a polyketide synthase molecule in crystal form. Diffraction data are used to calculate electron density maps of repeating protein units in the crystal (unit cell). Electron density maps are used to establish the positions of individual atoms within a crystal's unit cell. The term “crystal structure coordinates” refers to 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 synthase polypeptide (e.g., a chalcone synthase protein 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. The crystal structure coordinates of a synthase can be obtained from a chalcone synthase protein crystal having space group P3221 (a=b=97.54 Å, c=65.52 with a single monomer per asymmetric unit). The coordinates of the cynthase polypeptide can also be obtained by means of computational analysis.
The term “selenomethionine substitution” refers to the method of producing a chemically modified form of the crystal of a synthase (e.g., a chalcone synthase). The synthase protein is expressed by bacteria in media that is depleted in methionine and supplement with selenomethionine. Selenium is thereby incorporated into the crystal in place of methionine sulfurs. The location(s) of selenium are determined by X-ray diffraction analysis of the crystal. This information is used to generate the phase information used to construct a three-dimensional structure of the protein.
“Heavy atom derivatization” refers to a method of producing a chemically modified form of a synthase crystal. In practice, a crystal is soaked in a solution containing heavy atom salts or organometallic compounds, e.g., lead chloride, gold thiomalate, thimerosal, uranyl acetate, and the like, which can diffuse through the crystal and bind to the protein's surface. Locations of the bound heavy atoms can be determined by X-ray diffraction analysis of the soaked crystal. This information is then used to construct phase information which can then be used to construct three-dimensional structures of the enzyme as described in Blundel, T. L., and Johnson, N. L., Protein Crystallography, Academic Press (1976), which is incorporated herein by reference.
“Unit cell” refers to a basic parallelepiped shaped block. Regular assembly of such blocks may construct the entire volume of a crystal. Each unit cell comprises a complete representation of the unit pattern, the repetition of which builds up the crystal.
“Mutagenesis” refers to the changing of one R-group for another as defined herein. This can be most easily performed by changing the coding sequence of the nucleic acid encoding the amino acid residue. In the context of the present invention, mutagenesis does not change the carbon coordinates beyond the limits defined herein.
“Space Group” refers to the arrangement of symmetry elements within a crystal.
“Molecular replacement” refers to generating a preliminary model of a polyketide synthase whose structural coordinates are unknown, by orienting and positioning a molecule whose structural 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 (Lattman, E., 1985, in Methods in Enzyrnology, 11 5.55–77; Rossmann, M G., ed., “The Molecular Replacement Method” 1972, Int, Sci. Rev. Ser., No. 13, Gordon & Breach, New York). Using structure coordinates of the polyketide synthase provided in FIG. 1 molecular replacement may be used to determine the structural coordinates of a crystalline mutant, homologue, or a different crystal form of polyketide synthase.
A “synthase” or a “polyketide synthase” includes any one of a family of enzymes that catalyze the formation of polyketide compounds. Polyketide synthases are generally homodimers, with each monomer being enzymatically active.
“Substrate” refers to the Coenzyme-A (CoA) thioesters that are acted on by the polyketide synthases and mutants thereof disclosed herein, such as malonyl-CoA, coumaroyl-CoA, hexamoyl-CoA, and the like.
The present invention relates to crystallized polyketide synthases and mutants thereof from which the position of specific α-carbon atoms and R-groups associated therewith comprising the active site can be determined in three-dimensional space.
The invention also relates to structural coordinates of said polyketide synthases, use of said structural coordinates to develop structural information related to polyketide synthase homologues, mutants, and the like, and to crystal forms of such synthases. Furthermore, the invention, as disclosed herein, provides a method whereby said α-carbon structural coordinates specifically determined for atoms comprising the active site of said synthase, as shown in Table 1 and including C164, H303, and N336 (SEQ ID NO:1), can be used to develop synthases wherein R-groups associated with active site α-carbon atoms are different from the R-groups found in native CHS (SEQ ID NO:1), e.g., are mutant synthases. In addition, the present invention provides for production of mutant polyketide synthases based on the structural information provided herein and for use of said mutant synthases to make a variety of polyketide compounds using a variety of substrates.
The present invention further provides, for the first time, crystals of several polyketide synthases, as exemplified by chalcone synthase (CHS; PDB Accession No. 1B15), stilbene synthase (STS), and pyrone synthase (PS); see Table 3 for coordinates of PS (“molecule” denoted in the table refers to the particular monomer of the PS dimer). Also provided are coordinates for crystals which are grown in the presence and absence of substrate and substrate analogues, thus allowing definition of the structural or atomic coordinates associated therewith. Said structural coordinates allow determination of the carbon atoms comprising the active site, R-groups associated therewith, and the interaction of said α-carbons and said R-groups with each other. For example, Table 4 identifies various substrates and substrate analogues that were grown with chalcone synthase as well as their PDB accession numbers, all of which are incorporated herein by reference in their entirety.







TABLE 3







(SEQ ID NO:1)

















Atom










Atom
Type
Res.
#
X
Y
Z
OCC
B
Molec



















1
N
GLY
20
32.834
42.457
65.617
1.00
27.09
A


2
CA
GLY
20
33.866
41.428
65.356
1.00
23.93
A


3
C
GLY
20
33.175
40.130
64.906
1.00
21.83
A


4
O
GLY
20
31.967
40.073
64.809
1.00
20.10
A


5
N
LEU
21
34.001
39.120
64.701
1.00
19.92
A


6
CA
LEU
21
33.519
37.812
64.301
1.00
21.97
A


7
CB
LEU
21
34.698
36.928
63.924
1.00
20.90
A


8
CG
LEU
21
35.592
37.425
62.769
1.00
25.38
A


9
CD2
LEU
21
34.861
37.362
61.428
1.00
26.08
A


10
CD1
LEU
21
36.862
36.561
62.728
1.00
24.02
A


11
C
LEU
21
32.710
37.113
65.406
1.00
22.68
A


12
O
LEU
21
33.076
37.172
66.591
1.00
21.48
A


13
N
ALA
22
31.662
36.430
64.988
1.00
19.98
A


14
CA
ALA
22
30.941
35.520
65.863
1.00
19.22
A


15
CB
ALA
22
29.897
34.702
65.083
1.00
16.98
A


16
C
ALA
22
31.951
34.602
66.522
1.00
18.97
A


17
O
ALA
22
32.771
33.961
65.852
1.00
19.26
A


18
N
THR
23
31.887
34.515
67.854
1.00
17.74
A


19
CA
THR
23
32.840
33.659
68.577
1.00
15.74
A


20
CB
THR
23
33.699
34.563
69.497
1.00
17.10
A


21
OG1
THR
23
34.155
35.652
68.678
1.00
16.29
A


22
CG2
THR
23
34.824
33.809
70.184
1.00
18.53
A


23
C
THR
23
32.138
32.654
69.465
1.00
16.14
A


24
O
THR
23
31.100
32.951
70.060
1.00
15.79
A


25
N
ILE
24
32.680
31.455
69.500
1.00
15.97
A


26
CA
ILE
24
32.183
30.385
70.313
1.00
18.48
A


27
CB
ILE
24
32.620
29.024
69.816
1.00
17.83
A


28
CG2
ILE
24
32.097
27.975
70.825
1.00
18.50
A


29
CG1
ILE
24
32.052
28.700
68.408
1.00
18.53
A


30
CD1
ILE
24
32.633
27.424
67.841
1.00
16.89
A


31
C
ILE
24
32.790
30.650
71.729
1.00
20.41
A


32
O
ILE
24
34.005
30.764
71.810
1.00
19.04
A


33
N
LEU
25
31.928
30.814
72.709
1.00
20.83
A


34
CA
LEU
25
32.236
31.175
74.068
1.00
20.33
A


35
CB
LEU
25
31.368
32.388
74.458
1.00
19.36
A


36
CG
LEU
25
31.475
33.620
73.571
1.00
19.02
A


37
CD2
LEU
25
32.876
34.236
73.516
1.00
19.47
A


38
CD1
LEU
25
30.514
34.693
74.104
1.00
17.79
A


39
C
LEU
25
32.009
30.093
75.092
1.00
19.34
A


40
O
LEU
25
32.480
30.255
76.215
1.00
17.65
A


41
N
ALA
26
31.231
29.051
74.796
1.00
17.56
A


42
CA
ALA
26
31.065
27.958
75.712
1.00
18.21
A


43
CB
ALA
26
30.071
28.315
76.844
1.00
16.77
A


44
C
ALA
26
30.487
26.777
74.961
1.00
20.23
A


45
O
ALA
26
29.882
26.972
73.895
1.00
18.85
A


46
N
ILE
27
30.855
25.588
75.429
1.00
18.15
A


47
CA
ILE
27
30.356
24.366
74.843
1.00
19.79
A


48
CB
ILE
27
31.390
23.696
73.930
1.00
18.91
A


49
CG2
ILE
27
30.719
22.521
73.240
1.00
17.49
A


50
CG1
ILE
27
31.984
24.650
72.859
1.00
17.58
A


51
CD1
ILE
27
33.157
24.057
72.094
1.00
17.89
A


52
C
ILE
27
29.968
23.380
75.929
1.00
19.93
A


53
O
ILE
27
30.842
23.024
76.725
1.00
20.00
A


54
N
GLY
28
28.798
22.788
75.853
1.00
19.91
A


55
CA
GLY
28
28.297
21.759
76.759
1.00
18.80
A


56
C
GLY
28
27.802
20.540
75.993
1.00
20.61
A


57
O
GLY
28
27.170
20.667
74.905
1.00
19.24
A


58
N
THR
29
28.111
19.333
76.457
1.00
16.87
A


59
CA
THR
29
27.545
18.133
75.816
1.00
19.02
A


60
CB
THR
29
28.603
17.320
75.080
1.00
20.16
A


61
OG1
THR
29
29.629
16.843
75.950
1.00
21.21
A


62
CG2
THR
29
29.373
18.154
74.032
1.00
20.41
A


63
C
THR
29
26.787
17.267
76.813
1.00
20.90
A


64
O
THR
29
27.106
17.274
78.025
1.00
22.12
A


65
N
ALA
30
25.942
16.358
76.393
1.00
17.49
A


66
CA
ALA
30
25.211
15.395
77.185
1.00
17.35
A


67
CB
ALA
30
23.866
15.947
77.664
1.00
14.17
A


68
C
ALA
30
24.876
14.187
76.310
1.00
18.08
A


69
O
ALA
30
24.631
14.306
75.082
1.00
17.60
A


70
N
THR
31
24.696
13.046
76.908
1.00
19.58
A


71
CA
THR
31
24.246
11.823
76.246
1.00
19.85
A


72
CB
THR
31
25.412
10.856
76.014
1.00
21.41
A


73
OG1
THR
31
26.049
10.534
77.282
1.00
26.09
A


74
CG2
THR
31
26.542
11.344
75.122
1.00
19.56
A


75
C
THR
31
23.225
11.139
77.136
1.00
22.26
A


76
O
THR
31
23.198
11.407
78.329
1.00
20.45
A


77
N
PRO
32
22.355
10.302
76.602
1.00
21.50
A


78
CA
PRO
32
21.537
9.421
77.401
1.00
21.71
A


79
CD
PRO
32
22.201
10.080
75.137
1.00
21.81
A


80
CB
PRO
32
20.893
8.493
76.344
1.00
19.90
A


81
CG
PRO
32
20.880
9.325
75.091
1.00
21.81
A


82
C
PRO
32
22.424
8.561
78.299
1.00
22.41
A


83
O
PRO
32
23.584
8.337
77.979
1.00
22.75
A


84
N
PRO
33
21.905
8.074
79.421
1.00
24.52
A


85
CA
PRO
33
22.653
7.254
80.353
1.00
26.49
A


86
CD
PRO
33
20.524
8.372
79.888
1.00
24.57
A


87
CB
PRO
33
21.713
7.159
81.571
1.00
26.31
A


88
CG
PRO
33
20.346
7.355
81.014
1.00
27.68
A


89
C
PRO
33
23.045
5.870
79.845
1.00
27.55
A


90
O
PRO
33
24.179
5.435
80.070
1.00
28.73
A


91
N
ASN
34
22.175
5.154
79.163
1.00
29.66
A


92
CA
ASN
34
22.410
3.783
78.649
1.00
32.41
A


93
CB
ASN
34
21.101
3.280
78.056
1.00
36.26
A


94
CG
ASN
34
20.948
2.142
77.083
1.00
38.95
A


95
OD1
ASN
34
21.662
1.127
77.183
1.00
39.62
A


96
ND2
ASN
34
19.989
2.192
76.138
1.00
35.37
A


97
C
ASN
34
23.523
3.807
77.609
1.00
32.31
A


98
O
ASN
34
23.469
4.526
76.610
1.00
29.54
A


99
N
CYS
35
24.576
3.052
77.829
1.00
30.93
A


100
CA
CYS
35
25.723
2.919
76.965
1.00
31.69
A


101
CB
CYS
35
26.917
3.153
77.906
1.00
35.11
A


102
SG
CYS
35
28.474
3.296
77.056
1.00
37.85
A


103
C
CYS
35
25.768
1.499
76.438
1.00
31.58
A


104
O
CYS
35
25.523
0.623
77.272
1.00
31.97
A


105
N
VAL
36
26.041
1.225
75.182
1.00
30.94
A


106
CA
VAL
36
26.161
−0.144
74.669
1.00
31.93
A


107
CB
VAL
36
25.047
−0.605
73.706
1.00
32.84
A


108
CG1
VAL
36
25.372
−1.969
73.087
1.00
33.47
A


109
CG2
VAL
36
23.689
−0.721
74.407
1.00
33.32
A


110
C
VAL
36
27.500
−0.299
73.944
1.00
31.29
A


111
O
VAL
36
27.768
0.506
73.036
1.00
30.05
A


112
N
ALA
37
28.310
−1.286
74.343
1.00
30.79
A


113
CA
ALA
37
29.594
−1.466
73.680
1.00
29.79
A


114
CB
ALA
37
30.543
−2.436
74.385
1.00
29.23
A


115
C
ALA
37
29.342
−1.982
72.250
1.00
28.16
A


116
O
ALA
37
28.620
−2.955
72.083
1.00
26.46
A


117
N
GLN
38
30.143
−1.521
71.312
1.00
28.15
A


118
CA
GLN
38
30.007
−1.958
69.912
1.00
27.67
A


119
CB
GLN
38
30.846
−1.049
69.021
1.00
28.50
A


120
CG
GLN
38
30.657
−1.221
67.506
1.00
26.41
A


121
CD
GLN
38
29.350
−0.581
67.053
1.00
27.26
A


122
OE1
GLN
38
28.360
−0.689
67.767
1.00
26.46
A


123
NE2
GLN
38
29.296
0.067
65.877
1.00
25.63
A


124
C
GLN
38
30.382
−3.409
69.734
1.00
29.10
A


125
O
GLN
38
29.688
−4.212
69.107
1.00
27.00
A


126
N
ALA
39
31.355
−3.895
70.531
1.00
31.28
A


127
CA
ALA
39
31.738
−5.301
70.547
1.00
31.16
A


128
CB
ALA
39
32.950
−5.519
71.448
1.00
32.49
A


129
C
ALA
39
30.592
−6.189
71.009
1.00
32.31
A


130
O
ALA
39
30.519
−7.353
70.605
1.00
34.94
A


131
N
ASP
40
29.574
−5.650
71.681
1.00
31.27
A


132
CA
ASP
40
28.403
−6.433
72.036
1.00
32.18
A


133
CB
ASP
40
28.042
−6.187
73.503
1.00
33.60
A


134
CG
ASP
40
29.167
−6.530
74.462
1.00
35.07
A


135
OD1
ASP
40
29.914
−7.480
74.174
1.00
35.48
A


136
OD2
ASP
40
29.312
−5.832
75.481
1.00
36.82
A


137
C
ASP
40
27.156
−6.106
71.203
1.00
30.15
A


138
O
ASP
40
26.137
−6.760
71.362
1.00
27.91
A


139
N
TYR
41
27.225
−5.055
70.383
1.00
29.82
A


140
CA
TYR
41
26.045
−4.632
69.634
1.00
27.44
A


141
CB
TYR
41
26.336
−3.302
68.891
1.00
28.10
A


142
CG
TYR
41
24.958
−2.680
68.620
1.00
28.23
A


143
CD1
TYR
41
24.354
−1.940
69.628
1.00
28.38
A


144
CD2
TYR
41
24.306
−2.853
67.404
1.00
26.85
A


145
CE1
TYR
41
23.104
−1.367
69.427
1.00
30.06
A


146
CE2
TYR
41
23.066
−2.289
67.183
1.00
27.54
A


147
CZ
TYR
41
22.468
−1.558
68.190
1.00
30.20
A


148
OH
TYR
41
21.230
−0.987
68.015
1.00
31.22
A


149
C
TYR
41
25.416
−5.639
68.706
1.00
26.97
A


150
O
TYR
41
24.185
−5.796
68.753
1.00
24.64
A


151
N
ALA
42
26.191
−6.432
67.949
1.00
27.02
A


152
CA
ALA
42
25.599
−7.424
67.061
1.00
27.20
A


153
CB
ALA
42
26.651
−8.140
66.232
1.00
26.68
A


154
C
ALA
42
24.723
−8.413
67.805
1.00
28.00
A


155
O
ALA
42
23.616
−8.774
67.405
1.00
26.11
A


156
N
ASP
43
25.240
−8.969
68.907
1.00
30.84
A


157
CA
ASP
43
24.475
−9.891
69.734
1.00
31.33
A


158
CB
ASP
43
25.385
−10.470
70.825
1.00
34.03
A


159
CG
ASP
43
26.273
−11.584
70.276
1.00
36.27
A


160
OD1
ASP
43
27.305
−11.885
70.905
1.00
37.42
A


161
OD2
ASP
43
25.960
−12.163
69.214
1.00
37.57
A


162
C
ASP
43
23.237
−9.246
70.351
1.00
30.78
A


163
O
ASP
43
22.130
−9.796
70.356
1.00
31.39
A


164
N
TYR
44
23.350
−8.026
70.836
1.00
28.82
A


165
CA
TYR
44
22.211
−7.302
71.395
1.00
30.46
A


166
CB
TYR
44
22.687
−5.932
71.934
1.00
31.63
A


167
CG
TYR
44
21.497
−5.043
72.238
1.00
34.09
A


168
CD1
TYR
44
20.706
−5.350
73.352
1.00
34.43
A


169
CD2
TYR
44
21.139
−3.967
71.435
1.00
33.42
A


170
CE1
TYR
44
19.606
−4.577
73.661
1.00
35.43
A


171
CE2
TYR
44
20.031
−3.205
71.749
1.00
35.16
A


172
CZ
TYR
44
19.266
−3.514
72.859
1.00
35.11
A


173
OH
TYR
44
18.149
−2.773
73.173
1.00
36.24
A


174
C
TYR
44
21.124
−7.090
70.351
1.00
28.76
A


175
O
TYR
44
19.933
−7.443
70.461
1.00
29.56
A


176
N
TYR
45
21.556
−6.598
69.182
1.00
28.20
A


177
CA
TYR
45
20.616
−6.219
68.115
1.00
25.74
A


178
CB
TYR
45
21.435
−5.417
67.073
1.00
26.31
A


179
CG
TYR
45
20.733
−5.127
65.770
1.00
25.68
A


180
CD1
TYR
45
19.830
−4.066
65.699
1.00
25.75
A


181
CD2
TYR
45
20.938
−5.887
64.626
1.00
26.97
A


182
CE1
TYR
45
19.165
−3.757
64.534
1.00
26.81
A


183
CE2
TYR
45
20.273
−5.584
63.439
1.00
27.53
A


184
CZ
TYR
45
19.389
−4.531
63.406
1.00
26.52
A


185
OH
TYR
45
18.722
−4.205
62.248
1.00
25.82
A


186
C
TYR
45
19.800
−7.359
67.578
1.00
25.23
A


187
O
TYR
45
18.547
−7.365
67.499
1.00
25.18
A


188
N
PHE
46
20.460
−8.466
67.240
1.00
25.33
A


189
CA
PHE
46
19.805
−9.655
66.710
1.00
26.13
A


190
CB
PHE
46
20.872
−10.562
66.065
1.00
25.99
A


191
CG
PHE
46
21.118
−10.169
64.623
1.00
24.71
A


192
CD1
PHE
46
21.993
−9.158
64.295
1.00
24.42
A


193
CD2
PHE
46
20.408
−10.779
63.609
1.00
25.49
A


194
CE1
PHE
46
22.221
−8.832
62.952
1.00
24.01
A


195
CE2
PHE
46
20.609
−10.411
62.272
1.00
26.54
A


196
CZ
PHE
46
21.473
−9.380
61.941
1.00
22.32
A


197
C
PHE
46
18.980
−10.383
67.767
1.00
28.00
A


198
O
PHE
46
17.944
−10.985
67.459
1.00
29.01
A


199
N
ARG
47
19.297
−10.167
69.014
1.00
27.89
A


200
CA
ARG
47
18.537
−10.764
70.120
1.00
29.09
A


201
CB
ARG
47
19.399
−10.735
71.377
1.00
31.22
A


202
CG
ARG
47
18.961
−11.670
72.511
1.00
32.64
A


203
CD
ARG
47
19.652
−11.266
73.821
1.00
34.71
A


204
NE
ARG
47
18.780
−10.430
74.611
1.00
36.52
A


205
CZ
ARG
47
19.000
−9.232
75.181
1.00
36.76
A


206
NH1
ARG
47
20.169
−8.598
75.167
1.00
36.52
A


207
NH2
ARG
47
18.003
−8.579
75.805
1.00
38.61
A


208
C
ARG
47
17.230
−9.970
70.323
1.00
29.38
A


209
O
ARG
47
16.130
−10.531
70.338
1.00
27.87
A


210
N
VAL
48
17.371
−8.614
70.501
1.00
31.39
A


211
CA
VAL
48
16.155
−7.803
70.723
1.00
31.67
A


212
CB
VAL
48
16.483
−6.382
71.230
1.00
32.60
A


213
CG1
VAL
48
17.272
−6.551
72.529
1.00
34.07
A


214
CG2
VAL
48
17.262
−5.532
70.225
1.00
31.26
A


215
C
VAL
48
15.235
−7.692
69.524
1.00
31.64
A


216
O
VAL
48
14.027
−7.461
69.678
1.00
31.80
A


217
N
THR
49
15.773
−7.869
68.326
1.00
30.64
A


218
CA
THR
49
14.909
−7.845
67.137
1.00
31.47
A


219
CB
THR
49
15.625
−7.226
65.928
1.00
29.40
A


220
OG1
THR
49
16.731
−8.068
65.630
1.00
28.79
A


221
CG2
THR
49
16.076
−5.809
66.244
1.00
29.44
A


222
C
THR
49
14.501
−9.264
66.767
1.00
32.37
A


223
O
THR
49
13.890
−9.440
65.735
1.00
31.92
A


224
N
LYS
50
14.803
−10.271
67.599
1.00
35.30
A


225
CA
LYS
50
14.352
−11.635
67.379
1.00
36.93
A


226
CB
LYS
50
12.830
−11.671
67.617
1.00
39.91
A


227
CG
LYS
50
12.448
−11.295
69.053
1.00
43.14
A


228
CD
LYS
50
10.925
−11.120
69.148
1.00
46.09
A


229
CE
LYS
50
10.531
−10.612
70.521
1.00
48.94
A


230
NZ
LYS
50
9.159
−11.061
70.920
1.00
51.49
A


231
C
LYS
50
14.703
−12.190
65.998
1.00
36.27
A


232
O
LYS
50
13.882
−12.803
65.304
1.00
35.23
A


233
N
SER
51
15.952
−11.983
65.588
1.00
34.72
A


234
CA
SER
51
16.357
−12.292
64.227
1.00
36.62
A


235
CB
SER
51
16.761
−11.007
63.490
1.00
35.04
A


236
OG
SER
51
15.632
−10.153
63.401
1.00
35.75
A


237
C
SER
51
17.530
−13.264
64.196
1.00
37.21
A


238
O
SER
51
18.250
−13.326
63.202
1.00
35.82
A


239
N
GLU
52
17.644
−14.064
65.250
1.00
37.90
A


240
CA
GLU
52
18.726
−15.024
65.378
1.00
41.24
A


241
CB
GLU
52
18.664
−15.821
66.687
1.00
41.73
A


242
CG
GLU
52
18.714
−14.913
67.912
1.00
43.24
A


243
CD
GLU
52
20.093
−14.326
68.139
1.00
43.08
A


244
OE1
GLU
52
20.922
−14.295
67.206
1.00
43.85
A


245
OE2
GLU
52
20.335
−13.886
69.276
1.00
42.33
A


246
C
GLU
52
18.852
−16.016
64.237
1.00
41.56
A


247
O
GLU
52
19.962
−16.418
63.923
1.00
41.47
A


248
N
HIS
53
17.765
−16.368
63.591
1.00
43.15
A


249
CA
HIS
53
17.757
−17.277
62.462
1.00
46.02
A


250
ND1
HIS
53
15.020
−15.790
63.161
1.00
57.14
A


251
CG
HIS
53
15.414
−16.524
62.053
1.00
55.58
A


252
CB
HIS
53
16.321
−17.714
62.158
1.00
50.66
A


253
NE2
HIS
53
14.105
−14.866
61.430
1.00
57.55
A


254
CD2
HIS
53
14.842
−15.934
60.966
1.00
57.42
A


255
CE1
HIS
53
14.232
−14.810
62.745
1.00
58.02
A


256
C
HIS
53
18.409
−16.654
61.237
1.00
44.57
A


257
O
HIS
53
18.924
−17.441
60.437
1.00
44.24
A


258
N
MET
54
18.572
−15.331
61.178
1.00
41.09
A


259
CA
MET
54
19.348
−14.712
60.113
1.00
40.86
A


260
CB
MET
54
18.865
−13.279
59.877
1.00
39.34
A


261
CG
MET
54
17.345
−13.172
59.756
1.00
38.82
A


262
SD
MET
54
16.834
−11.433
59.565
1.00
38.46
A


263
CE
MET
54
15.087
−11.625
59.282
1.00
39.63
A


264
C
MET
54
20.843
−14.743
60.444
1.00
38.70
A


265
O
MET
54
21.471
−13.709
60.604
1.00
36.96
A


266
N
VAL
55
21.423
−15.930
60.471
1.00
37.47
A


267
CA
VAL
55
22.806
−16.179
60.826
1.00
38.20
A


268
CB
VAL
55
23.074
−17.704
60.781
1.00
37.95
A


269
CG1
VAL
55
24.539
−18.029
60.988
1.00
37.15
A


270
CG2
VAL
55
22.200
−18.366
61.852
1.00
38.75
A


271
C
VAL
55
23.808
−15.423
59.964
1.00
37.34
A


272
O
VAL
55
24.678
−14.746
60.485
1.00
35.85
A


273
N
ASP
56
23.671
−15.506
58.651
1.00
37.85
A


274
CA
ASP
56
24.592
−14.871
57.712
1.00
40.33
A


275
CB
ASP
56
24.342
−15.403
56.297
1.00
44.16
A


276
CG
ASP
56
24.760
−16.863
56.131
1.00
48.56
A


277
OD1
ASP
56
25.297
−17.563
57.035
1.00
49.83
A


278
OD2
ASP
56
24.494
−17.330
54.992
1.00
50.70
A


279
C
ASP
56
24.537
−13.352
57.759
1.00
38.30
A


280
O
ASP
56
25.568
−12.680
57.818
1.00
38.20
A


281
N
LEU
57
23.340
−12.789
57.909
1.00
35.70
A


282
CA
LEU
57
23.179
−11.369
58.144
1.00
34.76
A


283
CB
LEU
57
21.700
−10.988
58.141
1.00
36.41
A


284
CG
LEU
57
21.328
−9.731
57.367
1.00
38.75
A


285
CD2
LEU
57
19.810
−9.657
57.233
1.00
39.19
A


286
CD1
LEU
57
21.984
−9.704
55.983
1.00
38.62
A


287
C
LEU
57
23.777
−10.975
59.492
1.00
31.73
A


288
O
LEU
57
24.409
−9.936
59.642
1.00
30.50
A


289
N
LYS
58
23.517
−11.816
60.504
1.00
30.83
A


290
CA
LYS
58
24.186
−11.616
61.791
1.00
29.23
A


291
CB
LYS
58
23.802
−12.695
62.816
1.00
29.15
A


292
CG
LYS
58
24.327
−12.284
64.198
1.00
29.77
A


293
CD
LYS
58
23.767
−13.189
65.296
1.00
28.95
A


294
CE
LYS
58
24.413
−12.778
66.620
1.00
29.21
A


295
NZ
LYS
58
23.929
−13.667
67.738
1.00
30.34
A


296
C
LYS
58
25.691
−11.592
61.599
1.00
28.39
A


297
O
LYS
58
26.412
−10.672
62.017
1.00
26.22
A


298
N
GLU
59
26.223
−12.590
60.873
1.00
28.92
A


299
CA
GLU
59
27.676
−12.592
60.652
1.00
30.78
A


300
CB
GLU
59
28.071
−13.810
59.789
1.00
36.02
A


301
CG
GLU
59
28.228
−15.069
60.615
1.00
41.00
A


302
CD
GLU
59
29.133
−14.949
61.820
1.00
43.84
A


303
OE1
GLU
59
30.081
−14.148
61.926
1.00
46.35
A


304
OE2
GLU
59
28.890
−15.739
62.770
1.00
47.23
A


305
C
GLU
59
28.131
−11.334
59.950
1.00
28.91
A


306
O
GLU
59
29.200
−10.804
60.211
1.00
26.29
A


307
N
LYS
60
27.365
−10.903
58.932
1.00
27.65
A


308
CA
LYS
60
27.756
−9.676
58.235
1.00
28.35
A


309
CB
LYS
60
26.908
−9.608
56.978
1.00
31.60
A


310
CG
LYS
60
26.369
−8.247
56.605
1.00
34.59
A


311
CD
LYS
60
27.107
−7.755
55.389
1.00
36.17
A


312
CE
LYS
60
26.120
−7.195
54.355
1.00
34.07
A


313
NZ
LYS
60
26.854
−7.291
53.037
1.00
30.49
A


314
C
LYS
60
27.622
−8.441
59.120
1.00
27.63
A


315
O
LYS
60
28.495
−7.592
59.158
1.00
25.96
A


316
N
PHE
61
26.605
−8.378
59.980
1.00
27.76
A


317
CA
PHE
61
26.533
−7.279
60.954
1.00
27.20
A


318
CB
PHE
61
25.175
−7.344
61.691
1.00
26.83
A


319
CG
PHE
61
24.870
−6.020
62.361
1.00
25.57
A


320
CD1
PHE
61
24.793
−4.848
61.636
1.00
23.19
A


321
CD2
PHE
61
24.705
−5.974
63.742
1.00
25.42
A


322
CE1
PHE
61
24.589
−3.642
62.279
1.00
22.77
A


323
CE2
PHE
61
24.431
−4.765
64.394
1.00
24.47
A


324
CZ
PHE
61
24.410
−3.600
63.658
1.00
23.21
A


325
C
PHE
61
27.706
−7.291
61.918
1.00
27.60
A


326
O
PHE
61
28.204
−6.228
62.306
1.00
25.06
A


327
N
LYS
62
28.248
−8.470
62.281
1.00
28.63
A


328
CA
LYS
62
29.440
−8.434
63.161
1.00
30.01
A


329
CB
LYS
62
29.817
−9.798
63.712
1.00
33.50
A


330
CG
LYS
62
28.933
−10.363
64.817
1.00
36.21
A


331
CD
LYS
62
29.313
−11.795
65.201
1.00
39.57
A


332
CE
LYS
62
28.868
−12.139
66.632
1.00
42.71
A


333
NZ
LYS
62
28.743
−13.618
66.867
1.00
43.80
A


334
C
LYS
62
30.633
−7.820
62.432
1.00
27.66
A


335
O
LYS
62
31.408
−7.040
62.961
1.00
25.63
A


336
N
ARG
63
30.812
−8.129
61.160
1.00
28.40
A


337
CA
ARG
63
31.886
−7.532
60.345
1.00
26.83
A


338
CB
ARG
63
31.923
−8.166
58.949
1.00
28.80
A


339
CG
ARG
63
32.205
−9.670
58.860
1.00
31.04
A


340
CD
ARG
63
32.605
−10.075
57.429
1.00
31.67
A


341
NE
ARG
63
31.458
−10.007
56.496
1.00
31.18
A


342
CZ
ARG
63
30.568
−10.993
56.412
1.00
33.98
A


343
NH1
ARG
63
30.675
−12.080
57.183
1.00
33.69
A


344
NH2
ARG
63
29.552
−10.945
55.537
1.00
35.02
A


345
C
ARG
63
31.725
−6.028
60.234
1.00
26.47
A


346
O
ARG
63
32.707
−5.281
60.285
1.00
27.57
A


347
N
ILE
64
30.517
−5.531
59.967
1.00
26.34
A


348
CA
ILE
64
30.285
−4.079
59.832
1.00
25.94
A


349
CB
ILE
64
28.797
−3.821
59.461
1.00
25.49
A


350
CG2
ILE
64
28.386
−2.381
59.606
1.00
25.16
A


351
CG1
ILE
64
28.502
−4.295
58.011
1.00
24.16
A


352
CD1
ILE
64
27.030
−4.611
57.772
1.00
20.75
A


353
C
ILE
64
30.604
−3.364
61.149
1.00
26.57
A


354
O
ILE
64
31.299
−2.343
61.183
1.00
25.13
A


355
N
CYS
65
30.119
−3.920
62.268
1.00
25.79
A


356
CA
CYS
65
30.373
−3.275
63.569
1.00
29.16
A


357
CB
CYS
65
29.703
−4.001
64.744
1.00
27.03
A


358
SG
CYS
65
27.900
−3.813
64.788
1.00
27.03
A


359
C
CYS
65
31.870
−3.230
63.861
1.00
29.65
A


360
O
CYS
65
32.384
−2.241
64.393
1.00
27.74
A


361
N
GLU
66
32.557
−4.333
63.495
1.00
32.64
A


362
CA
GLU
66
34.017
−4.324
63.693
1.00
34.70
A


363
CB
GLU
66
34.616
−5.684
63.344
1.00
38.03
A


364
CG
GLU
66
36.078
−5.831
63.720
1.00
42.01
A


365
CD
GLU
66
37.051
−5.375
62.644
1.00
45.51
A


366
OE1
GLU
66
36.749
−5.306
61.421
1.00
45.11
A


367
OE2
GLU
66
38.211
−5.061
63.034
1.00
47.20
A


368
C
GLU
66
34.645
−3.235
62.842
1.00
33.45
A


369
O
GLU
66
35.633
−2.642
63.271
1.00
34.26
A


370
N
LYS
67
34.187
−2.990
61.610
1.00
31.58
A


371
CA
LYS
67
34.775
−1.966
60.759
1.00
30.20
A


372
CB
LYS
67
34.159
−2.078
59.335
1.00
30.36
A


373
CG
LYS
67
34.698
−3.350
58.673
1.00
31.77
A


374
CD
LYS
67
36.139
−3.095
58.230
1.00
30.35
A


375
CE
LYS
67
36.519
−4.248
57.282
1.00
32.61
A


376
NZ
LYS
67
37.969
−4.223
56.965
1.00
31.38
A


377
C
LYS
67
34.530
−0.539
61.207
1.00
28.50
A


378
O
LYS
67
35.301
0.330
60.826
1.00
26.35
A


379
N
THR
68
33.485
−0.253
61.990
1.00
28.16
A


380
CA
THR
68
33.117
1.117
62.321
1.00
26.38
A


381
CB
THR
68
31.755
1.142
63.079
1.00
28.00
A


382
OG1
THR
68
31.822
0.406
64.297
1.00
25.98
A


383
CG2
THR
68
30.640
0.516
62.232
1.00
26.36
A


384
C
THR
68
34.127
1.962
63.067
1.00
26.03
A


385
O
THR
68
34.035
3.198
63.074
1.00
23.26
A


386
N
ALA
69
35.020
1.367
63.862
1.00
25.08
A


387
CA
ALA
69
35.959
2.110
64.689
1.00
26.12
A


388
CB
ALA
69
36.881
3.014
63.885
1.00
24.83
A


389
C
ALA
69
35.146
2.920
65.730
1.00
25.89
A


390
O
ALA
69
35.516
4.026
66.108
1.00
25.89
A


391
N
ILE
70
34.088
2.282
66.214
1.00
25.60
A


392
CA
ILE
70
33.264
2.842
67.291
1.00
25.62
A


393
CB
ILE
70
31.757
2.933
66.959
1.00
24.18
A


394
CG2
ILE
70
30.904
3.310
68.168
1.00
21.69
A


395
CG1
ILE
70
31.559
3.928
65.795
1.00
22.58
A


396
CD1
ILE
70
30.160
3.904
65.163
1.00
20.62
A


397
C
ILE
70
33.454
1.913
68.493
1.00
25.45
A


398
O
ILE
70
33.249
0.715
68.340
1.00
23.85
A


399
N
LYS
71
33.762
2.463
69.667
1.00
26.85
A


400
CA
LYS
71
33.835
1.597
70.865
1.00
28.48
A


401
CB
LYS
71
34.913
2.162
71.797
1.00
31.60
A


402
CG
LYS
71
35.196
1.430
73.078
1.00
34.19
A


403
CD
LYS
71
36.308
2.012
73.935
1.00
36.61
A


404
CE
LYS
71
37.382
2.812
73.249
1.00
38.89
A


405
NZ
LYS
71
38.738
2.685
73.870
1.00
42.37
A


406
C
LYS
71
32.506
1.455
71.584
1.00
27.13
A


407
O
LYS
71
32.183
0.367
72.087
1.00
27.37
A


408
N
LYS
72
31.724
2.520
71.728
1.00
25.23
A


409
CA
LYS
72
30.442
2.474
72.414
1.00
25.15
A


410
CB
LYS
72
30.572
2.715
73.924
1.00
26.70
A


411
CG
LYS
72
31.332
3.981
74.244
1.00
28.08
A


412
CD
LYS
72
31.600
4.138
75.752
1.00
31.06
A


413
CE
LYS
72
32.583
5.268
75.965
1.00
34.19
A


414
NZ
LYS
72
32.080
6.648
75.842
1.00
30.79
A


415
C
LYS
72
29.588
3.650
71.915
1.00
24.42
A


416
O
LYS
72
30.117
4.578
71.299
1.00
20.97
A


417
N
ARG
73
28.302
3.536
72.187
1.00
22.40
A


418
CA
ARG
73
27.331
4.559
71.833
1.00
23.39
A


419
CB
ARG
73
26.539
4.093
70.579
1.00
22.84
A


420
CG
ARG
73
27.403
4.138
69.304
1.00
23.07
A


421
CD
ARG
73
26.641
3.582
68.115
1.00
24.33
A


422
NE
ARG
73
26.448
2.175
67.974
1.00
21.31
A


423
CZ
ARG
73
25.538
1.589
67.211
1.00
22.61
A


424
NH1
ARG
73
25.470
0.280
67.165
1.00
21.98
A


425
NH2
ARG
73
24.660
2.250
66.446
1.00
23.67
A


426
C
ARG
73
26.362
4.735
73.009
1.00
21.07
A


427
O
ARG
73
25.989
3.699
73.545
1.00
20.95
A


428
N
TYR
74
25.869
5.907
73.273
1.00
20.99
A


429
CA
TYR
74
24.812
6.072
74.270
1.00
20.56
A


430
CB
TYR
74
25.038
7.416
74.957
1.00
21.25
A


431
CG
TYR
74
26.352
7.376
75.718
1.00
23.79
A


432
CD1
TYR
74
27.511
7.806
75.099
1.00
25.16
A


433
CD2
TYR
74
26.369
6.913
77.030
1.00
23.96
A


434
CE1
TYR
74
28.712
7.779
75.806
1.00
27.20
A


435
CE2
TYR
74
27.563
6.900
77.752
1.00
24.67
A


436
CZ
TYR
74
28.701
7.327
77.131
1.00
26.17
A


437
OH
TYR
74
29.894
7.334
77.795
1.00
28.39
A


438
C
TYR
74
23.464
6.090
73.583
1.00
20.11
A


439
O
TYR
74
23.401
6.600
72.434
1.00
22.54
A


440
N
LEU
75
22.467
5.355
74.035
1.00
20.26
A


441
CA
LEU
75
21.201
5.266
73.291
1.00
22.57
A


442
CB
LEU
75
21.119
3.864
72.671
1.00
22.46
A


443
CG
LEU
75
22.251
3.500
71.686
1.00
22.93
A


444
CD2
LEU
75
21.988
4.281
70.390
1.00
22.07
A


445
CD1
LEU
75
22.304
1.995
71.423
1.00
22.36
A


446
C
LEU
75
20.032
5.489
74.242
1.00
24.64
A


447
O
LEU
75
19.972
4.805
75.265
1.00
23.88
A


448
N
ALA
76
19.129
6.383
73.895
1.00
22.83
A


449
CA
ALA
76
17.935
6.662
74.660
1.00
24.54
A


450
CB
ALA
76
17.287
7.977
74.206
1.00
22.44
A


451
C
ALA
76
16.935
5.535
74.428
1.00
24.70
A


452
O
ALA
76
16.159
5.190
75.303
1.00
25.26
A


453
N
LEU
77
17.018
4.839
73.284
1.00
23.09
A


454
CA
LEU
77
16.187
3.672
73.024
1.00
22.26
A


455
CB
LEU
77
16.375
3.085
71.623
1.00
23.19
A


456
CG
LEU
77
15.196
2.566
70.826
1.00
25.81
A


457
CD2
LEU
77
13.985
2.125
71.624
1.00
24.97
A


458
CD1
LEU
77
15.597
1.526
69.775
1.00
26.58
A


459
C
LEU
77
16.565
2.512
73.969
1.00
22.32
A


460
O
LEU
77
17.692
2.038
73.916
1.00
21.09
A


461
N
THR
78
15.602
1.990
74.719
1.00
23.09
A


462
CA
THR
78
15.918
0.875
75.627
1.00
23.42
A


463
CB
THR
78
15.463
1.118
77.082
1.00
23.04
A


464
OG1
THR
78
14.015
1.098
77.049
1.00
21.65
A


465
CG2
THR
78
15.990
2.406
77.693
1.00
22.61
A


466
C
THR
78
15.313
−0.421
75.135
1.00
23.97
A


467
O
THR
78
14.357
−0.475
74.363
1.00
21.55
A


468
N
GLU
79
15.805
−1.535
75.697
1.00
25.13
A


469
CA
GLU
79
15.223
−2.840
75.440
1.00
25.90
A


470
CB
GLU
79
16.075
−3.912
76.147
1.00
29.42
A


471
CG
GLU
79
15.500
−5.306
75.879
1.00
32.50
A


472
CD
GLU
79
16.417
−6.432
76.330
1.00
33.94
A


473
OE1
GLU
79
17.572
−6.275
76.719
1.00
33.93
A


474
OE2
GLU
79
15.928
−7.572
76.300
1.00
34.93
A


475
C
GLU
79
13.786
−2.939
75.909
1.00
26.56
A


476
O
GLU
79
12.933
−3.542
75.219
1.00
26.00
A


477
N
ASP
80
13.469
−2.306
77.047
1.00
25.28
A


478
CA
ASP
80
12.130
−2.360
77.604
1.00
26.58
A


479
CB
ASP
80
11.991
−1.707
78.992
1.00
29.59
A


480
CG
ASP
80
12.565
−2.545
80.145
1.00
34.54
A


481
OD1
ASP
80
13.268
−3.561
80.003
1.00
36.70
A


482
OD2
ASP
80
12.324
−2.141
81.293
1.00
35.94
A


483
C
ASP
80
11.185
−1.624
76.630
1.00
23.74
A


484
O
ASP
80
10.052
−1.982
76.364
1.00
20.67
A


485
N
TYR
81
11.655
−0.470
76.146
1.00
21.73
A


486
CA
TYR
81
10.830
0.280
75.179
1.00
21.01
A


487
CB
TYR
81
11.538
1.572
74.807
1.00
22.38
A


488
CG
TYR
81
10.553
2.569
74.238
1.00
20.79
A


489
CD1
TYR
81
9.658
3.258
75.038
1.00
22.40
A


490
CD2
TYR
81
10.539
2.777
72.863
1.00
21.60
A


491
CE1
TYR
81
8.774
4.180
74.482
1.00
22.22
A


492
CE2
TYR
81
9.653
3.680
72.284
1.00
21.70
A


493
CZ
TYR
81
8.780
4.368
73.083
1.00
21.39
A


494
OH
TYR
81
7.857
5.281
72.616
1.00
16.70
A


495
C
TYR
81
10.538
−0.518
73.927
1.00
21.01
A


496
O
TYR
81
9.414
−0.513
73.417
1.00
23.40
A


497
N
LEU
82
11.502
−1.279
73.447
1.00
22.80
A


498
CA
LEU
82
11.360
−2.117
72.269
1.00
25.21
A


499
CB
LEU
82
12.729
−2.691
71.876
1.00
25.32
A


500
CG
LEU
82
13.677
−1.731
71.130
1.00
25.98
A


501
CD2
LEU
82
13.000
−1.237
69.843
1.00
24.58
A


502
CD1
LEU
82
14.986
−2.446
70.884
1.00
26.48
A


503
C
LEU
82
10.427
−3.297
72.489
1.00
26.98
A


504
O
LEU
82
9.554
−3.654
71.680
1.00
26.48
A


505
N
GLN
83
10.470
−3.811
73.739
1.00
27.34
A


506
CA
GLN
83
9.551
−4.924
74.047
1.00
27.90
A


507
CB
GLN
83
10.054
−5.610
75.334
1.00
34.21
A


508
CG
GLN
83
11.214
−6.537
75.052
1.00
43.19
A


509
CD
GLN
83
11.745
−7.361
76.215
1.00
48.60
A


510
OE1
GLN
83
11.137
−7.539
77.284
1.00
52.11
A


511
NE2
GLN
83
12.957
−7.920
76.033
1.00
48.78
A


512
C
GLN
83
8.140
−4.386
74.173
1.00
23.34
A


513
O
GLN
83
7.165
−5.046
73.827
1.00
23.48
A


514
N
GLU
84
7.989
−3.150
74.641
1.00
21.80
A


515
CA
GLU
84
6.664
−2.532
74.774
1.00
24.16
A


516
CB
GLU
84
6.714
−1.345
75.751
1.00
27.24
A


517
CG
GLU
84
7.145
−1.787
77.172
1.00
35.14
A


518
CD
GLU
84
7.088
−0.745
78.267
1.00
38.58
A


519
OE1
GLU
84
6.536
0.370
78.077
1.00
42.49
A


520
OE2
GLU
84
7.598
−0.973
79.396
1.00
39.80
A


521
C
GLU
84
6.119
−2.062
73.410
1.00
24.58
A


522
O
GLU
84
4.910
−1.871
73.194
1.00
22.41
A


523
N
ASN
85
7.041
−1.795
72.475
1.00
20.65
A


524
CA
ASN
85
6.620
−1.284
71.143
1.00
22.51
A


525
CB
ASN
85
7.195
0.155
71.062
1.00
20.97
A


526
CG
ASN
85
6.600
1.055
72.157
1.00
23.78
A


527
OD1
ASN
85
7.224
1.315
73.225
1.00
24.08
A


528
ND2
ASN
85
5.402
1.527
71.973
1.00
22.00
A


529
C
ASN
85
7.201
−2.159
70.073
1.00
22.06
A


530
O
ASN
85
8.196
−1.765
69.417
1.00
22.54
A


531
N
PRO
86
6.768
−3.408
69.944
1.00
22.24
A


532
CA
PRO
86
7.455
−4.412
69.147
1.00
22.73
A


533
CD
PRO
86
5.579
−4.002
70.612
1.00
23.00
A


534
CB
PRO
86
6.642
−5.700
69.362
1.00
21.97
A


535
CG
PRO
86
5.268
−5.173
69.702
1.00
22.61
A


536
C
PRO
86
7.574
−4.119
67.655
1.00
21.69
A


537
O
PRO
86
8.435
−4.678
66.960
1.00
21.61
A


538
N
THR
87
6.700
−3.276
67.148
1.00
21.21
A


539
CA
THR
87
6.722
−2.936
65.704
1.00
22.08
A


540
CB
THR
87
5.501
−2.171
65.242
1.00
22.22
A


541
OG1
THR
87
5.367
−0.934
65.949
1.00
20.60
A


542
CG2
THR
87
4.223
−3.026
65.356
1.00
24.78
A


543
C
THR
87
7.946
−2.127
65.342
1.00
22.35
A


544
O
THR
87
8.374
−2.191
64.187
1.00
22.21
A


545
N
MET
88
8.672
−1.544
66.313
1.00
21.23
A


546
CA
MET
88
9.949
−0.933
66.036
1.00
24.04
A


547
CB
MET
88
10.510
−0.178
67.257
1.00
22.23
A


548
CG
MET
88
9.720
1.118
67.459
1.00
22.19
A


549
SD
MET
88
10.285
2.038
68.920
1.00
22.06
A


550
CE
MET
88
11.960
2.446
68.441
1.00
20.27
A


551
C
MET
88
10.972
−1.939
65.533
1.00
25.74
A


552
O
MET
88
11.933
−1.517
64.887
1.00
25.43
A


553
N
CYS
89
10.841
−3.217
65.850
1.00
28.09
A


554
CA
CYS
89
11.782
−4.230
65.434
1.00
31.78
A


555
CB
CYS
89
11.943
−5.303
66.544
1.00
31.86
A


556
SG
CYS
89
12.464
−4.554
68.102
1.00
33.92
A


557
C
CYS
89
11.381
−4.988
64.175
1.00
32.89
A


558
O
CYS
89
12.193
−5.791
63.718
1.00
33.74
A


559
N
GLU
90
10.199
−4.765
63.654
1.00
35.14
A


560
CA
GLU
90
9.642
−5.420
62.477
1.00
35.99
A


561
CB
GLU
90
8.163
−5.761
62.680
1.00
39.05
A


562
CG
GLU
90
7.781
−6.609
63.870
1.00
43.25
A


563
CD
GLU
90
6.323
−6.617
64.296
1.00
45.32
A


564
OE1
GLU
90
5.381
−6.341
63.517
1.00
45.87
A


565
OE2
GLU
90
6.084
−6.930
65.499
1.00
46.74
A


566
C
GLU
90
9.827
−4.495
61.266
1.00
35.00
A


567
O
GLU
90
9.299
−3.382
61.198
1.00
30.90
A


568
N
PHE
91
10.664
−4.939
60.336
1.00
35.74
A


569
CA
PHE
91
11.073
−4.068
59.227
1.00
37.10
A


570
CB
PHE
91
12.146
−4.707
58.353
1.00
37.29
A


571
CG
PHE
91
12.830
−3.748
57.416
1.00
37.01
A


572
CD1
PHE
91
13.960
−3.053
57.790
1.00
37.87
A


573
CD2
PHE
91
12.304
−3.526
56.152
1.00
37.36
A


574
CE1
PHE
91
14.568
−2.151
56.927
1.00
38.21
A


575
CE2
PHE
91
12.896
−2.622
55.278
1.00
37.76
A


576
CZ
PHE
91
14.012
−1.925
55.677
1.00
38.01
A


577
C
PHE
91
9.837
−3.535
58.508
1.00
37.33
A


578
O
PHE
91
8.908
−4.199
58.081
1.00
37.45
A


579
N
MET
92
9.721
−2.218
58.577
1.00
37.74
A


580
CA
MET
92
8.643
−1.430
58.010
1.00
39.99
A


581
CB
MET
92
8.708
−1.524
56.475
1.00
42.01
A


582
CG
MET
92
10.005
−0.872
55.965
1.00
44.68
A


583
SD
MET
92
10.124
0.894
56.343
1.00
48.32
A


584
CE
MET
92
11.755
0.952
57.098
1.00
47.67
A


585
C
MET
92
7.246
−1.634
58.579
1.00
38.29
A


586
O
MET
92
6.265
−1.145
57.986
1.00
37.09
A


587
N
ALA
93
7.088
−2.278
59.744
1.00
33.03
A


588
CA
ALA
93
5.776
−2.292
60.378
1.00
30.77
A


589
CB
ALA
93
5.784
−3.241
61.579
1.00
30.88
A


590
C
ALA
93
5.566
−0.833
60.801
1.00
26.21
A


591
O
ALA
93
6.519
−0.061
60.984
1.00
26.39
A


592
N
PRO
94
4.339
−0.414
60.993
1.00
25.45
A


593
CA
PRO
94
4.001
0.911
61.454
1.00
24.71
A


594
CD
PRO
94
3.138
−1.282
60.866
1.00
27.05
A


595
CB
PRO
94
2.498
0.937
61.426
1.00
24.24
A


596
CG
PRO
94
2.063
−0.488
61.540
1.00
27.58
A


597
C
PRO
94
4.586
1.134
62.853
1.00
23.01
A


598
O
PRO
94
4.182
0.405
63.771
1.00
22.00
A


599
N
SER
95
5.380
2.177
63.030
1.00
21.95
A


600
CA
SER
95
6.074
2.390
64.307
1.00
19.65
A


601
CB
SER
95
7.371
1.567
64.279
1.00
17.85
A


602
OG
SER
95
8.170
1.976
63.168
1.00
19.02
A


603
C
SER
95
6.433
3.842
64.540
1.00
21.19
A


604
O
SER
95
6.984
4.232
65.590
1.00
20.42
A


605
N
LEU
96
6.014
4.734
63.620
1.00
19.13
A


606
CA
LEU
96
6.309
6.159
63.800
1.00
18.01
A


607
CB
LEU
96
5.732
6.987
62.625
1.00
15.73
A


608
CG
LEU
96
6.021
8.495
62.787
1.00
18.09
A


609
CD2
LEU
96
5.344
9.254
61.649
1.00
19.36
A


610
CD1
LEU
96
7.517
8.788
62.715
1.00
17.55
A


611
C
LEU
96
5.786
6.727
65.121
1.00
17.50
A


612
O
LEU
96
6.447
7.588
65.720
1.00
16.57
A


613
N
ASN
97
4.572
6.396
65.508
1.00
17.74
A


614
CA
ASN
97
3.962
6.946
66.729
1.00
17.67
A


615
CB
ASN
97
2.536
6.418
66.878
1.00
18.54
A


616
CG
ASN
97
1.559
6.945
65.844
1.00
20.15
A


617
OD1
ASN
97
0.373
6.530
65.830
1.00
22.49
A


618
ND2
ASN
97
1.996
7.888
65.040
1.00
14.75
A


619
C
ASN
97
4.789
6.539
67.971
1.00
17.57
A


620
O
ASN
97
5.114
7.411
68.765
1.00
17.20
A


621
N
ALA
98
5.239
5.299
68.063
1.00
17.89
A


622
CA
ALA
98
6.116
4.874
69.156
1.00
19.90
A


623
CB
ALA
98
6.459
3.382
69.117
1.00
18.51
A


624
C
ALA
98
7.418
5.641
69.147
1.00
18.57
A


625
O
ALA
98
8.035
6.005
70.196
1.00
18.22
A


626
N
ARG
99
8.000
5.788
67.939
1.00
15.38
A


627
CA
ARG
99
9.198
6.584
67.808
1.00
15.91
A


628
CB
ARG
99
9.736
6.561
66.322
1.00
17.77
A


629
CG
ARG
99
9.922
5.102
65.894
1.00
18.85
A


630
CD
ARG
99
10.377
5.051
64.441
1.00
17.09
A


631
NE
ARG
99
10.364
3.734
63.832
1.00
17.08
A


632
CZ
ARG
99
11.483
3.005
63.637
1.00
19.23
A


633
NH1
ARG
99
12.582
3.470
64.438
1.00
15.98
A


634
NH2
ARG
99
11.439
1.825
63.211
1.00
21.09
A


635
C
ARG
99
9.010
8.007
68.270
1.00
14.62
A


636
O
ARG
99
9.813
8.566
69.052
1.00
16.83
A


637
N
GLN
100
8.013
8.687
67.759
1.00
14.76
A


638
CA
GLN
100
7.755
10.093
68.096
1.00
15.89
A


639
CB
GLN
100
6.471
10.518
67.386
1.00
16.39
A


640
CG
GLN
100
6.589
10.774
65.861
1.00
16.04
A


641
CD
GLN
100
7.193
12.136
65.634
1.00
14.40
A


642
OE1
GLN
100
6.499
12.946
65.003
1.00
21.02
A


643
NE2
GLN
100
8.372
12.458
66.071
1.00
14.10
A


644
C
GLN
100
7.475
10.202
69.622
1.00
15.87
A


645
O
GLN
100
7.777
11.189
70.280
1.00
17.94
A


646
N
ASP
101
6.725
9.238
70.173
1.00
16.61
A


647
CA
ASP
101
6.404
9.336
71.629
1.00
19.76
A


648
CB
ASP
101
5.522
8.146
72.016
1.00
20.02
A


649
CG
ASP
101
4.103
8.330
71.534
1.00
19.83
A


650
OD1
ASP
101
3.727
9.441
71.188
1.00
17.95
A


651
OD2
ASP
101
3.359
7.357
71.523
1.00
24.70
A


652
C
ASP
101
7.715
9.313
72.423
1.00
20.87
A


653
O
ASP
101
7.824
10.021
73.446
1.00
27.99
A


654
N
LEU
102
8.774
8.667
71.954
1.00
19.31
A


655
CA
LEU
102
10.082
8.718
72.603
1.00
16.53
A


656
CB
LEU
102
10.931
7.530
72.208
1.00
18.29
A


657
CG
LEU
102
12.276
7.281
72.888
1.00
19.63
A


658
CD2
LEU
102
13.256
8.393
72.584
1.00
25.96
A


659
CD1
LEU
102
13.019
6.034
72.414
1.00
20.49
A


660
C
LEU
102
10.752
10.043
72.329
1.00
19.62
A


661
O
LEU
102
11.269
10.746
73.227
1.00
17.52
A


662
N
VAL
103
10.980
10.374
71.032
1.00
18.18
A


663
CA
VAL
103
11.888
11.468
70.699
1.00
15.75
A


664
CB
VAL
103
12.449
11.309
69.236
1.00
18.04
A


665
CG1
VAL
103
13.122
9.941
69.142
1.00
14.19
A


666
CG2
VAL
103
11.350
11.445
68.181
1.00
13.15
A


667
C
VAL
103
11.299
12.833
70.858
1.00
13.49
A


668
O
VAL
103
12.044
13.813
71.001
1.00
13.92
A


669
N
VAL
104
9.981
13.018
70.850
1.00
14.88
A


670
CA
VAL
104
9.346
14.321
71.017
1.00
14.37
A


671
CB
VAL
104
7.856
14.282
70.698
1.00
18.72
A


672
CG1
VAL
104
7.102
15.492
71.202
1.00
17.65
A


673
CG2
VAL
104
7.622
14.322
69.122
1.00
16.40
A


674
C
VAL
104
9.589
14.926
72.420
1.00
17.96
A


675
O
VAL
104
9.844
16.140
72.563
1.00
16.58
A


676
N
THR
105
9.657
14.018
73.414
1.00
14.93
A


677
CA
THR
105
10.082
14.554
74.730
1.00
18.23
A


678
CB
THR
105
9.356
13.736
75.842
1.00
18.83
A


679
CG1
THR
105
9.653
12.375
75.611
1.00
20.03
A


680
CG2
THR
105
7.843
13.834
75.729
1.00
19.34
A


681
C
THR
105
11.581
14.428
74.919
1.00
17.76
A


682
O
THR
105
12.297
15.321
75.390
1.00
16.74
A


683
N
GLY
106
12.156
13.355
74.408
1.00
18.35
A


684
CA
GLY
106
13.588
13.075
74.646
1.00
20.22
A


685
C
GLY
106
14.573
14.040
74.076
1.00
17.61
A


686
O
GLY
106
15.617
14.427
74.619
1.00
18.07
A


687
N
VAL
107
14.283
14.500
72.828
1.00
18.39
A


688
CA
VAL
107
15.253
15.382
72.150
1.00
14.98
A


689
CB
VAL
107
14.794
15.578
70.688
1.00
15.76
A


690
CG1
VAL
107
15.372
16.793
70.033
1.00
12.18
A


691
CG2
VAL
107
15.172
14.301
69.879
1.00
14.81
A


692
C
VAL
107
15.409
16.665
72.929
1.00
14.08
A


693
O
VAL
107
16.524
17.141
73.159
1.00
14.20
A


694
N
PRO
108
14.341
17.395
73.241
1.00
14.43
A


695
CA
PRO
108
14.438
18.640
73.962
1.00
16.42
A


696
CD
PRO
108
12.948
17.026
72.949
1.00
16.38
A


697
CB
PRO
108
13.039
19.206
73.945
1.00
17.29
A


698
CG
PRO
108
12.103
18.080
73.638
1.00
17.10
A


699
C
PRO
108
15.030
18.462
75.375
1.00
17.39
A


700
O
PRO
108
15.717
19.340
75.899
1.00
16.11
A


701
N
MET
109
14.681
17.377
76.050
1.00
18.23
A


702
CA
MET
109
15.216
17.142
77.417
1.00
19.54
A


703
CB
MET
109
14.579
15.892
78.030
1.00
18.80
A


704
CG
MET
109
15.141
15.705
79.453
1.00
24.55
A


705
SD
MET
109
14.681
17.096
80.548
1.00
30.03
A


706
CE
MET
109
12.892
17.062
80.237
1.00
23.66
A


707
C
MET
109
16.726
16.932
77.368
1.00
19.02
A


708
O
MET
109
17.498
17.514
78.126
1.00
17.91
A


709
N
LEU
110
17.197
16.076
76.453
1.00
18.49
A


710
CA
LEU
110
18.611
15.843
76.232
1.00
18.20
A


711
CB
LEU
110
18.821
14.757
75.163
1.00
18.64
A


712
CG
LEU
110
20.275
14.405
74.813
1.00
19.58
A


713
CD2
LEU
110
20.325
13.371
73.673
1.00
18.33
A


714
CD1
LEU
110
20.970
13.816
76.051
1.00
18.07
A


715
C
LEU
110
19.337
17.100
75.806
1.00
18.48
A


716
O
LEU
110
20.433
17.435
76.297
1.00
20.76
A


717
N
GLY
111
18.711
17.945
74.981
1.00
16.22
A


718
CA
GLY
111
19.304
19.235
74.604
1.00
14.18
A


719
C
GLY
111
19.371
20.178
75.812
1.00
16.43
A


720
O
GLY
111
20.299
20.948
76.061
1.00
15.13
A


721
N
LYS
112
18.371
20.116
76.685
1.00
15.61
A


722
CA
LYS
112
18.401
20.945
77.898
1.00
16.57
A


723
CB
LYS
112
17.103
20.710
78.684
1.00
18.18
A


724
CG
LYS
112
16.987
21.680
79.892
1.00
20.77
A


725
CD
LYS
112
16.318
20.904
81.048
1.00
22.71
A


726
CE
LYS
112
17.323
19.962
81.667
1.00
27.09
A


727
NZ
LYS
112
16.687
19.337
82.890
1.00
32.10
A


728
C
LYS
112
19.597
20.512
78.747
1.00
14.36
A


729
O
LYS
112
20.258
21.371
79.299
1.00
16.03
A


730
N
GLU
113
19.915
19.227
78.831
1.00
17.89
A


731
CA
GLU
113
21.055
18.838
79.690
1.00
19.13
A


732
CB
GLU
113
21.089
17.313
79.820
1.00
22.35
A


733
CG
GLU
113
19.889
16.849
80.643
1.00
27.59
A


734
CD
GLU
113
19.575
15.381
80.477
1.00
30.72
A


735
OE1
GLU
113
20.383
14.636
79.816
1.00
34.90
A


736
OE2
GLU
113
18.516
14.896
81.021
1.00
33.21
A


737
C
GLU
113
22.372
19.390
79.154
1.00
20.94
A


738
O
GLU
113
23.264
19.789
79.915
1.00
15.83
A


739
N
ALA
114
22.498
19.420
77.852
1.00
17.27
A


740
CA
ALA
114
23.708
19.962
77.235
1.00
16.41
A


741
CB
ALA
114
23.731
19.648
75.742
1.00
13.77
A


742
C
ALA
114
23.749
21.485
77.439
1.00
14.62
A


743
O
ALA
114
24.791
22.066
77.757
1.00
13.91
A


744
N
ALA
115
22.598
22.115
77.260
1.00
13.33
A


745
CA
ALA
115
22.480
23.585
77.361
1.00
13.34
A


746
CB
ALA
115
21.060
24.038
77.044
1.00
13.34
A


747
C
ALA
115
22.825
24.103
78.766
1.00
16.12
A


748
O
ALA
115
23.455
25.153
78.930
1.00
14.73
A


749
N
VAL
116
22.393
23.380
79.782
1.00
16.09
A


750
CA
VAL
116
22.668
23.795
81.168
1.00
17.57
A


751
CB
VAL
116
22.046
22.819
82.168
1.00
16.56
A


752
CG1
VAL
116
22.547
23.031
83.602
1.00
16.83
A


753
CG2
VAL
116
20.521
22.936
82.249
1.00
14.36
A


754
C
VAL
116
24.182
23.858
81.387
1.00
16.32
A


755
O
VAL
116
24.702
24.791
82.013
1.00
17.09
A


756
N
LYS
117
24.861
22.859
80.850
1.00
18.67
A


757
CA
LYS
117
26.324
22.751
80.965
1.00
19.95
A


758
CB
LYS
117
26.822
21.443
80.365
1.00
20.22
A


759
CG
LYS
117
26.532
20.235
81.251
1.00
23.41
A


760
CD
LYS
117
27.018
18.925
80.638
1.00
25.60
A


761
CE
LYS
117
26.247
17.704
81.136
1.00
27.45
A


762
NZ
LYS
117
26.879
16.439
80.735
1.00
27.56
A


763
C
LYS
117
27.024
23.902
80.231
1.00
19.45
A


764
O
LYS
117
27.988
24.489
80.726
1.00
17.34
A


765
N
ALA
118
26.549
24.220
79.039
1.00
17.17
A


766
CA
ALA
118
27.157
25.309
78.250
1.00
15.71
A


767
CB
ALA
118
26.501
25.415
76.875
1.00
17.47
A


768
C
ALA
118
26.985
26.651
78.976
1.00
15.84
A


769
O
ALA
118
27.908
27.466
79.068
1.00
16.06
A


770
N
ILE
119
25.792
26.861
79.486
1.00
18.12
A


771
CA
ILE
119
25.446
28.109
80.181
1.00
18.00
A


772
CB
ILE
119
23.937
28.145
80.409
1.00
19.24
A


773
CG2
ILE
119
23.498
29.252
81.368
1.00
18.79
A


774
CG1
ILE
119
23.163
28.373
79.109
1.00
18.13
A


775
CD1
ILE
119
21.670
28.086
79.241
1.00
16.38
A


776
C
ILE
119
26.190
28.215
81.517
1.00
18.79
A


777
O
ILE
119
26.612
29.301
81.913
1.00
20.34
A


778
N
ASP
120
26.457
27.099
82.123
0.50
19.78
A


779
CA
ASP
120
27.191
27.069
83.392
0.50
21.23
A


780
CB
ASP
120
27.043
25.701
84.032
0.50
21.61
A


781
CG
ASP
120
25.743
25.622
84.821
0.50
23.09
A


782
OD1
ASP
120
25.277
24.484
85.185
0.50
25.77
A


783
OD2
ASP
120
25.114
26.712
85.115
0.50
24.50
A


784
C
ASP
120
28.652
27.452
83.140
0.50
21.63
A


785
O
ASP
120
29.263
28.203
83.913
0.50
20.32
A


778
N
2ASP
120
26.430
27.095
82.148
0.50
18.97
A


779
CA
2ASP
120
27.176
27.073
83.414
0.50
19.78
A


780
CB
2ASP
120
27.105
25.691
84.055
0.50
18.04
A


781
CG
2ASP
120
27.823
25.634
85.402
0.50
18.53
A


782
OD
12ASP
120
27.378
26.311
86.405
0.50
18.96
A


783
OD
22ASP
120
28.811
24.912
85.525
0.50
14.37
A


784
C
2ASP
120
28.633
27.483
83.139
0.50
20.73
A


785
O
2ASP
120
29.225
28.289
83.868
0.50
19.80
A


794
N
GLU
121
29.255
26.892
82.096
1.00
20.48
A


795
CA
GLU
121
30.577
27.296
81.668
1.00
19.07
A


796
CB
GLU
121
31.089
26.472
80.454
1.00
20.06
A


797
CG
GLU
121
32.459
27.012
79.979
1.00
21.09
A


798
CD
GLU
121
32.816
26.412
78.600
1.00
22.32
A


799
OE1
GLU
121
32.182
25.479
78.093
1.00
21.05
A


800
OE2
GLU
121
33.843
26.890
78.072
1.00
22.00
A


801
C
GLU
121
30.625
28.776
81.369
1.00
20.81
A


802
O
GLU
121
31.521
29.554
81.776
1.00
20.90
A


803
N
TRP
122
29.653
29.236
80.583
1.00
18.77
A


804
CA
TRP
122
29.584
30.620
80.181
1.00
18.63
A


805
CB
TRP
122
28.334
30.801
79.294
1.00
16.48
A


806
CG
TRP
122
28.155
32.174
78.726
1.00
16.28
A


807
CD2
TRP
122
26.923
32.873
78.518
1.00
15.79
A


808
CD1
TRP
122
29.116
32.990
78.194
1.00
16.70
A


809
NE1
TRP
122
28.583
34.161
77.731
1.00
16.88
A


810
CE2
TRP
122
27.211
34.093
77.901
1.00
15.08
A


811
CE3
TRP
122
25.577
32.560
78.829
1.00
17.00
A


812
CZ2
TRP
122
26.262
35.047
77.609
1.00
13.22
A


813
CZ3
TRP
122
24.614
33.522
78.531
1.00
13.93
A


814
CH2
TRP
122
24.969
34.717
77.916
1.00
13.27
A


815
C
TRP
122
29.538
31.499
81.441
1.00
21.18
A


816
O
TRP
122
30.143
32.595
81.471
1.00
21.65
A


817
N
GLY
123
28.546
31.276
82.290
1.00
21.20
A


818
CA
GLY
123
28.464
31.926
83.601
1.00
20.30
A


819
C
GLY
123
27.636
33.178
83.633
1.00
22.55
A


820
O
GLY
123
27.223
33.591
84.711
1.00
23.03
A


821
N
LEU
124
27.214
33.734
82.476
1.00
19.56
A


822
CA
LEU
124
26.387
34.911
82.452
1.00
18.14
A


823
CB
LEU
124
26.671
35.733
81.199
1.00
23.08
A


824
CG
LEU
124
27.898
36.660
81.262
1.00
24.54
A


825
CD2
LEU
124
27.913
37.634
80.089
1.00
23.57
A


826
CD1
LEU
124
29.206
35.864
81.321
1.00
24.28
A


827
C
LEU
124
24.926
34.504
82.604
1.00
18.48
A


828
O
LEU
124
24.566
33.340
82.410
1.00
18.76
A


829
N
PRO
125
24.055
35.423
82.938
1.00
19.11
A


830
CA
PRO
125
22.654
35.144
83.097
1.00
20.89
A


831
CD
PRO
125
24.389
36.861
83.156
1.00
19.83
A


832
CB
PRO
125
22.040
36.459
83.557
1.00
21.21
A


833
CG
PRO
125
23.163
37.368
83.904
1.00
23.77
A


834
C
PRO
125
22.003
34.619
81.809
1.00
21.34
A


835
O
PRO
125
22.193
35.136
80.694
1.00
21.43
A


836
N
LYS
126
21.174
33.600
81.942
1.00
19.50
A


837
CA
LYS
126
20.433
32.982
80.835
1.00
21.62
A


838
CB
LYS
126
19.846
31.624
81.228
1.00
20.60
A


839
CG
LYS
126
18.716
31.656
82.265
1.00
24.65
A


840
CD
LYS
126
18.268
30.231
82.580
1.00
24.08
A


841
CE
LYS
126
17.293
30.086
83.743
1.00
27.19
A


842
NZ
LYS
126
16.268
31.128
83.772
1.00
28.11
A


843
C
LYS
126
19.451
33.949
80.210
1.00
20.79
A


844
O
LYS
126
19.057
33.887
79.024
1.00
19.00
A


845
N
SER
127
19.054
35.006
80.960
1.00
18.95
A


846
CA
SER
127
18.198
36.061
80.448
1.00
19.28
A


847
CB
SER
127
17.769
37.070
81.561
1.00
18.43
A


848
OG
SER
127
18.972
37.718
81.982
1.00
20.37
A


849
C
SER
127
18.880
36.875
79.350
1.00
19.12
A


850
O
SER
127
18.226
37.612
78.598
1.00
19.26
A


851
N
LYS
128
20.207
36.775
79.241
1.00
18.44
A


852
CA
LYS
128
20.934
37.466
78.202
1.00
19.59
A


853
CB
LYS
128
22.371
37.809
78.645
1.00
22.71
A


854
CG
LYS
128
22.360
38.988
79.650
1.00
28.47
A


855
CD
LYS
128
23.798
39.358
80.030
1.00
33.65
A


856
CE
LYS
128
23.837
40.734
80.699
1.00
37.84
A


857
NZ
LYS
128
25.066
40.919
81.542
1.00
40.83
A


858
C
LYS
128
20.970
36.648
76.886
1.00
17.61
A


859
O
LYS
128
21.654
37.100
75.975
1.00
17.90
A


860
N
ILE
129
20.492
35.446
76.817
1.00
16.00
A


861
CA
ILE
129
20.418
34.665
75.559
1.00
15.86
A


862
CB
ILE
129
20.184
33.196
75.852
1.00
14.94
A


863
CG2
ILE
129
19.853
32.386
74.563
1.00
13.22
A


864
CG1
ILE
129
21.464
32.641
76.525
1.00
15.39
A


865
CD1
ILE
129
21.251
31.266
77.182
1.00
12.48
A


866
C
ILE
129
19.323
35.309
74.719
1.00
16.47
A


867
O
ILE
129
18.190
35.359
75.206
1.00
15.12
A


868
N
THR
130
19.660
35.830
73.526
1.00
14.40
A


869
CA
THR
130
18.674
36.537
72.722
1.00
15.90
A


870
CB
THR
130
19.356
37.780
72.073
1.00
16.78
A


871
OG1
THR
130
20.588
37.405
71.457
1.00
14.61
A


872
CG2
THR
130
19.600
38.797
73.226
1.00
20.14
A


873
C
THR
130
18.116
35.718
71.552
1.00
14.97
A


874
O
THR
130
17.072
36.074
71.030
1.00
13.58
A


875
N
HIS
131
18.817
34.672
71.133
1.00
14.54
A


876
CA
HIS
131
18.460
33.849
69.997
1.00
14.88
A


877
ND1
HIS
131
19.656
36.778
68.871
1.00
14.87
A


878
CG
HIS
131
19.134
35.633
68.252
1.00
14.61
A


879
CB
HIS
131
19.347
34.251
68.754
1.00
11.60
A


880
NE2
HIS
131
18.565
37.480
67.118
1.00
12.92
A


881
CD2
HIS
131
18.458
36.092
67.140
1.00
10.98
A


882
CE1
HIS
131
19.361
37.852
68.159
1.00
15.43
A


883
C
HIS
131
18.769
32.417
70.382
1.00
15.66
A


884
O
HIS
131
19.744
32.127
71.106
1.00
14.95
A


885
N
LEU
132
17.935
31.487
69.947
1.00
11.48
A


886
CA
LEU
132
18.046
30.095
70.167
1.00
13.97
A


887
CB
LEU
132
16.883
29.525
71.004
1.00
11.50
A


888
CG
LEU
132
16.800
28.010
71.055
1.00
13.95
A


889
CD2
LEU
132
15.496
27.637
71.783
1.00
12.94
A


890
CD1
LEU
132
17.976
27.318
71.746
1.00
13.85
A


891
C
LEU
132
17.915
29.322
68.823
1.00
14.21
A


892
O
LEU
132
16.909
29.490
68.133
1.00
12.57
A


893
N
ILE
133
18.927
28.543
68.531
1.00
16.16
A


894
CA
ILE
133
18.880
27.710
67.311
1.00
14.73
A


895
CB
ILE
133
20.145
27.803
66.434
1.00
14.29
A


896
CG2
ILE
133
20.083
26.754
65.321
1.00
13.55
A


897
CG1
ILE
133
20.306
29.227
65.887
1.00
12.77
A


898
CD1
ILE
133
21.732
29.488
65.391
1.00
13.14
A


899
C
ILE
133
18.758
26.263
67.829
1.00
14.02
A


900
O
ILE
133
19.669
25.807
68.529
1.00
15.60
A


901
N
PHE
134
17.637
25.617
67.546
1.00
12.75
A


902
CA
PHE
134
17.508
24.222
67.961
1.00
14.31
A


903
CB
PHE
134
16.173
23.968
68.718
1.00
13.08
A


904
CG
PHE
134
16.243
22.661
69.465
1.00
14.84
A


905
CD1
PHE
134
16.267
22.700
70.896
1.00
13.62
A


906
CD2
PHE
134
16.177
21.453
68.831
1.00
13.56
A


907
CE1
PHE
134
16.304
21.485
71.584
1.00
12.53
A


908
CE2
PHE
134
16.288
20.257
69.520
1.00
15.13
A


909
CZ
PHE
134
16.360
20.278
70.926
1.00
14.68
A


910
C
PHE
134
17.524
23.349
66.693
1.00
15.71
A


911
O
PHE
134
16.787
23.619
65.706
1.00
16.42
A


912
N
CYS
135
18.358
22.353
66.708
1.00
15.75
A


913
CA
CYS
135
18.522
21.499
65.502
1.00
16.73
A


914
CB
CYS
135
19.884
21.859
64.834
1.00
15.26
A


915
SG
CYS
135
20.328
20.732
63.445
1.00
15.19
A


916
C
CYS
135
18.465
20.056
65.836
1.00
15.01
A


917
O
CYS
135
19.009
19.629
66.880
1.00
13.86
A


918
N
THR
136
17.663
19.285
65.092
1.00
13.11
A


919
CA
THR
136
17.623
17.854
65.246
1.00
12.65
A


920
CB
THR
136
16.572
17.458
66.335
1.00
11.65
A


921
CG1
THR
136
16.660
16.068
66.616
1.00
10.20
A


922
CG2
THR
136
15.131
17.740
65.909
1.00
9.93
A


923
C
THR
136
17.249
17.186
63.922
1.00
14.69
A


924
O
THR
136
16.870
17.854
62.950
1.00
16.07
A


925
N
THR
137
17.383
15.874
63.928
1.00
12.78
A


926
CA
THR
137
17.043
15.032
62.777
1.00
15.31
A


927
CB
THR
137
18.310
14.389
62.186
1.00
15.76
A


928
OG1
THR
137
19.338
15.362
62.046
1.00
14.12
A


929
CG2
THR
137
18.077
13.777
60.800
1.00
17.92
A


930
C
THR
137
16.079
13.931
63.231
1.00
16.12
A


931
O
THR
137
15.720
13.030
62.467
1.00
15.44
A


932
N
ALA
138
15.649
14.027
64.484
1.00
14.51
A


933
CA
ALA
138
14.776
12.996
65.074
1.00
15.90
A


934
CB
ALA
138
15.496
12.320
66.243
1.00
16.72
A


935
C
ALA
138
13.447
13.566
65.597
1.00
16.75
A


936
O
ALA
138
13.405
14.229
66.644
1.00
16.22
A


937
N
GLY
139
12.400
13.265
64.836
1.00
15.47
A


938
CA
GLY
139
11.003
13.646
65.154
1.00
16.54
A


939
C
GLY
139
10.724
15.135
64.881
1.00
13.58
A


940
O
GLY
139
11.632
15.933
64.641
1.00
16.14
A


941
N
VAL
140
9.439
15.447
64.906
1.00
12.00
A


942
CA
VAL
140
8.917
16.821
64.769
1.00
14.02
A


943
CB
VAL
140
8.583
17.186
63.313
1.00
14.96
A


944
CG1
VAL
140
9.745
16.964
62.348
1.00
14.96
A


945
CG2
VAL
140
7.402
16.393
62.754
1.00
15.30
A


946
C
VAL
140
7.642
16.903
65.587
1.00
11.68
A


947
O
VAL
140
7.008
15.887
65.877
1.00
15.88
A


948
N
ASP
141
7.288
18.095
65.956
1.00
12.22
A


949
CA
ASP
141
6.082
18.329
66.748
1.00
14.96
A


950
CB
ASP
141
6.343
17.905
68.200
1.00
15.56
A


951
CG
ASP
141
5.068
17.708
69.024
1.00
18.13
A


952
OD1
ASP
141
4.036
17.140
68.502
1.00
19.29
A


953
OD2
ASP
141
5.026
18.111
70.249
1.00
18.44
A


954
C
ASP
141
5.777
19.796
66.672
1.00
15.17
A


955
O
ASP
141
6.630
20.646
66.329
1.00
16.33
A


956
N
MET
142
4.573
20.198
67.043
1.00
12.47
A


957
CA
MET
142
4.163
21.576
67.107
1.00
12.35
A


958
CB
MET
142
3.274
22.034
65.937
1.00
12.65
A


959
CG
MET
142
3.849
21.519
64.560
1.00
13.17
A


960
SD
MET
142
2.778
22.129
63.249
1.00
17.73
A


961
CE
MET
142
3.238
23.820
63.168
1.00
12.70
A


962
C
MET
142
3.430
21.833
68.425
1.00
14.69
A


963
O
MET
142
2.530
21.028
68.630
1.00
11.86
A


964
N
PRO
143
3.862
22.750
69.210
1.00
15.28
A


965
CA
PRO
143
5.051
23.558
69.203
1.00
13.24
A


966
CD
PRO
143
3.201
23.007
70.527
1.00
16.57
A


967
CB
PRO
143
5.128
24.447
70.428
1.00
16.21
A


968
CG
PRO
143
3.868
24.173
71.156
1.00
17.09
A


969
C
PRO
143
6.270
22.671
69.122
1.00
11.50
A


970
O
PRO
143
6.231
21.479
69.430
1.00
11.80
A


971
N
GLY
144
7.360
23.233
68.554
1.00
12.53
A


972
CA
GLY
144
8.509
22.371
68.317
1.00
14.94
A


973
C
GLY
144
9.454
22.196
69.510
1.00
15.09
A


974
O
GLY
144
9.214
22.737
70.580
1.00
15.08
A


975
N
ALA
145
10.535
21.443
69.291
1.00
13.80
A


976
CA
ALA
145
11.507
21.238
70.340
1.00
14.14
A


977
CB
ALA
145
12.609
20.293
69.930
1.00
12.47
A


978
C
ALA
145
12.124
22.560
70.844
1.00
15.66
A


979
O
ALA
145
12.599
22.643
71.986
1.00
16.32
A


980
N
ASP
146
12.118
23.600
70.015
1.00
13.22
A


981
CA
ASP
146
12.685
24.908
70.430
1.00
15.87
A


982
CB
ASP
146
12.738
25.912
69.268
1.00
14.01
A


983
CG
ASP
146
11.381
26.189
68.621
1.00
15.41
A


984
OD1
ASP
146
10.555
25.222
68.427
1.00
13.88
A


985
OD2
ASP
146
11.069
27.386
68.257
1.00
14.80
A


986
C
ASP
146
11.848
25.508
71.565
1.00
16.26
A


987
O
ASP
146
12.383
26.053
72.542
1.00
13.83
A


988
N
TYR
147
10.545
25.393
71.410
1.00
15.62
A


989
CA
TYR
147
9.603
25.906
72.404
1.00
17.56
A


990
CB
TYR
147
8.168
25.788
71.901
1.00
19.53
A


991
CG
TYR
147
7.155
25.905
73.035
1.00
21.75
A


992
CD1
TYR
147
6.720
27.164
73.453
1.00
22.18
A


993
CD2
TYR
147
6.675
24.750
73.659
1.00
21.43
A


994
CE1
TYR
147
5.808
27.271
74.503
1.00
24.05
A


995
CE2
TYR
147
5.764
24.859
74.715
1.00
22.89
A


996
CZ
TYR
147
5.332
26.121
75.137
1.00
25.54
A


997
OH
TYR
147
4.451
26.235
76.165
1.00
26.85
A


998
C
TYR
147
9.747
25.121
73.716
1.00
15.68
A


999
O
TYR
147
9.762
25.699
74.810
1.00
17.55
A


1000
N
GLN
148
9.854
23.800
73.597
1.00
14.99
A


1001
CA
GLN
148
10.007
22.931
74.782
1.00
17.49
A


1002
CB
GLN
148
10.130
21.449
74.400
1.00
16.80
A


1003
CG
GLN
148
8.907
20.883
73.674
1.00
19.62
A


1004
CD
GLN
148
7.584
21.077
74.426
1.00
22.64
A


1005
OE1
GLN
148
7.583
21.469
75.592
1.00
17.96
A


1006
NE2
GLN
148
6.440
20.831
73.808
1.00
18.78
A


1007
C
GLN
148
11.278
23.313
75.549
1.00
18.28
A


1008
O
GLN
148
11.298
23.343
76.787
1.00
16.95
A


1009
N
LEU
149
12.325
23.605
74.786
1.00
16.52
A


1010
CA
LEU
149
13.630
23.968
75.363
1.00
16.17
A


1011
CB
LEU
149
14.715
24.128
74.302
1.00
17.15
A


1012
CG
LEU
149
16.068
24.444
74.947
1.00
18.85
A


1013
CD2
LEU
149
17.171
24.749
73.939
1.00
20.01
A


1014
CD1
LEU
149
16.590
23.296
75.816
1.00
17.08
A


1015
C
LEU
149
13.560
25.293
76.138
1.00
16.77
A


1016
O
LEU
149
14.180
25.447
77.198
1.00
13.50
A


1017
N
VAL
150
12.816
26.246
75.606
1.00
14.16
A


1018
CA
VAL
150
12.653
27.557
76.263
1.00
18.01
A


1019
CB
VAL
150
11.792
28.485
75.406
1.00
18.11
A


1020
CG1
VAL
150
11.328
29.731
76.168
1.00
17.86
A


1021
CG2
VAL
150
12.526
28.994
74.163
1.00
15.15
A


1022
C
VAL
150
11.982
27.372
77.636
1.00
19.70
A


1023
O
VAL
150
12.395
27.973
78.635
1.00
19.11
A


1024
N
LYS
151
10.961
26.534
77.638
1.00
17.83
A


1025
CA
LYS
151
10.164
26.208
78.842
1.00
21.77
A


1026
CB
LYS
151
9.010
25.297
78.420
1.00
24.68
A


1027
CG
LYS
151
8.072
24.921
79.561
1.00
30.91
A


1028
CD
LYS
151
6.971
23.958
79.115
1.00
34.30
A


1029
CE
LYS
151
5.718
24.044
79.983
1.00
37.33
A


1030
NZ
LYS
151
4.774
22.947
79.728
1.00
38.19
A


1031
C
LYS
151
11.031
25.487
79.880
1.00
21.42
A


1032
O
LYS
151
11.128
25.883
81.027
1.00
19.15
A


1033
N
LEU
152
11.742
24.446
79.471
1.00
17.46
A


1034
CA
LEU
152
12.633
23.653
80.236
1.00
21.09
A


1035
CB
LEU
152
13.200
22.522
79.373
1.00
22.56
A


1036
CG
LEU
152
12.813
21.079
79.538
1.00
27.28
A


1037
CD2
LEU
152
12.742
20.286
78.238
1.00
25.41
A


1038
CD1
LEU
152
11.558
20.840
80.389
1.00
29.19
A


1039
C
LEU
152
13.763
24.480
80.833
1.00
23.13
A


1040
O
LEU
152
14.106
24.209
81.996
1.00
20.16
A


1041
N
LEU
153
14.358
25.403
80.070
1.00
18.40
A


1042
CA
LEU
153
15.503
26.119
80.574
1.00
20.40
A


1043
CB
LEU
153
16.382
26.485
79.359
1.00
20.57
A


1044
CG
LEU
153
17.877
26.358
79.291
1.00
24.59
A


1045
CD2
LEU
153
18.308
26.399
77.813
1.00
22.59
A


1046
CD1
LEU
153
18.411
25.111
80.019
1.00
23.12
A


1047
C
LEU
153
15.101
27.398
81.283
1.00
19.64
A


1048
O
LEU
153
15.945
27.971
81.967
1.00
17.34
A


1049
N
GLY
154
13.914
27.915
81.043
1.00
17.94
A


1050
CA
GLY
154
13.496
29.218
81.518
1.00
19.41
A


1051
C
GLY
154
14.175
30.350
80.739
1.00
20.74
A


1052
O
GLY
154
14.546
31.389
81.322
1.00
19.81
A


1053
N
LEU
155
14.299
30.195
79.399
1.00
18.06
A


1054
CA
LEU
155
14.766
31.359
78.612
1.00
15.78
A


1055
CB
LEU
155
15.148
30.916
77.196
1.00
14.66
A


1056
CG
LEU
155
16.221
29.829
77.137
1.00
16.04
A


1057
CD2
LEU
155
17.522
30.344
77.738
1.00
13.61
A


1058
CD1
LEU
155
16.555
29.414
75.701
1.00
17.31
A


1059
C
LEU
155
13.675
32.397
78.493
1.00
16.11
A


1060
O
LEU
155
12.512
32.103
78.776
1.00
15.33
A


1061
N
SER
156
14.004
33.608
78.057
1.00
14.91
A


1062
CA
SER
156
13.052
34.662
77.854
1.00
15.86
A


1063
CB
SER
156
13.735
35.930
77.301
1.00
16.39
A


1064
OG
SER
156
12.766
36.841
76.777
1.00
19.30
A


1065
C
SER
156
11.985
34.196
76.887
1.00
19.09
A


1066
O
SER
156
12.285
33.526
75.906
1.00
17.54
A


1067
N
PRO
157
10.716
34.489
77.156
1.00
20.48
A


1068
CA
PRO
157
9.620
34.161
76.291
1.00
18.95
A


1069
CD
PRO
157
10.268
35.254
78.374
1.00
20.56
A


1070
CB
PRO
157
8.354
34.731
76.945
1.00
19.94
A


1071
CG
PRO
157
8.761
35.066
78.359
1.00
24.08
A


1072
C
PRO
157
9.825
34.836
74.935
1.00
16.61
A


1073
O
PRO
157
9.197
34.433
73.935
1.00
16.75
A


1074
N
SER
158
10.577
35.929
74.902
1.00
15.33
A


1075
CA
SER
158
10.845
36.681
73.714
1.00
16.28
A


1076
CB
SER
158
10.896
38.175
74.113
1.00
14.87
A


1077
OG
SER
158
9.537
38.540
74.283
1.00
16.79
A


1078
C
SER
158
12.142
36.283
73.006
1.00
17.03
A


1079
O
SER
158
12.630
37.122
72.222
1.00
16.14
A


1080
N
VAL
159
12.735
35.168
73.382
1.00
16.44
A


1081
CA
VAL
159
13.966
34.735
72.740
1.00
17.16
A


1082
CB
VAL
159
14.577
33.517
73.432
1.00
15.62
A


1083
CG1
VAL
159
13.754
32.261
73.262
1.00
16.89
A


1084
CG2
VAL
159
15.983
33.232
72.875
1.00
17.19
A


1085
C
VAL
159
13.586
34.422
71.247
1.00
18.63
A


1086
O
VAL
159
12.501
33.899
70.964
1.00
15.76
A


1087
N
LYS
160
14.497
34.792
70.343
1.00
17.02
A


1088
CA
LYS
160
14.195
34.594
68.899
1.00
16.47
A


1089
CB
LYS
160
14.946
35.648
68.051
1.00
17.21
A


1090
CG
LYS
160
14.129
36.945
67.956
1.00
18.56
A


1091
CD
LYS
160
14.968
38.011
67.176
1.00
19.23
A


1092
CE
LYS
160
14.133
39.270
66.945
1.00
22.12
A


1093
NZ
LYS
160
14.866
40.323
66.149
1.00
18.24
A


1094
C
LYS
160
14.629
33.212
68.520
1.00
15.67
A


1095
O
LYS
160
15.775
32.823
68.712
1.00
13.89
A


1096
N
ARG
161
13.722
32.382
68.017
1.00
16.27
A


1097
CA
ARG
161
13.994
31.006
67.744
1.00
15.63
A


1098
CB
ARG
161
12.920
30.092
68.418
1.00
14.77
A


1099
CG
ARG
161
12.859
30.457
69.955
1.00
13.42
A


1100
CD
ARG
161
11.629
29.691
70.465
1.00
15.07
A


1101
NE
ARG
161
10.485
30.516
70.367
1.00
16.22
A


1102
CZ
ARG
161
9.230
30.233
70.015
1.00
15.96
A


1103
NH1
ARG
161
8.942
29.048
69.548
1.00
15.82
A


1104
NH2
ARG
161
8.378
31.242
70.124
1.00
13.11
A


1105
C
ARG
161
14.081
30.571
66.279
1.00
15.67
A


1106
O
ARG
161
13.536
31.211
65.414
1.00
16.22
A


1107
N
TYR
162
14.886
29.535
66.068
1.00
13.46
A


1108
CA
TYR
162
15.183
29.022
64.699
1.00
14.97
A


1109
CB
TYR
162
16.603
29.451
64.219
1.00
12.61
A


1110
CG
TYR
162
16.719
30.966
64.212
1.00
15.38
A


1111
CD1
TYR
162
16.990
31.658
65.423
1.00
13.80
A


1112
CD2
TYR
162
16.410
31.745
63.117
1.00
13.23
A


1113
CE1
TYR
162
16.851
33.033
65.496
1.00
13.36
A


1114
CE2
TYR
162
16.385
33.119
63.142
1.00
14.86
A


1115
CZ
TYR
162
16.591
33.775
64.371
1.00
14.39
A


1116
OH
TYR
162
16.511
35.148
64.453
1.00
11.49
A


1117
C
TYR
162
15.086
27.512
64.810
1.00
12.99
A


1118
O
TYR
162
15.963
26.894
65.399
1.00
16.13
A


1119
N
MET
163
13.928
26.973
64.441
1.00
13.54
A


1120
CA
MET
163
13.702
25.539
64.663
1.00
11.42
A


1121
CB
MET
163
12.225
25.362
65.030
1.00
12.72
A


1122
CG
MET
163
11.753
23.939
65.240
1.00
13.77
A


1123
SD
MET
163
12.554
23.120
66.666
1.00
14.60
A


1124
CE
MET
163
13.550
21.883
65.892
1.00
14.05
A


1125
C
MET
163
14.051
24.763
63.396
1.00
15.21
A


1126
O
MET
163
13.257
24.841
62.437
1.00
9.57
A


1127
N
LEU
164
15.169
24.076
63.480
1.00
12.99
A


1128
CA
LEU
164
15.733
23.268
62.412
1.00
15.09
A


1129
CB
LEU
164
17.233
23.559
62.323
1.00
13.13
A


1130
CG
LEU
164
17.587
25.043
62.253
1.00
16.94
A


1131
CD2
LEU
164
16.854
25.783
61.134
1.00
17.73
A


1132
CD1
LEU
164
19.081
25.277
62.002
1.00
19.46
A


1133
C
LEU
164
15.472
21.773
62.629
1.00
15.31
A


1134
O
LEU
164
16.150
21.115
63.428
1.00
16.41
A


1135
N
TYR
165
14.489
21.302
61.875
1.00
13.24
A


1136
CA
TYR
165
14.031
19.901
61.897
1.00
12.58
A


1137
CB
TYR
165
12.494
19.860
61.889
1.00
13.09
A


1138
CG
TYR
165
11.838
19.868
63.280
1.00
13.99
A


1139
CD1
TYR
165
12.277
18.989
64.279
1.00
15.08
A


1140
CD2
TYR
165
10.781
20.751
63.548
1.00
13.57
A


1141
CE1
TYR
165
11.658
18.992
65.539
1.00
15.28
A


1142
CE2
TYR
165
10.162
20.752
64.804
1.00
14.15
A


1143
CZ
TYR
165
10.599
19.872
65.799
1.00
15.62
A


1144
OH
TYR
165
9.995
19.872
67.019
1.00
15.74
A


1145
C
TYR
165
14.508
19.150
60.634
1.00
13.25
A


1146
O
TYR
165
14.711
19.763
59.572
1.00
12.61
A


1147
N
GLN
166
14.658
17.838
60.813
1.00
13.51
A


1148
CA
GLN
166
15.057
16.877
59.749
1.00
16.56
A


1149
CB
GLN
166
13.934
16.754
58.711
1.00
16.59
A


1150
CG
GLN
166
13.819
15.349
58.130
1.00
14.49
A


1151
CD
GLN
166
13.619
14.297
59.214
1.00
18.48
A


1152
OE1
GLN
166
14.376
13.332
59.281
1.00
23.45
A


1153
NE2
GLN
166
12.635
14.435
60.083
1.00
11.19
A


1154
C
GLN
166
16.305
17.349
59.003
1.00
18.25
A


1155
O
GLN
166
16.386
17.232
57.772
1.00
16.01
A


1156
N
GLN
167
17.258
17.839
59.778
1.00
14.94
A


1157
CA
GLN
167
18.472
18.490
59.238
1.00
15.04
A


1158
CB
GLN
167
19.053
19.437
60.279
1.00
14.35
A


1159
CG
GLN
167
18.094
20.593
60.611
1.00
11.77
A


1160
CD
GLN
167
17.858
21.565
59.441
1.00
15.34
A


1161
OE1
GLN
167
18.805
22.183
58.950
1.00
13.72
A


1162
NE2
GLN
167
16.637
21.751
58.967
1.00
14.07
A


1163
C
GLN
167
19.556
17.508
58.748
1.00
16.24
A


1164
O
GLN
167
20.109
17.669
57.658
1.00
18.12
A


1165
N
GLY
168
19.908
16.510
59.531
1.00
14.08
A


1166
CA
GLY
168
20.893
15.502
59.065
1.00
13.80
A


1167
C
GLY
168
22.334
15.870
59.376
1.00
15.39
A


1168
O
GLY
168
22.695
16.824
60.095
1.00
15.87
A


1169
N
CYS
169
23.253
15.041
58.924
1.00
16.61
A


1170
CA
CYS
169
24.682
15.033
59.298
1.00
16.82
A


1171
CB
CYS
169
25.392
13.842
58.674
1.00
17.31
A


1172
SG
CYS
169
25.104
12.267
59.615
1.00
21.12
A


1173
C
CYS
169
25.514
16.259
58.887
1.00
17.71
A


1174
O
CYS
169
26.670
16.404
59.292
1.00
17.95
A


1177
N
ALA
170
25.000
17.157
58.089
1.00
15.93
A


1178
CA
ALA
170
25.814
18.331
57.718
1.00
16.42
A


1179
CB
ALA
170
25.609
18.686
56.245
1.00
16.83
A


1180
C
ALA
170
25.422
19.552
58.565
1.00
15.01
A


1181
O
ALA
170
26.081
20.595
58.520
1.00
12.25
A


1182
N
ALA
171
24.404
19.320
59.459
1.00
13.18
A


1183
CA
ALA
171
23.796
20.439
60.092
1.00
15.70
A


1184
CB
ALA
171
22.323
20.192
60.450
1.00
14.62
A


1185
C
ALA
171
24.522
20.972
61.337
1.00
13.32
A


1186
O
ALA
171
24.239
22.106
61.766
1.00
16.93
A


1187
N
GLY
172
25.605
20.304
61.727
1.00
14.02
A


1188
CA
GLY
172
26.464
20.929
62.776
1.00
14.32
A


1189
C
GLY
172
27.204
22.091
62.113
1.00
16.85
A


1190
O
GLY
172
27.435
23.150
62.690
1.00
15.28
A


1191
N
GLY
173
27.475
21.983
60.779
1.00
15.85
A


1192
CA
GLY
173
28.015
23.142
60.031
1.00
14.31
A


1193
C
GLY
173
26.917
24.195
59.844
1.00
13.19
A


1194
O
GLY
173
27.078
25.405
60.058
1.00
14.41
A


1195
N
THR
174
25.696
23.736
59.546
1.00
14.08
A


1196
CA
THR
174
24.559
24.669
59.387
1.00
14.30
A


1197
CB
THR
174
23.256
23.908
59.150
1.00
14.77
A


1198
OG1
THR
174
23.371
22.999
58.044
1.00
16.92
A


1199
CG2
THR
174
21.994
24.718
58.884
1.00
13.40
A


1200
C
THR
174
24.387
25.619
60.573
1.00
12.21
A


1201
O
THR
174
24.172
26.823
60.469
1.00
11.17
A


1202
N
VAL
175
24.253
25.072
61.798
1.00
12.71
A


1203
CA
VAL
175
23.972
25.900
62.985
1.00
11.72
A


1204
CB
VAL
175
23.782
25.045
64.260
1.00
9.02
A


1205
CG1
VAL
175
22.608
24.053
64.123
1.00
8.41
A


1206
CG2
VAL
175
24.965
24.150
64.598
1.00
9.19
A


1207
C
VAL
175
25.053
26.949
63.145
1.00
12.00
A


1208
O
VAL
175
24.783
28.079
63.531
1.00
14.66
A


1209
N
LEU
176
26.321
26.603
62.868
1.00
10.98
A


1210
CA
LEU
176
27.388
27.587
63.021
1.00
14.02
A


1211
CB
LEU
176
28.774
26.955
62.842
1.00
14.19
A


1212
CG
LEU
176
29.087
25.850
63.873
1.00
17.06
A


1213
CD2
LEU
176
29.215
26.495
65.278
1.00
18.24
A


1214
CD1
LEU
176
30.354
25.076
63.597
1.00
15.24
A


1215
C
LEU
176
27.214
28.669
61.980
1.00
14.29
A


1216
O
LEU
176
27.468
29.825
62.221
1.00
14.46
A


1217
N
ARG
177
26.849
28.243
60.752
1.00
13.39
A


1218
CA
ARG
177
26.635
29.238
59.649
1.00
13.19
A


1219
CB
ARG
177
26.339
28.381
58.383
1.00
10.10
A


1220
CG
ARG
177
25.772
29.254
57.250
1.00
12.26
A


1221
CD
ARG
177
25.868
28.471
55.943
1.00
12.34
A


1222
NE
ARG
177
25.193
27.181
55.925
1.00
11.28
A


1223
CZ
ARG
177
23.867
27.101
55.696
1.00
10.47
A


1224
NH1
ARG
177
23.120
28.157
55.494
1.00
14.49
A


1225
NH2
ARG
177
23.223
25.969
55.624
1.00
12.71
A


1226
C
ARG
177
25.557
30.211
59.969
1.00
11.64
A


1227
O
ARG
177
25.600
31.430
59.752
1.00
12.90
A


1228
N
LEU
178
24.429
29.643
60.505
1.00
13.45
A


1229
CA
LEU
178
23.350
30.539
60.953
1.00
12.99
A


1230
CB
LEU
178
22.125
29.678
61.304
1.00
14.12
A


1231
CG
LEU
178
20.929
30.356
61.974
1.00
15.67
A


1232
CD2
LEU
178
19.757
29.384
62.173
1.00
15.35
A


1233
CD1
LEU
178
20.337
31.455
61.031
1.00
16.46
A


1234
C
LEU
178
23.703
31.380
62.177
1.00
14.59
A


1235
O
LEU
178
23.447
32.558
62.244
1.00
10.66
A


1236
N
ALA
179
24.311
30.780
63.228
1.00
15.25
A


1237
CA
ALA
179
24.626
31.617
64.424
1.00
15.23
A


1238
CB
ALA
179
25.331
30.699
65.446
1.00
14.84
A


1239
C
ALA
179
25.567
32.747
64.126
1.00
14.68
A


1240
O
ALA
179
25.504
33.869
64.599
1.00
11.42
A


1241
N
LYS
180
26.496
32.500
63.150
1.00
16.39
A


1242
CA
LYS
180
27.444
33.589
62.797
1.00
16.05
A


1243
CB
LYS
180
28.389
33.004
61.699
1.00
17.99
A


1244
CG
LYS
180
29.171
34.095
60.937
1.00
18.86
A


1245
CD
LYS
180
30.424
33.429
60.340
1.00
20.68
A


1246
CE
LYS
180
31.167
34.451
59.505
1.00
21.58
A


1247
NZ
LYS
180
32.094
35.357
60.253
1.00
18.53
A


1248
C
LYS
180
26.758
34.834
62.307
1.00
16.60
A


1249
O
LYS
180
27.022
35.991
62.690
1.00
15.08
A


1250
N
ASP
181
25.747
34.703
61.412
1.00
12.78
A


1251
CA
ASP
181
25.033
35.864
60.910
1.00
13.37
A


1252
CB
ASP
181
24.129
35.506
59.687
1.00
14.96
A


1253
CG
ASP
181
24.955
35.406
58.367
1.00
18.01
A


1254
OD1
ASP
181
25.922
36.128
58.171
1.00
17.53
A


1255
OD2
ASP
181
24.596
34.523
57.518
1.00
16.78
A


1256
C
ASP
181
24.159
36.504
61.998
1.00
14.64
A


1257
O
ASP
181
24.037
37.711
62.116
1.00
14.14
A


1258
N
LEU
182
23.464
35.676
62.791
1.00
13.09
A


1259
CA
LEU
182
22.647
36.267
63.882
1.00
14.86
A


1260
CB
LEU
182
21.940
35.130
64.632
1.00
14.93
A


1261
CG
LEU
182
21.095
34.159
63.851
1.00
13.65
A


1262
CD2
LEU
182
19.988
34.928
63.166
1.00
13.56
A


1263
CD1
LEU
182
20.487
33.085
64.754
1.00
14.92
A


1264
C
LEU
182
23.510
36.991
64.913
1.00
13.35
A


1265
O
LEU
182
23.267
38.149
65.233
1.00
16.44
A


1266
N
ALA
183
24.642
36.381
65.294
1.00
14.86
A


1267
CA
ALA
183
25.462
37.136
66.296
1.00
17.00
A


1268
CB
ALA
183
26.553
36.188
66.788
1.00
17.27
A


1269
C
ALA
183
26.025
38.414
65.744
1.00
17.58
A


1270
O
ALA
183
26.111
39.473
66.378
1.00
16.18
A


1271
N
GLU
184
26.560
38.361
64.491
1.00
16.77
A


1272
CA
GLU
184
27.232
39.496
63.886
1.00
17.91
A


1273
CB
GLU
184
28.123
39.113
62.670
1.00
17.73
A


1274
CG
GLU
184
29.387
38.347
63.096
1.00
16.98
A


1275
CD
GLU
184
30.040
37.632
61.910
1.00
16.92
A


1276
OE1
GLU
184
29.602
37.871
60.746
1.00
16.69
A


1277
OE2
GLU
184
30.968
36.851
62.189
1.00
16.83
A


1278
C
GLU
184
26.295
40.607
63.446
1.00
18.12
A


1279
O
GLU
184
26.702
41.773
63.532
1.00
17.46
A


1280
N
ASN
185
25.035
40.318
63.153
1.00
16.96
A


1281
CA
ASN
185
24.107
41.367
62.780
1.00
17.76
A


1282
CB
ASN
185
23.063
40.888
61.747
1.00
16.68
A


1283
CG
ASN
185
22.468
42.081
61.003
1.00
17.01
A


1284
OD1
ASN
185
23.233
42.919
60.513
1.00
15.96
A


1285
ND2
ASN
185
21.149
42.265
60.951
1.00
15.43
A


1286
C
ASN
185
23.328
41.964
63.955
1.00
18.03
A


1287
O
ASN
185
22.731
43.013
63.716
1.00
18.68
A


1288
N
ASN
186
23.371
41.368
65.135
1.00
17.08
A


1289
CA
ASN
186
22.608
41.863
66.288
1.00
18.13
A


1290
CB
ASN
186
21.572
40.807
66.699
1.00
16.10
A


1291
CG
ASN
186
20.523
40.578
65.611
1.00
18.64
A


1292
OD1
ASN
186
19.547
41.299
65.579
1.00
19.86
A


1293
ND2
ASN
186
20.682
39.594
64.747
1.00
14.98
A


1294
C
ASN
186
23.499
42.226
67.487
1.00
18.41
A


1295
O
ASN
186
24.114
41.367
68.114
1.00
17.04
A


1296
N
LYS
187
23.815
43.507
67.599
1.00
20.13
A


1297
CA
LYS
187
24.735
43.999
68.612
1.00
25.18
A


1298
CB
LYS
187
24.825
45.515
68.465
1.00
29.17
A


1299
CG
LYS
187
25.281
46.242
69.710
1.00
36.89
A


1300
CD
LYS
187
26.705
46.759
69.568
1.00
40.48
A


1301
CE
LYS
187
26.622
48.236
69.176
1.00
42.38
A


1302
NZ
LYS
187
27.043
49.080
70.346
1.00
44.71
A


1303
C
LYS
187
24.293
43.578
70.027
1.00
21.89
A


1304
O
LYS
187
23.147
43.753
70.387
1.00
21.34
A


1305
N
GLY
188
25.201
42.940
70.743
1.00
22.90
A


1306
CA
GLY
188
24.942
42.452
72.108
1.00
22.17
A


1307
C
GLY
188
24.279
41.090
72.129
1.00
23.50
A


1308
O
GLY
188
24.146
40.430
73.170
1.00
20.50
A


1309
N
SER
189
23.977
40.511
70.908
1.00
17.92
A


1310
CA
SER
189
23.208
39.275
70.958
1.00
16.34
A


1311
CB
SER
189
22.596
38.969
69.534
1.00
17.81
A


1312
OG
SER
189
23.703
38.733
68.684
1.00
17.96
A


1313
C
SER
189
24.062
38.132
71.413
1.00
16.41
A


1314
O
SER
189
25.284
38.081
71.236
1.00
14.81
A


1315
N
ARG
190
23.377
37.146
72.057
1.00
13.48
A


1316
CA
ARG
190
24.074
35.932
72.446
1.00
15.78
A


1317
CB
ARG
190
24.387
35.898
73.980
1.00
15.30
A


1318
CG
ARG
190
25.474
36.948
74.311
1.00
13.88
A


1319
CD
ARG
190
26.866
36.358
74.045
1.00
14.87
A


1320
NE
ARG
190
27.965
37.244
74.479
1.00
15.65
A


1321
CZ
ARG
190
28.310
38.313
73.779
1.00
19.62
A


1322
NH1
ARG
190
27.701
38.627
72.589
1.00
19.54
A


1323
NH2
ARG
190
29.389
39.040
74.102
1.00
17.37
A


1324
C
ARC
190
23.168
34.787
72.015
1.00
15.73
A


1325
O
ARG
190
22.016
34.631
72.455
1.00
14.59
A


1326
N
VAL
191
23.774
33.904
71.215
1.00
17.00
A


1327
CA
VAL
191
23.000
32.845
70.579
1.00
16.41
A


1328
CB
VAL
191
23.477
32.589
69.110
1.00
16.72
A


1329
CG1
VAL
191
22.585
31.538
68.437
1.00
17.65
A


1330
CG2
VAL
191
23.506
33.925
68.368
1.00
15.63
A


1331
C
VAL
191
23.314
31.535
71.285
1.00
14.89
A


1332
O
VAL
191
24.477
31.161
71.305
1.00
16.89
A


1333
N
LEU
192
22.278
30.833
71.640
1.00
13.18
A


1334
CA
LEU
192
22.388
29.495
72.157
1.00
14.87
A


1335
CB
LEU
192
21.339
29.259
73.258
1.00
15.46
A


1336
CG
LEU
192
21.225
27.836
73.770
1.00
14.61
A


1337
CD2
LEU
192
20.226
27.716
74.951
1.00
13.51
A


1338
CD1
LEU
192
22.565
27.288
74.246
1.00
15.01
A


1339
C
LEU
192
22.035
28.561
70.981
1.00
14.56
A


1340
O
LEU
192
20.963
28.662
70.425
1.00
15.45
A


1341
N
ILE
193
22.942
27.654
70.681
1.00
14.79
A


1342
CA
ILE
193
22.789
26.668
69.667
1.00
14.89
A


1343
CB
ILE
193
24.110
26.468
68.853
1.00
16.51
A


1344
CG2
ILE
193
24.031
25.107
68.138
1.00
16.50
A


1345
CG1
ILE
193
24.419
27.631
67.941
1.00
17.44
A


1346
CD1
ILE
193
25.800
27.406
67.296
1.00
15.17
A


1347
C
ILE
193
22.575
25.355
70.404
1.00
14.33
A


1348
O
ILE
193
23.389
25.066
71.298
1.00
16.41
A


1349
N
VAL
194
21.534
24.615
70.077
1.00
12.33
A


1350
CA
VAL
194
21.446
23.263
70.571
1.00
13.58
A


1351
CB
VAL
194
20.284
23.160
71.617
1.00
14.48
A


1352
CG1
VAL
194
20.089
21.727
72.073
1.00
13.80
A


1353
CG2
VAL
194
20.576
24.108
72.783
1.00
14.46
A


1354
C
VAL
194
21.168
22.237
69.459
1.00
15.13
A


1355
O
VAL
194
20.115
22.302
68.808
1.00
14.72
A


1356
N
CYS
195
22.058
21.275
69.288
1.00
14.44
A


1357
CA
CYS
195
21.840
20.129
68.445
1.00
16.01
A


1358
CB
CYS
195
23.012
19.805
67.449
1.00
14.49
A


1359
SG
CYS
195
23.288
21.237
66.355
1.00
14.90
A


1360
C
CYS
195
21.621
18.905
69.326
1.00
15.76
A


1361
O
CYS
195
22.498
18.457
70.095
1.00
17.80
A


1362
N
SER
196
20.512
18.230
69.122
1.00
15.08
A


1363
CA
SER
196
20.194
17.064
69.931
1.00
15.38
A


1364
CB
SER
196
19.267
17.612
71.050
1.00
14.75
A


1365
OG
SER
196
18.738
16.521
71.723
1.00
15.86
A


1366
C
SER
196
19.588
15.963
69.093
1.00
14.38
A


1367
O
SER
196
18.577
16.134
68.396
1.00
12.93
A


1368
N
GLU
197
20.252
14.821
69.090
1.00
14.38
A


1369
CA
GLU
197
19.909
13.695
68.263
1.00
15.07
A


1370
CB
GLU
197
21.097
13.510
67.286
1.00
13.16
A


1371
CG
GLU
197
21.425
14.751
66.442
1.00
13.62
A


1372
CD
GLU
197
20.440
14.885
65.267
1.00
15.07
A


1373
OE1
GLU
197
19.321
14.316
65.326
1.00
13.89
A


1374
OE2
GLU
197
20.778
15.640
64.309
1.00
14.15
A


1375
C
GLU
197
19.705
12.424
69.072
1.00
16.83
A


1376
O
GLU
197
20.486
11.959
69.907
1.00
14.52
A


1377
N
ILE
198
18.557
11.810
68.811
1.00
17.45
A


1378
CA
ILE
198
18.225
10.502
69.365
1.00
19.36
A


1379
CB
ILE
198
16.999
10.591
70.293
1.00
18.13
A


1380
CG2
ILE
198
16.549
9.194
70.648
1.00
16.69
A


1381
CG1
ILE
198
17.415
11.418
71.536
1.00
19.63
A


1382
CD1
ILE
198
16.404
11.432
72.627
1.00
20.82
A


1383
C
ILE
198
17.917
9.599
68.162
1.00
18.68
A


1384
O
ILE
198
16.932
9.889
67.485
1.00
19.71
A


1385
N
THR
199
18.669
8.546
68.000
1.00
20.32
A


1386
CA
THR
199
18.566
7.649
66.867
1.00
20.53
A


1387
CB
THR
199
19.908
6.914
66.663
1.00
21.13
A


1388
OG1
THR
199
20.133
6.001
67.771
1.00
22.12
A


1389
CG2
THR
199
21.040
7.914
66.532
1.00
19.49
A


1390
C
THR
199
17.489
6.604
66.896
1.00
21.10
A


1391
O
THR
199
17.331
5.862
65.920
1.00
21.48
A


1392
N
ALA
200
16.593
6.623
67.874
1.00
20.86
A


1393
CA
ALA
200
15.422
5.794
67.919
1.00
20.57
A


1394
CB
ALA
200
14.586
6.016
69.159
1.00
17.68
A


1395
C
ALA
200
14.528
5.992
66.662
1.00
20.56
A


1396
O
ALA
200
13.901
5.003
66.291
1.00
17.87
A


1389
N
ILE
201
14.547
7.157
66.115
0.50
18.88
A


1390
CA
ILE
201
13.719
7.458
64.936
0.50
17.99
A


1391
CB
ILE
201
13.789
8.952
64.592
0.50
16.30
A


1392
CG2
ILE
201
15.132
9.358
63.985
0.50
16.91
A


1393
CG1
ILE
201
12.719
9.394
63.580
0.50
14.60
A


1394
CD1
ILE
201
11.286
9.202
64.089
0.50
11.06
A


1395
C
ILE
201
14.173
6.625
63.720
0.50
17.10
A


1396
O
ILE
201
13.389
6.383
62.788
0.50
18.59
A


1389
N
2ILE
201
14.461
7.125
66.061
0.50
21.70
A


1390
CA
2ILE
201
13.570
7.231
64.885
0.50
22.76
A


1391
CB
2ILE
201
13.310
8.649
64.373
0.50
25.16
A


1392
CG
22ILE
201
12.019
9.250
64.939
0.50
26.21
A


1393
CG
12ILE
201
14.427
9.629
64.673
0.50
25.65
A


1394
CD
12ILE
201
15.720
9.309
63.921
0.50
24.86
A


1395
C
2ILE
201
14.119
6.461
63.693
0.50
20.27
A


1396
O
2ILE
201
13.383
6.161
62.745
0.50
21.36
A


1413
N
LEU
202
15.425
6.166
63.668
1.00
18.05
A


1414
CA
LEU
202
15.958
5.380
62.578
1.00
18.89
A


1415
CB
LEU
202
17.156
6.013
61.864
1.00
18.54
A


1416
CG
LEU
202
18.292
6.576
62.683
1.00
21.58
A


1417
CD2
LEU
202
19.114
7.548
61.835
1.00
23.11
A


1418
CD1
LEU
202
19.180
5.447
63.207
1.00
23.74
A


1419
C
LEU
202
16.372
3.959
62.913
1.00
19.82
A


1420
O
LEU
202
16.979
3.290
62.059
1.00
17.73
A


1421
N
PHE
203
16.030
3.486
64.099
1.00
17.98
A


1422
CA
PHE
203
16.279
2.073
64.420
1.00
18.62
A


1423
CB
PHE
203
15.884
1.869
65.914
1.00
20.06
A


1424
CG
PHE
203
16.111
0.444
66.338
1.00
19.04
A


1425
CD1
PHE
203
15.077
−0.457
66.334
1.00
19.36
A


1426
CD2
PHE
203
17.365
0.075
66.797
1.00
21.11
A


1427
CE1
PHE
203
15.269
−1.767
66.759
1.00
22.06
A


1428
CE2
PHE
203
17.564
−1.245
67.228
1.00
20.23
A


1429
CZ
PHE
203
16.526
−2.143
67.219
1.00
21.46
A


1430
C
PHE
203
15.403
1.154
63.588
1.00
19.66
A


1431
O
PHE
203
14.192
1.422
63.431
1.00
21.19
A


1432
N
HIS
204
15.926
0.051
63.083
1.00
18.97
A


1433
CA
HIS
204
15.164
−0.889
62.266
1.00
22.20
A


1434
ND1
HIS
204
13.226
0.964
60.442
1.00
19.42
A


1435
CG
HIS
204
14.587
0.752
60.363
1.00
19.49
A


1436
CB
HIS
204
15.203
−0.575
60.729
1.00
19.31
A


1437
NE2
HIS
204
14.099
2.829
59.844
1.00
21.11
A


1438
CD2
HIS
204
15.140
1.937
59.994
1.00
19.11
A


1439
CE1
HIS
204
12.945
2.213
60.115
1.00
20.21
A


1440
C
HIS
204
15.725
−2.304
62.461
1.00
21.64
A


1441
O
HIS
204
16.945
−2.480
62.553
1.00
21.58
A


1442
N
GLY
205
14.849
−3.303
62.435
1.00
21.09
A


1443
CA
GLY
205
15.291
−4.707
62.453
1.00
23.18
A


1444
C
GLY
205
15.947
−5.065
61.114
1.00
24.77
A


1445
O
GLY
205
16.032
−4.267
60.168
1.00
25.98
A


1446
N
PRO
206
16.644
−6.190
61.054
1.00
25.87
A


1447
CA
PRO
206
17.458
−6.545
59.904
1.00
27.34
A


1448
CD
PRO
206
16.742
−7.204
62.137
1.00
26.44
A


1449
CB
PRO
206
18.398
−7.619
60.444
1.00
27.19
A


1450
CG
PRO
206
17.584
−8.280
61.507
1.00
26.88
A


1451
C
PRO
206
16.617
−7.054
58.768
1.00
29.39
A


1452
O
PRO
206
15.548
−7.658
58.967
1.00
30.52
A


1453
N
ASN
207
17.039
−6.756
57.545
1.00
31.69
A


1454
CA
ASN
207
16.328
−7.260
56.358
1.00
32.51
A


1455
CB
ASN
207
15.114
−6.402
56.029
1.00
33.65
A


1456
CG
ASN
207
14.435
−6.828
54.729
1.00
35.71
A


1457
OD1
ASN
207
14.943
−6.533
53.648
1.00
35.08
A


1458
ND2
ASN
207
13.310
−7.515
54.771
1.00
34.18
A


1459
C
ASN
207
17.302
−7.345
55.168
1.00
33.19
A


1460
O
ASN
207
17.979
−6.366
54.821
1.00
29.39
A


1461
N
GLU
208
17.310
−8.541
54.610
1.00
35.87
A


1462
CA
GLU
208
18.174
−8.962
53.489
1.00
39.04
A


1463
CB
GLU
208
17.633
−10.223
52.845
1.00
45.25
A


1464
CG
GLU
208
18.171
−11.507
53.439
1.00
51.38
A


1465
CD
GLU
208
17.231
−12.656
53.137
1.00
55.49
A


1466
OE1
GLU
208
16.975
−12.963
51.911
1.00
55.90
A


1467
OE2
GLU
208
16.679
−13.292
54.105
1.00
59.14
A


1468
C
GLU
208
18.217
−7.998
52.308
1.00
36.43
A


1469
O
GLU
208
19.268
−7.797
51.687
1.00
35.95
A


1470
N
ASN
209
17.074
−7.441
51.993
1.00
34.14
A


1471
CA
ASN
209
16.938
−6.577
50.818
1.00
34.13
A


1472
CB
ASN
209
15.522
−6.698
50.279
1.00
37.32
A


1473
CG
ASN
209
15.163
−8.157
50.012
1.00
39.65
A


1474
OD1
ASN
209
15.910
−8.850
49.320
1.00
40.89
A


1475
ND2
ASN
209
14.070
−8.676
50.533
1.00
39.96
A


1476
C
ASN
209
17.276
−5.115
51.130
1.00
32.88
A


1477
O
ASN
209
17.180
−4.237
50.270
1.00
32.04
A


1478
N
HIS
210
17.679
−4.841
52.354
1.00
31.55
A


1479
CA
HIS
210
18.060
−3.464
52.732
1.00
30.75
A


1480
ND1
HIS
210
14.723
−3.581
52.479
1.00
34.00
A


1481
CG
HIS
210
15.677
−2.583
52.636
1.00
34.22
A


1482
CB
HIS
210
16.921
−2.790
53.503
1.00
32.00
A


1483
NE2
HIS
210
14.076
−1.906
51.315
1.00
34.55
A


1484
CD2
HIS
210
15.246
−1.527
51.891
1.00
34.19
A


1485
CE1
HIS
210
13.779
−3.129
51.675
1.00
33.70
A


1486
C
HIS
210
19.335
−3.500
53.572
1.00
29.56
A


1487
O
HIS
210
19.313
−3.274
54.785
1.00
27.00
A


1488
N
LEU
211
20.435
−3.774
52.892
1.00
27.70
A


1489
CA
LEU
211
21.737
−3.913
53.553
1.00
28.08
A


1490
CB
LEU
211
22.744
−4.590
52.630
1.00
27.02
A


1491
CG
LEU
211
22.351
−6.031
52.294
1.00
29.47
A


1492
CD2
LEU
211
22.327
−6.959
53.513
1.00
30.67
A


1493
CD1
LEU
211
23.297
−6.685
51.286
1.00
29.25
A


1494
C
LEU
211
22.293
−2.583
54.019
1.00
26.99
A


1495
O
LEU
211
23.056
−2.576
54.983
1.00
24.96
A


1496
N
ASP
212
21.908
−1.479
53.384
1.00
27.06
A


1497
CA
ASP
212
22.377
−0.158
53.810
1.00
26.42
A


1498
CB
ASP
212
22.061
0.892
52.762
1.00
26.67
A


1499
CG
ASP
212
20.705
0.831
52.114
1.00
26.42
A


1500
OD1
ASP
212
19.920
−0.127
52.306
1.00
26.01
A


1501
OD2
ASP
212
20.376
1.811
51.396
1.00
26.03
A


1502
C
ASP
212
21.683
0.226
55.132
1.00
25.93
A


1503
O
ASP
212
22.225
0.860
56.034
1.00
23.85
A


1504
N
SER
213
20.410
−0.169
55.210
1.00
25.35
A


1505
CA
SER
213
19.657
0.004
56.454
1.00
28.05
A


1506
CB
SER
213
18.169
−0.310
56.239
1.00
29.07
A


1507
OG
SER
213
17.504
−0.103
57.466
1.00
34.43
A


1508
C
SER
213
20.269
−0.842
57.571
1.00
27.93
A


1509
O
SER
213
20.327
−0.407
58.727
1.00
27.08
A


1510
N
LEU
214
20.842
−2.005
57.258
1.00
26.89
A


1511
CA
LEU
214
21.562
−2.810
58.245
1.00
26.87
A


1512
CB
LEU
214
21.833
−4.241
57.732
1.00
25.91
A


1513
CG
LEU
214
22.581
−5.164
58.693
1.00
27.85
A


1514
CD2
LEU
214
23.032
−6.438
57.972
1.00
26.84
A


1515
CD1
LEU
214
21.682
−5.519
59.887
1.00
24.51
A


1516
C
LEU
214
22.857
−2.137
58.664
1.00
25.66
A


1517
O
LEU
214
23.122
−1.961
59.870
1.00
23.41
A


1518
N
VAL
215
23.617
−1.571
57.715
1.00
24.14
A


1519
CA
VAL
215
24.837
−0.863
58.008
1.00
24.72
A


1520
CB
VAL
215
25.566
−0.287
56.771
1.00
25.01
A


1521
CG1
VAL
215
26.611
0.742
57.174
1.00
21.78
A


1522
CG2
VAL
215
26.240
−1.392
55.945
1.00
26.32
A


1523
C
VAL
215
24.533
0.295
58.950
1.00
24.78
A


1524
O
VAL
215
25.259
0.482
59.939
1.00
25.77
A


1525
N
ALA
216
23.443
1.009
58.663
1.00
22.29
A


1526
CA
ALA
216
23.021
2.120
59.478
1.00
22.75
A


1527
CB
ALA
216
21.743
2.766
58.928
1.00
22.71
A


1528
C
ALA
216
22.722
1.774
60.943
1.00
23.23
A


1529
O
ALA
216
22.973
2.640
61.770
1.00
20.20
A


1530
N
GLN
217
22.412
0.526
61.287
1.00
24.45
A


1531
CA
GLN
217
22.177
0.159
62.695
1.00
24.33
A


1532
CB
GLN
217
21.419
−1.166
62.722
1.00
23.47
A


1533
CG
GLN
217
20.120
−1.190
61.895
1.00
24.28
A


1534
CD
GLN
217
19.244
0.031
62.195
1.00
24.61
A


1535
OE1
GLN
217
18.890
0.212
63.378
1.00
22.76
A


1536
NE2
GLN
217
18.951
0.862
61.205
1.00
19.95
A


1537
C
GLN
217
23.472
0.162
63.501
1.00
25.07
A


1538
O
GLN
217
23.441
0.169
64.758
1.00
26.55
A


1539
N
ALA
218
24.616
0.201
62.826
1.00
22.34
A


1540
CA
ALA
218
25.916
0.220
63.470
1.00
23.77
A


1541
CB
ALA
218
26.896
−0.742
62.787
1.00
22.04
A


1542
C
ALA
218
26.550
1.591
63.530
1.00
22.94
A


1543
O
ALA
218
27.586
1.694
64.221
1.00
23.52
A


1544
N
LEU
219
26.005
2.632
62.876
1.00
20.23
A


1545
CA
LEU
219
26.816
3.853
62.773
1.00
20.51
A


1546
CB
LEU
219
26.501
4.568
61.419
1.00
21.57
A


1547
CG
LEU
219
26.846
3.797
60.116
1.00
23.93
A


1548
CD2
LEU
219
28.345
3.552
60.007
1.00
23.19
A


1549
CD1
LEU
219
26.443
4.588
58.861
1.00
22.16
A


1550
C
LEU
219
26.567
4.911
63.838
1.00
20.63
A


1551
O
LEU
219
27.411
5.786
64.020
1.00
22.27
A


1552
N
PHE
220
25.307
5.047
64.276
1.00
18.63
A


1553
CA
PHE
220
24.840
6.263
64.910
1.00
18.81
A


1554
CB
PHE
220
23.429
6.607
64.343
1.00
19.71
A


1555
CG
PHE
220
23.451
6.886
62.842
1.00
19.21
A


1556
CD1
PHE
220
22.923
5.928
61.969
1.00
18.79
A


1557
CD2
PHE
220
24.015
8.040
62.364
1.00
18.11
A


1558
CE1
PHE
220
22.944
6.174
60.588
1.00
19.76
A


1559
CE2
PHE
220
24.023
8.299
60.982
1.00
22.11
A


1560
CZ
PHE
220
23.516
7.348
60.110
1.00
20.52
A


1561
C
PHE
220
24.662
6.123
66.429
1.00
17.23
A


1562
O
PHE
220
24.062
5.140
66.839
1.00
14.86
A


1563
N
GLY
221
24.914
7.207
67.127
1.00
19.72
A


1564
CA
GLY
221
24.738
7.156
68.607
1.00
22.07
A


1565
C
GLY
221
23.953
8.443
68.933
1.00
23.22
A


1566
O
GLY
221
23.705
9.294
68.031
1.00
20.48
A


1567
N
ASP
222
23.608
8.517
70.219
1.00
21.18
A


1568
CA
ASP
222
22.810
9.647
70.715
1.00
18.61
A


1569
CB
ASP
222
21.625
9.171
71.574
1.00
17.56
A


1570
CG
ASP
222
20.686
8.258
70.871
1.00
19.05
A


1571
OD1
ASP
222
20.865
7.974
69.631
1.00
19.17
A


1572
OD2
ASP
222
19.735
7.705
71.479
1.00
20.12
A


1573
C
ASP
222
23.581
10.656
71.492
1.00
16.80
A


1574
O
ASP
222
24.528
10.296
72.204
1.00
18.14
A


1575
N
GLY
223
23.198
11.939
71.329
1.00
16.62
A


1576
CA
GLY
223
23.863
13.007
72.027
1.00
16.89
A


1577
C
GLY
223
23.341
14.403
71.684
1.00
18.35
A


1578
O
GLY
223
22.634
14.608
70.699
1.00
19.09
A


1579
N
ALA
224
23.716
15.348
72.540
1.00
16.74
A


1580
CA
ALA
224
23.382
16.765
72.339
1.00
15.69
A


1581
CB
ALA
224
22.184
17.191
73.187
1.00
15.29
A


1582
C
ALA
224
24.574
17.641
72.719
1.00
16.88
A


1583
O
ALA
224
25.284
17.362
73.696
1.00
16.03
A


1584
N
ALA
225
24.748
18.662
71.915
1.00
17.12
A


1585
CA
ALA
225
25.781
19.675
72.125
1.00
17.04
A


1586
CB
ALA
225
26.822
19.628
71.005
1.00
17.62
A


1587
C
ALA
225
25.107
21.039
72.133
1.00
16.59
A


1588
O
ALA
225
24.143
21.276
71.394
1.00
16.15
A


1589
N
ALA
226
25.619
21.901
72.974
1.00
14.82
A


1590
CA
ALA
226
25.105
23.266
73.101
1.00
14.36
A


1591
CB
ALA
226
24.302
23.405
74.395
1.00
15.96
A


1592
C
ALA
226
26.277
24.237
73.106
1.00
15.68
A


1593
O
ALA
226
27.324
23.977
73.709
1.00
16.67
A


1594
N
LEU
227
26.079
25.338
72.426
1.00
14.94
A


1595
CA
LEU
227
27.102
26.376
72.311
1.00
15.69
A


1596
CB
LEU
227
27.635
26.458
70.871
1.00
15.95
A


1597
CG
LEU
227
28.772
25.490
70.547
1.00
18.96
A


1598
CD2
LEU
227
29.427
25.789
69.191
1.00
19.61
A


1599
CD1
LEU
227
28.306
24.038
70.472
1.00
21.33
A


1600
C
LEU
227
26.510
27.745
72.569
1.00
14.11
A


1601
O
LEU
227
25.330
27.989
72.297
1.00
15.41
A


1602
N
ILE
228
27.345
28.596
73.096
1.00
14.17
A


1603
CA
ILE
228
27.012
30.006
73.236
1.00
14.85
A


1604
CB
ILE
228
27.267
30.526
74.651
1.00
18.48
A


1605
CG2
ILE
228
26.980
32.030
74.778
1.00
19.00
A


1606
CG1
ILE
228
26.412
29.838
75.718
1.00
19.80
A


1607
CD1
ILE
228
24.934
30.231
75.668
1.00
16.73
A


1608
C
ILE
228
27.912
30.731
72.252
1.00
15.99
A


1609
O
ILE
228
29.141
30.575
72.293
1.00
14.79
A


1610
N
VAL
229
27.286
31.478
71.376
1.00
15.18
A


1611
CA
VAL
229
28.003
32.237
70.344
1.00
15.14
A


1612
CB
VAL
229
27.635
31.739
68.949
1.00
16.86
A


1613
CG1
VAL
229
28.226
32.615
67.839
1.00
14.92
A


1614
CG2
VAL
229
28.124
30.320
68.673
1.00
14.91
A


1615
C
VAL
229
27.623
33.703
70.402
1.00
15.54
A


1616
O
VAL
229
26.450
34.056
70.565
1.00
16.90
A


1617
N
GLY
230
28.626
34.534
70.256
1.00
15.38
A


1618
CA
GLY
230
28.415
35.976
70.275
1.00
15.59
A


1619
C
GLY
230
29.611
36.714
69.662
1.00
14.62
A


1620
O
GLY
230
30.710
36.182
69.655
1.00
15.54
A


1621
N
SER
231
29.365
37.939
69.206
1.00
15.66
A


1622
CA
SER
231
30.393
38.816
68.696
1.00
18.35
A


1623
CB
SER
231
29.874
39.655
67.476
1.00
19.73
A


1624
OG
SER
231
29.673
38.784
66.362
1.00
20.99
A


1625
C
SER
231
30.744
39.837
69.801
1.00
17.97
A


1626
O
SER
231
29.907
40.112
70.654
1.00
18.04
A


1627
N
GLY
232
31.911
40.446
69.789
1.00
17.80
A


1628
CA
GLY
232
32.231
41.445
70.839
1.00
19.53
A


1629
C
GLY
232
32.215
40.831
72.236
1.00
19.73
A


1630
O
GLY
232
31.435
41.187
73.120
1.00
22.75
A


1631
N
PRO
233
33.015
39.819
72.495
1.00
20.79
A


1632
CA
PRO
233
33.130
39.161
73.784
1.00
22.44
A


1633
CD
PRO
233
34.020
39.273
71.545
1.00
21.24
A


1634
CB
PRO
233
34.172
38.049
73.590
1.00
21.15
A


1635
CG
PRO
233
34.400
37.954
72.120
1.00
21.44
A


1636
C
PRO
233
33.604
40.149
74.864
1.00
22.27
A


1637
O
PRO
233
34.330
41.141
74.640
1.00
19.50
A


1638
N
HIS
234
32.901
40.097
76.002
1.00
22.16
A


1639
CA
HIS
234
33.339
40.937
77.165
1.00
23.15
A


1640
ND1
HIS
234
29.958
41.328
76.884
1.00
35.17
A


1641
CG
HIS
234
31.078
41.977
77.390
1.00
30.81
A


1642
CB
HIS
234
32.182
41.269
78.102
1.00
27.51
A


1643
NE2
HIS
234
29.741
43.370
76.323
1.00
35.82
A


1644
CD2
HIS
234
30.941
43.265
77.019
1.00
35.34
A


1645
CE1
HIS
234
29.175
42.190
76.256
1.00
34.13
A


1646
C
HIS
234
34.418
40.103
77.832
1.00
20.60
A


1647
O
HIS
234
34.116
39.200
78.630
1.00
19.16
A


1648
N
LEU
235
35.651
40.448
77.520
1.00
16.35
A


1649
CA
LEU
235
36.796
39.635
77.925
1.00
18.16
A


1650
CB
LEU
235
38.083
40.119
77.236
1.00
18.81
A


1651
CG
LEU
235
38.000
40.095
75.692
1.00
21.47
A


1652
CD2
LEU
235
37.807
38.679
75.168
1.00
21.10
A


1653
CD1
LEU
235
39.310
40.642
75.081
1.00
21.54
A


1654
C
LEU
235
37.066
39.504
79.428
1.00
17.07
A


1655
O
LEU
235
37.672
38.503
79.830
1.00
17.50
A


1656
N
ALA
236
36.583
40.438
80.209
1.00
19.10
A


1657
CA
ALA
236
36.751
40.302
81.675
1.00
21.23
A


1658
CB
ALA
236
36.162
41.556
82.316
1.00
20.52
A


1659
C
ALA
236
36.064
39.026
82.109
1.00
20.15
A


1660
O
ALA
236
36.467
38.329
83.046
1.00
20.26
A


1661
N
VAL
237
34.912
38.674
81.517
1.00
19.13
A


1662
CA
VAL
237
34.101
37.552
82.009
1.00
17.70
A


1663
CB
VAL
237
32.801
38.109
82.621
1.00
16.79
A


1664
CG1
VAL
237
33.087
39.149
83.738
1.00
17.70
A


1665
CG2
VAL
237
31.887
38.838
81.616
1.00
18.15
A


1666
C
VAL
237
33.776
36.489
80.979
1.00
20.33
A


1667
O
VAL
237
33.406
35.369
81.379
1.00
20.85
A


1668
N
GLU
238
33.953
36.754
79.675
1.00
20.13
A


1669
CA
GLU
238
33.642
35.691
78.681
1.00
20.82
A


1670
CB
GLU
238
32.698
36.229
77.592
1.00
21.43
A


1671
CG
GLU
238
31.368
36.751
78.026
1.00
20.52
A


1672
CD
GLU
238
30.490
37.238
76.859
1.00
22.45
A


1673
OE1
GLU
238
30.889
38.201
76.181
1.00
20.38
A


1674
OE2
GLU
238
29.398
36.671
76.665
1.00
21.83
A


1675
C
GLU
238
34.926
35.177
78.082
1.00
19.34
A


1676
O
GLU
238
35.877
35.955
77.983
1.00
21.58
A


1677
N
ARG
239
35.009
33.910
77.733
1.00
21.12
A


1678
CA
ARG
239
36.216
33.263
77.257
1.00
22.23
A


1679
CB
ARG
239
36.524
32.072
78.207
1.00
25.73
A


1680
CG
ARG
239
37.759
31.259
77.923
1.00
30.57
A


1681
CD
ARG
239
38.148
30.209
78.941
1.00
35.65
A


1682
NE
ARG
239
37.243
29.095
79.152
1.00
39.77
A


1683
CZ
ARG
239
37.280
27.784
79.297
1.00
42.53
A


1684
NH1
ARG
239
38.385
27.022
79.243
1.00
42.40
A


1685
NH2
ARG
239
36.137
27.097
79.519
1.00
42.16
A


1686
C
ARG
239
36.026
32.719
75.832
1.00
19.54
A


1687
O
ARG
239
35.664
31.556
75.686
1.00
18.01
A


1688
N
PRO
240
36.545
33.430
74.842
1.00
20.95
A


1689
CA
PRO
240
36.590
32.962
73.452
1.00
18.08
A


1690
CD
PRO
240
36.999
34.836
74.914
1.00
21.55
A


1691
CB
PRO
240
37.390
34.047
72.724
1.00
21.14
A


1692
CG
PRO
240
36.962
35.309
73.449
1.00
21.46
A


1693
C
PRO
240
37.277
31.643
73.337
1.00
19.07
A


1694
O
PRO
240
38.297
31.353
73.986
1.00
19.18
A


1695
N
ILE
241
36.721
30.753
72.523
1.00
18.31
A


1696
CA
ILE
241
37.291
29.428
72.275
1.00
19.83
A


1697
CB
ILE
241
36.234
28.333
72.548
1.00
19.49
A


1698
CG2
ILE
241
36.878
26.957
72.345
1.00
19.51
A


1699
CG1
ILE
241
35.632
28.482
73.949
1.00
20.96
A


1700
CD1
ILE
241
34.579
27.465
74.392
1.00
19.62
A


1701
C
ILE
241
37.791
29.336
70.829
1.00
21.55
A


1702
O
ILE
241
38.882
28.859
70.512
1.00
19.61
A


1703
N
PHE
242
36.934
29.754
69.894
1.00
20.18
A


1704
CA
PHE
242
37.174
29.805
68.462
1.00
21.43
A


1705
CB
PHE
242
36.689
28.534
67.733
1.00
18.71
A


1706
CG
PHE
242
37.494
27.318
68.067
1.00
20.98
A


1707
CD1
PHE
242
38.802
27.211
67.612
1.00
21.85
A


1708
CD2
PHE
242
36.968
26.314
68.866
1.00
19.93
A


1709
CE1
PHE
242
39.558
26.106
67.927
1.00
22.01
A


1710
CE2
PHE
242
37.725
25.213
69.185
1.00
20.01
A


1711
CZ
PHE
242
39.028
25.096
68.707
1.00
23.41
A


1712
C
PHE
242
36.346
30.925
67.827
1.00
21.27
A


1713
O
PHE
242
35.205
31.172
68.262
1.00
21.03
A


1714
N
GLU
243
36.884
31.605
66.819
1.00
21.66
A


1715
CA
GLU
243
36.073
32.593
66.108
1.00
21.05
A


1716
CB
GLU
243
36.812
33.838
65.740
1.00
23.06
A


1717
CG
GLU
243
37.306
34.658
66.935
1.00
26.19
A


1718
CD
GLU
243
38.280
35.712
66.421
1.00
28.12
A


1719
OE1
GLU
243
39.310
35.317
65.866
1.00
28.85
A


1720
OE2
GLU
243
37.934
36.889
66.576
1.00
29.67
A


1721
C
GLU
243
35.556
31.867
64.822
1.00
20.93
A


1722
O
GLU
243
36.297
31.031
64.298
1.00
19.28
A


1723
N
ILE
244
34.369
32.235
64.370
1.00
20.74
A


1724
CA
ILE
244
33.792
31.627
63.147
1.00
18.87
A


1725
CB
ILE
244
32.303
31.303
63.242
1.00
19.41
A


1726
CG2
ILE
244
31.879
30.417
62.045
1.00
17.16
A


1727
CG1
ILE
244
31.924
30.529
64.535
1.00
19.59
A


1728
CD1
ILE
244
30.399
30.611
64.826
1.00
19.07
A


1729
C
ILE
244
34.152
32.547
61.977
1.00
16.35
A


1730
O
ILE
244
33.588
33.605
61.829
1.00
16.20
A


1731
N
VAL
245
35.191
32.157
61.222
1.00
17.78
A


1732
CA
VAL
245
35.720
33.000
60.151
1.00
18.85
A


1733
CB
VAL
245
37.140
32.519
59.749
1.00
19.07
A


1734
CG1
VAL
245
37.680
33.512
58.717
1.00
19.26
A


1735
CG2
VAL
245
38.073
32.496
60.995
1.00
20.02
A


1736
C
VAL
245
34.866
33.034
58.877
1.00
16.35
A


1737
O
VAL
245
34.518
34.094
58.380
1.00
17.59
A


1738
N
SER
246
34.580
31.860
58.307
1.00
15.50
A


1739
CA
SER
246
33.761
31.847
57.092
1.00
15.90
A


1740
CB
SER
246
34.758
32.000
55.872
1.00
17.77
A


1741
CG
SER
246
35.465
30.750
55.794
1.00
18.94
A


1742
C
SER
246
33.005
30.556
57.051
1.00
16.37
A


1743
O
SER
246
33.348
29.541
57.697
1.00
14.51
A


1744
N
THR
247
31.898
30.536
56.278
1.00
15.35
A


1745
CA
THR
247
31.083
29.353
56.113
1.00
16.46
A


1746
CB
THR
247
29.760
29.445
56.919
1.00
16.78
A


1747
OG1
THR
247
29.052
30.622
56.477
1.00
17.47
A


1748
CG2
THR
247
30.077
29.665
58.403
1.00
16.52
A


1749
C
THR
247
30.694
29.237
54.622
1.00
18.21
A


1750
O
THR
247
30.504
30.205
53.889
1.00
16.99
A


1735
N
ASP
248
30.618
28.005
54.197
0.50
18.71
A


1736
CA
ASP
248
30.218
27.675
52.827
0.50
19.09
A


1737
CB
ASP
248
31.440
27.391
51.944
0.50
19.78
A


1738
CG
ASP
248
32.410
28.566
51.812
0.50
20.71
A


1739
OD1
ASP
248
31.968
29.747
51.547
0.50
21.41
A


1740
OD2
ASP
248
33.677
28.369
51.963
0.50
23.49
A


1741
C
ASP
248
29.379
26.409
52.848
0.50
19.03
A


1742
O
ASP
248
29.599
25.514
53.671
0.50
18.88
A


1735
N
2ASP
248
30.604
28.004
54.204
0.50
18.31
A


1736
CA
2ASP
248
30.193
27.679
52.839
0.50
18.44
A


1737
CB
2ASP
248
31.407
27.434
51.937
0.50
18.29
A


1738
CG
2ASP
248
31.017
26.889
50.555
0.50
18.92
A


1739
OD
12ASP
248
30.690
27.704
49.608
0.50
18.93
A


1740
OD
22ASP
248
31.012
25.617
50.335
0.50
19.50
A


1741
C
2ASP
248
29.358
26.413
52.864
0.50
18.56
A


1742
O
2ASP
248
29.566
25.532
53.705
0.50
18.48
A


1767
N
GLN
249
28.356
26.417
51.935
1.00
18.12
A


1768
CA
GLN
249
27.549
25.224
51.800
1.00
15.48
A


1769
CB
GLN
249
26.099
25.564
52.196
1.00
14.70
A


1770
CG
GLN
249
25.215
24.313
52.232
1.00
17.53
A


1771
CD
GLN
249
23.779
24.633
52.622
1.00
18.03
A


1772
OE1
GLN
249
23.386
25.788
52.526
1.00
20.85
A


1773
NE2
GLN
249
22.986
23.664
53.058
1.00
16.17
A


1774
C
GLN
249
27.516
24.887
50.297
1.00
17.28
A


1775
O
GLN
249
27.276
25.811
49.490
1.00
16.93
A


1752
N
THR
250
27.724
23.697
49.878
0.50
18.63
A


1753
CA
THR
250
27.626
23.389
48.445
0.50
19.72
A


1754
CB
THR
250
28.923
23.758
47.706
0.50
20.75
A


1755
OG1
THR
250
28.976
23.090
46.452
0.50
20.74
A


1756
CG2
THR
250
30.197
23.409
48.469
0.50
19.75
A


1757
C
THR
250
27.254
21.928
48.211
0.50
19.36
A


1758
O
THR
250
27.694
21.020
48.928
0.50
20.20
A


1752
N
2THR
250
27.757
23.701
49.893
0.50
17.80
A


1753
CA
2THR
250
27.697
23.337
48.471
0.50
18.17
A


1754
CB
2THR
250
29.094
23.333
47.827
0.50
17.92
A


1755
OG
12THR
250
29.903
22.324
48.410
0.50
19.85
A


1756
CG
22THR
250
29.837
24.663
47.974
0.50
13.72
A


1757
C
2THR
250
27.085
21.959
48.296
0.50
18.46
A


1758
O
2THR
250
27.144
21.111
49.195
0.50
19.35
A


1790
N
ILE
251
26.420
21.812
47.160
1.00
18.11
A


1791
CA
ILE
251
25.899
20.518
46.744
1.00
18.91
A


1792
CB
ILE
251
24.566
20.777
46.018
1.00
21.43
A


1793
CG2
ILE
251
24.079
19.563
45.255
1.00
21.91
A


1794
CG1
ILE
251
23.458
21.230
47.008
1.00
19.84
A


1795
CD1
ILE
251
22.343
21.902
46.184
1.00
21.62
A


1796
C
ILE
251
26.917
19.804
45.865
1.00
20.29
A


1797
O
ILE
251
27.373
20.421
44.904
1.00
18.39
A


1798
N
LEU
252
27.242
18.561
46.132
1.00
19.21
A


1799
CA
LEU
252
28.247
17.856
45.333
1.00
21.24
A


1800
CB
LEU
252
28.874
16.732
46.167
1.00
20.16
A


1801
CG
LEU
252
29.544
17.115
47.496
1.00
22.74
A


1802
CD2
LEU
252
30.589
18.196
47.306
1.00
20.38
A


1803
CD1
LEU
252
30.144
15.834
48.104
1.00
21.35
A


1804
C
LEU
252
27.540
17.343
44.067
1.00
21.53
A


1805
O
LEU
252
26.496
16.711
44.166
1.00
20.81
A


1806
N
PRO
253
28.125
17.540
42.891
1.00
23.96
A


1807
CA
PRO
253
27.503
17.137
41.637
1.00
24.00
A


1808
CD
PRO
253
29.384
18.295
42.669
1.00
24.04
A


1809
CB
PRO
253
28.477
17.645
40.537
1.00
27.26
A


1810
CG
PRO
253
29.758
17.845
41.256
1.00
26.43
A


1811
C
PRO
253
27.321
15.652
41.520
1.00
21.79
A


1812
O
PRO
253
28.160
14.836
41.927
1.00
23.62
A


1813
N
ASP
254
26.184
15.233
40.995
1.00
20.90
A


1814
CA
ASP
254
25.847
13.868
40.696
1.00
22.65
A


1815
CB
ASP
254
26.866
13.340
39.636
1.00
24.22
A


1816
CG
ASP
254
26.758
14.178
38.352
1.00
23.48
A


1817
OD1
ASP
254
25.656
14.260
37.820
1.00
23.35
A


1818
OD2
ASP
254
27.702
14.827
37.926
1.00
24.65
A


1819
C
ASP
254
25.915
12.933
41.901
1.00
23.89
A


1820
O
ASP
254
26.435
11.817
41.786
1.00
20.61
A


1821
N
THR
255
25.475
13.405
43.084
1.00
23.24
A


1822
CA
THR
255
25.539
12.504
44.271
1.00
22.38
A


1823
CB
THR
255
26.529
13.102
45.269
1.00
22.65
A


1824
OG1
THR
255
26.047
14.426
45.616
1.00
21.38
A


1825
CG2
THR
255
27.937
13.179
44.660
1.00
21.77
A


1826
C
THR
255
24.185
12.406
44.964
1.00
25.76
A


1827
O
THR
255
24.060
11.927
46.099
1.00
24.90
A


1828
N
GLU
256
23.128
12.826
44.279
1.00
26.04
A


1829
CA
GLU
256
21.798
12.886
44.836
1.00
30.86
A


1830
CB
GLU
256
20.747
13.428
43.862
1.00
32.70
A


1831
CG
GLU
256
19.388
13.594
44.527
1.00
36.12
A


1832
CD
GLU
256
18.316
14.007
43.540
1.00
38.83
A


1833
OE1
GLU
256
17.152
13.468
43.598
1.00
40.66
A


1834
OE2
GLU
256
18.588
14.893
42.648
1.00
38.96
A


1835
C
GLU
256
21.320
11.539
45.377
1.00
31.91
A


1836
O
GLU
256
20.679
11.464
46.430
1.00
31.93
A


1837
N
LYS
257
21.633
10.469
44.689
1.00
31.65
A


1838
CA
LYS
257
21.152
9.147
45.116
1.00
35.38
A


1839
CB
LYS
257
21.043
8.222
43.910
1.00
39.99
A


1840
CG
LYS
257
19.783
8.517
43.089
1.00
45.71
A


1841
CD
LYS
257
19.467
7.440
42.058
1.00
51.11
A


1842
CE
LYS
257
18.956
8.012
40.735
1.00
53.47
A


1843
NZ
LYS
257
18.536
6.968
39.790
1.00
56.09
A


1844
C
LYS
257
22.049
8.525
46.211
1.00
32.87
A


1845
O
LYS
257
21.790
7.419
46.698
1.00
34.25
A


1846
N
ALA
258
23.082
9.246
46.612
1.00
29.70
A


1847
CA
ALA
258
24.024
8.771
47.656
1.00
30.43
A


1848
CB
ALA
258
25.138
9.793
47.873
1.00
28.35
A


1849
C
ALA
258
23.323
8.565
49.021
1.00
27.90
A


1850
O
ALA
258
23.576
7.571
49.723
1.00
24.05
A


1851
N
MET
259
22.464
9.523
49.368
1.00
25.76
A


1852
CA
MET
259
21.726
9.522
50.658
1.00
25.87
A


1853
C
MET
259
20.309
10.047
50.545
1.00
21.93
A


1854
O
MET
259
20.083
11.221
50.262
1.00
23.58
A


1855
CB
MET
259
22.297
10.527
51.653
1.00
27.22
A


1856
CG
MET
259
23.705
10.233
52.098
1.00
28.27
A


1857
SD
MET
259
24.372
11.515
53.127
1.00
27.33
A


1858
CE
MET
259
26.025
11.066
53.579
1.00
25.33
A


1859
N
LYS
260
19.358
9.201
50.793
1.00
20.47
A


1860
CA
LYS
260
17.965
9.639
50.800
1.00
21.83
A


1861
CB
LYS
260
17.256
9.175
49.537
1.00
23.80
A


1862
CG
LYS
260
17.673
9.960
48.296
1.00
29.10
A


1863
CD
LYS
260
16.888
9.531
47.064
1.00
31.39
A


1864
CE
LYS
260
17.270
10.303
45.807
1.00
35.56
A


1865
NZ
LYS
260
16.189
10.333
44.812
1.00
38.58
A


1866
C
LYS
260
17.292
9.033
52.028
1.00
19.21
A


1867
O
LYS
260
17.425
7.840
52.275
1.00
22.29
A


1868
N
LEU
261
16.617
9.836
52.822
1.00
18.40
A


1869
CA
LEU
261
15.950
9.346
54.038
1.00
17.05
A


1870
CB
LEU
261
16.720
9.682
55.307
1.00
17.21
A


1871
CG
LEU
261
18.166
9.207
55.474
1.00
17.40
A


1872
CD2
LEU
261
18.529
9.086
56.953
1.00
16.95
A


1873
CD1
LEU
261
19.166
10.165
54.847
1.00
14.73
A


1874
C
LEU
261
14.536
9.894
54.066
1.00
16.09
A


1875
O
LEU
261
14.295
11.071
53.924
1.00
14.50
A


1876
N
HIS
262
13.548
9.015
54.169
1.00
18.30
A


1877
CA
HIS
262
12.152
9.422
54.155
1.00
17.72
A


1878
ND1
HIS
262
12.566
9.673
51.142
1.00
20.05
A


1879
CG
HIS
262
12.138
8.533
51.792
1.00
18.58
A


1880
CB
HIS
262
11.354
8.626
53.085
1.00
16.72
A


1881
NE2
HIS
262
13.145
7.985
49.930
1.00
19.75
A


1882
CD2
HIS
262
12.555
7.478
51.069
1.00
18.88
A


1883
CE1
HIS
262
13.214
9.296
50.004
1.00
21.26
A


1884
C
HIS
262
11.489
9.117
55.512
1.00
18.43
A


1885
O
HIS
262
11.784
8.058
56.049
1.00
18.61
A


1886
N
LEU
263
10.662
10.047
55.954
1.00
17.01
A


1887
CA
LEU
263
9.960
9.835
57.216
1.00
17.04
A


1888
CB
LEU
263
9.816
11.174
57.973
1.00
16.64
A


1889
CG
LEU
263
9.255
10.958
59.426
1.00
18.78
A


1890
CD2
LEU
263
9.028
12.298
60.090
1.00
17.69
A


1891
CD1
LEU
263
10.301
10.149
60.221
1.00
19.19
A


1892
C
LEU
263
8.608
9.231
56.922
1.00
16.73
A


1893
O
LEU
263
7.741
9.921
56.377
1.00
17.57
A


1894
N
ARG
264
8.469
7.931
57.163
1.00
16.36
A


1895
CA
ARG
264
7.290
7.216
56.840
1.00
17.70
A


1896
CB
ARG
264
7.666
6.046
55.898
1.00
20.34
A


1897
CG
ARG
264
8.681
6.392
54.814
1.00
22.37
A


1898
CD
ARG
264
7.994
7.130
53.685
1.00
20.91
A


1899
NE
ARG
264
7.169
6.277
52.808
1.00
20.51
A


1900
CZ
ARG
264
6.362
6.843
51.895
1.00
21.14
A


1901
NH1
ARG
264
6.375
8.164
51.651
1.00
20.32
A


1902
NH2
ARG
264
5.603
6.053
51.159
1.00
20.22
A


1903
C
ARG
264
6.594
6.569
58.039
1.00
20.22
A


1904
O
ARG
264
7.133
6.659
59.146
1.00
18.39
A


1905
N
GLU
265
5.471
5.899
57.772
1.00
17.87
A


1906
CA
GLU
265
4.790
5.177
58.862
1.00
18.98
A


1907
CB
GLU
265
3.556
4.407
58.303
1.00
16.37
A


1908
CG
GLU
265
2.643
5.476
57.656
1.00
20.82
A


1909
CD
GLU
265
1.563
4.861
56.766
1.00
20.66
A


1910
OE1
GLU
265
1.377
3.645
56.795
1.00
23.15
A


1911
OE2
GLU
265
0.921
5.616
56.020
1.00
22.61
A


1912
C
GLU
265
5.686
4.230
59.613
1.00
18.25
A


1913
O
GLU
265
5.444
3.929
60.795
1.00
18.46
A


1914
N
GLY
266
6.722
3.688
58.977
1.00
17.26
A


1915
CA
GLY
266
7.650
2.792
59.615
1.00
18.12
A


1916
C
GLY
266
8.861
3.481
60.227
1.00
17.40
A


1917
O
GLY
266
9.778
2.748
60.603
1.00
18.01
A


1918
N
GLY
267
8.923
4.798
60.337
1.00
19.74
A


1919
CA
GLY
267
10.100
5.458
60.917
1.00
20.63
A


1920
C
GLY
267
10.931
6.092
59.768
1.00
23.03
A


1921
O
GLY
267
10.497
6.138
58.616
1.00
20.28
A


1922
N
LEU
268
12.159
6.507
60.072
1.00
21.36
A


1923
CA
LEU
268
13.016
7.215
59.122
1.00
21.05
A


1924
CB
LEU
268
13.981
8.145
59.834
1.00
19.19
A


1925
CG
LEU
268
14.897
9.032
58.962
1.00
17.54
A


1926
CD2
LEU
268
15.779
9.886
59.886
1.00
17.15
A


1927
CD1
LEU
268
14.092
9.876
57.984
1.00
15.58
A


1928
C
LEU
268
13.778
6.178
58.285
1.00
21.30
A


1929
O
LEU
268
14.628
5.448
58.813
1.00
23.77
A


1930
N
THR
269
13.451
6.101
57.003
1.00
20.14
A


1931
CA
THR
269
14.056
5.101
56.137
1.00
22.90
A


1932
CB
THR
269
13.254
4.873
54.836
1.00
22.70
A


1933
OG1
THR
269
13.291
6.065
54.053
1.00
21.45
A


1934
CG2
THR
269
11.798
4.570
55.199
1.00
23.44
A


1935
C
THR
269
15.479
5.461
55.734
1.00
24.41
A


1936
O
THR
269
15.836
6.604
55.954
1.00
26.06
A


1937
N
PHE
270
16.186
4.525
55.142
1.00
25.77
A


1938
CA
PHE
270
17.545
4.694
54.678
1.00
30.89
A


1939
CB
PHE
270
18.501
3.800
55.499
1.00
33.60
A


1940
CG
PHE
270
19.068
4.507
56.692
1.00
35.25
A


1941
CD1
PHE
270
18.543
4.341
57.962
1.00
38.30
A


1942
CD2
PHE
270
20.116
5.377
56.499
1.00
36.35
A


1943
CE1
PHE
270
19.093
5.083
59.039
1.00
38.64
A


1944
CE2
PHE
270
20.654
6.118
57.517
1.00
37.80
A


1945
CZ
PHE
270
20.149
5.938
58.791
1.00
38.59
A


1946
C
PHE
270
17.781
4.204
53.238
1.00
31.79
A


1947
O
PHE
270
17.292
3.178
52.744
1.00
33.03
A


1948
N
GLN
271
18.437
5.045
52.478
1.00
29.75
A


1949
CA
GLN
271
19.027
4.697
51.203
1.00
30.30
A


1950
CB
GLN
271
18.181
5.184
50.041
1.00
32.83
A


1951
CG
GLN
271
18.831
5.074
48.669
1.00
37.28
A


1952
CD
GLN
271
17.923
5.507
47.534
1.00
40.09
A


1953
OE1
GLN
271
16.699
5.314
47.556
1.00
42.51
A


1954
NE2
GLN
271
18.436
6.098
46.459
1.00
40.55
A


1955
C
GLN
271
20.424
5.351
51.253
1.00
28.39
A


1956
O
GLN
271
20.552
6.564
51.138
1.00
27.71
A


1957
N
LEU
272
21.442
4.552
51.472
1.00
26.34
A


1958
CA
LEU
272
22.799
5.037
51.618
1.00
28.19
A


1959
CB
LEU
272
23.205
4.847
53.103
1.00
33.12
A


1960
CG
LEU
272
24.627
5.314
53.406
1.00
36.66
A


1961
CD2
LEU
272
25.100
4.817
54.771
1.00
38.65
A


1962
CD1
LEU
272
24.712
6.845
53.320
1.00
37.49
A


1963
C
LEU
272
23.744
4.251
50.704
1.00
27.33
A


1964
O
LEU
272
23.845
3.036
50.830
1.00
25.84
A


1965
N
HIS
273
24.286
4.916
49.706
1.00
27.33
A


1966
CA
HIS
273
25.070
4.272
48.676
1.00
29.58
A


1967
ND1
HIS
273
24.991
3.934
45.256
1.00
40.32
A


1968
CG
HIS
273
25.820
4.402
46.267
1.00
37.43
A


1969
CB
HIS
273
25.274
5.178
47.455
1.00
32.70
A


1970
NE2
HIS
273
26.990
3.337
44.776
1.00
40.36
A


1971
CD2
HIS
273
27.079
4.017
45.948
1.00
37.90
A


1972
CE1
HIS
273
25.742
3.297
44.378
1.00
39.49
A


1973
C
HIS
273
26.452
3.926
49.230
1.00
27.34
A


1974
O
HIS
273
27.034
4.676
50.023
1.00
24.81
A


1975
N
ARG
274
26.940
2.800
48.779
1.00
27.13
A


1976
CA
ARG
274
28.222
2.245
49.217
1.00
29.59
A


1977
CB
ARG
274
28.436
0.897
48.543
1.00
32.73
A


1978
CG
ARG
274
29.796
0.285
48.852
1.00
36.33
A


1979
CD
ARG
274
29.676
−1.035
49.605
1.00
38.66
A


1980
NE
ARG
274
30.959
−1.586
50.043
1.00
38.59
A


1981
CZ
ARG
274
31.496
−2.756
49.633
1.00
39.92
A


1982
NH1
ARG
274
30.899
−3.560
48.742
1.00
39.98
A


1983
NH2
ARG
274
32.670
−3.218
50.095
1.00
39.32
A


1984
C
ARG
274
29.427
3.145
48.864
1.00
27.69
A


1985
O
ARG
274
30.477
3.097
49.514
1.00
27.09
A


1986
N
ASP
275
29.301
3.971
47.837
1.00
24.66
A


1987
CA
ASP
275
30.438
4.816
47.405
1.00
26.48
A


1988
CB
ASP
275
30.422
5.042
45.901
1.00
30.30
A


1989
CG
ASP
275
30.708
3.772
45.112
1.00
35.19
A


1990
OD1
ASP
275
30.244
3.654
43.918
1.00
36.99
A


1991
OD2
ASP
275
31.402
2.826
45.645
1.00
37.66
A


1992
C
ASP
275
30.424
6.199
48.051
1.00
22.09
A


1993
O
ASP
275
31.151
7.111
47.643
1.00
19.23
A


1994
N
VAL
276
29.611
6.369
49.060
1.00
20.27
A


1995
CA
VAL
276
29.544
7.666
49.723
1.00
18.96
A


1996
CB
VAL
276
28.626
7.596
50.945
1.00
19.63
A


1997
CG1
VAL
276
28.923
8.677
51.989
1.00
19.71
A


1998
CG2
VAL
276
27.148
7.782
50.573
1.00
17.53
A


1999
C
VAL
276
30.971
8.126
50.086
1.00
18.02
A


2000
O
VAL
276
31.380
9.252
49.782
1.00
17.63
A


2001
N
PRO
277
31.831
7.331
50.754
1.00
18.36
A


2002
CA
PRO
277
33.169
7.800
51.096
1.00
20.79
A


2003
CD
PRO
277
31.512
5.973
51.202
1.00
19.97
A


2004
CB
PRO
277
33.785
6.649
51.849
1.00
19.99
A


2005
CG
PRO
277
32.739
5.555
51.962
1.00
19.83
A


2006
C
PRO
277
33.974
8.293
49.891
1.00
23.03
A


2007
O
PRO
277
34.726
9.302
50.018
1.00
21.62
A


2008
N
LEU
278
33.872
7.665
48.735
1.00
21.57
A


2009
CA
LEU
278
34.644
8.143
47.555
1.00
24.35
A


2010
CB
LEU
278
34.625
7.099
46.431
1.00
26.62
A


2011
CG
LEU
278
35.651
5.976
46.594
1.00
29.87
A


2012
CD2
LEU
278
37.099
6.467
46.565
1.00
27.31
A


2013
CD1
LEU
278
35.542
4.920
45.486
1.00
31.37
A


2014
C
LEU
278
34.025
9.394
46.975
1.00
23.03
A


2015
O
LEU
278
34.757
10.207
46.395
1.00
24.13
A


2016
N
MET
279
32.699
9.537
47.109
1.00
20.09
A


2017
CA
MET
279
32.098
10.793
46.607
1.00
20.81
A


2018
CB
MET
279
30.585
10.759
46.763
1.00
21.80
A


2019
CG
MET
279
29.956
9.554
46.087
1.00
21.49
A


2020
SD
MET
279
28.158
9.596
46.311
1.00
22.74
A


2021
CE
MET
279
27.814
7.886
45.932
1.00
22.20
A


2022
C
MET
279
32.620
11.950
47.432
1.00
21.26
A


2023
O
MET
279
32.843
13.056
46.902
1.00
21.41
A


2024
N
VAL
280
32.755
11.735
48.762
1.00
21.29
A


2025
CA
VAL
280
33.337
12.833
49.548
1.00
22.70
A


2026
CB
VAL
280
33.288
12.488
51.071
1.00
23.91
A


2027
CG1
VAL
280
34.082
13.494
51.898
1.00
22.39
A


2028
CG2
VAL
280
31.841
12.468
51.575
1.00
22.09
A


2029
C
VAL
280
34.770
13.083
49.071
1.00
24.53
A


2030
O
VAL
280
35.252
14.214
48.931
1.00
23.97
A


2031
N
ALA
281
35.564
12.025
48.891
1.00
25.87
A


2032
CA
ALA
281
36.967
12.124
48.489
1.00
27.38
A


2033
CB
ALA
281
37.578
10.723
48.367
1.00
27.95
A


2034
C
ALA
281
37.174
12.837
47.160
1.00
28.59
A


2035
O
ALA
281
38.056
13.701
47.016
1.00
29.65
A


2036
N
LYS
282
36.300
12.572
46.189
1.00
26.22
A


2037
CA
LYS
282
36.368
13.223
44.907
1.00
25.90
A


2038
CB
LYS
282
35.300
12.698
43.925
1.00
27.70
A


2039
CG
LYS
282
35.153
13.575
42.651
1.00
30.25
A


2040
CD
LYS
282
33.857
13.278
41.920
1.00
29.84
A


2041
CE
LYS
282
33.593
14.185
40.715
1.00
32.26
A


2042
NZ
LYS
282
32.243
13.849
40.139
1.00
30.29
A


2043
C
LYS
282
36.254
14.726
45.103
1.00
25.93
A


2044
O
LYS
282
36.845
15.456
44.303
1.00
23.37
A


2045
N
ASN
283
35.502
15.227
46.092
1.00
25.52
A


2046
CA
ASN
283
35.211
16.644
46.193
1.00
25.46
A


2047
CB
ASN
283
33.668
16.812
46.435
1.00
25.21
A


2048
CG
ASN
283
32.881
16.340
45.229
1.00
26.49
A


2049
OD1
ASN
283
32.704
17.126
44.310
1.00
25.47
A


2050
ND2
ASN
283
32.380
15.100
45.189
1.00
27.38
A


2051
C
ASN
283
35.863
17.400
47.333
1.00
24.11
A


2052
O
ASN
283
35.665
18.622
47.353
1.00
24.47
A


2053
N
ILE
284
36.517
16.739
48.251
1.00
25.53
A


2054
CA
ILE
284
36.995
17.393
49.477
1.00
26.10
A


2055
CB
ILE
284
37.328
16.279
50.494
1.00
26.34
A


2056
CG2
ILE
284
38.653
15.582
50.160
1.00
26.45
A


2057
CG1
ILE
284
37.371
16.753
51.938
1.00
26.40
A


2058
CD1
ILE
284
36.089
17.363
52.446
1.00
26.64
A


2059
C
ILE
284
38.133
18.365
49.270
1.00
28.21
A


2060
O
ILE
284
38.064
19.553
49.667
1.00
26.93
A


2061
N
GLU
285
39.048
18.054
48.349
1.00
28.53
A


2062
CA
GLU
285
40.191
18.985
48.139
1.00
30.46
A


2063
CB
GLU
285
41.241
18.332
47.222
1.00
33.52
A


2064
CG
GLU
285
42.182
19.313
46.561
1.00
39.10
A


2065
CD
GLU
285
43.388
19.749
47.365
1.00
42.79
A


2066
OE1
GLU
285
43.645
19.212
48.464
1.00
42.80
A


2067
OE2
GLU
285
44.117
20.670
46.879
1.00
44.61
A


2068
C
GLU
285
39.716
20.340
47.698
1.00
26.56
A


2069
O
GLU
285
40.175
21.419
48.100
1.00
25.80
A


2070
N
ASN
286
38.666
20.341
46.873
1.00
27.41
A


2071
CA
ASN
286
38.041
21.556
46.370
1.00
29.50
A


2072
CB
ASN
286
36.931
21.113
45.424
1.00
35.35
A


2073
CG
ASN
286
36.487
22.141
44.428
1.00
40.87
A


2074
OD1
ASN
286
36.837
22.003
43.230
1.00
45.15
A


2075
ND2
ASN
286
35.717
23.121
44.856
1.00
42.56
A


2076
C
ASN
286
37.392
22.389
47.486
1.00
26.71
A


2077
O
ASN
286
37.308
23.617
47.475
1.00
22.59
A


2078
N
ALA
287
36.790
21.654
48.434
1.00
24.05
A


2079
CA
ALA
287
36.132
22.320
49.573
1.00
23.78
A


2080
CB
ALA
287
35.286
21.334
50.345
1.00
22.36
A


2081
C
ALA
287
37.225
22.964
50.432
1.00
22.30
A


2082
O
ALA
287
37.135
24.138
50.758
1.00
24.71
A


2083
N
ALA
288
38.280
22.228
50.704
1.00
23.39
A


2084
CA
ALA
288
39.407
22.804
51.436
1.00
25.71
A


2085
CB
ALA
288
40.468
21.729
51.625
1.00
24.55
A


2086
C
ALA
288
40.000
24.044
50.791
1.00
25.87
A


2087
O
ALA
288
40.250
25.078
51.440
1.00
24.50
A


2088
N
GLU
289
40.198
23.985
49.463
1.00
27.07
A


2089
CA
GLU
289
40.813
25.091
48.741
1.00
28.27
A


2090
CB
GLU
289
41.130
24.674
47.271
1.00
30.88
A


2091
CG
GLU
289
42.340
23.762
47.245
1.00
35.87
A


2092
CD
GLU
289
42.625
23.071
45.921
1.00
40.56
A


2093
OE1
GLU
289
43.791
22.653
45.702
1.00
41.51
A


2094
OE2
GLU
289
41.708
22.906
45.088
1.00
41.76
A


2095
C
GLU
289
39.981
26.346
48.695
1.00
26.52
A


2096
O
GLU
289
40.511
27.452
48.830
1.00
25.15
A


2097
N
LYS
290
38.676
26.199
48.535
1.00
23.69
A


2098
CA
LYS
290
37.769
27.340
48.480
1.00
27.51
A


2099
CB
LYS
290
36.399
26.882
48.005
1.00
29.38
A


2100
CG
LYS
290
35.240
27.853
48.135
1.00
35.53
A


2101
CD
LYS
290
33.949
27.292
47.545
1.00
38.73
A


2102
CE
LYS
290
32.844
28.342
47.436
1.00
40.40
A


2103
NZ
LYS
290
31.560
27.684
47.011
1.00
41.39
A


2104
C
LYS
290
37.714
28.054
49.844
1.00
26.14
A


2105
O
LYS
290
37.657
29.278
49.879
1.00
24.24
A


2106
N
ALA
291
37.891
27.296
50.919
1.00
24.46
A


2107
CA
ALA
291
37.895
27.866
52.249
1.00
27.44
A


2108
CB
ALA
291
37.595
26.760
53.264
1.00
26.18
A


2109
C
ALA
291
39.262
28.465
52.626
1.00
27.57
A


2110
O
ALA
291
39.365
29.545
53.217
1.00
27.36
A


2111
N
LEU
292
40.304
27.720
52.266
1.00
26.84
A


2112
CA
LEU
292
41.624
28.202
52.710
1.00
28.86
A


2113
CB
LEU
292
42.422
26.986
53.134
1.00
26.99
A


2114
CG
LEU
292
41.871
26.217
54.337
1.00
28.38
A


2115
CD2
LEU
292
42.008
27.044
55.607
1.00
27.89
A


2116
CD1
LEU
292
42.631
24.899
54.444
1.00
26.16
A


2117
C
LEU
292
42.459
29.033
51.744
1.00
30.46
A


2118
O
LEU
292
43.188
29.940
52.207
1.00
30.17
A


2119
N
SER
293
42.120
29.018
50.451
1.00
31.81
A


2120
CA
SER
293
42.870
29.851
49.495
1.00
32.75
A


2121
CB
SER
293
42.477
29.604
48.025
1.00
32.73
A


2122
OG
SER
293
43.153
28.418
47.645
1.00
34.17
A


2123
C
SER
293
42.776
31.324
49.779
1.00
33.36
A


2124
O
SER
293
43.801
31.999
49.867
1.00
34.00
A


2125
N
PRO
294
41.603
31.876
50.029
1.00
34.41
A


2126
CA
PRO
294
41.480
33.287
50.381
1.00
35.42
A


2127
CD
PRO
294
40.295
31.190
50.023
1.00
34.17
A


2128
CB
PRO
294
39.981
33.501
50.548
1.00
34.86
A


2129
CG
PRO
294
39.306
32.337
49.921
1.00
34.65
A


2130
C
PRO
294
42.254
33.690
51.638
1.00
36.84
A


2131
O
PRO
294
42.481
34.881
51.909
1.00
36.47
A


2132
N
LEU
295
42.650
32.745
52.486
1.00
36.49
A


2133
CA
LEU
295
43.429
32.991
53.683
1.00
37.02
A


2134
CB
LEU
295
42.980
32.003
54.763
1.00
37.27
A


2135
CG
LEU
295
41.820
32.354
55.702
1.00
38.92
A


2136
CD2
LEU
295
41.008
31.102
56.046
1.00
38.57
A


2137
CD1
LEU
295
40.896
33.423
55.171
1.00
38.29
A


2138
C
LEU
295
44.925
32.827
53.416
1.00
36.97
A


2139
O
LEU
295
45.766
32.870
54.320
1.00
36.24
A


2140
N
GLY
296
45.308
32.560
52.176
1.00
36.33
A


2141
CA
GLY
296
46.679
32.361
51.749
1.00
36.08
A


2142
C
GLY
296
47.255
31.058
52.254
1.00
37.21
A


2143
O
GLY
296
48.472
30.915
52.457
1.00
37.99
A


2144
N
ILE
297
46.402
30.060
52.501
1.00
36.81
A


2145
CA
ILE
297
46.904
28.802
53.050
1.00
37.30
A


2146
CB
ILE
297
46.311
28.486
54.420
1.00
38.48
A


2147
CG2
ILE
297
45.103
29.359
54.728
1.00
40.59
A


2148
CG1
ILE
297
45.928
27.017
54.562
1.00
38.31
A


2149
CD1
ILE
297
46.901
26.269
55.416
1.00
40.48
A


2150
C
ILE
297
46.727
27.683
52.035
1.00
37.13
A


2151
O
ILE
297
45.686
27.505
51.409
1.00
37.08
A


2152
N
THR
298
47.803
26.927
51.890
1.00
36.87
A


2153
CA
THR
298
47.896
25.847
50.940
1.00
38.72
A


2154
CB
THR
298
48.874
26.221
49.786
1.00
39.90
A


2155
OG1
THR
298
50.117
26.627
50.374
1.00
39.12
A


2156
CG2
THR
298
48.278
27.325
48.927
1.00
39.83
A


2157
C
THR
298
48.369
24.568
51.589
1.00
39.07
A


2158
O
THR
298
48.122
23.494
51.045
1.00
42.28
A


2159
N
ASP
299
49.004
24.662
52.740
1.00
39.02
A


2160
CA
ASP
299
49.496
23.468
53.436
1.00
38.76
A


2161
CB
ASP
299
50.764
23.831
54.194
1.00
38.63
A


2162
CG
ASP
299
51.295
22.758
55.103
1.00
39.09
A


2163
OD1
ASP
299
50.863
21.591
55.031
1.00
37.72
A


2164
OD2
ASP
299
52.141
23.059
55.976
1.00
41.89
A


2165
C
ASP
299
48.408
22.909
54.362
1.00
38.43
A


2166
O
ASP
299
48.184
23.476
55.430
1.00
38.49
A


2167
N
TRP
300
47.826
21.767
54.023
1.00
37.66
A


2168
CA
TRP
300
46.745
21.149
54.790
1.00
37.33
A


2169
CB
TRP
300
46.076
20.035
54.030
1.00
35.24
A


2170
CG
TRP
300
45.615
20.311
52.635
1.00
33.53
A


2171
CD2
TRP
300
45.171
21.538
52.062
1.00
33.67
A


2172
CD1
TRP
300
45.493
19.374
51.649
1.00
33.49
A


2173
NE1
TRP
300
45.028
19.958
50.493
1.00
33.28
A


2174
CE2
TRP
300
44.800
21.288
50.730
1.00
34.25
A


2175
CE3
TRP
300
45.057
22.846
52.553
1.00
35.18
A


2176
CZ2
TRP
300
44.346
22.285
49.865
1.00
33.41
A


2177
CZ3
TRP
300
44.620
23.849
51.709
1.00
34.28
A


2178
CH2
TRP
300
44.241
23.551
50.385
1.00
34.92
A


2179
C
TRP
300
47.202
20.714
56.182
1.00
37.49
A


2180
O
TRP
300
46.418
20.813
57.163
1.00
36.40
A


2181
N
ASN
301
48.477
20.306
56.332
1.00
34.48
A


2182
CA
ASN
301
48.922
19.946
57.672
1.00
35.00
A


2183
CB
ASN
301
50.144
19.029
57.661
1.00
37.31
A


2184
CG
ASN
301
49.728
17.606
57.329
1.00
38.68
A


2185
OD1
ASN
301
48.920
16.951
57.987
1.00
37.57
A


2186
ND2
ASN
301
50.350
17.099
56.273
1.00
40.93
A


2187
C
ASN
301
49.175
21.173
58.550
1.00
32.26
A


2188
O
ASN
301
49.400
20.997
59.751
1.00
31.10
A


2189
N
SER
302
49.106
22.389
58.010
1.00
31.87
A


2190
CA
SER
302
49.245
23.552
58.893
1.00
32.12
A


2191
CB
SER
302
49.849
24.731
58.135
1.00
29.88
A


2192
OG
SER
302
48.880
25.107
57.168
1.00
32.74
A


2193
C
SER
302
47.906
23.992
59.499
1.00
30.90
A


2194
O
SER
302
47.842
25.052
60.118
1.00
31.20
A


2195
N
VAL
303
46.822
23.230
59.362
1.00
30.13
A


2196
CA
VAL
303
45.553
23.653
59.934
1.00
28.77
A


2197
CB
VAL
303
44.522
24.168
58.925
1.00
31.98
A


2198
CG1
VAL
303
45.062
25.161
57.904
1.00
32.26
A


2199
CG2
VAL
303
43.857
23.026
58.191
1.00
31.24
A


2200
C
VAL
303
44.978
22.498
60.741
1.00
26.82
A


2201
O
VAL
303
45.415
21.362
60.526
1.00
27.14
A


2202
N
PHE
304
44.090
22.798
61.685
1.00
24.01
A


2203
CA
PHE
304
43.475
21.704
62.438
1.00
23.42
A


2204
CB
PHE
304
43.325
22.054
63.911
1.00
23.36
A


2205
CG
PHE
304
42.463
23.232
64.237
1.00
22.32
A


2206
CD1
PHE
304
42.945
24.512
64.179
1.00
20.79
A


2207
CD2
PHE
304
41.127
23.039
64.629
1.00
24.15
A


2208
CE1
PHE
304
42.161
25.609
64.468
1.00
19.60
A


2209
CE2
PHE
304
40.346
24.133
64.947
1.00
21.08
A


2210
CZ
PHE
304
40.842
25.414
64.847
1.00
20.44
A


2211
C
PHE
304
42.147
21.355
61.776
1.00
24.89
A


2212
O
PHE
304
41.627
22.140
60.992
1.00
25.71
A


2213
N
TRP
305
41.666
20.119
61.929
1.00
25.44
A


2214
CA
TRP
305
40.584
19.613
61.118
1.00
25.60
A


2215
CB
TRP
305
41.051
18.536
60.093
1.00
25.55
A


2216
CG
TRP
305
41.959
19.100
59.049
1.00
26.83
A


2217
CD2
TRP
305
41.615
19.672
57.775
1.00
28.73
A


2218
CD1
TRP
305
43.318
19.207
59.176
1.00
27.96
A


2219
NE1
TRP
305
43.822
19.826
58.065
1.00
28.93
A


2220
CE2
TRP
305
42.806
20.120
57.187
1.00
29.39
A


2221
CE3
TRP
305
40.405
19.893
57.104
1.00
27.51
A


2222
CZ2
TRP
305
42.852
20.773
55.956
1.00
30.39
A


2223
CZ3
TRP
305
40.462
20.535
55.866
1.00
29.88
A


2224
CH2
TRP
305
41.657
20.981
55.292
1.00
30.23
A


2225
C
TRP
305
39.556
18.924
61.998
1.00
24.39
A


2226
O
TRP
305
39.918
18.180
62.892
1.00
25.90
A


2227
N
MET
306
38.308
19.223
61.746
1.00
22.65
A


2228
CA
MET
306
37.198
18.610
62.475
1.00
22.14
A


2229
CB
MET
306
36.522
19.736
63.268
1.00
22.15
A


2230
CG
MET
306
37.433
20.356
64.335
1.00
23.61
A


2231
SD
MET
306
37.057
22.087
64.614
1.00
24.09
A


2232
CE
MET
306
37.738
22.767
63.079
1.00
25.77
A


2233
C
MET
306
36.287
18.000
61.412
1.00
20.50
A


2234
O
MET
306
35.608
18.766
60.735
1.00
21.18
A


2235
N
VAL
307
36.296
16.682
61.268
1.00
19.97
A


2236
CA
VAL
307
35.652
16.070
60.113
1.00
20.97
A


2237
CB
VAL
307
36.711
15.240
59.325
1.00
22.15
A


2238
CG1
VAL
307
36.059
14.606
58.100
1.00
21.56
A


2239
CG2
VAL
307
37.843
16.138
58.808
1.00
19.03
A


2240
C
VAL
307
34.481
15.226
60.556
1.00
18.76
A


2241
O
VAL
307
34.671
14.319
61.368
1.00
18.36
A


2242
N
HIS
308
33.288
15.563
60.066
1.00
17.69
A


2243
CA
HIS
308
32.137
14.752
60.516
1.00
19.07
A


2244
ND1
HIS
308
29.082
14.287
61.340
1.00
19.45
A


2245
CG
HIS
308
29.736
14.291
60.117
1.00
18.52
A


2246
CB
HIS
308
30.860
15.253
59.823
1.00
17.91
A


2247
NE2
HIS
308
28.252
12.647
60.143
1.00
17.30
A


2248
CD2
HIS
308
29.273
13.240
59.426
1.00
18.98
A


2249
CE1
HIS
308
28.161
13.317
61.296
1.00
20.93
A


2250
C
HIS
308
32.401
13.295
60.187
1.00
22.00
A


2251
O
HIS
308
32.541
12.856
59.015
1.00
21.78
A


2252
N
PRO
309
32.393
12.441
61.212
1.00
20.32
A


2253
CA
PRO
309
32.739
11.051
61.029
1.00
20.18
A


2254
CD
PRO
309
32.301
12.831
62.657
1.00
20.49
A


2255
CB
PRO
309
33.298
10.657
62.401
1.00
20.80
A


2256
CG
PRO
309
32.498
11.496
63.364
1.00
20.59
A


2257
C
PRO
309
31.508
10.289
60.609
1.00
21.81
A


2258
O
PRO
309
30.997
9.378
61.269
1.00
19.24
A


2259
N
GLY
310
31.103
10.445
59.323
1.00
23.24
A


2260
CA
GLY
310
29.864
9.839
58.832
1.00
20.51
A


2261
C
GLY
310
30.019
8.326
58.903
1.00
20.61
A


2262
O
GLY
310
29.087
7.565
59.191
1.00
20.56
A


2263
N
GLY
311
31.239
7.863
58.784
1.00
22.70
A


2264
CA
GLY
311
31.640
6.482
59.010
1.00
22.41
A


2265
C
GLY
311
33.177
6.532
59.055
1.00
26.15
A


2266
O
GLY
311
33.732
7.545
58.622
1.00
23.11
A


2267
N
ARG
312
33.801
5.449
59.542
1.00
25.15
A


2268
CA
ARG
312
35.267
5.453
59.517
1.00
28.00
A


2269
CB
ARG
312
35.781
4.146
60.150
1.00
28.47
A


2270
CG
ARG
312
37.279
4.127
60.410
1.00
29.38
A


2271
CD
ARG
312
37.969
2.814
60.029
1.00
29.48
A


2272
NE
ARG
312
38.075
2.653
58.576
1.00
29.65
A


2273
CZ
ARG
312
37.412
1.794
57.833
1.00
29.04
A


2274
NH1
ARG
312
36.549
0.931
58.375
1.00
29.66
A


2275
NH2
ARG
312
37.562
1.804
56.502
1.00
29.86
A


2276
C
ARG
312
35.838
5.655
58.110
1.00
28.09
A


2277
O
ARG
312
36.840
6.360
57.932
1.00
26.45
A


2278
N
ALA
313
35.194
5.140
57.044
1.00
27.48
A


2279
CA
ALA
313
35.761
5.264
55.709
1.00
28.44
A


2280
CB
ALA
313
35.090
4.311
54.721
1.00
25.75
A


2281
C
ALA
313
35.789
6.710
55.238
1.00
27.78
A


2282
O
ALA
313
36.738
7.113
54.545
1.00
28.88
A


2283
N
ILE
314
34.847
7.571
55.640
1.00
25.33
A


2284
CA
ILE
314
34.863
8.967
55.278
1.00
24.23
A


2285
CB
ILE
314
33.593
9.715
55.711
1.00
24.88
A


2286
CG2
ILE
314
33.746
11.217
55.572
1.00
22.43
A


2287
CG1
ILE
314
32.389
9.150
54.926
1.00
25.63
A


2288
CD1
ILE
314
31.038
9.696
55.366
1.00
26.50
A


2289
C
ILE
314
36.096
9.645
55.864
1.00
25.33
A


2290
O
ILE
314
36.752
10.462
55.193
1.00
24.16
A


2291
N
LEU
315
36.403
9.283
57.131
1.00
23.77
A


2292
CA
LEU
315
37.587
9.932
57.718
1.00
24.34
A


2293
CB
LEU
315
37.682
9.524
59.191
1.00
24.34
A


2294
CG
LEU
315
36.536
10.054
60.091
1.00
25.06
A


2295
CD2
LEU
315
36.454
11.569
60.006
1.00
22.52
A


2296
CD1
LEU
315
36.748
9.592
61.524
1.00
24.58
A


2297
C
LEU
315
38.801
9.473
56.901
1.00
23.99
A


2298
O
LEU
315
39.630
10.293
56.546
1.00
20.41
A


2299
N
ASP
316
38.963
8.169
56.724
1.00
25.26
A


2300
CA
ASP
316
40.110
7.646
55.941
1.00
27.56
A


2301
CB
ASP
316
39.995
6.111
55.767
1.00
26.73
A


2302
CG
ASP
316
40.093
5.400
57.101
1.00
25.66
A


2303
OD1
ASP
316
40.437
6.079
58.096
1.00
26.87
A


2304
OD2
ASP
316
39.785
4.201
57.261
1.00
25.95
A


2305
C
ASP
316
40.253
8.299
54.580
1.00
29.51
A


2306
O
ASP
316
41.380
8.689
54.209
1.00
28.40
A


2307
N
GLN
317
39.156
8.489
53.828
1.00
28.98
A


2308
CA
GLN
317
39.264
9.121
52.514
1.00
29.43
A


2309
CB
GLN
317
37.937
9.114
51.714
1.00
29.81
A


2310
CG
GLN
317
37.628
7.668
51.398
1.00
32.45
A


2311
CD
GLN
317
38.330
7.080
50.206
1.00
34.76
A


2312
OE1
GLN
317
38.009
5.889
50.034
1.00
38.92
A


2313
NE2
GLN
317
39.119
7.750
49.373
1.00
31.51
A


2314
C
GLN
317
39.679
10.565
52.579
1.00
28.51
A


2315
O
GLN
317
40.430
11.043
51.730
1.00
26.77
A


2316
N
VAL
318
39.127
11.279
53.564
1.00
27.55
A


2317
CA
VAL
318
39.453
12.700
53.695
1.00
26.01
A


2318
CB
VAL
318
38.562
13.398
54.731
1.00
26.17
A


2319
CG1
VAL
318
39.100
14.786
55.062
1.00
24.19
A


2320
CG2
VAL
318
37.127
13.456
54.194
1.00
27.01
A


2321
C
VAL
318
40.931
12.801
54.056
1.00
27.36
A


2322
O
VAL
318
41.718
13.524
53.435
1.00
27.34
A


2323
N
GLU
319
41.346
11.967
55.006
1.00
26.26
A


2324
CA
GLU
319
42.771
11.972
55.396
1.00
29.48
A


2325
CB
GLU
319
42.954
10.913
56.476
1.00
28.76
A


2326
CG
GLU
319
44.416
10.778
56.949
1.00
32.30
A


2327
CD
GLU
319
44.448
9.601
57.916
1.00
33.55
A


2328
OE1
GLU
319
44.618
8.445
57.486
1.00
34.82
A


2329
OE2
GLU
319
44.106
9.866
59.086
1.00
34.46
A


2330
C
GLU
319
43.714
11.668
54.210
1.00
31.27
A


2331
O
GLU
319
44.646
12.423
53.936
1.00
29.97
A


2332
N
ARG
320
43.391
10.658
53.421
1.00
31.97
A


2333
CA
ARG
320
44.195
10.228
52.281
1.00
33.54
A


2334
CB
ARG
320
43.670
8.895
51.721
1.00
37.94
A


2335
CG
ARG
320
44.016
8.642
50.246
1.00
45.02
A


2336
CD
ARG
320
43.689
7.210
49.851
1.00
49.77
A


2337
NE
ARG
320
42.634
7.130
48.855
1.00
54.74
A


2338
CZ
ARG
320
42.006
6.021
48.473
1.00
57.64
A


2339
NH1
ARG
320
42.255
4.813
48.976
1.00
58.10
A


2340
NH2
ARG
320
41.067
6.113
47.529
1.00
59.70
A


2341
C
ARG
320
44.214
11.277
51.180
1.00
31.57
A


2342
O
ARG
320
45.260
11.735
50.748
1.00
26.69
A


2343
N
LYS
321
43.041
11.746
50.781
1.00
30.54
A


2344
CA
LYS
321
42.931
12.731
49.718
1.00
31.32
A


2345
CB
LYS
321
41.453
12.882
49.303
1.00
29.88
A


2346
CG
LYS
321
41.257
13.275
47.879
1.00
32.75
A


2347
CD
LYS
321
41.347
12.186
46.811
1.00
31.59
A


2348
CE
LYS
321
41.170
12.810
45.427
1.00
30.86
A


2349
NZ
LYS
321
40.794
11.823
44.359
1.00
28.78
A


2350
C
LYS
321
43.601
14.039
50.087
1.00
32.09
A


2351
O
LYS
321
44.231
14.651
49.185
1.00
30.42
A


2352
N
LEU
322
43.548
14.487
51.336
1.00
28.45
A


2353
CA
LEU
322
44.237
15.726
51.708
1.00
31.61
A


2354
CB
LEU
322
43.526
16.418
52.905
1.00
31.98
A


2355
CG
LEU
322
42.063
16.787
52.652
1.00
32.26
A


2356
CD2
LEU
322
41.968
17.752
51.468
1.00
31.43
A


2357
CD1
LEU
322
41.400
17.356
53.890
1.00
30.97
A


2358
C
LEU
322
45.687
15.492
52.143
1.00
32.01
A


2359
O
LEU
322
46.375
16.423
52.562
1.00
32.31
A


2360
N
ASN
323
46.106
14.241
52.199
1.00
33.80
A


2361
CA
ASN
323
47.422
13.770
52.591
1.00
33.98
A


2362
CBE
ASN
323
48.475
14.261
51.561
1.00
35.66
A


2363
CG
ASN
323
49.791
13.511
51.684
1.00
38.31
A


2364
OD1
ASN
323
49.908
12.416
52.265
1.00
38.69
A


2365
ND2
ASN
323
50.842
14.144
51.159
1.00
40.45
A


2366
C
ASN
323
47.771
14.239
53.999
1.00
34.07
A


2367
O
ASN
323
48.867
14.696
54.276
1.00
29.61
A


2368
N
LEU
324
46.797
14.196
54.919
1.00
32.49
A


2369
CA
LEU
324
47.006
14.645
56.276
1.00
31.44
A


2370
CB
LEU
324
45.659
14.630
57.024
1.00
30.01
A


2371
CG
LEU
324
44.538
15.505
56.458
1.00
29.87
A


2372
CD2
LEU
324
45.051
16.888
56.068
1.00
29.03
A


2373
CD1
LEU
324
43.382
15.665
57.456
1.00
28.63
A


2374
C
LEU
324
48.003
13.734
56.980
1.00
32.17
A


2375
O
LEU
324
47.906
12.515
56.758
1.00
31.89
A


2376
N
LYS
325
48.830
14.261
57.884
1.00
32.78
A


2377
CA
LYS
325
49.671
13.326
58.647
1.00
36.55
A


2378
CB
LYS
325
50.820
13.917
59.442
1.00
38.31
A


2379
CG
LYS
325
50.604
15.247
60.115
1.00
40.84
A


2380
CD
LYS
325
51.767
16.183
59.765
1.00
43.98
A


2381
CE
LYS
325
51.719
17.381
60.709
1.00
45.41
A


2382
NZ
LYS
325
52.075
16.951
62.089
1.00
46.52
A


2383
C
LYS
325
48.795
12.493
59.587
1.00
36.64
A


2384
O
LYS
325
47.635
12.774
59.821
1.00
35.10
A


2385
N
ALA
326
49.375
11.426
60.088
1.00
37.18
A


2386
CA
ALA
326
48.791
10.409
60.914
1.00
40.51
A


2387
C
ALA
326
47.837
10.816
62.029
1.00
39.91
A


2388
O
ALA
326
46.852
10.108
62.288
1.00
41.58
A


2389
CBE
ALA
326
49.955
9.618
61.562
1.00
41.19
A


2390
N
ASP
327
48.110
11.891
62.740
1.00
39.91
A


2391
CA
ASP
327
47.194
12.211
63.844
1.00
39.02
A


2392
CB
ASP
327
48.055
12.451
65.095
1.00
43.42
A


2393
CG
ASP
327
49.181
13.445
64.877
1.00
46.52
A


2394
OD1
ASP
327
50.142
13.411
65.694
1.00
50.17
A


2395
OD2
ASP
327
49.190
14.258
63.933
1.00
47.69
A


2396
C
ASP
327
46.335
13.405
63.535
1.00
35.51
A


2397
O
ASP
327
45.697
13.856
64.489
1.00
35.04
A


2398
N
LYS
328
46.284
13.931
62.295
1.00
31.04
A


2399
CA
LYS
328
45.477
15.122
62.094
1.00
29.47
A


2400
CB
LYS
328
45.546
15.701
60.680
1.00
29.91
A


2401
CG
LYS
328
46.875
16.254
60.230
1.00
31.30
A


2402
CD
LYS
328
47.479
17.280
61.208
1.00
30.94
A


2403
CE
LYS
328
46.703
18.557
61.104
1.00
30.10
A


2404
NZ
LYS
328
47.380
19.763
61.595
1.00
28.00
A


2405
C
LYS
328
44.002
14.872
62.475
1.00
26.96
A


2406
O
LYS
328
43.378
15.790
63.011
1.00
26.83
A


2407
N
LEU
329
43.456
13.707
62.207
1.00
24.37
A


2408
CA
LEU
329
42.034
13.458
62.500
1.00
24.60
A


2409
CB
LEU
329
41.499
12.602
61.342
1.00
23.58
A


2410
CG
LEU
329
41.496
13.306
59.962
1.00
23.22
A


2411
CD2
LEU
329
41.130
14.772
60.091
1.00
24.27
A


2412
CD1
LEU
329
40.574
12.571
58.994
1.00
21.79
A


2413
C
LEU
329
41.773
12.827
63.849
1.00
23.51
A


2414
O
LEU
329
40.705
12.252
64.112
1.00
23.49
A


2415
N
ARG
330
42.712
12.929
64.785
1.00
23.97
A


2416
CA
ARG
330
42.611
12.245
66.074
1.00
24.74
A


2417
CB
ARG
330
43.819
12.671
66.957
1.00
26.92
A


2418
CG
ARG
330
43.810
11.773
68.211
1.00
31.36
A


2419
CD
ARG
330
44.166
12.556
69.457
1.00
34.14
A


2420
NE
ARG
330
43.514
13.854
69.571
1.00
35.61
A


2421
CZ
ARG
330
42.415
14.135
70.285
1.00
35.45
A


2422
NH1
ARG
330
41.721
13.283
71.017
1.00
32.02
A


2423
NH2
ARG
330
41.988
15.386
70.304
1.00
35.69
A


2424
C
ARG
330
41.330
12.541
66.858
1.00
21.83
A


2425
O
ARG
330
40.580
11.694
67.327
1.00
22.99
A


2426
N
ALA
331
41.054
13.810
67.005
1.00
22.43
A


2427
CA
ALA
331
39.861
14.311
67.695
1.00
25.05
A


2428
CB
ALA
331
39.918
15.826
67.723
1.00
22.22
A


2429
C
ALA
331
38.584
13.791
67.027
1.00
23.68
A


2430
O
ALA
331
37.659
13.410
67.765
1.00
23.98
A


2431
N
SER
332
38.559
13.754
65.671
1.00
22.34
A


2432
CA
SER
332
37.361
13.275
64.986
1.00
21.43
A


2433
CB
SER
332
37.334
13.597
63.469
1.00
21.01
A


2434
OG
SER
332
37.614
14.946
63.212
1.00
22.05
A


2435
C
SER
332
37.186
11.789
65.222
1.00
22.98
A


2436
O
SER
332
36.098
11.271
65.497
1.00
21.41
A


2437
N
ARG
333
38.323
11.058
65.137
1.00
21.37
A


2438
CA
ARG
333
38.268
9.620
65.365
1.00
22.97
A


2439
CB
ARG
333
39.604
8.913
65.055
1.00
23.23
A


2440
CG
ARG
333
39.931
8.909
63.568
1.00
24.76
A


2441
CD
ARG
333
41.272
8.258
63.259
1.00
24.33
A


2442
NE
ARG
333
41.692
8.483
61.878
1.00
28.03
A


2443
CZ
ARG
333
41.188
7.825
60.832
1.00
25.05
A


2444
NH1
ARG
333
40.249
6.885
61.001
1.00
25.05
A


2445
NH2
ARG
333
41.568
8.043
59.568
1.00
26.62
A


2446
C
ARG
333
37.935
9.305
66.813
1.00
21.56
A


2447
O
ARG
333
37.314
8.273
67.116
1.00
19.77
A


2448
N
HIS
334
38.363
10.199
67.673
1.00
23.45
A


2449
CA
HIS
334
38.137
10.049
69.102
1.00
24.49
A


2450
ND1
HIS
334
39.373
10.257
72.270
1.00
32.33
A


2451
CG
HIS
334
38.572
10.993
71.400
1.00
29.22
A


2452
CB
HIS
334
38.881
11.104
69.907
1.00
26.66
A


2453
NE2
HIS
334
37.772
11.085
73.427
1.00
31.50
A


2454
CD2
HIS
334
37.567
11.508
72.152
1.00
30.73
A


2455
CE1
HIS
334
38.849
10.342
73.481
1.00
31.69
A


2456
C
HIS
334
36.641
10.147
69.435
1.00
22.86
A


2457
O
HIS
334
36.090
9.344
70.186
1.00
19.91
A


2458
N
VAL
335
35.895
11.125
68.906
1.00
22.31
A


2459
CA
VAL
335
34.474
11.147
69.315
1.00
21.53
A


2460
CB
VAL
335
33.777
12.523
69.238
1.00
24.33
A


2461
CG1
VAL
335
34.734
13.707
69.272
1.00
21.74
A


2462
CG2
VAL
335
32.872
12.708
68.024
1.00
23.21
A


2463
C
VAL
335
33.683
10.054
68.578
1.00
21.01
A


2464
O
VAL
335
32.677
9.556
69.084
1.00
20.79
A


2465
N
LEU
336
34.141
9.648
67.405
1.00
20.22
A


2466
CA
LEU
336
33.480
8.538
66.675
1.00
19.73
A


2467
CB
LEU
336
34.195
8.272
65.345
1.00
18.76
A


2468
CG
LEU
336
33.700
7.015
64.627
1.00
20.45
A


2469
CD2
LEU
336
34.552
6.652
63.407
1.00
21.80
A


2470
CD1
LEU
336
32.268
7.149
64.106
1.00
19.22
A


2471
C
LEU
336
33.557
7.265
67.510
1.00
19.35
A


2472
O
LEU
336
32.595
6.487
67.586
1.00
19.60
A


2473
N
SER
337
34.715
7.112
68.111
1.00
21.45
A


2474
CA
SER
337
35.045
5.950
68.934
1.00
22.61
A


2475
CB
SER
337
36.524
5.992
69.325
1.00
24.30
A


2476
OG
SER
337
36.847
4.864
70.124
1.00
24.53
A


2477
C
SER
337
34.223
5.914
70.225
1.00
21.12
A


2478
O
SER
337
33.638
4.885
70.583
1.00
21.62
A


2479
N
GLU
338
34.185
7.040
70.897
1.00
23.28
A


2480
CA
GLU
338
33.539
7.135
72.211
1.00
24.08
A


2481
CB
GLU
338
34.158
8.283
73.009
1.00
25.54
A


2482
CG
GLU
338
35.646
8.063
73.308
1.00
28.48
A


2483
CD
GLU
338
35.896
6.904
74.277
1.00
31.99
A


2484
OE1
GLU
338
34.960
6.520
75.077
1.00
32.49
A


2485
OE2
GLU
338
37.042
6.311
74.295
1.00
35.71
A


2486
C
GLU
338
32.016
7.368
72.142
1.00
24.98
A


2487
O
GLU
338
31.289
7.101
73.109
1.00
22.51
A


2488
N
TYR
339
31.510
7.851
71.012
1.00
22.37
A


2489
CA
TYR
339
30.068
8.187
70.920
1.00
21.48
A


2490
CB
TYR
339
29.868
9.700
70.855
1.00
22.32
A


2491
CG
TYR
339
30.391
10.422
72.084
1.00
22.93
A


2492
CD1
TYR
339
31.653
11.018
72.053
1.00
23.01
A


2493
CD2
TYR
339
29.604
10.485
73.235
1.00
22.61
A


2494
CE1
TYR
339
32.139
11.673
73.187
1.00
24.15
A


2495
CE2
TYR
339
30.091
11.137
74.370
1.00
25.87
A


2496
CZ
TYR
339
31.359
11.729
74.347
1.00
24.94
A


2497
OH
TYR
339
31.830
12.360
75.453
1.00
25.61
A


2498
C
TYR
339
29.354
7.673
69.667
1.00
21.23
A


2499
O
TYR
339
28.117
7.599
69.632
1.00
21.39
A


2500
N
GLY
340
30.114
7.335
68.654
1.00
20.88
A


2501
CA
GLY
340
29.532
6.927
67.362
1.00
18.86
A


2502
C
GLY
340
29.198
8.210
66.595
1.00
18.29
A


2503
O
GLY
340
29.529
9.317
67.031
1.00
16.14
A


2504
N
ASN
341
28.557
8.071
65.457
1.00
18.02
A


2505
CA
ASN
341
28.178
9.237
64.631
1.00
16.44
A


2506
CB
ASN
341
27.851
8.744
63.203
1.00
16.49
A


2507
CG
ASN
341
27.258
9.802
62.246
1.00
19.40
A


2508
OD1
ASN
341
26.919
10.909
62.657
1.00
16.32
A


2509
ND2
ASN
341
27.112
9.512
60.958
1.00
17.00
A


2510
C
ASN
341
26.946
9.900
65.254
1.00
15.55
A


2511
O
ASN
341
25.865
9.327
65.169
1.00
17.14
A


2512
N
LEU
342
27.075
11.088
65.794
1.00
15.07
A


2513
CA
LEU
342
26.022
11.805
66.477
1.00
16.85
A


2514
CB
LEU
342
26.592
12.599
67.636
1.00
16.75
A


2515
CG
LEU
342
27.392
11.768
68.685
1.00
18.49
A


2516
CD2
LEU
342
26.407
11.099
69.637
1.00
16.92
A


2517
CD1
LEU
342
28.336
12.687
69.441
1.00
17.96
A


2518
C
LEU
342
25.251
12.791
65.588
1.00
16.54
A


2519
O
LEU
342
24.662
13.772
66.027
1.00
13.14
A


2520
N
ILE
343
25.253
12.490
64.282
1.00
16.77
A


2521
CA
ILE
343
24.483
13.293
63.336
1.00
16.34
A


2522
CB
ILE
343
22.976
12.937
63.360
1.00
18.49
A


2523
CG2
ILE
343
22.340
13.465
62.050
1.00
19.03
A


2524
CG1
ILE
343
22.726
11.440
63.507
1.00
18.92
A


2525
CD1
ILE
343
21.287
10.952
63.369
1.00
18.26
A


2526
C
ILE
343
24.758
14.742
63.478
1.00
13.00
A


2527
O
ILE
343
25.974
15.082
63.555
1.00
14.01
A


2528
N
SER
344
23.791
15.673
63.583
1.00
13.53
A


2529
CA
SER
344
24.153
17.063
63.587
1.00
14.89
A


2530
CB
SER
344
22.943
18.003
63.525
1.00
15.82
A


2531
OG
SER
344
22.078
17.781
64.661
1.00
14.68
A


2532
C
SER
344
24.999
17.567
64.748
1.00
16.89
A


2533
O
SER
344
25.569
18.661
64.663
1.00
13.77
A


2534
N
ALA
345
24.957
16.858
65.866
1.00
18.14
A


2535
CA
ALA
345
25.788
17.298
66.982
1.00
19.06
A


2536
CB
ALA
345
25.213
16.583
68.249
1.00
17.68
A


2537
C
ALA
345
27.233
16.820
66.881
1.00
16.99
A


2538
O
ALA
345
28.076
17.324
67.643
1.00
16.29
A


2539
N
CYS
346
27.530
15.852
66.029
1.00
15.85
A


2540
CA
CYS
346
28.821
15.219
65.984
1.00
17.48
A


2541
CB
CYS
346
28.847
14.025
65.003
1.00
16.24
A


2542
SG
CYS
346
30.177
12.841
65.409
1.00
18.64
A


2543
C
CYS
346
30.039
16.118
65.840
1.00
18.21
A


2544
O
CYS
346
30.962
16.058
66.714
1.00
16.36
A


2545
N
VAL
347
29.990
17.100
64.942
1.00
17.34
A


2546
CA
VAL
347
31.124
18.004
64.761
1.00
16.15
A


2547
CB
VAL
347
31.090
18.801
63.461
1.00
18.24
A


2548
CG1
VAL
347
31.320
17.867
62.227
1.00
16.79
A


2549
CG2
VAL
347
29.802
19.570
63.224
1.00
15.47
A


2550
C
VAL
347
31.275
18.953
65.952
1.00
17.90
A


2551
O
VAL
347
32.346
19.518
66.204
1.00
17.22
A


2552
N
LEU
348
30.182
19.204
66.681
1.00
15.91
A


2553
CA
LEU
348
30.253
20.114
67.818
1.00
17.68
A


2554
CB
LEU
348
28.876
20.665
68.165
1.00
15.93
A


2555
CG
LEU
348
28.097
21.309
67.004
1.00
17.02
A


2556
CD2
LEU
348
28.818
22.548
66.483
1.00
11.37
A


2557
CD1
LEU
348
26.677
21.632
67.473
1.00
14.02
A


2558
C
LEU
348
30.922
19.412
69.020
1.00
17.18
A


2559
O
LEU
348
31.665
20.089
69.723
1.00
18.34
A


2560
N
PHE
349
30.772
18.110
69.128
1.00
17.77
A


2561
CA
PHE
349
31.489
17.315
70.110
1.00
20.37
A


2562
CB
PHE
349
31.015
15.893
70.220
1.00
18.65
A


2563
CG
PHE
349
29.812
15.572
71.076
1.00
17.81
A


2564
CD1
PHE
349
29.953
14.617
72.071
1.00
17.47
A


2565
CD2
PHE
349
28.573
16.149
70.840
1.00
16.73
A


2566
CE1
PHE
349
28.867
14.245
72.866
1.00
18.81
A


2567
CE2
PHE
349
27.469
15.824
71.627
1.00
15.30
A


2568
CZ
PHE
349
27.627
14.882
72.611
1.00
18.64
A


2569
C
PHE
349
32.981
17.269
69.715
1.00
22.63
A


2570
O
PHE
349
33.861
17.384
70.582
1.00
22.63
A


2571
N
ILE
350
33.242
17.259
68.400
1.00
20.47
A


2572
CA
ILE
350
34.634
17.300
67.944
1.00
20.13
A


2573
CB
ILE
350
34.781
16.955
66.449
1.00
19.92
A


2574
CG2
ILE
350
36.212
17.189
65.981
1.00
21.91
A


2575
CG1
ILE
350
34.380
15.492
66.269
1.00
22.03
A


2576
CD1
ILE
350
34.185
14.955
64.863
1.00
23.33
A


2577
C
ILE
350
35.241
18.642
68.284
1.00
18.34
A


2578
O
ILE
350
36.392
18.731
68.748
1.00
20.71
A


2579
N
ILE
351
34.563
19.759
68.097
1.00
15.23
A


2580
CA
ILE
351
35.113
21.067
68.451
1.00
15.59
A


2581
CB
ILE
351
34.097
22.179
68.172
1.00
16.23
A


2582
CG2
ILE
351
34.523
23.540
68.748
1.00
14.52
A


2583
CG1
ILE
351
33.911
22.394
66.616
1.00
16.07
A


2584
CD1
ILE
351
32.700
23.304
66.417
1.00
15.18
A


2585
C
ILE
351
35.478
21.063
69.958
1.00
19.03
A


2586
O
ILE
351
36.524
21.547
70.378
1.00
17.54
A


2587
N
ASP
352
34.642
20.452
70.794
1.00
18.69
A


2588
CA
ASP
352
34.905
20.482
72.268
1.00
19.86
A


2589
CB
ASP
352
33.659
19.938
72.959
1.00
17.51
A


2590
CG
ASP
352
33.525
20.315
74.445
1.00
17.73
A


2591
OD1
ASP
352
34.064
21.359
74.764
1.00
20.03
A


2592
OD2
ASP
352
32.878
19.514
75.136
1.00
17.82
A


2593
C
ASP
352
36.104
19.593
72.585
1.00
22.16
A


2594
O
ASP
352
36.945
19.946
73.433
1.00
22.49
A


2595
N
GLU
353
36.201
18.459
71.890
1.00
20.10
A


2596
CA
GLU
353
37.297
17.530
72.035
1.00
22.22
A


2597
CB
GLU
353
37.123
16.241
71.218
1.00
23.12
A


2598
CG
GLU
353
38.322
15.323
71.138
1.00
23.80
A


2599
CD
GLU
353
38.731
14.792
72.519
1.00
25.95
A


2600
OE1
GLU
353
37.898
14.679
73.443
1.00
24.69
A


2601
OE2
GLU
353
39.914
14.463
72.701
1.00
25.95
A


2602
C
GLU
353
38.598
18.227
71.651
1.00
23.07
A


2603
O
GLU
353
39.573
18.148
72.444
1.00
24.34
A


2604
N
VAL
354
38.657
18.959
70.560
1.00
21.51
A


2605
CA
VAL
354
39.856
19.673
70.127
1.00
20.65
A


2606
CB
VAL
354
39.648
20.396
68.779
1.00
20.92
A


2607
CG1
VAL
354
40.714
21.402
68.410
1.00
18.47
A


2608
CG2
VAL
354
39.581
19.346
67.669
1.00
23.03
A


2609
C
VAL
354
40.340
20.686
71.169
1.00
22.28
A


2610
O
VAL
354
41.538
20.670
71.535
1.00
19.37
A


2611
N
ARG
355
39.451
21.570
71.612
1.00
20.07
A


2612
CA
ARG
355
39.862
22.582
72.574
1.00
24.19
A


2613
CB
ARG
355
38.877
23.731
72.704
1.00
24.81
A


2614
CG
ARG
355
37.463
23.391
73.154
1.00
23.80
A


2615
CD
ARG
355
37.299
23.779
74.644
1.00
22.79
A


2616
NE
ARG
355
36.008
23.331
75.162
1.00
19.75
A


2617
CZ
ARG
355
35.280
24.057
76.030
1.00
21.29
A


2618
NH1
ARG
355
34.110
23.545
76.472
1.00
19.74
A


2619
NH2
ARG
355
35.690
25.217
76.527
1.00
17.69
A


2620
C
ARG
355
40.188
21.966
73.940
1.00
24.08
A


2621
O
ARG
355
41.151
22.428
74.534
1.00
25.32
A


2622
N
LYS
356
39.526
20.953
74.421
1.00
25.09
A


2623
CA
LYS
356
39.799
20.338
75.708
1.00
27.74
A


2624
CB
LYS
356
38.648
19.409
76.094
1.00
27.24
A


2625
CG
LYS
356
37.390
20.203
76.475
1.00
25.79
A


2626
CD
LYS
356
36.454
19.214
77.179
1.00
29.05
A


2627
CE
LYS
356
35.190
19.974
77.619
1.00
32.78
A


2628
NZ
LYS
356
34.318
19.032
78.386
1.00
36.70
A


2629
C
LYS
356
41.121
19.569
75.655
1.00
30.43
A


2630
O
LYS
356
41.947
19.680
76.565
1.00
27.52
A


2631
N
ARG
357
41.361
18.817
74.564
1.00
31.05
A


2632
CA
ARG
357
42.621
18.093
74.421
1.00
32.46
A


2633
CB
ARG
357
42.658
17.059
73.321
1.00
36.01
A


2634
CG
ARG
357
43.890
16.170
73.277
1.00
39.76
A


2635
CD
ARG
357
44.016
15.262
74.483
1.00
43.81
A


2636
NE
ARG
357
43.568
13.887
74.253
1.00
47.60
A


2637
CZ
ARG
357
44.317
13.006
73.567
1.00
50.39
A


2638
NH1
ARG
357
45.498
13.408
73.091
1.00
50.63
A


2639
NH2
ARG
357
43.900
11.761
73.354
1.00
52.74
A


2640
C
ARG
357
43.768
19.101
74.263
1.00
31.49
A


2641
O
ARG
357
44.814
18.907
74.929
1.00
29.47
A


2642
N
SER
358
43.528
20.233
73.605
1.00
27.94
A


2643
CA
SER
358
44.568
21.220
73.356
1.00
27.83
A


2644
CB
SER
358
44.117
22.313
72.371
1.00
26.50
A


2645
OG
SER
358
43.865
21.734
71.075
1.00
25.38
A


2646
C
SER
358
45.012
21.905
74.649
1.00
31.76
A


2647
O
SER
358
46.189
22.262
74.821
1.00
30.11
A


2648
N
MET
359
44.041
22.135
75.526
1.00
33.43
A


2649
CA
MET
359
44.364
22.748
76.811
1.00
36.99
A


2650
CB
MET
359
43.176
23.519
77.375
1.00
40.55
A


2651
CG
MET
359
42.966
24.791
76.524
1.00
45.08
A


2652
SD
MET
359
41.623
25.802
77.145
1.00
52.35
A


2653
CE
MET
359
40.359
24.601
77.538
1.00
48.97
A


2654
C
MET
359
44.954
21.716
77.750
1.00
35.16
A


2655
O
MET
359
45.929
22.078
78.412
1.00
35.83
A


2656
N
ALA
360
44.537
20.467
77.757
1.00
33.81
A


2657
CA
ALA
360
45.113
19.439
78.600
1.00
34.48
A


2658
CB
ALA
360
44.333
18.138
78.562
1.00
32.76
A


2659
C
ALA
360
46.574
19.153
78.219
1.00
36.33
A


2660
O
ALA
360
47.415
18.788
79.060
1.00
36.62
A


2661
N
GLU
361
46.928
19.300
76.949
1.00
35.22
A


2662
CA
GLU
361
48.292
19.058
76.489
1.00
35.33
A


2663
CB
GLU
361
48.299
18.568
75.036
1.00
34.20
A


2664
CG
GLU
361
47.649
17.207
74.839
1.00
36.67
A


2665
CD
GLU
361
47.522
16.832
73.369
1.00
36.07
A


2666
OE1
GLU
361
47.550
17.741
72.512
1.00
36.35
A


2667
OE2
GLU
361
47.428
15.624
73.088
1.00
37.56
A


2668
C
GLU
361
49.150
20.315
76.612
1.00
34.08
A


2669
O
GLU
361
50.302
20.258
76.180
1.00
32.86
A


2670
N
GLY
362
48.604
21.464
76.988
1.00
32.03
A


2671
CA
GLY
362
49.379
22.684
77.031
1.00
32.94
A


2672
C
GLY
362
49.730
23.307
75.688
1.00
33.44
A


2673
O
GLY
362
50.705
24.087
75.585
1.00
33.68
A


2674
N
LYS
363
48.944
23.049
74.654
1.00
30.95
A


2675
CA
LYS
363
49.193
23.643
73.341
1.00
32.10
A


2676
CB
LYS
363
48.229
23.096
72.281
1.00
34.04
A


2677
CG
LYS
363
48.245
21.589
72.100
1.00
36.23
A


2678
CD
LYS
363
49.675
21.121
71.840
1.00
40.53
A


2679
CE
LYS
363
49.688
19.986
70.821
1.00
42.21
A


2680
NZ
LYS
363
51.049
19.831
70.240
1.00
43.78
A


2681
C
LYS
363
49.095
25.150
73.474
1.00
29.77
A


2682
O
LYS
363
48.453
25.687
74.384
1.00
29.55
A


2683
N
SER
364
49.667
25.870
72.534
1.00
28.95
A


2684
CA
SER
364
49.649
27.325
72.569
1.00
28.77
A


2685
CB
SER
364
50.729
27.912
71.645
1.00
29.69
A


2686
OG
SER
364
50.550
27.443
70.314
1.00
30.42
A


2687
C
SER
364
48.325
27.920
72.116
1.00
26.66
A


2688
O
SER
364
48.166
29.123
72.216
1.00
23.83
A


2689
N
THR
365
47.454
27.155
71.452
1.00
26.85
A


2690
CA
THR
365
46.173
27.691
70.993
1.00
25.37
A


2691
CB
THR
365
46.096
28.110
69.509
1.00
26.90
A


2692
OG1
THR
365
45.908
26.904
68.742
1.00
22.84
A


2693
CG2
THR
365
47.305
28.882
68.987
1.00
26.67
A


2694
C
THR
365
45.075
26.655
71.253
1.00
24.62
A


2695
O
THR
365
45.373
25.479
71.461
1.00
25.62
A


2696
N
THR
366
43.801
27.030
71.180
1.00
23.49
A


2697
CA
THR
366
42.722
26.047
71.360
1.00
24.17
A


2698
CB
THR
366
41.362
26.761
71.570
1.00
22.41
A


2699
OG1
THR
366
41.195
27.696
70.499
1.00
20.38
A


2700
CG2
THR
366
41.325
27.528
72.880
1.00
23.95
A


2701
C
THR
366
42.551
25.109
70.164
1.00
23.10
A


2702
O
THR
366
41.855
24.097
70.270
1.00
21.41
A


2703
N
GLY
367
43.239
25.382
69.057
1.00
22.88
A


2704
CA
GLY
367
43.148
24.484
67.903
1.00
22.96
A


2705
C
GLY
367
44.462
23.746
67.678
1.00
23.68
A


2706
O
GLY
367
45.163
23.892
66.672
1.00
22.45
A


2707
N
GLU
368
44.834
22.922
68.642
1.00
22.76
A


2708
CA
GLU
368
45.999
22.046
68.632
1.00
25.26
A


2709
CB
GLU
368
45.767
20.982
67.542
1.00
24.97
A


2710
CG
GLU
368
44.482
20.181
67.744
1.00
26.24
A


2711
CD
GLU
368
44.200
19.090
66.749
1.00
26.19
A


2712
OE1
GLU
368
44.799
19.074
65.643
1.00
26.16
A


2713
OE2
GLU
368
43.352
18.215
67.011
1.00
26.44
A


2714
C
GLU
368
47.336
22.762
68.438
1.00
25.87
A


2715
O
GLU
368
48.273
22.206
67.826
1.00
25.65
A


2716
N
GLY
369
47.399
24.010
68.859
1.00
25.80
A


2717
CA
GLY
369
48.594
24.836
68.723
1.00
28.34
A


2718
C
GLY
369
48.656
25.551
67.394
1.00
29.47
A


2719
O
GLY
369
49.620
26.270
67.121
1.00
30.88
A


2720
N
LEU
370
47.682
25.345
66.514
1.00
28.55
A


2721
CA
LEU
370
47.632
25.953
65.206
1.00
28.68
A


2722
CB
LEU
370
47.219
24.933
64.126
1.00
25.24
A


2723
CG
LEU
370
48.087
23.679
64.134
1.00
27.19
A


2724
CD2
LEU
370
49.529
24.028
63.719
1.00
29.09
A


2725
CD1
LEU
370
47.540
22.629
63.195
1.00
26.28
A


2726
C
LEU
370
46.665
27.127
65.176
1.00
29.14
A


2727
O
LEU
370
45.843
27.293
66.083
1.00
27.98
A


2697
N
ASP
371
46.750
27.902
64.150
0.50
29.30
A


2698
CA
ASP
371
45.960
29.126
64.033
0.50
31.31
A


2699
CB
ASP
371
46.715
30.157
63.207
0.50
32.70
A


2700
CG
ASP
371
45.933
31.454
63.035
0.50
34.21
A


2701
OD1
ASP
371
45.675
32.198
64.055
0.50
35.27
A


2702
OD2
ASP
371
45.528
31.795
61.862
0.50
35.82
A


2703
C
ASP
371
44.570
28.897
63.404
0.50
30.67
A


2704
O
ASP
371
43.543
29.244
63.998
0.50
27.92
A


2697
N
2ASP
371
46.705
27.911
64.141
0.50
28.99
A


2698
CA
2ASP
371
45.915
29.152
64.058
0.50
30.87
A


2699
CB
2ASP
371
46.688
30.233
63.325
0.50
31.47
A


2700
CG
2ASP
371
47.790
30.848
64.182
0.50
32.85
A


2701
OD
12ASP
371
48.045
30.362
65.347
0.50
33.88
A


2702
OD
22ASP
371
48.466
31.846
63.731
0.50
31.60
A


2703
C
2ASP
371
44.563
29.022
63.333
0.50
30.36
A


2704
O
2ASP
371
43.571
29.636
63.734
0.50
28.09
A


2744
N
CYS
372
44.499
28.323
62.182
1.00
31.05
A


2745
CA
CYS
372
43.222
28.150
61.491
1.00
30.84
A


2746
CB
CYS
372
43.281
28.726
60.043
1.00
34.75
A


2747
SG
CYS
372
43.230
30.538
60.118
1.00
46.77
A


2748
C
CYS
372
42.771
26.726
61.387
1.00
27.81
A


2749
O
CYS
372
43.602
25.821
61.490
1.00
27.51
A


2750
N
GLY
373
41.450
26.476
61.320
1.00
25.16
A


2751
CA
GLY
373
40.983
25.098
61.238
1.00
22.49
A


2752
C
GLY
373
39.745
25.033
60.343
1.00
22.07
A


2753
O
GLY
373
39.087
26.034
60.091
1.00
20.72
A


2754
N
VAL
374
39.481
23.816
59.886
1.00
22.47
A


2755
CA
VAL
374
38.398
23.580
58.973
1.00
22.27
A


2756
CB
VAL
374
38.881
23.065
57.564
1.00
23.26
A


2757
CG1
VAL
374
37.691
22.725
56.672
1.00
22.41
A


2758
CG2
VAL
374
39.791
24.099
56.930
1.00
20.89
A


2759
C
VAL
374
37.529
22.467
59.506
1.00
19.69
A


2760
O
VAL
374
38.008
21.392
59.810
1.00
21.40
A


2761
N
LEU
375
36.263
22.800
59.562
1.00
18.61
A


2762
CA
LEU
375
35.227
21.858
59.985
1.00
20.84
A


2763
CB
LEU
375
34.399
22.581
61.033
1.00
19.48
A


2764
CG
LEU
375
32.960
22.370
61.454
1.00
24.36
A


2765
CD2
LEU
375
32.919
21.718
62.834
1.00
22.14
A


2766
CD1
LEU
375
31.916
21.827
60.498
1.00
21.76
A


2767
C
LEU
375
34.377
21.505
58.762
1.00
17.93
A


2768
O
LEU
375
34.032
22.409
57.997
1.00
17.39
A


2769
N
PHE
376
34.069
20.233
58.631
1.00
19.38
A


2770
CA
PHE
376
33.245
19.746
57.542
1.00
20.03
A


2771
CB
PHE
376
34.008
18.709
56.672
1.00
20.69
A


2772
CG
PHE
376
35.113
19.254
55.790
1.00
20.74
A


2773
CD1
PHE
376
36.372
18.688
55.794
1.00
20.92
A


2774
CD2
PHE
376
34.850
20.293
54.922
1.00
21.20
A


2775
CE1
PHE
376
37.362
19.182
54.955
1.00
21.74
A


2776
CE2
PHE
376
35.843
20.804
54.074
1.00
21.65
A


2777
CZ
PHE
376
37.105
20.254
54.097
1.00
21.09
A


2778
C
PHE
376
32.073
18.946
58.116
1.00
18.85
A


2779
O
PHE
376
32.268
18.040
58.913
1.00
20.24
A


2780
N
GLY
377
30.907
19.186
57.573
1.00
17.84
A


2781
CA
GLY
377
29.708
18.411
57.740
1.00
17.39
A


2782
C
GLY
377
29.323
17.792
56.379
1.00
17.57
A


2783
O
GLY
377
29.396
18.495
55.368
1.00
17.23
A


2784
N
PHE
378
28.794
16.596
56.360
1.00
17.66
A


2785
CA
PHE
378
28.372
15.939
55.104
1.00
19.03
A


2786
CB
PHE
378
29.288
14.720
54.791
1.00
17.54
A


2787
CG
PHE
378
30.774
15.021
54.880
1.00
18.27
A


2788
CD1
PHE
378
31.344
15.928
53.999
1.00
19.70
A


2789
CD2
PHE
378
31.589
14.415
55.812
1.00
19.70
A


2790
CE1
PHE
378
32.702
16.237
54.051
1.00
19.69
A


2791
CE2
PHE
378
32.959
14.670
55.856
1.00
18.59
A


2792
CZ
PHE
378
33.499
15.599
54.985
1.00
19.25
A


2793
C
PHE
378
26.956
15.424
55.248
1.00
21.11
A


2794
O
PHE
378
26.691
14.692
56.206
1.00
19.64
A


2795
N
GLY
379
26.024
15.749
54.358
1.00
18.60
A


2796
CA
GLY
379
24.655
15.284
54.458
1.00
18.83
A


2797
C
GLY
379
23.975
15.169
53.088
1.00
19.23
A


2798
O
GLY
379
24.676
15.268
52.089
1.00
16.57
A


2799
N
PRO
380
22.687
14.846
53.111
1.00
19.92
A


2800
CA
PRO
380
21.945
14.539
51.903
1.00
18.57
A


2801
CD
PRO
380
21.881
14.551
54.326
1.00
17.09
A


2802
CB
PRO
380
20.519
14.257
52.418
1.00
19.08
A


2803
CG
PRO
380
20.764
13.671
53.814
1.00
20.08
A


2804
C
PRO
380
22.017
15.713
50.940
1.00
17.30
A


2805
O
PRO
380
22.112
16.861
51.324
1.00
16.43
A


2806
N
GLY
381
22.008
15.392
49.637
1.00
18.61
A


2807
CA
GLY
381
22.098
16.455
48.592
1.00
16.07
A


2808
C
GLY
381
23.079
15.812
47.579
1.00
19.93
A


2809
O
GLY
381
22.724
15.621
46.442
1.00
17.52
A


2810
N
MET
382
24.286
15.299
47.676
1.00
18.83
A


2811
CA
MET
382
25.114
15.363
48.821
1.00
21.67
A


2812
CB
MET
382
26.411
14.578
48.884
1.00
23.56
A


2813
CG
MET
382
26.037
13.128
49.240
1.00
29.90
A


2814
SD
MET
382
27.518
12.143
49.463
1.00
35.81
A


2815
CE
MET
382
28.502
13.200
50.530
1.00
31.30
A


2816
C
MET
382
25.391
16.852
49.094
1.00
20.54
A


2817
O
MET
382
25.740
17.563
48.151
1.00
19.09
A


2818
N
THR
383
25.422
17.229
50.361
1.00
16.12
A


2819
CA
THR
383
25.811
18.613
50.712
1.00
18.02
A


2820
CB
THR
383
24.769
19.341
51.545
1.00
19.74
A


2821
OG1
THR
383
23.538
19.502
50.835
1.00
19.72
A


2822
CG2
THR
383
25.173
20.731
52.001
1.00
19.59
A


2823
C
THR
383
27.086
18.606
51.564
1.00
19.79
A


2824
O
THR
383
27.168
17.778
52.534
1.00
17.85
A


2825
N
VAL
384
27.977
19.564
51.364
1.00
18.96
A


2826
CA
VAL
384
29.141
19.665
52.260
1.00
19.75
A


2827
CB
VAL
384
30.529
19.605
51.599
1.00
22.71
A


2828
CG1
VAL
384
31.692
19.729
52.581
1.00
22.63
A


2829
CG2
VAL
384
30.661
18.336
50.801
1.00
24.06
A


2830
C
VAL
384
29.020
21.048
52.896
1.00
18.08
A


2831
O
VAL
384
28.778
22.056
52.209
1.00
17.98
A


2832
N
GLU
385
29.123
21.079
54.223
1.00
14.18
A


2833
CA
GLU
385
29.202
22.419
54.848
1.00
13.89
A


2834
CB
GLU
385
28.299
22.479
56.077
1.00
15.16
A


2835
CG
GLU
385
26.828
22.363
55.676
1.00
16.58
A


2836
CD
GLU
385
26.015
23.584
55.983
1.00
15.38
A


2837
OE1
GLU
385
26.525
24.650
56.402
1.00
18.10
A


2838
OE2
GLU
385
24.794
23.421
55.817
1.00
17.03
A


2839
C
GLU
385
30.674
22.620
55.247
1.00
14.43
A


2840
O
GLU
385
31.204
21.689
55.853
1.00
17.77
A


2841
N
THR
386
31.314
23.707
54.914
1.00
15.61
A


2842
CA
THR
386
32.715
23.927
55.296
1.00
16.74
A


2843
CB
THR
386
33.586
24.168
53.992
1.00
17.73
A


2844
OG1
THR
386
33.355
22.983
53.252
1.00
16.29
A


2845
CG2
THR
386
35.063
24.191
54.418
1.00
18.77
A


2846
C
THR
386
32.855
25.164
56.150
1.00
17.03
A


2847
O
THR
386
32.420
26.231
55.696
1.00
17.70
A


2848
N
VAL
387
33.308
25.006
57.417
1.00
16.84
A


2849
CA
VAL
387
33.355
26.208
58.276
1.00
17.13
A


2850
CB
VAL
387
32.508
25.999
59.558
1.00
17.99
A


2851
CG1
VAL
387
32.637
27.193
60.514
1.00
15.01
A


2852
CG2
VAL
387
31.034
25.779
59.133
1.00
17.10
A


2853
C
VAL
387
34.809
26.463
58.678
1.00
16.46
A


2854
O
VAL
387
35.443
25.504
59.132
1.00
17.67
A


2855
N
VAL
388
35.297
27.687
58.527
1.00
16.92
A


2856
CA
VAL
388
36.665
27.944
58.972
1.00
19.66
A


2857
CB
VAL
388
37.421
28.938
58.054
1.00
19.90
A


2858
CG1
VAL
388
38.737
29.427
58.644
1.00
21.93
A


2859
CG2
VAL
388
37.676
28.243
56.695
1.00
20.21
A


2860
C
VAL
388
36.588
28.537
60.402
1.00
19.79
A


2861
O
VAL
388
35.822
29.461
60.655
1.00
17.73
A


2862
N
LEU
389
37.399
27.914
61.275
1.00
20.60
A


2863
CA
LEU
389
37.505
28.438
62.639
1.00
22.00
A


2864
CB
LEU
389
37.299
27.352
63.703
1.00
19.81
A


2865
CG
LEU
389
35.932
26.671
63.609
1.00
19.87
A


2866
CD2
LEU
389
34.804
27.686
63.712
1.00
15.50
A


2867
CD1
LEU
389
35.782
25.592
64.677
1.00
21.26
A


2868
C
LEU
389
38.914
29.027
62.848
1.00
22.61
A


2869
O
LEU
389
39.864
28.586
62.198
1.00
20.80
A


2870
N
ARG
390
38.985
30.137
63.579
1.00
21.65
A


2871
CA
ARG
390
40.274
30.670
64.007
1.00
23.48
A


2872
CB
ARG
390
40.412
32.176
63.883
1.00
24.20
A


2873
CG
ARG
390
41.852
32.677
64.157
1.00
26.37
A


2874
CD
ARG
390
41.913
34.112
63.640
1.00
33.41
A


2875
NE
ARG
390
41.855
34.138
62.177
1.00
36.49
A


2876
CZ
ARG
390
41.265
34.873
61.257
1.00
39.62
A


2877
NH1
ARG
390
41.529
34.522
59.979
1.00
40.06
A


2878
NH2
ARG
390
40.440
35.914
61.389
1.00
37.97
A


2879
C
ARG
390
40.420
30.284
65.499
1.00
23.63
A


2880
O
ARG
390
39.512
30.603
66.269
1.00
21.29
A


2881
N
SER
391
41.536
29.674
65.881
1.00
24.10
A


2882
CA
SER
391
41.746
29.309
67.293
1.00
24.53
A


2883
CB
SER
391
42.907
28.303
67.371
1.00
25.80
A


2884
OG
SER
391
44.106
29.024
67.101
1.00
25.49
A


2885
C
SER
391
42.092
30.535
68.131
1.00
24.44
A


2886
O
SER
391
42.241
31.627
67.583
1.00
22.85
A


2887
N
VAL
392
42.135
30.383
69.462
1.00
25.39
A


2888
CA
VAL
392
42.446
31.497
70.350
1.00
27.60
A


2889
CB
VAL
392
41.215
31.668
71.270
1.00
29.90
A


2890
CG1
VAL
392
41.584
32.214
72.641
1.00
31.86
A


2891
CG2
VAL
392
40.138
32.520
70.627
1.00
29.27
A


2892
C
VAL
392
43.719
31.104
71.129
1.00
28.19
A


2893
O
VAL
392
43.979
29.932
71.429
1.00
23.40
A


2894
N
ARG
393
44.605
32.061
71.379
1.00
34.51
A


2895
CA
ARG
393
45.871
31.761
72.064
1.00
41.77
A


2896
CB
ARG
393
46.813
32.969
72.070
1.00
46.60
A


2897
CG
ARG
393
47.466
33.185
70.719
1.00
53.03
A


2898
CD
ARG
393
48.179
34.530
70.632
1.00
58.41
A


2899
NE
ARG
393
48.674
34.709
69.265
1.00
63.01
A


2900
CZ
ARG
393
49.502
35.647
68.825
1.00
65.65
A


2901
NH1
ARG
393
49.991
36.596
69.618
1.00
66.46
A


2902
NH2
ARG
393
49.820
35.628
67.530
1.00
66.47
A


2903
C
ARG
393
45.641
31.358
73.525
1.00
44.97
A


2904
O
ARG
393
44.855
32.011
74.195
1.00
41.97
A


2905
N
VAL
394
46.289
30.263
73.934
1.00
48.90
A


2906
CA
VAL
394
46.116
29.830
75.336
1.00
55.03
A


2907
CB
VAL
394
46.234
28.285
75.569
1.00
54.72
A


2908
CG1
VAL
394
45.934
28.121
77.130
1.00
54.65
A


2909
CG2
VAL
394
45.001
27.594
74.873
1.00
53.65
A


2910
C
VAL
394
47.334
30.484
76.041
1.00
59.46
A


2911
O
VAL
394
48.501
30.187
75.818
1.00
60.03
A


2912
N
THR
395
46.953
31.493
76.808
1.00
64.60
A


2913
CA
THR
395
47.832
32.357
77.563
1.00
68.25
A


2914
CB
THR
395
49.039
31.639
78.196
1.00
69.16
A


2915
OG1
THR
395
48.622
30.751
79.246
1.00
68.72
A


2916
CG2
THR
395
50.000
32.654
78.802
1.00
69.44
A


2917
C
THR
395
48.231
33.576
76.731
1.00
68.88
A


2918
OT
THR
395
48.680
33.459
75.570
1.00
71.94
A


2919
OXT
THR
395
48.680
33.459
75.570
1.00
71.94
A


2920
C8
AAC
396
29.088
−0.939
53.568
1.00
30.42
A


2921
N9
AAC
396
28.436
−2.108
53.270
1.00
32.14
A


2922
C4
AAC
396
27.290
−1.711
52.572
1.00
31.69
A


2923
C5
AAC
396
27.345
−0.331
52.498
1.00
30.04
A


2924
N7
AAC
396
28.425
0.168
53.194
1.00
30.04
A


2925
N3
AAC
396
26.249
−2.559
52.247
1.00
31.41
A


2926
C2
AAC
396
25.326
−1.874
51.601
1.00
30.53
A


2927
N1
AAC
396
25.230
−0.512
51.586
1.00
29.51
A


2928
C6
AAC
396
26.161
0.334
52.104
1.00
29.32
A


2929
N6
AAC
396
26.039
1.687
52.072
1.00
27.37
A


2930
C1′
AAC
396
28.970
−3.654
53.307
1.00
32.51
A


2931
C2′
AAC
396
30.145
−4.137
52.566
1.00
34.01
A


2932
O2′
AAC
396
29.559
−4.403
51.369
1.00
34.33
A


2933
C3′
AAC
396
30.770
−5.048
53.614
1.00
33.21
A


2934
O3′
AAC
396
30.180
−6.436
53.741
1.00
35.60
A


2935
C4′
AAC
396
30.447
−4.539
55.074
1.00
32.68
A


2936
O4′
AAC
396
29.243
−3.659
54.745
1.00
31.75
A


2937
C5′
AAC
396
31.558
−3.523
55.492
1.00
33.23
A


2938
O5′
AAC
396
32.462
−3.135
54.341
1.00
34.84
A


2939
P1
AAC
396
33.757
−3.149
54.009
1.00
35.11
A


2940
O11
AAC
396
33.972
−2.682
52.617
1.00
36.07
A


2941
O12
AAC
396
34.138
−4.565
54.285
1.00
34.22
A


2942
O6
AAC
396
34.317
−2.148
55.094
1.00
33.48
A


2943
P2
AAC
396
34.629
−0.608
55.274
1.00
31.67
A


2944
O21
AAC
396
34.091
0.157
54.141
1.00
29.47
A


2945
O22
AAC
396
36.088
−0.404
55.453
1.00
31.91
A


2946
O7
AAC
396
34.078
−0.103
56.587
1.00
33.38
A


2947
CPB
AAC
396
32.613
−0.372
56.779
1.00
31.59
A


2948
CPA
AAC
396
31.930
1.012
57.138
1.00
32.98
A


2949
CP7
AAC
396
32.377
2.047
56.089
1.00
32.64
A


2950
CP9
AAC
396
32.449
1.368
58.564
1.00
32.37
A


2951
CP8
AAC
396
30.388
0.907
57.120
1.00
31.38
A


2952
OP3
AAC
396
31.895
1.652
54.775
1.00
34.88
A


2953
CP6
AAC
396
31.780
3.481
56.251
1.00
32.61
A


2954
OP2
AAC
396
32.472
4.317
56.895
1.00
30.58
A


2955
NP2
AAC
396
30.924
3.796
55.273
1.00
31.11
A


2956
CP5
AAC
396
30.358
5.220
55.331
1.00
32.05
A


2957
CP4
AAC
396
29.035
5.178
56.067
1.00
32.87
A


2958
CP3
AAC
396
28.213
6.418
55.771
1.00
32.93
A


2959
OP1
AAC
396
27.905
6.418
54.570
1.00
32.85
A


2960
NP1
AAC
396
27.858
7.297
56.675
1.00
29.26
A


2961
CP2
AAC
396
27.034
8.515
56.304
1.00
28.60
A


2962
CP1
AAC
396
25.597
8.467
56.855
1.00
30.84
A


2963
S
AAC
396
24.755
9.968
56.383
1.00
33.02
A


2964
P3
AAC
396
30.702
−7.962
53.720
1.00
35.35
A


2965
O31
AAC
396
31.571
−8.202
54.889
1.00
34.33
A


2966
O32
AAC
396
31.470
−8.265
52.484
1.00
35.06
A


2967
O33
AAC
396
29.270
−8.684
53.804
1.00
36.14
A


2968
C51
AAC
396
23.138
9.614
56.893
1.00
35.73
A


2969
C52
AAC
396
22.130
10.649
56.436
1.00
37.65
A


2970
O51
AAC
396
22.832
8.462
57.127
1.00
37.20
A


2971
C53
AAC
396
21.523
11.431
57.594
1.00
38.75
A


2972
C54
AAC
396
20.940
10.674
58.762
1.00
37.79
A


2973
O52
AAC
396
21.600
12.643
57.568
1.00
38.80
A


2974
N
GLY
20
22.008
49.110
54.402
1.00
30.13
B


2975
CA
GLY
20
20.729
49.727
54.903
1.00
23.69
B


2976
C
GLY
20
19.882
48.505
55.299
1.00
20.92
B


2977
O
GLY
20
20.366
47.374
55.403
1.00
20.99
B


2978
N
LEU
21
18.625
48.779
55.519
1.00
17.75
B


2979
CA
LEU
21
17.682
47.768
55.953
1.00
20.77
B


2980
CB
LEU
21
16.341
48.472
56.276
1.00
18.00
B


2981
CG
LEU
21
16.409
49.431
57.481
1.00
21.40
B


2982
CD2
LEU
21
16.626
48.688
58.810
1.00
22.33
B


2983
CD1
LEU
21
15.145
50.253
57.628
1.00
19.17
B


2984
C
LEU
21
17.474
46.714
54.869
1.00
22.13
B


2985
O
LEU
21
17.475
47.035
53.636
1.00
19.43
B


2986
N
ALA
22
17.267
45.485
55.356
1.00
19.59
B


2987
CA
ALA
22
16.823
44.426
54.424
1.00
20.74
B


2988
CB
ALA
22
16.533
43.123
55.166
1.00
18.92
B


2989
C
ALA
22
15.560
44.925
53.725
1.00
19.75
B


2990
O
ALA
22
14.654
45.395
54.407
1.00
17.56
B


2991
N
THR
23
15.480
44.835
52.391
1.00
18.28
B


2992
CA
THR
23
14.275
45.344
51.708
1.00
17.46
B


2993
CB
THR
23
14.750
46.493
50.788
1.00
20.38
B


2994
OG1
THR
23
15.430
47.452
51.592
1.00
16.94
B


2995
CG2
THR
23
13.662
47.179
49.971
1.00
19.14
B


2996
C
THR
23
13.654
44.271
50.813
1.00
18.33
B


2997
O
THR
23
14.392
43.481
50.195
1.00
18.10
B


2998
N
ILE
24
12.338
44.231
50.809
1.00
15.97
B


2999
CA
ILE
24
11.616
43.299
49.966
1.00
16.44
B


3000
CB
ILE
24
10.167
43.151
50.443
1.00
16.72
B


3001
CG2
ILE
24
9.347
42.355
49.421
1.00
16.82
B


3002
CG1
ILE
24
10.141
42.392
51.809
1.00
17.90
B


3003
CD1
ILE
24
8.737
42.488
52.399
1.00
14.92
B


3004
C
ILE
24
11.634
43.907
48.544
1.00
15.66
B


3005
O
ILE
24
11.206
45.046
48.453
1.00
16.75
B


3006
N
LEU
25
12.196
43.200
47.566
1.00
17.77
B


3007
CA
LEU
25
12.300
43.723
46.203
1.00
18.64
B


3008
CB
LEU
25
13.748
43.484
45.728
1.00
17.20
B


3009
CG
LEU
25
14.865
44.002
46.651
1.00
17.92
B


3010
CD2
LEU
25
14.838
45.532
46.690
1.00
17.51
B


3011
CD1
LEU
25
16.263
43.583
46.185
1.00
20.19
B


3012
C
LEU
25
11.376
43.094
45.186
1.00
19.91
B


3013
O
LEU
25
11.280
43.565
44.022
1.00
20.36
B


3014
N
ALA
26
10.742
41.976
45.526
1.00
18.68
B


3015
CA
ALA
26
9.828
41.315
44.601
1.00
18.32
B


3016
CB
ALA
26
10.581
40.597
43.452
1.00
15.20
B


3017
C
ALA
26
9.007
40.302
45.374
1.00
18.51
B


3018
O
ALA
26
9.484
39.724
46.363
1.00
18.01
B


3019
N
ILE
27
7.758
40.130
44.969
1.00
15.99
B


3020
CA
ILE
27
6.897
39.116
45.522
1.00
18.77
B


3021
CB
ILE
27
5.792
39.725
46.452
1.00
17.13
B


3022
CG2
ILE
27
4.978
38.593
47.077
1.00
18.32
B


3023
CG1
ILE
27
6.452
40.581
47.537
1.00
20.55
B


3024
CD1
ILE
27
5.551
41.593
48.206
1.00
21.37
B


3025
C
ILE
27
6.199
38.314
44.451
1.00
16.71
B


3026
O
ILE
27
5.447
38.959
43.663
1.00
19.13
B


3027
N
GLY
28
6.238
36.988
44.527
1.00
17.02
B


3028
CA
GLY
28
5.416
36.216
43.587
1.00
18.19
B


3029
C
GLY
28
4.584
35.165
44.304
1.00
21.13
B


3030
O
GLY
28
5.026
34.712
45.367
1.00
19.81
B


3031
N
THR
29
3.373
34.841
43.855
1.00
16.70
B


3032
CA
THR
29
2.547
33.832
44.503
1.00
19.55
B


3033
CB
THR
29
1.326
34.437
45.216
1.00
19.77
B


3034
OG1
THR
29
0.531
35.210
44.302
1.00
19.35
B


3035
CG2
THR
29
1.778
35.415
46.306
1.00
16.94
B


3036
C
THR
29
2.025
32.802
43.504
1.00
20.47
B


3037
O
THR
29
1.910
33.080
42.300
1.00
18.54
B


3038
N
ALA
30
1.632
31.632
43.978
1.00
18.73
B


3039
CA
ALA
30
1.112
30.563
43.133
1.00
19.51
B


3040
CB
ALA
30
2.219
29.593
42.702
1.00
16.21
B


3041
C
ALA
30
0.154
29.747
44.000
1.00
21.06
B


3042
O
ALA
30
0.300
29.656
45.242
1.00
17.27
B


3043
N
THR
31
−0.779
29.058
43.380
1.00
18.81
B


3044
CA
THR
31
−1.678
28.138
44.037
1.00
20.19
B


3045
CB
THR
31
−3.071
28.716
44.280
1.00
21.90
B


3046
OG1
THR
31
−3.684
29.108
43.030
1.00
24.53
B


3047
CG2
THR
31
−3.097
30.004
45.138
1.00
20.79
B


3048
C
THR
31
−1.860
26.921
43.132
1.00
21.99
B


3049
O
THR
31
−1.635
27.056
41.944
1.00
20.19
B


3050
N
PRO
32
−2.230
25.791
43.694
1.00
20.90
B


3051
CA
PRO
32
−2.705
24.671
42.935
1.00
20.90
B


3052
CD
PRO
32
−2.474
25.621
45.182
1.00
19.82
B


3053
CB
PRO
32
−3.136
23.641
43.982
1.00
20.86
B


3054
CG
PRO
32
−2.397
24.104
45.236
1.00
19.96
B


3055
C
PRO
32
−3.900
25.112
42.079
1.00
20.14
B


3056
O
PRO
32
−4.609
26.075
42.354
1.00
18.10
B


3057
N
PRO
33
−4.067
24.465
40.936
1.00
21.96
B


3058
CA
PRO
33
−5.117
24.826
39.982
1.00
25.39
B


3059
CD
PRO
33
−3.227
23.355
40.446
1.00
22.41
B


3060
CB
PRO
33
−4.754
23.994
38.740
1.00
24.65
B


3061
CG
PRO
33
−4.085
22.781
39.334
1.00
26.31
B


3062
C
PRO
33
−6.536
24.549
40.458
1.00
25.18
B


3063
O
PRO
33
−7.360
25.395
40.193
1.00
28.12
B


3064
N
ASN
34
−6.852
23.480
41.129
1.00
27.34
B


3065
CA
ASN
34
−8.170
23.081
41.645
1.00
30.08
B


3066
CB
ASN
34
−8.087
21.643
42.171
1.00
33.39
B


3067
CG
ASN
34
−9.127
21.074
43.106
1.00
37.83
B


3068
OD1
ASN
34
−10.314
21.422
43.003
1.00
39.25
B


3069
ND2
ASN
34
−8.801
20.176
44.064
1.00
35.81
B


3070
C
ASN
34
−8.642
24.013
42.766
1.00
30.65
B


3071
O
ASN
34
−7.999
24.199
43.797
1.00
26.27
B


3072
N
CYS
35
−9.758
24.681
42.536
1.00
28.97
B


3073
CA
CYS
35
−10.386
25.618
43.431
1.00
30.72
B


3074
CB
CYS
35
−10.683
26.843
42.553
1.00
32.78
B


3075
SG
CYS
35
−11.330
28.291
43.356
1.00
34.81
B


3076
C
CYS
35
−11.733
25.077
43.899
1.00
30.56
B


3077
O
CYS
35
−12.564
24.726
43.026
1.00
28.14
B


3078
N
VAL
36
−12.010
25.115
45.195
1.00
27.43
B


3079
CA
VAL
36
−13.350
24.723
45.675
1.00
29.87
B


3080
CB
VAL
36
−13.365
23.513
46.620
1.00
29.99
B


3081
CG1
VAL
36
−14.794
23.072
46.955
1.00
32.05
B


3082
CG2
VAL
36
−12.676
22.281
46.041
1.00
29.23
B


3083
C
VAL
36
−13.999
25.907
46.381
1.00
31.35
B


3084
O
VAL
36
−13.382
26.519
47.293
1.00
30.21
B


3085
N
ALA
37
−15.257
26.231
46.004
1.00
28.89
B


3086
CA
ALA
37
−15.946
27.341
46.634
1.00
28.81
B


3087
CB
ALA
37
−17.171
27.768
45.838
1.00
30.11
B


3088
C
ALA
37
−16.333
26.966
48.066
1.00
28.01
B


3089
O
ALA
37
−16.783
25.827
48.269
1.00
27.02
B


3090
N
GLN
38
−16.248
27.912
49.003
1.00
28.89
B


3091
CA
GLN
38
−16.540
27.550
50.409
1.00
28.43
B


3092
CB
GLN
38
−16.187
28.665
51.390
1.00
28.73
B


3093
CG
GLN
38
−16.180
28.249
52.872
1.00
27.51
B


3094
CD
GLN
38
−15.036
27.352
53.262
1.00
25.61
B


3095
OE1
GLN
38
−14.701
26.373
52.601
1.00
24.71
B


3096
NE2
GLN
38
−14.350
27.608
54.384
1.00
23.66
B


3097
C
GLN
38
−18.013
27.191
50.566
1.00
29.33
B


3098
O
GLN
38
−18.363
26.188
51.189
1.00
28.34
B


3099
N
ALA
39
−18.862
27.896
49.808
1.00
30.07
B


3100
CA
ALA
39
−20.295
27.570
49.781
1.00
32.70
B


3101
CB
ALA
39
−21.051
28.568
48.896
1.00
33.57
B


3102
C
ALA
39
−20.549
26.146
49.335
1.00
30.85
B


3103
O
ALA
39
−21.575
25.584
49.736
1.00
33.70
B


3104
N
ASP
40
−19.654
25.458
48.632
1.00
30.62
B


3105
CA
ASP
40
−19.846
24.065
48.267
1.00
29.06
B


3106
CB
ASP
40
−19.346
23.872
46.817
1.00
32.72
B


3107
CG
ASP
40
−20.099
24.688
45.790
1.00
35.29
B


3108
OD1
ASP
40
−21.243
25.084
46.048
1.00
34.36
B


3109
OD2
ASP
40
−19.515
24.952
44.704
1.00
38.39
B


3110
C
ASP
40
−19.066
23.072
49.111
1.00
27.10
B


3111
O
ASP
40
−19.184
21.847
48.934
1.00
25.64
B


3112
N
TYR
41
−18.180
23.572
49.983
1.00
26.33
B


3113
CA
TYR
41
−17.195
22.686
50.602
1.00
25.45
B


3114
CB
TYR
41
−16.073
23.513
51.318
1.00
25.80
B


3115
CG
TYR
41
−14.950
22.533
51.647
1.00
26.69
B


3116
CD1
TYR
41
−14.085
22.167
50.613
1.00
26.77
B


3117
CD2
TYR
41
−14.762
21.968
52.905
1.00
26.47
B


3118
CE1
TYR
41
−13.046
21.271
50.818
1.00
28.14
B


3119
CE2
TYR
41
−13.722
21.066
53.108
1.00
27.32
B


3120
CZ
TYR
41
−12.866
20.718
52.081
1.00
29.44
B


3121
OH
TYR
41
−11.814
19.812
52.248
1.00
28.72
B


3122
C
TYR
41
−17.755
21.608
51.498
1.00
23.95
B


3123
O
TYR
41
−17.316
20.448
51.464
1.00
24.60
B


3124
N
ALA
42
−18.755
21.934
52.316
1.00
25.56
B


3125
CA
ALA
42
−19.353
20.914
53.201
1.00
25.76
B


3126
CB
ALA
42
−20.399
21.581
54.090
1.00
23.78
B


3127
C
ALA
42
−19.950
19.750
52.450
1.00
25.97
B


3128
O
ALA
42
−19.747
18.556
52.753
1.00
25.39
B


3129
N
ASP
43
−20.672
20.055
51.369
1.00
28.67
B


3130
CA
ASP
43
−21.195
18.932
50.555
1.00
30.08
B


3131
CB
ASP
43
−22.081
19.541
49.448
1.00
33.25
B


3132
CG
ASP
43
−23.443
19.995
49.962
1.00
34.98
B


3133
OD1
ASP
43
−23.930
19.541
51.007
1.00
33.60
B


3134
OD2
ASP
43
−24.052
20.858
49.282
1.00
37.96
B


3135
C
ASP
43
−20.077
18.126
49.912
1.00
28.64
B


3136
O
ASP
43
−20.097
16.901
49.768
1.00
27.36
B


3137
N
TYR
44
−19.069
18.830
49.357
1.00
28.91
B


3138
CA
TYR
44
−17.962
18.107
48.738
1.00
29.90
B


3139
CB
TYR
44
−16.920
19.101
48.198
1.00
32.45
B


3140
CG
TYR
44
−15.594
18.433
47.876
1.00
36.36
B


3141
CD1
TYR
44
−15.510
17.544
46.812
1.00
38.54
B


3142
CD2
TYR
44
−14.450
18.690
48.616
1.00
37.35
B


3143
CE1
TYR
44
−14.303
16.943
46.499
1.00
40.28
B


3144
CE2
TYR
44
−13.243
18.088
48.318
1.00
38.41
B


3145
CZ
TYR
44
−13.180
17.217
47.251
1.00
40.38
B


3146
OH
TYR
44
−12.000
16.594
46.922
1.00
41.35
B


3147
C
TYR
44
−17.309
17.225
49.814
1.00
29.19
B


3148
O
TYR
44
−17.130
16.030
49.643
1.00
28.55
B


3149
N
TYR
45
−17.041
17.861
50.971
1.00
27.03
B


3150
CA
TYR
45
−16.320
17.107
52.017
1.00
28.04
B


3151
CB
TYR
45
−15.961
18.141
53.101
1.00
25.24
B


3152
CG
TYR
45
−15.311
17.594
54.340
1.00
25.61
B


3153
CD1
TYR
45
−13.997
17.145
54.389
1.00
22.93
B


3154
CD2
TYR
45
−16.070
17.545
55.522
1.00
26.50
B


3155
CE1
TYR
45
−13.450
16.662
55.568
1.00
24.89
B


3156
CE2
TYR
45
−15.537
17.056
56.687
1.00
25.61
B


3157
CZ
TYR
45
−14.229
16.633
56.720
1.00
25.35
B


3158
OH
TYR
45
−13.730
16.155
57.908
1.00
23.72
B


3159
C
TYR
45
−17.099
15.943
52.584
1.00
27.22
B


3160
O
TYR
45
−16.593
14.809
52.694
1.00
30.23
B


3161
N
PHE
46
−18.371
16.127
52.930
1.00
27.26
B


3162
CA
PHE
46
−19.157
14.990
53.453
1.00
28.58
B


3163
CB
PHE
46
−20.503
15.493
53.995
1.00
27.85
B


3164
CG
PHE
46
−20.284
15.803
55.472
1.00
28.38
B


3165
CD1
PHE
46
−19.704
16.990
55.864
1.00
26.34
B


3166
CD2
PHE
46
−20.516
14.804
56.398
1.00
28.14
B


3167
CE1
PHE
46
−19.442
17.225
57.225
1.00
28.56
B


3168
CE2
PHE
46
−20.251
15.026
57.754
1.00
28.29
B


3169
CZ
PHE
46
−19.667
16.226
58.153
1.00
27.36
B


3170
C
PHE
46
−19.290
13.874
52.422
1.00
29.55
B


3171
O
PHE
46
−19.223
12.708
52.785
1.00
29.91
B


3172
N
ARG
47
−19.341
14.236
51.138
1.00
29.92
B


3173
CA
ARG
47
−19.427
13.212
50.087
1.00
29.82
B


3174
CB
ARG
47
−19.768
13.867
48.727
1.00
28.68
B


3175
CG
ARG
47
−19.805
12.878
47.555
1.00
31.40
B


3176
CD
ARG
47
−20.229
13.545
46.253
1.00
28.95
B


3177
NE
ARG
47
−19.376
14.627
45.753
1.00
27.46
B


3178
CZ
ARG
47
−18.239
14.330
45.107
1.00
26.32
B


3179
NH1
ARG
47
−17.870
13.079
44.917
1.00
26.37
B


3180
NH2
ARG
47
−17.457
15.269
44.656
1.00
27.46
B


3181
C
ARG
47
−18.103
12.488
49.936
1.00
27.74
B


3182
O
ARG
47
−18.094
11.272
50.065
1.00
26.68
B


3183
N
VAL
48
−16.999
13.213
49.690
1.00
27.28
B


3184
CA
VAL
48
−15.751
12.483
49.452
1.00
28.74
B


3185
CB
VAL
48
−14.552
13.314
48.955
1.00
31.08
B


3186
CG1
VAL
48
−14.846
13.784
47.514
1.00
33.19
B


3187
CG2
VAL
48
−14.201
14.486
49.857
1.00
29.64
B


3188
C
VAL
48
−15.314
11.665
50.651
1.00
28.98
B


3189
O
VAL
48
−14.649
10.649
50.437
1.00
27.72
B


3190
N
THR
49
−15.681
12.057
51.888
1.00
27.61
B


3191
CA
THR
49
−15.250
11.197
52.992
1.00
29.14
B


3192
CB
THR
49
−14.989
12.056
54.245
1.00
28.59
B


3193
OG1
THR
49
−16.199
12.664
54.686
1.00
26.82
B


3194
CG2
THR
49
−13.963
13.139
53.910
1.00
27.89
B


3195
C
THR
49
−16.256
10.105
53.263
1.00
32.25
B


3196
O
THR
49
−16.096
9.393
54.257
1.00
31.58
B


3197
N
LYS
50
−17.316
9.954
52.453
1.00
33.83
B


3198
CA
LYS
50
−18.345
8.930
52.695
1.00
34.87
B


3199
CB
LYS
50
−17.738
7.539
52.490
1.00
38.11
B


3200
CG
LYS
50
−17.129
7.347
51.099
1.00
40.70
B


3201
CD
LYS
50
−16.452
5.998
51.021
1.00
43.30
B


3202
CE
LYS
50
−15.934
5.688
49.621
1.00
45.65
B


3203
NZ
LYS
50
−15.174
4.391
49.724
1.00
47.82
B


3204
C
LYS
50
−18.992
9.033
54.076
1.00
34.08
B


3205
O
LYS
50
−19.219
8.064
54.802
1.00
32.77
B


3206
N
SER
51
−19.385
10.260
54.426
1.00
34.52
B


3207
CA
SER
51
−19.846
10.562
55.778
1.00
35.62
B


3208
CB
SER
51
−18.856
11.573
56.414
1.00
34.18
B


3209
OG
SER
51
−17.677
10.861
56.762
1.00
34.96
B


3210
C
SER
51
−21.228
11.171
55.798
1.00
35.96
B


3211
O
SER
51
−21.654
11.789
56.778
1.00
35.28
B


3212
N
GLU
52
−21.971
10.990
54.709
1.00
38.89
B


3213
CA
GLU
52
−23.324
11.491
54.550
1.00
40.11
B


3214
CB
GLU
52
−23.888
11.133
53.179
1.00
42.33
B


3215
CG
GLU
52
−23.062
11.610
51.985
1.00
44.09
B


3216
CD
GLU
52
−23.205
13.088
51.724
1.00
44.87
B


3217
OE1
GLU
52
−23.541
13.849
52.668
1.00
46.28
B


3218
OE2
GLU
52
−22.968
13.566
50.594
1.00
45.42
B


3219
C
GLU
52
−24.241
11.004
55.662
1.00
40.31
B


3220
O
GLU
52
−25.200
11.724
55.960
1.00
40.09
B


3221
N
HIS
53
−23.973
9.890
56.338
1.00
40.63
B


3222
CA
HIS
53
−24.778
9.462
57.468
1.00
43.33
B


3223
ND1
HIS
53
−22.007
7.845
57.264
1.00
48.85
B


3224
CG
HIS
53
−23.034
7.812
58.209
1.00
48.87
B


3225
CB
HIS
53
−24.475
8.000
57.818
1.00
45.61
B


3226
NE2
HIS
53
−21.114
7.488
59.199
1.00
49.66
B


3227
CD2
HIS
53
−22.472
7.597
59.426
1.00
48.98
B


3228
CE1
HIS
53
−20.866
7.646
57.906
1.00
49.30
B


3229
C
HIS
53
−24.600
10.323
58.714
1.00
42.97
B


3230
O
HIS
53
−25.449
10.299
59.615
1.00
40.95
B


3231
N
MET
54
−23.592
11.193
58.787
1.00
42.06
B


3232
CA
MET
54
−23.458
12.143
59.895
1.00
40.37
B


3233
CB
MET
54
−21.976
12.374
60.166
1.00
39.25
B


3234
CG
MET
54
−21.129
11.124
60.065
1.00
39.07
B


3235
SD
MET
54
−19.432
11.463
60.564
1.00
39.03
B


3236
CE
MET
54
−18.719
9.834
60.604
1.00
35.38
B


3237
C
MET
54
−24.133
13.462
59.580
1.00
40.50
B


3238
O
MET
54
−23.466
14.491
59.412
1.00
39.96
B


3239
N
VAL
55
−25.469
13.469
59.515
1.00
40.70
B


3240
CA
VAL
55
−26.225
14.645
59.127
1.00
41.24
B


3241
CB
VAL
55
−27.725
14.281
58.965
1.00
42.54
B


3242
CG1
VAL
55
−28.247
13.754
60.298
1.00
43.06
B


3243
CG2
VAL
55
−28.566
15.460
58.510
1.00
41.18
B


3244
C
VAL
55
−26.083
15.834
60.050
1.00
41.69
B


3245
O
VAL
55
−26.072
16.971
59.552
1.00
41.62
B


3246
N
ASP
56
−26.044
15.625
61.365
1.00
41.89
B


3247
CA
ASP
56
−25.971
16.772
62.276
1.00
42.82
B


3248
CB
ASP
56
−26.318
16.428
63.725
1.00
43.88
B


3249
CG
ASP
56
−27.747
15.911
63.870
1.00
47.81
B


3250
OD1
ASP
56
−27.958
14.828
64.467
1.00
48.73
B


3251
OD2
ASP
56
−28.711
16.529
63.373
1.00
48.34
B


3252
C
ASP
56
−24.580
17.408
62.166
1.00
39.80
B


3253
O
ASP
56
−24.486
18.615
62.022
1.00
39.83
B


3254
N
LEU
57
−23.543
16.580
62.126
1.00
38.46
B


3255
CA
LEU
57
−22.168
17.052
61.960
1.00
36.70
B


3256
CB
LEU
57
−21.208
15.880
62.088
1.00
37.93
B


3257
CG
LEU
57
−19.852
16.167
62.727
1.00
39.44
B


3258
CD2
LEU
57
−18.891
15.025
62.463
1.00
39.45
B


3259
CD1
LEU
57
−20.011
16.406
64.231
1.00
39.49
B


3260
C
LEU
57
−21.963
17.783
60.639
1.00
33.97
B


3261
O
LEU
57
−21.405
18.892
60.616
1.00
31.33
B


3262
N
LYS
58
−22.726
17.365
59.613
1.00
33.24
B


3263
CA
LYS
58
−22.690
18.074
58.335
1.00
31.91
B


3264
CB
LYS
58
−23.447
17.288
57.253
1.00
35.05
B


3265
CG
LYS
58
−23.342
17.963
55.885
1.00
35.27
B


3266
CD
LYS
58
−23.785
17.004
54.788
1.00
36.99
B


3267
CE
LYS
58
−24.081
17.788
53.522
1.00
38.02
B


3268
NZ
LYS
58
−24.138
16.923
52.309
1.00
38.14
B


3269
C
LYS
58
−23.278
19.454
58.476
1.00
31.37
B


3270
O
LYS
58
−22.764
20.468
57.989
1.00
29.09
B


3271
N
GLU
59
−24.409
19.515
59.214
1.00
31.49
B


3272
CA
GLU
59
−25.049
20.784
59.484
1.00
31.48
B


3273
CB
GLU
59
−26.360
20.582
60.291
1.00
35.68
B


3274
CG
GLU
59
−27.406
19.802
59.503
1.00
38.94
B


3275
CD
GLU
59
−28.727
19.621
60.251
1.00
42.98
B


3276
OE1
GLU
59
−29.707
19.210
59.577
1.00
42.91
B


3277
OE2
GLU
59
−28.801
19.894
61.476
1.00
42.63
B


3278
C
GLU
59
−24.105
21.696
60.260
1.00
30.72
B


3279
O
GLU
59
−23.912
22.872
59.932
1.00
32.00
B


3280
N
LYS
60
−23.491
21.165
61.306
1.00
30.16
B


3281
CA
LYS
60
−22.491
21.947
62.046
1.00
30.01
B


3282
CB
LYS
60
−21.904
21.105
63.180
1.00
29.34
B


3283
CG
LYS
60
−20.962
21.874
64.113
1.00
32.39
B


3284
CD
LYS
60
−20.162
20.902
64.990
1.00
32.26
B


3285
CE
LYS
60
−19.334
21.694
66.003
1.00
32.30
B


3286
NZ
LYS
60
−20.240
22.234
67.082
1.00
33.44
B


3287
C
LYS
60
−21.401
22.411
61.071
1.00
28.68
B


3288
O
LYS
60
−21.051
23.593
61.041
1.00
28.77
B


3289
N
PHE
61
−20.857
21.511
60.248
1.00
28.77
B


3290
CA
PHE
61
−19.768
21.971
59.340
1.00
27.65
B


3291
CB
PHE
61
−19.149
20.737
58.667
1.00
28.31
B


3292
CG
PHE
61
−17.881
21.034
57.904
1.00
26.08
B


3293
CD1
PHE
61
−16.802
21.661
58.507
1.00
25.71
B


3294
CD2
PHE
61
−17.803
20.688
56.559
1.00
26.70
B


3295
CE1
PHE
61
−15.652
21.924
57.767
1.00
26.72
B


3296
CE2
PHE
61
−16.640
20.942
55.817
1.00
26.65
B


3297
CZ
PHE
61
−15.557
21.547
56.438
1.00
26.34
B


3298
C
PHE
61
−20.246
23.020
58.376
1.00
28.42
B


3299
O
PHE
61
−19.525
23.965
58.031
1.00
29.26
B


3300
N
LYS
62
−21.524
22.978
57.941
1.00
30.24
B


3301
CA
LYS
62
−22.085
24.038
57.103
1.00
30.16
B


3302
CB
LYS
62
−23.503
23.658
56.642
1.00
33.40
B


3303
CG
LYS
62
−23.487
22.673
55.470
1.00
37.25
B


3304
CD
LYS
62
−24.767
22.671
54.634
1.00
40.54
B


3305
CE
LYS
62
−24.615
21.717
53.443
1.00
42.98
B


3306
NZ
LYS
62
−25.897
21.037
53.065
1.00
44.54
B


3307
C
LYS
62
−22.072
25.367
57.817
1.00
29.01
B


3308
O
LYS
62
−21.648
26.436
57.326
1.00
27.79
B


3309
N
ARG
63
−22.452
25.314
59.097
1.00
28.86
B


3310
CA
ARG
63
−22.337
26.528
59.927
1.00
27.90
B


3311
CB
ARG
63
−22.897
26.276
61.337
1.00
29.43
B


3312
CG
ARG
63
−24.422
26.185
61.444
1.00
31.90
B


3313
CD
ARG
63
−24.926
26.273
62.879
1.00
30.70
B


3314
NE
ARG
63
−24.460
25.182
63.711
1.00
32.36
B


3315
CZ
ARG
63
−24.895
23.936
63.817
1.00
33.89
B


3316
NH1
ARG
63
−25.922
23.479
63.102
1.00
34.24
B


3317
NH2
ARG
63
−24.339
23.077
64.678
1.00
32.87
B


3318
C
ARG
63
−20.884
26.992
60.005
1.00
27.06
B


3319
O
ARG
63
−20.596
28.194
59.911
1.00
26.93
B


3320
N
ILE
64
−19.951
26.093
60.300
1.00
26.97
B


3321
CA
ILE
64
−18.535
26.513
60.439
1.00
26.26
B


3322
CB
ILE
64
−17.663
25.318
60.850
1.00
26.23
B


3323
CG2
ILE
64
−16.163
25.617
60.649
1.00
26.15
B


3324
CG1
ILE
64
−17.861
24.910
62.322
1.00
23.46
B


3325
CD1
ILE
64
−17.695
23.413
62.551
1.00
24.95
B


3326
C
ILE
64
−18.036
27.210
59.168
1.00
26.51
B


3327
O
ILE
64
−17.593
28.372
59.180
1.00
24.26
B


3328
N
CYS
65
−18.293
26.615
57.993
1.00
27.01
B


3329
CA
CYS
65
−17.876
27.214
56.701
1.00
27.04
B


3330
CB
CYS
65
−18.262
26.250
55.579
1.00
25.72
B


3331
SG
CYS
65
−17.351
24.706
55.530
1.00
25.28
B


3332
C
CYS
65
−18.406
28.602
56.422
1.00
29.22
B


3333
O
CYS
65
−17.714
29.576
56.015
1.00
29.00
B


3334
N
GLU
66
−19.687
28.816
56.728
1.00
31.33
B


3335
CA
GLU
66
−20.340
30.110
56.626
1.00
33.56
B


3336
CB
GLU
66
−21.838
29.998
56.951
1.00
38.70
B


3337
CG
GLU
66
−22.626
31.310
56.818
1.00
44.46
B


3338
CD
GLU
66
−22.492
32.285
58.008
1.00
48.62
B


3339
OE1
GLU
66
−22.430
31.859
59.224
1.00
50.47
B


3340
OE2
GLU
66
−22.447
33.556
57.778
1.00
51.14
B


3341
C
GLU
66
−19.693
31.168
57.526
1.00
31.74
B


3342
O
GLU
66
−19.672
32.358
57.200
1.00
32.67
B


3343
N
LYS
67
−19.155
30.746
58.648
1.00
31.14
B


3344
CA
LYS
67
−18.549
31.692
59.602
1.00
28.65
B


3345
CB
LYS
67
−18.497
31.085
61.002
1.00
29.43
B


3346
CG
LYS
67
−19.869
30.994
61.664
1.00
29.62
B


3347
CD
LYS
67
−20.304
32.306
62.313
1.00
30.86
B


3348
CE
LYS
67
−21.584
32.167
63.134
1.00
30.74
B


3349
NZ
LYS
67
−22.186
33.465
63.467
1.00
32.87
B


3350
C
LYS
67
−17.101
32.068
59.231
1.00
27.59
B


3351
O
LYS
67
−16.571
33.089
59.681
1.00
25.43
B


3352
N
THR
68
−16.463
31.256
58.407
1.00
26.27
B


3353
CA
THR
68
−15.030
31.461
58.081
1.00
24.43
B


3354
CB
THR
68
−14.459
30.287
57.286
1.00
26.33
B


3355
OG1
THR
68
−15.189
30.094
56.086
1.00
27.29
B


3356
CG2
THR
68
−14.489
28.974
58.066
1.00
25.30
B


3357
C
THR
68
−14.739
32.730
57.259
1.00
23.11
B


3358
O
THR
68
−13.604
33.223
57.234
1.00
21.42
B


3359
N
ALA
69
−15.738
33.258
56.590
1.00
20.18
B


3360
CA
ALA
69
−15.548
34.442
55.727
1.00
18.52
B


3361
CB
ALA
69
−15.085
35.649
56.546
1.00
19.83
B


3362
C
ALA
69
−14.500
34.146
54.642
1.00
18.65
B


3363
O
ALA
69
−13.726
35.027
54.240
1.00
20.80
B


3364
N
ILE
70
−14.509
32.897
54.212
1.00
18.29
B


3365
CA
ILE
70
−13.647
32.403
53.123
1.00
21.02
B


3366
CB
ILE
70
−12.964
31.092
53.536
1.00
18.84
B


3367
CG2
ILE
70
−12.215
30.419
52.383
1.00
20.42
B


3368
CG1
ILE
70
−11.932
31.266
54.651
1.00
15.48
B


3369
CD1
ILE
70
−11.397
29.933
55.184
1.00
11.80
B


3370
C
ILE
70
−14.539
32.136
51.911
1.00
22.83
B


3371
O
ILE
70
−15.544
31.424
52.006
1.00
22.84
B


3372
N
LYS
71
−14.185
32.709
50.776
1.00
25.05
B


3373
CA
LYS
71
−15.000
32.535
49.558
1.00
28.31
B


3374
CB
LYS
71
−14.842
33.714
48.602
1.00
31.87
B


3375
CG
LYS
71
−15.875
33.684
47.469
1.00
36.10
B


3376
CD
LYS
71
−16.151
35.062
46.870
1.00
39.24
B


3377
CE
LYS
71
−15.029
35.543
45.950
1.00
41.09
B


3378
NZ
LYS
71
−15.126
36.972
45.626
1.00
43.39
B


3379
C
LYS
71
−14.614
31.257
48.805
1.00
27.83
B


3380
O
LYS
71
−15.477
30.508
48.329
1.00
29.51
B


3381
N
LYS
72
−13.321
31.026
48.703
1.00
27.04
B


3382
CA
LYS
72
−12.797
29.846
47.997
1.00
25.00
B


3383
CB
LYS
72
−12.757
30.116
46.492
1.00
25.89
B


3384
CG
LYS
72
−11.981
31.385
46.138
1.00
27.61
B


3385
CD
LYS
72
−12.203
31.838
44.695
1.00
28.83
B


3386
CE
LYS
72
−10.904
32.213
43.980
1.00
31.01
B


3387
NZ
LYS
72
−10.114
33.213
44.712
1.00
27.64
B


3388
C
LYS
72
−11.383
29.522
48.473
1.00
22.26
B


3389
O
LYS
72
−10.731
30.351
49.122
1.00
20.01
B


3390
N
ARG
73
−10.968
28.315
48.123
1.00
21.60
B


3391
CA
ARG
73
−9.637
27.786
48.463
1.00
22.36
B


3392
CB
ARG
73
−9.707
26.935
49.737
1.00
22.83
B


3393
CG
ARG
73
−9.954
27.764
50.996
1.00
22.90
B


3394
CD
ARG
73
−10.971
27.134
51.947
1.00
24.84
B


3395
NE
ARG
73
−10.648
25.750
52.247
1.00
21.88
B


3396
CZ
ARG
73
−11.387
24.791
52.828
1.00
24.18
B


3397
NH1
ARG
73
−12.644
24.923
53.218
1.00
23.73
B


3398
NH2
ARG
73
−10.817
23.640
53.204
1.00
21.04
B


3399
C
ARG
73
−9.117
26.879
47.346
1.00
23.89
B


3400
O
ARG
73
−9.870
26.102
46.748
1.00
22.54
B


3401
N
TYR
74
−7.830
27.005
47.084
1.00
21.64
B


3402
CA
TYR
74
−7.151
26.146
46.106
1.00
20.49
B


3403
CB
TYR
74
−6.076
26.933
45.369
1.00
20.77
B


3404
CG
TYR
74
−6.654
28.117
44.605
1.00
23.34
B


3405
CD1
TYR
74
−6.728
29.367
45.222
1.00
22.80
B


3406
CD2
TYR
74
−7.113
27.946
43.295
1.00
22.88
B


3407
CE1
TYR
74
−7.254
30.455
44.526
1.00
23.26
B


3408
CE2
TYR
74
−7.637
29.036
42.597
1.00
24.52
B


3409
CZ
TYR
74
−7.706
30.290
43.212
1.00
23.93
B


3410
OH
TYR
74
−8.212
31.351
42.531
1.00
28.25
B


3411
C
TYR
74
−6.548
24.980
46.876
1.00
19.76
B


3412
O
TYR
74
−5.942
25.162
47.940
1.00
19.96
B


3413
N
LEU
75
−6.730
23.797
46.339
1.00
17.38
B


3414
CA
LEU
75
−6.272
22.579
47.011
1.00
21.26
B


3415
CB
LEU
75
−7.476
21.856
47.611
1.00
20.25
B


3416
CG
LEU
75
−8.226
22.703
48.637
1.00
22.33
B


3417
CD2
LEU
75
−7.463
22.831
49.956
1.00
23.14
B


3418
CD1
LEU
75
−9.599
22.132
48.991
1.00
22.43
B


3419
C
LEU
75
−5.587
21.627
46.043
1.00
21.70
B


3420
O
LEU
75
−6.103
21.328
44.962
1.00
23.22
B


3421
N
ALA
76
−4.429
21.157
46.464
1.00
22.49
B


3422
CA
ALA
76
−3.651
20.202
45.670
1.00
21.99
B


3423
CB
ALA
76
−2.206
20.162
46.154
1.00
21.36
B


3424
C
ALA
76
−4.281
18.802
45.783
1.00
23.24
B


3425
O
ALA
76
−4.180
17.985
44.864
1.00
22.78
B


3426
N
LEU
77
−4.914
18.554
46.929
1.00
20.26
B


3427
CA
LEU
77
−5.626
17.275
47.211
1.00
21.63
B


3428
CB
LEU
77
−6.206
17.309
48.634
1.00
21.08
B


3429
CG
LEU
77
−6.036
16.032
49.475
1.00
24.27
B


3430
CD2
LEU
77
−6.094
14.731
48.678
1.00
22.09
B


3431
CD1
LEU
77
−7.115
15.900
50.566
1.00
21.69
B


3432
C
LEU
77
−6.836
17.157
46.285
1.00
19.11
B


3433
O
LEU
77
−7.734
18.003
46.317
1.00
18.26
B


3434
N
THR
78
−6.864
16.120
45.480
1.00
21.33
B


3435
CA
THR
78
−7.988
15.904
44.551
1.00
21.80
B


3436
CB
THR
78
−7.474
15.584
43.151
1.00
20.95
B


3437
OG1
THR
78
−6.745
14.365
43.168
1.00
20.65
B


3438
CG2
THR
78
−6.546
16.664
42.592
1.00
20.30
B


3439
C
THR
78
−8.826
14.713
45.004
1.00
21.99
B


3440
O
THR
78
−8.404
13.919
45.855
1.00
17.00
B


3441
N
GLU
79
−9.997
14.621
44.412
1.00
22.12
B


3442
CA
GLU
79
−10.936
13.534
44.694
1.00
22.76
B


3443
CB
GLU
79
−12.213
13.714
43.881
1.00
24.76
B


3444
CG
GLU
79
−13.136
14.782
44.455
1.00
31.51
B


3445
CD
GLU
79
−14.507
14.796
43.788
1.00
30.88
B


3446
OE1
GLU
79
−15.170
13.698
43.658
1.00
30.99
B


3447
OE2
GLU
79
−14.999
15.906
43.357
1.00
36.51
B


3448
C
GLU
79
−10.315
12.197
44.303
1.00
21.27
B


3449
O
GLU
79
−10.510
11.178
44.977
1.00
21.71
B


3450
N
ASP
80
−9.576
12.243
43.213
1.00
20.55
B


3451
CA
ASP
80
−8.928
11.052
42.659
1.00
21.74
B


3452
CB
ASP
80
−8.315
11.365
41.300
1.00
26.25
B


3453
CG
ASP
80
−9.287
11.078
40.154
1.00
30.13
B


3454
OD1
ASP
80
−10.537
10.879
40.408
1.00
31.09
B


3455
OD2
ASP
80
−8.861
11.036
38.939
1.00
31.25
B


3456
C
ASP
80
−7.849
10.525
43.607
1.00
20.12
B


3457
O
ASP
80
−7.704
9.314
43.808
1.00
20.55
B


3458
N
TYR
81
−7.084
11.423
44.198
1.00
19.89
B


3459
CA
TYR
81
−6.031
10.988
45.123
1.00
18.16
B


3460
CB
TYR
81
−5.151
12.153
45.578
1.00
18.76
B


3461
CG
TYR
81
−3.806
11.662
46.131
1.00
17.78
B


3462
CD1
TYR
81
−2.817
11.184
45.258
1.00
17.92
B


3463
CD2
TYR
81
−3.565
11.678
47.511
1.00
20.47
B


3464
CE1
TYR
81
−1.597
10.717
45.766
1.00
20.28
B


3465
CE2
TYR
81
−2.347
11.208
48.018
1.00
17.69
B


3466
CZ
TYR
81
−1.363
10.726
47.146
1.00
19.66
B


3467
OH
TYR
81
−0.182
10.265
47.640
1.00
17.94
B


3468
C
TYR
81
−6.663
10.316
46.349
1.00
16.11
B


3469
O
TYR
81
−6.168
9.296
46.846
1.00
19.25
B


3470
N
LEU
82
−7.761
10.898
46.809
1.00
18.19
B


3471
CA
LEU
82
−8.492
10.389
47.987
1.00
21.62
B


3472
CB
LEU
82
−9.627
11.340
48.368
1.00
21.73
B


3473
CG
LEU
82
−9.140
12.596
49.100
1.00
23.08
B


3474
CD2
LEU
82
−8.426
12.291
50.419
1.00
20.64
B


3475
CD1
LEU
82
−10.277
13.555
49.459
1.00
22.06
B


3476
C
LEU
82
−9.086
9.002
47.699
1.00
24.53
B


3477
O
LEU
82
−9.129
8.125
48.571
1.00
23.60
B


3478
N
GLN
83
−9.542
8.823
46.473
1.00
24.67
B


3479
CA
GLN
83
−10.128
7.545
46.045
1.00
25.38
B


3480
CB
GLN
83
−10.772
7.691
44.664
1.00
30.84
B


3481
CG
GLN
83
−11.992
8.615
44.677
1.00
36.26
B


3482
CD
GLN
83
−12.652
8.778
43.305
1.00
41.57
B


3483
OE1
GLN
83
−12.031
8.495
42.282
1.00
42.90
B


3484
NE2
GLN
83
−13.892
9.228
43.219
1.00
40.48
B


3485
C
GLN
83
−9.036
6.473
45.993
1.00
22.06
B


3486
O
GLN
83
−9.267
5.303
46.314
1.00
19.52
B


3487
N
GLU
84
−7.856
6.909
45.591
1.00
22.33
B


3488
CA
GLU
84
−6.691
6.020
45.457
1.00
24.13
B


3489
CB
GLU
84
−5.659
6.654
44.508
1.00
29.31
B


3490
CG
GLU
84
−6.195
6.801
43.076
1.00
32.81
B


3491
CD
GLU
84
−5.261
7.533
42.093
1.00
36.95
B


3492
OE1
GLU
84
−4.152
8.052
42.493
1.00
39.75
B


3493
OE2
GLU
84
−5.591
7.629
40.844
1.00
37.73
B


3494
C
GLU
84
−6.045
5.757
46.832
1.00
23.11
B


3495
O
GLU
84
−5.334
4.766
47.030
1.00
22.74
B


3496
N
ASN
85
−6.305
6.653
47.764
1.00
20.46
B


3497
CA
ASN
85
−5.740
6.574
49.127
1.00
22.14
B


3498
CB
ASN
85
−4.637
7.635
49.246
1.00
22.52
B


3499
CG
ASN
85
−3.539
7.471
48.183
1.00
24.04
B


3500
OD1
ASN
85
−2.645
6.642
48.353
1.00
26.52
B


3501
ND2
ASN
85
−3.552
8.211
47.087
1.00
20.49
B


3502
C
ASN
85
−6.871
6.812
50.134
1.00
19.09
B


3503
O
ASN
85
−6.929
7.869
50.779
1.00
22.00
B


3504
N
PRO
86
−7.777
5.823
50.317
1.00
20.37
B


3505
CA
PRO
86
−9.004
5.986
51.119
1.00
22.52
B


3506
CD
PRO
86
−7.621
4.488
49.726
1.00
22.90
B


3507
CB
PRO
86
−9.684
4.645
51.046
1.00
22.61
B


3508
CG
PRO
86
−8.809
3.721
50.223
1.00
23.46
B


3509
C
PRO
86
−8.753
6.261
52.570
1.00
24.83
B


3510
O
PRO
86
−9.589
6.949
53.233
1.00
27.06
B


3511
N
THR
87
−7.676
5.711
53.003
1.00
24.46
B


3512
CA
THR
87
−7.224
5.756
54.379
1.00
26.64
B


3513
CB
THR
87
−5.949
4.918
54.348
1.00
28.38
B


3514
OG1
THR
87
−6.082
3.795
55.204
1.00
29.91
B


3515
CG2
THR
87
−4.696
5.683
54.699
1.00
20.93
B


3516
C
THR
87
−7.125
7.240
54.852
1.00
25.88
B


3517
O
THR
87
−7.262
7.564
56.044
1.00
25.42
B


3518
N
MET
88
−6.920
8.147
53.905
1.00
25.14
B


3519
CA
MET
88
−6.837
9.592
54.201
1.00
24.00
B


3520
CB
MET
88
−6.437
10.384
52.951
1.00
23.65
B


3521
CG
MET
88
−4.962
10.208
52.585
1.00
21.30
B


3522
SD
MET
88
−4.397
11.362
51.354
1.00
22.70
B


3523
CE
MET
88
−4.716
13.026
51.897
1.00
14.99
B


3524
C
MET
88
−8.197
10.131
54.692
1.00
26.77
B


3525
O
MET
88
−8.272
11.161
55.368
1.00
24.35
B


3526
N
CYS
89
−9.275
9.430
54.355
1.00
28.86
B


3527
CA
CYS
89
−10.634
9.881
54.742
1.00
33.14
B


3528
CB
CYS
89
−11.652
9.565
53.651
1.00
33.44
B


3529
SG
CYS
89
−11.320
10.475
52.067
1.00
33.88
B


3530
C
CYS
89
−11.138
9.210
56.035
1.00
36.39
B


3531
O
CYS
89
−12.164
9.609
56.602
1.00
36.77
B


3532
N
GLU
90
−10.429
8.193
56.493
1.00
37.83
B


3533
CA
GLU
90
−10.822
7.464
57.722
1.00
39.76
B


3534
CB
GLU
90
−10.530
5.976
57.586
1.00
41.89
B


3535
CG
GLU
90
−10.914
5.423
56.221
1.00
47.23
B


3536
CD
GLU
90
−10.194
4.122
55.885
1.00
49.56
B


3537
OE1
GLU
90
−9.423
3.567
56.757
1.00
50.81
B


3538
OE2
GLU
90
−10.364
3.581
54.730
1.00
52.36
B


3539
C
GLU
90
−10.044
7.989
58.919
1.00
39.25
B


3540
O
GLU
90
−8.825
7.797
59.023
1.00
36.90
B


3541
N
PHE
91
−10.773
8.627
59.803
1.00
39.48
B


3542
CA
PHE
91
−10.181
9.247
60.980
1.00
41.22
B


3543
CB
PHE
91
−11.257
9.705
61.962
1.00
41.26
B


3544
CG
PHE
91
−10.731
10.830
62.846
1.00
41.77
B


3545
CD1
PHE
91
−10.719
12.152
62.378
1.00
41.67
B


3546
CD2
PHE
91
−10.241
10.529
64.114
1.00
41.52
B


3547
CE1
PHE
91
−10.197
13.171
63.185
1.00
42.64
B


3548
CE2
PHE
91
−9.712
11.544
64.918
1.00
41.82
B


3549
CZ
PHE
91
−9.689
12.865
64.454
1.00
43.06
B


3550
C
PHE
91
−9.181
8.298
61.674
1.00
40.11
B


3551
O
PHE
91
−9.541
7.203
62.137
1.00
38.76
B


3552
N
MET
92
−7.964
8.810
61.669
1.00
40.90
B


3553
CA
MET
92
−6.756
8.240
62.298
1.00
42.30
B


3554
CB
MET
92
−6.922
8.184
63.809
1.00
45.50
B


3555
CG
MET
92
−6.813
9.574
64.455
1.00
48.55
B


3556
SD
MET
92
−5.374
10.491
63.932
1.00
52.06
B


3557
CE
MET
92
−5.856
11.803
62.829
1.00
50.56
B


3558
C
MET
92
−6.344
6.844
61.774
1.00
39.48
B


3559
O
MET
92
−5.652
6.078
62.462
1.00
38.76
B


3560
N
ALA
93
−6.751
6.502
60.566
1.00
33.86
B


3561
CA
ALA
93
−6.259
5.267
59.929
1.00
28.92
B


3562
CB
ALA
93
−7.151
4.893
58.740
1.00
28.58
B


3563
C
ALA
93
−4.829
5.597
59.482
1.00
24.00
B


3564
O
ALA
93
−4.475
6.779
59.352
1.00
24.33
B


3565
N
PRO
94
−3.913
4.649
59.222
1.00
23.16
B


3566
CA
PRO
94
−2.555
5.007
58.805
1.00
24.97
B


3567
CD
PRO
94
−4.177
3.214
59.313
1.00
24.94
B


3568
CB
PRO
94
−1.853
3.683
58.656
1.00
24.03
B


3569
CG
PRO
94
−2.870
2.587
58.921
1.00
25.46
B


3570
C
PRO
94
−2.618
5.644
57.448
1.00
23.80
B


3571
O
PRO
94
−3.178
5.014
56.508
1.00
22.80
B


3572
N
SER
95
−2.070
6.836
57.278
1.00
20.76
B


3573
CA
SER
95
−2.154
7.500
55.953
1.00
21.62
B


3574
CB
SER
95
−3.448
8.307
55.863
1.00
19.16
B


3575
OG
SER
95
−3.519
9.222
56.949
1.00
22.28
B


3576
C
SER
95
−0.995
8.481
55.709
1.00
20.95
B


3577
O
SER
95
−1.043
9.263
54.758
1.00
16.39
B


3578
N
LEU
96
−0.046
8.552
56.654
1.00
17.56
B


3579
CA
LEU
96
1.080
9.424
56.446
1.00
17.73
B


3580
CB
LEU
96
2.103
9.253
57.589
1.00
16.08
B


3581
CG
LEU
96
3.280
10.249
57.467
1.00
17.92
B


3582
CD2
LEU
96
4.268
9.936
58.606
1.00
18.52
B


3583
CD1
LEU
96
2.838
11.689
57.558
1.00
17.61
B


3584
C
LEU
96
1.813
9.125
55.113
1.00
16.99
B


3585
O
LEU
96
2.327
10.088
54.586
1.00
16.66
B


3586
N
ASN
97
2.105
7.878
54.759
1.00
18.09
B


3587
CA
ASN
97
2.853
7.600
53.537
1.00
18.88
B


3588
CB
ASN
97
3.082
6.088
53.331
1.00
18.39
B


3589
CG
ASN
97
3.946
5.496
54.431
1.00
19.50
B


3590
OD1
ASN
97
4.562
6.212
55.213
1.00
18.63
B


3591
ND2
ASN
97
4.066
4.178
54.433
1.00
19.87
B


3592
C
ASN
97
2.176
8.190
52.295
1.00
18.30
B


3593
O
ASN
97
2.882
8.871
51.540
1.00
17.58
B


3594
N
ALA
98
0.878
8.102
52.167
1.00
19.70
B


3595
CA
ALA
98
0.097
8.722
51.085
1.00
20.62
B


3596
CB
ALA
98
−1.383
8.349
51.171
1.00
18.93
B


3597
C
ALA
98
0.178
10.236
51.134
1.00
20.78
B


3598
O
ALA
98
0.296
10.916
50.093
1.00
18.66
B


3599
N
ARG
99
0.082
10.825
52.357
1.00
16.74
B


3600
CA
ARG
99
0.260
12.255
52.446
1.00
16.82
B


3601
CB
ARG
99
0.044
12.787
53.895
1.00
16.52
B


3602
CG
ARG
99
−1.419
12.583
54.302
1.00
20.92
B


3603
CD
ARG
99
−1.621
12.631
55.803
1.00
19.06
B


3604
NE
ARG
99
−2.864
12.011
56.311
1.00
19.61
B


3605
CZ
ARG
99
−3.997
12.693
56.318
1.00
18.62
B


3606
NH1
ARG
99
−4.087
13.931
55.823
1.00
18.56
B


3607
NH2
ARG
99
−5.079
12.123
56.851
1.00
22.65
B


3608
C
ARG
99
1.647
12.710
51.977
1.00
16.01
B


3609
O
ARG
99
1.754
13.711
51.284
1.00
15.15
B


3610
N
GLN
100
2.689
12.074
52.483
1.00
15.37
B


3611
CA
GLN
100
4.052
12.421
52.139
1.00
16.70
B


3612
CB
GLN
100
4.998
11.468
52.858
1.00
15.63
B


3613
CG
GLN
100
5.091
11.699
54.391
1.00
16.85
B


3614
CD
GLN
100
6.155
12.731
54.679
1.00
14.79
B


3615
OE1
GLN
100
7.229
12.413
55.226
1.00
19.37
B


3616
NE2
GLN
100
5.894
13.950
54.297
1.00
13.40
B


3617
C
GLN
100
4.259
12.246
50.616
1.00
19.58
B


3618
O
GLN
100
4.960
13.028
49.977
1.00
19.18
B


3619
N
ASP
101
3.674
11.182
50.061
1.00
19.09
B


3620
CA
ASP
101
3.804
10.974
48.619
1.00
23.21
B


3621
CB
ASP
101
3.140
9.653
48.219
1.00
21.63
B


3622
CG
ASP
101
4.041
8.544
48.692
1.00
23.42
B


3623
OD1
ASP
101
5.237
8.713
49.026
1.00
23.05
B


3624
OD2
ASP
101
3.570
7.417
48.716
1.00
25.55
B


3625
C
ASP
101
3.272
12.181
47.866
1.00
23.52
B


3626
O
ASP
101
3.964
12.531
46.902
1.00
27.58
B


3627
N
LEU
102
2.221
12.858
48.283
1.00
21.41
B


3628
CA
LEU
102
1.773
14.076
47.645
1.00
21.13
B


3629
CB
LEU
102
0.365
14.429
48.148
1.00
22.49
B


3630
CG
LEU
102
−0.719
14.969
47.244
1.00
25.86
B


3631
CD2
LEU
102
−0.230
15.575
45.936
1.00
22.99
B


3632
CD1
LEU
102
−1.777
15.837
47.887
1.00
23.24
B


3633
C
LEU
102
2.661
15.269
47.949
1.00
18.50
B


3634
O
LEU
102
3.124
16.027
47.084
1.00
15.10
B


3635
N
VAL
103
2.771
15.633
49.228
1.00
16.27
B


3636
CA
VAL
103
3.469
16.877
49.594
1.00
15.16
B


3637
CB
VAL
103
3.174
17.330
51.057
1.00
16.22
B


3638
CG1
VAL
103
1.664
17.503
51.115
1.00
16.14
B


3639
CG2
VAL
103
3.685
16.265
52.039
1.00
17.61
B


3640
C
VAL
103
4.969
16.889
49.413
1.00
14.13
B


3641
O
VAL
103
5.475
18.019
49.242
1.00
16.57
B


3642
N
VAL
104
5.700
15.810
49.419
1.00
13.95
B


3643
CA
VAL
104
7.159
15.836
49.257
1.00
15.98
B


3644
CB
VAL
104
7.781
14.480
49.613
1.00
18.18
B


3645
CG1
VAL
104
9.208
14.278
49.122
1.00
18.90
B


3646
CG2
VAL
104
7.778
14.409
51.183
1.00
17.37
B


3647
C
VAL
104
7.551
16.307
47.837
1.00
18.14
B


3648
O
VAL
104
8.523
17.070
47.718
1.00
16.71
B


3649
N
THR
105
6.710
16.024
46.847
1.00
14.70
B


3650
CA
THR
105
7.037
16.606
45.508
1.00
18.73
B


3651
CB
THR
105
6.757
15.551
44.420
1.00
20.56
B


3652
OG1
THR
105
5.379
15.258
44.561
1.00
22.45
B


3653
CG2
THR
105
7.455
14.225
44.640
1.00
18.83
B


3654
C
THR
105
6.171
17.837
45.343
1.00
16.87
B


3655
O
THR
105
6.590
18.911
44.917
1.00
15.67
B


3656
N
GLY
106
4.926
17.804
45.845
1.00
17.08
B


3657
CA
GLY
106
4.009
18.958
45.686
1.00
15.04
B


3658
C
GLY
106
4.554
20.276
46.177
1.00
16.72
B


3659
O
GLY
106
4.402
21.388
45.604
1.00
14.12
B


3660
N
VAL
107
5.157
20.223
47.400
1.00
14.76
B


3661
CA
VAL
107
5.493
21.467
48.096
1.00
12.62
B


3662
CB
VAL
107
5.833
21.140
49.586
1.00
13.87
B


3663
CG1
VAL
107
6.694
22.259
50.147
1.00
12.26
B


3664
CG2
VAL
107
4.536
20.989
50.402
1.00
12.29
B


3665
C
VAL
107
6.582
22.191
47.332
1.00
8.49
B


3666
O
VAL
107
6.511
23.407
47.078
1.00
11.80
B


3667
N
PRO
108
7.674
21.564
46.995
1.00
11.13
B


3668
CA
PRO
108
8.738
22.249
46.244
1.00
13.03
B


3669
CD
PRO
108
8.030
20.167
47.314
1.00
11.98
B


3670
CB
PRO
108
9.881
21.276
46.221
1.00
14.96
B


3671
CG
PRO
108
9.373
19.937
46.672
1.00
14.09
B


3672
C
PRO
108
8.248
22.686
44.846
1.00
14.75
B


3673
O
PRO
108
8.700
23.764
44.357
1.00
14.99
B


3674
N
MET
109
7.454
21.855
44.195
1.00
15.61
B


3675
CA
MET
109
6.925
22.248
42.853
1.00
18.33
B


3676
CB
MET
109
6.203
21.093
42.175
1.00
20.39
B


3677
CG
MET
109
7.038
19.955
41.666
1.00
25.95
B


3678
SD
MET
109
7.845
20.136
40.010
1.00
32.81
B


3679
CE
MET
109
7.322
21.779
39.636
1.00
9.69
B


3680
C
MET
109
6.056
23.481
42.878
1.00
17.89
B


3681
O
MET
109
6.242
24.436
42.097
1.00
17.42
B


3682
N
LEU
110
5.114
23.641
43.826
1.00
17.16
B


3683
CA
LEU
110
4.337
24.836
44.023
1.00
16.55
B


3684
CB
LEU
110
3.398
24.742
45.228
1.00
18.81
B


3685
CG
LEU
110
1.993
25.234
45.279
1.00
22.87
B


3686
CD2
LEU
110
1.598
26.372
44.346
1.00
20.44
B


3687
CD1
LEU
110
1.416
25.406
46.675
1.00
18.22
B


3688
C
LEU
110
5.252
25.999
44.394
1.00
15.66
B


3689
O
LEU
110
5.045
27.150
43.989
1.00
17.04
B


3690
N
GLY
111
6.234
25.742
45.248
1.00
13.74
B


3691
CA
GLY
111
7.166
26.840
45.661
1.00
12.36
B


3692
C
GLY
111
7.929
27.331
44.384
1.00
13.67
B


3693
O
GLY
111
8.185
28.535
44.230
1.00
14.57
B


3694
N
LYS
112
8.380
26.429
43.534
1.00
13.85
B


3695
CA
LYS
112
9.083
26.871
42.300
1.00
15.97
B


3696
CB
LYS
112
9.404
25.577
41.506
1.00
17.11
B


3697
CG
LYS
112
10.259
25.800
40.255
1.00
19.11
B


3698
CD
LYS
112
9.866
24.819
39.132
1.00
22.92
B


3699
CE
LYS
112
8.518
25.307
38.571
1.00
25.00
B


3700
NZ
LYS
112
8.040
24.390
37.463
1.00
29.56
B


3701
C
LYS
112
8.194
27.809
41.497
1.00
14.17
B


3702
O
LYS
112
8.645
28.821
40.926
1.00
16.44
B


3703
N
GLU
113
6.905
27.506
41.360
1.00
16.44
B


3704
CA
GLU
113
5.999
28.347
40.568
1.00
18.98
B


3705
CB
GLU
113
4.598
27.718
40.523
1.00
20.29
B


3706
CG
GLU
113
4.716
26.355
39.814
1.00
26.33
B


3707
CD
GLU
113
3.450
25.543
39.850
1.00
30.51
B


3708
OE1
GLU
113
2.453
26.088
40.363
1.00
32.97
B


3709
OE2
GLU
113
3.469
24.372
39.401
1.00
32.07
B


3710
C
GLU
113
5.940
29.758
41.105
1.00
18.82
B


3711
O
GLU
113
5.968
30.776
40.398
1.00
14.21
B


3712
N
ALA
114
5.826
29.871
42.452
1.00
16.47
B


3713
CA
ALA
114
5.851
31.233
43.020
1.00
15.22
B


3714
CB
ALA
114
5.549
31.121
44.535
1.00
15.63
B


3715
C
ALA
114
7.223
31.849
42.825
1.00
10.70
B


3716
O
ALA
114
7.346
33.059
42.621
1.00
13.91
B


3717
N
ALA
115
8.294
31.104
43.001
1.00
11.13
B


3718
CA
ALA
115
9.627
31.678
42.960
1.00
11.73
B


3719
CB
ALA
115
10.620
30.551
43.272
1.00
11.44
B


3720
C
ALA
115
9.995
32.188
41.534
1.00
13.25
B


3721
O
ALA
115
10.562
33.247
41.379
1.00
12.18
B


3722
N
VAL
116
9.506
31.445
40.532
1.00
14.93
B


3723
CA
VAL
116
9.740
31.963
39.142
1.00
16.26
B


3724
CB
VAL
116
9.111
30.988
38.122
1.00
17.09
B


3725
CG1
VAL
116
9.033
31.537
36.668
1.00
17.13
B


3726
CG2
VAL
116
9.980
29.733
38.100
1.00
17.69
B


3727
C
VAL
116
9.129
33.334
38.971
1.00
17.01
B


3728
O
VAL
116
9.738
34.250
38.418
1.00
18.24
B


3729
N
LYS
117
7.908
33.529
39.490
1.00
18.30
B


3730
CA
LYS
117
7.255
34.835
39.360
1.00
19.80
B


3731
CB
LYS
117
5.810
34.793
39.887
1.00
16.76
B


3732
CG
LYS
117
4.990
33.768
39.096
1.00
17.71
B


3733
CD
LYS
117
3.540
33.813
39.556
1.00
20.14
B


3734
CE
LYS
117
2.755
32.582
39.050
1.00
21.53
B


3735
NZ
LYS
117
1.364
32.553
39.597
1.00
20.89
B


3736
C
LYS
117
8.012
35.925
40.102
1.00
19.46
B


3737
O
LYS
117
8.135
37.056
39.618
1.00
18.30
B


3738
N
ALA
118
8.482
35.601
41.311
1.00
18.05
B


3739
CA
ALA
118
9.255
36.602
42.058
1.00
17.77
B


3740
CB
ALA
118
9.626
36.045
43.456
1.00
18.31
B


3741
C
ALA
118
10.523
36.964
41.288
1.00
15.24
B


3742
O
ALA
118
10.868
38.122
41.231
1.00
14.63
B


3743
N
ILE
119
11.258
36.005
40.792
1.00
14.72
B


3744
CA
ILE
119
12.501
36.173
40.069
1.00
18.19
B


3745
CB
ILE
119
13.102
34.775
39.765
1.00
17.26
B


3746
CG2
ILE
119
14.281
34.889
38.784
1.00
17.26
B


3747
CG1
ILE
119
13.654
34.186
41.096
1.00
18.79
B


3748
CD1
ILE
119
14.055
32.715
40.937
1.00
17.54
B


3749
C
ILE
119
12.289
36.979
38.760
1.00
19.59
B


3750
O
ILE
119
13.059
37.877
38.470
1.00
20.21
B


3751
N
ASP
120
11.186
36.719
38.090
1.00
20.62
B


3752
CA
ASP
120
10.810
37.469
36.882
1.00
23.17
B


3753
CB
ASP
120
9.577
36.841
36.232
1.00
21.94
B


3754
CG
ASP
120
9.936
35.591
35.463
1.00
21.88
B


3755
OD1
ASP
120
9.058
34.818
35.026
1.00
25.46
B


3756
OD2
ASP
120
11.105
35.302
35.269
1.00
22.59
B


3757
C
ASP
120
10.485
38.895
37.254
1.00
22.73
B


3758
O
ASP
120
10.885
39.814
36.555
1.00
20.95
B


3759
N
GLU
121
9.724
39.123
38.369
1.00
18.54
B


3760
CA
GLU
121
9.479
40.507
38.702
1.00
17.30
B


3761
CB
GLU
121
8.466
40.604
39.888
1.00
17.31
B


3762
CG
GLU
121
8.541
41.968
40.550
1.00
18.93
B


3763
CD
GLU
121
7.682
42.145
41.799
1.00
18.71
B


3764
OE1
GLU
121
7.084
41.230
42.354
1.00
18.98
B


3765
OE2
GLU
121
7.474
43.302
42.175
1.00
20.98
B


3766
C
GLU
121
10.790
41.200
39.005
1.00
18.89
B


3767
O
GLU
121
11.038
42.381
38.667
1.00
18.49
B


3768
N
TRP
122
11.628
40.520
39.838
1.00
20.02
B


3769
CA
TRP
122
12.885
41.167
40.274
1.00
18.53
B


3770
CB
TRP
122
13.600
40.230
41.227
1.00
15.57
B


3771
CG
TRP
122
14.963
40.579
41.739
1.00
15.73
B


3772
CD2
TRP
122
16.105
39.697
41.830
1.00
17.08
B


3773
CD1
TRP
122
15.397
41.759
42.256
1.00
15.07
B


3774
NE1
TRP
122
16.706
41.665
42.632
1.00
16.21
B


3775
CE2
TRP
122
17.162
40.416
42.388
1.00
16.20
B


3776
CE3
TRP
122
16.328
38.365
41.459
1.00
18.05
B


3777
CZ2
TRP
122
18.442
39.883
42.586
1.00
18.57
B


3778
CZ3
TRP
122
17.576
37.828
41.663
1.00
20.98
B


3779
CH2
TRP
122
18.620
38.587
42.237
1.00
20.09
B


3780
C
TRP
122
13.725
41.503
39.025
1.00
21.21
B


3781
O
TRP
122
14.425
42.510
39.032
1.00
19.09
B


3782
N
GLY
123
13.902
40.536
38.089
1.00
20.57
B


3783
CA
GLY
123
14.458
40.851
36.771
1.00
21.40
B


3784
C
GLY
123
15.940
40.632
36.651
1.00
24.57
B


3785
O
GLY
123
16.522
40.777
35.566
1.00
25.85
B


3786
N
LEU
124
16.635
40.314
37.742
1.00
20.73
B


3787
CA
LEU
124
18.065
40.067
37.759
1.00
19.80
B


3788
CB
LEU
124
18.708
40.617
39.040
1.00
21.58
B


3789
CG
LEU
124
19.051
42.117
38.993
1.00
23.70
B


3790
CD2
LEU
124
19.563
42.678
40.330
1.00
23.32
B


3791
CD1
LEU
124
17.873
42.977
38.544
1.00
24.78
B


3792
C
LEU
124
18.354
38.592
37.589
1.00
19.77
B


3793
O
LEU
124
17.457
37.799
37.853
1.00
19.79
B


3794
N
PRO
125
19.570
38.236
37.228
1.00
20.42
B


3795
CA
PRO
125
19.936
36.861
37.051
1.00
22.86
B


3796
CD
PRO
125
20.662
39.172
36.902
1.00
23.62
B


3797
CB
PRO
125
21.363
36.893
36.550
1.00
22.60
B


3798
CG
PRO
125
21.722
38.309
36.274
1.00
26.47
B


3799
C
PRO
125
19.768
36.095
38.372
1.00
22.74
B


3800
O
PRO
125
20.269
36.477
39.430
1.00
21.45
B


3801
N
LYS
126
19.305
34.852
38.295
1.00
22.24
B


3802
CA
LYS
126
19.005
33.962
39.401
1.00
22.86
B


3803
CB
LYS
126
18.124
32.803
38.957
1.00
21.06
B


3804
CG
LYS
126
18.929
31.758
38.167
1.00
23.82
B


3805
CD
LYS
126
17.961
30.789
37.457
1.00
22.32
B


3806
CE
LYS
126
18.845
29.884
36.561
1.00
22.15
B


3807
NZ
LYS
126
17.961
28.791
36.027
1.00
24.49
B


3808
C
LYS
126
20.307
33.530
40.074
1.00
22.44
B


3809
O
LYS
126
20.382
33.087
41.219
1.00
21.24
B


3771
N
SER
127
21.377
33.758
39.322
0.50
22.04
B


3772
CA
SER
127
22.744
33.422
39.735
0.50
21.83
B


3773
CB
SER
127
23.690
33.643
38.551
0.50
22.82
B


3774
OG
SER
127
25.038
33.511
38.964
0.50
23.43
B


3775
C
SER
127
23.167
34.313
40.913
0.50
21.05
B


3776
O
SER
127
24.060
33.968
41.696
0.50
19.60
B


3771
N
2SER
127
21.411
33.697
39.339
0.50
19.47
B


3772
CA
2SER
127
22.756
33.339
39.826
0.50
17.14
B


3773
CB
2SER
127
23.775
33.421
38.687
0.50
14.50
B


3774
OG
2SER
127
23.950
34.771
38.291
0.50
7.29
B


3775
C
2SER
127
23.181
34.295
40.956
0.50
18.17
B


3776
O
2SER
127
24.097
34.012
41.735
0.50
16.66
B


3822
N
LYS
128
22.533
35.469
41.031
1.00
19.04
B


3823
CA
LYS
128
22.783
36.427
42.081
1.00
20.72
B


3824
CB
LYS
128
22.502
37.849
41.671
1.00
23.49
B


3825
CG
LYS
128
23.389
38.410
40.542
1.00
30.20
B


3826
CD
LYS
128
23.026
39.874
40.340
1.00
33.60
B


3827
CE
LYS
128
23.822
40.578
39.232
1.00
37.82
B


3828
NZ
LYS
128
25.202
40.880
39.721
1.00
39.55
B


3829
C
LYS
128
21.986
36.062
43.377
1.00
21.66
B


3830
O
LYS
128
22.241
36.770
44.382
1.00
20.03
B


3831
N
ILE
129
21.230
34.978
43.388
1.00
18.10
B


3832
CA
ILE
129
20.581
34.590
44.680
1.00
16.54
B


3833
CB
ILE
129
19.316
33.782
44.401
1.00
15.71
B


3834
CG2
ILE
129
18.718
33.127
45.663
1.00
11.23
B


3835
CG1
ILE
129
18.307
34.710
43.694
1.00
13.07
B


3836
CD1
ILE
129
17.061
33.962
43.180
1.00
15.51
B


3837
C
ILE
129
21.608
33.872
45.536
1.00
16.68
B


3838
O
ILE
129
22.165
32.871
45.084
1.00
15.39
B


3839
N
THR
130
21.957
34.462
46.705
1.00
15.34
B


3840
CA
THR
130
23.024
33.843
47.513
1.00
14.69
B


3841
CB
THR
130
23.876
34.966
48.174
1.00
14.81
B


3842
OG1
THR
130
23.019
35.931
48.807
1.00
13.89
B


3843
CG2
THR
130
24.706
35.623
47.041
1.00
17.84
B


3844
C
THR
130
22.560
32.969
48.666
1.00
14.07
B


3845
O
THR
130
23.308
32.122
49.204
1.00
16.08
B


3846
N
HIS
131
21.310
33.169
49.095
1.00
15.00
B


3847
CA
HIS
131
20.714
32.452
50.195
1.00
13.80
B


3848
ND1
HIS
131
22.691
34.795
51.389
1.00
13.62
B


3849
CG
HIS
131
21.955
33.803
52.010
1.00
13.18
B


3850
CB
HIS
131
20.636
33.364
51.471
1.00
10.47
B


3851
NE2
HIS
131
23.869
34.135
53.120
1.00
13.50
B


3852
CD2
HIS
131
22.700
33.398
53.113
1.00
12.01
B


3853
CE1
HIS
131
23.806
35.011
52.079
1.00
15.38
B


3854
C
HIS
131
19.298
32.060
49.795
1.00
12.63
B


3855
O
HIS
131
18.634
32.863
49.200
1.00
13.50
B


3856
N
LEU
132
18.831
30.924
50.313
1.00
13.69
B


3857
CA
LEU
132
17.473
30.501
50.116
1.00
13.61
B


3858
CB
LEU
132
17.465
29.221
49.300
1.00
10.62
B


3859
CG
LEU
132
16.188
28.382
49.191
1.00
14.13
B


3860
CD2
LEU
132
16.455
27.089
48.383
1.00
13.36
B


3861
CD1
LEU
132
15.047
29.149
48.528
1.00
13.56
B


3862
C
LEU
132
16.859
30.046
51.484
1.00
12.52
B


3863
O
LEU
132
17.454
29.195
52.156
1.00
12.11
B


3864
N
ILE
133
15.703
30.529
51.771
1.00
14.80
B


3865
CA
ILE
133
14.955
30.109
52.986
1.00
14.31
B


3866
CB
ILE
133
14.503
31.334
53.827
1.00
13.70
B


3867
CG2
ILE
133
13.588
30.819
54.982
1.00
12.52
B


3868
CG1
ILE
133
15.708
32.115
54.373
1.00
11.45
B


3869
CD1
ILE
133
15.251
33.498
54.892
1.00
11.04
B


3870
C
ILE
133
13.698
29.400
52.468
1.00
12.62
B


3871
O
ILE
133
12.926
30.087
51.772
1.00
13.96
B


3872
N
PHE
134
13.557
28.112
52.687
1.00
11.67
B


3873
CA
PHE
134
12.387
27.393
52.260
1.00
13.85
B


3874
CB
PHE
134
12.714
26.049
51.589
1.00
12.44
B


3875
CG
PHE
134
11.558
25.525
50.779
1.00
15.70
B


3876
CD1
PHE
134
11.633
25.605
49.361
1.00
15.31
B


3877
CD2
PHE
134
10.465
24.922
51.345
1.00
13.44
B


3878
CE1
PHE
134
10.524
25.216
48.602
1.00
13.92
B


3879
CE2
PHE
134
9.372
24.541
50.599
1.00
16.57
B


3880
CZ
PHE
134
9.395
24.662
49.177
1.00
15.48
B


3881
C
PHE
134
11.600
27.049
53.534
1.00
15.97
B


3882
O
PHE
134
12.189
26.468
54.472
1.00
17.75
B


3883
N
CYS
135
10.317
27.448
53.505
1.00
15.45
B


3884
CA
CYS
135
9.525
27.205
54.713
1.00
15.67
B


3885
CB
CYS
135
9.230
28.599
55.339
1.00
13.03
B


3886
SG
CYS
135
8.086
28.444
56.781
1.00
16.09
B


3887
C
CYS
135
8.214
26.506
54.398
1.00
15.14
B


3888
O
CYS
135
7.553
26.840
53.391
1.00
14.64
B


3889
N
THR
136
7.863
25.473
55.117
1.00
13.63
B


3890
CA
THR
136
6.561
24.815
54.979
1.00
12.82
B


3891
CB
THR
136
6.643
23.692
53.922
1.00
12.52
B


3892
OG1
THR
136
5.357
23.124
53.577
1.00
11.56
B


3893
CG2
THR
136
7.466
22.493
54.370
1.00
11.76
B


3894
C
THR
136
6.142
24.172
56.325
1.00
15.90
B


3895
O
THR
136
6.981
23.951
57.241
1.00
15.74
B


3896
N
THR
137
4.918
23.685
56.351
1.00
12.71
B


3897
CA
THR
137
4.337
22.970
57.499
1.00
15.88
B


3898
CB
THR
137
3.199
23.846
58.086
1.00
16.07
B


3899
OG1
THR
137
3.652
25.180
58.268
1.00
12.64
B


3900
CG2
THR
137
2.703
23.341
59.442
1.00
17.89
B


3901
C
THR
137
3.803
21.607
57.027
1.00
16.70
B


3902
O
THR
137
3.213
20.843
57.800
1.00
15.33
B


3903
N
ALA
138
4.045
21.306
55.754
1.00
14.66
B


3904
CA
ALA
138
3.515
20.073
55.135
1.00
16.54
B


3905
CB
ALA
138
2.639
20.440
53.934
1.00
16.96
B


3906
C
ALA
138
4.617
19.108
54.641
1.00
17.90
B


3907
O
ALA
138
5.237
19.333
53.590
1.00
18.24
B


3908
N
GLY
139
4.797
18.047
55.433
1.00
16.63
B


3909
CA
GLY
139
5.744
16.930
55.156
1.00
16.95
B


3910
C
GLY
139
7.213
17.318
55.420
1.00
14.53
B


3911
O
GLY
139
7.534
18.479
55.683
1.00
15.64
B


3912
N
VAL
140
8.063
16.293
55.362
1.00
11.63
B


3913
CA
VAL
140
9.539
16.427
55.474
1.00
13.84
B


3914
CB
VAL
140
10.068
16.286
56.910
1.00
13.57
B


3915
CG1
VAL
140
9.407
17.238
57.900
1.00
14.46
B


3916
CG2
VAL
140
9.903
14.878
57.479
1.00
13.38
B


3917
C
VAL
140
10.187
15.325
54.649
1.00
12.93
B


3918
O
VAL
140
9.553
14.310
54.338
1.00
17.79
B


3919
N
ASP
141
11.436
15.542
54.315
1.00
11.30
B


3920
CA
ASP
141
12.199
14.589
53.500
1.00
12.34
B


3921
CB
ASP
141
11.666
14.626
52.064
1.00
12.43
B


3922
CG
ASP
141
12.068
13.405
51.242
1.00
15.41
B


3923
OD1
ASP
141
12.095
12.240
51.790
1.00
16.79
B


3924
OD2
ASP
141
12.381
13.541
50.000
1.00
18.27
B


3925
C
ASP
141
13.674
14.980
53.510
1.00
10.73
B


3926
O
ASP
141
14.030
16.115
53.838
1.00
13.73
B


3927
N
MET
142
14.519
14.031
53.152
1.00
12.08
B


3928
CA
MET
142
15.977
14.258
53.095
1.00
12.54
B


3929
CB
MET
142
16.665
13.534
54.250
1.00
12.42
B


3930
CG
MET
142
16.027
13.847
55.607
1.00
14.21
B


3931
SD
MET
142
16.996
13.260
56.976
1.00
17.74
B


3932
CE
MET
142
18.395
14.329
57.212
1.00
14.81
B


3933
C
MET
142
16.518
13.753
51.747
1.00
14.99
B


3934
O
MET
142
16.298
12.575
51.633
1.00
13.32
B


3935
N
PRO
143
17.168
14.569
50.956
1.00
15.48
B


3936
CA
PRO
143
17.386
15.952
50.963
1.00
14.25
B


3937
CD
PRO
143
17.681
14.048
49.648
1.00
15.23
B


3938
CB
PRO
143
17.922
16.387
49.585
1.00
15.85
B


3939
CG
PRO
143
18.496
15.137
49.018
1.00
16.12
B


3940
C
PRO
143
16.059
16.669
51.159
1.00
13.65
B


3941
O
PRO
143
15.046
16.034
50.841
1.00
13.35
B


3942
N
GLY
144
16.011
17.906
51.657
1.00
12.74
B


3943
CA
GLY
144
14.736
18.559
51.848
1.00
14.31
B


3944
C
GLY
144
14.163
19.311
50.635
1.00
16.74
B


3945
O
GLY
144
14.744
19.323
49.539
1.00
15.00
B


3946
N
ALA
145
13.024
19.963
50.870
1.00
14.69
B


3947
CA
ALA
145
12.360
20.742
49.851
1.00
16.45
B


3948
CB
ALA
145
11.001
21.327
50.283
1.00
11.78
B


3949
C
ALA
145
13.284
21.862
49.365
1.00
19.61
B


3950
O
ALA
145
13.128
22.261
48.195
1.00
16.59
B


3951
N
ASP
146
14.180
22.370
50.228
1.00
17.60
B


3952
CA
ASP
146
15.134
23.390
49.763
1.00
18.57
B


3953
CB
ASP
146
16.007
23.868
50.924
1.00
18.75
B


3954
CG
ASP
146
16.880
22.821
51.582
1.00
17.58
B


3955
OD1
ASP
146
16.448
21.685
51.824
1.00
15.16
B


3956
OD2
ASP
146
18.073
23.072
51.863
1.00
16.33
B


3957
C
ASP
146
16.048
22.859
48.646
1.00
18.92
B


3958
O
ASP
146
16.314
23.574
47.647
1.00
17.71
B


3959
N
TYR
147
16.551
21.644
48.806
1.00
18.73
B


3960
CA
TYR
147
17.408
21.022
47.785
1.00
19.64
B


3961
CB
TYR
147
17.912
19.647
48.251
1.00
20.61
B


3962
CG
TYR
147
18.494
18.797
47.138
1.00
20.41
B


3963
CD1
TYR
147
19.822
18.953
46.757
1.00
21.27
B


3964
CD2
TYR
147
17.714
17.888
46.456
1.00
20.47
B


3965
CE1
TYR
147
20.376
18.182
45.758
1.00
23.19
B


3966
CE2
TYR
147
18.229
17.143
45.413
1.00
21.89
B


3967
CZ
TYR
147
19.566
17.297
45.083
1.00
24.50
B


3968
OH
TYR
147
20.091
16.548
44.065
1.00
27.67
B


3969
C
TYR
147
16.567
20.859
46.524
1.00
19.01
B


3970
O
TYR
147
17.125
21.097
45.442
1.00
16.71
B


3971
N
GLN
148
15.339
20.338
46.702
1.00
17.26
B


3972
CA
GLN
148
14.500
20.165
45.529
1.00
17.98
B


3973
CB
GLN
148
13.155
19.513
45.800
1.00
18.27
B


3974
CG
GLN
148
13.239
18.213
46.580
1.00
18.49
B


3975
CD
GLN
148
13.942
17.102
45.857
1.00
20.89
B


3976
OE1
GLN
148
14.271
17.217
44.645
1.00
19.88
B


3977
NE2
GLN
148
14.188
15.962
46.529
1.00
17.86
B


3978
C
GLN
148
14.258
21.474
44.775
1.00
19.24
B


3979
O
GLN
148
14.315
21.503
43.516
1.00
17.75
B


3980
N
LEU
149
14.073
22.586
45.489
1.00
16.00
B


3981
CA
LEU
149
13.885
23.879
44.884
1.00
16.60
B


3982
CB
LEU
149
13.565
24.981
45.874
1.00
19.06
B


3983
CG
LEU
149
12.552
26.080
45.648
1.00
22.52
B


3984
CD2
LEU
149
11.949
26.222
44.259
1.00
18.04
B


3985
CD1
LEU
149
13.010
27.450
46.157
1.00
19.02
B


3986
C
LEU
149
15.121
24.303
44.105
1.00
17.15
B


3987
O
LEU
149
14.996
24.881
42.998
1.00
14.65
B


3988
N
VAL
150
16.318
24.197
44.657
1.00
17.09
B


3989
CA
VAL
150
17.492
24.627
43.893
1.00
20.33
B


3990
CB
VAL
150
18.833
24.701
44.611
1.00
22.76
B


3991
CG1
VAL
150
18.725
24.838
46.133
1.00
19.08
B


3992
CG2
VAL
150
19.885
23.730
44.138
1.00
23.75
B


3993
C
VAL
150
17.620
23.854
42.558
1.00
20.24
B


3994
O
VAL
150
18.023
24.474
41.566
1.00
18.63
B


3995
N
LYS
151
17.357
22.565
42.591
1.00
18.77
B


3996
CA
LYS
151
17.432
21.733
41.387
1.00
23.02
B


3997
CB
LYS
151
17.289
20.272
41.809
1.00
26.22
B


3998
CG
LYS
151
17.340
19.281
40.655
1.00
31.92
B


3999
CD
LYS
151
17.313
17.833
41.158
1.00
35.35
B


4000
CE
LYS
151
17.095
16.899
39.977
1.00
38.72
B


4001
NZ
LYS
151
16.732
15.510
40.368
1.00
40.45
B


4002
C
LYS
151
16.347
22.157
40.397
1.00
22.83
B


4003
O
LYS
151
16.602
22.340
39.197
1.00
21.60
B


4004
N
LEU
152
15.135
22.388
40.901
1.00
18.66
B


4005
CA
LEU
152
14.031
22.838
40.101
1.00
20.27
B


4006
CB
LEU
152
12.710
22.942
40.869
1.00
18.41
B


4007
CG
LEU
152
12.055
21.606
41.224
1.00
20.69
B


4008
CD2
LEU
152
11.777
20.767
39.966
1.00
20.82
B


4009
CD1
LEU
152
10.743
21.748
41.980
1.00
20.71
B


4010
C
LEU
152
14.334
24.174
39.434
1.00
20.96
B


4011
O
LEU
152
13.898
24.429
38.289
1.00
17.97
B


4012
N
LEU
153
14.860
25.139
40.188
1.00
17.62
B


4013
CA
LEU
153
15.090
26.448
39.656
1.00
18.67
B


4014
CB
LEU
153
15.113
27.525
40.772
1.00
18.54
B


4015
CG
LEU
153
13.801
27.873
41.437
1.00
21.12
B


4016
CD2
LEU
153
12.835
28.385
40.361
1.00
21.73
B


4017
CD1
LEU
153
14.086
28.944
42.521
1.00
18.00
B


4018
C
LEU
153
16.448
26.607
38.957
1.00
18.37
B


4019
O
LEU
153
16.610
27.671
38.360
1.00
16.57
B


4020
N
GLY
154
17.373
25.682
39.144
1.00
16.87
B


4021
CA
GLY
154
18.735
25.830
38.659
1.00
19.10
B


4022
C
GLY
154
19.551
26.891
39.420
1.00
21.21
B


4023
O
GLY
154
20.314
27.728
38.876
1.00
17.48
B


4024
N
LEU
155
19.371
26.925
40.779
1.00
18.68
B


4025
CA
LEU
155
20.067
27.957
41.524
1.00
16.73
B


4026
CB
LEU
155
19.511
28.195
42.947
1.00
17.33
B


4027
CG
LEU
155
18.089
28.739
42.990
1.00
18.53
B


4028
CD2
LEU
155
17.948
30.088
42.289
1.00
14.57
B


4029
CD1
LEU
155
17.592
28.954
44.424
1.00
18.35
B


4030
C
LEU
155
21.502
27.466
41.709
1.00
15.61
B


4031
O
LEU
155
21.814
26.294
41.461
1.00
15.82
B


4032
N
SER
156
22.364
28.347
42.143
1.00
16.10
B


4033
CA
SER
156
23.761
27.979
42.394
1.00
17.10
B


4034
CB
SER
156
24.503
29.164
43.010
1.00
17.29
B


4035
OG
SER
156
25.755
28.741
43.526
1.00
19.70
B


4036
C
SER
156
23.809
26.790
43.369
1.00
19.78
B


4037
O
SER
156
23.096
26.770
44.387
1.00
19.11
B


4038
N
PRO
157
24.606
25.738
43.092
1.00
20.69
B


4039
CA
PRO
157
24.751
24.620
44.010
1.00
20.98
B


4040
CD
PRO
157
25.386
25.629
41.857
1.00
24.06
B


4041
CB
PRO
157
25.663
23.656
43.289
1.00
22.99
B


4042
CG
PRO
157
26.029
24.277
41.954
1.00
26.97
B


4043
C
PRO
157
25.367
25.061
45.321
1.00
18.59
B


4044
O
PRO
157
25.312
24.278
46.321
1.00
16.51
B


4045
N
SER
158
25.931
26.262
45.315
1.00
15.55
B


4046
CA
SER
158
26.589
26.829
46.508
1.00
15.78
B


4047
CB
SER
158
27.912
27.494
46.129
1.00
16.03
B


4048
OG
SER
158
28.903
26.496
45.929
1.00
19.38
B


4049
C
SER
158
25.698
27.871
47.210
1.00
14.51
B


4050
O
SER
158
26.160
28.654
48.048
1.00
15.60
B


4051
N
VAL
159
24.418
27.891
46.868
1.00
15.32
B


4052
CA
VAL
159
23.476
28.808
47.539
1.00
16.28
B


4053
CB
VAL
159
22.115
28.783
46.845
1.00
18.85
B


4054
CG1
VAL
159
21.381
27.456
47.026
1.00
18.11
B


4055
CG2
VAL
159
21.168
29.871
47.362
1.00
18.08
B


4056
C
VAL
159
23.358
28.337
49.028
1.00
14.43
B


4057
O
VAL
159
23.384
27.162
49.311
1.00
14.48
B


4058
N
LYS
160
23.404
29.274
49.965
1.00
15.01
B


4059
CA
LYS
160
23.265
28.918
51.398
1.00
14.62
B


4060
CB
LYS
160
23.819
30.055
52.286
1.00
12.92
B


4061
CG
LYS
160
25.364
29.932
52.258
1.00
16.86
B


4062
CD
LYS
160
25.946
31.113
53.073
1.00
19.51
B


4063
CE
LYS
160
27.425
30.781
53.328
1.00
22.56
B


4064
NZ
LYS
160
28.082
31.954
54.012
1.00
23.85
B


4065
C
LYS
160
21.809
28.709
51.739
1.00
11.89
B


4066
O
LYS
160
21.015
29.592
51.502
1.00
16.13
B


4067
N
ARG
161
21.442
27.560
52.268
1.00
13.89
B


4068
CA
ARG
161
20.056
27.201
52.491
1.00
13.32
B


4069
CB
ARG
161
19.838
25.813
51.845
1.00
15.41
B


4070
CG
ARG
161
20.039
25.987
50.298
1.00
14.72
B


4071
CD
ARG
161
19.982
24.565
49.751
1.00
17.76
B


4072
NE
ARG
161
21.232
23.881
49.799
1.00
18.42
B


4073
CZ
ARG
161
21.439
22.631
50.214
1.00
19.63
B


4074
NH1
ARG
161
20.545
21.803
50.732
1.00
19.49
B


4075
NH2
ARG
161
22.679
22.215
50.091
1.00
17.19
B


4076
C
ARG
161
19.645
27.069
53.960
1.00
15.16
B


4077
O
ARG
161
20.500
26.898
54.811
1.00
13.02
B


4078
N
TYR
162
18.384
27.386
54.235
1.00
14.69
B


4079
CA
TYR
162
17.778
27.412
55.579
1.00
15.19
B


4080
CB
TYR
162
17.548
28.876
56.044
1.00
12.87
B


4081
CG
TYR
162
18.884
29.590
56.047
1.00
17.46
B


4082
CD1
TYR
162
19.346
30.166
54.832
1.00
18.22
B


4083
CD2
TYR
162
19.743
29.587
57.114
1.00
15.37
B


4084
CE1
TYR
162
20.636
30.675
54.725
1.00
18.15
B


4085
CE2
TYR
162
20.998
30.152
57.047
1.00
18.00
B


4086
CZ
TYR
162
21.457
30.678
55.838
1.00
18.75
B


4087
OH
TYR
162
22.718
31.197
55.742
1.00
15.82
B


4088
C
TYR
162
16.477
26.633
55.469
1.00
12.63
B


4089
O
TYR
162
15.534
27.175
54.891
1.00
12.26
B


4090
N
MET
163
16.504
25.347
55.794
1.00
11.79
B


4091
CA
MET
163
15.323
24.518
55.566
1.00
10.61
B


4092
CB
MET
163
15.736
23.119
55.177
1.00
11.00
B


4093
CG
MET
163
14.681
22.041
54.967
1.00
13.38
B


4094
SD
MET
163
13.633
22.462
53.513
1.00
14.69
B


4095
CE
MET
163
12.076
22.822
54.259
1.00
15.70
B


4096
C
MET
163
14.426
24.539
56.819
1.00
13.04
B


4097
O
MET
163
14.803
23.911
57.803
1.00
10.67
B


4098
N
LEU
164
13.322
25.245
56.711
1.00
10.75
B


4099
CA
LEU
164
12.401
25.344
57.836
1.00
13.62
B


4100
CB
LEU
164
12.033
26.797
57.972
1.00
9.42
B


4101
CG
LEU
164
13.204
27.778
57.991
1.00
11.22
B


4102
CD2
LEU
164
14.160
27.441
59.168
1.00
11.90
B


4103
CD1
LEU
164
12.699
29.208
58.119
1.00
12.06
B


4104
C
LEU
164
11.181
24.457
57.667
1.00
13.25
B


4105
O
LEU
164
10.297
24.801
56.870
1.00
14.17
B


4106
N
TYR
165
11.170
23.345
58.378
1.00
11.58
B


4107
CA
TYR
165
10.071
22.417
58.360
1.00
12.91
B


4108
CB
TYR
165
10.715
21.024
58.356
1.00
14.17
B


4109
CG
TYR
165
10.993
20.431
56.983
1.00
16.40
B


4110
CD1
TYR
165
10.019
20.425
55.997
1.00
14.42
B


4111
CD2
TYR
165
12.233
19.860
56.727
1.00
15.87
B


4112
CE1
TYR
165
10.306
19.865
54.749
1.00
15.74
B


4113
CE2
TYR
165
12.515
19.284
55.511
1.00
17.46
B


4114
CZ
TYR
165
11.536
19.303
54.522
1.00
16.09
B


4115
OH
TYR
165
11.844
18.754
53.306
1.00
15.51
B


4116
C
TYR
165
9.179
22.465
59.639
1.00
15.72
B


4117
O
TYR
165
9.624
22.937
60.669
1.00
14.13
B


4118
N
GLN
166
7.953
22.041
59.464
1.00
15.27
B


4119
CA
GLN
166
6.925
21.948
60.475
1.00
16.47
B


4120
CB
GLN
166
7.300
20.779
61.448
1.00
17.57
B


4121
CG
GLN
166
6.035
20.172
62.121
1.00
15.02
B


4122
CD
GLN
166
5.209
19.481
61.039
1.00
19.41
B


4123
OE1
GLN
166
3.974
19.675
60.933
1.00
23.78
B


4124
NE2
GLN
166
5.823
18.751
60.159
1.00
14.10
B


4125
C
GLN
166
6.779
23.277
61.172
1.00
17.19
B


4126
O
GLN
166
6.732
23.328
62.400
1.00
17.83
B


4127
N
GLN
167
6.599
24.364
60.416
1.00
15.33
B


4128
CA
GLN
167
6.768
25.691
60.950
1.00
14.50
B


4129
CB
GLN
167
7.478
26.633
59.969
1.00
13.31
B


4130
CG
GLN
167
8.910
26.209
59.712
1.00
12.29
B


4131
CD
GLN
167
9.882
26.490
60.882
1.00
14.10
B


4132
OE1
GLN
167
9.991
27.627
61.346
1.00
16.04
B


4133
NE2
GLN
167
10.684
25.468
61.202
1.00
14.15
B


4134
C
GLN
167
5.469
26.312
61.429
1.00
17.24
B


4135
O
GLN
167
5.526
27.061
62.431
1.00
17.67
B


4136
N
GLY
168
4.351
26.064
60.787
1.00
14.58
B


4137
CA
GLY
168
3.075
26.597
61.180
1.00
13.86
B


4138
C
GLY
168
2.876
28.061
60.889
1.00
14.55
B


4139
O
GLY
168
3.556
28.794
60.162
1.00
14.79
B


4140
N
CSD
169
1.679
28.595
61.368
1.00
14.63
B


4141
CA
CSD
169
1.151
29.891
61.068
1.00
15.32
B


4142
CB
CSD
169
−0.314
30.034
61.451
1.00
15.26
B


4143
SG
CSD
169
−1.445
28.797
60.749
1.00
18.83
B


4144
C
CSD
169
1.842
31.150
61.523
1.00
16.05
B


4145
O
CSD
169
1.478
32.204
60.949
1.00
19.74
B


4146
OD1
CSD
169
−2.304
29.596
61.102
1.00
29.98
B


4147
OD2
CSD
169
−1.735
27.340
61.201
1.00
29.91
B


4148
N
ALA
170
2.841
31.159
62.375
1.00
14.11
B


4149
CA
ALA
170
3.557
32.429
62.584
1.00
15.04
B


4150
CB
ALA
170
4.094
32.429
64.055
1.00
12.79
B


4151
C
ALA
170
4.749
32.582
61.636
1.00
12.99
B


4152
O
ALA
170
5.405
33.630
61.710
1.00
12.65
B


4153
N
ALA
171
5.062
31.549
60.824
1.00
12.80
B


4154
CA
ALA
171
6.321
31.472
60.150
1.00
13.82
B


4155
CB
ALA
171
6.710
30.063
59.688
1.00
13.84
B


4156
C
ALA
171
6.520
32.369
58.919
1.00
12.96
B


4157
O
ALA
171
7.665
32.562
58.496
1.00
14.95
B


4158
N
GLY
172
5.494
33.072
58.472
1.00
13.38
B


4159
CA
GLY
172
5.613
34.140
57.526
1.00
14.64
B


4160
C
GLY
172
6.401
35.275
58.204
1.00
17.82
B


4161
O
GLY
172
7.195
35.990
57.566
1.00
15.56
B


4162
N
GLY
173
6.159
35.494
59.531
1.00
14.07
B


4163
CA
GLY
173
7.035
36.391
60.271
1.00
13.12
B


4164
C
GLY
173
8.426
35.844
60.453
1.00
13.41
B


4165
O
GLY
173
9.432
36.571
60.226
1.00
13.75
B


4166
N
THR
174
8.518
34.516
60.695
1.00
13.80
B


4167
CA
THR
174
9.851
33.931
60.889
1.00
16.34
B


4168
CB
THR
174
9.705
32.413
61.072
1.00
16.10
B


4169
OG1
THR
174
8.763
32.177
62.132
1.00
16.09
B


4170
CG2
THR
174
11.005
31.719
61.429
1.00
13.71
B


4171
C
THR
174
10.743
34.166
59.656
1.00
15.77
B


4172
O
THR
174
11.950
34.449
59.778
1.00
12.21
B


4173
N
VAL
175
10.135
33.979
58.440
1.00
14.73
B


4174
CA
VAL
175
11.040
34.031
57.264
1.00
12.67
B


4175
CB
VAL
175
10.428
33.481
55.984
1.00
9.99
B


4176
CG1
VAL
175
10.131
31.981
56.153
1.00
8.69
B


4177
CG2
VAL
175
9.074
34.126
55.663
1.00
7.67
B


4178
C
VAL
175
11.567
35.457
57.107
1.00
10.97
B


4179
O
VAL
175
12.715
35.616
56.683
1.00
14.18
B


4180
N
LEU
176
10.744
36.452
57.348
1.00
11.34
B


4181
CA
LEU
176
11.146
37.852
57.284
1.00
14.55
B


4182
CB
LEU
176
9.932
38.748
57.449
1.00
16.10
B


4183
CG
LEU
176
8.851
38.597
56.357
1.00
20.08
B


4184
CD2
LEU
176
9.477
38.939
55.004
1.00
20.87
B


4185
CD1
LEU
176
7.659
39.490
56.615
1.00
18.48
B


4186
C
LEU
176
12.204
38.154
58.334
1.00
14.60
B


4187
O
LEU
176
13.225
38.814
58.052
1.00
13.72
B


4188
N
ARG
177
11.989
37.637
59.562
1.00
14.11
B


4189
CA
ARG
177
13.035
37.819
60.615
1.00
11.32
B


4190
CB
ARG
177
12.440
37.125
61.879
1.00
11.84
B


4191
CG
ARG
177
13.463
37.052
63.039
1.00
10.17
B


4192
CD
ARG
177
12.575
36.798
64.308
1.00
10.62
B


4193
NE
ARG
177
11.849
35.547
64.299
1.00
9.67
B


4194
CZ
ARG
177
12.308
34.343
64.503
1.00
10.77
B


4195
NH1
ARG
177
13.600
34.147
64.768
1.00
14.32
B


4196
NH2
ARG
177
11.548
33.268
64.517
1.00
13.53
B


4197
C
ARG
177
14.384
37.265
60.283
1.00
10.45
B


4198
O
ARG
177
15.477
37.897
60.453
1.00
11.55
B


4199
N
LEU
178
14.432
36.029
59.766
1.00
12.38
B


4200
CA
LEU
178
15.626
35.379
59.269
1.00
13.93
B


4201
CB
LEU
178
15.389
33.915
58.876
1.00
13.12
B


4202
CG
LEU
178
16.561
33.133
58.286
1.00
13.30
B


4203
CD2
LEU
178
16.148
31.669
58.010
1.00
13.86
B


4204
CD1
LEU
178
17.777
33.097
59.247
1.00
13.76
B


4205
C
LEU
178
16.230
36.152
58.070
1.00
14.61
B


4206
O
LEU
178
17.436
36.374
58.000
1.00
11.90
B


4207
N
ALA
179
15.446
36.396
57.004
1.00
15.55
B


4208
CA
ALA
179
16.003
37.056
55.817
1.00
15.86
B


4209
CB
ALA
179
14.861
37.312
54.792
1.00
15.94
B


4210
C
ALA
179
16.606
38.423
56.114
1.00
16.96
B


4211
O
ALA
179
17.615
38.838
55.565
1.00
17.41
B


4212
N
LYS
180
15.988
39.189
57.028
1.00
17.85
B


4213
CA
LYS
180
16.568
40.453
57.494
1.00
15.94
B


4214
CB
LYS
180
15.667
41.086
58.560
1.00
19.01
B


4215
CG
LYS
180
16.295
42.352
59.178
1.00
17.50
B


4216
CD
LYS
180
15.147
43.189
59.748
1.00
18.63
B


4217
CE
LYS
180
15.715
44.188
60.760
1.00
17.33
B


4218
NZ
LYS
180
16.291
45.411
60.149
1.00
15.67
B


4219
C
LYS
180
17.996
40.304
57.985
1.00
16.75
B


4220
O
LYS
180
18.892
41.039
57.514
1.00
14.40
B


4221
N
ASP
181
18.322
39.325
58.833
1.00
15.83
B


4222
CA
ASP
181
19.697
39.191
59.317
1.00
14.80
B


4223
CB
ASP
181
19.735
38.260
60.541
1.00
17.26
B


4224
CG
ASP
181
19.301
38.908
61.876
1.00
16.08
B


4225
OD1
ASP
181
19.535
40.104
62.061
1.00
17.86
B


4226
OD2
ASP
181
18.712
38.258
62.743
1.00
15.80
B


4227
C
ASP
181
20.653
38.688
58.227
1.00
16.10
B


4228
O
ASP
181
21.795
39.120
58.095
1.00
16.73
B


4229
N
LEU
182
20.259
37.715
57.430
1.00
15.21
B


4230
CA
LEU
182
21.100
37.248
56.316
1.00
16.66
B


4231
CB
LEU
182
20.380
36.146
55.547
1.00
16.39
B


4232
CG
LEU
182
19.886
34.942
56.342
1.00
17.06
B


4233
CD2
LEU
182
21.100
34.312
57.009
1.00
17.01
B


4234
CD1
LEU
182
19.172
33.904
55.496
1.00
17.11
B


4235
C
LEU
182
21.434
38.389
55.353
1.00
14.47
B


4236
O
LEU
182
22.614
38.578
55.050
1.00
17.95
B


4237
N
ALA
183
20.461
39.166
54.954
1.00
15.14
B


4238
CA
ALA
183
20.652
40.215
53.938
1.00
17.15
B


4239
CB
ALA
183
19.292
40.789
53.562
1.00
17.03
B


4240
C
ALA
183
21.510
41.323
54.476
1.00
18.42
B


4241
O
ALA
183
22.395
41.831
53.811
1.00
16.11
B


4242
N
GLU
184
21.258
41.701
55.766
1.00
17.74
B


4243
CA
GLU
184
22.048
42.768
56.366
1.00
18.53
B


4244
CB
GLU
184
21.300
43.366
57.609
1.00
17.38
B


4245
CG
GLU
184
20.080
44.190
57.135
1.00
18.66
B


4246
CD
GLU
184
19.120
44.521
58.271
1.00
20.82
B


4247
OE1
GLU
184
19.502
44.277
59.444
1.00
19.61
B


4248
OE2
GLU
184
17.986
45.018
58.047
1.00
19.07
B


4249
C
GLU
184
23.441
42.360
56.778
1.00
16.95
B


4250
O
GLU
184
24.337
43.246
56.764
1.00
17.24
B


4251
N
ASN
185
23.699
41.086
57.024
1.00
13.32
B


4252
CA
ASN
185
25.053
40.743
57.464
1.00
15.62
B


4253
CB
ASN
185
25.065
39.580
58.508
1.00
14.79
B


4254
CG
ASN
185
26.403
39.531
59.220
1.00
14.88
B


4255
OD1
ASN
185
26.860
40.582
59.674
1.00
15.45
B


4256
ND2
ASN
185
27.144
38.441
59.247
1.00
15.11
B


4257
C
ASN
185
25.903
40.412
56.248
1.00
19.35
B


4258
O
ASN
185
27.106
40.302
56.402
1.00
17.69
B


4259
N
ASN
186
25.286
40.205
55.038
1.00
19.17
B


4260
CA
ASN
186
26.122
39.734
53.916
1.00
18.94
B


4261
CB
ASN
186
25.660
38.331
53.524
1.00
19.49
B


4262
CG
ASN
186
25.905
37.278
54.601
1.00
20.76
B


4263
OD1
ASN
186
26.931
36.628
54.616
1.00
19.30
B


4264
ND2
ASN
186
24.894
37.120
55.464
1.00
15.38
B


4265
C
ASN
186
26.069
40.686
52.728
1.00
20.75
B


4266
O
ASN
186
25.009
40.908
52.110
1.00
19.20
B


4267
N
LYS
187
27.113
41.511
52.646
1.00
21.83
B


4268
CA
LYS
187
27.157
42.526
51.601
1.00
25.25
B


4269
CB
LYS
187
28.511
43.248
51.653
1.00
29.81
B


4270
CG
LYS
187
28.575
44.332
50.603
1.00
36.57
B


4271
CD
LYS
187
29.598
45.433
50.924
1.00
41.20
B


4272
CE
LYS
187
29.104
46.675
50.149
1.00
43.93
B


4273
NZ
LYS
187
27.758
47.038
50.715
1.00
47.95
B


4274
C
LYS
187
26.917
41.925
50.215
1.00
21.96
B


4275
O
LYS
187
27.485
40.901
49.880
1.00
21.53
B


4276
N
GLY
188
25.966
42.457
49.477
1.00
24.02
B


4277
CA
GLY
188
25.673
42.019
48.104
1.00
22.40
B


4278
C
GLY
188
24.674
40.876
48.095
1.00
23.25
B


4279
O
GLY
188
24.196
40.436
47.028
1.00
20.66
B


4280
N
SER
189
24.256
40.404
49.313
1.00
17.56
B


4281
CA
SER
189
23.515
39.145
49.256
1.00
14.19
B


4282
CB
SER
189
23.551
38.426
50.639
1.00
13.25
B


4283
OG
SER
189
22.876
39.291
51.554
1.00
13.20
B


4284
C
SER
189
22.109
39.436
48.806
1.00
15.05
B


4285
O
SER
189
21.571
40.532
48.958
1.00
17.38
B


4286
N
ARG
190
21.487
38.445
48.182
1.00
14.62
B


4287
CA
ARG
190
20.096
38.511
47.766
1.00
15.71
B


4288
CB
ARG
190
19.897
38.718
46.217
1.00
13.97
B


4289
CG
ARG
190
20.434
40.137
45.851
1.00
13.63
B


4290
CD
ARG
190
19.361
41.172
46.158
1.00
14.77
B


4291
NE
ARG
190
19.686
42.563
45.843
1.00
17.01
B


4292
CZ
ARG
190
20.443
43.380
46.550
1.00
20.81
B


4293
NH1
ARG
190
21.162
42.937
47.632
1.00
19.67
B


4294
NH2
ARG
190
20.572
44.652
46.200
1.00
15.95
B


4295
C
ARG
190
19.454
37.199
48.194
1.00
14.14
B


4296
O
ARG
190
19.804
36.099
47.792
1.00
14.54
B


4297
N
VAL
191
18.414
37.349
49.012
1.00
15.36
B


4298
CA
VAL
191
17.760
36.199
49.639
1.00
12.79
B


4299
CB
VAL
191
17.461
36.518
51.153
1.00
14.80
B


4300
CG1
VAL
191
16.898
35.281
51.866
1.00
15.86
B


4301
CG2
VAL
191
18.744
37.016
51.804
1.00
12.63
B


4302
C
VAL
191
16.425
35.919
48.977
1.00
12.57
B


4303
O
VAL
191
15.569
36.765
48.870
1.00
15.60
B


4304
N
LEU
192
16.254
34.676
48.573
1.00
13.56
B


4305
CA
LEU
192
15.004
34.147
48.089
1.00
13.98
B


4306
CB
LEU
192
15.196
33.091
46.984
1.00
11.83
B


4307
CG
LEU
192
13.955
32.395
46.462
1.00
11.19
B


4308
CD2
LEU
192
14.314
31.376
45.351
1.00
12.26
B


4309
CD1
LEU
192
12.912
33.384
45.934
1.00
11.62
B


4310
C
LEU
192
14.313
33.410
49.255
1.00
12.76
B


4311
O
LEU
192
14.776
32.434
49.806
1.00
12.16
B


4312
N
ILE
193
13.131
33.883
49.540
1.00
14.99
B


4313
CA
ILE
193
12.253
33.305
50.553
1.00
14.26
B


4314
CB
ILE
193
11.539
34.395
51.365
1.00
15.44
B


4315
CG2
ILE
193
10.399
33.757
52.157
1.00
15.15
B


4316
CG1
ILE
193
12.573
35.095
52.283
1.00
15.62
B


4317
CD1
ILE
193
11.926
36.312
52.946
1.00
16.17
B


4318
C
ILE
193
11.136
32.571
49.790
1.00
15.15
B


4319
O
ILE
193
10.528
33.172
48.912
1.00
17.37
B


4320
N
VAL
194
10.932
31.311
50.091
1.00
14.25
B


4321
CA
VAL
194
9.762
30.613
49.656
1.00
13.35
B


4322
CB
VAL
194
10.191
29.433
48.700
1.00
14.38
B


4323
CG1
VAL
194
8.965
28.675
48.213
1.00
13.71
B


4324
CG2
VAL
194
10.993
29.982
47.503
1.00
12.10
B


4325
C
VAL
194
9.026
29.930
50.816
1.00
14.29
B


4326
O
VAL
194
9.570
29.017
51.418
1.00
15.09
B


4327
N
CYS
195
7.741
30.304
50.991
1.00
13.22
B


4328
CA
CYS
195
6.880
29.553
51.870
1.00
13.97
B


4329
CB
CYS
195
6.053
30.454
52.825
1.00
13.41
B


4330
SG
CYS
195
7.200
31.332
53.970
1.00
13.51
B


4331
C
CYS
195
5.940
28.750
50.981
1.00
12.18
B


4332
O
CYS
195
5.167
29.357
50.230
1.00
14.80
B


4333
N
SER
196
5.786
27.474
51.172
1.00
14.50
B


4334
CA
SER
196
4.895
26.697
50.348
1.00
13.53
B


4335
CB
SER
196
5.703
25.956
49.252
1.00
13.31
B


4336
OG
SER
196
4.731
25.204
48.538
1.00
15.99
B


4337
C
SER
196
4.115
25.682
51.194
1.00
14.19
B


4338
O
SER
196
4.712
24.852
51.890
1.00
12.43
B


4339
N
GLU
197
2.801
25.854
51.117
1.00
12.15
B


4340
CA
GLU
197
1.949
25.019
51.989
1.00
14.71
B


4341
CB
GLU
197
1.229
25.971
52.957
1.00
12.55
B


4342
CG
GLU
197
2.212
26.780
53.826
1.00
12.64
B


4343
CD
GLU
197
2.723
25.947
54.994
1.00
13.06
B


4344
OE1
GLU
197
2.769
24.708
54.939
1.00
12.15
B


4345
OE2
GLU
197
3.182
26.579
55.977
1.00
12.05
B


4346
C
GLU
197
0.907
24.245
51.209
1.00
15.35
B


4347
O
GLU
197
0.119
24.817
50.424
1.00
15.96
B


4348
N
ILE
198
0.849
22.954
51.481
1.00
14.10
B


4349
CA
ILE
198
−0.172
22.062
51.017
1.00
15.54
B


4350
CB
ILE
198
0.382
21.039
49.982
1.00
17.24
B


4351
CG2
ILE
198
−0.677
19.984
49.684
1.00
14.51
B


4352
CG1
ILE
198
0.746
21.854
48.680
1.00
17.38
B


4353
CD1
ILE
198
1.479
20.936
47.707
1.00
17.59
B


4354
C
ILE
198
−0.921
21.398
52.165
1.00
16.49
B


4355
O
ILE
198
−0.372
20.539
52.858
1.00
16.18
B


4356
N
THR
199
−2.205
21.756
52.307
1.00
17.00
B


4357
CA
THR
199
−2.983
21.232
53.431
1.00
19.19
B


4358
CB
THR
199
−4.254
22.122
53.649
1.00
19.78
B


4359
OG1
THR
199
−5.150
21.959
52.526
1.00
21.03
B


4360
CG2
THR
199
−3.805
23.546
53.817
1.00
18.34
B


4361
C
THR
199
−3.406
19.808
53.390
1.00
18.73
B


4362
O
THR
199
−3.991
19.378
54.389
1.00
20.23
B


4363
N
ALA
200
−3.032
18.966
52.437
1.00
17.18
B


4364
CA
ALA
200
−3.293
17.567
52.378
1.00
16.00
B


4365
CB
ALA
200
−2.716
16.854
51.158
1.00
16.69
B


4366
C
ALA
200
−2.722
16.809
53.619
1.00
19.26
B


4367
O
ALA
200
−3.231
15.757
53.967
1.00
12.21
B


4368
N
ILE
201
−1.612
17.337
54.180
1.00
16.68
B


4369
CA
ILE
201
−1.007
16.728
55.362
1.00
18.76
B


4370
CB
ILE
201
0.304
17.474
55.700
1.00
16.90
B


4371
CG2
ILE
201
0.016
18.875
56.251
1.00
18.55
B


4372
CG1
ILE
201
1.280
16.784
56.650
1.00
20.46
B


4373
CD1
ILE
201
1.753
15.422
56.130
1.00
18.57
B


4374
C
ILE
201
−1.960
16.730
56.559
1.00
15.39
B


4375
O
ILE
201
−1.810
15.844
57.397
1.00
16.53
B


4376
N
LEU
202
−2.902
17.650
56.652
1.00
16.21
B


4377
CA
LEU
202
−3.835
17.728
57.754
1.00
21.36
B


4378
CB
LEU
202
−3.592
19.031
58.485
1.00
23.96
B


4379
CG
LEU
202
−4.019
20.405
58.098
1.00
28.83
B


4380
CD2
LEU
202
−5.087
20.600
57.035
1.00
28.62
B


4381
CD1
LEU
202
−2.821
21.317
57.825
1.00
30.75
B


4382
C
LEU
202
−5.310
17.525
57.462
1.00
22.61
B


4383
O
LEU
202
−6.194
17.799
58.275
1.00
19.31
B


4384
N
PHE
203
−5.629
17.079
56.251
1.00
22.50
B


4385
CA
PHE
203
−6.982
16.715
55.860
1.00
20.37
B


4386
CB
PHE
203
−7.012
16.398
54.339
1.00
20.23
B


4387
CG
PHE
203
−8.352
15.853
53.883
1.00
20.06
B


4388
CD1
PHE
203
−8.609
14.510
53.948
1.00
18.64
B


4389
CD2
PHE
203
−9.284
16.690
53.311
1.00
20.57
B


4390
CE1
PHE
203
−9.842
13.981
53.547
1.00
21.29
B


4391
CE2
PHE
203
−10.503
16.156
52.883
1.00
22.67
B


4392
CZ
PHE
203
−10.795
14.783
52.990
1.00
19.78
B


4393
C
PHE
203
−7.402
15.465
56.633
1.00
18.11
B


4394
O
PHE
203
−6.679
14.478
56.768
1.00
19.21
B


4395
N
HIS
204
−8.612
15.480
57.181
1.00
18.25
B


4396
CA
HIS
204
−9.105
14.326
57.953
1.00
20.33
B


4397
ND1
HIS
204
−6.645
13.362
59.835
1.00
19.25
B


4398
CG
HIS
204
−7.412
14.477
59.880
1.00
20.81
B


4399
CB
HIS
204
−8.873
14.493
59.484
1.00
19.67
B


4400
NE2
HIS
204
−5.336
14.915
60.477
1.00
21.13
B


4401
CD2
HIS
204
−6.588
15.472
60.301
1.00
21.97
B


4402
CE1
HIS
204
−5.415
13.646
60.176
1.00
21.17
B


4403
C
HIS
204
−10.615
14.228
57.741
1.00
20.16
B


4404
O
HIS
204
−11.284
15.242
57.578
1.00
22.41
B


4405
N
GLY
205
−11.145
13.023
57.795
1.00
23.54
B


4406
CA
GLY
205
−12.584
12.827
57.732
1.00
24.24
B


4407
C
GLY
205
−13.205
13.258
59.062
1.00
26.72
B


4408
O
GLY
205
−12.514
13.592
60.020
1.00
25.43
B


4409
N
PRO
206
−14.533
13.398
59.071
1.00
29.13
B


4410
CA
PRO
206
−15.254
13.891
60.219
1.00
30.03
B


4411
CD
PRO
206
−15.440
13.080
57.932
1.00
29.68
B


4412
CB
PRO
206
−16.639
14.259
59.690
1.00
31.08
B


4413
CG
PRO
206
−16.819
13.450
58.454
1.00
32.10
B


4414
C
PRO
206
−15.313
12.905
61.364
1.00
31.36
B


4415
O
PRO
206
−15.395
11.692
61.190
1.00
33.66
B


4416
N
ASN
207
−15.222
13.421
62.582
1.00
32.19
B


4417
CA
ASN
207
−15.349
12.570
63.767
1.00
32.89
B


4418
CB
ASN
207
−14.021
11.922
64.099
1.00
35.19
B


4419
CG
ASN
207
−14.147
11.102
65.387
1.00
36.73
B


4420
OD1
ASN
207
−14.218
9.881
65.296
1.00
36.20
B


4421
ND2
ASN
207
−14.231
11.812
66.507
1.00
35.51
B


4422
C
ASN
207
−15.897
13.406
64.917
1.00
33.85
B


4423
O
ASN
207
−15.367
14.435
65.341
1.00
29.88
B


4424
N
ALA
208
−17.054
12.971
65.422
1.00
35.11
B


4425
CA
ALA
208
−17.849
13.627
66.447
1.00
36.05
B


4426
C
ALA
208
−17.072
13.998
67.693
1.00
35.44
B


4427
O
ALA
208
−17.409
14.992
68.318
1.00
37.83
B


4428
CB
ALA
208
−19.035
12.722
66.862
1.00
36.08
B


4429
N
ASN
209
−16.042
13.280
68.084
1.00
37.00
B


4430
CA
ASN
209
−15.220
13.565
69.233
1.00
39.36
B


4431
CB
ASN
209
−14.483
12.300
69.705
1.00
43.23
B


4432
CG
ASN
209
−15.411
11.124
69.843
1.00
47.10
B


4433
OD1
ASN
209
−16.521
11.246
70.386
1.00
48.34
B


4434
ND2
ASN
209
−15.021
9.956
69.351
1.00
50.28
B


4435
C
ASN
209
−14.106
14.582
68.963
1.00
39.10
B


4436
O
ASN
209
−13.268
14.824
69.859
1.00
36.18
B


4437
N
HIS
210
−13.946
14.940
67.682
1.00
36.31
B


4438
CA
HIS
210
−12.852
15.852
67.359
1.00
36.10
B


4439
ND1
HIS
210
−10.048
14.222
68.273
1.00
38.38
B


4440
CG
HIS
210
−11.110
14.011
67.418
1.00
37.24
B


4441
CB
HIS
210
−11.763
15.090
66.606
1.00
36.59
B


4442
NE2
HIS
210
−10.500
12.139
68.386
1.00
37.27
B


4443
CD2
HIS
210
−11.400
12.690
67.518
1.00
36.88
B


4444
CE1
HIS
210
−9.706
13.084
68.853
1.00
38.15
B


4445
C
HIS
210
−13.402
17.025
66.588
1.00
33.97
B


4446
O
HIS
210
−13.100
17.184
65.415
1.00
32.73
B


4447
N
LEU
211
−14.174
17.876
67.263
1.00
31.22
B


4448
CA
LEU
211
−14.756
19.025
66.584
1.00
30.65
B


4449
CB
LEU
211
−15.922
19.582
67.415
1.00
31.31
B


4450
CG
LEU
211
−16.990
18.529
67.788
1.00
33.04
B


4451
CD2
LEU
211
−17.760
18.036
66.566
1.00
32.52
B


4452
CD1
LEU
211
−17.972
19.040
68.848
1.00
31.68
B


4453
C
LEU
211
−13.696
20.046
66.181
1.00
29.64
B


4454
O
LEU
211
−13.918
20.865
65.279
1.00
26.09
B


4455
N
ASP
212
−12.556
20.106
66.903
1.00
28.39
B


4456
CA
ASP
212
−11.536
21.099
66.535
1.00
26.92
B


4457
CB
ASP
212
−10.460
21.241
67.600
1.00
27.92
B


4458
CG
ASP
212
−9.945
19.948
68.192
1.00
27.65
B


4459
OD1
ASP
212
−10.461
18.838
67.974
1.00
27.95
B


4460
OD2
ASP
212
−8.961
20.022
68.973
1.00
27.71
B


4461
C
ASP
212
−10.937
20.655
65.185
1.00
26.20
B


4462
O
ASP
212
−10.730
21.467
64.293
1.00
25.48
B


4463
N
SER
213
−10.739
19.365
65.008
1.00
25.13
B


4464
CA
SER
213
−10.322
18.789
63.751
1.00
27.51
B


4465
CB
SER
213
−10.133
17.276
63.869
1.00
26.98
B


4466
OG
SER
213
−9.376
16.834
62.750
1.00
32.33
B


4467
C
SER
213
−11.308
19.063
62.614
1.00
28.19
B


4468
O
SER
213
−10.856
19.339
61.484
1.00
26.21
B


4469
N
LEU
214
−12.609
19.062
62.939
1.00
27.08
B


4470
CA
LEU
214
−13.609
19.371
61.912
1.00
26.77
B


4471
CB
LEU
214
−15.053
19.166
62.403
1.00
28.10
B


4472
CG
LEU
214
−16.159
19.393
61.349
1.00
28.20
B


4473
CD2
LEU
214
−17.536
19.343
62.046
1.00
30.09
B


4474
CD1
LEU
214
−16.064
18.273
60.324
1.00
26.98
B


4475
C
LEU
214
−13.500
20.819
61.490
1.00
25.85
B


4476
O
LEU
214
−13.590
21.198
60.314
1.00
23.18
B


4477
N
VAL
215
−13.363
21.687
62.503
1.00
23.90
B


4478
CA
VAL
215
−13.231
23.111
62.261
1.00
23.37
B


4479
CB
VAL
215
−13.112
23.971
63.525
1.00
23.34
B


4480
CG1
VAL
215
−12.673
25.397
63.229
1.00
20.26
B


4481
CG2
VAL
215
−14.451
24.021
64.288
1.00
25.40
B


4482
C
VAL
215
−12.023
23.342
61.339
1.00
23.58
B


4483
O
VAL
215
−12.121
24.202
60.472
1.00
22.67
B


4484
N
ALA
216
−10.937
22.618
61.570
1.00
22.55
B


4485
CA
ALA
216
−9.715
22.759
60.797
1.00
22.68
B


4486
CB
ALA
216
−8.704
21.736
61.360
1.00
23.19
B


4487
C
ALA
216
−9.913
22.460
59.310
1.00
22.95
B


4488
O
ALA
216
−9.207
23.048
58.504
1.00
20.51
B


4489
N
GLN
217
−10.822
21.575
58.954
1.00
21.68
B


4490
CA
GLN
217
−11.191
21.251
57.572
1.00
24.69
B


4491
CB
GLN
217
−12.134
20.032
57.533
1.00
24.18
B


4492
CG
GLN
217
−11.556
18.851
58.303
1.00
25.26
B


4493
CD
GLN
217
−10.116
18.545
57.946
1.00
26.41
B


4494
OE1
GLN
217
−9.790
18.449
56.762
1.00
24.12
B


4495
NE2
GLN
217
−9.241
18.364
58.947
1.00
23.75
B


4496
C
GLN
217
−11.813
22.373
56.767
1.00
23.78
B


4497
O
GLN
217
−11.779
22.355
55.521
1.00
24.24
B


4498
N
ALA
218
−12.276
23.424
57.415
1.00
20.67
B


4499
CA
ALA
218
−12.817
24.588
56.748
1.00
21.53
B


4500
CB
ALA
218
−14.054
25.052
57.549
1.00
23.45
B


4501
C
ALA
218
−11.837
25.747
56.677
1.00
20.66
B


4502
O
ALA
218
−12.146
26.740
56.022
1.00
22.63
B


4503
N
LEU
219
−10.715
25.702
57.416
1.00
18.68
B


4504
CA
LEU
219
−9.909
26.882
57.570
1.00
19.47
B


4505
CB
LEU
219
−9.145
26.825
58.942
1.00
18.91
B


4506
CG
LEU
219
−10.037
26.789
60.198
1.00
21.08
B


4507
CD2
LEU
219
−10.925
28.016
60.331
1.00
20.43
B


4508
CD1
LEU
219
−9.132
26.792
61.458
1.00
20.16
B


4509
C
LEU
219
−8.833
27.161
56.511
1.00
19.17
B


4510
O
LEU
219
−8.508
28.323
56.309
1.00
21.06
B


4511
N
PHE
220
−8.145
26.148
56.049
1.00
19.83
B


4512
CA
PHE
220
−6.873
26.238
55.376
1.00
19.95
B


4513
CB
PHE
220
−5.901
25.187
55.953
1.00
18.15
B


4514
CG
PHE
220
−5.679
25.255
57.455
1.00
19.86
B


4515
CD1
PHE
220
−6.328
24.358
58.290
1.00
18.28
B


4516
CD2
PHE
220
−4.939
26.286
58.002
1.00
19.81
B


4517
CE1
PHE
220
−6.205
24.482
59.692
1.00
19.83
B


4518
CE2
PHE
220
−4.760
26.391
59.391
1.00
23.21
B


4519
CZ
PHE
220
−5.401
25.476
60.229
1.00
20.13
B


4520
C
PHE
220
−6.986
25.993
53.865
1.00
19.57
B


4521
O
PHE
220
−7.588
24.990
53.457
1.00
17.92
B


4522
N
GLY
221
−6.146
26.768
53.161
1.00
20.10
B


4523
CA
GLY
221
−6.032
26.501
51.716
1.00
18.64
B


4524
C
GLY
221
−4.550
26.418
51.354
1.00
20.22
B


4525
O
GLY
221
−3.693
26.584
52.246
1.00
14.78
B


4526
N
ASP
222
−4.303
26.051
50.080
1.00
17.81
B


4527
CA
ASP
222
−2.948
25.837
49.590
1.00
15.49
B


4528
CB
ASP
222
−2.864
24.580
48.675
1.00
15.81
B


4529
CG
ASP
222
−3.288
23.347
49.408
1.00
17.74
B


4530
OD1
ASP
222
−3.586
23.384
50.652
1.00
18.97
B


4531
OD2
ASP
222
−3.374
22.273
48.797
1.00
18.32
B


4532
C
ASP
222
−2.372
26.987
48.828
1.00
14.88
B


4533
O
ASP
222
−3.120
27.652
48.085
1.00
17.37
B


4534
N
GLY
223
−1.046
27.224
48.932
1.00
14.43
B


4535
CA
GLY
223
−0.490
28.359
48.200
1.00
15.06
B


4536
C
GLY
223
0.990
28.461
48.442
1.00
17.49
B


4537
O
GLY
223
1.432
27.950
49.507
1.00
15.78
B


4538
N
ALA
224
1.700
29.227
47.632
1.00
13.37
B


4539
CA
ALA
224
3.102
29.468
47.953
1.00
13.80
B


4540
CB
ALA
224
4.098
28.580
47.233
1.00
14.95
B


4541
C
ALA
224
3.401
30.902
47.587
1.00
16.27
B


4542
O
ALA
224
2.750
31.424
46.672
1.00
15.25
B


4543
N
ALA
225
4.222
31.521
48.423
1.00
14.47
B


4544
CA
ALA
225
4.677
32.875
48.161
1.00
15.02
B


4545
CB
ALA
225
4.129
33.882
49.156
1.00
16.77
B


4546
C
ALA
225
6.190
32.880
48.111
1.00
15.87
B


4547
O
ALA
225
6.859
32.196
48.926
1.00
14.87
B


4548
N
ALA
226
6.769
33.734
47.254
1.00
13.33
B


4549
CA
ALA
226
8.209
33.816
47.152
1.00
13.75
B


4550
CB
ALA
226
8.802
33.161
45.896
1.00
13.91
B


4551
C
ALA
226
8.598
35.280
47.167
1.00
15.62
B


4552
O
ALA
226
7.872
36.126
46.616
1.00
17.43
B


4553
N
LEU
227
9.677
35.596
47.892
1.00
14.60
B


4554
CA
LEU
227
10.089
36.990
47.945
1.00
14.38
B


4555
CB
LEU
227
9.963
37.569
49.368
1.00
17.61
B


4556
CG
LEU
227
8.613
38.091
49.833
1.00
17.91
B


4557
CD2
LEU
227
8.694
38.832
51.164
1.00
18.91
B


4558
CD1
LEU
227
7.665
36.907
49.927
1.00
18.08
B


4559
C
LEU
227
11.580
37.083
47.610
1.00
13.22
B


4560
O
LEU
227
12.295
36.151
47.952
1.00
13.64
B


4561
N
ILE
228
12.055
38.203
47.088
1.00
14.27
B


4562
CA
ILE
228
13.477
38.487
46.965
1.00
14.63
B


4563
CB
ILE
228
13.922
39.043
45.582
1.00
16.79
B


4564
CG2
ILE
228
15.381
39.487
45.613
1.00
15.68
B


4565
CG1
ILE
228
13.660
37.954
44.508
1.00
16.16
B


4566
CD1
ILE
228
14.595
36.753
44.642
1.00
17.11
B


4567
C
ILE
228
13.752
39.586
48.022
1.00
14.29
B


4568
O
ILE
228
13.008
40.554
48.078
1.00
14.75
B


4569
N
VAL
229
14.784
39.411
48.845
1.00
15.28
B


4570
CA
VAL
229
15.076
40.381
49.912
1.00
16.09
B


4571
CB
VAL
229
14.743
39.799
51.307
1.00
16.66
B


4572
CG1
VAL
229
15.267
40.706
52.425
1.00
16.72
B


4573
CG2
VAL
229
13.228
39.551
51.444
1.00
15.55
B


4574
C
VAL
229
16.559
40.717
49.872
1.00
14.72
B


4575
O
VAL
229
17.385
39.845
49.691
1.00
15.04
B


4576
N
GLY
230
16.891
41.990
50.035
1.00
14.63
B


4577
CA
GLY
230
18.323
42.287
50.038
1.00
15.35
B


4578
C
GLY
230
18.439
43.690
50.666
1.00
13.66
B


4579
O
GLY
230
17.498
44.456
50.586
1.00
14.33
B


4580
N
SER
231
19.645
44.041
51.070
1.00
13.97
B


4581
CA
SER
231
19.952
45.371
51.523
1.00
15.98
B


4582
CB
SER
231
20.991
45.316
52.687
1.00
14.94
B


4583
OG
SER
231
20.274
44.737
53.802
1.00
17.50
B


4584
C
SER
231
20.666
46.119
50.385
1.00
17.76
B


4585
O
SER
231
21.247
45.407
49.544
1.00
17.44
B


4586
N
GLY
232
20.668
47.439
50.443
1.00
17.64
B


4587
CA
GLY
232
21.461
48.143
49.423
1.00
21.35
B


4588
C
GLY
232
20.916
47.928
48.002
1.00
21.72
B


4589
O
GLY
232
21.655
47.442
47.155
1.00
22.80
B


4590
N
PRO
233
19.675
48.249
47.730
1.00
21.24
B


4591
CA
PRO
233
19.092
48.084
46.435
1.00
22.08
B


4592
CD
PRO
233
18.696
48.793
48.716
1.00
24.18
B


4593
CB
PRO
233
17.620
48.319
46.596
1.00
22.49
B


4594
CG
PRO
233
17.426
48.985
47.913
1.00
24.32
B


4595
C
PRO
233
19.731
48.966
45.358
1.00
23.61
B


4596
O
PRO
233
20.127
50.120
45.544
1.00
23.70
B


4597
N
HIS
234
19.912
48.360
44.185
1.00
23.26
B


4598
CA
HIS
234
20.456
49.160
43.035
1.00
25.59
B


4599
ND1
HIS
234
22.480
46.369
43.308
1.00
36.45
B


4600
CG
HIS
234
22.400
47.631
42.760
1.00
34.08
B


4601
CB
HIS
234
21.150
48.164
42.113
1.00
29.49
B


4602
NE2
HIS
234
24.413
47.262
43.570
1.00
37.58
B


4603
CD2
HIS
234
23.617
48.186
42.931
1.00
36.49
B


4604
CE1
HIS
234
23.691
46.180
43.802
1.00
37.67
B


4605
C
HIS
234
19.246
49.814
42.403
1.00
23.40
B


4606
O
HIS
234
18.578
49.156
41.574
1.00
21.79
B


4607
N
LEU
235
18.901
51.021
42.810
1.00
18.81
B


4608
CA
LEU
235
17.636
51.633
42.434
1.00
20.01
B


4609
CB
LEU
235
17.533
52.978
43.124
1.00
21.02
B


4610
CG
LEU
235
17.572
52.902
44.667
1.00
24.52
B


4611
CD2
LEU
235
16.400
52.135
45.242
1.00
22.44
B


4612
CD1
LEU
235
17.568
54.336
45.202
1.00
25.00
B


4613
C
LEU
235
17.338
51.823
40.943
1.00
20.03
B


4614
O
LEU
235
16.155
51.945
40.563
1.00
19.96
B


4615
N
ALA
236
18.360
51.915
40.105
1.00
19.87
B


4616
CA
ALA
236
17.982
52.005
38.653
1.00
21.88
B


4617
CB
ALA
236
19.244
52.318
37.890
1.00
22.39
B


4618
C
ALA
236
17.308
50.705
38.224
1.00
20.16
B


4619
O
ALA
236
16.498
50.743
37.287
1.00
21.64
B


4620
N
VAL
237
17.633
49.525
38.743
1.00
18.36
B


4621
CA
VAL
237
17.088
48.251
38.264
1.00
21.06
B


4622
CB
VAL
237
18.149
47.357
37.605
1.00
22.43
B


4623
CG1
VAL
237
18.923
48.123
36.501
1.00
22.33
B


4624
CG2
VAL
237
19.193
46.875
38.617
1.00
21.47
B


4625
C
VAL
237
16.320
47.409
39.274
1.00
23.18
B


4626
O
VAL
237
15.517
46.553
38.862
1.00
20.17
B


4627
N
GLU
238
16.532
47.678
40.575
1.00
23.12
B


4628
CA
GLU
238
15.717
46.968
41.592
1.00
24.28
B


4629
CB
GLU
238
16.573
46.412
42.756
1.00
20.87
B


4630
CG
GLU
238
17.547
45.322
42.328
1.00
22.37
B


4631
CD
GLU
238
18.508
44.782
43.383
1.00
21.53
B


4632
OE1
GLU
238
19.213
45.594
44.013
1.00
21.50
B


4633
OE2
GLU
238
18.638
43.542
43.508
1.00
20.73
B


4634
C
GLU
238
14.668
47.930
42.114
1.00
23.86
B


4635
O
GLU
238
14.928
49.131
42.206
1.00
26.30
B


4636
N
ARG
239
13.500
47.445
42.482
1.00
25.15
B


4637
CA
ARG
239
12.408
48.245
42.998
1.00
25.86
B


4638
CB
ARG
239
11.225
47.996
42.064
1.00
30.88
B


4639
CG
ARG
239
9.888
48.635
42.354
1.00
37.20
B


4640
CD
ARG
239
9.027
48.768
41.085
1.00
42.07
B


4641
NE
ARG
239
8.117
47.635
40.971
1.00
46.99
B


4642
CZ
ARG
239
7.975
46.768
39.976
1.00
49.94
B


4643
NH1
ARG
239
7.059
45.790
40.047
1.00
49.43
B


4644
NH2
ARG
239
8.743
46.867
38.874
1.00
51.54
B


4645
C
ARG
239
11.980
47.845
44.426
1.00
23.77
B


4646
O
ARG
239
11.099
46.999
44.587
1.00
20.90
B


4647
N
PRO
240
12.408
48.616
45.405
1.00
21.88
B


4648
CA
PRO
240
11.962
48.377
46.791
1.00
22.18
B


4649
CD
PRO
240
13.553
49.537
45.400
1.00
23.80
B


4650
CB
PRO
240
12.570
49.513
47.603
1.00
23.53
B


4651
CG
PRO
240
13.816
49.902
46.861
1.00
24.77
B


4652
C
PRO
240
10.458
48.477
46.877
1.00
22.38
B


4653
O
PRO
240
9.789
49.344
46.311
1.00
23.13
B


4654
N
ILE
241
9.883
47.575
47.635
1.00
21.04
B


4655
CA
ILE
241
8.470
47.539
47.964
1.00
18.55
B


4656
CB
ILE
241
7.865
46.177
47.673
1.00
18.72
B


4657
CG2
ILE
241
6.354
46.207
47.855
1.00
17.22
B


4658
CG1
ILE
241
8.257
45.697
46.248
1.00
17.91
B


4659
CD1
ILE
241
7.763
44.285
45.958
1.00
19.18
B


4660
C
ILE
241
8.327
47.861
49.467
1.00
21.37
B


4661
O
ILE
241
7.483
48.704
49.794
1.00
21.17
B


4662
N
PHE
242
9.103
47.245
50.366
1.00
19.00
B


4663
CA
PHE
242
9.008
47.549
51.777
1.00
21.33
B


4664
CB
PHE
242
8.031
46.667
52.600
1.00
19.86
B


4665
CG
PHE
242
6.569
46.842
52.271
1.00
19.00
B


4666
CD1
PHE
242
5.872
47.952
52.680
1.00
20.22
B


4667
CD2
PHE
242
5.902
45.898
51.512
1.00
19.55
B


4668
CE1
PHE
242
4.518
48.133
52.362
1.00
19.56
B


4669
CE2
PHE
242
4.563
46.078
51.186
1.00
19.20
B


4670
CZ
PHE
242
3.873
47.177
51.607
1.00
17.64
B


4671
C
PHE
242
10.376
47.282
52.401
1.00
21.54
B


4672
O
PHE
242
11.055
46.394
51.894
1.00
20.44
B


4673
N
GLU
243
10.699
48.070
53.433
1.00
20.95
B


4674
CA
GLU
243
11.948
47.754
54.148
1.00
20.26
B


4675
CB
GLU
243
12.557
49.082
54.594
1.00
23.58
B


4676
CG
GLU
243
13.077
49.907
53.400
1.00
26.69
B


4677
CD
GLU
243
13.781
51.146
53.920
1.00
30.46
B


4678
OE1
GLU
243
13.132
52.026
54.543
1.00
32.78
B


4679
OE2
GLU
243
14.999
51.197
53.750
1.00
30.83
B


4680
C
GLU
243
11.526
46.987
55.433
1.00
19.80
B


4681
O
GLU
243
10.442
47.304
55.920
1.00
18.51
B


4682
N
ILE
244
12.295
46.075
55.954
1.00
18.47
B


4683
CA
ILE
244
11.955
45.333
57.181
1.00
20.25
B


4684
CB
ILE
244
12.401
43.868
57.101
1.00
19.02
B


4685
CG2
ILE
244
11.838
43.071
58.309
1.00
17.85
B


4686
CG1
ILE
244
11.931
43.284
55.746
1.00
17.69
B


4687
CD1
ILE
244
12.590
41.934
55.415
1.00
16.92
B


4688
C
ILE
244
12.689
46.071
58.321
1.00
18.43
B


4689
O
ILE
244
13.909
46.028
58.391
1.00
19.97
B


4690
N
VAL
245
11.984
46.828
59.103
1.00
19.22
B


4691
CA
VAL
245
12.499
47.686
60.171
1.00
18.08
B


4692
CB
VAL
245
11.439
48.736
60.578
1.00
19.80
B


4693
CG1
VAL
245
11.979
49.666
61.669
1.00
18.28
B


4694
CG2
VAL
245
11.087
49.596
59.330
1.00
22.69
B


4695
C
VAL
245
12.924
46.920
61.412
1.00
18.38
B


4696
O
VAL
245
14.098
47.031
61.843
1.00
18.98
B


4697
N
SER
246
12.034
46.083
61.921
1.00
17.27
B


4698
CA
SER
246
12.373
45.309
63.145
1.00
18.32
B


4699
CB
SER
246
12.079
46.190
64.417
1.00
17.08
B


4700
OG
SER
246
10.656
46.389
64.402
1.00
16.05
B


4701
C
SER
246
11.497
44.099
63.232
1.00
15.69
B


4702
O
SER
246
10.431
43.979
62.604
1.00
15.37
B


4703
N
THR
247
11.944
43.067
63.969
1.00
17.49
B


4704
CA
THR
247
11.206
41.813
64.093
1.00
17.94
B


4705
CB
THR
247
11.874
40.706
63.264
1.00
18.33
B


4706
OG1
THR
247
13.257
40.548
63.674
1.00
18.76
B


4707
CG2
THR
247
11.887
41.109
61.776
1.00
16.41
B


4708
C
THR
247
11.215
41.411
65.587
1.00
21.08
B


4709
O
THR
247
12.203
41.716
66.268
1.00
21.65
B


4710
N
ASP
248
10.087
40.998
66.102
1.00
18.99
B


4711
CA
ASP
248
10.043
40.506
67.481
1.00
20.27
B


4712
CB
ASP
248
9.209
41.452
68.360
1.00
19.31
B


4713
CG
ASP
248
9.724
42.860
68.406
1.00
23.48
B


4714
OD1
ASP
248
10.953
42.990
68.662
1.00
25.47
B


4715
OD2
ASP
248
8.968
43.866
68.227
1.00
25.53
B


4716
C
ASP
248
9.447
39.119
67.406
1.00
18.31
B


4717
O
ASP
248
8.597
38.848
66.529
1.00
17.06
B


4718
N
GLN
249
9.811
38.250
68.355
1.00
15.25
B


4719
CA
GLN
249
9.058
37.000
68.484
1.00
14.33
B


4720
CB
GLN
249
9.920
35.822
68.053
1.00
14.91
B


4721
CG
GLN
249
9.131
34.535
67.927
1.00
14.29
B


4722
CD
GLN
249
10.002
33.361
67.594
1.00
15.87
B


4723
OE1
GLN
249
11.214
33.498
67.835
1.00
20.00
B


4724
NE2
GLN
249
9.452
32.259
67.103
1.00
14.13
B


4725
C
GLN
249
8.769
36.772
69.979
1.00
19.39
B


4726
O
GLN
249
9.706
37.032
70.759
1.00
19.23
B


4727
N
THR
250
7.561
36.367
70.339
1.00
19.32
B


4728
CA
THR
250
7.315
36.159
71.779
1.00
19.87
B


4729
CB
THR
250
6.773
37.389
72.527
1.00
21.59
B


4730
OG1
THR
250
7.683
38.481
72.307
1.00
28.35
B


4731
CG2
THR
250
6.983
37.166
74.051
1.00
18.89
B


4732
C
THR
250
6.319
35.038
71.977
1.00
18.75
B


4733
O
THR
250
5.428
34.865
71.142
1.00
20.02
B


4734
N
ILE
251
6.403
34.338
73.096
1.00
17.68
B


4735
CA
ILE
251
5.474
33.306
73.502
1.00
16.89
B


4736
CB
ILE
251
6.238
32.151
74.147
1.00
18.89
B


4737
CG2
ILE
251
5.264
31.172
74.834
1.00
18.52
B


4738
CG1
ILE
251
7.169
31.378
73.226
1.00
16.02
B


4739
CD1
ILE
251
8.288
30.632
74.067
1.00
15.23
B


4740
C
ILE
251
4.433
33.911
74.466
1.00
20.13
B


4741
O
ILE
251
4.769
34.618
75.425
1.00
17.32
B


4742
N
LEU
252
3.157
33.767
74.176
1.00
18.45
B


4743
CA
LEU
252
2.066
34.321
74.976
1.00
19.07
B


4744
CB
LEU
252
0.774
34.286
74.175
1.00
19.46
B


4745
CG
LEU
252
0.396
35.463
73.278
1.00
23.24
B


4746
CD2
LEU
252
−0.436
34.990
72.112
1.00
21.25
B


4747
CD1
LEU
252
1.508
36.394
72.882
1.00
23.75
B


4748
C
LEU
252
1.877
33.442
76.244
1.00
18.19
B


4749
O
LEU
252
1.836
32.204
76.181
1.00
17.28
B


4750
N
PRO
253
1.931
34.084
77.404
1.00
18.72
B


4751
CA
PRO
253
1.871
33.337
78.656
1.00
19.30
B


4752
CD
PRO
253
1.946
35.524
77.633
1.00
19.70
B


4753
CB
PRO
253
2.007
34.415
79.738
1.00
20.88
B


4754
CG
PRO
253
1.469
35.648
79.089
1.00
23.61
B


4755
C
PRO
253
0.618
32.514
78.761
1.00
18.39
B


4756
O
PRO
253
−0.418
32.946
78.274
1.00
20.01
B


4757
N
ASP
254
0.699
31.301
79.292
1.00
17.80
B


4758
CA
ASP
254
−0.433
30.459
79.586
1.00
19.42
B


4759
CB
ASP
254
−1.281
31.191
80.662
1.00
20.10
B


4760
CG
ASP
254
−0.420
31.437
81.902
1.00
21.35
B


4761
OD1
ASP
254
−0.125
32.573
82.229
1.00
24.83
B


4762
OD2
ASP
254
−0.004
30.451
82.485
1.00
23.09
B


4763
C
ASP
254
−1.326
30.155
78.392
1.00
21.18
B


4764
O
ASP
254
−2.512
29.857
78.582
1.00
18.72
B


4765
N
THR
255
−0.693
29.973
77.208
1.00
20.77
B


4766
CA
THR
255
−1.488
29.570
76.040
1.00
20.62
B


4767
CB
THR
255
−1.491
30.706
75.020
1.00
19.84
B


4768
OG1
THR
255
−0.108
30.933
74.638
1.00
22.29
B


4769
CG2
THR
255
−2.078
31.975
75.567
1.00
17.24
B


4770
C
THR
255
−0.914
28.333
75.379
1.00
23.88
B


4771
O
THR
255
−1.322
27.957
74.270
1.00
24.06
B


4772
N
GLU
256
−0.161
27.518
76.091
1.00
24.98
B


4773
CA
GLU
256
0.400
26.312
75.484
1.00
28.54
B


4774
CB
GLU
256
1.353
25.581
76.416
1.00
28.97
B


4775
CG
GLU
256
1.916
24.280
75.757
1.00
32.11
B


4776
CD
GLU
256
2.856
23.589
76.744
1.00
34.01
B


4777
OE1
GLU
256
3.578
24.233
77.533
1.00
34.39
B


4778
OE2
GLU
256
2.934
22.359
76.755
1.00
38.83
B


4779
C
GLU
256
−0.655
25.350
74.953
1.00
30.36
B


4780
O
GLU
256
−0.459
24.781
73.858
1.00
29.20
B


4781
N
LYS
257
−1.807
25.254
75.618
1.00
29.61
B


4782
CA
LYS
257
−2.880
24.389
75.134
1.00
31.41
B


4783
CB
LYS
257
−3.962
24.226
76.251
1.00
33.87
B


4784
CG
LYS
257
−4.745
25.533
76.410
1.00
37.41
B


4785
CD
LYS
257
−5.474
25.653
77.752
1.00
40.71
B


4786
CE
LYS
257
−6.368
26.895
77.668
1.00
42.65
B


4787
NZ
LYS
257
−7.353
26.923
78.786
1.00
44.31
B


4788
C
LYS
257
−3.592
24.923
73.907
1.00
28.64
B


4789
O
LYS
257
−4.535
24.304
73.415
1.00
30.31
B


4790
N
ALA
258
−3.389
26.174
73.532
1.00
26.22
B


4791
CA
ALA
258
−4.085
26.740
72.402
1.00
26.57
B


4792
CB
ALA
258
−3.496
28.091
72.058
1.00
25.14
B


4793
C
ALA
258
−3.971
25.820
71.162
1.00
25.74
B


4794
O
ALA
258
−4.987
25.614
70.519
1.00
23.24
B


4795
N
MET
259
−2.743
25.414
70.804
1.00
24.83
B


4796
CA
MET
259
−2.558
24.626
69.586
1.00
24.97
B


4797
C
MET
259
−1.424
23.629
69.654
1.00
22.87
B


4798
O
MET
259
−0.266
23.943
69.985
1.00
21.95
B


4799
CB
MET
259
−2.372
25.468
68.335
1.00
27.17
B


4800
CG
MET
259
−2.036
26.893
68.507
1.00
31.07
B


4801
SD
MET
259
−1.716
27.869
67.058
1.00
27.58
B


4802
CE
MET
259
−2.943
29.164
67.238
1.00
27.63
B


4803
N
LYS
260
−1.799
22.390
69.465
1.00
20.37
B


4804
CA
LYS
260
−0.861
21.301
69.406
1.00
22.25
B


4805
CB
LYS
260
−0.885
20.387
70.631
1.00
25.95
B


4806
CG
LYS
260
−0.545
21.132
71.927
1.00
29.48
B


4807
CD
LYS
260
−0.438
20.128
73.087
1.00
31.73
B


4808
CE
LYS
260
−0.473
20.914
74.395
1.00
34.61
B


4809
NZ
LYS
260
0.575
20.474
75.367
1.00
37.61
B


4810
C
LYS
260
−1.180
20.491
68.149
1.00
23.25
B


4811
O
LYS
260
−2.358
20.209
67.870
1.00
22.97
B


4812
N
LEU
261
−0.140
20.192
67.388
1.00
18.66
B


4813
CA
LEU
261
−0.314
19.380
66.160
1.00
19.19
B


4814
CB
LEU
261
−0.311
20.232
64.885
1.00
17.81
B


4815
CG
LEU
261
−1.332
21.363
64.779
1.00
19.40
B


4816
CD2
LEU
261
−1.651
21.592
63.295
1.00
20.42
B


4817
CD1
LEU
261
−0.745
22.621
65.381
1.00
19.17
B


4818
C
LEU
261
0.833
18.400
66.123
1.00
16.88
B


4819
O
LEU
261
1.988
18.807
66.270
1.00
14.68
B


4820
N
HIS
262
0.554
17.117
66.085
1.00
16.56
B


4821
CA
HIS
262
1.503
16.049
66.123
1.00
15.24
B


4822
ND1
HIS
262
1.625
16.568
69.085
1.00
19.24
B


4823
CG
HIS
262
0.770
15.663
68.504
1.00
19.32
B


4824
CB
HIS
262
1.044
15.004
67.169
1.00
17.45
B


4825
NE2
HIS
262
−0.141
16.475
70.325
1.00
19.03
B


4826
CD2
HIS
262
−0.390
15.677
69.229
1.00
20.60
B


4827
CE1
HIS
262
1.076
16.990
70.237
1.00
20.53
B


4828
C
HIS
262
1.577
15.306
64.756
1.00
18.43
B


4829
O
HIS
262
0.525
15.030
64.192
1.00
18.48
B


4830
N
LEU
263
2.791
14.947
64.349
1.00
17.35
B


4831
CA
LEU
263
2.932
14.217
63.051
1.00
18.01
B


4832
CB
LEU
263
4.127
14.711
62.235
1.00
18.24
B


4833
CG
LEU
263
4.232
14.166
60.785
1.00
20.07
B


4834
CD2
LEU
263
5.537
14.610
60.120
1.00
19.19
B


4835
CD1
LEU
263
3.068
14.736
59.968
1.00
18.51
B


4836
C
LEU
263
2.954
12.737
63.327
1.00
15.51
B


4837
O
LEU
263
3.868
12.177
63.915
1.00
18.64
B


4838
N
ARG
264
1.810
12.079
63.059
1.00
16.36
B


4839
CA
ARG
264
1.621
10.682
63.421
1.00
17.97
B


4840
CB
ARG
264
0.401
10.622
64.354
1.00
18.60
B


4841
CG
ARG
264
0.297
11.651
65.444
1.00
22.94
B


4842
CD
ARG
264
1.329
11.371
66.546
1.00
22.99
B


4843
NE
ARG
264
0.805
10.246
67.392
1.00
22.21
B


4844
CZ
ARG
264
1.569
9.755
68.375
1.00
23.91
B


4845
NH1
ARG
264
2.772
10.312
68.609
1.00
21.04
B


4846
NH2
ARG
264
1.170
8.752
69.133
1.00
23.70
B


4847
C
ARG
264
1.321
9.833
62.183
1.00
18.71
B


4848
O
ARG
264
1.180
10.358
61.045
1.00
19.40
B


4849
N
GLU
265
1.144
8.552
62.383
1.00
18.65
B


4850
CA
GLU
265
0.868
7.619
61.297
1.00
20.01
B


4851
CB
GLU
265
0.747
6.181
61.842
1.00
18.81
B


4852
CG
GLU
265
2.094
5.619
62.323
1.00
20.62
B


4853
CD
GLU
265
1.927
4.549
63.405
1.00
22.60
B


4854
OE1
GLU
265
0.932
3.802
63.364
1.00
22.66
B


4855
OE2
GLU
265
2.845
4.350
64.218
1.00
20.42
B


4856
C
GLU
265
−0.401
8.001
60.524
1.00
19.67
B


4857
O
GLU
265
−0.517
7.643
59.349
1.00
19.98
B


4858
N
GLY
266
−1.349
8.705
61.111
1.00
19.90
B


4859
CA
GLY
266
−2.585
9.157
60.528
1.00
19.35
B


4860
C
GLY
266
−2.557
10.572
59.965
1.00
19.40
B


4861
O
GLY
266
−3.581
11.135
59.554
1.00
19.85
B


4862
N
GLY
267
−1.365
11.167
59.892
1.00
19.43
B


4863
CA
GLY
267
−1.241
12.525
59.343
1.00
20.17
B


4864
C
GLY
267
−0.946
13.511
60.478
1.00
20.17
B


4865
O
GLY
267
−0.585
13.130
61.594
1.00
19.59
B


4866
N
LEU
268
−0.988
14.789
60.178
1.00
18.97
B


4867
CA
LEU
268
−0.762
15.841
61.152
1.00
21.63
B


4868
CB
LEU
268
−0.402
17.137
60.429
1.00
19.78
B


4869
CG
LEU
268
−0.074
18.357
61.290
1.00
20.29
B


4870
CD2
LEU
268
0.211
19.555
60.382
1.00
18.85
B


4871
CD1
LEU
268
1.119
18.054
62.234
1.00
16.00
B


4872
C
LEU
268
−2.057
16.011
61.959
1.00
22.49
B


4873
O
LEU
268
−3.049
16.446
61.351
1.00
23.93
B


4874
N
THR
269
−2.042
15.706
63.255
1.00
20.56
B


4875
CA
THR
269
−3.252
15.807
64.064
1.00
21.29
B


4876
CB
THR
269
−3.154
14.968
65.379
1.00
21.74
B


4877
OG1
THR
269
−2.214
15.681
66.180
1.00
20.22
B


4878
CG2
THR
269
−2.629
13.582
65.127
1.00
22.50
B


4879
C
THR
269
−3.500
17.219
64.544
1.00
24.25
B


4880
O
THR
269
−2.571
18.012
64.488
1.00
24.29
B


4881
N
PHE
270
−4.688
17.529
65.067
1.00
25.87
B


4882
CA
PHE
270
−5.070
18.864
65.476
1.00
31.34
B


4883
CB
PHE
270
−6.166
19.305
64.483
1.00
35.31
B


4884
CG
PHE
270
−5.748
20.288
63.453
1.00
37.32
B


4885
CD1
PHE
270
−5.602
19.976
62.109
1.00
41.39
B


4886
CD2
PHE
270
−5.516
21.582
63.840
1.00
38.00
B


4887
CE1
PHE
270
−5.182
20.955
61.208
1.00
41.19
B


4888
CE2
PHE
270
−5.119
22.571
62.989
1.00
39.05
B


4889
CZ
PHE
270
−4.930
22.227
61.676
1.00
41.09
B


4890
C
PHE
270
−5.676
18.977
66.873
1.00
34.01
B


4891
O
PHE
270
−6.331
18.047
67.412
1.00
35.09
B


4892
N
GLN
271
−5.144
19.903
67.662
1.00
32.32
B


4893
CA
GLN
271
−5.707
20.246
68.971
1.00
30.70
B


4894
CB
GLN
271
−4.865
19.770
70.136
1.00
34.37
B


4895
CG
GLN
271
−5.390
20.206
71.513
1.00
38.69
B


4896
CD
GLN
271
−4.616
19.515
72.638
1.00
39.85
B


4897
OE1
GLN
271
−4.175
18.365
72.522
1.00
40.73
B


4898
NE2
GLN
271
−4.417
20.204
73.761
1.00
40.59
B


4899
C
GLN
271
−5.804
21.760
68.944
1.00
29.55
B


4900
O
GLN
271
−4.772
22.432
68.988
1.00
30.22
B


4901
N
LEU
272
−6.971
22.329
68.747
1.00
26.55
B


4902
CA
LEU
272
−7.183
23.742
68.583
1.00
28.69
B


4903
CB
LEU
272
−7.720
24.105
67.203
1.00
31.23
B


4904
CG
LEU
272
−7.246
25.228
66.324
1.00
36.49
B


4905
CD2
LEU
272
−6.759
26.504
67.004
1.00
36.59
B


4906
CD1
LEU
272
−8.320
25.592
65.271
1.00
36.39
B


4907
C
LEU
272
−8.238
24.220
69.595
1.00
28.44
B


4908
O
LEU
272
−9.415
23.843
69.455
1.00
24.19
B


4909
N
HIS
273
−7.736
25.027
70.534
1.00
25.56
B


4910
CA
HIS
273
−8.663
25.539
71.542
1.00
26.63
B


4911
ND1
HIS
273
−8.590
25.102
74.753
1.00
34.69
B


4912
CG
HIS
273
−8.633
26.161
73.892
1.00
32.95
B


4913
CB
HIS
273
−7.797
26.215
72.646
1.00
28.30
B


4914
NE2
HIS
273
−10.052
26.478
75.526
1.00
35.08
B


4915
CD2
HIS
273
−9.561
27.046
74.366
1.00
33.09
B


4916
CE1
HIS
273
−9.453
25.329
75.739
1.00
34.70
B


4917
C
HIS
273
−9.624
26.565
71.014
1.00
24.27
B


4918
O
HIS
273
−9.253
27.528
70.305
1.00
21.53
B


4919
N
ARG
274
−10.897
26.506
71.421
1.00
26.35
B


4920
CA
ARG
274
−11.885
27.498
70.993
1.00
26.02
B


4921
CB
ARG
274
−13.299
27.078
71.470
1.00
30.33
B


4922
CG
ARG
274
−14.406
27.884
70.784
1.00
34.79
B


4923
CD
ARG
274
−15.809
27.333
71.119
1.00
37.50
B


4924
NE
ARG
274
−16.871
28.118
70.487
1.00
38.88
B


4925
CZ
ARG
274
−18.172
27.994
70.777
1.00
40.68
B


4926
NH1
ARG
274
−18.541
27.099
71.700
1.00
39.89
B


4927
NH2
ARG
274
−19.089
28.742
70.154
1.00
38.89
B


4928
C
ARG
274
−11.588
28.907
71.456
1.00
23.71
B


4929
O
ARG
274
−12.007
29.877
70.823
1.00
22.59
B


4930
N
ASP
275
−10.768
29.152
72.483
1.00
23.58
B


4931
CA
ASP
275
−10.497
30.501
72.936
1.00
24.04
B


4932
CB
ASP
275
−10.343
30.538
74.465
1.00
27.42
B


4933
CG
ASP
275
−11.632
30.300
75.239
1.00
31.03
B


4934
OD1
ASP
275
−12.743
30.473
74.687
1.00
32.66
B


4935
OD2
ASP
275
−11.456
29.933
76.422
1.00
33.99
B


4936
C
ASP
275
−9.237
31.107
72.328
1.00
22.28
B


4937
O
ASP
275
−8.887
32.239
72.671
1.00
20.30
B


4938
N
VAL
276
−8.754
30.506
71.227
1.00
21.31
B


4939
CA
VAL
276
−7.590
31.114
70.567
1.00
18.63
B


4940
CB
VAL
276
−7.141
30.306
69.325
1.00
19.27
B


4941
CG1
VAL
276
−6.304
31.145
68.349
1.00
21.02
B


4942
CG2
VAL
276
−6.400
29.081
69.808
1.00
18.70
B


4943
C
VAL
276
−7.785
32.552
70.267
1.00
15.46
B


4944
O
VAL
276
−6.921
33.346
70.606
1.00
16.12
B


4945
N
PRO
277
−8.904
33.001
69.692
1.00
17.02
B


4946
CA
PRO
277
−9.088
34.406
69.391
1.00
18.84
B


4947
CD
PRO
277
−10.016
32.159
69.207
1.00
17.63
B


4948
CB
PRO
277
−10.521
34.464
68.820
1.00
19.05
B


4949
CG
PRO
277
−10.718
33.106
68.215
1.00
18.29
B


4950
C
PRO
277
−8.906
35.279
70.621
1.00
19.45
B


4951
O
PRO
277
−8.372
36.389
70.553
1.00
18.40
B


4952
N
LEU
278
−9.543
34.876
71.735
1.00
19.69
B


4953
CA
LEU
278
−9.411
35.668
72.990
1.00
20.31
B


4954
CB
LEU
278
−10.361
35.068
74.035
1.00
22.50
B


4955
CG
LEU
278
−11.868
35.358
73.838
1.00
25.67
B


4956
CD2
LEU
278
−12.104
36.848
73.863
1.00
26.14
B


4957
CD1
LEU
278
−12.735
34.631
74.880
1.00
25.47
B


4958
C
LEU
278
−7.994
35.648
73.520
1.00
18.30
B


4959
O
LEU
278
−7.545
36.608
74.150
1.00
19.70
B


4960
N
MET
279
−7.252
34.541
73.319
1.00
19.49
B


4961
CA
MET
279
−5.837
34.574
73.740
1.00
19.53
B


4962
CB
MET
279
−5.202
33.205
73.600
1.00
19.87
B


4963
CG
MET
279
−5.986
32.085
74.264
1.00
19.95
B


4964
SD
MET
279
−5.197
30.502
73.968
1.00
22.16
B


4965
CE
MET
279
−6.496
29.371
74.455
1.00
22.34
B


4966
C
MET
279
−5.023
35.550
72.913
1.00
21.00
B


4967
O
MET
279
−4.159
36.294
73.426
1.00
20.65
B


4968
N
VAL
280
−5.405
35.759
71.635
1.00
20.55
B


4969
CA
VAL
280
−4.738
36.800
70.853
1.00
19.11
B


4970
CB
VAL
280
−5.061
36.677
69.321
1.00
20.89
B


4971
CG1
VAL
280
−4.516
37.881
68.551
1.00
19.38
B


4972
CG2
VAL
280
−4.493
35.369
68.775
1.00
18.88
B


4973
C
VAL
280
−5.214
38.144
71.374
1.00
20.36
B


4974
O
VAL
280
−4.408
39.065
71.561
1.00
18.34
B


4975
N
ALA
281
−6.507
38.281
71.737
1.00
19.24
B


4976
CA
ALA
281
−6.975
39.620
72.148
1.00
20.88
B


4977
CB
ALA
281
−8.491
39.556
72.402
1.00
22.00
B


4978
C
ALA
281
−6.293
40.164
73.395
1.00
20.35
B


4979
O
ALA
281
−5.938
41.340
73.517
1.00
22.71
B


4980
N
LYS
282
−6.003
39.261
74.326
1.00
20.86
B


4981
CA
LYS
282
−5.389
39.607
75.600
1.00
22.27
B


4982
CB
LYS
282
−5.374
38.346
76.506
1.00
21.78
B


4983
CG
LYS
282
−4.629
38.624
77.830
1.00
25.23
B


4984
CD
LYS
282
−4.444
37.340
78.625
1.00
24.84
B


4985
CE
LYS
282
−3.471
37.568
79.802
1.00
26.57
B


4986
NZ
LYS
282
−3.093
36.253
80.366
1.00
26.17
B


4987
C
LYS
282
−3.973
40.126
75.411
1.00
23.61
B


4988
O
LYS
282
−3.455
40.929
76.190
1.00
23.04
B


4989
N
ASN
283
−3.257
39.565
74.431
1.00
22.39
B


4990
CA
ASN
283
−1.846
39.928
74.252
1.00
21.71
B


4991
CB
ASN
283
−1.121
38.583
73.976
1.00
21.25
B


4992
CG
ASH
283
−1.243
37.725
75.255
1.00
23.44
B


4993
OD1
ASN
283
−0.471
37.967
76.191
1.00
23.77
B


4994
ND2
ASN
283
−2.088
36.721
75.343
1.00
21.55
B


4995
C
ASN
283
−1.552
40.913
73.151
1.00
21.06
B


4996
O
ASN
283
−0.396
41.341
73.072
1.00
21.73
B


4997
N
ILE
284
−2.472
41.229
72.245
1.00
20.12
B


4998
CA
ILE
284
−2.068
41.940
71.020
1.00
19.95
B


4999
CB
ILE
284
−3.168
41.791
69.926
1.00
20.33
B


5000
CG2
ILE
284
−4.349
42.702
70.204
1.00
19.28
B


5001
CG1
ILE
284
−2.545
42.172
68.551
1.00
22.20
B


5002
CD1
ILE
284
−1.701
41.017
68.025
1.00
19.74
B


5003
C
ILE
284
−1.685
43.374
71.172
1.00
18.24
B


5004
O
ILE
284
−0.680
43.802
70.567
1.00
17.37
B


5005
N
GLU
285
−2.223
44.176
72.104
1.00
19.63
B


5006
CA
GLU
285
−1.807
45.548
72.254
1.00
19.85
B


5007
CB
GLU
285
−2.656
46.404
73.204
1.00
23.34
B


5008
CG
GLU
285
−4.113
46.332
72.892
1.00
28.25
B


5009
CD
GLU
285
−4.950
46.886
74.064
1.00
30.04
B


5010
OE1
GLU
285
−5.555
46.026
74.748
1.00
30.75
B


5011
OE2
GLU
285
−4.905
48.109
74.215
1.00
28.37
B


5012
C
GLU
285
−0.371
45.610
72.760
1.00
20.50
B


5013
O
GLU
285
0.354
46.521
72.328
1.00
20.03
B


5014
N
ASN
286
0.000
44.672
73.635
1.00
20.12
B


5015
CA
ASN
286
1.409
44.689
74.075
1.00
20.92
B


5016
CB
ASN
286
1.631
43.638
75.167
1.00
23.97
B


5017
CG
ASN
286
0.951
43.931
76.494
1.00
27.46
B


5018
OD1
ASN
286
0.637
45.068
76.838
1.00
30.66
B


5019
ND2
ASN
286
0.716
42.905
77.291
1.00
30.06
B


5020
C
ASN
286
2.358
44.405
72.910
1.00
18.86
B


5021
O
ASN
286
3.454
44.955
72.867
1.00
18.21
B


5022
N
ALA
287
2.023
43.529
71.960
1.00
18.22
B


5023
CA
ALA
287
2.953
43.315
70.818
1.00
20.10
B


5024
CB
ALA
287
2.511
42.080
70.016
1.00
19.75
B


5025
C
ALA
287
3.021
44.544
69.926
1.00
18.86
B


5026
O
ALA
287
4.084
44.973
69.485
1.00
21.40
B


5027
N
ALA
288
1.931
45.242
69.672
1.00
19.69
B


5028
CA
ALA
288
1.877
46.486
68.906
1.00
20.76
B


5029
CB
ALA
288
0.407
46.944
68.814
1.00
18.71
B


5030
C
ALA
288
2.708
47.586
69.534
1.00
21.70
B


5031
O
ALA
288
3.608
48.189
68.957
1.00
21.81
B


5032
N
GLU
289
2.515
47.753
70.868
1.00
23.39
B


5033
CA
GLU
289
3.205
48.774
71.637
1.00
24.00
B


5034
CB
GLU
289
2.681
48.845
73.114
1.00
27.17
B


5035
CG
GLU
289
1.232
49.280
73.130
1.00
35.05
B


5036
CD
GLU
289
0.407
49.305
74.411
1.00
39.46
B


5037
OE1
GLU
289
0.395
48.320
75.195
1.00
41.32
B


5038
OE2
GLU
289
−0.305
50.327
74.642
1.00
40.70
B


5039
C
GLU
289
4.695
48.525
71.684
1.00
22.51
B


5040
O
GLU
289
5.466
49.478
71.569
1.00
22.73
B


5041
N
LYS
290
5.070
47.253
71.839
1.00
20.97
B


5042
CA
LYS
290
6.487
46.923
71.888
1.00
22.45
B


5043
CB
LYS
290
6.709
45.455
72.206
1.00
21.35
B


5044
CG
LYS
290
8.158
45.018
72.272
1.00
26.33
B


5045
CD
LYS
290
8.304
43.599
72.868
1.00
30.29
B


5046
CE
LYS
290
9.796
43.226
72.880
1.00
30.50
B


5047
NZ
LYS
290
9.952
41.875
73.506
1.00
31.52
B


5048
C
LYS
290
7.137
47.258
70.529
1.00
22.29
B


5049
O
LYS
290
8.279
47.671
70.537
1.00
20.37
B


5050
N
ALA
291
6.420
47.025
69.425
1.00
22.31
B


5051
CA
ALA
291
7.010
47.304
68.110
1.00
23.67
B


5052
CB
ALA
291
6.223
46.530
67.045
1.00
22.69
B


5053
C
ALA
291
7.015
48.776
67.683
1.00
22.63
B


5054
O
ALA
291
7.965
49.262
67.026
1.00
20.29
B


5055
N
LEU
292
5.959
49.466
68.074
1.00
21.09
B


5056
CA
LEU
292
5.778
50.862
67.678
1.00
22.30
B


5057
CB
LEU
292
4.285
51.008
67.371
1.00
20.82
B


5058
CG
LEU
292
3.811
50.103
66.212
1.00
22.17
B


5059
CD2
LEU
292
4.468
50.583
64.907
1.00
21.85
B


5060
CD1
LEU
292
2.295
50.171
66.117
1.00
23.60
B


5061
C
LEU
292
6.248
51.940
68.638
1.00
25.08
B


5062
O
LEU
292
6.779
53.007
68.223
1.00
21.43
B


5063
N
SER
293
6.298
51.610
69.948
1.00
24.60
B


5064
CA
SER
293
6.843
52.638
70.869
1.00
28.76
B


5065
CB
SER
293
6.729
52.236
72.353
1.00
27.81
B


5066
OG
SER
293
5.327
52.280
72.664
1.00
31.12
B


5067
C
SER
293
8.253
53.052
70.542
1.00
28.18
B


5068
O
SER
293
8.565
54.245
70.546
1.00
29.17
B


5069
N
PRO
294
9.184
52.185
70.179
1.00
30.83
B


5070
CA
PRO
294
10.532
52.588
69.789
1.00
32.60
B


5071
CD
PRO
294
9.014
50.707
70.150
1.00
30.64
B


5072
CB
PRO
294
11.221
51.289
69.374
1.00
33.07
B


5073
CG
PRO
294
10.446
50.226
70.086
1.00
32.36
B


5074
C
PRO
294
10.590
53.579
68.631
1.00
35.35
B


5075
O
PRO
294
11.626
54.234
68.415
1.00
34.68
B


5076
N
LEU
295
9.536
53.638
67.818
1.00
34.49
B


5077
CA
LEU
295
9.417
54.513
66.679
1.00
35.33
B


5078
CB
LEU
295
8.662
53.766
65.560
1.00
37.28
B


5079
CG
LEU
295
9.477
52.920
64.581
1.00
38.81
B


5080
CD2
LEU
295
8.746
51.638
64.198
1.00
39.17
B


5081
CD1
LEU
295
10.878
52.584
65.048
1.00
40.23
B


5082
C
LEU
295
8.625
55.766
67.031
1.00
34.72
B


5083
O
LEU
295
8.343
56.566
66.144
1.00
33.16
B


5084
N
GLY
296
8.207
55.888
68.297
1.00
32.08
B


5085
CA
GLY
296
7.417
57.025
68.714
1.00
30.94
B


5086
C
GLY
296
6.003
56.960
68.177
1.00
29.68
B


5087
O
GLY
296
5.339
57.979
68.025
1.00
30.58
B


5088
N
ILE
297
5.504
55.781
67.829
1.00
28.93
B


5089
CA
ILE
297
4.162
55.700
67.271
1.00
27.98
B


5090
CB
ILE
297
4.196
54.756
66.055
1.00
29.23
B


5091
CG2
ILE
297
2.770
54.493
65.608
1.00
28.73
B


5092
CG1
ILE
297
5.134
55.385
65.002
1.00
29.11
B


5093
CD1
ILE
297
5.184
54.647
63.667
1.00
29.61
B


5094
C
ILE
297
3.208
55.137
68.305
1.00
29.24
B


5095
O
ILE
297
3.448
54.026
68.774
1.00
26.04
B


5096
N
THR
298
2.129
55.872
68.586
1.00
28.94
B


5097
CA
THR
298
1.171
55.364
69.577
1.00
31.35
B


5098
CB
THR
298
1.160
56.274
70.828
1.00
33.69
B


5099
CG1
THR
298
1.076
57.636
70.377
1.00
34.34
B


5100
CG2
THR
298
2.431
56.102
71.635
1.00
34.41
B


5101
C
THR
298
−0.233
55.324
69.014
1.00
30.57
B


5102
O
THR
298
−1.145
54.760
69.629
1.00
32.05
B


5103
N
ASP
299
−0.438
55.922
67.857
1.00
29.91
B


5104
CA
ASP
299
−1.754
55.880
67.211
1.00
31.43
B


5105
CB
ASP
299
−2.025
57.228
66.540
1.00
32.66
B


5106
CG
ASP
299
−3.314
57.240
65.753
1.00
33.63
B


5107
OD1
ASP
299
−4.070
56.258
65.713
1.00
34.14
B


5108
OD2
ASP
299
−3.582
58.283
65.114
1.00
37.07
B


5109
C
ASP
299
−1.794
54.717
66.221
1.00
30.88
B


5110
O
ASP
299
−1.306
54.815
65.091
1.00
29.67
B


5111
N
TRP
300
−2.507
53.654
66.575
1.00
29.51
B


5112
CA
TRP
300
−2.663
52.451
65.798
1.00
29.64
B


5113
CB
TRP
300
−3.461
51.372
66.511
1.00
28.99
B


5114
CG
TRP
300
−3.030
51.004
67.903
1.00
32.00
B


5115
CD2
TRP
300
−1.724
51.098
68.469
1.00
31.35
B


5116
CD1
TRP
300
−3.848
50.537
68.900
1.00
30.36
B


5117
NE1
TRP
300
−3.124
50.326
70.052
1.00
30.99
B


5118
CE2
TRP
300
−1.816
50.637
69.801
1.00
33.33
B


5119
CE3
TRP
300
−0.484
51.486
67.982
1.00
33.69
B


5120
CZ2
TRP
300
−0.715
50.618
70.663
1.00
33.05
B


5121
CZ3
TRP
300
0.617
51.459
68.826
1.00
33.58
B


5122
CH2
TRP
300
0.480
51.026
70.145
1.00
34.60
B


5123
C
TRP
300
−3.291
52.646
64.410
1.00
30.15
B


5124
O
TRP
300
−3.070
51.810
63.516
1.00
27.40
B


5125
N
ASN
301
−4.042
53.738
64.235
1.00
28.62
B


5126
CA
ASN
301
−4.662
53.984
62.943
1.00
28.51
B


5127
CB
ASN
301
−5.999
54.705
63.081
1.00
29.21
B


5128
CG
ASN
301
−7.055
53.672
63.443
1.00
30.49
B


5129
OD1
ASN
301
−7.398
52.778
62.667
1.00
32.58
B


5130
ND2
ASN
301
−7.614
53.885
64.623
1.00
30.87
B


5131
C
ASN
301
−3.746
54.771
62.024
1.00
28.08
B


5132
O
ASN
301
−4.043
54.847
60.839
1.00
27.24
B


5133
N
SER
302
−2.611
55.230
62.548
1.00
27.38
B


5134
CA
SER
302
−1.657
55.926
61.691
1.00
28.99
B


5135
CB
SER
302
−0.871
56.918
62.534
1.00
29.19
B


5136
OG
SER
302
0.091
56.350
63.383
1.00
28.39
B


5137
C
SER
302
−0.742
54.941
60.948
1.00
27.37
B


5138
O
SER
302
0.178
55.410
60.274
1.00
28.02
B


5139
N
VAL
303
−0.938
53.638
61.044
1.00
26.60
B


5140
CA
VAL
303
−0.036
52.657
60.427
1.00
24.47
B


5141
CB
VAL
303
0.927
51.952
61.382
1.00
26.94
B


5142
CG1
VAL
303
1.838
52.902
62.175
1.00
26.73
B


5143
CG2
VAL
303
0.177
51.030
62.353
1.00
23.00
B


5144
C
VAL
303
−0.889
51.602
59.722
1.00
23.52
B


5145
O
VAL
303
−2.086
51.588
60.015
1.00
23.22
B


5146
N
PHE
304
−0.317
50.836
58.804
1.00
21.05
B


5147
CA
PHE
304
−1.087
49.856
58.039
1.00
22.26
B


5148
CB
PHE
304
−0.718
49.829
56.550
1.00
21.58
B


5149
CG
PHE
304
0.724
49.572
56.199
1.00
22.76
B


5150
CD1
PHE
304
1.655
50.599
56.139
1.00
22.21
B


5151
CD2
PHE
304
1.141
48.296
55.854
1.00
25.40
B


5152
CE1
PHE
304
2.966
50.345
55.832
1.00
22.11
B


5153
CE2
PHE
304
2.477
48.048
55.529
1.00
24.12
B


5154
CZ
PHE
304
3.393
49.072
55.509
1.00
23.69
B


5155
C
PHE
304
−0.838
48.507
58.695
1.00
23.31
B


5156
O
PHE
304
0.151
48.437
59.448
1.00
24.50
B


5157
N
TRP
305
−1.717
47.552
58.594
1.00
23.36
B


5158
CA
TRP
305
−1.655
46.298
59.330
1.00
24.97
B


5159
CB
TRP
305
−2.870
46.216
60.328
1.00
24.89
B


5160
CG
TRP
305
−2.765
47.319
61.334
1.00
25.03
B


5161
CD2
TRP
305
−2.010
47.280
62.562
1.00
25.82
B


5162
CD1
TRP
305
−3.232
48.600
61.221
1.00
25.61
B


5163
NE1
TRP
305
−2.827
49.342
62.298
1.00
24.83
B


5164
CE2
TRP
305
−2.106
48.538
63.149
1.00
24.79
B


5165
CE3
TRP
305
−1.288
46.258
63.219
1.00
24.79
B


5166
CZ2
TRP
305
−1.483
48.842
64.367
1.00
26.05
B


5167
CZ3
TRP
305
−0.721
46.562
64.445
1.00
24.46
B


5168
CH2
TRP
305
−0.777
47.838
64.998
1.00
25.19
B


5169
C
TRP
305
−1.787
45.096
58.424
1.00
24.85
B


5170
O
TRP
305
−2.672
45.104
57.578
1.00
26.94
B


5171
N
MET
306
−0.972
44.077
58.531
1.00
21.95
B


5172
CA
MET
306
−1.054
42.816
57.822
1.00
21.34
B


5173
CB
MET
306
0.209
42.563
56.995
1.00
21.09
B


5174
CG
MET
306
0.421
43.672
55.972
1.00
20.03
B


5175
SD
MET
306
2.139
44.089
55.648
1.00
22.51
B


5176
CE
MET
306
2.495
45.049
57.167
1.00
26.87
B


5177
C
MET
306
−1.211
41.711
58.880
1.00
20.66
B


5178
O
MET
306
−0.221
41.358
59.534
1.00
20.48
B


5179
N
VAL
307
−2.402
41.163
59.023
1.00
20.73
B


5180
CA
VAL
307
−2.707
40.294
60.137
1.00
18.05
B


5181
CB
VAL
307
−3.902
40.811
61.011
1.00
17.93
B


5182
CG1
VAL
307
−4.095
39.898
62.206
1.00
18.14
B


5183
CG2
VAL
307
−3.687
42.236
61.425
1.00
18.06
B


5184
C
VAL
307
−3.014
38.909
59.662
1.00
18.96
B


5185
O
VAL
307
−3.948
38.717
58.893
1.00
19.14
B


5186
N
HIS
308
−2.203
37.946
60.168
1.00
17.07
B


5187
CA
HIS
308
−2.425
36.566
59.814
1.00
17.63
B


5188
ND1
HIS
308
−1.407
33.596
58.952
1.00
17.99
B


5189
CG
HIS
308
−1.774
34.169
60.146
1.00
17.55
B


5190
CB
HIS
308
−1.500
35.594
60.541
1.00
16.64
B


5191
NE2
HIS
308
−2.452
32.080
60.105
1.00
19.33
B


5192
CD2
HIS
308
−2.392
33.200
60.862
1.00
16.86
B


5193
CE1
HIS
308
−1.784
32.330
58.955
1.00
20.71
B


5194
C
HIS
308
−3.862
36.171
60.146
1.00
20.15
B


5195
O
HIS
308
−4.196
36.218
61.336
1.00
20.31
B


5196
N
PRO
309
−4.609
35.703
59.157
1.00
19.60
B


5197
CA
PRO
309
−6.036
35.406
59.367
1.00
18.69
B


5198
CD
PRO
309
−4.216
35.666
57.711
1.00
17.25
B


5199
CB
PRO
309
−6.662
35.672
57.992
1.00
18.47
B


5200
CG
PRO
309
−5.542
35.330
57.035
1.00
19.57
B


5201
C
PRO
309
−6.227
34.020
59.848
1.00
17.62
B


5202
O
PRO
309
−6.848
33.191
59.186
1.00
20.03
B


5203
N
GLY
310
−5.701
33.632
61.041
1.00
18.19
B


5204
CA
GLY
310
−5.794
32.245
61.493
1.00
15.27
B


5205
C
GLY
310
−7.267
31.831
61.383
1.00
15.92
B


5206
O
GLY
310
−7.560
30.671
61.100
1.00
16.29
B


5207
N
GLY
311
−8.160
32.765
61.656
1.00
17.99
B


5208
CA
GLY
311
−9.596
32.551
61.436
1.00
20.00
B


5209
C
GLY
311
−10.183
33.951
61.373
1.00
19.56
B


5210
O
GLY
311
−9.534
34.864
61.873
1.00
20.74
B


5211
N
ARG
312
−11.407
34.144
60.868
1.00
20.47
B


5212
CA
ARG
312
−12.059
35.449
60.868
1.00
21.63
B


5213
CB
ARG
312
−13.527
35.256
60.375
1.00
24.00
B


5214
CG
ARG
312
−14.198
36.603
60.071
1.00
24.43
B


5215
CD
ARG
312
−15.709
36.524
60.340
1.00
28.53
B


5216
NE
ARG
312
−15.986
36.682
61.777
1.00
29.01
B


5217
CZ
ARG
312
−16.395
35.674
62.557
1.00
30.38
B


5218
NH1
ARG
312
−16.772
34.499
62.084
1.00
29.87
B


5219
NH2
ARG
312
−16.516
35.880
63.870
1.00
29.12
B


5220
C
ARG
312
−12.135
36.173
62.222
1.00
20.82
B


5221
O
ARG
312
−11.958
37.366
62.433
1.00
21.21
B


5222
N
ALA
313
−12.359
35.383
63.262
1.00
21.23
B


5223
CA
ALA
313
−12.522
35.849
64.666
1.00
22.59
B


5224
CB
ALA
313
−13.057
34.734
65.538
1.00
20.95
B


5225
C
ALA
313
−11.200
36.359
65.219
1.00
20.52
B


5226
O
ALA
313
−11.195
37.326
65.970
1.00
21.79
B


5227
N
ILE
314
−10.091
35.774
64.710
1.00
20.33
B


5228
CA
ILE
314
−8.813
36.388
65.138
1.00
20.36
B


5229
CB
ILE
314
−7.647
35.495
64.674
1.00
20.12
B


5230
CG2
ILE
314
−6.334
36.309
64.729
1.00
21.33
B


5231
CG1
ILE
314
−7.638
34.216
65.466
1.00
20.77
B


5232
CD1
ILE
314
−6.582
33.203
65.035
1.00
24.17
B


5233
C
ILE
314
−8.697
37.794
64.591
1.00
20.44
B


5234
O
ILE
314
−8.270
38.752
65.252
1.00
22.07
B


5235
N
LEU
315
−9.019
37.994
63.274
1.00
20.11
B


5236
CA
LEU
315
−8.984
39.339
62.709
1.00
18.16
B


5237
CB
LEU
315
−9.481
39.390
61.240
1.00
19.31
B


5238
CG
LEU
315
−8.629
38.553
60.225
1.00
18.63
B


5239
CD2
LEU
315
−7.183
38.975
60.278
1.00
16.29
B


5240
CD1
LEU
315
−9.181
38.712
58.804
1.00
19.25
B


5241
C
LEU
315
−9.871
40.276
63.539
1.00
18.51
B


5242
O
LEU
315
−9.550
41.443
63.803
1.00
20.92
B


5243
N
ASP
316
−11.070
39.827
63.846
1.00
17.94
B


5244
CA
ASP
316
−12.060
40.658
64.535
1.00
21.13
B


5245
CB
ASP
316
−13.352
39.852
64.669
1.00
22.57
B


5246
CG
ASP
316
−14.070
39.660
63.321
1.00
25.48
B


5247
OD1
ASP
316
−13.674
40.262
62.282
1.00
24.54
B


5248
OD2
ASP
316
−15.020
38.860
63.289
1.00
23.59
B


5249
C
ASP
316
−11.526
41.095
65.906
1.00
22.99
B


5250
O
ASP
316
−11.613
42.276
66.275
1.00
21.67
B


5251
N
GLN
317
−10.904
40.140
66.604
1.00
22.42
B


5252
CA
GLN
317
−10.360
40.506
67.953
1.00
22.73
B


5253
CB
GLN
317
−9.911
39.228
68.636
1.00
22.43
B


5254
CG
GLN
317
−11.056
38.391
69.222
1.00
23.87
B


5255
CD
GLN
317
−11.747
39.122
70.380
1.00
24.67
B


5256
OE1
GLN
317
−11.435
40.246
70.782
1.00
23.10
B


5257
NE2
GLN
317
−12.762
38.460
70.919
1.00
26.57
B


5258
C
GLN
317
−9.238
41.497
67.816
1.00
23.11
B


5259
O
GLN
317
−9.156
42.493
68.549
1.00
23.40
B


5260
N
VAL
318
−8.397
41.338
66.756
1.00
22.30
B


5261
CA
VAL
318
−7.305
42.320
66.610
1.00
21.68
B


5262
CB
VAL
318
−6.277
41.896
65.529
1.00
20.13
B


5263
CG1
VAL
318
−5.305
43.002
65.214
1.00
19.83
B


5264
CG2
VAL
318
−5.580
40.612
65.982
1.00
21.31
B


5265
C
VAL
318
−7.865
43.688
66.335
1.00
21.70
B


5266
O
VAL
318
−7.373
44.694
66.872
1.00
19.93
B


5267
N
GLU
319
−8.872
43.758
65.412
1.00
21.94
B


5268
CA
GLU
319
−9.491
45.053
65.091
1.00
23.27
B


5269
CB
GLU
319
−10.589
44.781
64.056
1.00
26.24
B


5270
CG
GLU
319
−11.395
45.943
63.519
1.00
29.12
B


5271
CD
GLU
319
−12.405
45.393
62.505
1.00
32.43
B


5272
OE1
GLU
319
−12.103
45.337
61.287
1.00
32.08
B


5273
OE2
GLU
319
−13.434
44.837
62.945
1.00
33.65
B


5274
C
GLU
319
−10.168
45.698
66.325
1.00
22.56
B


5275
O
GLU
319
−9.996
46.893
66.538
1.00
21.16
B


5276
N
ARG
320
−10.779
44.858
67.154
1.00
21.69
B


5277
CA
ARG
320
−11.410
45.381
68.390
1.00
23.35
B


5278
CB
ARG
320
−12.202
44.246
69.060
1.00
23.74
B


5279
CG
ARG
320
−12.782
44.760
70.420
1.00
25.66
B


5280
CD
ARG
320
−13.698
43.703
71.016
1.00
25.35
B


5281
NE
ARG
320
−12.941
42.596
71.621
1.00
26.01
B


5282
CZ
ARG
320
−12.502
42.520
72.886
1.00
25.36
B


5283
NH1
ARG
320
−12.793
43.513
73.735
1.00
22.52
B


5284
NH2
ARG
320
−11.849
41.417
73.296
1.00
22.41
B


5285
C
ARG
320
−10.374
45.888
69.365
1.00
24.31
B


5286
O
ARG
320
−10.303
47.082
69.618
1.00
25.73
B


5287
N
LYS
321
−9.399
45.049
69.751
1.00
24.51
B


5288
CA
LYS
321
−8.379
45.431
70.734
1.00
25.04
B


5289
CB
LYS
321
−7.697
44.101
71.190
1.00
26.27
B


5290
CG
LYS
321
−8.653
43.378
72.207
1.00
26.39
B


5291
CD
LYS
321
−8.195
43.887
73.557
1.00
30.28
B


5292
CE
LYS
321
−9.029
43.942
74.743
1.00
31.04
B


5293
NZ
LYS
321
−9.608
45.187
75.225
1.00
33.95
B


5294
C
LYS
321
−7.472
46.540
70.285
1.00
26.90
B


5295
O
LYS
321
−7.150
47.466
71.081
1.00
23.68
B


5296
N
LEU
322
−7.238
46.718
68.961
1.00
23.57
B


5297
CA
LEU
322
−6.435
47.852
68.517
1.00
24.43
B


5298
CB
LEU
322
−5.438
47.544
67.382
1.00
24.57
B


5299
CG
LEU
322
−4.381
46.474
67.731
1.00
25.26
B


5300
CD2
LEU
322
−3.464
46.950
68.854
1.00
25.41
B


5301
CD1
LEU
322
−3.551
46.075
66.505
1.00
25.95
B


5302
C
LEU
322
−7.332
49.018
68.132
1.00
23.91
B


5303
O
LEU
322
−6.806
50.057
67.724
1.00
22.61
B


5304
N
ASN
323
−8.653
48.845
68.240
1.00
25.03
B


5305
CA
ASN
323
−9.538
49.965
67.936
1.00
28.29
B


5306
CB
ASN
323
−9.422
51.126
68.954
1.00
31.89
B


5307
CG
ASN
323
−10.763
51.879
68.879
1.00
37.60
B


5308
OD1
ASN
323
−10.786
53.101
68.699
1.00
39.93
B


5309
ND2
ASN
323
−11.895
51.176
68.964
1.00
38.45
B


5310
C
ASN
323
−9.313
50.519
66.521
1.00
28.33
B


5311
O
ASN
323
−9.227
51.714
66.293
1.00
25.80
B


5312
N
LEU
324
−9.202
49.604
65.567
1.00
28.13
B


5313
CA
LEU
324
−8.933
49.902
64.180
1.00
29.48
B


5314
CB
LEU
324
−8.423
48.575
63.569
1.00
28.51
B


5315
CG
LEU
324
−6.923
48.372
63.396
1.00
30.27
B


5316
CD2
LEU
324
−6.565
46.882
63.341
1.00
28.32
B


5317
CD1
LEU
324
−6.002
49.137
64.326
1.00
27.79
B


5318
C
LEU
324
−10.181
50.368
63.448
1.00
29.19
B


5319
O
LEU
324
−11.238
49.776
63.601
1.00
27.17
B


5320
N
LYS
325
−10.039
51.350
62.562
1.00
33.48
B


5321
CA
LYS
325
−11.117
51.696
61.640
1.00
34.34
B


5322
CB
LYS
325
−10.679
52.796
60.698
1.00
36.67
B


5323
CG
LYS
325
−10.462
54.151
61.347
1.00
40.37
B


5324
CD
LYS
325
−10.216
55.199
60.259
1.00
43.88
B


5325
CE
LYS
325
−8.958
56.003
60.542
1.00
45.94
B


5326
NZ
LYS
325
−8.243
56.352
59.268
1.00
48.86
B


5327
C
LYS
325
−11.489
50.437
60.864
1.00
36.02
B


5328
O
LYS
325
−10.691
49.501
60.657
1.00
32.28
B


5329
N
GLU
326
−12.735
50.396
60.397
1.00
36.53
B


5330
CA
GLU
326
−13.322
49.268
59.705
1.00
38.57
B


5331
CB
GLU
326
−14.808
49.610
59.371
1.00
42.33
B


5332
CG
GLU
326
−15.651
49.277
60.588
1.00
48.46
B


5333
CD
GLU
326
−16.884
50.070
60.959
1.00
50.98
B


5334
OE1
GLU
326
−17.559
50.689
60.096
1.00
52.47
B


5335
OE2
GLU
326
−17.211
50.069
62.179
1.00
52.37
B


5336
C
GLU
326
−12.635
48.741
58.449
1.00
35.41
B


5337
O
GLU
326
−12.849
47.584
58.079
1.00
33.05
B


5338
N
ASP
327
−11.855
49.565
57.779
1.00
33.65
B


5339
CA
ASP
327
−11.150
49.105
56.597
1.00
36.31
B


5340
CB
ASP
327
−11.257
50.183
55.507
1.00
39.96
B


5341
CG
ASP
327
−10.669
51.502
55.930
1.00
45.67
B


5342
OD1
ASP
327
−10.291
51.751
57.100
1.00
48.30
B


5343
OD2
ASP
327
−10.657
52.409
55.062
1.00
49.05
B


5344
C
ASP
327
−9.693
48.777
56.864
1.00
32.45
B


5345
O
ASP
327
−9.055
48.309
55.915
1.00
30.64
B


5346
N
LYS
328
−9.167
49.007
58.082
1.00
28.05
B


5347
CA
LYS
328
−7.747
48.697
58.273
1.00
25.57
B


5348
CB
LYS
328
−7.294
49.051
59.709
1.00
25.04
B


5349
CG
LYS
328
−7.158
50.594
59.741
1.00
26.94
B


5350
CD
LYS
328
−5.687
50.955
59.478
1.00
26.71
B


5351
CE
LYS
328
−5.597
52.434
59.374
1.00
30.21
B


5352
NZ
LYS
328
−4.359
52.984
58.773
1.00
29.75
B


5353
C
LYS
328
−7.367
47.293
57.853
1.00
22.32
B


5354
O
LYS
328
−6.269
47.121
57.305
1.00
21.65
B


5355
N
LEU
329
−8.165
46.286
58.130
1.00
19.10
B


5356
CA
LEU
329
−7.811
44.905
57.824
1.00
20.35
B


5357
CB
LEU
329
−8.246
43.988
58.953
1.00
20.66
B


5358
CG
LEU
329
−7.625
44.367
60.337
1.00
22.03
B


5359
CD2
LEU
329
−6.111
44.528
60.248
1.00
22.71
B


5360
CD1
LEU
329
−8.061
43.297
61.325
1.00
23.16
B


5361
C
LEU
329
−8.349
44.383
56.493
1.00
20.28
B


5362
O
LEU
329
−8.392
43.197
56.280
1.00
19.00
B


5363
N
ARG
330
−8.760
45.279
55.610
1.00
23.20
B


5364
CA
ARG
330
−9.284
44.875
54.303
1.00
24.04
B


5365
CB
ARG
330
−9.453
46.132
53.424
1.00
26.77
B


5366
CG
ARG
330
−10.046
45.772
52.057
1.00
31.36
B


5367
CD
ARG
330
−9.558
46.633
50.901
1.00
33.97
B


5368
NE
ARG
330
−8.123
46.497
50.624
1.00
35.77
B


5369
CZ
ARG
330
−7.493
45.536
49.966
1.00
37.17
B


5370
NH1
ARG
330
−6.168
45.684
49.904
1.00
36.94
B


5371
NH2
ARG
330
−8.130
44.507
49.416
1.00
35.70
B


5372
C
ARG
330
−8.352
43.901
53.612
1.00
21.92
B


5373
O
ARG
330
−8.758
42.840
53.148
1.00
23.05
B


5374
N
ALA
331
−7.062
44.251
53.487
1.00
23.62
B


5375
CA
ALA
331
−6.152
43.396
52.711
1.00
22.13
B


5376
CB
ALA
331
−4.805
44.092
52.541
1.00
20.83
B


5377
C
ALA
331
−6.005
42.026
53.326
1.00
22.56
B


5378
O
ALA
331
−5.973
41.014
52.634
1.00
19.86
B


5379
N
SER
332
−6.054
41.933
54.683
1.00
20.56
B


5380
CA
SER
332
−5.993
40.664
55.376
1.00
18.63
B


5381
CB
SER
332
−5.796
40.926
56.918
1.00
19.54
B


5382
OG
SER
332
−4.538
41.563
57.076
1.00
21.55
B


5383
C
SER
332
−7.257
39.866
55.187
1.00
17.66
B


5384
O
SER
332
−7.263
38.648
54.994
1.00
17.37
B


5385
N
ARG
333
−8.407
40.587
55.268
1.00
17.66
B


5386
CA
ARG
333
−9.653
39.840
55.053
1.00
19.55
B


5387
CB
ARG
333
−10.859
40.731
55.411
1.00
22.26
B


5388
CG
ARG
333
−10.991
41.072
56.906
1.00
22.49
B


5389
CD
ARG
333
−12.232
41.922
57.195
1.00
23.61
B


5390
NE
ARG
333
−12.174
42.505
58.557
1.00
23.67
B


5391
CZ
ARG
333
−12.452
41.727
59.616
1.00
21.99
B


5392
NH1
ARG
333
−12.806
40.459
59.458
1.00
20.57
B


5393
NH2
ARG
333
−12.376
42.243
60.844
1.00
23.81
B


5394
C
ARG
333
−9.750
39.432
53.566
1.00
17.99
B


5395
O
ARG
333
−10.373
38.431
53.266
1.00
17.75
B


5396
N
HIS
334
−9.270
40.276
52.665
1.00
20.00
B


5397
CA
HIS
334
−9.342
39.895
51.221
1.00
21.81
B


5398
ND1
HIS
334
−9.552
41.251
48.032
1.00
29.33
B


5399
CG
HIS
334
−8.665
40.805
48.969
1.00
27.40
B


5400
CB
HIS
334
−8.819
41.098
50.436
1.00
24.11
B


5401
NE2
HIS
334
−8.080
40.166
46.964
1.00
29.21
B


5402
CD2
HIS
334
−7.713
40.103
48.291
1.00
27.91
B


5403
CE1
HIS
334
−9.180
40.853
46.829
1.00
29.04
B


5404
C
HIS
334
−8.591
38.606
50.922
1.00
20.31
B


5405
O
HIS
334
−9.089
37.653
50.282
1.00
18.30
B


5406
N
VAL
335
−7.370
38.457
51.474
1.00
18.88
B


5407
CA
VAL
335
−6.608
37.204
51.276
1.00
18.05
B


5408
CB
VAL
335
−5.172
37.361
51.835
1.00
16.25
B


5409
CG1
VAL
335
−4.408
36.038
51.905
1.00
14.81
B


5410
CG2
VAL
335
−4.370
38.358
51.024
1.00
17.43
B


5411
C
VAL
335
−7.352
36.022
51.845
1.00
18.69
B


5412
O
VAL
335
−7.462
34.911
51.264
1.00
16.92
B


5413
N
LEU
336
−7.857
36.177
53.089
1.00
18.84
B


5414
CA
LEU
336
−8.618
35.068
53.695
1.00
19.92
B


5415
CB
LEU
336
−9.112
35.538
55.092
1.00
18.93
B


5416
CG
LEU
336
−10.066
34.551
55.785
1.00
19.29
B


5417
CD2
LEU
336
−10.662
35.253
57.023
1.00
19.97
B


5418
CD1
LEU
336
−9.366
33.235
56.203
1.00
18.15
B


5419
C
LEU
336
−9.823
34.722
52.808
1.00
19.48
B


5420
O
LEU
336
−10.203
33.582
52.645
1.00
20.21
B


5421
N
SER
337
−10.528
35.740
52.296
1.00
20.81
B


5422
CA
SER
337
−11.673
35.416
51.431
1.00
23.18
B


5423
CB
SER
337
−12.370
36.729
51.034
1.00
24.45
B


5424
OG
SER
337
−13.518
36.378
50.302
1.00
26.44
B


5425
C
SER
337
−11.290
34.649
50.165
1.00
23.02
B


5426
O
SER
337
−11.873
33.600
49.897
1.00
22.24
B


5427
N
GLU
338
−10.259
35.081
49.455
1.00
22.57
B


5428
CA
GLU
338
−9.929
34.488
48.138
1.00
23.78
B


5429
CB
GLU
338
−9.131
35.534
47.340
1.00
25.65
B


5430
CG
GLU
338
−9.970
36.764
47.019
1.00
29.62
B


5431
CD
GLU
338
−11.085
36.437
46.034
1.00
33.44
B


5432
OE1
GLU
338
−11.086
35.397
45.350
1.00
34.88
B


5433
OE2
GLU
338
−12.028
37.240
45.911
1.00
35.93
B


5434
C
GLU
338
−9.093
33.245
48.215
1.00
23.79
B


5435
O
GLU
338
−9.026
32.430
47.283
1.00
22.08
B


5436
N
TYR
339
−8.427
32.976
49.366
1.00
20.54
B


5437
CA
TYR
339
−7.572
31.801
49.454
1.00
19.28
B


5438
CB
TYR
339
−6.097
32.268
49.464
1.00
20.25
B


5439
CG
TYR
339
−5.684
33.114
48.294
1.00
21.60
B


5440
CD1
TYR
339
−5.299
32.478
47.107
1.00
22.56
B


5441
CD2
TYR
339
−5.709
34.480
48.355
1.00
20.36
B


5442
CE1
TYR
339
−4.931
33.258
46.020
1.00
24.72
B


5443
CE2
TYR
339
−5.263
35.261
47.295
1.00
23.36
B


5444
CZ
TYR
339
−4.936
34.617
46.110
1.00
24.79
B


5445
OH
TYR
339
−4.534
35.348
45.019
1.00
27.21
B


5446
C
TYR
339
−7.681
30.965
50.745
1.00
19.15
B


5447
O
TYR
339
−7.009
29.946
50.763
1.00
16.70
B


5448
N
GLY
340
−8.364
31.454
51.773
1.00
19.15
B


5449
CA
GLY
340
−8.343
30.639
53.023
1.00
19.44
B


5450
C
GLY
340
−7.039
31.024
53.756
1.00
18.69
B


5451
O
GLY
340
−6.274
31.904
53.291
1.00
16.73
B


5452
N
ASN
341
−6.834
30.345
54.877
1.00
17.38
B


5453
CA
ASN
341
−5.644
30.512
55.712
1.00
17.00
B


5454
CB
ASN
341
−5.971
29.944
57.141
1.00
15.71
B


5455
CG
ASN
341
−4.786
29.996
58.098
1.00
22.10
B


5456
OD1
ASN
341
−3.607
30.225
57.760
1.00
20.41
B


5457
ND2
ASN
341
−5.035
29.790
59.417
1.00
18.04
B


5458
C
ASN
341
−4.531
29.705
55.073
1.00
12.66
B


5459
O
ASN
341
−4.573
28.497
55.103
1.00
13.74
B


5460
N
LEU
342
−3.480
30.293
54.531
1.00
13.87
B


5461
CA
LEU
342
−2.401
29.692
53.796
1.00
14.38
B


5462
CB
LEU
342
−1.947
30.703
52.713
1.00
13.53
B


5463
CG
LEU
342
−3.059
31.003
51.662
1.00
16.45
B


5464
CD2
LEU
342
−3.341
29.764
50.827
1.00
13.74
B


5465
CD1
LEU
342
−2.612
32.163
50.779
1.00
14.62
B


5466
C
LEU
342
−1.176
29.399
54.666
1.00
16.21
B


5467
O
LEU
342
−0.015
29.263
54.262
1.00
15.04
B


5468
N
ILE
343
−1.460
29.262
55.970
1.00
15.11
B


5469
CA
ILE
343
−0.383
28.954
56.925
1.00
12.87
B


5470
CB
ILE
343
−0.128
27.445
56.926
1.00
15.47
B


5471
CG2
ILE
343
0.552
27.109
58.289
1.00
17.57
B


5472
CG1
ILE
343
−1.420
26.625
56.838
1.00
14.46
B


5473
CD1
ILE
343
−1.178
25.109
56.887
1.00
16.26
B


5474
C
ILE
343
0.786
29.845
56.750
1.00
9.81
B


5475
O
ILE
343
0.620
31.104
56.721
1.00
12.86
B


5476
N
SER
344
2.035
29.387
56.667
1.00
12.79
B


5477
CA
SER
344
3.187
30.285
56.635
1.00
15.12
B


5478
CB
SER
344
4.537
29.588
56.676
1.00
17.57
B


5479
OG
SER
344
4.777
28.651
55.605
1.00
15.67
B


5480
C
SER
344
3.210
31.252
55.477
1.00
15.66
B


5481
O
SER
344
3.799
32.325
55.634
1.00
14.54
B


5482
N
ALA
345
2.565
30.927
54.352
1.00
16.70
B


5483
CA
ALA
345
2.555
31.866
53.226
1.00
18.03
B


5484
CB
ALA
345
2.162
31.047
51.946
1.00
15.91
B


5485
C
ALA
345
1.499
32.946
53.339
1.00
17.12
B


5486
O
ALA
345
1.627
33.940
52.626
1.00
17.06
B


5487
N
CYS
346
0.507
32.815
54.229
1.00
16.09
B


5488
CA
CYS
346
−0.582
33.775
54.299
1.00
16.82
B


5489
CB
CYS
346
−1.665
33.372
55.326
1.00
15.07
B


5490
SG
CYS
346
−3.346
33.982
54.889
1.00
16.25
B


5491
C
CYS
346
−0.234
35.239
54.412
1.00
16.79
B


5492
O
CYS
346
−0.687
36.081
53.561
1.00
13.66
B


5493
N
VAL
347
0.621
35.631
55.385
1.00
13.44
B


5494
CA
VAL
347
0.895
37.041
55.567
1.00
13.45
B


5495
CB
VAL
347
1.646
37.422
56.860
1.00
15.94
B


5496
CG1
VAL
347
0.748
37.144
58.075
1.00
13.87
B


5497
CG2
VAL
347
2.913
36.572
57.036
1.00
12.41
B


5498
C
VAL
347
1.700
37.559
54.355
1.00
14.78
B


5499
O
VAL
347
1.654
38.775
54.099
1.00
14.01
B


5500
N
LEU
348
2.447
36.691
53.694
1.00
15.03
B


5501
CA
LEU
348
3.216
37.183
52.508
1.00
14.71
B


5502
CB
LEU
348
4.233
36.090
52.165
1.00
13.20
B


5503
CG
LEU
348
5.101
35.645
53.362
1.00
14.08
B


5504
CD2
LEU
348
5.873
36.854
53.911
1.00
11.50
B


5505
CD1
LEU
348
6.129
34.629
52.878
1.00
13.45
B


5506
C
LEU
348
2.262
37.392
51.313
1.00
14.54
B


5507
O
LEU
348
2.382
38.426
50.654
1.00
16.63
B


5508
N
PHE
349
1.187
36.608
51.202
1.00
14.95
B


5509
CA
PHE
349
0.129
37.022
50.248
1.00
17.74
B


5510
CB
PHE
349
−1.008
36.024
50.119
1.00
15.15
B


5511
CG
PHE
349
−0.761
34.816
49.245
1.00
15.70
B


5512
CD1
PHE
349
−1.616
34.488
48.192
1.00
15.27
B


5513
CD2
PHE
349
0.314
33.972
49.493
1.00
14.11
B


5514
CE1
PHE
349
−1.368
33.348
47.444
1.00
16.03
B


5515
CE2
PHE
349
0.557
32.856
48.765
1.00
13.96
B


5516
CZ
PHE
349
−0.294
32.531
47.715
1.00
15.84
B


5517
C
PHE
349
−0.464
38.351
50.665
1.00
19.78
B


5518
O
PHE
349
−0.854
39.123
49.785
1.00
19.74
B


5519
N
ILE
350
−0.519
38.684
51.986
1.00
17.56
B


5520
CA
ILE
350
−1.132
39.939
52.372
1.00
17.74
B


5521
CB
ILE
350
−1.558
39.872
53.868
1.00
20.05
B


5522
CG2
ILE
350
−1.921
41.274
54.361
1.00
20.52
B


5523
CG1
ILE
350
−2.707
38.902
54.050
1.00
21.14
B


5524
CD1
ILE
350
−2.920
38.374
55.478
1.00
22.04
B


5525
C
ILE
350
−0.215
41.099
52.050
1.00
17.77
B


5526
O
ILE
350
−0.623
42.184
51.627
1.00
17.64
B


5527
N
ILE
351
1.112
40.911
52.209
1.00
15.39
B


5528
CA
ILE
351
2.041
41.992
51.833
1.00
17.61
B


5529
CB
ILE
351
3.483
41.508
52.029
1.00
17.55
B


5530
CG2
ILE
351
4.522
42.500
51.525
1.00
18.23
B


5531
CG1
ILE
351
3.766
41.162
53.517
1.00
19.15
B


5532
CD1
ILE
351
5.164
40.697
53.856
1.00
17.76
B


5533
C
ILE
351
1.785
42.294
50.322
1.00
18.50
B


5534
O
ILE
351
1.669
43.450
49.934
1.00
17.39
B


5535
N
ASP
352
1.656
41.234
49.549
1.00
13.85
B


5536
CA
ASP
352
1.474
41.464
48.063
1.00
19.00
B


5537
CB
ASP
352
1.548
40.106
47.393
1.00
16.36
B


5538
CG
ASP
352
1.879
40.216
45.870
1.00
17.87
B


5539
OD1
ASP
352
2.620
41.136
45.537
1.00
17.05
B


5540
OD2
ASP
352
1.552
39.234
45.190
1.00
17.08
B


5541
C
ASP
352
0.200
42.220
47.749
1.00
18.60
B


5542
O
ASP
352
0.182
43.149
46.939
1.00
21.09
B


5543
N
GLU
353
−0.875
41.885
48.453
1.00
19.67
B


5544
CA
GLU
353
−2.183
42.496
48.349
1.00
20.84
B


5545
CB
GLU
353
−3.252
41.729
49.160
1.00
17.41
B


5546
CG
GLU
353
−4.585
42.461
49.264
1.00
18.96
B


5547
CD
GLU
353
−5.299
42.580
47.896
1.00
20.82
B


5548
OE1
GLU
353
−4.986
41.788
46.991
1.00
22.39
B


5549
OE2
GLU
353
−6.170
43.442
47.721
1.00
18.42
B


5550
C
GLU
353
−2.148
43.966
48.707
1.00
21.56
B


5551
O
GLU
353
−2.645
44.865
47.990
1.00
19.49
B


5552
N
VAL
354
−1.529
44.254
49.870
1.00
21.53
B


5553
CA
VAL
354
−1.359
45.637
50.269
1.00
19.53
B


5554
CB
VAL
354
−0.630
45.761
51.630
1.00
19.84
B


5555
CG1
VAL
354
−0.323
47.206
51.960
1.00
17.36
B


5556
CG2
VAL
354
−1.557
45.178
52.690
1.00
19.82
B


5557
C
VAL
354
−0.627
46.433
49.197
1.00
20.27
B


5558
O
VAL
354
−1.080
47.545
48.852
1.00
20.16
B


5559
N
ARG
355
0.531
45.958
48.734
1.00
19.44
B


5560
CA
ARG
355
1.250
46.810
47.768
1.00
19.84
B


5561
CB
ARG
355
2.721
46.412
47.684
1.00
19.29
B


5562
CG
ARG
355
2.981
45.022
47.124
1.00
19.67
B


5563
CD
ARG
355
3.288
45.092
45.607
1.00
20.57
B


5564
NE
ARG
355
3.551
43.739
45.088
1.00
20.45
B


5565
CZ
ARG
355
4.488
43.429
44.194
1.00
21.00
B


5566
NH1
ARG
355
4.602
42.143
43.898
1.00
18.29
B


5567
NH2
ARG
355
5.350
44.316
43.658
1.00
20.14
B


5568
C
ARG
355
0.492
46.833
46.435
1.00
19.22
B


5569
O
ARG
355
0.418
47.907
45.844
1.00
20.61
B


5570
N
LYS
356
−0.157
45.763
46.019
1.00
20.34
B


5571
CA
LYS
356
−0.839
45.853
44.690
1.00
24.47
B


5572
CB
LYS
356
−1.229
44.485
44.141
1.00
21.60
B


5573
CG
LYS
356
0.070
43.739
43.786
1.00
22.62
B


5574
CD
LYS
356
−0.334
42.322
43.335
1.00
23.63
B


5575
CE
LYS
356
0.907
41.662
42.714
1.00
27.97
B


5576
NZ
LYS
356
0.502
40.324
42.167
1.00
30.54
B


5577
C
LYS
356
−2.022
46.810
44.746
1.00
25.59
B


5578
O
LYS
356
−2.201
47.685
43.892
1.00
23.97
B


5579
N
ARG
357
−2.798
46.682
45.837
1.00
25.23
B


5580
CA
ARG
357
−3.947
47.566
46.023
1.00
27.07
B


5581
CB
ARG
357
−4.781
47.087
47.204
1.00
29.98
B


5582
CG
ARG
357
−6.178
47.652
47.317
1.00
35.68
B


5583
CD
ARG
357
−7.002
47.478
46.029
1.00
38.99
B


5584
NE
ARG
357
−8.381
47.139
46.377
1.00
43.61
B


5585
CZ
ARG
357
−8.810
45.887
46.232
1.00
45.64
B


5586
NH1
ARG
357
−7.882
45.063
45.749
1.00
47.63
B


5587
NH2
ARG
357
−10.027
45.488
46.532
1.00
45.96
B


5588
C
ARG
357
−3.510
49.010
46.139
1.00
26.78
B


5589
O
ARG
357
−4.176
49.875
45.544
1.00
25.31
B


5590
N
SER
358
−2.412
49.299
46.835
1.00
22.91
B


5591
CA
SER
358
−1.967
50.678
46.985
1.00
24.66
B


5592
CB
SER
358
−0.732
50.694
47.910
1.00
23.49
B


5593
OG
SER
358
−1.166
50.289
49.224
1.00
24.21
B


5594
C
SER
358
−1.607
51.302
45.620
1.00
27.34
B


5595
O
SER
358
−1.985
52.457
45.341
1.00
26.59
B


5596
N
MET
359
−0.858
50.559
44.815
1.00
26.09
B


5597
CA
MET
359
−0.523
51.022
43.465
1.00
30.84
B


5598
CB
MET
359
0.399
50.042
42.754
1.00
33.37
B


5599
CG
MET
359
1.786
49.827
43.339
1.00
38.48
B


5600
SD
MET
359
2.611
51.373
43.748
1.00
45.78
B


5601
CE
MET
359
3.869
51.528
42.477
1.00
46.83
B


5602
C
MET
359
−1.805
51.181
42.632
1.00
30.24
B


5603
O
MET
359
−1.950
52.156
41.885
1.00
30.09
B


5604
N
ALA
360
−2.728
50.229
42.701
1.00
30.18
B


5605
CA
ALA
360
−3.943
50.276
41.910
1.00
32.29
B


5606
CB
ALA
360
−4.771
49.013
42.014
1.00
31.29
B


5607
C
ALA
360
−4.767
51.506
42.313
1.00
34.93
B


5608
O
ALA
360
−5.338
52.186
41.440
1.00
34.14
B


5609
N
GLU
361
−4.830
51.830
43.601
1.00
33.11
B


5610
CA
GLU
361
−5.603
52.981
44.033
1.00
33.75
B


5611
CB
GLU
361
−5.950
52.889
45.524
1.00
34.64
B


5612
CG
GLU
361
−7.009
51.862
45.846
1.00
38.36
B


5613
CD
GLU
361
−7.184
51.611
47.342
1.00
40.23
B


5614
OE1
GLU
361
−6.414
52.155
48.169
1.00
41.96
B


5615
OE2
GLU
361
−8.084
50.819
47.709
1.00
40.25
B


5616
C
GLU
361
−4.865
54.299
43.849
1.00
33.05
B


5617
O
GLU
361
−5.419
55.320
44.263
1.00
33.22
B


5618
N
GLY
362
−3.626
54.300
43.383
1.00
31.44
B


5619
CA
GLY
362
−2.840
55.498
43.290
1.00
32.90
B


5620
C
GLY
362
−2.459
56.088
44.636
1.00
32.35
B


5621
O
GLY
362
−2.209
57.290
44.693
1.00
31.88
B


5622
N
LYS
363
−2.171
55.284
45.668
1.00
31.50
B


5623
CA
LYS
363
−1.670
55.864
46.921
1.00
30.05
B


5624
CB
LYS
363
−1.644
54.791
48.023
1.00
30.86
B


5625
CG
LYS
363
−3.040
54.215
48.216
1.00
33.25
B


5626
CD
LYS
363
−3.979
55.369
48.550
1.00
35.05
B


5627
CE
LYS
363
−4.775
55.105
49.814
1.00
37.36
B


5628
NZ
LYS
363
−6.023
54.336
49.478
1.00
40.20
B


5629
C
LYS
363
−0.298
56.434
46.770
1.00
28.83
B


5630
O
LYS
363
0.489
55.922
45.979
1.00
26.37
B


5631
N
SER
364
0.114
57.272
47.729
1.00
26.81
B


5632
CA
SER
364
1.436
57.836
47.715
1.00
26.31
B


5633
CB
SER
364
1.553
59.069
48.633
1.00
28.44
B


5634
OG
SER
364
1.180
58.757
49.996
1.00
29.99
B


5635
C
SER
364
2.500
56.828
48.155
1.00
25.84
B


5636
O
SER
364
3.690
57.173
48.039
1.00
25.10
B


5637
N
THR
365
2.127
55.708
48.768
1.00
24.01
B


5638
CA
THR
365
3.170
54.793
49.260
1.00
23.87
B


5639
CB
THR
365
3.595
54.923
50.744
1.00
24.26
B


5640
OG1
THR
365
2.599
54.302
51.577
1.00
22.66
B


5641
CG2
THR
365
3.809
56.344
51.255
1.00
24.18
B


5642
C
THR
365
2.665
53.373
49.009
1.00
20.88
B


5643
O
THR
365
1.461
53.211
48.843
1.00
21.82
B


5644
N
THR
366
3.531
52.379
49.055
1.00
19.45
B


5645
CA
THR
366
3.127
50.989
48.920
1.00
19.21
B


5646
CB
THR
366
4.356
50.070
48.826
1.00
19.40
B


5647
OG1
THR
366
5.355
50.375
49.834
1.00
19.38
B


5648
CG2
THR
366
5.113
50.310
47.476
1.00
19.02
B


5649
C
THR
366
2.321
50.536
50.146
1.00
20.36
B


5650
O
THR
366
1.783
49.427
50.118
1.00
17.90
B


5651
N
GLY
367
2.373
51.274
51.261
1.00
20.93
B


5652
CA
GLY
367
1.638
50.740
52.463
1.00
22.97
B


5653
C
GLY
367
0.374
51.547
52.679
1.00
26.02
B


5654
O
GLY
367
0.262
52.285
53.679
1.00
27.99
B


5655
N
GLU
368
−0.571
51.492
51.742
1.00
23.43
B


5656
CA
GLU
368
−1.825
52.213
51.782
1.00
25.30
B


5657
CB
GLU
368
−2.740
51.605
52.867
1.00
25.99
B


5658
CG
GLU
368
−2.864
50.082
52.649
1.00
26.74
B


5659
CD
GLU
368
−3.660
49.375
53.720
1.00
27.59
B


5660
OE1
GLU
368
−3.896
49.979
54.799
1.00
28.76
B


5661
OE2
GLU
368
−4.129
48.229
53.528
1.00
28.71
B


5662
C
GLU
368
−1.687
53.709
51.963
1.00
25.50
B


5663
O
GLU
368
−2.570
54.337
52.557
1.00
27.62
B


5664
N
GLY
369
−0.681
54.348
51.399
1.00
23.87
B


5665
CA
GLY
369
−0.372
55.750
51.575
1.00
25.69
B


5666
C
GLY
369
0.250
56.102
52.936
1.00
26.59
B


5667
O
GLY
369
0.609
57.262
53.147
1.00
25.34
B


5668
N
LEU
370
0.505
55.138
53.818
1.00
26.36
B


5669
CA
LEU
370
1.065
55.425
55.134
1.00
27.96
B


5670
CB
LEU
370
0.305
54.613
56.159
1.00
28.99
B


5671
CG
LEU
370
−0.934
55.141
56.879
1.00
32.83
B


5672
CD2
LEU
370
−1.958
54.032
57.020
1.00
31.97
B


5673
CD1
LEU
370
−1.577
56.404
56.350
1.00
31.33
B


5674
C
LEU
370
2.549
55.042
55.156
1.00
28.04
B


5675
O
LEU
370
3.002
54.292
54.267
1.00
25.33
B


5676
N
ASP
371
3.284
55.512
56.155
1.00
25.78
B


5677
CA
ASP
371
4.693
55.240
56.240
1.00
28.14
B


5678
CB
ASP
371
5.406
56.400
56.980
1.00
31.72
B


5679
CG
ASP
371
5.397
57.639
56.081
1.00
35.24
B


5680
OD1
ASP
371
5.239
57.540
54.829
1.00
36.93
B


5681
OD2
ASP
371
5.612
58.738
56.641
1.00
37.53
B


5682
C
ASP
371
5.119
53.923
56.873
1.00
28.06
B


5683
O
ASP
371
6.097
53.374
56.357
1.00
27.73
B


5684
N
CYS
372
4.521
53.467
57.945
1.00
26.47
B


5685
CA
CYS
372
4.957
52.294
58.676
1.00
27.36
B


5686
CB
CYS
372
5.465
52.696
60.116
1.00
30.70
B


5687
SG
CYS
372
7.205
53.185
59.931
1.00
44.11
B


5688
C
CYS
372
3.823
51.329
58.851
1.00
23.53
B


5689
O
CYS
372
2.683
51.773
58.776
1.00
23.11
B


5690
N
GLY
373
4.083
50.033
58.853
1.00
23.03
B


5691
CA
GLY
373
3.019
49.047
58.989
1.00
18.94
B


5692
C
GLY
373
3.445
47.954
59.951
1.00
18.22
B


5693
O
GLY
373
4.647
47.710
60.134
1.00
19.54
B


5694
N
VAL
374
2.494
47.171
60.435
1.00
17.08
B


5695
CA
VAL
374
2.871
46.075
61.344
1.00
16.30
B


5696
CB
VAL
374
2.286
46.326
62.777
1.00
16.99
B


5697
CG1
VAL
374
2.416
45.059
63.638
1.00
20.31
B


5698
CG2
VAL
374
2.956
47.519
63.414
1.00
16.30
B


5699
C
VAL
374
2.280
44.782
60.849
1.00
14.24
B


5700
O
VAL
374
1.101
44.701
60.559
1.00
17.05
B


5701
N
LEU
375
3.081
43.754
60.803
1.00
15.98
B


5702
CA
LEU
375
2.644
42.427
60.368
1.00
16.70
B


5703
CB
LEU
375
3.564
42.006
59.272
1.00
15.92
B


5704
CG
LEU
375
4.091
40.684
58.767
1.00
22.02
B


5705
CD2
LEU
375
3.879
40.397
57.264
1.00
17.43
B


5706
CD1
LEU
375
3.941
39.445
59.608
1.00
19.27
B


5707
C
LEU
375
2.676
41.465
61.571
1.00
18.05
B


5708
O
LEU
375
3.693
41.521
62.292
1.00
16.00
B


5709
N
PHE
376
1.639
40.658
61.680
1.00
17.80
B


5710
CA
PHE
376
1.593
39.671
62.750
1.00
18.15
B


5711
CB
PHE
376
0.371
39.904
63.685
1.00
17.61
B


5712
CG
PHE
376
0.366
41.130
64.554
1.00
17.61
B


5713
CD1
PHE
376
−0.677
42.049
64.488
1.00
18.03
B


5714
CD2
PHE
376
1.379
41.351
65.481
1.00
18.64
B


5715
CE1
PHE
376
−0.708
43.188
65.298
1.00
18.81
B


5716
CE2
PHE
376
1.327
42.451
66.333
1.00
18.23
B


5717
CZ
PHE
376
0.315
43.380
66.256
1.00
17.54
B


5718
C
PHE
376
1.387
38.260
62.226
1.00
18.59
B


5719
O
PHE
376
0.529
38.023
61.355
1.00
20.07
B


5720
N
GLY
377
2.190
37.329
62.737
1.00
15.47
B


5721
CA
GLY
377
2.020
35.901
62.468
1.00
16.40
B


5722
C
GLY
377
1.637
35.252
63.842
1.00
18.96
B


5723
O
GLY
377
2.159
35.695
64.854
1.00
17.94
B


5724
N
PHE
378
0.750
34.276
63.879
1.00
17.37
B


5725
CA
PHE
378
0.330
33.615
65.119
1.00
18.50
B


5726
CB
PHE
378
−1.180
33.911
65.355
1.00
16.49
B


5727
CG
PHE
378
−1.543
35.378
65.328
1.00
17.95
B


5728
CD1
PHE
378
−1.008
36.232
66.285
1.00
19.64
B


5729
CD2
PHE
378
−2.473
35.897
64.464
1.00
19.18
B


5730
CE1
PHE
378
−1.360
37.565
66.364
1.00
19.64
B


5731
CE2
PHE
378
−2.837
37.233
64.522
1.00
18.80
B


5732
CZ
PHE
378
−2.295
38.100
65.467
1.00
19.16
B


5733
C
PHE
378
0.461
32.116
64.999
1.00
21.02
B


5734
O
PHE
378
−0.085
31.607
64.010
1.00
17.15
B


5735
N
GLY
379
1.195
31.419
65.870
1.00
18.50
B


5736
CA
GLY
379
1.310
29.967
65.746
1.00
16.05
B


5737
C
GLY
379
1.477
29.269
67.103
1.00
18.11
B


5738
O
GLY
379
1.224
29.923
68.128
1.00
13.64
B


5739
N
PRO
380
1.698
27.981
67.076
1.00
16.69
B


5740
CA
PRO
380
1.810
27.143
68.262
1.00
18.42
B


5741
CD
PRO
380
1.817
27.123
65.851
1.00
17.87
B


5742
CB
PRO
380
2.208
25.758
67.754
1.00
17.47
B


5743
CG
PRO
380
1.525
25.751
66.384
1.00
17.91
B


5744
C
PRO
380
2.873
27.669
69.228
1.00
17.32
B


5745
O
PRO
380
3.789
28.431
68.937
1.00
15.87
B


5746
N
GLY
381
2.380
27.682
70.496
1.00
17.73
B


5747
CA
GLY
381
3.330
28.035
71.601
1.00
15.93
B


5748
C
GLY
381
2.404
28.745
72.615
1.00
19.96
B


5749
O
GLY
381
2.433
28.322
73.753
1.00
16.38
B


5750
N
MET
382
1.457
29.648
72.505
1.00
17.53
B


5751
CA
MET
382
1.169
30.444
71.371
1.00
20.52
B


5752
CB
MET
382
−0.113
31.256
71.399
1.00
22.19
B


5753
CG
MET
382
−1.299
30.362
70.985
1.00
26.18
B


5754
SD
MET
382
−2.727
31.449
70.761
1.00
32.93
B


5755
CE
MET
382
−2.158
32.688
69.628
1.00
27.98
B


5756
C
MET
382
2.362
31.353
71.087
1.00
20.26
B


5757
O
MET
382
2.926
31.939
72.035
1.00
20.98
B


5758
N
THR
383
2.754
31.504
69.808
1.00
16.62
B


5759
CA
THR
383
3.776
32.487
69.441
1.00
16.94
B


5760
CB
THR
383
4.893
31.794
68.616
1.00
18.30
B


5761
OG1
THR
383
5.435
30.774
69.448
1.00
18.88
B


5762
CG2
THR
383
6.019
32.696
68.195
1.00
22.48
B


5763
C
THR
383
3.178
33.600
68.606
1.00
17.58
B


5764
O
THR
383
2.329
33.349
67.715
1.00
16.35
B


5765
N
VAL
384
3.645
34.824
68.789
1.00
15.64
B


5766
CA
VAL
384
3.293
35.954
67.931
1.00
15.95
B


5767
CB
VAL
384
2.706
37.166
68.658
1.00
16.79
B


5768
CG1
VAL
384
2.348
38.316
67.731
1.00
14.79
B


5769
CG2
VAL
384
1.437
36.785
69.437
1.00
20.42
B


5770
C
VAL
384
4.600
36.415
67.268
1.00
17.25
B


5771
O
VAL
384
5.590
36.546
67.986
1.00
15.34
B


5772
N
GLU
385
4.628
36.652
65.970
1.00
15.93
B


5773
CA
GLU
385
5.803
37.249
65.345
1.00
15.57
B


5774
CB
GLU
385
6.347
36.531
64.111
1.00
17.18
B


5775
CG
GLU
385
6.769
35.108
64.574
1.00
15.17
B


5776
CD
GLU
385
8.199
34.782
64.267
1.00
14.81
B


5777
OE1
GLU
385
8.997
35.669
63.884
1.00
17.65
B


5778
OE2
GLU
385
8.582
33.590
64.374
1.00
17.30
B


5779
C
GLU
385
5.312
38.639
64.968
1.00
14.54
B


5780
O
GLU
385
4.208
38.682
64.432
1.00
13.38
B


5781
N
THR
386
6.076
39.655
65.321
1.00
14.53
B


5782
CA
THR
386
5.612
41.011
65.010
1.00
15.70
B


5783
CB
THR
386
5.389
41.810
66.331
1.00
14.93
B


5784
OG1
THR
386
4.345
41.085
67.016
1.00
13.01
B


5785
CG2
THR
386
4.828
43.180
65.969
1.00
18.33
B


5786
C
THR
386
6.681
41.684
64.175
1.00
16.99
B


5787
O
THR
386
7.803
41.803
64.640
1.00
18.66
B


5788
N
VAL
387
6.425
41.983
62.916
1.00
17.17
B


5789
CA
VAL
387
7.424
42.576
62.036
1.00
15.47
B


5790
CB
VAL
387
7.542
41.744
60.737
1.00
17.25
B


5791
CG1
VAL
387
8.506
42.348
59.715
1.00
14.14
B


5792
CG2
VAL
387
7.871
40.298
61.076
1.00
16.11
B


5793
C
VAL
387
7.006
43.998
61.692
1.00
16.18
B


5794
O
VAL
387
5.859
44.154
61.228
1.00
18.67
B


5795
N
VAL
388
7.905
44.989
61.840
1.00
15.51
B


5796
CA
VAL
388
7.492
46.323
61.370
1.00
16.80
B


5797
CB
VAL
388
8.007
47.489
62.229
1.00
18.85
B


5798
CG1
VAL
388
7.739
48.850
61.608
1.00
18.96
B


5799
CG2
VAL
388
7.348
47.475
63.649
1.00
17.50
B


5800
C
VAL
388
8.054
46.524
59.936
1.00
17.03
B


5801
O
VAL
388
9.223
46.185
59.694
1.00
15.43
B


5802
N
LEU
389
7.204
47.053
59.075
1.00
17.33
B


5803
CA
LEU
389
7.663
47.282
57.679
1.00
21.43
B


5804
CB
LEU
389
6.629
46.538
56.807
1.00
19.43
B


5805
CG
LEU
389
6.944
45.190
56.210
1.00
20.03
B


5806
CD2
LEU
389
5.720
44.326
55.988
1.00
24.09
B


5807
CD1
LEU
389
8.107
44.417
56.764
1.00
18.41
B


5808
C
LEU
389
7.640
48.776
57.359
1.00
22.48
B


5809
O
LEU
389
6.684
49.409
57.842
1.00
23.82
B


5810
N
ARG
390
8.609
49.319
56.613
1.00
21.15
B


5811
CA
ARG
390
8.450
50.711
56.201
1.00
23.63
B


5812
CB
ARG
390
9.704
51.527
56.376
1.00
24.73
B


5813
CG
ARG
390
9.523
53.027
56.166
1.00
28.86
B


5814
CD
ARG
390
10.849
53.665
56.587
1.00
33.04
B


5815
NE
ARG
390
10.748
53.623
58.056
1.00
39.70
B


5816
CZ
ARG
390
11.635
53.406
59.003
1.00
41.83
B


5817
NH1
ARG
390
12.913
53.163
58.732
1.00
42.21
B


5818
NH2
ARG
390
11.191
53.429
60.265
1.00
43.28
B


5819
C
ARG
390
8.065
50.720
54.705
1.00
24.27
B


5820
O
ARG
390
8.725
50.052
53.923
1.00
22.53
B


5776
N
SER
391
7.049
51.498
54.388
0.60
24.71
B


5777
CA
SER
391
6.574
51.636
52.995
0.60
25.35
B


5778
CB
SER
391
5.341
52.544
52.900
0.60
25.10
B


5779
CG
SER
391
4.292
52.065
53.716
0.60
27.83
B


5780
C
SER
391
7.627
52.319
52.134
0.60
24.39
B


5781
O
SER
391
8.558
52.959
52.645
0.60
21.88
B


5776
N
2SER
391
7.051
51.444
54.373
0.40
23.03
B


5777
CA
2SER
391
6.591
51.532
52.978
0.40
22.31
B


5778
CB
2SER
391
5.260
52.277
52.904
0.40
19.63
B


5779
OG
2SER
391
5.425
53.608
53.370
0.40
16.14
B


5780
C
2SER
391
7.609
52.296
52.133
0.40
22.84
B


5781
O
2SER
391
8.490
52.991
52.661
0.40
21.30
B


5833
N
VAL
392
7.379
52.266
50.840
1.00
25.27
B


5834
CA
VAL
392
8.301
52.842
49.870
1.00
24.69
B


5835
CB
VAL
392
8.910
51.880
48.857
1.00
24.47
B


5836
CG1
VAL
392
9.681
52.695
47.782
1.00
25.05
B


5837
CG2
VAL
392
9.956
51.001
49.538
1.00
23.37
B


5838
C
VAL
392
7.443
53.929
49.183
1.00
28.14
B


5839
O
VAL
392
6.285
53.803
48.807
1.00
24.87
B


5840
N
ARG
393
8.071
55.076
49.196
1.00
33.33
B


5841
CA
ARG
393
7.439
56.253
48.669
1.00
41.36
B


5842
CB
ARG
393
8.174
57.532
49.050
1.00
44.63
B


5843
CG
ARG
393
7.379
58.740
48.576
1.00
48.73
B


5844
CD
ARG
393
7.291
59.792
49.682
1.00
52.29
B


5845
NE
ARG
393
5.910
60.250
49.820
1.00
54.82
B


5846
CZ
ARG
393
5.205
60.204
50.937
1.00
57.38
B


5847
NH1
ARG
393
5.726
59.726
52.067
1.00
57.43
B


5848
NH2
ARG
393
3.944
60.631
51.002
1.00
59.22
B


5849
C
ARG
393
7.382
56.113
47.147
1.00
44.23
B


5850
O
ARG
393
8.329
55.772
46.435
1.00
43.53
B


5851
N
VAL
394
6.168
56.338
46.646
1.00
46.97
B


5852
CA
VAL
394
5.966
56.264
45.214
1.00
50.68
B


5853
CB
VAL
394
5.165
55.055
44.684
1.00
50.32
B


5854
CG1
VAL
394
5.853
53.737
45.032
1.00
51.04
B


5855
CG2
VAL
394
3.721
55.066
45.118
1.00
49.56
B


5856
C
VAL
394
5.332
57.503
44.599
1.00
53.03
B


5857
OT
VAL
394
5.552
57.739
43.379
1.00
54.09
B


5858
OXT
VAL
394
5.105
58.606
45.112
1.00
55.26
B


5859
C8
AAC
395
−15.192
26.893
66.832
1.00
31.85
B


5860
N9
AAC
395
−15.934
25.758
67.103
1.00
32.08
B


5861
C4
AAC
395
−15.088
24.934
67.869
1.00
30.84
B


5862
C5
AAC
395
−13.832
25.530
67.809
1.00
30.43
B


5863
N7
AAC
395
−13.885
26.781
67.173
1.00
31.11
B


5864
N3
AAC
395
−15.294
23.593
68.102
1.00
30.53
B


5865
C2
AAC
395
−14.261
23.062
68.719
1.00
31.39
B


5866
N1
AAC
395
−12.944
23.490
68.590
1.00
30.31
B


5867
C6
AAC
395
−12.707
24.772
68.167
1.00
28.56
B


5868
N6
AAC
395
−11.444
25.259
68.054
1.00
27.76
B


5869
C1′
AAC
395
−17.565
25.621
67.019
1.00
33.80
B


5870
C2′
AAC
395
−18.568
26.410
67.757
1.00
33.92
B


5871
O2′
AAC
395
−18.460
25.742
68.939
1.00
35.53
B


5872
C3′
AAC
395
−19.659
26.490
66.695
1.00
34.93
B


5873
O3′
AAC
395
−20.567
25.398
66.547
1.00
37.60
B


5874
C4′
AAC
395
−19.026
26.473
65.246
1.00
34.24
B


5875
O4′
AAC
395
−17.686
25.823
65.578
1.00
31.70
B


5876
C5′
AAC
395
−18.654
27.909
64.805
1.00
34.89
B


5877
O5′
AAC
395
−18.589
28.914
66.006
1.00
36.12
B


5878
P1
AAC
395
−19.171
30.068
66.347
1.00
37.11
B


5879
O11
AAC
395
−18.851
30.453
67.744
1.00
36.83
B


5880
O12
AAC
395
−20.610
29.791
66.064
1.00
35.72
B


5881
O6
AAC
395
−18.515
31.021
65.274
1.00
34.92
B


5882
P2
AAC
395
−17.280
31.992
65.062
1.00
33.36
B


5883
O21
AAC
395
−16.471
31.770
66.293
1.00
30.55
B


5884
O22
AAC
395
−17.679
33.362
64.915
1.00
30.96
B


5885
O7
AAC
395
−16.646
31.579
63.771
1.00
32.38
B


5886
CPB
AAC
395
−16.080
30.192
63.750
1.00
31.68
B


5887
CPA
AAC
395
−14.542
30.319
63.372
1.00
30.89
B


5888
CP7
AAC
395
−13.888
31.248
64.422
1.00
31.27
B


5889
CP9
AAC
395
−14.489
30.884
61.936
1.00
30.17
B


5890
CP8
AAC
395
−13.807
28.985
63.475
1.00
30.74
B


5891
OP3
AAC
395
−14.107
30.729
65.756
1.00
32.31
B


5892
CP6
AAC
395
−12.343
31.291
64.332
1.00
31.20
B


5893
OP2
AAC
395
−11.876
32.045
63.433
1.00
29.03
B


5894
NP2
AAC
395
−11.624
30.543
65.153
1.00
32.06
B


5895
CP5
AAC
395
−10.533
29.754
64.393
1.00
33.24
B


5896
CP4
AAC
395
−9.228
30.266
64.907
1.00
33.51
B


5897
CP3
AAC
395
−8.159
29.225
64.583
1.00
33.61
B


5898
OP1
AAC
395
−7.893
28.716
65.682
1.00
32.17
B


5899
NP1
AAC
395
−7.229
29.455
63.650
1.00
30.09
B


5900
CP2
AAC
395
−5.812
29.049
64.048
1.00
28.37
B


5901
CP1
AAC
395
−5.272
27.710
63.569
1.00
30.17
B


5902
S
AAC
395
−3.497
27.744
63.958
1.00
34.21
B


5903
P3
AAC
395
−22.168
25.197
66.560
1.00
36.14
B


5904
O31
AAC
395
−22.761
25.893
65.401
1.00
35.36
B


5905
O32
AAC
395
−22.781
25.733
67.803
1.00
36.64
B


5906
O33
AAC
395
−22.188
23.595
66.448
1.00
36.54
B


5907
C51
AAC
395
−3.048
26.178
63.366
1.00
32.89
B


5908
C52
AAC
395
−1.642
25.785
63.820
1.00
34.16
B


5909
O51
AAC
395
−3.937
25.359
63.416
1.00
32.53
B


5910
C53
AAC
395
−0.644
25.743
62.664
1.00
34.31
B


5911
C54
AAC
395
−0.798
24.634
61.645
1.00
31.81
B


5912
O52
AAC
395
0.489
26.137
62.899
1.00
34.83
B


5913
OW0
WAT
1
34.833
42.831
79.558
1.00
24.60
W


5914
OW0
WAT
2
3.851
18.304
58.076
1.00
15.19
W


5915
OW0
WAT
3
10.671
17.830
49.206
1.00
12.89
W


5916
OW0
WAT
4
10.141
17.602
68.259
1.00
12.07
W


5917
OW0
WAT
5
32.698
32.703
80.877
1.00
22.54
W


5918
OW0
WAT
6
28.164
16.600
62.904
1.00
18.35
W


5919
OW0
WAT
7
−8.681
23.005
55.960
1.00
23.89
W


5920
OW0
WAT
8
18.659
24.304
57.009
1.00
14.47
W


5921
OW0
WAT
9
37.188
5.906
65.616
1.00
21.40
W


5922
OW0
WAT
10
9.584
18.395
70.986
1.00
16.40
W


5923
OW0
WAT
11
17.062
36.363
62.243
1.00
11.16
W


5924
OW0
WAT
12
13.451
23.284
60.136
1.00
10.89
W


5925
OW0
WAT
13
24.265
17.082
39.849
1.00
31.15
W


5926
OW0
WAT
14
4.587
15.225
66.740
1.00
16.62
W


5927
OW0
WAT
15
2.745
19.417
70.978
1.00
18.45
W


5928
OW0
WAT
16
2.872
55.277
59.456
1.00
21.70
W


5929
OW0
WAT
17
7.130
19.586
71.177
1.00
14.85
W


5930
OW0
WAT
18
23.610
32.233
58.057
1.00
10.85
W


5931
OW0
WAT
19
13.279
44.644
42.430
1.00
23.27
W


5932
OW0
WAT
20
−5.728
46.578
54.624
1.00
21.51
W


5933
OW0
WAT
21
31.220
−7.039
65.899
1.00
35.39
W


5934
OW0
WAT
22
11.942
28.570
63.201
1.00
15.27
W


5935
OW0
WAT
23
12.975
12.459
62.075
1.00
16.09
W


5936
OW0
WAT
24
27.265
29.217
41.221
1.00
45.85
W


5937
OW0
WAT
25
−4.415
43.306
73.997
1.00
21.65
W


5938
OW0
WAT
26
4.080
28.969
63.728
1.00
17.36
W


5939
OW0
WAT
27
−0.674
37.643
45.198
1.00
26.53
W


5940
OW0
WAT
28
−12.011
31.967
59.137
1.00
21.56
W


5941
OW0
WAT
29
9.814
17.806
52.000
1.00
11.02
W


5942
OW0
WAT
30
32.277
16.861
75.083
1.00
22.34
W


5943
OW0
WAT
31
−5.887
8.918
58.081
1.00
24.91
W


5944
OW0
WAT
32
14.641
12.037
49.335
1.00
20.01
W


5945
OW0
WAT
33
−5.901
28.682
48.527
1.00
15.15
W


5946
OW0
WAT
34
9.867
33.328
71.420
1.00
16.19
W


5947
OW0
WAT
35
7.243
23.184
65.189
1.00
12.89
W


5948
OW0
WAT
36
12.471
22.810
36.544
1.00
22.46
W


5949
OW0
WAT
37
−4.886
4.535
51.739
1.00
21.52
W


5950
OW0
WAT
38
7.963
25.910
67.738
1.00
18.53
W


5951
OW0
WAT
39
7.137
18.587
51.905
1.00
14.48
W


5952
OW0
WAT
40
15.459
40.211
62.055
1.00
17.02
W


5953
OW0
WAT
41
6.682
20.285
57.647
1.00
12.75
W


5954
OW0
WAT
42
18.453
17.014
54.016
1.00
17.42
W


5955
OW0
WAT
43
15.988
17.744
55.089
1.00
14.59
W


5956
OW0
WAT
44
9.657
27.916
66.070
1.00
21.06
W


5957
OW0
WAT
45
5.409
25.121
66.215
1.00
19.96
W


5958
OW0
WAT
46
1.102
33.642
57.497
1.00
14.88
W


5959
OW0
WAT
47
9.921
11.878
53.540
1.00
18.78
W


5960
OW0
WAT
48
−1.104
35.179
81.753
1.00
20.52
W


5961
OW0
WAT
49
−4.358
19.825
49.529
1.00
18.00
W


5962
OW0
WAT
50
32.742
32.506
77.847
1.00
19.42
W


5963
OW0
WAT
51
10.471
30.328
64.937
1.00
22.26
W


5964
OW0
WAT
52
29.066
−6.518
67.728
1.00
29.12
W


5965
OW0
WAT
53
23.893
38.780
44.707
1.00
22.24
W


5966
OW0
WAT
54
36.495
37.126
69.107
1.00
25.16
W


5967
OW0
WAT
55
27.620
4.330
52.694
1.00
26.50
W


5968
OW0
WAT
56
2.961
34.006
59.532
1.00
14.45
W


5969
OW0
WAT
57
25.883
33.854
55.114
1.00
18.60
W


5970
OW0
WAT
58
23.934
24.479
48.784
1.00
17.20
W


5971
OW0
WAT
59
−11.213
45.118
57.839
1.00
30.98
W


5972
OW0
WAT
60
−0.796
29.899
40.488
1.00
21.41
W


5973
OW0
WAT
61
9.058
44.419
65.396
1.00
16.69
W


5974
OW0
WAT
62
33.639
20.536
47.167
1.00
26.62
W


5975
OW0
WAT
63
17.361
46.985
62.113
1.00
28.80
W


5976
OW0
WAT
64
28.774
26.262
56.335
1.00
16.05
W


5977
OW0
WAT
65
8.319
17.938
74.501
1.00
29.07
W


5978
OW0
WAT
66
22.954
26.285
83.799
1.00
27.43
W


5979
OW0
WAT
67
26.549
36.290
50.427
1.00
25.74
W


5980
OW0
WAT
68
21.904
42.229
51.024
1.00
14.99
W


5981
OW0
WAT
69
11.885
15.625
68.435
1.00
16.06
W


5982
OW0
WAT
70
3.727
3.076
66.509
1.00
17.85
W


5983
OW0
WAT
71
27.566
41.917
69.685
1.00
25.81
W


5984
OW0
WAT
72
33.346
−2.248
71.890
1.00
32.26
W


5985
OW0
WAT
73
16.793
34.027
77.388
1.00
14.06
W


5986
OW0
WAT
74
3.307
30.509
80.393
1.00
26.64
W


5987
OW0
WAT
75
13.567
3.944
75.261
1.00
27.89
W


5988
OW0
WAT
76
9.592
38.551
63.829
1.00
17.98
W


5989
OW0
WAT
77
9.389
45.293
42.566
1.00
30.18
W


5990
OW0
WAT
78
−5.191
21.436
42.415
1.00
25.88
W


5991
OW0
WAT
79
21.648
31.139
42.786
1.00
17.08
W


5992
OW0
WAT
80
19.191
21.778
54.198
1.00
20.38
W


5993
OW0
WAT
81
26.780
39.147
69.085
1.00
17.18
W


5994
OW0
WAT
82
8.246
10.309
52.119
1.00
16.38
W


5995
OW0
WAT
83
3.964
12.812
68.057
1.00
14.72
W


5996
OW0
WAT
84
−9.721
27.929
67.632
1.00
32.83
W


5997
OW0
WAT
85
−4.054
15.227
45.174
1.00
24.29
W


5998
OW0
WAT
86
18.075
5.893
70.745
1.00
16.23
W


5999
OW0
WAT
87
22.585
17.373
56.517
1.00
18.76
W


6000
OW0
WAT
88
26.487
8.160
71.794
1.00
18.93
W


6001
OW0
WAT
89
6.429
43.196
69.535
1.00
19.11
W


6002
OW0
WAT
90
17.488
39.092
65.113
1.00
19.91
W


6003
OW0
WAT
91
16.700
42.492
65.311
1.00
25.17
W


6004
OW0
WAT
92
−7.482
22.305
53.597
1.00
35.05
W


6005
OW0
WAT
93
39.257
16.047
46.333
1.00
21.17
W


6006
OW0
WAT
94
36.318
43.091
76.325
1.00
25.27
W


6007
OW0
WAT
95
−12.497
37.547
54.922
1.00
21.19
W


6008
OW0
WAT
96
21.901
12.704
48.744
1.00
22.39
W


6009
OW0
WAT
97
−4.916
44.148
56.306
1.00
19.43
W


6010
OW0
WAT
98
21.194
31.992
84.275
1.00
35.72
W


6011
OW0
WAT
99
33.840
39.368
68.085
1.00
21.99
W


6012
OW0
WAT
100
8.893
−0.172
62.082
1.00
22.49
W


6013
OW0
WAT
101
18.453
−4.480
57.253
1.00
25.92
W


6014
OW0
WAT
102
13.569
16.019
62.639
1.00
13.04
W


6015
OW0
WAT
103
22.781
39.492
75.427
1.00
21.42
W


6016
OW0
WAT
104
−7.834
44.025
77.416
1.00
33.20
W


6017
OW0
WAT
105
29.427
5.861
61.950
1.00
20.36
W


6018
OW0
WAT
106
3.539
0.402
69.939
1.00
29.39
W


6019
OW0
WAT
107
18.155
19.548
52.456
1.00
16.41
W


6020
OW0
WAT
108
27.601
18.356
60.638
1.00
17.86
W


6021
OW0
WAT
109
2.260
40.202
73.144
1.00
20.92
W


6022
OW0
WAT
110
−9.554
18.969
50.641
1.00
32.12
W


6023
OW0
WAT
111
4.563
−1.441
68.389
1.00
19.23
W


6024
OW0
WAT
112
48.869
20.302
51.779
1.00
37.00
W


6025
OW0
WAT
113
−4.533
52.328
56.005
1.00
27.04
W


6026
OW0
WAT
114
5.063
37.094
76.058
1.00
29.92
W


6027
OW0
WAT
115
−0.474
5.884
53.613
1.00
20.80
W


6028
OW0
WAT
116
19.360
40.801
69.648
1.00
23.52
W


6029
OW0
WAT
117
20.908
23.658
55.291
1.00
25.91
W


6030
OW0
WAT
118
−6.751
15.614
64.282
1.00
30.02
W


6031
OW0
WAT
119
14.215
52.423
37.362
1.00
24.66
W


6032
OW0
WAT
120
17.895
−2.536
59.148
1.00
30.62
W


6033
OW0
WAT
121
33.040
37.124
58.297
1.00
27.56
W


6034
OW0
WAT
122
34.452
25.507
50.774
1.00
20.94
W


6035
OW0
WAT
123
17.664
41.847
62.811
1.00
21.31
W


6036
OW0
WAT
124
5.485
30.235
37.732
1.00
18.76
W


6037
OW0
WAT
125
−1.898
7.686
64.040
1.00
19.63
W


6038
OW0
WAT
126
19.019
48.698
52.195
1.00
20.04
W


6039
OW0
WAT
127
−3.037
31.394
63.373
1.00
18.81
W


6040
OW0
WAT
128
15.630
33.770
81.050
1.00
22.48
W


6041
OW0
WAT
129
23.983
44.352
50.610
1.00
25.96
W


6042
OW0
WAT
130
28.110
28.669
50.206
1.00
15.08
W


6043
OW0
WAT
131
−1.806
43.291
75.344
1.00
22.63
W


6044
OW0
WAT
132
28.287
−8.666
69.293
1.00
26.47
W


6045
OW0
WAT
133
7.361
31.080
64.997
1.00
25.48
W


6046
OW0
WAT
134
20.560
41.099
75.976
1.00
35.84
W


6047
OW0
WAT
135
−10.673
19.682
54.611
1.00
27.63
W


6048
OW0
WAT
136
12.764
16.066
49.078
1.00
18.12
W


6049
OW0
WAT
137
15.512
38.206
71.556
1.00
22.76
W


6050
OW0
WAT
138
2.289
29.709
76.361
1.00
20.87
W


6051
OW0
WAT
139
27.607
12.017
56.955
1.00
21.54
W


6052
OW0
WAT
140
43.717
10.364
62.596
1.00
29.34
W


6053
OW0
WAT
141
22.855
3.440
64.232
1.00
24.50
W


6054
OW0
WAT
142
39.489
28.943
75.323
1.00
25.73
W


6055
OW0
WAT
143
18.435
3.949
68.723
1.00
22.83
W


6056
OW0
WAT
144
22.017
29.915
39.105
1.00
26.92
W


6057
OW0
WAT
145
−13.904
15.849
62.886
1.00
23.40
W


6058
OW0
WAT
146
6.078
39.444
68.567
1.00
16.60
W


6059
OW0
WAT
147
−12.455
45.712
55.387
1.00
35.99
W


6060
OW0
WAT
148
3.763
16.311
71.884
1.00
23.06
W


6061
OW0
WAT
149
6.607
34.616
35.798
1.00
32.25
W


6062
OW0
WAT
150
37.996
18.102
44.945
1.00
29.62
W


6063
OW0
WAT
151
−18.165
30.197
48.373
1.00
25.75
W


6064
OW0
WAT
152
0.334
27.287
79.026
1.00
25.74
W


6065
OW0
WAT
153
10.426
48.456
66.152
1.00
21.45
W


6066
OW0
WAT
154
42.624
16.000
65.750
1.00
23.86
W


6067
OW0
WAT
155
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1.00
33.50
W


6068
OW0
WAT
156
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1.00
33.17
W


6069
OW0
WAT
157
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1.00
24.80
W


6070
OW0
WAT
158
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1.00
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W


6071
OW0
WAT
159
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1.00
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W


6072
OW0
WAT
160
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1.00
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W


6073
OW0
WAT
161
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1.00
30.11
W


6074
OW0
WAT
162
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1.00
21.49
W


6075
OW0
WAT
163
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1.00
20.71
W


6076
OW0
WAT
164
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1.00
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W


6077
OW0
WAT
165
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1.00
17.20
W


6078
OW0
WAT
166
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1.00
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W


6079
OW0
WAT
167
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1.00
26.50
W


6080
OW0
WAT
168
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1.00
19.03
W


6081
OW0
WAT
169
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1.00
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W


6082
OW0
WAT
170
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1.00
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W


6083
OW0
WAT
171
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1.00
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W


6084
OW0
WAT
172
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1.00
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W


6085
OW0
WAT
173
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1.00
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W


6086
OW0
WAT
174
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1.00
24.24
W


6087
OW0
WAT
175
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1.00
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W


6088
OW0
WAT
176
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1.00
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W


6089
OW0
WAT
177
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1.00
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W


6090
OW0
WAT
178
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1.00
21.81
W


6091
OW0
WAT
179
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1.00
28.51
W


6092
OW0
WAT
180
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1.00
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W


6093
OW0
WAT
181
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1.00
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W


6094
OW0
WAT
182
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1.00
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W


6095
OW0
WAT
183
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1.00
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W


6096
OW0
WAT
184
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1.00
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W


6097
OW0
WAT
185
9.316
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1.00
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W


6098
OW0
WAT
186
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1.00
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W


6099
OW0
WAT
187
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1.00
27.73
W


6100
OW0
WAT
188
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1.00
29.77
W


6101
OW0
WAT
189
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1.00
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W


6102
OW0
WAT
190
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1.00
22.77
W


6103
OW0
WAT
191
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1.00
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W


6104
OW0
WAT
192
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1.00
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W


6105
OW0
WAT
193
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1.00
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W


6106
OW0
WAT
194
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1.00
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W


6107
OW0
WAT
195
20.208
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1.00
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W


6108
OW0
WAT
196
22.288
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1.00
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W


6109
OW0
WAT
197
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1.00
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W


6110
OW0
WAT
198
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1.00
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W


6111
OW0
WAT
199
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1.00
26.17
W


6112
OW0
WAT
200
40.226
8.346
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1.00
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W


6113
OW0
WAT
201
5.142
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1.00
39.12
W


6114
OW0
WAT
202
31.834
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1.00
26.81
W


6115
OW0
WAT
203
−9.914
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1.00
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W


6116
OW0
WAT
204
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1.00
27.58
W


6117
OW0
WAT
205
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1.00
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W


6118
OW0
WAT
206
8.359
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1.00
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W


6119
OW0
WAT
207
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1.00
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W


6120
OW0
WAT
208
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1.00
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W


6121
OW0
WAT
209
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1.00
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W


6122
OW0
WAT
210
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1.00
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W


6123
OW0
WAT
211
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1.00
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W


6124
OW0
WAT
212
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1.00
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W


6125
OW0
WAT
213
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1.00
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W


6126
OW0
WAT
214
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1.00
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W


6127
OW0
WAT
215
34.539
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1.00
33.94
W


6128
OW0
WAT
216
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1.00
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W


6129
OW0
WAT
217
38.172
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1.00
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W


6130
OW0
WAT
218
44.142
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1.00
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W


6131
OW0
WAT
219
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1.00
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W


6132
OW0
WAT
220
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1.00
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W


6133
OW0
WAT
221
21.010
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1.00
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W


6134
OW0
WAT
222
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1.00
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W


6135
OW0
WAT
223
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1.00
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W


6136
OW0
WAT
224
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1.00
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W


6137
OW0
WAT
225
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1.00
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W


6138
OW0
WAT
226
12.946
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1.00
35.45
W


6139
OW0
WAT
227
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1.00
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W


6140
OW0
WAT
228
29.044
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1.00
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W


6141
OW0
WAT
229
52.147
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1.00
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W


6142
OW0
WAT
230
24.831
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1.00
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W


6143
OW0
WAT
231
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1.00
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W


6144
OW0
WAT
232
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1.00
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W


6145
OW0
WAT
233
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1.00
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W


6146
OW0
WAT
234
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1.00
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W


6147
OW0
WAT
235
9.776
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1.00
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W


6148
OW0
WAT
236
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1.00
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W


6149
OW0
WAT
237
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W


6150
OW0
WAT
236
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1.00
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W


6151
OW0
WAT
239
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1.00
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W


6152
OW0
WAT
240
−1.966
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1.00
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W


6153
OW0
WAT
241
18.480
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1.00
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W


6154
OW0
WAT
242
9.409
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1.00
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W


6155
OW0
WAT
243
27.641
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1.00
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W


6156
OW0
WAT
244
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1.00
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W


6157
OW0
WAT
245
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1.00
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W


6158
OW0
WAT
246
28.817
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1.00
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W


6159
OW0
WAT
247
14.247
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1.00
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W


6160
OW0
WAT
248
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1.00
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W


6161
OW0
WAT
249
−1.422
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1.00
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W


6162
OW0
WAT
250
28.196
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1.00
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W


6163
OW0
WAT
251
−6.712
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1.00
36.33
W


6164
OW0
WAT
252
−0.371
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1.00
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W


6165
OW0
WAT
253
25.280
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1.00
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W


6166
OW0
WAT
254
−15.928
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W


6167
OW0
WAT
255
4.853
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1.00
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W


6169
OW0
WAT
257
15.700
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1.00
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W


6170
OW0
WAT
258
−13.951
35.748
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1.00
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W


6171
OW0
WAT
259
−0.528
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1.00
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W


6172
OW0
WAT
260
11.005
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1.00
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W


6173
OW0
WAT
261
27.583
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W


6174
OW0
WAT
262
24.221
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1.00
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W


6176
OW0
WAT
264
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1.00
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W


6177
OW0
WAT
265
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W


6178
OW0
WAT
266
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1.00
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W


6179
OW0
WAT
267
34.994
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1.00
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W


6180
OW0
WAT
268
18.804
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1.00
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W


6181
OW0
WAT
269
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1.00
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W


6182
OW0
WAT
270
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1.00
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W


6183
OW0
WAT
271
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1.00
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W


6184
OW0
WAT
272
1.623
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1.00
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W


6185
OW0
WAT
273
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1.00
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W


6186
OW0
WAT
274
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W


6187
OW0
WAT
275
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1.00
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W


6188
OW0
WAT
276
10.495
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1.00
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W


6189
OW0
WAT
277
23.022
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1.00
23.37
W


6190
OW0
WAT
278
29.535
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1.00
32.39
W


6191
OW0
WAT
279
9.656
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1.00
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W


6192
OW0
WAT
280
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1.00
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W


6193
OW0
WAT
281
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1.00
36.63
W


6194
OW0
WAT
282
40.022
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1.00
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W


6195
OW0
WAT
283
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1.00
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W


6196
OW0
WAT
284
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1.00
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W


6197
OW0
WAT
285
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1.00
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W


6198
OW0
WAT
286
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1.00
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W


6199
OW0
WAT
287
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1.00
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W


6200
OW0
WAT
288
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1.00
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W


6201
OW0
WAT
289
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1.00
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W


6202
OW0
WAT
290
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1.00
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W


6203
OW0
WAT
291
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1.00
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W


6204
OW0
WAT
292
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1.00
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W


6205
OW0
WAT
293
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1.00
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W


6206
OW0
WAT
294
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1.00
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W


6207
OW0
WAT
295
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1.00
39.76
W


6208
OW0
WAT
296
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1.00
39.41
W


6209
OW0
WAT
297
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1.00
29.98
W


6210
OW0
WAT
298
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1.00
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W


6211
OW0
WAT
299
30.906
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1.00
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W


6212
OW0
WAT
300
29.458
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1.00
28.09
W


6213
OW0
WAT
301
12.248
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1.00
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W


6214
OW0
WAT
302
6.586
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1.00
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W


6215
OW0
WAT
303
26.731
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1.00
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W


6216
OW0
WAT
304
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9.188
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1.00
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W


6217
OW0
WAT
305
33.333
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1.00
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W


6218
OW0
WAT
306
6.619
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1.00
32.54
W


6219
OW0
WAT
307
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1.00
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W


6220
OW0
WAT
308
52.161
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1.00
43.46
W


6221
OW0
WAT
309
1.147
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1.00
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W


6222
OW0
WAT
310
42.839
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1.00
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W


6223
OW0
WAT
311
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1.00
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W


6224
OW0
WAT
312
4.967
28.723
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1.00
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W


6225
OW0
WAT
313
22.707
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W


6226
OW0
WAT
314
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1.00
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W


6227
OW0
WAT
315
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1.00
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W


6228
OW0
WAT
316
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1.00
36.65
W


6229
OW0
WAT
317
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1.00
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W


6230
OW0
WAT
318
9.368
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1.00
32.10
W


6231
OW0
WAT
319
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1.00
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W


6232
OW0
WAT
320
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1.00
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W


6233
OW0
WAT
321
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1.00
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W


6234
OW0
WAT
322
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5.939
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1.00
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W


6235
OW0
WAT
323
9.860
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1.00
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W


6236
OW0
WAT
324
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1.00
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W


6237
OW0
WAT
325
23.190
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1.00
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W


6238
OW0
WAT
326
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1.00
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W


6239
OW0
WAT
327
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8.984
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1.00
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W


6240
OW0
WAT
328
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1.00
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W


6241
OW0
WAT
329
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1.00
33.01
W


6242
OW0
WAT
330
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1.00
39.08
W


6244
OW0
WAT
332
0.127
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1.00
39.89
W


6245
OW0
WAT
333
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1.00
32.97
W


6246
OW0
WAT
334
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59.784
1.00
37.45
W


6247
OW0
WAT
335
24.653
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1.00
30.48
W


6248
OW0
WAT
336
11.415
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48.239
1.00
26.80
W


6249
OW0
WAT
337
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51.704
1.00
36.48
W


6250
OW0
WAT
338
2.066
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1.00
35.34
W


6251
OW0
WAT
339
1.824
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43.644
1.00
37.35
W


6252
OW0
WAT
340
12.771
9.948
46.645
1.00
32.82
W


6253
OW0
WAT
341
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54.375
54.379
1.00
30.72
W


6254
OW0
WAT
342
6.100
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38.122
1.00
32.64
W


6255
OW0
WAT
343
17.546
34.296
36.005
1.00
32.50
W


6256
OW0
WAT
344
27.816
0.717
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1.00
35.00
W


6257
OW0
WAT
345
18.540
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1.00
34.20
W


6258
OW0
WAT
346
33.678
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55.722
1.00
33.65
W


6259
OW0
WAT
347
15.061
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1.00
33.22
W


6260
OW0
WAT
348
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1.00
37.41
W


6261
OW0
WAT
349
11.124
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1.00
33.64
W


6262
OW0
WAT
350
12.477
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1.00
35.64
W


6263
OW0
WAT
351
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1.00
35.79
W


6264
OW0
WAT
352
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1.00
38.78
W


6265
OW0
WAT
353
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1.00
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W


6266
OW0
WAT
354
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1.00
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W


6267
OW0
WAT
355
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1.00
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W


6268
OW0
WAT
356
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1.00
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W


6269
OW0
WAT
357
20.857
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1.00
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W


6270
OW0
WAT
358
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1.00
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W


6271
OW0
WAT
359
2.073
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1.00
30.86
W


6272
OW0
WAT
360
45.440
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1.00
36.34
W


6273
OW0
WAT
361
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1.00
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W


6274
OW0
WAT
362
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1.00
38.05
W


6275
OW0
WAT
363
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1.00
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W


6276
OW0
WAT
364
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1.00
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W


6277
OW0
WAT
365
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1.00
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W


6278
OW0
WAT
366
27.548
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1.00
67.95
W


6279
OW0
WAT
367
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1.00
53.38
W


6280
OW0
WAT
368
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1.00
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W


6281
OW0
WAT
369
13.547
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1.00
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W


6282
OW0
WAT
370
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1.00
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W


6283
OW0
WAT
371
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1.00
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W


6284
OW0
WAT
372
0.306
24.495
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1.00
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W


6285
OW0
WAT
373
48.962
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1.00
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W


6286
OW0
WAT
374
10.444
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1.00
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W


6287
OW0
WAT
375
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1.00
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W


6288
OW0
WAT
376
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1.00
33.16
W


6289
OW0
WAT
377
40.462
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1.00
42.45
W


6290
OW0
WAT
378
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1.00
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W


6291
OW0
WAT
379
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1.00
46.13
W


6292
OW0
WAT
380
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1.00
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W


6293
OW0
WAT
381
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1.00
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W


6294
OW0
WAT
382
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1.00
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W


6295
OW0
WAT
383
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1.00
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W


6296
OW0
WAT
384
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1.00
36.33
W


6297
OW0
WAT
385
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1.00
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W


6298
OW0
WAT
386
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1.00
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W


6299
OW0
WAT
387
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1.00
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W


6300
OW0
WAT
388
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1.00
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W


6301
OW0
WAT
389
22.450
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1.00
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W


6302
OW0
WAT
390
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1.00
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W


6303
OW0
WAT
391
23.977
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1.00
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W


6304
OW0
WAT
392
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1.00
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W


6305
OW0
WAT
393
30.244
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1.00
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W


6306
OW0
WAT
394
23.254
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1.00
39.03
W


6307
OW0
WAT
395
22.318
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1.00
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W


6308
OW0
WAT
396
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1.00
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W


6309
OW0
WAT
397
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1.00
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W


6310
OW0
WAT
398
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1.00
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W


6311
OW0
WAT
399
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1.00
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W


6312
OW0
WAT
400
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1.00
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W


6313
OW0
WAT
401
32.383
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1.00
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W


6314
OW0
WAT
402
49.790
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1.00
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W


6316
OW0
WAT
404
33.541
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1.00
48.59
W


6317
OW0
WAT
405
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1.00
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W


6318
OW0
WAT
406
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1.00
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W


6319
OW0
WAT
407
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1.00
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W


6320
OW0
WAT
408
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1.00
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W


6321
OW0
WAT
409
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1.00
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W


6322
OW0
WAT
410
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1.00
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W


6323
OW0
WAT
411
35.604
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1.00
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W


6324
OW0
WAT
412
15.177
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1.00
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W


6325
OW0
WAT
413
44.585
9.274
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1.00
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W


6326
OW0
WAT
414
18.417
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1.00
31.40
W


6327
OW0
WAT
415
18.832
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1.00
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W


6328
OW0
WAT
416
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1.00
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W


6329
OW0
WAT
417
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1.00
39.02
W


6330
OW0
WAT
418
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1.00
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W


6331
OW0
WAT
419
18.978
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1.00
48.35
W


6332
OW0
WAT
420
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1.00
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W


6333
OW0
WAT
421
35.294
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1.00
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W


6334
OW0
WAT
422
21.103
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1.00
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W


6335
OW0
WAT
423
5.611
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1.00
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W


6336
OW0
WAT
424
30.155
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1.00
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W


6337
OW0
WAT
425
42.663
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1.00
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W


6338
OW0
WAT
426
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1.00
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W


6339
OW0
WAT
427
33.849
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W


6340
OW0
WAT
428
39.602
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1.00
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W


6341
OW0
WAT
429
13.310
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1.00
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W


6342
OW0
WAT
430
15.435
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1.00
39.15
W


6343
OW0
WAT
431
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1.00
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W


6344
OW0
WAT
432
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1.00
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W


6345
OW0
WAT
433
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1.00
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W


6346
OW0
WAT
434
19.352
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1.00
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W


6347
OW0
WAT
435
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1.00
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W


6348
OW0
WAT
436
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1.00
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W


6349
OW0
WAT
437
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1.00
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W


6350
OW0
WAT
438
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1.00
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W


6351
OW0
WAT
439
17.511
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1.00
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W


6352
OW0
WAT
440
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1.00
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W


6353
OW0
WAT
441
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1.00
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W


6354
OW0
WAT
442
29.502
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1.00
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W


6355
OW0
WAT
443
9.666
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1.00
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W


6356
OW0
WAT
444
38.197
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1.00
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W


6357
OW0
WAT
445
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1.00
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W


6358
OW0
WAT
446
10.150
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1.00
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W


6359
OW0
WAT
447
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1.00
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W


6360
OW0
WAT
448
26.881
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1.00
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W


6361
OW0
WAT
449
9.031
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1.00
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W


6362
OW0
WAT
450
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1.00
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W


6363
OW0
WAT
451
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1.00
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W


6364
OW0
WAT
452
7.509
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1.00
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W


6365
OW0
WAT
453
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1.00
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W


6367
OW0
WAT
455
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1.00
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W


6369
OW0
WAT
457
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1.00
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W


6370
OW0
WAT
458
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1.00
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W


6371
OW0
WAT
459
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1.00
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W


6372
OW0
WAT
460
45.906
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1.00
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W


6373
OW0
WAT
461
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1.00
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W


6374
OW0
WAT
462
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1.00
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W


6375
OW0
WAT
463
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1.00
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W


6376
OW0
WAT
464
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W


6377
OW0
WAT
465
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W


6378
OW0
WAT
466
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1.00
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W


6379
OW0
WAT
467
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1.00
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W


6380
OW0
WAT
468
7.117
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1.00
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W


6381
OW0
WAT
469
45.294
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1.00
46.87
W


6382
OW0
WAT
470
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1.00
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W


6383
OW0
WAT
471
9.793
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1.00
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W


6384
OW0
WAT
472
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1.00
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W


6385
OW0
WAT
473
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1.00
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W


6386
OW0
WAT
474
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1.00
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W


6387
OW0
WAT
475
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1.00
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W


6388
OW0
WAT
476
27.423
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1.00
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W


6389
OW0
WAT
477
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1.00
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W


6390
OW0
WAT
478
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1.00
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W


6391
OW0
WAT
479
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W


6392
OW0
WAT
480
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1.00
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W


6393
OW0
WAT
481
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1.00
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W


6394
OW0
WAT
482
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1.00
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W


6395
OW0
WAT
483
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1.00
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W


6396
OW0
WAT
484
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1.00
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W


6397
OW0
WAT
485
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1.00
45.20
W


6398
OW0
WAT
486
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1.00
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W


6399
OW0
WAT
487
42.987
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1.00
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W


6400
OW0
WAT
488
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1.00
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W


6401
OW0
WAT
489
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1.00
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W


6403
OW0
WAT
491
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W


6404
OW0
WAT
492
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1.00
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W


6405
OW0
WAT
493
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1.00
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W


6406
OW0
WAT
494
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1.00
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W


6407
OW0
WAT
495
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1.00
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W


6408
OW0
WAT
496
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1.00
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W


6409
OW0
WAT
497
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1.00
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W


6410
OW0
WAT
498
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1.00
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W


6411
OW0
WAT
499
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1.00
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W


6412
OW0
WAT
500
5.606
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1.00
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W


6413
OW0
WAT
501
0.585
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1.00
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W


6414
OW0
WAT
502
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1.00
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W


6415
OW0
WAT
503
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1.00
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W


6416
OW0
WAT
504
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1.00
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W


6417
OW0
WAT
505
2.799
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1.00
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W


6418
OW0
WAT
506
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1.00
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W


6419
OW0
WAT
507
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1.00
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W


6420
OW0
WAT
508
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1.00
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W


6421
OW0
WAT
509
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1.00
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W


6422
OW0
WAT
510
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1.00
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W


6423
OW0
WAT
511
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1.00
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W


6424
OW0
WAT
512
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1.00
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W


6425
OW0
WAT
513
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1.00
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W


6426
OW0
WAT
514
3.804
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1.00
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W


6427
OW0
WAT
515
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1.00
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W


6428
OW0
WAT
516
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1.00
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W


6429
OW0
WAT
517
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W


6430
OW0
WAT
518
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68.748
1.00
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W


6431
OW0
WAT
519
23.423
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1.00
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W


6432
OW0
WAT
520
8.730
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1.00
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W


6433
OW0
WAT
521
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1.00
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W


6434
OW0
WAT
522
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1.00
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W


6435
OW0
WAT
523
40.029
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1.00
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W


6436
OW0
WAT
524
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1.00
34.99
W


6437
OW0
WAT
525
36.464
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1.00
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W


6438
OW0
WAT
526
51.637
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1.00
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W


6439
OW0
WAT
527
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1.00
45.70
W


6440
OW0
WAT
528
26.307
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1.00
45.20
W


6441
OW0
WAT
529
21.836
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42.723
1.00
33.95
W


6442
OW0
WAT
530
37.472
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1.00
47.53
W


6443
OW0
WAT
531
26.392
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1.00
37.05
W


6444
OW0
WAT
532
9.807
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37.207
1.00
37.60
W


6445
OW0
WAT
533
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39.508
1.00
42.70
W


6446
OW0
WAT
534
40.926
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74.588
1.00
44.27
W


6447
OW0
WAT
535
21.981
23.595
40.662
1.00
49.79
W


6448
OW0
WAT
536
12.398
50.065
65.683
1.00
39.01
W


6449
OW0
WAT
537
23.603
42.961
45.081
1.00
49.97
W


6450
OW0
WAT
538
−10.352
47.740
76.915
1.00
46.80
W


6451
OW0
WAT
539
−15.806
39.195
57.947
1.00
39.96
W


6452
OW0
WAT
541
14.503
−5.582
79.614
1.00
53.05
W


6453
OW0
WAT
542
0.684
18.258
44.653
1.00
33.50
W


6454
OW0
WAT
543
5.269
23.624
37.419
1.00
46.63
W


6455
OW0
WAT
544
14.440
−9.982
79.496
1.00
51.43
W


6456
OW0
WAT
545
13.044
−10.837
56.679
1.00
52.73
W


6457
OW0
WAT
546
−13.064
43.674
53.671
1.00
45.82
W


6458
OW0
WAT
547
24.822
10.978
80.940
1.00
44.36
W


6459
OW0
WAT
548
−12.481
48.719
70.168
1.00
41.45
W


6460
OW0
WAT
549
−3.052
4.179
44.889
1.00
58.63
W



















TABLE 4







Complex
PDB Accession No.









CHS-coA complex
1BQ6



CHS-malonyl-CoA complex
1CM1



CHS-hexanoyl-CoA complex
1CHW



CHS-naringenin complex
1CGK



CHS-resveratrol complex
1CGZ










The crystals of the present invention belong to the tetragonal space group. The unit cell dimensions vary by a few angstroms between crystals but on average, chalcone synthase native (SEQ ID NO:1) crystals belong to space group P3221 with unit cell dimensions of a=b=97.54 Å; c=65.52 Å, α=β=90°, γ=120° with a single monomer per asymmetric unit. Stilbene synthase crystals belong to space group C222 with unit cell dimensions of a=74.94 Å, b=86.63 Å, c=364.18 Å, α=β=γ=90°. Pyrone synthase crystals belong to space group P3121 with unit cell dimensions of a=82.15 Å, b=241.33 Å, α=β=90°, γ=120° with one PS dimer per asymmetric unit.
Crystal structures are preferably obtained at a resolution of about 1.56 angstroms to about 3 angstroms for a polyketide synthase in the presence and in the absence of bound substrate or substrate analog. Coordinates for a polyketide synthase in the absence of a substrate bound in the active site have been deposited at the Brookhaven National Laboratory Protein Data Bank, accession number 1CGK. Those skilled in the art understand that a set of structure coordinates determined by X-ray crystallography is not without standard error. Therefore, for the purpose of this invention, any set of structure coordinates wherein the active site α-carbons of a polyketide synthase, synthase homologue, or mutants thereof, have a root mean square deviation less than ±2.3 angstroms when superimposed using the structural coordinates listed in Table 1 and PDB Accession No. 1BI5, shall be considered identical.
A schematic representation of the three-dimensional shape of a CHS homodimer is shown in FIG. 2a, which was prepared by MOLSCRIPT (Kraulis, J. Appl. Crystallogr. 24:946–950, 1991). CHS functions as a homodimer of two 42 kDa polypeptides. The structure of CHS reveals that the enzyme forms a symmetric dimer with each monomer related by a 2-fold crystallographic axis. The dimer interface buries approximately 1580 angstroms with interactions occurring along a fairly flat surface. Two distinct structural features delineate the ends of this interface. First, the N-terminal helix of monomer A entwines with the corresponding helix of monomer B. Second, a tight loop containing a cis-peptide bond between Met137 and Pro138 exposes the methionine sidechain as a knob on the monomer surface. Across the interface, Met137 protrudes into a hole found in the surface of the adjoining monomer to form part of the cyclization pocket (discussed below).
The CHS homodimer contains two functionally independent active sites (Tropf, et al, J. Biol. Chem. 270:7922–7928, 1995). Consistent with this information, bound CoA thioesters and product analogs occupy both active sites of the homodimer in the CHS complex structures. These structures identify the location of the active site at the cleft between the upper and lower domains of each monomer. Each active site consists almost entirely of residues from a single monomer, with Met137 from the adjoining monomer being the only exception. A detailed description of the active site structure is presented in the Examples section, below.
An isolated, polyketide synthase of the invention comprises at least fourteen active site α-carbons having the structural coordinates of Table 1 ±2.3 angstroms. The active site α-carbons of Table 1 generally are not all contiguous, i.e., are not adjacent to one another in the primary amino acid sequence of a polyketide synthase due to intervening amino acid residues between various active site α-carbons. Nevertheless, it should be appreciated that certain active site α-carbons can be adjacent to one another in some instances. Active site α-carbons are numbered in Table 1 for convenience only and may be situated in any suitable order in the primary amino acid sequence that achieves the structural coordinates given in Table 1.
An appropriate combination of R-groups, linked to active site α-carbons, can facilitate the formation of one or more desired reaction products. The combination of R-groups selected for use in a synthase can be any combination other than the ordered arrangements of R-groups found in known native isolated polyketide synthases. Typically, R-groups found on active site α-carbons are those found in naturally occurring amino acids. In some embodiments, however, R-groups other than those found in naturally occurring amino acids can be used.
The present invention permits the use of molecular design techniques to design, select, and synthesize genes encoding mutant polyketide synthases that produce different and/or novel polyketide compounds using substrates. Mutant proteins of the present invention and nucleic acids encoding the same can be designed by genetic manipulation based on structural information about polyketide synthases. For example, one or more R-groups associated with the active site α-carbon atoms of CHS can be changed by altering the nucleotide sequence of the corresponding CHS gene, thus making one or more mutant polyketide synthases. Such genetic manipulations can be guided by structural information concerning the R-groups found in the active site α-carbons when substrate is bound to the protein upon crystallization.
Mutant proteins of the present invention may be prepared in a number of ways available to the skilled artisan. For example, the gene encoding wild-type CHS (SEQ ID NO:1) may be mutated at those sites identified herein as corresponding to amino acid residues identified in the active site by means currently available to the artisan skilled in molecular biology techniques. Said techniques include oligonucleotide-directed mutagenesis, deletion, chemical mutagenesis, and the like. The protein encoded by the mutant gene is then produced by expressing the gene in, for example, a bacterial or plant expression system.
Alternatively, polyketide synthase mutants may be generated by site specific-replacement of a particular amino acid with an unnaturally occurring amino acid. As such, polyketide synthase mutants may be generated through replacement of an amino acid residue or a particular cysteine or methionine residue with selenocysteine or selenomethionine. This may be achieved by growing a host organism capable of expressing either the wild-type or mutant polypeptide on a growth medium depleted of natural cysteine or methionine or both and growing on medium enriched with either selenocysteine, selenomethionine, or both. These and similar techniques are described in Sambrook et al., (Molecular Cloning, A Laboratory Manual, 2nd Ed. (1989) Cold Spring Harbor Laboratory Press).
Another suitable method of creating mutant synthases of the present invention is based on a procedure described in Noel and Tsal (1989) J. Cell. Biochem., 40:309–320. In so doing, the nucleic acids encoding said polyketide synthase can be synthetically produced using oligonucleotides having overlapping regions, said oligonucleotides being degenerate at specific bases so that mutations are induced.
According to the present invention, nucleic acid sequences encoding a mutated polyketide synthase can be produced by the methods described herein, or any alternative methods available to the skilled artisan. In designing the nucleic acid sequence of interest, it may be desirable to reengineer said gene for improved expression in a particular expression system. For example, it has been shown that many bacterially derived genes do not express well in plant systems. In some cases, plant-derived genes do not express well in bacteria. This phenomenon may be due to the non-optimal G+C content and/or A+T content of said gene relative to the expression system being used. For example, the very low G+C content of many bacterial genes results in the generation of sequences mimicking or duplicating plant gene control sequences that are highly A+T rich. The presence of A+T rich sequences within the genes introduced into plants (e.g., TATA box regions normally found in promoters) may result in aberrant transcription of the gene(s). In addition, the presence of other regulatory sequences residing in the transcribed mRNA (e.g. polyadenylation signal sequences (AAUAAA) or sequences complementary to small nuclear RNAs involved in pre-mRNA splicing) may lead to RNA instability. Therefore, one goal in the design of genes is to generate nucleic acid sequences that have a G+C content that affords mRNA stability and translation accuracy for a particular expression system.
Due to the plasticity afforded by the redundancy of the genetic code (i.e., some amino acids are specified by more than one codon), evolution of the genomes of different organisms or classes of organisms has resulted in differential usage of redundant codons. This “codon bias” is reflected in the mean base composition of protein coding regions. For example, organisms with relatively low G+C contents utilize codons having A or T in the third position of redundant codons, whereas those having higher G+C contents utilize codons having G or C in the third position. Therefore, in reengineering genes for expression, one may wish to determine the codon bias of the organism in which the gene is to be expressed. Looking at the usage of the codons as determined for genes of a particular organism deposited in GenBank can provide this information. After determining the bias thereof, the new gene sequence can be analyzed for restriction enzyme sites as well as other sites that could affect transcription such as exon:intron junctions, polyA addition signals, or RNA polymerase termination signals.
Genes encoding polyketide synthases can be placed in an appropriate vector, depending on the artisan's interest, and can be expressed using a suitable expression system. An expression vector, as is well known in the art, typically includes elements that permit replication of said vector within the host cell and may contain one or more phenotypic markers for selection of cells containing said gene. The expression vector will typically contain sequences that control expression such as promoter sequences, ribosome binding sites, and translational initiation and termination sequences. Expression vectors may also contain elements such as subgenomic promoters, a repressor gene or various activator genes. The artisan may also choose to include nucleic acid sequences that result in secretion of the gene product, movement of said product to a particular organelle such as a plant plastid (see U.S. Pat. Nos. 4,762,785; 5,451,513 and 5,545,817, which are incorporated herein by reference) or other sequences that increase the ease of peptide purification, such as an affinity tag.
A wide variety of expression control sequences are useful in expressing the mutated polyketide synthases when operably linked thereto. Such expression control sequences include, for example, the early and late promoters of SV40 for animal cells, the lac system, the trp system, major operator and promoter systems of phage S, and the control regions of coat proteins, particularly those from RNA viruses in plants. In E. coli, a useful transcriptional control sequence is the T7 RNA polymerase binding promoter, which can be incorporated into a pET vector as described by Studier et al., (1990) Methods Enzymology, 185:60–89, which is incorporated herein by reference.
For expression, a desired gene should be operably linked to the expression control sequence and maintain the appropriate reading frame to permit production of the desired polyketide synthase. Any of a wide variety of well-known expression vectors are of use to the present invention. These include, for example, vectors comprising segments of chromosomal, non-chromosomal and synthetic DNA sequences such as those derived from SV40, bacterial plasmids including those from E. coli such as col E1, pCR1, pBR322 and derivatives thereof, pMB9), wider host range plasmids such as RP4, phage DNA such as phage S, NM989, M13, and other such systems as described by Sambrook et al., (Molecular Cloning, A Laboratory Manual, 2nd Ed. (1989) Cold Spring Harbor Laboratory Press), which is incorporated herein by reference.
A wide variety of host cells are available for expressing synthase mutants of the present invention. Such host cells include, for example, bacteria such as E. coli, Bacillus and Streptomyces, fungi, yeast, animal cells, plant cells, insect cells, and the like. Preferred embodiments of the present invention include chalcone synthase mutants that are expressed in E. coli or in plant cells. Said plant cells can either be in suspension culture or a transgenic plant as further described herein.
As stated previously, genes encoding synthases of the present invention can be expressed in transgenic plant cells. In order to produce transgenic plants, vectors containing the nucleic acid construct encoding polyketide synthases and mutants thereof are inserted into the plant genome. Preferably, these recombinant vectors are capable of stable integration into the plant genome. One variable in making a transgenic plant is the choice of a selectable marker. A selectable marker is used to identify transformed cells against a high background of untransformed cells. The preference for a particular marker is at the discretion of the artisan, but any of the selectable markers may be used along with any other gene not listed herein that could function as a selectable marker. Such selectable markers include aminoglycoside phosphotransferase gene of transposon Tn5 (Aph 11) (which encodes resistance to the antibiotics kanamycin), neomycin, G418, as well as those genes which code for resistance or tolerance to glyphosate, hygromycin, methotrexate, phosphinothricin, imidazolinones, sulfonylureas, triazolophyrimidine herbicides, such as chlorosulfuron, bromoxynil, dalapon, and the like. In addition to a selectable marker, it may be desirable to use a reporter gene. In some instances a reporter gene may be used with a selectable marker. Reporter genes allow the detection of transformed cells and may be used at the discretion of the artisan. A list of these reporter genes is provided in K. Wolsing et al., 1988, Ann. Rev. Genetics, 22:421.
Said genes are expressed either by promoters expressing in all tissues at all times (constitutive promoters), by promoters expressing in specific tissues (tissue-specific promoters), promoters expressing at specific stages of development (developmental promoters), and/or promoter expression in response to a stimulus or stimuli (inducible promoters). The choice of these is at the discretion of the artisan.
Several techniques exist for introducing foreign genes into plant cells, and for obtaining plants that stably maintain and express the introduced gene. Such techniques include acceleration of genetic material coated on a substrate directly into cells (U.S. Pat. No. 4,945,050 to Comell): Plant cells may also be transformed using Agrobacterium technology (see, for example, U.S. Pat. No. 5,177,010 to University of Toledo, U.S. Pat. No. 5,104,310 to Texas A & M, U.S. Pat. Nos. 5,149,645, 5,469,976, 5,464,763, 4,940,838, and 4,693,976 to Schilperoot, European Patent Applications 116718, 290799, 320500 to Max Planck, European Patent Applications 604662, 627752 and U.S. Pat. No. 5,591,616 to Japan Tobacco, European Patent Applications 0267159, 0292435 and U.S. Pat. No. 5,231,01.q to Ciba-Geigy, U.S. Pat. Nos. 5,463,174 and 4,762,785 to Calgene, and U.S. Pat. Nos. 5,004,863 and 5,159,135 to Agracetus). Other transformation technologies include whiskers technology (see U.S. Pat. Nos. 5,302,523 and 5,464,765 to Zeneca). Electroporation technology has also been used to transform plants (see WO 87106614 to Boyce Thompson Institute, U.S. Pat. Nos. 5,472,869 and 5,384,253 to Dakalb, and WO 92/09696 and WO 93/21335 to Plant Genetic Systems, all which are incorporated by reference). Viral vector expression systems can also be used such as those described in U.S. Pat. Nos. 5,316,931, 5,589,367, 5,811,653, and 5,866,785 to BioSource, which are incorporated herein by reference.
In addition to numerous technologies for transforming plants, the type of tissue that is contacted with the genes of interest may vary as well. Suitable tissue includes, for example, embryonic tissue, callus tissue, hypocotyl, meristem, and the like. Almost all plant tissues may be transformed during de-differentiation using the appropriate techniques described herein.
Regardless of the transformation system used, a gene encoding a mutant polyketide synthase is preferably incorporated into a gene transfer vector adapted to express said gene in a plant cell by including in the vector an expression control sequence (plant promoter regulatory element). In addition to plant promoter regulatory elements, promoter regulatory elements from a variety of sources can be used efficiently in plant cells to express foreign genes. For example, promoter regulatory elements of bacterial origin, such as the octopine synthase promoter, the nopaline synthase promoter, the mannopine synthase promoter, and the like, may be used. Promoters of viral origin, such as the cauliflower mosaic virus (35S and 198) are also desirable. Plant promoter regulatory elements also include ribulose-1,6-bisphosphate carboxylase small subunit promoter, beta-conglycinin promoter, phaseolin promoter, ADH promoter, heat-shock promoters, tissue specific promoters, and the like. Numerous promoters are available to skilled artisans for use at their discretion.
It should be understood that not all expression vectors and expression systems function in the same way to express the mutated gene sequences of the present invention. Neither do all host cells function equally well with the same expression system. However, one skilled in the art may make a selection among these vectors, expression control sequences, and host without undue experimentation and without departing from the scope of this invention.
Once a synthase of the present invention is expressed, the protein obtained therefrom can be purified so that structural analysis, modeling, and/or biochemical analysis can be performed, as exemplified herein. The nature of the protein obtained can be dependent on the expression system used. For example, genes, when expressed in mammalian or other eukaryotic cells, may contain latent signal sequences that may result in glycosylation, phosphorylation, or other post-translational modifications, which may or may not alter function. Therefore, a preferred embodiment of the present invention is the expression of mutant synthase genes in E. coli calls. Once said proteins are expressed, they can be easily purified using techniques common to the person having ordinary skill in the art of protein biochemistry, such as, for example, techniques described in Colligan at al., (1997) Current Protocols in Protein Science, Chanda, V. B., Ed., John Wiley & Sons, Inc., which is incorporated herein by reference. Such techniques often include the use of cation-exchange or anion-exchange chromatography, gel filtration-size exclusion chromatography, and the like. Another technique that may be commonly used is affinity chromatography. Affinity chromatography can include the use of antibodies, substrate analogs, or histidine residues (His-tag technology).
Once purified, mutants of the present invention may be characterized by any of several different properties. For example, such mutants may have altered active site surface charges of one or more charge units. In addition, said mutants may have altered substrate specificity or product capability relative to a non-mutated polyketide synthase.
The present invention allows for the characterization of polyketide synthase mutants by crystallization followed by X-ray diffraction. Polypeptide crystallization occurs in solutions where the polypeptide concentration exceeds it solubility maximum (i.e., the polypeptide solution is supersaturated). Such solutions may be restored to equilibrium by reducing the polypeptide concentration, preferably through precipitation of the polypeptide crystals. Often polypeptides may be induced to crystallize from supersaturated solutions by adding agents that alter the polypeptide surface charges or perturb the interaction between the polypeptide and bulk water to promote associations that lead to crystallization.
Compounds known as “precipitants” are often used to decrease the solubility of the polypeptide in a concentrated solution by forming an energetically unfavorable precipitating layer around the polypeptide molecules (Weber, Advances in Protein Chemistry, 41:1–36, 1991). In addition to precipitants, other materials are sometimes added to the polypeptide crystallization solution. These include buffers to adjust the pH of the solution and salts to reduce the solubility of the polypeptide. Various precipitants are known in the art and include the following: ethanol, 3-ethyl-2–4 pentanediol, and many of the polyglycols, such as polyethylene glycol.
Commonly used polypeptide crystallization methods include the following techniques: batch, hanging drop, seed initiation, and dialysis. In each of these methods, it is important to promote continued crystallization after nucleation by maintaining a supersaturated solution. In the batch method, polypeptide is mixed with precipitants to achieve supersaturation, the vessel is sealed, and set aside until crystals appear. In the dialysis method, polypeptide is retained in a sealed dialysis membrane that is placed into a solution containing precipitant. Equilibration across the membrane increases the polypeptide and precipitant concentrations thereby causing the polypeptide to reach supersaturation levels.
In the preferred hanging drop technique (McPherson, J. Biot Chem, 6300–6306, 1976), an initial polypeptide mixture is created by adding a precipitant to a concentrated polypeptide solution. The concentrations of the polypeptide and precipitants are such that in this initial form, the polypeptide does not crystallize. A small drop of this mixture is placed on a glass slide that is inverted and suspended over a reservoir of a second solution. The system is then sealed. Typically, the second solution contains a higher concentration of precipitant or other dehydrating agent. The difference in the precipitant concentrations causes the protein solution to have a higher vapor pressure than the solution. Since the system containing the two solutions is sealed, an equilibrium is established, and water from the polypeptide mixture transfers to the second solution. This equilibrium increases the polypeptide and precipitant concentration in the polypeptide solution. At the critical concentration of polypeptide and precipitant, a crystal of the polypeptide will form.
Another method of crystallization introduces a nucleation site into a concentrated polypeptide solution. Generally, a concentrated polypeptide solution is prepared and a seed crystal of the polypeptide is introduced into this solution. If the concentration of the polypeptide and any precipitants are correct, the seed crystal will provide a nucleation site around which a larger crystal forms. In preferred embodiments, the crystals of the present invention are formed in hanging drops with (15% PEG 8000; 200 mM magnesium acetate or magnesium chloride, 100 mM 3-(N-morpholino)-2-hydroxypropanesulfonic acid (pH 7.0), 1 mM dithiothreitol as precipitant).
Some proteins may be recalcitrant to crystallization. However, several techniques are available to the skilled artisan. Quite often the removal of polypeptide segments at the amino or caroxy terminal end of the protein is necessary to produce crystalline protein samples. Said procedures involve either the treatment of the protein with one of several proteases including trypsin, chymotrypsin, substilisin, and the like. This treatment often results in the removal of flexible polypeptide segments that are likely to negatively affect crystallization. Alternatively, the removal of coding sequences from the protein's gene facilitates the recombinant expression of shortened proteins that can be screened for crystallization.
The crystals so produced have a wide range of uses. For example, high quality crystals are suitable for X-ray or neutron diffraction analysis to determine the three-dimensional structure of a mutant polyketide synthase and to design additional mutants thereof. In addition, crystallization can serve as a further purification method. In some instances, a polypeptide or protein will crystallize from a heterogeneous mixture into crystals. Isolation of such crystals by filtration, centrifugation, etc., followed by redissolving the polypeptide affords a purified solution suitable for use in growing the high-quality crystals needed for diffraction studies. The high-quality crystals may also be dissolved in water and then formulated to provide an aqueous solution having other uses as desired.
Because synthases may crystallize in more than one crystal form, the structural coordinates of α-carbons of an active site determined from a synthase or portions thereof, as provided by this invention, are particularly useful to solve the structure of other crystal forms of synthases. Said structural coordinates, as provided herein, may also be used to solve the structure of synthases having α-carbons positioned within the active sites in a manner similar to the wild-type, yet having R-groups that may or may not be identical.
Furthermore, the structural coordinates disclosed herein may be used to determine the structure of the crystalline form of other proteins with significant amino acid or structural homology to any functional domain of a synthase. One method that may be employed for such purpose is molecular replacement. In this method, the unknown crystal structure, whether it is another crystal form of a synthase, a synthase having a mutated active site, or the crystal of some other protein with significant sequence and/or structural homology to a polyketide synthase may be determined using the coordinates given in Table 1. This method provides sufficient structural form for the unknown crystal more efficiently than attempting to determine such information ab initio. In addition, this method can be used to determine whether or not a given polyketide synthase in question falls within the scope of this invention.
As further disclosed herein, polyketide synthases and mutants thereof may be crystallized in the presence or absence of substrates and substrate analogs. The crystal structures of a series of complexes may then be solved by molecular replacement and compared to that of the wild-type to assist in determination of suitable replacements for R-groups within the active site, thus making synthase mutants according to the present invention.
All mutants of the present inventions may be modeled using the information disclosed herein without necessarily having to crystallize and solve the structure for each and every mutant. For example, one skilled in the art may use one of several specialized computer programs to assist in the process of designing synthases having mutated active sites relative to the wild-type. Examples of such programs include: GRID (Goodford, 1985, J. Mod. Chem., 28:849–857), MCSS (Miranker and Karplus, 1991, Proteins: Structure, Function and Genetics, 11:29–34); AUTODOCK (Goodsell and Olsen, 1990, Proteins. Structure, Fumtion, and Genetics, 8:195–202); and DOCK (Kuntz et al., 1982, J. Mot Biol., 161:269–288), and the like, as well as those discussed in the Examples below. In addition, specific computer programs are also available to evaluate specific substrate-active site interactions and the deformation energies and electrostatic interactions resulting therefrom. MODELLER is a computer program often used for homology or comparative modeling of the three-dimensional structure of a protein. A. Saii & T. L. Blundell. J. Mol. Biol. 234:779–815, 1993. A sequence to be modeled is aligned with one or more known related structures and the MODELLER program is used to calculate a full-atom model, based on optimum satisfaction of spatial restraints. Such restraints can include, inter alia, homologous structures, site-directed mutagenesis, fluorescence spectroscopy, NMR experiments, or atom—atom potentials of mean force.
The present invention enables polyketide synthase mutants to be made and the crystal structure thereof to be solved. Moreover, by virtue of the present invention, the location of the active site and the interface of substrate therewith permit the identification of desirable R-groups for mutagenesis.
The three-dimensional coordinates of the polyketide synthase provided herein may additionally be used to predict the activity and or substrate specificity of a protein whose primary amino acid sequence suggests that it may have polyketide synthase activity. The family of CHS-related enzymes is defined, in part, by the presence of four highly conserved amino acid residues, Cys164, Phe215, His303, and Asn336. More than 150 enzymes having these conserved residues have been identified to date, including several bacterial proteins. The functions, substrates, and products of many of these enzymes remains unknown. However, by employing the three-dimensional coordinates disclosed herein and computer modeling programs, structural comparisons of CHS can be made with a putative enzyme. Differences between the two would provide the skilled artisan with information regarding the activity and/or substrate specificity of the putative enzyme. This procedure is demonstrated in the Examples section below.
Thus, in another embodiment of the invention, there is provided a method of predicting the activity and/or substrate specificity of a putative polyketide synthase comprising (a) generating a three-dimensional representation of a known polyketide synthase using three-dimensional coordinate data, (b) generating a predicted three-dimensional representation of a putative polyketide synthase, and (c) comparing the representation of the known polyketide synthase with the representation of the putative polyketide synthase, wherein the differences between the two representations are predictive of activity and/or substrate specificity of the putative polyketide synthase.
In a further embodiment of the present invention, there is also provided a method of identifying a potential substrate of a polyketide synthase comprising (a) defining the active site of the polyketide synthase based on the atomic coordinates of said polyketide synthase, (b) identifying a potential substrate that fits the defined active site, and (c) contacting the polyketide synthase with the potential substrate of (b) and determining the activity thereon. Techniques for computer modeling and structural comparisons similar to those described herein for predicting putative polyketide synthase activity and/or substrate specificity can be used to identify novel substrates for polyketide synthases.
In addition, the structural coordinates and three-dimensional models disclosed herein can be used to design or identify polyketide synthase inhibitors. Using the modeling techniques disclosed herein, potential inhibitor structures can be modeled with the polyketide synthase active site and those that appear to interact therewith can subsequently be tested in activity assays in the presence of substrate.
Methods of using crystal structure data to design binding agents or substrates are known in the art. Thus, the crystal structure data provided herein can be used in the design of new or improved inhibitors, substrates or binding agents. For example, the synthase polypeptide coordinates can be superimposed onto other available coordinates of similar enzymes to identify modifications in the active sites of the enzymes to create novel byproducts of enzymatic activity or to modulate polyketide synthesis. Alternatively, the synthase polypeptide coordinates can be superimposed onto other available coordinates of similar enzymes which have substrates or inhibitors bound to them to give an approximation of the way these and related substrates or inhibitors might bind to a synthase. Alternatively, computer programs employed in the practice of rational drug design can be used to identify compounds that reproduce interaction characteristics similar to those found between a synthase polypeptide and a co-crystalized substrate. Furthermore, detailed knowledge of the nature of binding site interactions allows for the modification of compounds to alter or improve solubility, pharmacokinetics, etc. without affecting binding activity.
Computer programs are widely available that are capable of carrying out the activities necessary to design agents using the crystal structure information provided herein. Examples include, but are not limited to, the computer programs listed below:

    
    
        Catalyst DatabasesTM—an information retrieval program accessing chemical databases such as BioByte Master File, Derwent WDI and ACD;
        Catalyst/HYPOTM—generates models of compounds and hypotheses to explain variations of activity with the structure of drug candidates;
        LudiTM—fits molecules into the active site of a protein by identifying and matching complementary polar and hydrophobic groups;
        LeapfrogTM—“grows” new ligands using a genetic algorithm with parameters under the control of the user.
    
    


In addition, various general purpose machines may be used with programs written in accordance with the teachings herein, or it may be more convenient to construct more specialized apparatus to perform the operations. However, preferably the embodiment is implemented in one or more computer programs executing on programmable systems each comprising at least one processor, at least one data storage system (including volatile and non-volatile memory and/or storage elements), at least one input device, and at least one output device. The program is executed on the processor to perform the functions described herein.
Each such program may be implemented in any desired computer language (including machine, assembly, high level procedural, object oriented programming languages, or the like) to communicate with a computer system. In any case, the language may be a compiled or interpreted language. The computer program will typically be stored on a storage media or device (e.g., ROM, CD-ROM, or magnetic or optical media) readable by a general or special purpose programmable computer, for configuring and operating the computer when the storage media or device is read by the computer to perform the procedures described herein. The system may also be considered to be implemented as a computer-readable storage medium, configured with a computer program, where the storage medium so configured causes a computer to operate in a specific and predefined manner to perform the functions described herein.
Embodiments of the invention include systems (e.g., internet based systems), particularly computer systems which store and manipulate the coordinate and sequence information described herein. One example of a computer system 100 is illustrated in block diagram form in FIG. 9. As used herein, “a computer system” refers to the hardware components, software components, and data storage components used to analyze the coordinates and sequences as set forth in Accession Nos. 1BI5, 1D6F, 1D6I, 1D6H, 1BQ6, 1CML, 1CHW, 1CGK, 1CGZ, Table 1, and Table 3. The computer system 100 typically includes a processor for processing, accessing and manipulating the sequence data. The processor 105 can be any well-known type of central processing unit, such as, for example, the Pentium III from Intel Corporation, or similar processor from Sun, Motorola, Compaq, AMD or International Business Machines.
Typically the computer system 100 is a general purpose system that comprises the processor 105 and one or more internal data storage components 110 for storing data, and one or more data retrieving devices for retrieving the data stored on the data storage components. A skilled artisan can readily appreciate that any one of the currently available computer systems are suitable.
In one particular embodiment, the computer system 100 includes a processor 105 connected to a bus which is connected to a main memory 115 (preferably implemented as RAM) and one or more internal data storage devices 110, such as a hard drive and/or other computer readable media having data recorded thereon. In some embodiments, the computer system 100 further includes one or more data retrieving device 118 for reading the data stored on the internal data storage devices 110.
The data retrieving device 118 may represent, for example, a floppy disk drive, a compact disk drive, a magnetic tape drive, or a modem capable of connection to a remote data storage system (e.g., via the internet) etc. In some embodiments, the internal data storage device 110 is a removable computer readable medium such as a floppy disk, a compact disk, a magnetic tape, etc. containing control logic and/or data recorded thereon. The computer system 100 may advantageously include or be programmed by appropriate software for reading the control logic and/or the data from the data storage component once inserted in the data retrieving device.
The computer system 100 includes a display 120 which is used to display output to a computer user. It should also be noted that the computer system 100 can be linked to other computer systems 125a–c in a network or wide area network to provide centralized access to the computer system 100.
Software for accessing and processing the coordinate and sequences described herein, (such as search tools, compare tools, and modeling tools etc.) may reside in main memory 115 during execution.
For the first time, the present invention permits the use of molecular design techniques to design, select and synthesize novel enzymes, chemical entities and compounds, including inhibitory compounds, capable of binding to a polyketide synthase polypeptide (e.g., a chalcone synthase polypeptide), in whole or in part.
One approach enabled by this invention, is to use the structure coordinates as set forth in Accession Nos. 1BI5, 1D6F, 1D6I, 1D6H, 1BQ6, 1CML, 1CHW, 1CGK, 1CGZ, Table 1, and Table 3 to design new enzymes capable of synthesizing novel polyketides. For example, polyketide synthases (PKSs) generate molecular diversity in their products by utilizing different starter molecule sand by varying the final size of the polyketide chain. The structural coordinates disclosed herein allowed the elucidation of the nature by which PKSs achieve starter molecule selectivity and control polyketide chain length. By comparing the structure of chalcone synthase, which yields a tetraketide product to 2-pyrone synthases which forms a triketide product the invention demonstrated that 2-pyrone synthase maintains a smaller initiation/elongation cavity. Accordingly, generation of a chalcone synthase mutant with an active site sterically analogous to 2-pyrone synthase resulted in the synthesis of a polyketide product of a different size. As discussed more fully below, this invention allows for the strategic development and biosynthesis of more diverse polyketides and demonstrates a structural basis for control of polyketide chain length in other PKSs. In addition, the structural coordinates allow for the development of substrates or binding agents that bind to the polypeptide and alter the physical properties of the compounds in different ways, e.g., solubility.
In another approach a polyketide synthase polypeptide crystal is probed with molecules composed of a variety of different chemical entities to determine optimal sites for interaction between candidate binding molecules (e.g., substrates) and the polyketide synthase (e.g., chalcone synthase).
In another embodiment, an approach made possible and enabled by this invention, is to screen computationally small molecule data bases for chemical entities or compounds that can bind in whole, or in part, to a polyketide synthase polypeptide or fragment thereof. In this screening, the quality of fit of such entities or compounds to the binding site may be judged either by shape complementarity or by estimated interaction energy. Meng, E. C. et al., J. Comp. Chem., 13, pp. 505–524 (1992).
Because chalcone synthase is one member of a family of polyketide synthase polypeptides, many of which have similar functional activity, many polyketide synthase polypeptides may crystallize in more than one crystal form, the structure coordinates of chalcone synthase, or portions thereof, as provided by this invention are particularly useful to solve the structure, function or activity of other crystal forms of polyketide synthase molecules. They may also be used to solve the structure of a polyketide synthase or a chalcone synthase mutant.
One method that may be employed for this purpose is molecular replacement. In this method, the unknown crystal structure, whether it is another polyketide synthase crystal form, a polyketide synthase or chalcone synthase mutant, or a polyketide synthase complexed with a substrate or other molecule, or the crystal of some other protein with significant amino acid sequence homology to any polyketide synthase polypeptide, may be determined using the structure coordinates as provided in Accession Nos. 1BI5, 1D6F, 1D6I, 1D6H, 1BQ6, 1CML, 1CHW, 1CGK, 1CGZ, Table 1, or Table 3. This method will provide 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 the present invention, a polyketide synthase or chalcone synthase polypeptide mutant may be crystallized in association or complex with known polyketide synthase binding agents, substrates, or inhibitors. The crystal structures of a series of such complexes may then be solved by molecular replacement and compared with that of wild-type polyketide synthase molecules. Potential sites for modification within the synthase molecule may thus be identified. This information provides an additional tool for determining the most efficient binding interactions between a polyketide synthase and a chemical entity, substrate or compound.
All of the complexes referred to above may be studied using well-known X-ray diffraction techniques and may be refined to 2–3 Å resolution X-ray data to an R value of about 0.20 or less using computer software, such as X-PLOR (Yale University, 1992, distributed by Molecular Simulations, Inc.). See, e.g., Blundel & Johnson, supra; Methods in Enzymology, vol. 114 and 115, H. W. Wyckoff et al., eds., Academic Press (1985). This information may thus be used to optimize known classes of polyketide synthase substrates or binding agents (e.g., inhibitors), and to design and synthesize novel classes of polyketide synthases, substrates, and binding agents (e.g., inhibitors).
The design of substrates, compounds or binding agents that bind to or inhibit a polyketide synthase polypeptide according to the invention generally involves consideration of two factors. First, the substrate, compound or binding agent must be capable of physically and structurally associating with a polyketide synthase molecule. Non-covalent molecular interactions important in the association of a polyketide synthase with a substrate include hydrogen bonding, van der Waals and hydrophobic interactions, and the like.
Second, the substrate, compound or binding agent must be able to assume a conformation that allows it to associate with a polyketide synthase molecule. Although certain portions of the substrate, compound or binding agent will not directly participate in this association, those portions may still influence the overall conformation of the molecule. This, in turn, may 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., active site or accessory binding site of a polyketide synthase (e.g., a chalcone synthase polypeptide), or the spacing between functional groups of a substrate or compound comprising several chemical entities that directly interact with a polyketide synthase.
The potential binding effect of a substrate or chemical compound on a polyketide synthase or the activity a newly synthesized or mutated polyketide synthase might have on a known substrate may be analyzed prior to its actual synthesis and testing by the use of computer modeling techniques. For example, if the theoretical structure of the given substrate or compound suggests insufficient interaction and association between it and a polyketide synthase, synthesis and testing of the compound may be obviated. However, if computer modeling indicates a strong interaction, the molecule may then be tested for its ability to bind to, initiate catalysis or elongation of a polyketide by a polyketide synthase. Methods of assaying for polyketide synthase activity are known in the art (as identified and discussed herein). Methods for assaying the effect of a newly created polyketide synthase or a potential substrate or binding agent can be performed in the presence of a known binding agent or polyketide synthase. For example, the effect of the potential binding agent can be assayed by measuring the ability of the potential binding agent to compete with a known substrate.
A mutagenized synthase, novel synthase, substrate or other binding compound of an polyketide synthase may be computationally evaluated and designed by means of a series of steps in which chemical entities or fragments are screened and selected for their ability to associate with the individual binding pockets or other areas of the polyketide synthase.
One skilled in the art may use one of several methods to screen chemical entities or fragments for their ability to associate with a polyketide synthase and more particularly with the individual binding pockets of a chalcone synthase polypeptide. This process may begin by visual inspection of, for example, the active site on the computer screen based on the coordinates in Accession Nos. 1BI5, 1D6F, 1D6I, 1D6H, 1BQ6, 1CML, 1CHW, 1CGK, 1CGZ, Table 1, or Table 3. Selected fragments or substrates or chemical entities may then be positioned in a variety of orientations, or docked, within an individual binding pocket of a polyketide synthase. Docking may be accomplished using software such as Quanta and Sybyl, followed by energy minimization and molecular dynamics with standard molecular mechanics forcefields, such as CHARMM and AMBER.
Specialized computer programs may also assist in the process of selecting fragments or chemical entities. These include:
1. GRID (Goodford, P. J., “A Computational Procedure for Determining Energetically Favorable Binding Sites on Biologically Important Macromolecules”, J. Med. Chem., 28, pp. 849–857 (1985)). GRID is available from Oxford University, Oxford, UK.
2. MCSS (Miranker, A. and M. Karplus, “Functionality Maps of Binding Sites: A Multiple Copy Simultaneous Search Method.” Proteins: Structure. Function and Genetics, 11, pp. 29–34 (1991)). MCSS is available from Molecular Simulations, Burlington, Mass.
3. AUTODOCK (Goodsell, D. S. and A. J. Olsen, “Automated Docking of Substrates to Proteins by Simulated Annealing”, Proteins: Structure. Function, and Genetics, 8, pp. 195–202 (1990)). AUTODOCK is available from Scripps Research Institute, La Jolla, Calif.
4. DOCK (Kuntz, I. D. et al., “A Geometric Approach to Macromolecule-Ligand Interactions”, J. Mol. Biol., 161, pp. 269–288 (1982)). DOCK is available from University of California, San Francisco, Calif.
Once suitable substrates, chemical entities or fragments have been selected, they can be assembled into a single polypeptide, compound or binding agent (e.g., an inhibitor). Assembly may be performed 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 the molecules as set forth in Accession Nos. IBIS, 1D6F, 1D6I, 1D6H, 1BQ6, 1CML, 1CHW, 1CGK, 1CGZ, Table 1, or Table 3. This would be followed by manual model building using software such as Quanta or Sybyl.
Useful programs to aid one of skill in the art in connecting the individual chemical entities or fragments include:
1. CAVEAT (Bartlett, P. A. et al, “CAVEAT: A Program to Facilitate the Structure-Derived Design of Biologically Active Molecules”. In “Molecular Recognition in Chemical and Biological Problems”, Special Pub., Royal Chem. Soc., 78, pp. 182–196 (1989)). CAVEAT is available from the University of California, Berkeley, Calif.
2. 3D Database systems such as MACCS-3D (MDL Information Systems, San Leandro, Calif.). This area is reviewed in Martin, Y. C., “3D Database Searching in Drug Design”, J. Med. Chem., 35, pp. 2145–2154 (1992)).
3. HOOK (available from Molecular Simulations, Burlington, Mass.).
In addition to the method of building or identifying novel enzymes or a polyketide synthase substrate or binding agent in a step-wise fashion one fragment or chemical entity at a time as described above, substrates, inhibitors or other polyketide synthase interactions may be designed as a whole or “de novo” using either an empty active site or optionally including some portion(s) of known substrates, binding agents or inhibitors. These methods include:
1. LUDI (Bohm, H.-J., “The Computer Program LUDI: A New Method for the De Novo Design of Enzyme Inhibitors”, J. Comp. Aid. Molec. Design, 6, pp. 61–78 (1992)). LUDI is available from Biosym Technologies, San Diego, Calif.
2. LEGEND (Nishibata, Y. and A. Itai, Tetrahedron, 47, p. 8985 (1991)). LEGEND is available from Molecular Simulations, Burlington, Mass.
3. LeapFrog (available from Tripos Associates, St. Louis, Mo.).
Other molecular modeling techniques may also be employed in accordance with this invention. See, e.g., Cohen, N. C. et al., “Molecular Modeling Software and Methods for Medicinal Chemistry”, J. Med. Chem., 33, pp. 883–894 (1990). See also, Navia, M. A. and M. A. Murcko, “The Use of Structural Information in Drug Design”, Current Opinions in Structural Biology, 2, pp. 202–210 (1992).
Once a substrate, compound or binding agent has been designed or selected by the above methods, the efficiency with which that substrate, compound or binding agent may bind to a polyketide synthase may be tested and optimized by computational evaluation.
A substrate or compound designed or selected as a polyketide binding agent may be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the target site. 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 binding agent and the polyketide synthase when the binding agent is bound to the polyketide synthase, 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: Gaussian 92, revision C (M. J. Frisch, Gaussian, Inc., Pittsburgh, Pa., 1992); AMBER, version 4.0 (P. A. Kollman, University of California at San Francisco, 1994); QUANTA/CHARMM (Molecular Simulations, Inc., Burlington, Mass. 1994); and Insight II/Discover (Biosysm Technologies Inc., San Diego, Calif., 1994). These programs may be implemented, for example, using a Silicon Graphics workstation, IRIS 4D/35 or IBM RISC/6000 workstation model 550. Other hardware systems and software packages will be known to those skilled in the art of which the speed and capacity are continually modified
Once a polyketide synthase, polyketide synthase substrate or polyketide synthase binding agent has been selected or designed, as described above, substitutions may 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, e.g., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. Such substituted chemical compounds may then be analyzed for efficiency of fit to a polyketide synthase substrate or fit of a modified substrate to a polyketide synthase having a structure defined by the coordinates in Accession Nos. 1BI5, 1D6F, 1D6I, 1D6H, 1BQ6, 1CML, 1CHW, 1CGK, 1CGZ, Table 1, or Table 3, by the same computer methods described, above.
Conserved regions of the polyketide family synthases lend themselves to the methods and compositions of the invention. For example, pyrone synthase and chalcone synthase have conserved residues present within their active sites (as described more fully below). Accordingly, modification to the active site of chalcone synthase or a chalcone synthase substrate can be extrapolated to other conserved members of the polyketide family of synthases such as, for example, pyrone synthase.
Functional fragments of polyketide synthase polypeptides such as, for example, fragments of chalcone synthase can be designed based on the crystal structure and atomic coordinates described herein. Fragments of a chalcone synthase polypeptide and the fragment's corresponding atomic coordinates can be used in the modeling described herein. In addition, such fragments may be used to design novel substrates or modified active sites to create new diverse polyketides.
In one embodiment of the present invention, the crystal structure and atomic coordinates allow for the design of novel polyketide synthases and novel polyketide synthase substrates. The development of new polyketide synthases will lead to the development a biodiverse repetoir of polyketides for use as antibiotics, anti-cancer agents, anti-fungal agents and other therapeutic agents as described herein or known in the art. In vitro assay systems for production and determination of activity are known in the art. For example, antibiotic activities of novel polyketides can be measured by any number of anti-microbial techniques currently used in hospitals and laboratories. In addition, anticancer activity can be determined by contacting cells having a cell proliferative disorder with a newly synthesized polyketide and measuring the proliferation or apoptosis of the cells before and after contact with the polyketide. Specific examples of apoptosis assays are provided in the following references: Lymphocyte: C. J. Li et al., Science, 2:429–431, 1995; D. Gibellini et al., Br. J. Haematol. 89:24–33, 1995; S. J. Martin et al., J. Immunol. 152:330–42, 1994; C. Terai et al., J. Clin Invest. 87:1710–5, 1991; J. Dhein et al., Nature 373:438–441, 1995; P. D. Katsikis et al., J. Exp. Med. 1815:2029–2036, 1995; Michael O. Westendorp et al., Nature 375:497, 1995; DeRossi et al., Virology 198:234–44, 1994. Fibroblasts: H. Vossbeck et al, Int. J. Cancer 61:92–97, 1995; S. Goruppi et al., Oncogene 9:1537–44, 1994; A. Fernandez et al, Oncogene 9:2009–17, 1994; E. A. Harrington et al, Embo J. 13:3286–3295, 1994; N. Itoh et al., J. Biol. Chem. 268:10932–7, 1993. Neuronal Cells: G. Melino et al., Mol. Cell. Biol. 14:6584–6596, 1994; D. M. Rosenbaum et al, Ann. Neurol. 36:864–870, 1994; N. Sato et al, J. Neurobiol 25:1227–1234, 1994; G. Ferrari et al., J. Neurosci. 1516:2857–2866, 1995; A. K. Talley et al., Mol. Cell. Biol. 1585:2359–2366, 1995; A. K. Talley et al., Mol. and Cell. Biol. 15:2359–2366, 1995; G. Walkinshaw et al, J. Clin. Invest. 95:2458–2464, 1995. Insect Cells: R. J. Clem et al, Science 24:1388–90, 1991; N. E. Crook et al., J. Virol. 67:2168–74, 1993; S. Rabizadeh et al, J. Neurochem. 61:2318–21, 1993; M. J. Birnbaum et al, J. Virol 68:2521–8, 1994; R. J. Clem et al., Mol. Cell. Biol. 14:5212–5222, (1994). Other assays are well within the ability of those of skill in the art.
Product of novel polyketides or polyketide synthases can be carried out in culture. For example, mammalian expression constructs carrying polyketide synthases can be introduced into various cell lines such as CHO, 3T3, HL60, Rat-1, or Jurkart cells, for example. In addition, SF21 insect cells may be used in which case the polyketide synthase gene is expressed using an insect heat shock promotor.
In another embodiment of the present invention, once a novel substrate or binding agent is developed by the computer methodology discussed above, the invention provides a method for determining the ability of the substrate or agent to be acted upon by a polyketide synthase. The method includes contacting components comprising the substrate or agent and a polyketide synthase polypeptide, or a recombinant cell expressing a polyketide synthase polypeptide, under conditions sufficient to allow the substrate or agent to interact and determining the affect of the agent on the activity of the polypeptide. The term “affect”, as used herein, encompasses any means by which protein activity can be modulated, and includes measuring the interaction of the agent with the polyketide synthase molecule by physical means including, for example, fluorescence detection of the binding of an agent to the polypeptide. Such agents can include, for example, polypeptides, peptidomimetics, chemical compounds, small molecules, substrates and biologic agents as described herein. Examples of small molecules include but are not limited to small peptides or peptide-like molecules.
Contacting or incubating includes conditions which allow contact between the test agent or substrate and a polyketide synthase or modified polyketide synthase polypeptide or a cell expressing a polyketide synthase or modified polyketide synthase polypeptide. Contacting includes in solution and in solid phase. The substrate or test agent may optionally be a combinatorial library for screening a plurality of substrates or test agents. Agents identified in the method of the invention can be further evaluated by chromatography, cloning, sequencing, and the like.
Although methods and materials similar or equivalent to those described herein can be used to practice the invention, suitable methods and materials are described below. All publications, patent applications, patents and other references mentioned herein are incorporated by reference in their entirety. The invention will now be described in greater detail by reference to the following non-limiting examples.
EXAMPLES
Mutagenesis, expression, and purification. Alfalfa CHS2 cDNA (Junghans, H., et al., Plant Mol. Biol. 22:239–253, 1993) was subcloned into pHIS8 plasmid vector derived from pET-28a (+) (Novagen). PCR-based mutagenesis using the QUIKCHANGETM system (Stratagene) generated the various mutants including C164S, C164D, H303A, H303Q, H303D, H303T, N336A, N336D, N336Q, N336H, F215S, F215Y and F215W. N-terminal His8-tagged CHS was expressed in BL21 (DE3) E. coli cells. Cells were harvested and lysed by sonication. His-tagged CHS was purified from bacterial sonicates using a NI-NTA (Qiagen) column. Thrombin digest removed the His-tag and the protein was passed over another NI-NTA column and a benzamidine SEPHAROSE® (Pharmacia) column. The final purification step used a SUPERDEXTM 200 16/60 (Pharmacia) column.
Crystallization. CHS crystals (wild-type and C164S mutant, SEQ ID NO:1) were grown by vapor diffusion at 4° C. in 2 μl drops containing a 1:1 mixture of 25 mg/ml protein and crystallization buffer (2.2–2.4 M ammonium sulfate and 0.1 M PIPES, pH 6.5) in the presence or absence of 5 mM DTT. Prior to freezing at 105° K, crystals were stabilized in 40% (v/v) PEG400, 0.1 M PIPES (pH 6.5), and 0.050–0.075 M ammonium sulfate. This cryoprotectant was used for heavy atom soaks. Likewise, all substrate and product analog complexes were obtained by soaking crystals in cryoprotectant containing 10–20 mM of the compound.
Data Collection and Processing. X-ray diffraction data were collected at 105° K using a DIP2000 imaging plate system (Mac-Science Corporation, Japan) and CuK radiation produced by a rotating anode operated at 45 kV and 100 mA and equipped with double focusing Pt/Ni coated mirrors. Native CHS crystals (SEQ ID NO:1) belong to space group P32,21 with unit cell dimensions of a=b=97.54 Å; c=65.52 Å with a single monomer per asymmetric unit. Data were indexed and integrated using DENZO (Otwinowski & Minor, Meth. Enzymol. 276:307–326, 1997) and scaled with SCALEPACK (Otwinowski & Minor, Meth. Enzymol. 276:307–326, 1997). The heavy atom derivative datasets were scaled against the native dataset with SCALEIT (CCP4 Suite: Programs for protein crystallography, Acta Crystallogr. D 50:760–763, 1994).
Structure determination. MIRAS was used to solve the structure of native CHS (SEQ ID NO:1) using native data set 1 (1.8 Å). Initial phasing was performed with derivative datasets including reflections to 2.3 A resolution. Heavy atom positions for the Hg (OAc) 2 derivative were estimated by inspection of difference Patterson maps using the program XTALVIEW (McRee, J. Mol. Graph. 10:44–46, 1992) and initially refined with MLPHARE (Otwinowski, Z. in CCP4 Proc. 80–88, Daresbury Laboratory, Warrington, UK, 1991). Heavy atom positions for the additional derivative data sets were determined by difference Fourier analysis using phases calculated from the Hg (OAc)2 data set and the Hg positions. These sites were confirmed by inspection of difference Patterson maps. Final refinement of heavy atom parameters, identification of minor heavy atom binding sites, and phase-angle calculations were performed with the program SHARP (de La Fortelle, & Bricogne, Meth. Enzymol. 276:472–494, 1997). MIRAS phases were improved and extended to 1.8 Å by solvent flipping using the CCP4 program SOLOMON (Abrahams, & Leslie, Acta Crystallogr. D 52: 30–42, 1996).
Model building and refinement. The program O (Jones, et al, Acta Crystallogr. D 49:148–157, 1993) was used for model building and graphical display of the molecules and electron-density maps. The experimental map for the native 1 dataset at 1.8 Å was of high quality and allowed unambiguous modeling of residues 3 to 389. The model was first refined with REFMAC (Murshudov, et al, Acta Crystallogr. D 53:240–255, 1997) and ARP (Lamzin & Wilson, Acta Crystallogr. D 49:129–147, 1993) against the native 1 dataset. This was followed by manual adjustments using I2Fo-Fc1 difference maps. Water molecules introduced by ARP were edited using the I2Fo-Fc1 and IFo-Fc1 maps. A second refinement with SHELX-97 (Sheldrick & Schneider, Meth. Enzymol. 277:319–343, 1997) was then carried out against the native 2 data set to 1.56 Å resolution. Structures of CHS complexed with naringenin and resveratrol and the C164S mutant complexed with malonyl- and hexanoyl-CoA were obtained using difference Fourier methods and were refined with REFMAC and ARP. All structures were checked with PROCHECK (Laskowski, et al, J. Appl. Crystallogr. 26:283–291, 1993). 91.3% of the residues in CHS are in the most favored regions of the Ramachandran plot, 8.4% in the additional allowed region, and 0.3% in the generously allowed region.
Three Dimensional Structure Determination and Description
Recombinant alfalfa CHS2 was expressed in E. coli, affinity purified using an N-terminal poly-His linker, and crystallized. The structure of wild-type CHS (SEQ ID NO:1) was determined using multiple isomorphous replacement supplemented with anomalous scattering (MIRAS) (Table X). The final 1.56 Å resolution apoenzyme model of CHS included 2982 protein atoms and 355 water molecules. In addition, the structures of a series of complexes were obtained by difference Fourier analysis. First, a crystal of a mutant (C164S) was soaked with malonyl-CoA. This mutant retains limited catalytic activity, and the resulting acetyl-CoA complex yields insight on the decarboxylation reaction. The same mutant was also complexed with hexanoyl-CoA to mimic the structure of a linear polyketide-CoA reaction intermediate. Finally, two product analogs, naringenin and resveratrol (see FIG. 1) were complexed with CHS to provide information on how the enzyme governs sequential addition of acetates to the coumaroyl moiety and how CHS controls the stereochemistry of the polyketide cyclization reaction. In plants, chalcone isomerase rapidly and stereospecifically converts chalcone to naringenin ((−)(2S)-5,7,4′-trihydroxyflavanone) through an additional ring closure. This reaction also occurs at a slower rate and non-stereospecifically in solution. As such, naringenin provides a suitable mimic of the CHS reaction product. Finally, since STS uses the same substrates as CHS but a different cyclization pathway for the biosynthesis of resveratrol, resveratrol was also soaked into CHS to investigate the structural features governing cyclization of the same substrates into two different products.
CHS functions as a homodimer of two 42 kDa polypeptides. The structure of CHS revealed that the enzyme forms a symmetric dimer with each monomer related by a 2-fold crystallographic axis (See FIGS. 2a and 2b). The dimer interface buries approximately 1580 Å2 with interactions occurring along a fairly flat surface. Two distinct structural features delineate the ends of this interface. First, the N-terminal helix of monomer A entwines with the corresponding helix of monomer B. Second, a tight loop containing a cis-peptide bond between Met137 and Pro138 exposes the methionine sidechain as a knob on the monomer surface. Across the interface, Met137 protrudes into a hole found in the surface of the adjoining monomer to form part of the cyclization pocket.
Each CHS monomer consists of two structural domains (see FIG. 3). The upper domain exhibits an xBxBx pseudo-symmetric motif originally observed in thiolase from Saccharomyces cerevisiae (Mathieu, et al, Structure 2:797–808, 1994). The upper domains of CHS and thiolase are superimposeable with a r.m.s. deviation of 3.3 Å for 266 equivalent C-atoms. Both enzymes use a cysteine as a nucleophile and shuttle reaction intermediates via CoA molecules. However, CHS condenses a p-coumaroyl- and three malonyl-CoA molecules through an iterative series of reactions, whereas thiolase generates two acetyl-CoA molecules from acetoacetyl-CoA and free CoA. The drastic structural differences in the lower domain of CHS create a larger active site than that of thiolase and provide space for the polyketide reaction intermediates required for chalcone formation.
The CHS homodimer contains two functionally independent active sites. Consistent with this information, bound CoA thioesters and product analogs occupy both active sites of the homodimer in the CHS complex structures. These structures identify the location of the active site at the cleft between the upper and lower domains of each monomer. Each active site consists almost entirely of residues from a single monomer with Met, 3, from the adjoining monomer being the only exception. There are remarkably few chemically reactive residues in the active site. Four residues conserved in all the known CHS-related enzymes (Cys164, Phe215, His303, and Asn336 of SEQ ED NO:1) define the active site. Cys164 apparently serves as the nucleophile and as the attachment site for polyketide intermediates as previously suggested for both CHS and STS (Lanz, et al, J. Biol. Chem. 266: 9971–9976, 1991). His303 most likely acts as a general base during the generation of a nucleophilic thiolate anion from Cys, since the N of His303 is within hydrogen bonding distance of the sulfur of Cys164. Phe215 and Asn336 may function in the decarboxylation reaction, as discussed below. Topologically, three interconnected cavities intersect with these four residues and form the active site architecture of CHS. These cavities include a CoA-binding tunnel, a coumaroyl-binding pocket, and a cyclization pocket.
The CoA-binding tunnel is 16 angstroms long and links the surrounding solvent with the buried active site. Binding of the CoA moiety in this tunnel positions substrates at the active site, as observed in the C164S mutant of SEQ ID NO:1 (described in greater detail below) complexed with malonyl- or hexanoyl-CoA. The conformation of the CoA molecules bound to CHS resembles that observed in other CoA binding enzymes. The adenosine nucleoside is in the 2′-endo conformation with an anti-glycosidic bond torsion angle. At the tunnel entrance, Lys55, Arg58, and Lys62 of SEQ ID NO:1 hydrogen bond with two phosphates of CoA. Apart from these interactions, and an additional hydrogen bond between the backbone amide nitrogen of Ala308 of SEQ ID NO:1 and the first carbonyl of the pantetheine moiety, van der Waals contacts dominate the remaining interactions between CHS and CoA. The pantetheine arm of the CoA extends into the enzyme positioning the terminally bound thioester-linked substrates near Cys164 of SEQ ID NO:1.
Both naringenin and resveratrol bind at the active site end of the CoA-binding tunnel. The interactions observed in the naringenin and resveratrol complexes define the coumaroyl-binding and cyclization pockets (see FIG. 5). The space to the lower left of the CoA-binding tunnel's end serves as the coumaroyl-binding pocket Residues of this pocket (Ser133, Glu192, Thr194, Thr197, and Ser338 of SEQ ID NO:1) surround the coumaroyl-derived portion of the bound naringenin and resveratrol molecules and interact primarily trough van der Waals contacts. However, the carbonyl oxygen of Gly216 of SEQ ID NO:1 hydrogen bonds to the phenolic oxygen of both naringenin and resveratrol and the hydroxyl of Thr197 of SEQ ID NO:1 interacts with the carbonyl of naringenin derived from coumaroyl-CoA. The identity of the residues in this pocket likely contributes to the preference for coumaroyl-CoA as a substrate for parsley CHS over other cinnamoyl CoA starter molecules, like caffeoyl- or feruloyl-CoA.
In both the naringenin and resveratrol complexes, the malonyl-derived portion of each molecule occupies a large pocket adjacent to Cys164 of SEQ ID NO:1 suggesting this is where the polyketide reaction intermediate cyclizes into the new ring system and where aromatization of the ring occurs. The six-carbon chain of hexanoyl-CoA also binds in this pocket. Physically, the size of the pocket limits the number of acetate additions to three. Phe265 of SEQ ID NO:1 separates the coumaroyl-binding site from the cyclization pocket and may function as a mobile steric gate during successive rounds of polyketide elongation. Although a polyketide possesses a number of hydrogen bond acceptors through which specific interactions could aid in proper folding for the cyclization reaction, the residues of the cyclization pockets including Thr132, Met137, Phe215, Ile254, Gly256, Phe265, and Pro375 of SEQ ID NO:1 provide few potential hydrogen bond donors. As in the coumaroyl-binding pocket, van der Waals contacts dominate the interaction between CHS and both naringenin and resveratrol. Thus, the surface topology of the cyclization pocket dictates how the malonyl-derived portion of the polyketide is folded and how the stereochemistry of the cyclization reaction leading to chalcone formation in CHS and resveratrol formation in STS is controlled.
Reaction Mechanism
The position of the CoA thioesters and product analogs in the CHS active site suggest binding modes for substrates and intermediates in the polyketide elongation mechanism that are consistent with the known product specificity of CHS. In addition, the stereochemical features of the substrate and product analog complexes elucidate the roles of Cys164, Phe215, His303, and Asn336 in the reaction mechanism. Utilizing structural constraints derived from the available complexes, the following reaction sequence is proposed (see FIG. 6).
In the mechanism, binding of p-coumaroyl-CoA initiates the CHS reaction. Functional and structural evidence supports a coumaroyl-first mechanism over a malonyl-first one. Cerulenin, a potent irreversible inhibitor of CHS, covalently modifies Cys164 in CHS (Lanz, et al., J. Biol. Chem. 266:9971–9976, 1991). Preincubation of CHS with coumaroyl-CoA prevents inactivation by cerulenin, but pre-incubation with malonyl-CoA does not (Preisig-Mueller, et al., Biochemistry 36:8349–8358, 1997). Also, the location of the coumaroyl-derived portion of naringenin and resveratrol in the CHS complexes agrees with a coumaroyl first mechanism, since the presence of a triketide reaction intermediate attached to Cys164 would limit access to the coumaroyl-binding pocket.
After p-coumaroyl-CoA binds to CHS, Cys164, activated by His303, attacks the thioester linkage, transferring the coumaroyl moiety to Cys164 (Monoketide Intermediate). Asn336 hydrogen bonds with the carbonyl oxygen of the thioester further stabilizing formation of the tetrahedral reaction intermediate. CoA then dissociates from the enzyme, leaving a coumaroyl-thioester at Cys164. Binding of the first malonyl-CoA positions the bridging methylene carbon of the malonyl moiety near the carbonyl carbon of the covalently attached coumaroyl-thioester. Decarboxylation of malonyl-CoA leads to carbanion formation. Resonance between the keto and enol species stabilizes the carbanion. Attack of this carbanion on the coumaroyl-thioester releases the thiolate anion of Cys164 and transfers the coumaroyl group to the acetyl moiety of the CoA thioester (Diketide CoA Thioester). Capture of this elongated diketide-CoA by Cys164 and release of CoA sets the stage for two additional rounds of elongation resulting in formation of the tetraketide reaction intermediate.
Asn336 appears to play a crucial role in the decarboxylation reaction. Structural evidence shows that the decarboxylation reaction does not require transfer of the malonyl moiety to Cys1,6 as originally indicated by CO2 exchange assays. Decarboxylation occurs without Cys164, since the C164S mutant produces acetyl-CoA as determined crystallographically and confirmed by a functional assay. In the hexanoyl-CoA complex, the side chain amide of Asn336 provides a hydrogen bond to the carbonyl oxygen of the thioester. This interaction would stabilize the enolate anion resulting from decarboxylation of malonyl-CoA (see FIG. 6). At the same time, the lack of formal positive charge at Asn336 may preserve the partial carbanion character of this resonance-stabilized anion, and thus the nucleophilicity of the carbanion form.
The role of Phe215 in the catalytic mechanism is subtler than that of Asn336. Its position in both CoA complexes suggests that it provide van der Waals interactions for substrate binding. However, its conservation in bacterial enzymes related to CHS that do not make flavonoids or stilbenes may indicate a more general catalytic role for Phe215. Its position near the acetyl moiety of the malonyl-CoA complex suggests that it participates in decarboxylation by favoring conversion of the negatively charged carboxyl group to a neutral carbon dioxide molecule.
FIG. 7A depicts the addition of the third malonyl-CoA molecule as a three-dimensional model. The position of the coumaroyl ring in the modeled triketide intermediate is as observed in the naringenin and resveratrol complexes. The coumaroyl-binding pocket locks this moiety in position, while the acetate units added in subsequent chain extension steps bend to fill the cyclization pocket. The backbone of bound hexanoyl-CoA provides a guide for modeling the triketide reaction intermediate attached to Cys164. Based on the observed acetyl-CoA complex, a rotation of the acetyl group would place the terminal methylene of the decarboxylated malonyl-CoA in position for nucleophilic attack on the triketide thioester linkage resulting in formation of a tetraketide CoA thioester.
The cyclization reaction catalyzed by CHS is an intramolecular Claisen condensation encompassing the three acetate units derived from three malonyl-CoAs. During cyclization, the nucleophilic methylene group nearest the coumaroyl moiety attacks the carbonyl carbon of the thioester linked to Cys164. Ring closure proceeds through an internal proton transfer from the nucleophilic carbon to the carbonyl oxygen. Modeling of the tetraketide intermediate in a conformation leading to chalcone formation places one of the acidic protons of the nucleophilic carbon (C6) proximal to the target carbonyl (C1) (see FIG. 7B). Since there is no base capable of proton abstraction from the tetraketide, it is proposed that the intermediate itself provides the driving force for carbanion formation. Protonation of the carbonyl oxygen would also stabilize the negative charge on the tetrahedral intermediate. Breakdown of this tetrahedral intermediate expels the newly cyclized ring system from Cys164. Subsequent aromatization of the trione ring through a second series of facile internal proton transfers yields chalcone.
Although the cyclization reaction has been modeled as occurring via a polyketide intermediate attached to Cys164, it is possible that the reaction proceeds when the polyketide is attached to CoA. The rate of cyclization versus the rate of reattachment to Cys164 would dictate which of the two cyclization alternatives is mechanistically preferred.
An important question in the biosynthesis of chalcones concerns the exchangeability of the polyketide reaction intermediates. In the presence of chalcone reductase (CHR), CHS produces 6-deoxychalcone (Welle & Grisebach, FEBS Lett. 236:22–225, 1988). Mechanistically, CHR must reduce a ketone on the polyketide intermediate before cyclization occurs. Based on the CHS structure, any polyketide attached to Cys164 would be inaccessible to CHR unless a drastic structural change occurs in CHS upon interaction with CHR. While this conformational change is possible, such a change is difficult to imagine given the buried nature of the CHS active site. This would argue for the presence of moderately exchangeable polyketide-CoA reaction intermediates. Consistent with this idea, a recently identified CHS-like enzyme from Pinus strobus involved in the biosynthesis of C-methylated chalcones is active only with a starter molecule that is sterically analogous to the diketide-CoA intermediate postulated to be formed after the first condensation reaction in CHS30. These results suggest that the enzymes involved in the biosynthesis of plant polyketides may require specific localization in the plant cell to allow efficient channeling of intermediates from one enzyme to another during the production of particular products.
Cyclization Specificity of CHS and STS
Both CHS and STS use the same precursor molecules and reaction mechanism to create a common tetraketide intermediate. Each enzyme must then impart a different folded conformation on this intermediate to facilitate the different cyclization reactions that yield chalcone and resveratrol. Although the three-dimensional structure of STS remains unknown, determination of the CHS structure allows speculation about the basis for the intramolecular aldol condensation and cyclization reaction catalyzed by STS. This alternate pathway involves nucleophilic attack of the methylene group (C2) nearest the thioester linkage to Cys164 on the carbonyl carbon (C7) of the coumaroyl moiety (see FIG. 7c). Again, modeling of the tetraketide intermediate in a conformation leading to cyclization suggests an internal proton transfer mechanism. Unlike CHS, this cyclization intermediate remains covalently attached to STS. Completion of the reaction sequence requires hydrolysis from Cys164 and an additional decarboxylation step prior to formation of resveratrol. These extra steps may account for the lower product formation rates observed with STS than with CHS (Schroeder J., et al., Biochemistry 37:8417–8425, 1998). Alternatively, the cyclization reaction may use a tetraketide-CoA thioester reaction intermediate, and subsequent hydrolysis and decarboxylation in solution.
The identity of the residue or residues involved in modulating between the intramolecular Claisen condensation in CHS and the aldol condensation in STS remains equivocal. The known CHS and STS enzymes exhibit no consistent differences in the residues lining the active site, although sequence variability between the CHS and STS enzymes does occur in the solvent exposed residues of strands β1d (residues 253 to 259) and β2d (residues 262–268) lining the cyclization pocket (see FIGS. 5b and 5c). Comparison of the naringenin and resveratrol complexes provides a possible explanation for modulation of the cyclization stereochemistry.
The cyclization pocket of CHS accommodates the newly cyclized ring of naringenin more easily than that of resveratrol. Strand β1d (residues 253 to 259) moves slightly to enlarge the cyclization pocket in the resveratrol complex compared to the naringenin complex. Two residues that consistently vary between CHS-like and STS-like enzymes, Asp255 and Leu268, move closer together in the resveratrol complex as β1d shifts position. Sequence variations of the solvent exposed residues of strands β1d and β2d may determine the conformation of the tetraketide intermediate before ring formation. Therefore, alterations in the surface topology of the cyclization pocket, mediated partially by the position of strand β1d, may affect the stereochemistry of the cyclization reaction and modulate product selectivity.
Structural Basis for Functionally Novel CHS-Like Enzymes
Absolute conservation of Cys164, Phe215, His303, and Asn336 of SEQ ID NO:1 occurs in CHS-like sequences, including several bacterial proteins possessing very low (typically 2030%) amino acid sequence identity. Moreover, all CHS-like proteins exhibit strong conservation of residues shaping the geometry of the active site (Pro138, Gly163, Gly167, Leu214, Asp217, Gly262, Pro304, Gly305, Gly306, Gly335, Gly374, Pro375, and Glu376 of SEQ ID NO:1). Although the functions of the bacterial CHS-like proteins remain known, these enzymes likely form polyketides or polyketide-CoA thioesters in a manner resembling CHS. However, steric differences resulting from sequence variation in both the coumaroyl-binding pocket and the cyclization pocket strongly suggest alternate substrate and product specificity in the bacterial enzymes.
The sequence databases include approximately 150 plant enzyme sequences classified as CHS like proteins. The substrate and product specificity of a majority of these sequences remains to be determined. In addition, the high sequence similarity of all plant sequences complicates classification of these sequences as authentic CHS, STS, ACS, or BBS enzymes. The information provided by the three-dimensional structure of CHS should make new substrate and product specificity more readily discernible from sequence information.
To illustrate the usefulness of structural information in identifying potentially new activities, a CHS-related sequence from Gerbera hybrids (GCHS2)32 that is 74% identical with alfalfa CHS2 was examined. Modeling the active site architecture of GCHS2 using the structure of alfalfa CHS2 as a template indicates that GCHS2 will not catalyze either the CHS-like or STS-like reaction (see FIG. 8). This variation in reaction specificity results from striking steric differences in the coumaroyl binding and cyclization pockets that substantially reduce the volume of both pockets from 923 Å3 in CHS to 269 Å3 in GCHS2. Side chain variation at positions 197 and 338 alter the coumaroyl binding pocket, while the identity of residue 256 dictates major steric changes in the cychzation pocket. The reduced size of these pockets in GCHS2 suggests that fewer than three acetate additions will occur, and that a CoA thioester with an acyl moiety smaller than p-coumaroyl initiates the reaction. Recent functional characterization of GCHS2 confirms this prediction and demonstrates that this enzyme uses acetyl-CoA or benzoyl-CoA and two condensation reactions with malonyl-CoA to form pyrone products (Eckermann, et al., Nature 396:397–396, 1998).
Crystallization of Additional Polyketide Synthases
Stilbene synthase from Pinus strubus was overexpressed in E. coli as an octahistidyl N-terminal fusion protein, purified to >90% homogeneity by metal affinity and gel filtration chromatography, and crystallized in the preparation lacking the N-terminal polyhistidine tag (removed by thrombin cleavage) from 13% (w/v) polyethylene glycol (PEG8000), 0.05 M MOPSO, 0.3 M ammonium acetate at pH 7.0. This STS is 396 amino acids in length and, like alfalfa CHS exists as a homodimer in solution. A partial data set on a frozen crystal (!))K) has been collected to 2.7 Å. The crystals belong to space group C222 with unit cell dimensions of a=74.94 Å, b=86.63 Å, c=364.18 Å, α=β=γ=90°.
2-Pyrone synthase (2-PS) from Gerbera hybrida was expressed and purified from E. coli in a similar manner to CHS and STS. Crystals were obtained from 1.5 M ammonium sulfate, 011 M Na+-succinate, 0.002 M DTT at pH 5.5.
2-Pyrone synthase (2-PS) from Gerbera hybrida forms a triketide from an acetyl-CoA initiator and two acetyl-CoA α-carbanions derived from decarboxylation of two malonyl-CoAs that cyclizes into the 6-methyl-4-hydroxy-2-pyrone. In comparison, alfalfa chalcone synthase 2 (CHS2; 74% amino acid sequence identity to 2-PS), condenses p-coumaroyl-CoA and three acetyl-CoA α-carbanions derived from decarboxylation of three malonyl-CoAs into a tetraketide that cyclizes into chalcone. A homology model of 2-PS based on the structure of CHS suggested that the 2-PS initiation/elongation cavity is smaller than that of CHS. A smaller cavity would account for the terminal formation of a triketide intermediate prior to cyclization by 2-PS.
Expression, Purification and Crystallization of 2-PS.
2-PS was expressed in E. coli, purified and crystallized as described above. Gerbera hybrida 2-PS was expressed in E. coli using the pHIS8 vector and was purified as described for CHS. 2-PS crystals grew at 4° C. in hanging-drops containing a 1:1 mixture of 25 mg ml−1 protein and crystallization buffer (1.5 M ammonium sulfate, 50 mM succinic acid (pH 5.5), and 5 mM DTT). Before freezing at 105 K, crystals (P3121; unit cell dimensions a=82.15 Å, c=241.33 Å; one 2-PS dimer per asymmetric unit) were stepped through stabilizer (50 mM succinic acid (pH 5.5), 50 mM ammonium sulfate, and 5 mM DTT) containing 5 mM acetoacetyl-CoA and increasing concentrations of glycerol (30% (v/v) final). Diffraction data were collected using a DIP2030 imaging plate system and CuK radiation produced by a rotating anode (wavelength 1.54 Å). All images were processed with DENZO/SCALEPACK (Z. Otwinowski, W. Minor, Methods Enzymol. 276:307 (1997)). A total of 179,623 reflections were merged to give 60,824 unique reflections (98.2% complete overall to 2.05 Å and 98.1% complete in the highest resolution shell) with an Rsym=0.042 (0.206 in the highest resolution shell) and an I/_of 21.7 (4.5 in the highest resolution shell). The structure of 2-PS complexed with acetoacetyl-CoA was determined by molecular replacement using CHS as a search model and was refined to 2.05 Å resolution. The overall fold of 2-PS is the αβαβα motif found in CHS and β-ketoacyl synthase II (KAS II). In addition, the positions of the catalytic residues of 2-PS (Cys169, His308, and Asn341), CHS (Cys163, His303, Asn336), and KAS II (Cys163, His303, and His340) are structurally analogous. As expected from sequence homology, the structures of 2-PS and CHS are nearly identical and superimpose with a r.m.s. deviation of 0.64 Å for the two proteins' α-carbon atoms. Similar to CHS, the 2-PS dimerization surface buries 1805 Å2 of surface area per monomer and a loop containing a cis-peptide bond between Met142 and Pro143 allows the methionine of one monomer to protrude into the adjoining monomer's active site. Thus, dimerization allows formation of the complete 2-PS active site.
Acetoacetyl-CoA is a reaction intermediate of 2-PS. Electron density for the ligand is well defined in the 2-PS active site and shows that the acetoacetyl moiety extends from the CoA pantetheine arm into a large internal cavity. The electron density also reveals oxidation of the catalytic cysteine's (Cys169) sulfhydryl to sulfinic acid (—SO2H). This oxidation state prevents formation of a covalent acetoacetyl-enzyme complex but allows trapping of the bound acetoacetyl-CoA intermediate. Extensive protein-ligand contacts position CoA at the entrance to the active site and orient the acetoacetyl moiety at the end of a 15 Å long tunnel that opens into a cavity that defines the initiation and elongation steps of polyketide formation.
The 2-PS active site cavity consists of twenty-seven residues from one monomer and Met142 from the adjoining monomer. Phe220 and Phe270 mark the boundary between the CoA binding site and the initiation/elongation cavity. Near the CoA thioester, Cys169, His308, and Asn341, form the catalytic center of 2-PS. These residues are conserved in all homodimeric iterative PKSs. Based on this, catalytic roles were proposed for each residue that are analogous to the corresponding residues in CHS. Cys169 acts as the nucleophile in the reaction and as the attachment site for the elongating polyketide chain. Interaction between His308 and Cys169 maintains the thiolate required for condensation of the starter molecule. His308 and Asn341 catalyze malonyl-CoA decarboxylation and stabilize the transition states during the condensation steps by forming an oxyanion hole that accommodates the negatively charged tetravalent transition state. Following the first condensation reaction, a diketide remains attached to Cys169. The second malonyl-CoA then binds, undergoes decarboxylation, and the resulting nucleophilic acetyl-coA α-carbanion performs a second condensation reaction with the enzyme bound diketide, ultimately generating the triketide that cyclizes into methylpyrone.
Comparison of the initiation/elongation cavities of 2-PS and CHS reveal four amino acid differences. In 2-PS, Leu202, Met259, Leu261, and Ile343 replace Thr197, Ile254, Gly256, and Ser338, respectively, of CHS. These four substitutions reduce cavity volume from 923 Å3 in CHS to 274 Å3 in 2-PS. A model of methylpyrone in the 2-PS cavity, based on the position of acetoacetyl-CoA, emphasizes the volume change compared to the CHS-naringenin complex (Accession No. 1CGK). Leu202 and Ile343 occlude the portion of the 2-PS cavity corresponding to the coumaroyl-binding site of CHS. Replacement of Gly256 in CHS by Leu261 in 2-PS severely reduces the size of the active site cavity. Substitution of Met259 in 2-PS for Ile254 in CHS produces a modest alteration in cavity volume. To examine the functional importance of these amino acid differences, the initiation/elongation cavity of CHS was altered by mutagenesis to resemble that of 2-PS. The resulting mutant proteins were screened for activity using either p-coumaroyl-CoA or acetyl-CoA as starter molecules. Activities of 2-PS, CHS, and the CHS mutants were determined by monitoring product formation using a TLC-based radiometric assay. Assay conditions were 100 mM Hepes (pH 7.0), 30 μM starter-CoA (either p-coumaroyl-CoA or acetyl-CoA), and 60 μM [14C]-malonyl-CoA (50,000 cpm) in 100 μl at 25° C. Reactions were quenched with 5% acetic acid, extracted with ethyl acetate, and applied to TLC plates and developed. Due to the spontaneous cyclization of chalcone into the flavanone naringenin, activities of CHS are referenced to naringenin formation.
The x-ray crystal structures of 2-PS and CHS imply that the size of the active site cavity limits polyketide length and modulates folding of the polyketide chain. Wild-type CHS(SEQ ID NO:1) generates the tetraketide chalcone and 2-PS produces the triketide methylpyrone. Likewise, the CHS I254M mutant (SEQ ID NO:1) also yields chalcone. Interestingly, the T197L, G256L, and S338I mutants (SEQ ID NO:1) do not form chalcone. Crystallographic analysis of the G256L and S338I mutants (SEQ ID NO:1) demonstrates that the substituted sidechains adopt conformations similar to the corresponding residues in 2-PS without altering the position of the protein backbone. Since the T197L, G256L, and S338I mutants altered product formation, a CHS triple mutant was generated. Consistent with the proposal that cavity volume dictates polyketide length, the T197L/G256L/S338I mutant produces only methylpyrone, as confirmed by liquid chromatography/mass spectroscopy (LC/MS). LC/MS/MS analysis was performed by the Mass Spectroscopy facility of the Scripps Research Institute. Scaled-up assays (2 ml reaction volume) with the CHS T197L/G256L/S338I mutant and 2-PS were performed. Extracts were analyzed on a Hewlett-Packard HP1100 MSD single quadrupole mass spectrometer coupled to a ZorbaxSB-C18 column (5 μm, 2.1 mm×150 mm). HPLC conditions were as follows: gradient system from 0 to 100% methanol in water (each containing 0.2% acetic acid) within 10 min; flow rate 0.25 ml min−1. LC/MS/MS data from both reactions were identical: 6-methyl-4-hydroxy-2pyrone, Rt=5.068 min; [M-H]−125 (41); [M-H—CO2]−181 (100). The numbers show m/z values with relative intensities in parenthesis. The observed fragmentation matches previously published data.
In addition, the size of the cavity in 2-PS and CHS confers starter molecule specificity. 2-PS accepts acetyl-CoA but does not use p-coumaroyl-CoA. Structurally, the constricted 2-PS active site excludes the bulky coumaroyl group. As such, incubation of 2-PS in the presence of coumaroyl-CoA and malonyl-CoA yields methylpyrone produced from three malonyl-CoA molecules. In comparison, the larger initiation/elongation cavity of CHS allows for different sized aliphatic and aromatic starter molecules to be used in vitro with varying efficiencies. CHS exhibits a 230-fold preference for p-coumaroyl-CoA versus acetyl-CoA. Alterations in the active site cavity of CHS, affect starter molecule preference. The CHS I254M mutant is functionally comparable to wild-type enzyme with a modest reduction in specific activity. The T197L and S338I mutants exhibit 10-fold and 3-fold preferences, respectively, for coumaroyl-CoA. Moreover, both form a distinct product using coumaroyl-CoA as a starter molecule. In contrast, the G256L mutant favors acetyl-CoA 3-fold. Like 2-PS, the CHS T197L/G256L/S338I (3×) mutant only accepts acetyl-CoA (or malonyl-CoA) as the starter molecule.
Functional diversity among other homodimeric iterative PKSs, like p-coumaroyltriacetic acid synthase (CTAS), acridone synthase (ACS), and the rppA protein from Streptomyces griseus, likely results from variations of residues lining the initiation/elongation cavity. As demonstrated, positions 197, 256, and 338 of SEQ ID NO:1 distinguish between tetraketide products derived from a final Claisen condensation in wild-type CHS (SEQ ID NO:1) and triketide products derived from an enolate-directed condensation in the CHS triple mutant. Although CHS, CTAS, and ACS generate tetraketides, each enzyme differs in either the cyclization reaction or in the identity of the starter molecule. CTAS forms the same enzyme-bound tetraketide as CHS but does not catalyze the final cyclization reaction. Comparison of these two enzymes reveals that substitution of Thr 197 of SEQ ID NO:1 in CHS with an asparagine in CTAS may prevent the covalently-bound tetraketide intermediate from undergoing cyclization into chalcone. ACS uses N-methylanthranoyl-CoA as a starting substrate to produce the alkaloid acridone. Three differences between CHS (Thr132, Ser133, and Phe265 of SEQ ID NO:1) and ACS (Ser132, Ala133, and Val265) may alter starter molecule specificity. In ACS, these changes likely widen the portion of the cavity corresponding to the p-coumaroyl-binding site in CHS to accommodate N-methylanthranoyl-CoA binding. Comparative changes in the active site cavity allow formation of longer polyketides. The rppA protein forms a pentaketide from five acetates derived from malonyl-CoA decarboxylation. Thr137, Ala138, Thr199, Leu202, Met259, Leu261, Leu268, Pro304, and Ile343 of 2-PS are replaced by Cys106, Thr107, Cys168, Cys171, Ile228, Tyr230, Phe237, Ala261, and Ala295, respectively, in the rppA protein. Models of the rppA protein based on the 2-PS and CHS structures show that cavity volume is 1145 Å3 in the rppA protein versus 274 Å3 in 2-PS (or 923 Å3 in CHS). Manipulation of the active site through amino acid substitutions offers a strategy for increasing the molecular diversity of polyketide formation through both the choice of starter molecule and the number of subsequent condensation steps.
The reaction mechanism for polyketide formation and the structural basis for controlling polyketide length described here may be shared with other more complex iterative (e.g., actinorhodin (act) PKS and tetracenomycin (tcm) PKS) and modular PKSs (e.g., 6-deoxyerythronolide B synthase (DEBS)). The structural similarity of the 2-PS, CHS, and KAS II active sites, the sequence homology of KAS II and the ketosynthases of act PKS, tcm PKS, and DEBS, and mutagenesis studies of CHS and act PKS demonstrating similar roles for the catalytic residues of each protein indicate that a conserved active site architecture catalyzes similar reactions in these enzymes.
As in 2-PS and CHS, the volume of the active site cavities in other PKSs likely limits the size of the final polyketide. For example, act PKS and tcm PKS generate octaketide and decaketide products, respectively, at a single active site. This suggests that the active site cavities of these PKSs differ in size, and are larger than those of 2-PS or CHS. Similarly, the ketosynthases of different DEBS modules accept polyketide intermediates ranging in length from five to twelve carbons. Modular PKSs, like DEBS, use an assembly-line system in which an individual module catalyzes one elongation reaction and passes the growing polyketide to the next module. Although the ketosynthase domains of DEBS are functionally permissive, modulation of active site volume in each module's ketosynthase would provide selectivity for the proper sized intermediate at each elongation step. Structural differences among PKSs alter the volume of the initiation/elongation cavity to allow discrimination between starter molecules and to vary the number of elongation steps to ultimately direct the nature and length of the polyketide product.
While the foregoing has been presented with reference to particular embodiments of the invention, it will be appreciated by those skilled in the art that changes in these embodiments may be made without departing from the principles and spirit of the invention, the scope of which is defined by the appended claims.
Table 5. PDB Accession No. 1BI5. The content of Table 5 is hereby incorporated by reference under 37 C.F.R. § 1.52(e)(1)(iii) to file “Table5.txt” of CD-R disk “Tab-5-8”, created Sep. 6, 2005, with size 619,981 bytes.
Table 6. PDB Accession No. 1 D6F. The content of Table 6 is hereby incorporated by reference under 37 C.F.R. § 1.52(e)(1)(iii) to file “Table6.txt” of CD-R disk “Tab-5-8”, created Sep. 6, 2005, with size 313,711 bytes.
Table 7. PDB Accession No. 1 D61. The content of Table 7 is hereby incorporated by reference under 37 C.F.R. § 1.52(e)(1)(iii) to file “Table7.txt” of CD-R disk “Tab-5-8”, created Sep. 6, 2005, with size 557,743 bytes.
Table 8. PDB Accession No. 1D6H. The content of Table 8 is hereby incorporated by reference under 37 C.F.R. § 1.52(e)(1)(iii) to file “Table8.txt” of CD-R disk “Tab-5-8”, created Sep. 6, 2005, with size 302,313 bytes.

## Claims

1. A method for crystallizing the chalcone synthase of SEQ ID NO:1 or mutant thereof,
wherein said mutant chalcone synthase has one or more mutations selected from the group consisting of Xaa164S, Xaa164D, H303A, H303Q, H303D, H303T, N336A, N336D, N336Q, N336H, F215S, F215Y, and F215W,
wherein said method comprises growing crystals of said chalcone synthase or mutant thereof by vapor diffusion at 4° C. in 2 μL drops,
wherein said drops contain a 1:1 mixture of 25 mg/mL of said chalcone synthase and crystallization buffer, and
wherein said crystallization buffer comprises 2.2–2.4 M ammonium sulfate and 0.1 M PIPES, pH 6.5.

2. The method of claim 1 further comprising 5 mM DTT.

3. A crystal produced by the method of claim 1.

4. The crystal of claim 3 where said chalcone synthase is defined by SEQ ID NO:1.

5. The crystal of claim 3 wherein said mutation is Xaa164S.

6. The crystal of claim 3 wherein said mutation is Xaa164D.

7. The crystal of claim 3 wherein said mutation is H303A.

8. The crystal of claim 3 wherein said mutation is H303Q.

9. The crystal of claim 3 wherein said mutation is H303D.

10. The crystal of claim 3 wherein said mutation is H303T.

11. The crystal of claim 3 wherein said mutation is N336A.

12. The crystal of claim 3 wherein said mutation is N336D.

13. The crystal of claim 3 wherein said mutation is N336Q.

14. The crystal of claim 3 wherein said mutation is N336H.

15. The crystal of claim 3 wherein said mutation is F215S.

16. The crystal of claim 3 wherein said mutation is F215Y.

17. The crystal of claim 3 wherein said mutation is F215W.

18. A crystalline form of the chalcone synthase of SEQ ID NO:1, wherein said crystalline form has space group P 32 2 1, unit cell dimensions 97.54 Å, 97.54 Å, 65.52 Å, and unit cell angles alpha=90°, beta=90°, gamma=120°,
wherein residue Xaa164 of SEQ ID NO:1 is selected from the group consisting of Cys and Ser.

19. A crystalline complex comprising said crystalline form of chalcone synthase according to claim 18 and a chalcone synthase substrate.

20. The crystalline complex of claim 19, wherein said substrate is selected from the group consisting of chalcone, naringenin, resveratrol, cerulenin, acyl-CoA, malonyl-CoA, and hexanoyl-CoA.