# Patent

## Title
Methods of producing polyketide synthase mutants and compositions and uses thereof

## Abstract

The present invention comprises crystalline polyketide synthases, isolated non-native polyketide synthases having the structural coordinates of said crystalline polyketide synthases, and nucleic acid encoding such non-native polyketide synthases. Also disclosed are methods of producing mutant polyketide synthases, and methods of altering the activity and/or substrate specificity of putative polyketide synthases.

## Background
FIELD OF THE INVENTION
The present invention relates to methods for producing mutant polyketide synthases, and for altering the activity and/or substrate specificity of putative native and mutant polyketide synthases. The present invention further relates to compositions and uses of mutant polyketide synthases.
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 active and inactive mutants thereof, both with and without substrate or substrate analog. Similar results have been obtained for the polyketide synthases stilbene synthase (STS) and pyrone synthase (2-PS).
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 a 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 (see, for example Table 1) and one or more R-groups other than those found in native polyketide 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 altering the activity and/or substrate specificity of a putative polyketide synthase. There are further provided methods for altering the polyketide content of a plant.
Other aspects, embodiments, advantages, and features of the present invention will become apparent from the following specification.



BRIEF DESCRIPTION OF FIGURES
FIG. 1 presents the chemical structures of chalcone, naringenin, resveratrol, and cerulenin.
FIG. 2 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. 3 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. 4 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. 5 collectively shows structures of CHS-Acyl-CoA complexes. The ribbon diagram in panel FIG. 5A (on the top left) is the same as FIG. 3. 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. 5B and 5C, 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. 6A 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. 3. 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. 6B 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. 4). β2d does not change in all the complexes examined, but β1d moves in the CHS-resveratrol complex. FIG. 6C presents representative sequence alignment of the β1d-β2d region is given with positions 255, 266, and 268 highlighted. The first three sequences follow a CHS-like cyclization pathway, while the last three use the STS-cyclization pathway. Figure prepared with MOLSCRIPT and rendered with POV-Ray.
FIG. 7 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 1 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. 8 presents a comparison of the active site volumes of CHS from alfalfa and CHS from Gerbera hybrida. 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.
FIG. 10 shows the chalcone synthase reaction sequence including initiation, elongation and cyclization.
FIG. 11 shows an amino acid sequence alignment of P. sylvestris STS and M. sativa CHS, along with an evolutionary intermediate, P. sylvestris CHS.
FIG. 12 shows phenylpropanoid metabolism. From a common linear phenylpropanoid tetraketide intermediate, resveratrol is formed by STS and chalcone is formed by CHS.
FIG. 13 shows different reaction schemes of CHS and STS. STS forms resveratrol via an intramolecular aldol condensation and CHS utilizes an intramolecular Claisen condensation to produce chalcone.
FIG. 14 shows an autoradiographic gel following thin layer chromatography. Wild type CHS produces chalcone, which spontaneously converts to naringenin, the position of which is indicated by the arrow on the left. Wild type STS produces resveratrol, the position of which is indicated by the arrow of the right. Function conversion of CHS to STS (i.e., the production of the alternate product from the same intermediate) results in diminished production of naringenin and increased production of resveratrol. Various mutants of CHS produce varying degrees of resveratrol, showing that CHS activity can be altered to STS-like activity to different extents by different mutations.
FIG. 15 shows the crystalline structure of CHS. Circled areas A1 to A4 represent regions in which mutations result in the conversion of CHS activity to STS-like activity. The 18xCHS mutant contains mutations in these regions.
FIG. 16 shows the crystalline structure of CHS with area B1, mutated in the 22xCHS mutant circled.
FIG. 17 shows amino acid sequences of homologous sequences from STS family members.
FIG. 18 shows the kinetics of the 18xCHS in comparison to the wild type CHS and STS.
FIG. 19 shows a comparison of the crystal structures of the wild type CHS (alfalfa), two types of STS (pine and peanut) and the 18xCHS mutant. Areas A1 to A4 are as indicated in FIG. 14. A comparison of the amino acid sequence in these areas is also provided. The stars indicated the residues mutated in the 8xCHS mutant.
FIG. 20 shows that the 8xCHS mutant has activity that is similar to the 18xCHS mutant, i.e. an alteration of the CHS activity to an STS-like activity. The 8xCHS mutant contains five mutations in Area A2 and three additional changes in Areas A1 and A3. The mutations in the 8xCHS are a subset of the mutations in the 18xCHS mutant, eliminating 10 neutral mutations found in the 18xCHS mutant.
FIG. 21 shows the proposed mechanism of cyclization specificity in STS as compared to CHS, which results in the different end-products. STS elimination of terminal CO2 favors intramolecular C2 to C7 Aldol Condensation, while CHS causes intramolecullar C6 to C1 Claisen Condensation coupled to thioester cleavage.
FIG. 22 shows the aldol cyclization switch region as viewed from the CoA-ginding tunnel, involved in the mechanisms depicted in FIG. 21.



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 and bacterial 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 through a structurally distinct cyclization intermediate.
While the cloning of over 400 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. The α-carbon atoms can also be referred to by their crystal structure coordinates as a convenient reference point. Table 1 provides the structural coordinates of α-carbons found in the active site of a polyketide of the present invention.











TABLE 1





Active Site-Carbon



Amino Acid


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






“Positively charged amino acid” and “positively charged R-group” includes any naturally occurring or unnatural amino acid having a side chain which is positively charged 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 side chain which is to negatively charged 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 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 that is relatively soluble in water. Examples of naturally occurring hydrophilic amino acids include serine, threonine, tyrosine, asparagine, glutainine, cysteine, and the like.
“Mutant” or “mutated synthase” refers to a polyketide synthase polypeptide containing amino acid residues that have been substituted or modified with respect to a wild type polyketide synthase (for example, the alfalfa CHS having the crystal structure coordinates of Protein Data Bank (PDB) Accession No. 1BI5, SEQ ID NO:69). Examples of mutant or mutated synthase polypeptides include those having PDB Accession Nos. 1D6F (SEQ ID NO:69), 1D6I (SEQ ID NO:69), and 1D6H (SEQ ID NO:69) (the content of which are incorporated by reference herein in their entirety). Further examples of mutant or mutated synthase polypeptides are set forth in a set of crystal structure coordinates in Appendix C, the 18x CHS mutant. (SEQ ID NO:67). Access to the foregoing information in the Protein Data Bank can be found on the World Wide Web at rcsb.org/pdb. The Protein Data Bank is operated by the Research Collaboratory for Structural Bioinformatics (RCSB).
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” refers to the configuration of R-groups within the active site and/or groups involved in second-tier interactions, for example those resulting in the alteration of CHS native activity.
“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 Nos. 1D6F, 1D6I, 1D6H and Appendix C).
“Native” or “native synthase” or “wild type synthase” refers to synthase proteins that are produced in nature, e.g., are not mutants (see, for example, PDB Accession Nos. 1BI5 (CHS), 1EE0 (2-PS)).
“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 mutations. Mutations include deletions and additions of amino acid residues, and substitutions of one amino acid residue for another. For example substitutions include: D96A (where D at position 96 of a wild type CHS is changed toA), V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, C164A, Q165H, D255G, H257K, L258V, H266Q, L268K, K269G, D270A, G273D, H303Q, 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 QQGCFAGGTV 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 50% homology, preferably at least 60% homology, more preferably 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.
Sequence homology and identity are 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). The term “identity” in the context of two or more nucleic acids or polypeptide sequences, refers 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. The term “homology” in the context of two or more nucleic acids or polypeptide sequences, refers to two or more sequences or subsequences that are homologous or have a specified percentage of amino acid residues or nucleotides that are homologous 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. Programs as mentioned above allow for amino acid substitutions with similar amino acids matches by assigning degrees of homology to determine a degree of homology between the sequences being compared.
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 SequenceComparison), LALIGN (Local Sequence Alignment), LCP (Local Content Program), MACAW (Multiple Alignment Construction & Analysis Workbench), MAP (Multiple Alignment Program), MBLKP, MBLKN, PIMA (Pattern-Induced Multi-sequence 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, 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 organization, and are accessible via the internet, for example, on the World Wide Web at tigr.org/tdb, genetics.wisc.edu, genome-www.stanford.edu, hiv-web.lanl.gov, ncbi.nlm.nih.gov, cbi.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. For example, 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. Active sites can be specified by a set of amino acid residues. Other residues can play a role in substrate specificity and enzyme activity by modulating size, shape, charge, and the like of the active site. In addition, second tier residues may also modulate the specificity and/or activity of the enzyme.
In CHS, at least five areas of primary sequence containing residues that play a role modulating enzyme specificity and/or activity are found. Each area contains a total of about four to about fifteen amino acid residues. Within each area, about three to six, and preferably four or five amino acid residues that interact with substrate are found. Residues may be directly within or lining the active site to modulate specificity and/or activity. Residues may also be involved in second tier interactions that modulate the specificity and/or activity of the active site, without being physically located within the active site. Various mutants of these residues have been prepared to evaluate the role of these residues in CHS function and activity, including substrate specificity and product formation. Table 3 presents some of the mutations of CHS that have been made to affect CHS function.







TABLE 3







Mutants of CHS











Mutant
Mutant
Mutations relative to alfalfa CHS



Name
Code
(SEQ ID NO:1)







A4
0002
A4 (L268K, K269G, D270A, G273D)



14B
1200
A1 (V98L,)



(=6 × CHS)

A2 (T131S, S133T, G134T, V135P,





M137L)



2B
2200
A1 (D96A, V98L, V99A, V100M)





A2 (T131S, S133T, G134T, V135P,





M137L)



16B
1210
A1 (V98L,)



(=8 × CHS)

A2 (T131S, S133T, G134T, V135P,





M137L)





A3 (M158G, Y160F)



4B
2211
A1 (D96A, V98L, V99A, V100M)





A2 (T131S, S133T, G134T, V135P,





M137L)





A3 (M158G, Y160F)





A4 (K269G)



6B
1220
A1 (V98L,)





A2 (T131S, S133T, G134T, V135P,





M137L)





A3 (Y157V, M158G, M159V, Y160F,





F165H);



18 × CHS
2222
A1 (D96A, V98L, V99A, V100M)





A2 (T131S, S133T, G134T, V135P,





M137L)





A3 (Y157V, M158G, M159V, Y160F,





F165H)





A4 (L268K, K269G, D270A, G273D)



22 × CHS
2222
A1 (D96A, V98L, V99A, V100M)




+ Area B1
A2 (T131S, S133T, G134T, V135P,





M137L)





A3 (Y157V, MI58G, M159V, Y160F,





F165H)





B1 (D255G, H257K, L258V,H266Q)





A4 (L268K, K269G, D270A, G273D)










A polyketide synthase can be divided into regional areas A1-A4 and B1. Areas A1 and A3 flank area A2, from below and above, respectively (see FIG. 15). Both areas seem to have importance mainly in regards to compensatory steric changes which allow a proline induced kink in area A2 relative to the CHS position. The backbone C-alpha traces of A1 and A3 do not actually vary much from CHS to STS, but length of indicated residues does. In area A1, amino acids involved in the modulation of enzyme specificity and/or activity for chalcone synthase include D96, V98, V99 and V100. In area A3, such amino acids include Y157, M158, M159, Y160 and Q165. Mutations at V98 and V99 in area A1, and at M158 and Y160 in area A3 appear especially important for modifying activity.
Area A2 appears to be the most important area, and is located at the dimer interface, directly between the active site cavities of each monomer. In area A2 amino acids involved in the modulation of enzyme specificity and/or activity include T131, S133, G134, V135 and M137. Mutations at G134 and V135 appear especially important for modifying activity.
Area A4 is located on the outside of the protein, near the active site entrance. A4 mutations made to wild type CHS seems to have no effect on cyclization specificity, indicating that this area is not important to the conversion of activity seen in the certain mutants, for example, the 18xCHS mutant. However, this area may be important in the improvements to conversion seen with the addition of four more mutants (at B1, see FIG. 16 and below) in the 22xCHS mutant. In area A4, amino acids involved in the modulation of enzyme specificity and/or activity include L268, K269, D270 and G273.
Area B1 flanks A4 and bridges the gap between A1-A3 and A4. In area B1, amino acids involved in the modulation of enzyme specificity and/or activity include D255, H257, L258 and H266. These mutations are in an area predicted in byFerrer, et al. and are important for cyclization specificity.
“Altered substrate specificity” or “altered activity” includes a change in the ability of a mutant synthase to use a particular substrate and/or 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 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 crystals and 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 by reference herein.
“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 Enzymology, 115.55-77; 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 herein (see e.g., PDB Accession Numbers) 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 ofpolyketide compounds. Polyketide synthases are generally homodimers, with each monomer being enzymatically acitve.
“Substrate” refers to the Coenzyme-A (CoA) tlhioesters that are acted on by the polyketide synthases and mutants thereof disclosed herein, such as malonyl-CoA, coumaroyl-CoA, hexamoyl-CoA, ACP or NAC thioesters 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, 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, e.g., are mutant synthases. In addition, the present invention provides for production of mutant polyketide synthases based on the structural information of synthases (and provided herein) and for use of said mutant synthases to make a variety of polyketide compounds using a variety of substrates (as described in PCT Application US00/20674, filed Jul. 27, 2000, incorporated by reference in its entirety herein). The present invention also provides methods of producing novel mutant polyketide synthases by comparing the crystal structures of two different polyketide synthases.
The present invention further provides, for the first time, crystals of several polyketide synthases, as exemplified by chalcone synthase (CHS; PDB Accession No. 1B15, SEQ: ID NO69), stilbene synthase (STS; Pinus syhlestris, pine—Appendix A, SEQ ID NO:65); and Arachis hypogaea, peanut—Appendix B, SEQ ID NO:66), and pyrone synthase (2-PS; PDB Accession No. 1EE0, SEQ ID NO:68). Also provided are coordinates for crystals which are grown in the presence and absence of substrate, substrate analogues, and products, 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 products that were grown with chalcone synthase as well as their PDB accession numbers, all of which are incorporated by reference herein in their entirety.









TABLE 4





Complex
PDB Accession No.
(SEQ ID NO:)







CHS-coA complex
1BQ6
(SEQ ID NO:69)


CHS-malonyl-CoA
1CML
(SEQ ID NO:69)


complex


CHS-hexanoyl-CoA comlex
1CHW
(SEQ ID NO:69)


CHS-naringenin complex
1CGK
(SEQ ID NO:69)


CHS-resveratrol complex
1CGZ
(SEQ ID NO:69)









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 belong to the space groups with unit cell dimensions as in Table 5.







TABLE 5







Crystals of Polyketide Synthases










Space
Unit Cell Dimensions














Crystal
Group
a (Å)
b (Å)
c (Å)
α (°)
β (°)
γ (°)

















CHS (alfalfa)
P 32 2 1
97.54
97.54
65.52
90.00
90.00
120.00


(SEQ ID NO:1)


STS (pine)
P2 (1)
57.221
361.291
57.317
90.00
98.39
90.00


(SEQ ID NO:65)


STS (peanut)
P2 (1)
74.348
101.747
113.609
90.00
108.84
90.00


(SEQ ID NO:66)


2-PS
P3121
83.41
83.41
240.62
90.00
90.00
120.00


(SEQ ID NO:68)


18 × CHS
P2 (1)
71.638
59.753
82.539
90.00
108.166
90.00


(SEQ ID NO:67)









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 Protein Data Bank, accession number 1BI5. 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 mutant polyketide synthases that produce different and/or novel polyketide compounds using the same 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. Alternatively, mutant polyketide syntases can be prepared by standard protocols for polypeptide synthesis as is well known in the art.
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 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. Alternatively, traditional method of protein or polypeptide synthesis may be used.
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., many 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 by reference herein) 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 by reference herein.
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 by reference herein.
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), genes encoding resistance to neomycin or 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. 5,231,019 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 by reference herein.
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.
In addition, it may be desirable to change the polyketide production of a polyketide synthase within a plant. For example, it may be beneficial to increase the production of resveratrol in a plant. Resveratrol, the natural product made by the CHS-related stilbene synthase (STS) enzymes, is an antifungal compound produced in a few families of plants, including pine trees, grapevines, and peanuts. When stilbene synthase is introduced into plants like tobacco or alfalfa, which normally lack this enzyme, the transgenic plant becomes resistant to fungal infection (Mol. Plant. Microbe Interact. 13(5):551-62, 2000; and Nature 361(6408):153-6, 1993). Since STS uses the exact sanme substrates as CHS, which is ubiquitous in higher plants, expression of the STS gene in any of these species should be sufficient to achieve the in vivo biosynthesis of resveratrol.
Furthermore, resveratrol has also been shown to have a number of beneficial medicinal activities, including copper chelation, anti-oxidant scavenging of free radicals, inhibition of both platelet aggregation and lipid peroxidation, anti-inflammation, vasodilation, anti-cancer (Life Sci. 66(8):663-73, 2000), and the like. These effects of resveratrol contribute to the health benefits of the moderate consumption of red wine, known as “the French paradox”. Red wine has a higher resveratrol content than grape juice or white wine, due to the inclusion of the resveratrol-rich grape skins during the fermentation process.
Thus, production of resveratrol in plants which lack it is biologically useful for the plant, and medicinally useful for humans who consume the plant. While transgenic introduction of the stilbene synthase gene has proven effective, enzymes are often best-adapted for expression and stability within their own species. The ability to engineer full or partial STS activity into a native CHS of a given species confers the benefits of resveratrol production to that species, while avoiding all of the negative effects of foreign transgene expression.
The mutants of the present invention show that it is possible to mutate a native CHS to a STS-like activity (see FIG. 14). Furthermore, it is possible to produce the STS product resveratrol to varying degrees with different mutants. Thus, a plant can be manipulated to produce varying levels of resveratrol, without eliminating the production of the chalcone product required for viability.
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 cells. Once said proteins are expressed, they can be easily purified using techniques conmmon to the person having ordinary skill in the art of protein biochemistry, such as, for example, techniques described in Colligan et al., (1997) Current Protocols in Protein Science, Chanda, V. B., Ed., John Wiley & Sons, Inc., which is incorporated by reference herein. 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. Biol 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.
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 carboxy 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, subtilisin, 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. Mol 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. Sail & 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 400 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. Similarities and 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 similarities and/or 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 products 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-crystallized 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 one or more of Accession Nos. 1BI5, 1D6F, 1D6I, 1D6H, 1BQ6, 1CML, 1CHW, 1CGK, 1CGZ, Table 1, and Appendix A. 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 one or more of Accession Nos. 1BI5 (SEQ ID NO:69), 1D6F (SEQ ID NO:69), 1D6I (SEQ ID NO:69), 1D6H (SEQ ID NO:69), 1BQ6 (SEQ ID NO:69), 1CML (SEQ ID NO:69), 1CHW (SEQ ID NO:69), 1CGK (SEQ ID NO:69), 1CGZ (SEQ ID NO:69), 1EE0 (SEQ ID NO:68), Table 1, Appendix A, (SEQ ID NO:65), Appendix B (SEQ ID NO:66), and Appendix C (SEQ ID NO:67) to design new enzymes capable of synthesizing novel and known polyketides. For example, polyketide synthases (PKSs) generate molecular diversity in their products by utilizing different starter molecules and by varying the final size of the polyketide chain. The structural coordinates disclosed herein allow the elucidation of the nature by which PKSs achieve starter molecule selectivity and control polyketide chain length. For example, 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 results 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., 13:505-524 (1992).
Because chalcone synthase is a highly representative member of a family of polyketide synthase polypeptides, many of which have similar functional activity, 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 one or more of Accession Nos. 1BI5 (SEQ ID NO:69), 1D6F (SEQ ID NO:69), 1D6I (SEQ ID NO:69), 1D6H (SEQ ID NO:69), 1BQ6 (SEQ ID NO:69), 1CML (SEQ ID NO:69), 1CHW (SEQ ID NO:69), 1CGK (SEQ ID NO:69), 1CGZ (SEQ ID NO:69), 1EE0 (SEQ ID NO:68), Table 1, Appendix A (SEQ ID NO:65), Appendix B (SEQ ID NO:66) or Appendix C (SEQ ID NO:67). This method will provide an accurate structural foilii 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, products 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, product 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 ofpolyketide synthase substrates or binding agents (e.g., inhibitors), and to design and synthesize novel classes ofpolyketide 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 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 one or more of Accession Nos. 1BI5 (SEQ ID NO:69), 1D6F (SEQ ID NO:69), 1D6I (SEQ ID NO:69), 1D6H (SEQ ID NO:69), 1BQ6 (SEQ ID NO:69), 1CML (SEQ ID NO:69), 1CHW (SEQ ID NO:69), 1CGK (SEQ ID NO:69), 1CGZ (SEQ ID NO:69), 1EE0 (SEQ ID NO:68), Table 1, Appendix A (SEQ ID NO:65), Appendix B (SEQ ID NO:66) or Appendix C (SEQ ID NO:67). 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., 28:849-857 (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, 11:29-34 (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, 8:195-202 (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., 161:269-288 (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 one or more of Accession Nos. 1BI5 (SEQ ID NO:69), 1D6F (SEQ ID NO:69), 1D6I (SEQ ID NO:69), 1D6H (SEQ ID NO:69), 1BQ6 (SEQ ID NO:69), 1CML (SEQ ID NO:69), 1CHW (SEQ ID NO:69), 1CGK (SEQ ID NO:69), 1CGZ (SEQ ID NO:69), 1EE0 (SEQ ID NO:68), Table 1, Appendix A (SEQ ID NO:65), Appendix B (SEQ ID NO:66) or Appendix C (SEQ ID NO:67). 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., 35:2145-2154 (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, 6:61-78 (1992)). LUDI is available from Biosym Technologies, San Diego, Calif.
2. LEGEND (Nishibata, Y. and A. Itai, Tetrahedron, 47:8985 (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., 33:883-894 (1990). See also, Navia, M. A. and M. A. Murcko, “The Use of Structural Information in Drug Design”, Current Opinions in Structural Biology, 2:202-210 (1992).
Once a substrate, compound or binding agent has been designed or selected by the above methods, the efficiency with which that substrate, 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 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 one or more of Accession Nos. 1BI5, 1D6F, 1D6I, 1D6H, 1BQ6, 1CML, 1CHW, 1CGK, 1CGZ, 1EE0, Table 1, Appendix A, Appendix B, or Appendix C, 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, 268:429-431, 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 254:1388-90, 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, there is provided a method of designing a mutant polyketide synthese. The method include comparing a crystal structure of a wild type polyketide synthase with the crystal structure of a second polyketide synthase and substituting one or more amino acids with the amino acid residues at homologous positions in the second polyketide synthase. Invention methods can guide the required areas or active sites, and second tier interaction residues for synthase activity. Such areas can be mutated to modify one synthase to resemble another synthase, thereby allowing production of a product not typically synthesized by the wild type enzyme.
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 is described in greater detail by reference to the following non-limiting examples.
EXAMPLES
Mutagenesis, expression, and purification. Alfalfa CHS2 (SEQ ID NO:1) 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 QuikChange system (Stratagene) generated the various mutants including C164S, C164D, H303A, H303Q, H303D, H303T, N336A, N336D, N336Q, N336H, F215S, F215Y and F215W (see SEQ ID NO:1). N-teminal His8-tagged CHS (see SEQ ID NO:1) was expressed in BL21(DE3) E. coli cells. Cells were harvested and lysed by sonication. His-tagged CHS (see SEQ ID NO:1) 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 Superdex 200 16/60 (Pharmacia) column.
Crystallization. CHS crystals (wild-type and C164S mutant; see 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.
STS from Pinus sylvestris (SEQ ID NO:65) was crystallized using 13-14% PEG 8000, 0.3M ammonium acetate, 0.1M HEPES buffer (pH 7.4) at 4° C. Crystals were soaked for 60 seconds in the same solution plus 10% glycerol.
STS from Arachis hypogaea (SEQ ID NO:66) was crystallized using 14% PEG 8000, 0.1M MOPSO buffer (pH 7.0), with 3% ethylene glycol at 4° C. Crystals were soaked for 30 seconds in the same solution plus 10% ethylene glycol.
18xCHS mutant (SEQ ID NO:67) was crystallized using 21% PEG 8000, 0.3M ammonium acetate, 0.1M HEPES buffer (pH 7.5) at 4° C. Crystals were soaked for 60 seconds in the same solution plus 10% glycerol.
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 belong to space group P3221 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 Å 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 deteimined 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 and Leslie, Acta Oystallogr. 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 and Wilson, Acta Crystallogr. D 49:129-147, 1993) against the native 1 dataset. This was followed by manual adjustments using I2Fo-Fcl difference maps. Water molecules introduced by ARP were edited using the I2Fo-Fcl and IFo-Fcl 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 C164 S 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 was determined using multiple isomorphous replacement supplemented with anomalous scattering (MIRAS). 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 (C164 S) 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 FIG. 2). 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. 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 Met137 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) define the active site. Cys164 apparently serves as the nucleophile and as the to 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 Cys164, since the Nγ 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 C164 S mutant (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 hydrogen bond with two phosphates of CoA. Apart from these interactions, and an additional hydrogen bond between the backbone amide nitrogen of Ala308 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.
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. 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) surround the coumaroyl-derived portion of the bound naringenin and resveratrol molecules and interact primarily through van der Waals contacts. However, the carbonyl oxygen of Gly216 hydrogen bonds to the phenolic oxygen of both naringenin and resveratrol and the hydroxyl of Thr197 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 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 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 pocket, including Thr132, Met137, Phe215, Ile254, Gly256, Phe265, and Pro375, 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-courmaroyl-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 Cys164 as originally indicated by CO2 exchange assays. Decarboxylation occurs without Cys164, since the C164 S 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
Elucidation of the structure of CHS provided mechanistic insight and active site configuration for CHS reaction. Homology modeling and sequence alignments suggested evolutionary functional divergence of CHS superfamily (type III PKSs) occurs via the preservation of catalytic residues while using steric variation of other active site residues. Elucidation of the structure of 2-PS confirms the above ‘steric modulation’ model, by revealing substrate and product specificity differences achieved by only three active site mutations, as suggested by homology model of 2-PS based upon CHS 3D structure.
However, with these structures alone, the structural cause/determinants of the alternate cyclization seen in the stilbene synthase (STS) subfamily of CHS-like enzymes remained unknown. STS makes the same tetraketide intermediate as CHS, but cyclizes it differently (C2->C7 attack instead of C6->C1). STS evolved from CHS independently at least three times, with no clear STS consensus sequence.
Elucidation of the structure of pine (Pinus sylvestris) STS according to the present invention reveals a similar active site configuration, with minor differences. Furthermore, an 18xCHS mutant encompassing observed STS structural backbone differences proves to have activity and kinetics similar to STS (see FIG. 18), confirming that observed structural differences between CHS and STS are relevant to mechanistic differences.
It was further determined that ten of the eighteen mutations in 18xCHS prove to be neutral (not related to functional conversion, i.e. an alteration in CHS activity), and an 8xCHS mutant with similar STS-like activity is made. All of the 8xCHS changes are clustered in a single area, although encoded on three different stretches of primary sequence (see FIG. 19). This area is thus implicated as important for STS-like versus CHS-like cyclization.
Elucidation of the structure of peanut (Arachis hypogaea) STS, as well as of the 18xCHS engineered STS, show similar three-dimensional conformational changes in the area implicated by the 8xCHS mutagenic conversion of CHS to STS (see FIG. 20). This implies that a single 3D solution to the CHS to STS conversion problem has been found by all three STS subfamilies, despite variation in primary sequence. A compensatory increase in bulkiness at CHS residue 98 seems to be involved in all three families of STS.
A closer look at where the altered region meets the active site (see FIG. 22) reveals a consistent change in STS-like enzymes that suggests a cyclization switch mechanism (see FIG. 21), involving movement of Thr132 to allow a hydrogen-bond chain to transfer an electron from Glu192, through Thr132 and a water (bonded to Ser 338). This electron is proposed to encourage hydrolysis of the tetraketide intermediate off of the catalytic cysteine, where decarboxylation of the terminal carboxyl group drives the STS reaction toward a C2->C7 cyclization. In CHS, this hydrolysis does not occur, and so the C6->C1 cyclization is encouraged, as it serves to break the thioester bond to cysteine.
To test this proposed mechanism, various mutations were made in the 18xCHS engineered STS enzyme, in an attempt to revert the product specificity back to that of CHS, without reversing the other structural changes. Single mutations designed to disrupt only the hydrogen-bonding character in the relevant region succeeded in reverting 18CHS's activity from STS-like to CHS-like. A few of these mutants produce almost equal amounts of resveratrol and chalcone, which might be useful when engineered into a plant. This way, the beneficial resveratrol antifungal natural product could be made, without completely abrogating the vital CHS-like activity necessary in plants.
The residue implicated as the crucial base for STS-like behavior (Glu192) is not altered in STS. Instead, the adjacent Thr132 changes positions. As a further test of the proposed aldol mechanism, the residue equivalent to CHS Glu192 was mutated to Gln in both the pine and peanut STS wild type enzymes. As predicted, both of these single mutants made more chalcone and less resveratrol than the wild type STS enzymes. The ratio of products supports the proposed mechanism. The decrease in overall activity of these mutants is due to the fact that Glu192 is also important for folding and/or stability, apart from its role in cyclization specificity.
Structural Basis for Functionally Novel Chs-Like Enzymes
Absolute conservation of Cys164, Phe215, His303, and Asn336 occurs in CHS-like sequences, including several bacterial proteins possessing very low (typically 20-30%) amino acid sequence identity. Moreover, all CHS-like proteins exhibit strong conservation of residues shaping the geometry of the active site. Although the functions of the bacterial CHS-like proteins remain unknown, 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 hybrida (GCHS2)32 that is 74% identical with alfalfa CHS2 (SEQ ID NO:1) 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 (see SEQ ID NO:1) alter the coumaroyl binding pocket, while the identity of residue 256 (see SEQ ID NO:1) dictates major steric changes in the cyclization 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 pyronc products (Eckermann, et al., Nature 396:397-396, 1998).
Crystallization of Additional Polyketide Synthases
Stilbene synthase from Pinus sylvestris (SEQ ID NO:65) 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 (SEQ ID NO:1), exists as a homodimer in solution. The structural coordinates of this pine STS are presented in Appendix A. STS from Arachis hypogaea (SEQ ID NO:66) was similarly expressed and crystallized. The structural coordinates of this peanut STS are presented in Appendix B.
2-Pyrone synthase (2-PS) from Gerbera hybrida (SEQ ID NO:68) was expressed and purified from E. coli in a similar manner to CHS (SEQ ID NO:1) and STS (SEQ ID NO:65). 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 (SEQ ID NO:68) 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 (SEQ ID NO:1; CHS2; 74% amino acid sequence identity to 2-PS), condenses p-oumaroyl-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 (SEQ ID NO:1) 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 (SEQ ID NO:68) was expressed in E. coil 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 Enzyrnol. 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 α/_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 (SEQ ID NO:1) 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; see SEQ ID NO:68), CHS (Cys163, His303, Asn336; see SEQ ID NO:1), 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.ms. 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 (SEQ ID NO:68). 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) (see SEQ ID NO:1). 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 (SEQ ID NO:68) active site cavity consists of twenty-seven residues from one monomer and Met142 from the adjoining monomer. Phe220 and Phe270 (see SEQ ID NO:68) 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 (see SEQ ID NO:68). 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 (see SEQ ID NO:68) acts as the nucleophile in the reaction and as the attachment site for the elongating polyketide chain. Interaction between His308 and Cys169 (see SEQ ID NO:68) maintains the thiolate required for condensation of the starter molecule. His308 and Asn341 (see SEQ ID NO:68) 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 (see SEQ ID NO:68). 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 (SEQ ID NO:68) and CHS (SEQ ID NO:1) reveal four amino acid differences. In 2-PS, Leu202, Met259, Leu261, and Ile343 replace Thr197, Ile245, Gly256, and Ser338, respectively, of CHS. These four substitutions reduce cavity volume from 923 521 3 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, SEQ ID NO:69). 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 (SEQ ID NO:68) and CHS (SEQ ID NO:1) 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 (see SEQ ID NO:1) also yields chalcone. Interestingly, the T197L, G256L, and S338I mutants (see SEQ ID NO:1) do not form chalcone. Crystallographic analysis of the G256L and S338I mutants (see SEQ ID NO:1) demonstrates that the substituted side-chains 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 (see SEQ ID NO:1) altered product formation, a CHS triple mutant was generated. Consistent with the proposal that cavity volume dictates polyketide length, the T197L/G256L/S338I mutant (see SEQ ID NO:1) 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 (see SEQ ID NO:1) and 2-PS (SEQ ID NO:68) were performed. Extracts were analyzed on a Hewlett-Packard HP1100MSD single quadrupole mass spectrometer coupled to a Zorbax SB-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-2-pyrone, Rt=5.068 min; [M-H]−125; [M-H—CO2]−81. 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 (SEQ ID NO:68) and CHS (SEQ ID NO:1) 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 lamer 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 (see SEQ ID NO:1) 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 (SEQ ID NO:68), the CHS T197L/G256L/S3381 (3x) mutant (see SEQ ID NO:1) 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 (see SEQ ID NO:1) distinguish between tetraketide products derived from a final Claisen condensation in wild-type CHS 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 in CHS (see SEQ ID NO:1) with an asparagine in CTAS may prevent the covalently-bound tetraketide intei mediate 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; see 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 Å 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.
Functional Conversion of Chalcone Synthase to Stilbene Synthase
All CHS-like enzymes utilize a small number of absolutely conserved catalytic residues within a single active site to catalyze the iterative addition of acetate units to a starter molecule. A chalcone synthase reaction sequence starts with initiation, is followed by elongation, and ends with cyclization (see FIG. 10). CHS family members differ in their choice of starter molecule, number of acetyl additions and cyclization pathway of the resulting polyketide. Structural and functional characterization of CHS from M. sativa (SEQ ID NO:1) suggested that substrate specificity is modulated in the chalcone synthase superfamily by steric constraints. Such constraints are provided by a set of variable residues lining the active site. Functional conversion through mutagenesis of alfalfa CHS to a pyrone synthase, and the structural characterization of pyrone synthase (PS) from G. hybricia (daisy) (SEQ ID NO:68) support this model. Thus, homology modeling is a valid approach to gain insight into the specificity's of chalcone synthase superfamily members, including members that are identified and/or characterized as well as those still to be identified and characterized.
Stilbene synthase (STS) is related to CHS, and is thought to have arisen from CHS on at least three independent occasions. An amino acid sequence alignment of P. sylvestris STS (SEQ ID NO:8) and M. saliva CHS (SEQ ID NO:10), along with an evolutionary intermediate, P. sylvestris CHS (SEQ ID NO:9) shows amino acid sequence homology (FIG. 11). Both CHS and STS form the same linear phenylpropanoid tetraketide intermediate via the sequential condensation of three acetyl units derived from decarboxylation of malonyl-CoA with one coumaroyl-CoA starter (FIG. 12). STS forms resveratrol via an intramolecular aldol condensation. In contrast, CHS utilizes an intramolecular Claisen condensation to produce chalcone (FIG. 13).
Function conversion is achieved by mutations of CHS. Mutation of M. saliva (alfalfa) CHS (SEQ ID NO:1) confers wild type STS activity resulting in an STS-like product profile from mutant CHS activity. Specifically, alfalfa wild type CHS activity results in the production of the plant polyketide synthase product, naringenin, a flavanone product resulting from spontaneous ring closure of chalcone product. Mutant CHS activity results in the production of resveratrol, an expected product of wild type STS activity, and a decrease in the production of naringenin (see FIG. 14).
Based on the structural information, a variety of mutant CHS (SEQ ID NO:1) molecules can be designed. Mutant CHS enzymes can vary with respect to starter preference, activity, product formation, and the like. Various CHS mutants as shown in Table 3 above were designed by invention methods and prepared, and were tested for activity.
Mutant CHS (SEQ ID NO:1) has altered activity based on assays conducted with 14C malonyl-CoA. Products were extracted with ethyl acetate and analyzed by silica gel thin layer chromatography (TLC) and visualized by autoradiography. Mutants 14B and 2B (Table 3) showed reduced amounts of naringenin compared to wild type CHS and little or no resveratrol. Mutants 16B, 4B, 6B, 18x and 22x (Table 3) showed reduced amounts of naringenin compared to wild type CHS and various amounts of resveratrol. Mutants 18xCHS (SEQ ID NO:67) and 22xCHS (Table 3) showed the lowest naringenin amounts and the highest resveratrol amounts, in fact, in 22x the naringenin:resveratrol ratio is similar to that seen with wild type STS from P. sylvestris (SEQ ID NO:65).
Specific mutations in 18xCHS (SEQ ID NO:67) by area are as follows. with areas underlined showing residue changes especially important for altering activity (Appendix C, SEQ ID NO:67): A1: D96A, V98L, V99A, V100M; A2: T131S, S133T, G134T, V135P, M137L; A3: Y157V, M158G, M159V, Y160F, Q165H; A4: L268K, K269G, D270A, G273D.
The 22x mutant consists of 18xCHS (SEQ ID NO:67) plus four additional mutations in area B1, which flanks A4, and bridges the gap between A1-A3 and A4 (see FIG. 16). The 22xCHS has decreased naringenin production (relative to 18xCHS), matching identically the product profile of wild type STS. These mutations are in an area predicted to be important for cyclization specificity, due to changes seen here in comparing the CHS/resveratrol complex structure to apo and other complexes of CHS. Note that final mutation is only two residues before the first change in A4 region.
Specific mutations in 22xCHS (Table 3) by area are as follows, with areas underlined showing residue changes especially important for altering activity: A1: D96A, V98L, V99A, V100M; A2: T131S, S133T, G134T, V135P, M137L; A3: Y157V, M158G, M159V, Y160F, Q165H; A4: L268K, K269G, D270A, G273D; B1: D255G, H257K, L258V, H266Q.
The crystal structural coordinates of the 18xCHS mutant (SEQ ID NO:67) are presented in Appendix C. Table 6 shows the relative active site α-carbon coordinates of the 18xCHS mutant possessing STS-like activity.











TABLE 6





Active Site α-



Amino Acid


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



















1
3.754
−8.620
58.411
Thr 132


2
0.541
−10.075
59.960
Thr 133


3
0.228
−9.423
49.613
Met 137*


4
0.230
−7.076
55.634
Gln 161


5
9.260
−15.931
61.148
Thr 194


6
6.542
−18.097
57.263
Thr 197


7
13.288
−17.295
51.888
Gly 211


8
15.195
−13.751
60.585
Gly 216


9
6.827
−10.404
45.169
Ile 254


10
2.304
−13.379
49.664
Gly 256


11
1.944
−17.210
54.954
Leu 263


12
5.520
−16.124
49.059
Phe 265


13
8.197
−14.531
42.889
Leu 267


14
11.540
−7.480
56.987
Ser 338


15
8.611
−9.306
62.954
Glu 192





* Met 137 from the second monomer






Table 7 shows the wild type CHS (SEQ ID NO:1) active site positions that differ from the coordinates listed in Table 6. The unlisted positions are equivalent for both CHS-like Claissen and STS-like aldol cyclization specificity.











TABLE 7





Active Site α-



Amino Acid


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



















1
4.033
−8.884
58.744
Thr 132


2
3.656
−11.697
61.297
Ser 133









Table 8 shows various amino acid positions where mutations thereof can enable or enhance STS-like activity in CHS mutants. The α-carbon positions are those observed in the 18xCHS (SEQ ID NO:67) crystal sturcture. The comparison of crystal structure may identify further positions that produce similar results.












TABLE 8









Mutation



Enabling α-
X
Y
Z
(SEQ ID
Location


Carbon Number
Position
Position
Position
NO:1)
Designation




















1
2.452
−14.634
67.063
V98L
A1


2
−0.144
−13.492
69.602
V99A
A1


3
2.537
−13.818
72.285
V100M
A1


4
4.117
−6.516
61.579
S131T
A2


5
0.541
−10.075
59.960
T133S
A2


6
−1.599
−9.886
63.127
G134T
A2


7
−3.665
−12.840
64.483
V135P
A2


8
0.228
−9.423
49.613
M137L*
A2


9
−1.725
−0.801
63.145
M158G
A3


10
−0.401
−5.049
58.793
Y160F
A3


11
3.525
−11.762
46.471
D255G
B1


12
−0.844
−15.289
50.586
H257K
B1


13
−2.269
−15.735
54.104
L258V
B1


14
5.803
−16.354
45.249
H266Q
B1


15
8.069
−13.510
39.218
L268K
A4


16
10.985
−12.040
37.288
K269G
A4


17
14.223
−10.808
38.865
D270A
A4









These results show that a function conversion of CHS to STS can be achieved by desigiing mutations in the CHS sequence (SEQ ID NO:1) based on CHS structural information.
ADDITIONAL REFERENCES CITED
Schroeder, J. (1999) The Chalcone/Stilbene Synthase-type Family of Condensing Enzymes in Comprehensive Natural Products Chemistry Barton, D. & Nakanishi, K. (ed.) 1 (Elsevier Science Ltd., Amsterdam 1999).
Ferrer, J.-L., Jez, J. M., Bowman, M. E., Dixon, R. A., and Noel, J. P. (1999) Structure of Chalcone Synthase and the Molecular Basis of Plant Polyketide Biosynthesis. Nature Structural Biology, 6: 775-783.
Jez, J. M., Ferrer, J.-L., Bowman, M. E., Dixon, R. A., and Noel, J. P. (2000) Dissection of malonyl-CoA decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase. Biochemistiy, 39: 890-902.
Jez, J. M. & Noel, J. P. (2000) Mechanism of chalcone synthase: pKa of the catalytic cysteine and the role of the conserved histidine in a plant polyketide synthase. J. Biol. Chem. 2000 Sep. 26 [epub ahead of print—in press].
Jez, J. M., Austin, M. B., Ferrer, J.-L., Bowman, M. E., Schroder, J., and Noel, J. P. (2000) Structural control ofpolyketide formation in plant-specific polyketide synthases. Chemistry & Biology 7(12):919-930.
Tropf S, Lanz T, Rensing S A, Schroder J, Schroder G Evidence that stilbene synthases have developed from chalcone synthases several times in the course of evolution J Mol Evol 1994 June; 38(6):610-8.
Suh D Y, Fukuma K, Kagami J, Yamazaki Y, Shibuya M, Ebizuka Y, Sankawa U Identification of amino acid residues important in the cyclization reactions of chalcone and stilbene synthases Biochem J 2000 Aug. 15; 350(Pt 1):229-235.
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.







APPENDIX A







Pinus sylvestris STS
















ATOM
#
TYPE
RES
X
Y
Z
OCC
B





















ATOM
1
CB
ASP
A
5
15.478
−29.459
49.168
1.00
67.43
A


ATOM
2
CG
ASP
A
5
16.008
−30.062
47.877
1.00
68.10
A


ATOM
3
OD1
ASP
A
5
17.184
−30.480
47.850
1.00
68.26
A


ATOM
4
OD2
ASP
A
5
15.247
−30.116
46.890
1.00
68.59
A


ATOM
5
C
ASP
A
5
16.056
−27.113
48.532
1.00
65.16
A


ATOM
6
O
ASP
A
5
17.024
−26.582
47.995
1.00
64.39
A


ATOM
7
N
ASP
A
5
15.729
−27.703
50.902
1.00
67.43
A


ATOM
8
CA
ASP
A
5
16.237
−28.193
49.588
1.00
66.83
A


ATOM
9
N
PHE
A
6
14.800
−26.782
48.261
1.00
64.20
A


ATOM
10
CA
PHE
A
6
14.453
−25.779
47.266
1.00
63.13
A


ATOM
11
CB
PHE
A
6
12.938
−25.783
47.053
1.00
63.60
A


ATOM
12
CG
PHE
A
6
12.353
−27.157
46.885
1.00
64.51
A


ATOM
13
CD1
PHE
A
6
11.522
−27.695
47.866
1.00
66.17
A


ATOM
14
CD2
PHE
A
6
12.642
−27.923
45.760
1.00
63.90
A


ATOM
15
CE1
PHE
A
6
10.987
−28.976
47.729
1.00
65.63
A


ATOM
16
CE2
PHE
A
6
12.113
−29.206
45.613
1.00
63.56
A


ATOM
17
CZ
PHE
A
6
11.285
−29.734
46.598
1.00
64.57
A


ATOM
18
C
PHE
A
6
14.926
−24.360
47.606
1.00
62.05
A


ATOM
19
O
PHE
A
6
15.234
−23.577
46.707
1.00
61.61
A


ATOM
20
N
GLU
A
7
14.982
−24.029
48.895
1.00
61.34
A


ATOM
21
CA
GLU
A
7
15.416
−22.699
49.317
1.00
59.88
A


ATOM
22
CB
GLU
A
7
15.345
−22.556
50.845
1.00
61.69
A


ATOM
23
CG
GLU
A
7
15.802
−21.182
51.365
1.00
63.25
A


ATOM
24
CD
GLU
A
7
15.466
−20.956
52.840
1.00
64.35
A


ATOM
25
OE1
GLU
A
7
14.263
−20.904
53.183
1.00
64.96
A


ATOM
26
OE2
GLU
A
7
16.401
−20.823
53.661
1.00
64.20
A


ATOM
27
C
GLU
A
7
16.832
−22.421
48.838
1.00
57.91
A


ATOM
28
O
GLU
A
7
17.322
−21.298
48.950
1.00
58.52
A


ATOM
29
N
GLY
A
8
17.487
−23.455
48.315
1.00
56.11
A


ATOM
30
CA
GLY
A
8
18.839
−23.312
47.796
1.00
52.75
A


ATOM
31
C
GLY
A
8
18.787
−23.324
46.277
1.00
50.24
A


ATOM
32
O
GLY
A
8
19.523
−22.595
45.601
1.00
49.08
A


ATOM
33
N
PHE
A
9
17.899
−24.163
45.748
1.00
47.36
A


ATOM
34
CA
PHE
A
9
17.696
−24.287
44.312
1.00
45.44
A


ATOM
35
CB
PHE
A
9
16.631
−25.347
44.028
1.00
46.27
A


ATOM
36
CG
PHE
A
9
16.463
−25.670
42.569
1.00
46.38
A


ATOM
37
CD1
PHE
A
9
17.453
−26.362
41.878
1.00
45.31
A


ATOM
38
CD2
PHE
A
9
15.308
−25.296
41.889
1.00
46.41
A


ATOM
39
CE1
PHE
A
9
17.294
−26.678
40.532
1.00
46.87
A


ATOM
40
CE2
PHE
A
9
15.139
−25.608
40.540
1.00
46.26
A


ATOM
41
CZ
PHE
A
9
16.131
−26.299
39.862
1.00
46.36
A


ATOM
42
C
PHE
A
9
17.219
−22.938
43.779
1.00
43.88
A


ATOM
43
O
PHE
A
9
17.610
−22.503
42.695
1.00
42.95
A


ATOM
44
N
ARG
A
10
16.369
−22.285
44.559
1.00
42.46
A


ATOM
45
CA
ARG
A
10
15.820
−20.988
44.199
1.00
41.78
A


ATOM
46
CB
ARG
A
10
14.759
−20.587
45.227
1.00
42.76
A


ATOM
47
CG
ARG
A
10
13.336
−20.513
44.699
1.00
45.24
A


ATOM
48
CD
ARG
A
10
13.108
−19.253
43.870
1.00
46.91
A


ATOM
49
NE
ARG
A
10
13.803
−19.267
42.582
1.00
47.12
A


ATOM
50
CZ
ARG
A
10
13.848
−18.226
41.753
1.00
47.04
A


ATOM
51
NH1
ARG
A
10
13.243
−17.092
42.083
1.00
46.16
A


ATOM
52
NH2
ARG
A
10
14.490
−18.316
40.599
1.00
45.13
A


ATOM
53
C
ARG
A
10
16.912
−19.923
44.145
1.00
41.81
A


ATOM
54
O
ARG
A
10
17.039
−19.191
43.158
1.00
40.31
A


ATOM
55
N
LYS
A
11
17.704
−19.848
45.211
1.00
41.51
A


ATOM
56
CA
LYS
A
11
18.771
−18.859
45.306
1.00
42.45
A


ATOM
57
CB
LYS
A
11
19.441
−18.946
46.679
1.00
44.35
A


ATOM
58
CG
LYS
A
11
18.520
−18.561
47.831
1.00
47.24
A


ATOM
59
CD
LYS
A
11
19.157
−18.828
49.194
1.00
47.39
A


ATOM
60
CE
LYS
A
11
18.222
−18.392
50.321
1.00
48.83
A


ATOM
61
NZ
LYS
A
11
18.760
−18.701
51.673
1.00
49.79
A


ATOM
62
C
LYS
A
11
19.819
−18.981
44.214
1.00
41.73
A


ATOM
63
O
LYS
A
11
20.409
−17.980
43.801
1.00
41.36
A


ATOM
64
N
LEU
A
12
20.048
−20.206
43.749
1.00
41.94
A


ATOM
65
CA
LEU
A
12
21.042
−20.465
42.705
1.00
41.33
A


ATOM
66
CB
LEU
A
12
21.631
−21.869
42.864
1.00
41.99
A


ATOM
67
CG
LEU
A
12
23.057
−21.952
43.411
1.00
42.59
A


ATOM
68
CD1
LEU
A
12
23.449
−23.403
43.608
1.00
44.32
A


ATOM
69
CD2
LEU
A
12
24.010
−21.276
42.445
1.00
42.25
A


ATOM
70
C
LEU
A
12
20.483
−20.321
41.299
1.00
40.77
A


ATOM
71
O
LEU
A
12
21.224
−20.037
40.357
1.00
41.09
A


ATOM
72
N
GLN
A
13
19.175
−20.520
41.167
1.00
39.79
A


ATOM
73
CA
GLN
A
13
18.490
−20.431
39.884
1.00
38.24
A


ATOM
74
CB
GLN
A
13
17.119
−21.113
39.996
1.00
38.10
A


ATOM
75
CG
GLN
A
13
16.185
−20.943
38.793
1.00
38.78
A


ATOM
76
CD
GLN
A
13
14.899
−21.761
38.934
1.00
39.17
A


ATOM
77
OE1
GLN
A
13
14.231
−21.723
39.975
1.00
35.94
A


ATOM
78
NE2
GLN
A
13
14.549
−22.500
37.884
1.00
36.91
A


ATOM
79
C
GLN
A
13
18.329
−18.996
39.395
1.00
38.22
A


ATOM
80
O
GLN
A
13
18.228
−18.764
38.195
1.00
39.15
A


ATOM
81
N
ARG
A
14
18.328
−18.040
40.322
1.00
37.88
A


ATOM
82
CA
ARG
A
14
18.149
−16.628
39.990
1.00
37.89
A


ATOM
83
CB
ARG
A
14
17.136
−16.013
40.950
1.00
40.76
A


ATOM
84
CG
ARG
A
14
17.583
−16.012
42.406
1.00
44.03
A


ATOM
85
CD
ARG
A
14
16.477
−15.471
43.280
1.00
46.98
A


ATOM
86
NE
ARG
A
14
16.898
−15.263
44.661
1.00
49.61
A


ATOM
87
CZ
ARG
A
14
16.112
−14.748
45.600
1.00
50.12
A


ATOM
88
NH1
ARG
A
14
14.868
−14.394
45.298
1.00
51.87
A


ATOM
89
NH2
ARG
A
14
16.567
−14.577
46.833
1.00
49.78
A


ATOM
90
C
ARG
A
14
19.431
−15.796
40.010
1.00
37.27
A


ATOM
91
O
ARG
A
14
20.383
−16.128
40.708
1.00
37.71
A


ATOM
92
N
ALA
A
15
19.434
−14.702
39.250
1.00
36.59
A


ATOM
93
CA
ALA
A
15
20.592
−13.811
39.144
1.00
36.04
A


ATOM
94
CB
ALA
A
15
20.561
−13.083
37.805
1.00
35.74
A


ATOM
95
C
ALA
A
15
20.675
−12.797
40.285
1.00
36.64
A


ATOM
96
O
ALA
A
15
19.668
−12.470
40.906
1.00
36.28
A


ATOM
97
N
ASP
A
16
21.877
−12.284
40.540
1.00
36.70
A


ATOM
98
CA
ASP
A
16
22.093
−11.331
41.626
1.00
37.04
A


ATOM
99
CB
ASP
A
16
23.517
−11.467
42.181
1.00
37.71
A


ATOM
100
CG
ASP
A
16
23.864
−12.885
42.578
1.00
39.12
A


ATOM
101
OD1
ASP
A
16
23.005
−13.579
43.161
1.00
41.62
A


ATOM
102
OD2
ASP
A
16
25.010
−13.301
42.319
1.00
39.23
A


ATOM
103
C
ASP
A
16
21.871
−9.857
41.292
1.00
37.37
A


ATOM
104
O
ASP
A
16
21.127
−9.152
41.978
1.00
38.64
A


ATOM
105
N
GLY
A
17
22.523
−9.387
40.240
1.00
35.60
A


ATOM
106
CA
GLY
A
17
22.422
−7.984
39.903
1.00
35.63
A


ATOM
107
C
GLY
A
17
21.159
−7.453
39.272
1.00
35.92
A


ATOM
108
O
GLY
A
17
20.077
−8.023
39.380
1.00
35.96
A


ATOM
109
N
PHE
A
18
21.329
−6.318
38.607
1.00
36.31
A


ATOM
110
CA
PHE
A
18
20.253
−5.636
37.923
1.00
34.75
A


ATOM
111
CB
PHE
A
18
20.466
−4.126
38.012
1.00
37.21
A


ATOM
112
CG
PHE
A
18
19.578
−3.441
39.004
1.00
39.74
A


ATOM
113
CD1
PHE
A
18
20.048
−2.351
39.732
1.00
39.87
A


ATOM
114
CD2
PHE
A
18
18.262
−3.862
39.195
1.00
40.31
A


ATOM
115
CE1
PHE
A
18
19.223
−1.690
40.637
1.00
40.82
A


ATOM
116
CE2
PHE
A
18
17.426
−3.204
40.101
1.00
40.34
A


ATOM
117
CZ
PHE
A
18
17.910
−2.119
40.823
1.00
41.49
A


ATOM
118
C
PHE
A
18
20.257
−6.048
36.469
1.00
33.11
A


ATOM
119
O
PHE
A
18
21.321
−6.251
35.886
1.00
30.89
A


ATOM
120
N
ALA
A
19
19.066
−6.184
35.895
1.00
32.19
A


ATOM
121
CA
ALA
A
19
18.932
−6.528
34.488
1.00
32.21
A


ATOM
122
CB
ALA
A
19
17.458
−6.639
34.106
1.00
32.97
A


ATOM
123
C
ALA
A
19
19.593
−5.362
33.746
1.00
32.44
A


ATOM
124
O
ALA
A
19
19.319
−4.187
34.039
1.00
30.18
A


ATOM
125
N
SER
A
20
20.464
−5.673
32.792
1.00
30.51
A


ATOM
126
CA
SER
A
20
21.158
−4.611
32.095
1.00
29.55
A


ATOM
127
CB
SER
A
20
22.575
−4.502
32.646
1.00
29.41
A


ATOM
128
OG
SER
A
20
22.544
−4.494
34.062
1.00
31.94
A


ATOM
129
C
SER
A
20
21.210
−4.779
30.598
1.00
29.71
A


ATOM
130
O
SER
A
20
21.222
−5.897
30.083
1.00
31.07
A


ATOM
131
N
ILE
A
21
21.231
−3.651
29.900
1.00
28.89
A


ATOM
132
CA
ILE
A
21
21.324
−3.651
28.454
1.00
29.32
A


ATOM
133
CB
ILE
A
21
20.827
−2.328
27.862
1.00
29.06
A


ATOM
134
CG2
ILE
A
21
20.864
−2.401
26.358
1.00
29.04
A


ATOM
135
CG1
ILE
A
21
19.403
−2.033
28.344
1.00
30.26
A


ATOM
136
CD1
ILE
A
21
18.400
−3.115
28.026
1.00
33.08
A


ATOM
137
C
ILE
A
21
22.817
−3.802
28.185
1.00
30.88
A


ATOM
138
O
ILE
A
21
23.619
−2.964
28.602
1.00
30.81
A


ATOM
139
N
LEU
A
22
23.194
−4.872
27.500
1.00
30.73
A


ATOM
140
CA
LEU
A
22
24.600
−5.121
27.240
1.00
29.37
A


ATOM
141
CB
LEU
A
22
24.926
−6.563
27.606
1.00
27.95
A


ATOM
142
CG
LEU
A
22
24.496
−6.947
29.019
1.00
26.37
A


ATOM
143
CD1
LEU
A
22
24.854
−8.404
29.301
1.00
26.97
A


ATOM
144
CD2
LEU
A
22
25.178
−6.019
30.006
1.00
27.73
A


ATOM
145
C
LEU
A
22
25.000
−4.843
25.801
1.00
30.57
A


ATOM
146
O
LEU
A
22
26.190
−4.902
25.457
1.00
30.82
A


ATOM
147
N
ALA
A
23
24.007
−4.537
24.966
1.00
29.20
A


ATOM
148
CA
ALA
A
23
24.255
−4.240
23.556
1.00
27.79
A


ATOM
149
CB
ALA
A
23
24.867
−5.449
22.865
1.00
24.35
A


ATOM
150
C
ALA
A
23
22.989
−3.804
22.825
1.00
27.34
A


ATOM
151
O
ALA
A
23
21.877
−4.233
23.150
1.00
25.25
A


ATOM
152
N
ILE
A
24
23.169
−2.934
21.837
1.00
27.98
A


ATOM
153
CA
ILE
A
24
22.048
−2.444
21.054
1.00
27.20
A


ATOM
154
CB
ILE
A
24
21.643
−1.002
21.444
1.00
26.17
A


ATOM
155
CG2
ILE
A
24
20.398
−.596
20.665
1.00
26.40
A


ATOM
156
CG1
ILE
A
24
21.361
−.895
22.945
1.00
26.96
A


ATOM
157
CD1
ILE
A
24
20.943
.540
23.399
1.00
22.86
A


ATOM
158
C
ILE
A
24
22.409
−2.437
19.572
1.00
27.82
A


ATOM
159
O
ILE
A
24
23.418
−1.859
19.165
1.00
27.57
A


ATOM
160
N
GLY
A
25
21.568
−3.098
18.782
1.00
28.16
A


ATOM
161
CA
GLY
A
25
21.746
−3.166
17.347
1.00
26.42
A


ATOM
162
C
GLY
A
25
20.512
−2.563
16.685
1.00
28.50
A


ATOM
163
O
GLY
A
25
19.409
−2.612
17.241
1.00
26.10
A


ATOM
164
N
THR
A
26
20.699
−2.012
15.490
1.00
28.50
A


ATOM
165
CA
THR
A
26
19.621
−1.377
14.741
1.00
30.82
A


ATOM
166
CB
THR
A
26
19.708
.168
14.908
1.00
32.46
A


ATOM
167
OG1
THR
A
26
18.878
.576
16.003
1.00
32.28
A


ATOM
168
CG2
THR
A
26
19.302
.894
13.629
1.00
34.07
A


ATOM
169
C
THR
A
26
19.691
−1.746
13.258
1.00
30.38
A


ATOM
170
O
THR
A
26
20.776
−1.870
12.694
1.00
30.95
A


ATOM
171
N
ALA
A
27
18.533
−1.914
12.630
1.00
28.84
A


ATOM
172
CA
ALA
A
27
18.495
−2.263
11.220
1.00
27.36
A


ATOM
173
CB
ALA
A
27
18.361
−3.753
11.075
1.00
26.92
A


ATOM
174
C
ALA
A
27
17.346
−1.564
10.506
1.00
26.05
A


ATOM
175
O
ALA
A
27
16.306
−1.337
11.089
1.00
23.77
A


ATOM
176
N
ASN
A
28
17.536
−1.231
9.235
1.00
28.03
A


ATOM
177
CA
ASN
A
28
16.490
−.573
8.457
1.00
28.64
A


ATOM
178
CB
ASN
A
28
16.646
.948
8.528
1.00
27.80
A


ATOM
179
CG
ASN
A
28
16.309
1.503
9.893
1.00
29.20
A


ATOM
180
OD1
ASN
A
28
17.197
1.766
10.715
1.00
28.54
A


ATOM
181
ND2
ASN
A
28
15.013
1.675
10.152
1.00
26.02
A


ATOM
182
C
ASN
A
28
16.481
−1.001
6.989
1.00
28.59
A


ATOM
183
O
ASN
A
28
17.525
−1.282
6.420
1.00
28.02
A


ATOM
184
N
PRO
A
29
15.292
−1.034
6.356
1.00
29.65
A


ATOM
185
CD
PRO
A
29
13.967
−.696
6.908
1.00
28.87
A


ATOM
186
CA
PRO
A
29
15.179
−1.425
4.947
1.00
29.12
A


ATOM
187
CB
PRO
A
29
13.671
−1.388
4.686
1.00
30.72
A


ATOM
188
CG
PRO
A
29
13.061
−1.530
6.048
1.00
32.13
A


ATOM
189
C
PRO
A
29
15.932
−.409
4.083
1.00
31.07
A


ATOM
190
O
PRO
A
29
16.037
.768
4.444
1.00
29.67
A


ATOM
191
N
PRO
A
30
16.452
−.853
2.927
1.00
32.61
A


ATOM
192
CD
PRO
A
30
16.229
−2.205
2.388
1.00
33.12
A


ATOM
193
CA
PRO
A
30
17.210
−.045
1.966
1.00
33.75
A


ATOM
194
CB
PRO
A
30
17.300
−.956
.748
1.00
33.69
A


ATOM
195
CG
PRO
A
30
17.308
−2.305
1.351
1.00
34.85
A


ATOM
196
C
PRO
A
30
16.553
1.276
1.618
1.00
34.72
A


ATOM
197
O
PRO
A
30
17.123
2.352
1.826
1.00
33.78
A


ATOM
198
N
ASN
A
31
15.342
1.172
1.084
1.00
36.47
A


ATOM
199
CA
ASN
A
31
14.577
2.332
.656
1.00
35.87
A


ATOM
200
CB
ASN
A
31
13.179
1.898
.222
1.00
37.58
A


ATOM
201
CG
ASN
A
31
12.379
3.033
−.377
1.00
38.77
A


ATOM
202
OD1
ASN
A
31
12.852
3.738
−1.267
1.00
42.91
A


ATOM
203
ND2
ASN
A
31
11.158
3.208
.097
1.00
38.97
A


ATOM
204
C
ASN
A
31
14.466
3.444
1.682
1.00
36.12
A


ATOM
205
O
ASN
A
31
13.752
3.330
2.678
1.00
35.66
A


ATOM
206
N
ALA
A
32
15.190
4.526
1.431
1.00
35.45
A


ATOM
207
CA
ALA
A
32
15.139
5.680
2.300
1.00
35.87
A


ATOM
208
CB
ALA
A
32
16.501
6.300
2.428
1.00
34.90
A


ATOM
209
C
ALA
A
32
14.186
6.633
1.603
1.00
36.32
A


ATOM
210
O
ALA
A
32
14.450
7.062
.481
1.00
36.89
A


ATOM
211
N
VAL
A
33
13.066
6.935
2.254
1.00
37.11
A


ATOM
212
CA
VAL
A
33
12.072
7.838
1.687
1.00
38.65
A


ATOM
213
CB
VAL
A
33
10.628
7.294
1.858
1.00
39.24
A


ATOM
214
CG1
VAL
A
33
10.507
5.921
1.248
1.00
38.32
A


ATOM
215
CG2
VAL
A
33
10.255
7.256
3.337
1.00
39.28
A


ATOM
216
C
VAL
A
33
12.135
9.195
2.371
1.00
40.05
A


ATOM
217
O
VAL
A
33
12.190
9.281
3.597
1.00
40.74
A


ATOM
218
N
ASP
A
34
12.120
10.259
1.579
1.00
41.52
A


ATOM
219
CA
ASP
A
34
12.159
11.601
2.140
1.00
42.79
A


ATOM
220
CB
ASP
A
34
12.984
12.526
1.239
1.00
45.56
A


ATOM
221
CG
ASP
A
34
14.476
12.234
1.316
1.00
47.51
A


ATOM
222
OD1
ASP
A
34
15.219
12.722
.439
1.00
49.63
A


ATOM
223
OD2
ASP
A
34
14.905
11.524
2.258
1.00
48.98
A


ATOM
224
C
ASP
A
34
10.735
12.120
2.287
1.00
42.33
A


ATOM
225
O
ASP
A
34
9.951
12.093
1.338
1.00
42.08
A


ATOM
226
N
GLN
A
35
10.407
12.582
3.490
1.00
41.73
A


ATOM
227
CA
GLN
A
35
9.076
13.098
3.787
1.00
41.81
A


ATOM
228
CB
GLN
A
35
9.020
13.584
5.243
1.00
40.69
A


ATOM
229
CG
GLN
A
35
7.627
13.923
5.764
1.00
40.17
A


ATOM
230
CD
GLN
A
35
6.798
12.688
6.067
1.00
40.34
A


ATOM
231
OE1
GLN
A
35
6.692
11.785
5.244
1.00
39.84
A


ATOM
232
NE2
GLN
A
35
6.200
12.649
7.252
1.00
39.72
A


ATOM
233
C
GLN
A
35
8.686
14.241
2.843
1.00
42.93
A


ATOM
234
O
GLN
A
35
7.504
14.483
2.613
1.00
44.31
A


ATOM
235
N
SER
A
36
9.677
14.940
2.294
1.00
43.00
A


ATOM
236
CA
SER
A
36
9.404
16.056
1.391
1.00
42.43
A


ATOM
237
CB
SER
A
36
10.701
16.798
1.060
1.00
42.98
A


ATOM
238
OG
SER
A
36
11.126
17.582
2.162
1.00
44.09
A


ATOM
239
C
SER
A
36
8.705
15.666
.092
1.00
41.13
A


ATOM
240
O
SER
A
36
7.772
16.339
−.345
1.00
39.36
A


ATOM
241
N
THR
A
37
9.155
14.579
−.522
1.00
39.75
A


ATOM
242
CA
THR
A
37
8.575
14.134
−1.783
1.00
39.31
A


ATOM
243
CB
THR
A
37
9.686
13.652
−2.762
1.00
39.54
A


ATOM
244
OG1
THR
A
37
10.694
14.666
−2.877
1.00
39.51
A


ATOM
245
CG2
THR
A
37
9.107
13.383
−4.151
1.00
40.15
A


ATOM
246
C
THR
A
37
7.557
13.010
−1.590
1.00
38.36
A


ATOM
247
O
THR
A
37
7.066
12.434
−2.564
1.00
38.53
A


ATOM
248
N
TYR
A
38
7.225
12.697
−.342
1.00
36.06
A


ATOM
249
CA
TYR
A
38
6.274
11.625
−.124
1.00
36.72
A


ATOM
250
CB
TYR
A
38
6.232
11.187
1.335
1.00
35.69
A


ATOM
251
CG
TYR
A
38
5.647
9.801
1.479
1.00
35.07
A


ATOM
252
CD1
TYR
A
38
6.260
8.704
.873
1.00
35.39
A


ATOM
253
CE1
TYR
A
38
5.724
7.420
.983
1.00
34.19
A


ATOM
254
CD2
TYR
A
38
4.476
9.585
2.201
1.00
35.84
A


ATOM
255
CE2
TYR
A
38
3.930
8.308
2.320
1.00
34.78
A


ATOM
256
CZ
TYR
A
38
4.561
7.229
1.710
1.00
33.22
A


ATOM
257
OH
TYR
A
38
4.037
5.967
1.840
1.00
30.24
A


ATOM
258
C
TYR
A
38
4.875
12.002
−.572
1.00
37.11
A


ATOM
259
O
TYR
A
38
4.125
11.151
−1.057
1.00
36.68
A


ATOM
260
N
PRO
A
39
4.495
13.279
−.407
1.00
36.61
A


ATOM
261
CD
PRO
A
39
5.087
14.349
.413
1.00
35.84
A


ATOM
262
CA
PRO
A
39
3.151
13.648
−.841
1.00
36.96
A


ATOM
263
CB
PRO
A
39
3.068
15.118
−.459
1.00
37.53
A


ATOM
264
CG
PRO
A
39
3.869
15.155
.811
1.00
37.43
A


ATOM
265
C
PRO
A
39
2.917
13.399
−2.330
1.00
36.68
A


ATOM
266
O
PRO
A
39
1.939
12.749
−2.700
1.00
37.75
A


ATOM
267
N
ASP
A
40
3.803
13.901
−3.187
1.00
35.67
A


ATOM
268
CA
ASP
A
40
3.626
13.681
−4.617
1.00
37.12
A


ATOM
269
CB
ASP
A
40
4.714
14.387
−5.438
1.00
38.06
A


ATOM
270
CG
ASP
A
40
4.556
15.905
−5.457
1.00
41.46
A


ATOM
271
OD1
ASP
A
40
3.426
16.411
−5.246
1.00
41.34
A


ATOM
272
OD2
ASP
A
40
5.570
16.595
−5.709
1.00
43.90
A


ATOM
273
C
ASP
A
40
3.663
12.187
−4.913
1.00
36.95
A


ATOM
274
O
ASP
A
40
2.752
11.654
−5.547
1.00
38.21
A


ATOM
275
N
PHE
A
41
4.715
11.521
−4.439
1.00
35.19
A


ATOM
276
CA
PHE
A
41
4.907
10.090
−4.637
1.00
35.05
A


ATOM
277
CB
PHE
A
41
6.236
9.647
−4.021
1.00
35.93
A


ATOM
278
CG
PHE
A
41
6.379
8.155
−3.916
1.00
34.85
A


ATOM
279
CD1
PHE
A
41
6.487
7.375
−5.051
1.00
36.28
A


ATOM
280
CD2
PHE
A
41
6.354
7.527
−2.681
1.00
36.32
A


ATOM
281
CE1
PHE
A
41
6.566
5.982
−4.960
1.00
36.91
A


ATOM
282
CE2
PHE
A
41
6.431
6.138
−2.579
1.00
35.53
A


ATOM
283
CZ
PHE
A
41
6.536
5.365
−3.724
1.00
35.23
A


ATOM
284
C
PHE
A
41
3.792
9.203
−4.071
1.00
34.73
A


ATOM
285
O
PHE
A
41
3.370
8.253
−4.724
1.00
32.31
A


ATOM
286
N
TYR
A
42
3.347
9.501
−2.848
1.00
35.03
A


ATOM
287
CA
TYR
A
42
2.283
8.734
−2.189
1.00
36.12
A


ATOM
288
CB
TYR
A
42
2.042
9.251
−.761
1.00
37.39
A


ATOM
289
CG
TYR
A
42
.882
8.580
−.041
1.00
39.07
A


ATOM
290
CD1
TYR
A
42
.912
7.220
.270
1.00
38.88
A


ATOM
291
CE1
TYR
A
42
−.164
6.599
.908
1.00
40.03
A


ATOM
292
CD2
TYR
A
42
−.256
9.306
.311
1.00
41.58
A


ATOM
293
CE2
TYR
A
42
−1.339
8.695
.950
1.00
42.57
A


ATOM
294
CZ
TYR
A
42
−1.286
7.340
1.242
1.00
42.03
A


ATOM
295
OH
TYR
A
42
−2.371
6.730
1.837
1.00
42.82
A


ATOM
296
C
TYR
A
42
.972
6.797
−2.966
1.00
35.76
A


ATOM
297
O
TYR
A
42
.263
7.794
−3.067
1.00
35.92
A


ATOM
298
N
PHE
A
43
.657
9.973
−3.511
1.00
35.17
A


ATOM
299
CA
PHE
A
43
−.570
10.157
−4.275
1.00
35.00
A


ATOM
300
CB
PHE
A
43
−1.008
11.621
−4.227
1.00
34.32
A


ATOM
301
CG
PHE
A
43
−1.821
11.946
−3.019
1.00
35.42
A


ATOM
302
CD1
PHE
A
43
−1.258
11.874
−1.749
1.00
36.46
A


ATOM
303
CD2
PHE
A
43
−3.182
12.209
−3.131
1.00
36.17
A


ATOM
304
CE1
PHE
A
43
−2.043
12.050
−.605
1.00
36.76
A


ATOM
305
CE2
PHE
A
43
−3.973
12.385
−1.995
1.00
36.73
A


ATOM
306
CZ
PHE
A
43
−3.402
12.303
−.733
1.00
36.01
A


ATOM
307
C
PHE
A
43
−.466
9.674
−5.711
1.00
34.97
A


ATOM
308
O
PHE
A
43
−1.464
9.296
−6.324
1.00
35.50
A


ATOM
309
N
ARG
A
44
.749
9.670
−6.238
1.00
35.11
A


ATOM
310
CA
ARG
A
44
.978
9.213
−7.594
1.00
36.10
A


ATOM
311
CB
ARG
A
44
2.377
9.628
−8.067
1.00
35.40
A


ATOM
312
CG
ARG
A
44
2.664
9.344
−9.535
1.00
35.13
A


ATOM
313
CD
ARG
A
44
4.163
9.339
−9.811
1.00
35.91
A


ATOM
314
NE
ARG
A
44
4.677
7.973
−9.832
1.00
37.90
A


ATOM
315
CZ
ARG
A
44
5.852
7.593
−9.347
1.00
36.82
A


ATOM
316
NH1
ARG
A
44
6.669
8.472
−8.787
1.00
35.87
A


ATOM
317
NH2
ARG
A
44
6.203
6.319
−9.420
1.00
35.52
A


ATOM
318
C
ARG
A
44
.875
7.692
−7.596
1.00
36.32
A


ATOM
319
O
ARG
A
44
.045
7.116
−8.289
1.00
37.41
A


ATOM
320
N
ILE
A
45
1.724
7.051
−6.801
1.00
36.73
A


ATOM
321
CA
ILE
A
45
1.761
5.597
−6.709
1.00
36.73
A


ATOM
322
CB
ILE
A
45
2.832
5.150
−5.657
1.00
37.01
A


ATOM
323
CG2
ILE
A
45
2.165
4.717
−4.354
1.00
36.42
A


ATOM
324
CG1
ILE
A
45
3.705
4.028
−6.238
1.00
36.57
A


ATOM
325
CD1
ILE
A
45
2.967
2.746
−6.571
1.00
38.47
A


ATOM
326
C
ILE
A
45
.391
4.990
−6.379
1.00
36.30
A


ATOM
327
O
ILE
A
45
.153
3.810
−6.621
1.00
34.20
A


ATOM
328
N
THR
A
46
−.515
5.801
−5.838
1.00
38.01
A


ATOM
329
CA
THR
A
46
−1.850
5.310
−5.493
1.00
37.39
A


ATOM
330
CB
THR
A
46
−2.252
5.740
−4.074
1.00
36.17
A


ATOM
331
OG1
THR
A
46
−1.982
7.136
−3.893
1.00
33.06
A


ATOM
332
CG2
THR
A
46
−1.479
4.926
−3.048
1.00
37.56
A


ATOM
333
C
THR
A
46
−2.958
5.728
−6.457
1.00
38.51
A


ATOM
334
O
THR
A
46
−4.132
5.436
−6.219
1.00
37.81
A


ATOM
335
N
GLY
A
47
−2.584
6.408
−7.540
1.00
39.96
A


ATOM
336
CA
GLY
A
47
−3.565
6.846
−8.521
1.00
42.56
A


ATOM
337
C
GLY
A
47
−4.502
7.909
−7.984
1.00
44.81
A


ATOM
338
O
GLY
A
47
−5.650
8.022
−8.420
1.00
43.82
A


ATOM
339
N
ASN
A
48
−4.005
8.694
−7.035
1.00
46.78
A


ATOM
340
CA
ASN
A
48
−4.797
9.746
−6.421
1.00
49.83
A


ATOM
341
CB
ASN
A
48
−4.906
9.495
−4.911
1.00
49.33
A


ATOM
342
CG
ASN
A
48
−5.900
8.388
−4.562
1.00
49.27
A


ATOM
343
OD1
ASN
A
48
−7.092
8.641
−4.364
1.00
47.01
A


ATOM
344
ND2
ASN
A
48
−5.410
7.156
−4.494
1.00
47.58
A


ATOM
345
C
ASN
A
48
−4.222
11.141
−6.674
1.00
52.04
A


ATOM
346
O
ASN
A
48
−4.160
11.965
−5.765
1.00
51.94
A


ATOM
347
N
GLU
A
49
−3.800
11.407
−7.906
1.00
54.73
A


ATOM
348
CA
GLU
A
49
−3.246
12.720
−8.234
1.00
57.69
A


ATOM
349
CB
GLU
A
49
−2.369
12.637
−9.485
1.00
59.73
A


ATOM
350
CG
GLU
A
49
−.879
12.518
−9.183
1.00
63.54
A


ATOM
351
CD
GLU
A
49
−.007
12.726
−10.417
1.00
66.25
A


ATOM
352
OE1
GLU
A
49
−.282
13.681
−11.186
1.00
65.49
A


ATOM
353
OE2
GLU
A
49
.959
11.945
−10.605
1.00
66.00
A


ATOM
354
C
GLU
A
49
−4.329
13.776
−8.446
1.00
58.31
A


ATOM
355
O
GLU
A
49
−4.185
14.927
−8.035
1.00
59.07
A


ATOM
356
N
HIS
A
50
−5.418
13.371
−9.084
1.00
58.62
A


ATOM
357
CA
HIS
A
50
−6.527
14.268
−9.374
1.00
59.61
A


ATOM
358
CB
HIS
A
50
−7.610
13.497
−10.121
1.00
60.54
A


ATOM
359
CG
HIS
A
50
−8.106
12.301
−9.376
1.00
61.50
A


ATOM
360
CD2
HIS
A
50
−7.982
10.977
−9.629
1.00
62.11
A


ATOM
361
ND1
HIS
A
50
−8.800
12.402
−8.190
1.00
62.16
A


ATOM
362
CE1
HIS
A
50
−9.084
11.191
−7.744
1.00
62.79
A


ATOM
363
NE2
HIS
A
50
−8.599
10.309
−8.599
1.00
62.52
A


ATOM
364
C
HIS
A
50
−7.149
14.957
−8.153
1.30
59.88
A


ATOM
365
O
HIS
A
50
−7.651
16.080
−8.270
1.00
60.59
A


ATOM
366
N
ASN
A
51
−7.128
14.296
−6.995
1.00
58.82
A


ATOM
367
CA
ASN
A
51
−7.719
14.870
−5.781
1.00
56.81
A


ATOM
368
CB
ASN
A
51
−8.203
13.767
−4.843
1.00
56.29
A


ATOM
369
CG
ASN
A
51
−9.152
14.286
−3.790
1.00
56.26
A


ATOM
370
OD1
ASN
A
51
−8.874
15.284
−3.123
1.00
56.98
A


ATOM
371
ND2
ASN
A
51
−10.282
13.614
−3.632
1.00
56.27
A


ATOM
372
C
ASN
A
51
−6.760
15.785
−5.028
1.00
56.35
A


ATOM
373
O
ASN
A
51
−6.394
15.529
−3.877
1.00
55.87
A


ATOM
374
N
THR
A
52
−6.376
16.860
−5.705
1.00
55.80
A


ATOM
375
CA
THR
A
52
−5.463
17.865
−5.188
1.00
54.81
A


ATOM
376
CB
THR
A
52
−5.459
19.087
−6.111
1.00
55.61
A


ATOM
377
OG1
THR
A
52
−6.814
19.464
−6.398
1.00
54.96
A


ATOM
378
CG2
THR
A
52
−4.736
18.764
−7.417
1.00
55.96
A


ATOM
379
C
THR
A
52
−5.750
18.336
−3.767
1.00
53.99
A


ATOM
380
O
THR
A
52
−4.838
18.786
−3.071
1.00
53.61
A


ATOM
381
N
GLU
A
53
−7.007
18.241
−3.339
1.00
53.25
A


ATOM
382
CA
GLU
A
53
−7.384
18.670
−1.991
1.00
52.66
A


ATOM
383
CB
GLU
A
53
−8.908
18.712
−1.848
1.03
53.87
A


ATOM
384
CG
GLU
A
53
−9.545
19.936
−2.469
1.00
56.65
A


ATOM
385
CD
GLU
A
53
−9.077
21.226
−1.809
1.00
58.56
A


ATOM
386
OE1
GLU
A
53
−9.448
21.471
−.638
1.00
59.21
A


ATOM
387
OE2
GLU
A
53
−8.331
21.990
−2.460
1.00
59.26
A


ATOM
388
C
GLU
A
53
−6.795
17.774
−.902
1.00
51.50
A


ATOM
389
O
GLU
A
53
−6.097
18.248
−.001
1.00
50.48
A


ATOM
390
N
LEU
A
54
−7.084
16.479
−.986
1.00
50.21
A


ATOM
391
CA
LEU
A
54
−6.580
15.524
−.006
1.00
49.09
A


ATOM
392
CB
LEU
A
54
−7.098
14.123
−.324
1.00
46.64
A


ATOM
393
CG
LEU
A
54
−6.867
13.107
.787
1.00
45.40
A


ATOM
394
CD1
LEU
A
54
−7.488
13.628
2.071
1.00
43.87
A


ATOM
395
CD2
LEU
A
54
−7.464
11.766
.393
1.00
44.37
A


ATOM
396
C
LEU
A
54
−5.057
15.524
−.019
1.00
49.00
A


ATOM
397
O
LEU
A
54
−4.411
15.498
1.033
1.00
47.49
A


ATOM
398
N
LYS
A
55
−4.497
15.556
−1.226
1.00
48.68
A


ATOM
399
CA
LYS
A
55
−3.055
15.572
−1.408
1.00
47.72
A


ATOM
400
CB
LYS
A
55
−2.729
15.647
−2.901
1.00
48.44
A


ATOM
401
CG
LYS
A
55
−1.262
15.406
−3.270
1.00
50.21
A


ATOM
402
CD
LYS
A
55
−1.057
15.477
−4.794
1.00
50.11
A


ATOM
403
CE
LYS
A
55
.398
15.232
−5.188
1.00
51.15
A


ATOM
404
NZ
LYS
A
55
.637
15.423
−6.646
1.00
51.72
A


ATOM
405
C
LYS
A
55
−2.465
16.773
−.667
1.00
46.95
A


ATOM
406
O
LYS
A
55
−1.555
16.624
.148
1.00
45.99
A


ATOM
407
N
ASP
A
56
−2.993
17.962
−.938
1.00
47.40
A


ATOM
408
CA
ASP
A
56
−2.487
19.158
−.277
1.00
48.44
A


ATOM
409
CB
ASP
A
56
−3.171
20.423
−.811
1.00
50.05
A


ATOM
410
CG
ASP
A
56
−2.567
21.706
−.233
1.00
52.26
A


ATOM
411
OD1
ASP
A
56
−1.327
21.769
−.059
1.00
52.72
A


ATOM
412
OD2
ASP
A
56
−3.332
22.656
.038
1.00
53.74
A


ATOM
413
C
ASP
A
56
−2.716
19.027
1.217
1.00
47.51
A


ATOM
414
O
ASP
A
56
−1.932
19.538
2.026
1.00
47.63
A


ATOM
415
N
LYS
A
57
−3.793
18.337
1.582
1.00
46.00
A


ATOM
416
CA
LYS
A
57
−4.098
18.115
2.988
1.00
45.09
A


ATOM
417
CB
LYS
A
57
−5.500
17.525
3.150
1.00
46.26
A


ATOM
418
CG
LYS
A
57
−5.753
16.920
4.524
1.00
47.34
A


ATOM
419
CD
LYS
A
57
−7.006
17.481
5.180
1.00
48.29
A


ATOM
420
CE
LYS
A
57
−8.282
17.064
4.462
1.00
46.87
A


ATOM
421
NZ
LYS
A
57
−9.480
17.627
5.149
1.00
46.62
A


ATOM
422
C
LYS
A
57
−3.068
17.164
3.593
1.00
42.98
A


ATOM
423
O
LYS
A
57
−2.712
17.280
4.762
1.00
41.90
A


ATOM
424
N
PHE
A
58
−2.587
16.229
2.786
1.00
41.09
A


ATOM
425
CA
PHE
A
58
−1.606
15.270
3.261
1.00
40.95
A


ATOM
426
CB
PHE
A
58
−1.620
14.033
2.371
1.00
40.96
A


ATOM
427
CG
PHE
A
58
−.646
12.975
2.786
1.00
42.12
A


ATOM
428
CD1
PHE
A
58
.574
12.838
2.128
1.00
42.03
A


ATOM
429
CD2
PHE
A
58
−.957
12.093
3.815
1.00
41.57
A


ATOM
430
CE1
PHE
A
58
1.470
11.834
2.484
1.00
42.26
A


ATOM
431
CE2
PHE
A
58
−.064
11.085
4.181
1.00
42.43
A


ATOM
432
CZ
PHE
A
58
1.150
10.955
3.512
1.00
40.79
A


ATOM
433
C
PHE
A
58
−.219
15.888
3.300
1.00
41.74
A


ATOM
434
O
PHE
A
58
.610
15.528
4.141
1.00
40.63
A


ATOM
435
N
LYS
A
59
.034
16.823
2.389
1.00
42.14
A


ATOM
436
CA
LYS
A
59
1.327
17.496
2.363
1.00
42.84
A


ATOM
437
CB
LYS
A
59
1.445
18.441
1.158
1.00
44.84
A


ATOM
438
CG
LYS
A
59
1.444
17.756
−.206
1.00
47.75
A


ATOM
439
CD
LYS
A
59
1.788
18.739
−1.329
1.00
49.41
A


ATOM
440
CE
LYS
A
59
1.789
18.050
−2.697
1.00
51.02
A


ATOM
441
NZ
LYS
A
59
2.057
18.999
−3.823
1.00
51.85
A


ATOM
442
C
LYS
A
59
1.403
18.307
3.639
1.00
41.25
A


ATOM
443
O
LYS
A
59
2.446
18.388
4.278
1.00
40.75
A


ATOM
444
N
ARG
A
60
.274
18.898
4.005
1.00
40.74
A


ATOM
445
CA
ARG
A
60
.198
19.713
5.205
1.00
42.28
A


ATOM
446
CB
ARG
A
60
−1.133
20.473
5.239
1.00
46.48
A


ATOM
447
CG
ARG
A
60
−1.243
21.564
4.174
1.00
51.56
A


ATOM
448
CD
ARG
A
60
−.227
22.673
4.426
1.00
56.26
A


ATOM
449
NE
ARG
A
60
−.197
23.681
3.364
1.00
60.76
A


ATOM
450
CZ
ARG
A
60
.504
24.812
3.426
1.00
62.22
A


ATOM
451
NH1
ARG
A
60
1.233
25.084
4.501
1.00
62.02
A


ATOM
452
NH2
ARG
A
60
.486
25.670
2.412
1.00
62.68
A


ATOM
453
C
ARG
A
60
.374
18.885
6.475
1.00
40.66
A


ATOM
454
O
ARG
A
60
.823
19.402
7.496
1.00
41.04
A


ATOM
455
N
ILE
A
61
.024
17.603
6.421
1.00
38.03
A


ATOM
456
CA
ILE
A
61
.192
16.746
7.590
1.00
34.21
A


ATOM
457
CB
ILE
A
61
−.631
15.456
7.497
1.00
32.45
A


ATOM
458
CG2
ILE
A
61
−.228
14.520
8.638
1.00
29.47
A


ATOM
459
CG1
ILE
A
61
−2.127
15.776
7.548
1.00
31.31
A


ATOM
460
CD1
ILE
A
61
−3.010
14.567
7.320
1.00
30.86
A


ATOM
461
C
ILE
A
61
1.654
16.344
7.689
1.00
33.40
A


ATOM
462
O
ILE
A
61
2.230
16.326
8.773
1.00
30.59
A


ATOM
463
N
CYS
A
62
2.235
16.012
6.539
1.00
34.39
A


ATOM
464
CA
CYS
A
62
3.630
15.605
6.469
1.00
36.39
A


ATOM
465
CB
CYS
A
62
4.009
15.211
5.035
1.00
35.67
A


ATOM
466
SG
CYS
A
62
3.392
13.621
4.435
1.00
36.68
A


ATOM
467
C
CYS
A
62
4.543
16.736
6.937
1.00
37.23
A


ATOM
468
O
CYS
A
62
5.539
16.498
7.615
1.00
36.14
A


ATOM
469
N
GLU
A
63
4.190
17.968
6.585
1.00
38.33
A


ATOM
470
CA
GLU
A
63
4.996
19.124
6.961
1.00
39.37
A


ATOM
471
CB
GLU
A
63
4.608
20.325
6.097
1.00
41.87
A


ATOM
472
CG
GLU
A
63
5.008
20.131
4.637
1.00
44.04
A


ATOM
473
CD
GLU
A
63
4.621
21.296
3.752
1.00
45.93
A


ATOM
474
OE1
GLU
A
63
3.407
21.593
3.652
1.00
47.07
A


ATOM
475
OE2
GLU
A
63
5.533
21.909
3.152
1.00
46.35
A


ATOM
476
C
GLU
A
63
4.957
19.483
8.442
1.00
37.95
A


ATOM
477
O
GLU
A
63
5.798
20.250
8.915
1.00
37.13
A


ATOM
478
N
ARG
A
64
3.986
18.934
9.166
1.00
36.39
A


ATOM
479
CA
ARG
A
64
3.886
19.163
10.608
1.00
37.43
A


ATOM
480
CB
ARG
A
64
2.428
19.371
11.037
1.00
37.43
A


ATOM
481
CG
ARG
A
64
1.829
20.731
10.710
1.00
40.40
A


ATOM
482
CD
ARG
A
64
.612
20.995
11.592
1.00
42.29
A


ATOM
483
NE
ARG
A
64
−.415
19.974
11.406
1.00
43.14
A


ATOM
484
CZ
ARG
A
64
−1.196
19.897
10.335
1.00
44.35
A


ATOM
485
NH1
ARG
A
64
−1.065
20.785
9.360
1.00
44.07
A


ATOM
486
NH2
ARG
A
64
−2.103
18.933
10.234
1.00
44.06
A


ATOM
487
C
ARG
A
64
4.454
17.952
11.377
1.00
37.08
A


ATOM
488
O
ARG
A
64
4.840
18.067
12.539
1.00
38.38
A


ATOM
489
N
SER
A
65
4.506
16.801
10.714
1.00
36.12
A


ATOM
490
CA
SER
A
65
4.997
15.570
11.314
1.00
35.70
A


ATOM
491
CB
SER
A
65
5.048
14.464
10.265
1.00
35.60
A


ATOM
492
OG
SER
A
65
6.067
14.711
9.310
1.00
34.83
A


ATOM
493
C
SER
A
65
6.364
15.665
11.982
1.00
36.13
A


ATOM
494
O
SER
A
65
6.655
14.899
12.890
1.00
36.64
A


ATOM
495
N
ALA
A
66
7.207
16.593
11.540
1.00
36.59
A


ATOM
496
CA
ALA
A
66
8.544
16.736
12.115
1.00
34.73
A


ATOM
497
CB
ALA
A
66
8.451
16.912
13.624
1.00
34.03
A


ATOM
498
C
ALA
A
66
9.372
15.497
11.780
1.00
35.37
A


ATOM
499
O
ALA
A
66
10.364
15.199
12.444
1.00
37.03
A


ATOM
500
N
ILE
A
67
8.947
14.765
10.753
1.00
34.92
A


ATOM
501
CA
ILE
A
67
9.651
13.566
10.312
1.00
33.47
A


ATOM
502
CB
ILE
A
67
8.673
12.386
10.079
1.00
30.76
A


ATOM
503
CG2
ILE
A
67
9.438
11.146
9.666
1.00
29.23
A


ATOM
504
CG1
ILE
A
67
7.872
12.108
11.348
1.00
28.84
A


ATOM
505
CD1
ILE
A
67
6.788
11.067
11.151
1.00
28.29
A


ATOM
506
C
ILE
A
67
10.312
13.925
8.989
1.00
34.28
A


ATOM
507
O
ILE
A
67
9.624
14.239
8.017
1.00
36.16
A


ATOM
508
N
LYS
A
68
11.638
13.873
8.943
1.00
34.27
A


ATOM
509
CA
LYS
A
68
12.352
14.235
7.724
1.00
34.52
A


ATOM
510
CB
LYS
A
68
13.688
14.891
8.090
1.00
35.42
A


ATOM
511
CG
LYS
A
68
13.505
16.015
9.091
1.00
41.45
A


ATOM
512
CD
LYS
A
68
14.753
16.865
9.328
1.00
44.25
A


ATOM
513
CE
LYS
A
68
14.409
18.006
10.300
1.00
45.99
A


ATOM
514
NZ
LYS
A
68
15.554
18.899
10.677
1.00
46.24
A


ATOM
515
C
LYS
A
68
12.569
13.077
6.760
1.00
33.29
A


ATOM
516
O
LYS
A
68
12.737
13.287
5.555
1.00
33.72
A


ATOM
517
N
GLN
A
69
12.560
11.854
7.283
1.00
31.93
A


ATOM
518
CA
GLN
A
69
12.756
10.679
6.441
1.00
30.12
A


ATOM
519
CB
GLN
A
69
14.211
10.591
5.963
1.00
32.01
A


ATOM
520
CG
GLN
A
69
15.208
10.263
7.060
1.00
34.66
A


ATOM
521
CD
GLN
A
69
15.994
8.989
6.779
1.00
37.65
A


ATOM
522
OE1
GLN
A
69
15.416
7.908
6.627
1.00
42.24
A


ATOM
523
NE2
GLN
A
69
17.317
9.108
6.717
1.00
35.40
A


ATOM
524
C
GLN
A
69
12.410
9.400
7.174
1.00
27.55
A


ATOM
525
O
GLN
A
69
12.518
9.318
8.389
1.00
26.69
A


ATOM
526
N
ARG
A
70
12.009
8.396
6.414
1.00
26.61
A


ATOM
527
CA
ARG
A
70
11.648
7.110
6.973
1.00
28.66
A


ATOM
528
CB
ARG
A
70
10.129
6.982
7.054
1.00
29.52
A


ATOM
529
CG
ARG
A
70
9.441
7.999
7.946
1.00
31.27
A


ATOM
530
CD
ARG
A
70
7.912
7.856
7.848
1.00
32.64
A


ATOM
531
NE
ARG
A
70
7.373
8.476
6.636
1.00
31.85
A


ATOM
532
CZ
ARG
A
70
6.126
8.330
6.190
1.00
33.49
A


ATOM
533
NH1
ARG
A
70
5.253
7.571
6.844
1.00
33.87
A


ATOM
534
NH2
ARG
A
70
5.746
8.952
5.083
1.00
33.20
A


ATOM
535
C
ARG
A
70
12.202
6.021
6.065
1.00
28.42
A


ATOM
536
O
ARG
A
70
12.528
6.280
4.908
1.00
26.75
A


ATOM
537
N
TYR
A
71
12.322
4.809
6.596
1.00
28.10
A


ATOM
538
CA
TYR
A
71
12.811
3.683
5.814
1.00
28.19
A


ATOM
539
CB
TYR
A
71
13.940
2.958
6.556
1.00
28.62
A


ATOM
540
CG
TYR
A
71
15.224
3.761
6.650
1.00
29.33
A


ATOM
541
CD1
TYR
A
71
15.475
4.597
7.735
1.00
29.31
A


ATOM
542
CE1
TYR
A
71
16.651
5.341
7.812
1.00
31.09
A


ATOM
543
CD2
TYR
A
71
16.180
3.690
5.643
1.00
28.03
A


ATOM
544
CE2
TYR
A
71
17.350
4.426
5.710
1.00
30.76
A


ATOM
545
CZ
TYR
A
71
17.581
5.248
6.794
1.00
30.97
A


ATOM
546
OH
TYR
A
71
18.748
5.974
6.847
1.00
34.98
A


ATOM
547
C
TYR
A
71
11.637
2.740
5.558
1.00
29.16
A


ATOM
548
O
TYR
A
71
11.068
2.161
6.486
1.00
26.84
A


ATOM
549
N
MET
A
72
11.275
2.599
4.288
1.00
28.94
A


ATOM
550
CA
MET
A
72
10.147
1.773
3.907
1.00
27.84
A


ATOM
551
CB
MET
A
72
9.169
2.600
3.062
1.00
27.20
A


ATOM
552
CG
MET
A
72
8.753
3.911
3.706
1.00
27.56
A


ATOM
553
SD
MET
A
72
7.148
4.518
3.144
1.00
22.93
A


ATOM
554
CE
MET
A
72
6.139
3.616
4.227
1.00
26.94
A


ATOM
555
C
MET
A
72
10.528
.516
3.151
1.00
26.70
A


ATOM
556
O
MET
A
72
11.360
.551
2.241
1.00
25.56
A


ATOM
557
N
TYR
A
73
9.918
−.597
3.549
1.00
24.06
A


ATOM
558
CA
TYR
A
73
10.147
−1.876
2.895
1.00
23.85
A


ATOM
559
CB
TYR
A
73
9.463
−3.014
3.658
1.00
24.18
A


ATOM
560
CG
TYR
A
73
9.171
−4.217
2.779
1.00
24.55
A


ATOM
561
CD1
TYR
A
73
10.193
−5.055
2.348
1.00
21.59
A


ATOM
562
CE1
TYR
A
73
9.928
−6.136
1.525
1.00
27.28
A


ATOM
563
CD2
TYR
A
73
7.869
−4.495
2.357
1.00
26.09
A


ATOM
564
CE2
TYR
A
73
7.594
−5.581
1.531
1.00
26.05
A


ATOM
565
CZ
TYR
A
73
8.630
−6.395
1.125
1.00
26.65
A


ATOM
566
OH
TYR
A
73
8.371
−7.483
.340
1.00
30.63
A


ATOM
567
C
TYR
A
73
9.501
−1.756
1.531
1.00
24.72
A


ATOM
568
O
TYR
A
73
10.066
−2.153
.516
1.00
25.42
A


ATOM
569
N
LEU
A
74
8.291
−1.220
1.529
1.00
24.58
A


ATOM
570
CA
LEU
A
74
7.547
−1.023
.297
1.00
27.00
A


ATOM
571
CB
LEU
A
74
6.134
−.524
.597
1.00
26.63
A


ATOM
572
CG
LEU
A
74
5.223
−1.486
1.347
1.00
23.99
A


ATOM
573
CD1
LEU
A
74
4.071
−.711
1.932
1.00
24.50
A


ATOM
574
CD2
LEU
A
74
4.749
−2.579
.420
1.00
23.90
A


ATOM
575
C
LEU
A
74
8.242
.004
−.576
1.00
27.44
A


ATOM
576
O
LEU
A
74
8.339
1.174
−.211 
1.00
26.38
A


ATOM
577
N
THR
A
75
8.733
−.447
−1.724
1.00
29.33
A


ATOM
578
CA
THR
A
75
9.385
.427
−2.685
1.00
28.26
A


ATOM
579
CB
THR
A
75
10.624
−.258
−3.316
1.00
27.99
A


ATOM
580
OG1
THR
A
75
10.243
−1.499
−3.918
1.00
27.29
A


ATOM
581
CG2
THR
A
75
11.671
−.542
−2.260
1.00
30.37
A


ATOM
582
C
THR
A
75
8.331
.701
−3.764
1.00
29.52
A


ATOM
583
O
THR
A
75
7.188
.229
−3.664
1.00
25.85
A


ATOM
584
N
GLU
A
76
8.699
1.464
−4.788
1.00
30.38
A


ATOM
585
CA
GLU
A
76
7.758
1.758
−5.853
1.00
31.86
A


ATOM
586
CB
GLU
A
76
8.277
2.888
−6.730
1.00
34.29
A


ATOM
587
CG
GLU
A
76
7.227
3.361
−7.709
1.00
37.84
A


ATOM
588
CD
GLU
A
76
7.774
4.305
−8.738
1.00
40.62
A


ATOM
589
OE1
GLU
A
76
8.541
5.215
−8.359
1.00
41.20
A


ATOM
590
OE2
GLU
A
76
7.422
4.144
−9.926
1.00
44.13
A


ATOM
591
C
GLU
A
76
7.562
.511
−6.707
1.00
32.06
A


ATOM
592
O
GLU
A
76
6.453
.199
−7.154
1.00
31.57
A


ATOM
593
N
GLU
A
77
8.662
−.192
−6.936
1.00
30.45
A


ATOM
594
CA
GLU
A
77
8.656
−1.412
−7.720
1.00
32.97
A


ATOM
595
CB
GLU
A
77
10.080
−1.949
−7.790
1.00
35.54
A


ATOM
596
CG
GLU
A
77
10.284
−3.126
−8.705
1.00
43.11
A


ATOM
597
CD
GLU
A
77
11.767
−3.446
−8.885
1.00
46.08
A


ATOM
598
OE1
GLU
A
77
12.485
−2.654
−9.543
1.00
47.40
A


ATOM
599
OE2
GLU
A
77
12.218
−4.484
−8.358
1.00
47.34
A


ATOM
600
C
GLU
A
77
7.727
−2.445
−7.089
1.00
33.13
A


ATOM
601
O
GLU
A
77
7.005
−3.150
−7.789
1.00
33.97
A


ATOM
602
N
ILE
A
78
7.737
−2.525
−5.761
1.00
32.98
A


ATOM
603
CA
ILE
A
78
6.890
−3.482
−5.045
1.00
33.29
A


ATOM
604
CB
ILE
A
78
7.368
−3.668
−3.584
1.00
32.97
A


ATOM
605
CG2
ILE
A
78
6.397
−4.556
−2.814
1.00
34.53
A


ATOM
606
CG1
ILE
A
78
8.745
−4.330
−3.571
1.00
31.63
A


ATOM
607
CD1
ILE
A
78
9.382
−4.396
−2.195
1.00
33.04
A


ATOM
608
C
ILE
A
78
5.419
−3.066
−5.051
1.00
34.05
A


ATOM
609
O
ILE
A
78
4.544
−3.902
−5.262
1.00
32.38
A


ATOM
610
N
LEU
A
79
5.145
−1.782
−4.813
1.00
35.12
A


ATOM
611
CA
LEU
A
79
3.770
−1.297
−4.834
1.00
36.98
A


ATOM
612
CB
LEU
A
79
3.698
.167
−4.389
1.00
37.47
A


ATOM
613
CG
LEU
A
79
3.811
.411
−2.887
1.00
37.60
A


ATOM
614
CD1
LEU
A
79
3.898
1.899
−2.597
1.00
36.08
A


ATOM
615
CD2
LEU
A
79
2.611
−.216
−2.202
1.00
35.79
A


ATOM
616
C
LEU
A
79
3.191
−1.433
−6.243
1.00
38.11
A


ATOM
617
O
LEU
A
79
2.002
−1.705
−6.405
1.00
39.23
A


ATOM
618
N
LYS
A
80
4.038
−1.262
−7.257
1.00
39.10
A


ATOM
619
CA
LYS
A
80
3.600
−1.368
−8.649
1.00
40.27
A


ATOM
620
CB
LYS
A
80
4.706
−.885
−9.589
1.00
42.10
A


ATOM
621
CG
LYS
A
80
4.913
.627
−9.598
1.00
43.49
A


ATOM
622
CD
LYS
A
80
4.325
1.294
−10.844
1.00
44.07
A


ATOM
623
CE
LYS
A
80
2.802
1.242
−10.867
1.00
46.55
A


ATOM
624
NZ
LYS
A
80
2.232
2.001
−12.020
1.00
47.24
A


ATOM
625
C
LYS
A
80
3.171
−2.787
−9.043
1.00
39.71
A


ATOM
626
O
LYS
A
80
2.313
−2.958
−9.910
1.00
39.42
A


ATOM
627
N
LYS
A
81
3.777
−3.799
−8.425
1.00
39.39
A


ATOM
628
CA
LYS
A
81
3.420
−5.188
−8.709
1.00
39.36
A


ATOM
629
CB
LYS
A
81
4.599
−6.129
−8.454
1.00
40.38
A


ATOM
630
CG
LYS
A
81
5.848
−5.880
−9.269
1.00
42.46
A


ATOM
631
CD
LYS
A
81
6.940
−6.882
−8.883
1.00
44.35
A


ATOM
632
CE
LYS
A
81
6.480
−8.334
−9.111
1.00
45.75
A


ATOM
633
NZ
LYS
A
81
7.512
−9.371
−8.780
1.00
43.48
A


ATOM
634
C
LYS
A
81
2.289
−5.598
−7.772
1.00
38.94
A


ATOM
635
O
LYS
A
81
1.782
−6.711
−7.850
1.00
40.01
A


ATOM
636
N
ASN
A
82
1.897
−4.693
−6.884
1.00
39.20
A


ATOM
637
CA
ASN
A
82
.849
−4.992
−5.918
1.00
38.88
A


ATOM
638
CB
ASN
A
82
1.475
−5.246
−4.543
1.00
38.01
A


ATOM
639
CG
ASN
A
82
2.231
−6.562
−4.482
1.00
36.74
A


ATOM
640
OD1
ASN
A
82
1.639
−7.619
−4.291
1.00
35.51
A


ATOM
641
ND2
ASN
A
82
3.541
−6.500
−4.663
1.00
34.42
A


ATOM
642
C
ASN
A
82
−.193
−3.890
−5.807
1.00
38.13
A


ATOM
643
O
ASN
A
82
−.275
−3.195
−4.788
1.00
39.26
A


ATOM
644
N
PRO
A
83
−1.017
−3.724
−6.851
1.00
36.98
A


ATOM
645
CD
PRO
A
83
−1.086
−4.574
−8.051
1.00
34.43
A


ATOM
646
CA
PRO
A
83
−2.069
−2.698
−6.867
1.00
37.02
A


ATOM
647
CB
PRO
A
83
−2.780
−2.957
−8.195
1.00
36.28
A


ATOM
648
CG
PRO
A
83
−2.530
−4.442
−8.435
1.00
34.63
A


ATOM
649
C
PRO
A
83
−3.042
−2.735
−5.673
1.00
37.05
A


ATOM
650
O
PRO
A
83
−3.478
−1.686
−5.192
1.00
39.34
A


ATOM
651
N
ASP
A
84
−3.367
−3.930
−5.185
1.00
35.56
A


ATOM
652
CA
ASP
A
84
−4.308
−4.062
−4.078
1.00
33.46
A


ATOM
653
CB
ASP
A
84
−4.649
−5.530
−3.853
1.00
34.51
A


ATOM
654
CG
ASP
A
84
−5.314
−6.158
−5.061
1.00
35.83
A


ATOM
655
OD1
ASP
A
84
−6.199
−5.499
−5.646
1.00
37.72
A


ATOM
656
OD2
ASP
A
84
−4.961
−7.308
−5.420
1.00
37.56
A


ATOM
657
C
ASP
A
84
−3.845
−3.426
−2.774
1.00
33.39
A


ATOM
658
O
ASP
A
84
−4.665
−2.968
−1.982
1.00
31.87
A


ATOM
659
N
VAL
A
85
−2.534
−3.411
−2.547
1.00
31.84
A


ATOM
660
CA
VAL
A
85
−1.970
−2.804
−1.349
1.00
29.40
A


ATOM
661
CB
VAL
A
85
−.464
−3.168
−1.201
1.00
31.38
A


ATOM
662
CG1
VAL
A
85
.244
−2.216
−.222
1.00
32.10
A


ATOM
663
CG2
VAL
A
85
−.336
−4.600
−.718
1.00
29.20
A


ATOM
664
C
VAL
A
85
−2.134
−1.282
−1.449
1.00
29.43
A


ATOM
665
O
VAL
A
85
−2.082
−.574
−.445
1.00
26.13
A


ATOM
666
N
CYS
A
86
−2.344
−.791
−2.670
1.00
29.46
A


ATOM
667
CA
CYS
A
88
−2.524
.638
−2.904
1.00
29.39
A


ATOM
668
CB
CYS
A
86
−2.097
1.001
−4.328
1.00
30.74
A


ATOM
669
SG
CYS
A
86
−.317
.843
−4.599
1.00
36.69
A


ATOM
670
C
CYS
A
86
−3.953
1.107
−2.664
1.00
29.64
A


ATOM
671
O
CYS
A
86
−4.179
2.262
−2.306
1.00
30.15
A


ATOM
672
N
ALA
A
87
−4.925
.228
−2.864
1.00
26.40
A


ATOM
673
CA
ALA
A
87
−6.295
.642
−2.636
1.00
28.82
A


ATOM
674
CB
ALA
A
87
−7.256
−.483
−2.988
1.00
25.62
A


ATOM
675
C
ALA
A
87
−6.429
1.031
−1.161
1.00
29.47
A


ATOM
676
O
ALA
A
87
−5.489
.881
−.385
1.00
29.21
A


ATOM
677
N
PHE
A
88
−7.591
1.548
−.779
1.00
30.50
A


ATOM
678
CA
PHE
A
88
−7.817
1.946
.604
1.00
31.87
A


ATOM
679
CB
PHE
A
88
−8.753
3.157
.667
1.00
31.60
A


ATOM
680
CG
PHE
A
88
−9.116
3.567
2.064
1.00
31.92
A


ATOM
681
CD1
PHE
A
88
−8.127
3.926
2.979
1.00
32.89
A


ATOM
682
CD2
PHE
A
88
−10.443
3.592
2.471
1.00
30.33
A


ATOM
683
CE1
PHE
A
88
−8.463
4.303
4.271
1.00
31.78
A


ATOM
684
CE2
PHE
A
88
−10.786
3.967
3.761
1.00
30.31
A


ATOM
685
CZ
PHE
A
88
−9.798
4.323
4.663
1.00
30.55
A


ATOM
686
C
PHE
A
88
−8.432
.775
1.352
1.00
32.46
A


ATOM
687
O
PHE
A
88
−7.846
.258
2.297
1.00
33.36
A


ATOM
688
N
VAL
A
89
−9.614
.358
.907
1.00
31.48
A


ATOM
689
CA
VAL
A
89
−10.315
−.759
1.518
1.00
31.02
A


ATOM
690
CB
VAL
A
89
−11.000
−.330
2.835
1.00
32.10
A


ATOM
691
CG1
VAL
A
89
−12.350
.336
2.543
1.00
30.78
A


ATOM
692
CG2
VAL
A
89
−11.183
−1.527
3.737
1.00
33.25
A


ATOM
693
C
VAL
A
89
−11.377
−1.316
.563
1.00
30.23
A


ATOM
694
O
VAL
A
89
−12.263
−2.036
.997
1.00
26.54
A


ATOM
695
N
GLU
A
90
−11.284
−.980
−.729
1.00
32.29
A


ATOM
696
CA
GLU
A
90
−12.246
−1.465
−1.729
1.00
32.87
A


ATOM
697
CB
GLU
A
90
−12.260
−.598
−2.989
1.00
35.11
A


ATOM
698
CG
GLU
A
90
−12.132
.884
−2.780
1.00
39.52
A


ATOM
699
CD
GLU
A
90
−10.703
1.296
−2.502
1.00
40.81
A


ATOM
700
OE1
GLU
A
90
−10.391
1.564
−1.326
1.00
44.46
A


ATOM
701
OE2
GLU
A
90
−9.893
1.341
−3.457
1.00
42.34
A


ATOM
702
C
GLU
A
90
−11.945
−2.885
−2.166
1.00
32.49
A


ATOM
703
O
GLU
A
90
−12.815
−3.577
−2.663
1.00
32.58
A


ATOM
704
N
VAL
A
91
−10.696
−3.311
−2.019
1.00
34.49
A


ATOM
705
CA
VAL
A
91
−10.318
−4.673
−2.384
1.00
34.27
A


ATOM
706
CB
VAL
A
91
−9.548
−4.719
−3.734
1.00
34.98
A


ATOM
707
CG1
VAL
A
91
−10.522
−4.597
−4.887
1.00
36.02
A


ATOM
708
CG2
VAL
A
91
−8.528
−3.595
−3.805
1.00
34.63
A


ATOM
709
C
VAL
A
91
−9.450
−5.265
−1.282
1.00
34.25
A


ATOM
710
O
VAL
A
91
−8.662
−4.553
−.650
1.00
36.76
A


ATOM
711
N
PRO
A
92
−9.587
−6.573
−1.022
1.00
32.30
A


ATOM
712
CD
PRO
A
92
−10.508
−7.541
−1.637
1.00
31.68
A


ATOM
713
CA
PRO
A
92
−8.783
−7.210
.027
1.00
31.47
A


ATOM
714
CB
PRO
A
92
−9.387
−8.608
.120
1.00
28.44
A


ATOM
715
CG
PRO
A
92
−9.877
−8.851
−1.263
1.00
30.17
A


ATOM
716
C
PRO
A
92
−7.282
−7.223
−.286
1.00
30.77
A


ATOM
717
O
PRO
A
92
−6.888
−7.231
−1.457
1.00
31.24
A


ATOM
718
N
SER
A
93
−6.450
−7.213
.756
1.00
29.04
A


ATOM
719
CA
SER
A
93
−5.000
−7.212
.560
1.00
28.86
A


ATOM
720
CB
SER
A
93
−4.488
−5.774
.406
1.00
27.99
A


ATOM
721
OG
SER
A
93
−4.609
−5.050
1.615
1.00
24.98
A


ATOM
722
C
SER
A
93
−4.222
−7.900
1.679
1.00
28.57
A


ATOM
723
O
SER
A
93
−2.994
−7.841
1.710
1.00
30.63
A


ATOM
724
N
LEU
A
94
−4.934
−8.567
2.584
1.00
27.50
A


ATOM
725
CA
LEU
A
94
−4.311
−9.263
3.712
1.00
24.56
A


ATOM
726
CB
LEU
A
94
−5.394
−9.949
4.558
1.00
22.81
A


ATOM
727
CG
LEU
A
94
−5.266
−10.012
6.088
1.00
24.83
A


ATOM
728
CD1
LEU
A
94
−5.765
−11.375
6.568
1.00
20.33
A


ATOM
729
CD2
LEU
A
94
−3.824
−9.778
6.536
1.00
21.99
A


ATOM
730
C
LEU
A
94
−3.260
−10.310
3.295
1.00
23.22
A


ATOM
731
O
LEU
A
94
−2.144
−10.312
3.799
1.00
21.73
A


ATOM
732
N
ASP
A
95
−3.631
−11.198
2.381
1.00
22.41
A


ATOM
733
CA
ASP
A
95
−2.733
−12.253
1.923
1.00
24.20
A


ATOM
734
CB
ASP
A
95
−3.446
−13.139
.896
1.00
25.44
A


ATOM
735
CG
ASP
A
95
−4.614
−13.932
1.507
1.00
29.88
A


ATOM
736
OD1
ASP
A
95
−5.294
−14.653
.749
1.00
34.47
A


ATOM
737
OD2
ASP
A
95
−4.851
−13.849
2.737
1.00
29.62
A


ATOM
738
C
ASP
A
95
−1.426
−11.727
1.356
1.00
24.33
A


ATOM
739
O
ASP
A
95
−.349
−12.190
1.731
1.00
24.02
A


ATOM
740
N
ALA
A
96
−1.515
−10.759
.451
1.00
24.12
A


ATOM
741
CA
ALA
A
96
−.318
−10.173
−.124
1.00
23.91
A


ATOM
742
CB
ALA
A
96
−.685
−9.090
−1.113
1.00
24.59
A


ATOM
743
C
ALA
A
96
.550
−9.585
.975
1.00
25.17
A


ATOM
744
O
ALA
A
96
1.776
−9.679
.906
1.00
28.05
A


ATOM
745
N
ARG
A
97
−.076
−8.981
1.987
1.00
22.01
A


ATOM
746
CA
ARG
A
97
.679
−8.381
3.084
1.00
21.90
A


ATOM
747
CB
ARG
A
97
−.208
−7.447
3.911
1.00
20.08
A


ATOM
748
CG
ARG
A
97
−.695
−6.199
3.155
1.00
21.02
A


ATOM
749
CD
ARG
A
97
−1.827
−5.559
3.909
1.00
19.89
A


ATOM
750
NE
ARG
A
97
−2.538
−4.543
3.141
1.00
24.71
A


ATOM
751
CZ
ARG
A
97
−2.095
−3.307
2.938
1.00
23.62
A


ATOM
752
NH1
ARG
A
97
−.931
−2.931
3.443
1.00
23.02
A


ATOM
753
NH2
ARG
A
97
−2.832
−2.440
2.254
1.00
25.63
A


ATOM
754
C
ARG
A
97
1.315
−9.415
4.008
1.00
23.99
A


ATOM
755
O
ARG
A
97
2.438
−9.221
4.495
1.00
25.02
A


ATOM
756
N
GLN
A
98
.603
−10.510
4.255
1.00
22.43
A


ATOM
757
CA
GLN
A
98
1.124
−11.538
5.125
1.00
22.91
A


ATOM
758
CB
GLN
A
98
.081
−12.645
5.340
1.00
21.13
A


ATOM
759
CG
GLN
A
98
−1.261
−12.154
5.938
1.00
20.57
A


ATOM
760
CD
GLN
A
98
−1.161
−11.687
7.391
1.00
19.43
A


ATOM
761
OE1
GLN
A
98
−1.797
−12.254
8.283
1.00
19.15
A


ATOM
762
NE2
GLN
A
98
−.366
−10.654
7.630
1.00
15.68
A


ATOM
763
C
GLN
A
98
2.400
−12.097
4.504
1.00
24.91
A


ATOM
764
O
GLN
A
98
3.366
−12.364
5.218
1.00
24.11
A


ATOM
765
N
ALA
A
99
2.410
−12.238
3.174
1.00
26.86
A


ATOM
766
CA
ALA
A
99
3.580
−12.766
2.455
1.00
28.83
A


ATOM
767
CB
ALA
A
99
3.268
−12.934
.961
1.00
28.35
A


ATOM
768
C
ALA
A
99
4.764
−11.825
2.640
1.00
27.98
A


ATOM
769
O
ALA
A
99
5.875
−12.258
2.955
1.00
29.15
A


ATOM
770
N
MET
A
100
4.515
−10.535
2.438
1.00
27.72
A


ATOM
771
CA
MET
A
100
5.537
−9.507
2.599
1.00
26.42
A


ATOM
772
CB
MET
A
100
4.941
−8.106
2.390
1.00
24.11
A


ATOM
773
CG
MET
A
100
4.634
−7.739
.940
1.00
24.57
A


ATOM
774
SD
MET
A
100
3.735
−6.165
.749
1.00
18.38
A


ATOM
775
CE
MET
A
100
2.752
−6.545
−.586
1.00
21.64
A


ATOM
776
C
MET
A
100
6.096
−9.597
4.005
1.00
25.75
A


ATOM
777
O
MET
A
100
7.305
−9.547
4.203
1.00
24.42
A


ATOM
778
N
LEU
A
101
5.194
−9.742
4.971
1.00
26.33
A


ATOM
779
CA
LEU
A
101
5.540
−9.819
6.388
1.00
27.46
A


ATOM
780
CB
LEU
A
101
4.262
−9.777
7.225
1.00
26.83
A


ATOM
781
CG
LEU
A
101
4.012
−8.510
8.029
1.00
29.59
A


ATOM
782
CD1
LEU
A
101
4.229
−7.300
7.144
1.00
30.34
A


ATOM
783
CD2
LEU
A
101
2.600
−8.536
8.587
1.00
28.87
A


ATOM
784
C
LEU
A
101
6.349
−11.050
6.785
1.00
27.33
A


ATOM
785
O
LEU
A
101
7.377
−10.944
7.457
1.00
28.56
A


ATOM
786
N
ALA
A
102
5.881
−12.218
6.371
1.00
25.00
A


ATOM
787
CA
ALA
A
102
6.560
−13.457
6.716
1.00
27.48
A


ATOM
788
CB
ALA
A
102
5.894
−14.627
5.994
1.00
23.71
A


ATOM
789
C
ALA
A
102
8.056
−13.395
6.381
1.00
28.69
A


ATOM
790
O
ALA
A
102
8.870
−13.987
7.084
1.00
29.73
A


ATOM
791
N
MET
A
103
8.415
−12.661
5.329
1.00
29.35
A


ATOM
792
CA
MET
A
103
9.818
−12.560
4.924
1.00
32.04
A


ATOM
793
CB
MET
A
103
9.941
−12.662
3.401
1.00
34.43
A


ATOM
794
CG
MET
A
103
9.850
−14.076
2.841
1.00
38.55
A


ATOM
795
SD
MET
A
103
11.158
−15.155
3.475
1.00
44.76
A


ATOM
796
CE
MET
A
103
10.276
−16.041
4.747
1.00
39.47
A


ATOM
797
C
MET
A
103
10.568
−11.314
5.387
1.00
31.24
A


ATOM
798
O
MET
A
103
11.695
−11.402
5.864
1.00
31.61
A


ATOM
799
N
GLU
A
104
9.951
−10.153
5.257
1.00
31.59
A


ATOM
800
CA
GLU
A
104
10.626
−8.915
5.630
1.00
31.31
A


ATOM
801
CB
GLU
A
104
9.865
−7.731
5.045
1.00
30.05
A


ATOM
802
CG
GLU
A
104
10.553
−6.406
5.240
1.00
32.44
A


ATOM
803
CD
GLU
A
104
11.995
−6.407
4.762
1.00
33.01
A


ATOM
804
OE1
GLU
A
104
12.390
−7.309
3.989
1.00
33.54
A


ATOM
805
OE2
GLU
A
104
12.735
−5.485
5.158
1.00
33.64
A


ATOM
806
C
GLU
A
104
10.900
−8.671
7.118
1.00
30.88
A


ATOM
807
O
GLU
A
104
11.992
−8.211
7.482
1.00
29.95
A


ATOM
808
N
VAL
A
105
9.926
−8.974
7.976
1.00
30.76
A


ATOM
809
CA
VAL
A
105
10.085
−8.749
9.417
1.00
29.41
A


ATOM
810
CB
VAL
A
105
8.766
−8.996
10.161
1.00
28.39
A


ATOM
811
CG1
VAL
A
105
8.985
−8.867
11.646
1.00
28.65
A


ATOM
812
CG2
VAL
A
105
7.715
−8.003
9.688
1.00
27.81
A


ATOM
813
C
VAL
A
105
11.199
−9.569
10.062
1.00
28.24
A


ATOM
814
O
VAL
A
105
11.977
−9.046
10.858
1.00
28.68
A


ATOM
815
N
PRO
A
106
11.264
−10.877
9.762
1.00
28.43
A


ATOM
816
CD
PRO
A
106
10.166
−11.740
9.283
1.00
28.16
A


ATOM
817
CA
PRO
A
106
12.336
−11.688
10.357
1.00
25.95
A


ATOM
818
CB
PRO
A
106
11.905
−13.120
10.035
1.00
25.33
A


ATOM
819
CG
PRO
A
106
10.418
−13.032
10.058
1.00
27.25
A


ATOM
820
C
PRO
A
106
13.703
−11.332
9.742
1.00
24.31
A


ATOM
821
O
PRO
A
106
14.732
−11.423
10.400
1.00
20.89
A


ATOM
822
N
ARG
A
107
13.695
−10.934
8.473
1.00
24.37
A


ATOM
823
CA
ARG
A
107
14.920
−10.556
7.785
1.00
29.22
A


ATOM
824
CB
ARG
A
107
14.641
−10.194
6.330
1.00
32.72
A


ATOM
825
CG
ARG
A
107
15.902
−9.914
5.510
1.00
36.87
A


ATOM
826
CD
ARG
A
107
15.684
−8.778
4.525
1.00
40.02
A


ATOM
827
NE
ARG
A
107
15.873
−7.473
5.164
1.00
45.13
A


ATOM
828
CZ
ARG
A
107
15.466
−6.313
4.653
1.00
47.15
A


ATOM
829
NH1
ARG
A
107
14.832
−6.282
3.488
1.00
50.56
A


ATOM
830
NH2
ARG
A
107
15.702
−5.181
5.304
1.00
47.09
A


ATOM
831
C
ARG
A
107
15.504
−9.341
8.485
1.00
28.90
A


ATOM
832
O
ARG
A
107
16.661
−9.357
8.908
1.00
29.13
A


ATOM
833
N
LEU
A
108
14.695
−8.289
8.616
1.00
28.98
A


ATOM
834
CA
LEU
A
108
15.142
−7.067
9.280
1.00
28.70
A


ATOM
835
CB
LEU
A
108
14.043
−6.000
9.261
1.00
30.81
A


ATOM
836
CG
LEU
A
108
14.376
−4.716
8.483
1.00
34.16
A


ATOM
837
CD1
LEU
A
108
13.264
−3.690
8.653
1.00
33.94
A


ATOM
838
CD2
LEU
A
108
15.694
−4.138
8.981
1.00
33.48
A


ATOM
839
C
LEU
A
108
15.558
−7.350
10.716
1.00
26.96
A


ATOM
840
O
LEU
A
108
16.597
−6.879
11.170
1.00
27.32
A


ATOM
841
N
ALA
A
109
14.748
−8.124
11.429
1.00
25.77
A


ATOM
842
CA
ALA
A
109
15.052
−8.471
12.816
1.00
24.84
A


ATOM
843
CB
ALA
A
109
13.973
−9.388
13.379
1.00
26.69
A


ATOM
844
C
ALA
A
109
16.409
−9.161
12.914
1.00
25.54
A


ATOM
845
O
ALA
A
109
17.164
−8.924
13.855
1.00
23.26
A


ATOM
846
N
LYS
A
110
16.710
−10.008
11.934
1.00
25.63
A


ATOM
847
CA
LYS
A
110
17.966
−10.745
11.917
1.00
27.86
A


ATOM
848
CB
LYS
A
110
17.955
−11.805
10.811
1.00
29.07
A


ATOM
849
CG
LYS
A
110
19.306
−12.492
10.620
1.00
28.94
A


ATOM
850
CD
LYS
A
110
19.309
−13.385
9.389
1.00
30.99
A


ATOM
851
CE
LYS
A
110
20.569
−14.242
9.321
1.00
31.04
A


ATOM
852
NZ
LYS
A
110
21.804
−13.436
9.126
1.00
31.14
A


ATOM
853
C
LYS
A
110
19.166
−9.831
11.716
1.00
28.05
A


ATOM
854
O
LYS
A
110
20.223
−10.049
12.296
1.00
28.69
A


ATOM
855
N
GLU
A
111
19.011
−8.821
10.873
1.00
27.50
A


ATOM
856
CA
GLU
A
111
20.100
−7.897
10.622
1.00
28.58
A


ATOM
857
CB
GLU
A
111
19.718
−6.956
9.487
1.00
33.09
A


ATOM
858
CG
GLU
A
111
20.666
−5.789
9.264
1.00
37.76
A


ATOM
859
CD
GLU
A
111
20.122
−4.809
8.231
1.00
41.62
A


ATOM
860
OE1
GLU
A
111
19.723
−5.269
7.138
1.00
42.07
A


ATOM
861
OE2
GLU
A
111
20.094
−3.586
8.512
1.00
45.45
A


ATOM
862
C
GLU
A
111
20.407
−7.097
11.886
1.00
28.49
A


ATOM
863
O
GLU
A
111
21.571
−6.841
12.205
1.00
27.38
A


ATOM
864
N
ALA
A
112
19.359
−6.720
12.612
1.00
26.03
A


ATOM
865
CA
ALA
A
112
19.512
−5.944
13.833
1.00
26.94
A


ATOM
866
CB
ALA
A
112
18.143
−5.504
14.354
1.00
28.28
A


ATOM
867
C
ALA
A
112
20.241
−6.715
14.918
1.00
27.67
A


ATOM
868
O
ALA
A
112
21.086
−6.161
15.616
1.00
25.90
A


ATOM
869
N
ASP
A
113
19.918
−7.995
15.066
1.00
28.66
A


ATOM
870
CA
ASP
A
113
20.551
−8.775
16.109
1.00
29.69
A


ATOM
871
CB
ASP
A
113
19.677
−9.961
16.490
1.00
36.80
A


ATOM
872
CG
ASP
A
113
18.955
−10.548
15.311
1.00
42.93
A


ATOM
873
OD1
ASP
A
113
19.629
−10.976
14.352
1.00
47.19
A


ATOM
874
OD2
ASP
A
113
17.707
−10.583
15.346
1.00
49.00
A


ATOM
875
C
ASP
A
113
21.951
−9.231
15.791
1.00
27.88
A


ATOM
876
O
ASP
A
113
22.744
−9.424
16.696
1.00
29.10
A


ATOM
877
N
GLU
A
114
22.270
−9.411
14.520
1.00
27.42
A


ATOM
878
CA
GLU
A
114
23.629
−9.802
14.181
1.00
29.07
A


ATOM
879
CB
GLU
A
114
23.759
−10.072
12.679
1.00
32.21
A


ATOM
880
CG
GLU
A
114
23.033
−11.347
12.216
1.00
36.51
A


ATOM
881
CD
GLU
A
114
23.752
−12.637
12.619
1.00
37.69
A


ATOM
882
OE1
GLU
A
114
24.350
−12.673
13.715
1.00
38.62
A


ATOM
883
OE2
GLU
A
114
23.710
−13.621
11.842
1.00
39.78
A


ATOM
884
C
GLU
A
114
24.514
−8.632
14.616
1.00
28.69
A


ATOM
885
O
GLU
A
114
25.608
−8.834
15.156
1.00
26.64
A


ATOM
886
N
LYS
A
115
24.030
−7.409
14.394
1.00
28.82
A


ATOM
887
CA
LYS
A
115
24.757
−6.213
14.815
1.00
29.61
A


ATOM
888
CB
LYS
A
115
24.007
−4.929
14.448
1.00
31.35
A


ATOM
889
CG
LYS
A
115
24.182
−4.438
13.028
1.00
33.87
A


ATOM
890
CD
LYS
A
115
23.587
−3.040
12.893
1.00
37.24
A


ATOM
891
CE
LYS
A
115
23.869
−2.444
11.530
1.00
38.63
A


ATOM
892
NZ
LYS
A
115
23.370
−3.328
10.448
1.00
40.84
A


ATOM
893
C
LYS
A
115
24.863
−6.276
16.324
1.00
28.63
A


ATOM
894
O
LYS
A
115
25.950
−6.214
16.688
1.00
29.75
A


ATOM
895
N
ALA
A
116
23.711
−6.412
16.971
1.00
28.40
A


ATOM
896
CA
ALA
A
116
23.637
−6.497
18.427
1.00
28.89
A


ATOM
897
CB
ALA
A
116
22.187
−6.743
18.864
1.00
29.26
A


ATOM
898
C
ALA
A
116
24.538
−7.605
18.976
1.00
28.49
A


ATOM
899
O
ALA
A
116
25.285
−7.391
19.931
1.00
29.43
A


ATOM
900
N
ILE
A
117
24.462
−8.782
18.374
1.00
28.53
A


ATOM
901
CA
ILE
A
117
25.265
−9.910
18.829
1.00
31.21
A


ATOM
902
CB
ILE
A
117
25.027
−11.179
17.971
1.00
29.88
A


ATOM
903
CG2
ILE
A
117
25.823
−12.339
18.538
1.00
28.55
A


ATOM
904
CG1
ILE
A
117
23.549
−11.577
17.997
1.00
32.55
A


ATOM
905
CD1
ILE
A
117
23.062
−12.008
19.351
1.00
33.54
A


ATOM
906
C
ILE
A
117
26.738
−9.563
18.766
1.00
32.35
A


ATOM
907
O
ILE
A
117
27.474
−9.769
19.732
1.00
30.97
A


ATOM
908
N
GLN
A
118
27.152
−9.024
17.625
1.00
34.54
A


ATOM
909
CA
GLN
A
118
28.544
−8.646
17.402
1.00
37.18
A


ATOM
910
CB
GLN
A
118
28.690
−7.981
16.039
1.00
40.03
A


ATOM
911
CG
GLN
A
118
30.113
−7.648
15.668
1.00
44.57
A


ATOM
912
CD
GLN
A
118
30.200
−7.018
14.300
1.00
47.69
A


ATOM
913
OE1
GLN
A
118
29.776
−7.611
13.302
1.00
49.39
A


ATOM
914
NE2
GLN
A
118
30.748
−5.807
14.239
1.00
49.45
A


ATOM
915
C
GLN
A
118
29.112
−7.727
18.478
1.00
37.04
A


ATOM
916
O
GLN
A
118
30.203
−7.977
18.988
1.00
37.17
A


ATOM
917
N
GLU
A
119
28.380
−6.666
18.820
1.00
36.89
A


ATOM
918
CA
GLU
A
119
28.828
−5.715
19.846
1.00
36.40
A


ATOM
919
CB
GLU
A
119
27.773
−4.638
20.082
1.00
36.37
A


ATOM
920
CG
GLU
A
119
28.216
−3.559
21.045
1.00
36.77
A


ATOM
921
CD
GLU
A
119
27.063
−2.710
21.534
1.00
38.45
A


ATOM
922
OE1
GLU
A
119
26.097
−2.525
20.768
1.00
38.88
A


ATOM
923
OE2
GLU
A
119
27.132
−2.213
22.677
1.00
38.52
A


ATOM
924
C
GLU
A
119
29.071
−6.444
21.161
1.00
35.77
A


ATOM
925
O
GLU
A
119
30.134
−6.340
21.778
1.00
36.48
A


ATOM
926
N
TRP
A
120
28.054
−7.177
21.580
1.00
35.05
A


ATOM
927
CA
TRP
A
120
28.097
−7.950
22.805
1.00
34.32
A


ATOM
928
CB
TRP
A
120
26.802
−8.747
22.903
1.00
31.27
A


ATOM
929
CG
TRP
A
120
26.695
−9.670
24.050
1.00
29.64
A


ATOM
930
CD2
TRP
A
120
26.228
−11.019
24.001
1.00
28.18
A


ATOM
931
CE2
TRP
A
120
26.168
−11.486
25.328
1.00
28.95
A


ATOM
932
CE3
TRP
A
120
25.849
−11.879
22.960
1.00
28.14
A


ATOM
933
CD1
TRP
A
120
26.903
−9.380
25.365
1.00
27.98
A


ATOM
934
NE1
TRP
A
120
26.583
−10.464
26.141
1.00
28.05
A


ATOM
935
CZ2
TRP
A
120
25.742
−12.788
25.647
1.00
30.03
A


ATOM
936
CZ3
TRP
A
120
25.425
−13.172
23.278
1.00
30.61
A


ATOM
937
CH2
TRP
A
120
25.378
−13.612
24.611
1.00
27.55
A


ATOM
938
C
TRP
A
120
29.309
−8.863
22.735
1.00
34.10
A


ATOM
939
O
TRP
A
120
29.861
−9.269
23.757
1.00
36.05
A


ATOM
940
N
GLY
A
121
29.711
−9.178
21.510
1.00
34.61
A


ATOM
941
CA
GLY
A
121
30.864
−10.028
21.283
1.00
35.14
A


ATOM
942
C
GLY
A
121
30.900
−11.386
21.961
1.00
35.69
A


ATOM
943
O
GLY
A
121
31.983
−11.912
22.194
1.00
36.76
A


ATOM
944
N
GLN
A
122
29.743
−11.960
22.273
1.00
35.13
A


ATOM
945
CA
GLN
A
122
29.683
−13.276
22.910
1.00
35.20
A


ATOM
946
CB
GLN
A
122
29.897
−13.209
24.224
1.00
35.80
A


ATOM
947
CG
GLN
A
122
29.639
−12.555
25.362
1.00
38.25
A


ATOM
948
CD
GLN
A
122
30.903
−13.313
25.745
1.00
40.71
A


ATOM
949
OE1
GLN
A
122
30.849
−14.458
26.210
1.00
41.52
A


ATOM
950
NE2
GLN
A
122
32.050
−12.678
25.549
1.00
40.42
A


ATOM
951
C
GLN
A
122
29.022
−14.291
21.977
1.00
34.64
A


ATOM
952
O
GLN
A
122
28.359
−13.922
21.009
1.00
34.92
A


ATOM
953
N
SER
A
123
29.205
−15.571
22.268
1.00
33.07
A


ATOM
954
CA
SER
A
123
28.622
−16.626
21.449
1.00
33.33
A


ATOM
955
CB
SER
A
123
28.974
−17.989
22.045
1.00
31.42
A


ATOM
956
OG
SER
A
123
28.341
−19.041
21.349
1.00
29.57
A


ATOM
957
C
SER
A
123
27.103
−16.487
21.352
1.00
34.17
A


ATOM
958
O
SER
A
123
26.471
−15.885
22.220
1.00
35.47
A


ATOM
959
N
LYS
A
124
26.529
−17.018
20.276
1.00
35.18
A


ATOM
960
CA
LYS
A
124
25.083
−16.992
20.093
1.00
33.65
A


ATOM
961
CB
LYS
A
124
24.689
−17.401
18.674
1.00
33.98
A


ATOM
962
CG
LYS
A
124
24.815
−16.325
17.623
1.00
36.96
A


ATOM
963
CD
LYS
A
124
24.322
−16.850
16.280
1.00
37.21
A


ATOM
964
CE
LYS
A
124
24.557
−15.840
15.171
1.00
40.53
A


ATOM
965
NZ
LYS
A
124
24.053
−14.487
15.527
1.00
40.81
A


ATOM
966
C
LYS
A
124
24.527
−18.021
21.060
1.00
32.99
A


ATOM
967
O
LYS
A
124
23.502
−17.791
21.707
1.00
31.91
A


ATOM
968
N
SER
A
125
25.224
−19.154
21.157
1.00
30.09
A


ATOM
969
CA
SER
A
125
24.813
−20.243
22.037
1.00
31.14
A


ATOM
970
CB
SER
A
125
25.904
−21.328
22.104
1.00
30.57
A


ATOM
971
OG
SER
A
125
27.056
−20.885
22.806
1.00
29.74
A


ATOM
972
C
SER
A
125
24.503
−19.733
23.438
1.00
29.64
A


ATOM
973
O
SER
A
125
23.612
−20.245
24.109
1.00
30.79
A


ATOM
974
N
GLY
A
126
25.236
−18.712
23.867
1.00
29.37
A


ATOM
975
CA
GLY
A
126
25.018
−18.154
25.192
1.00
29.53
A


ATOM
976
C
GLY
A
126
23.653
−17.512
25.375
1.00
27.71
A


ATOM
977
O
GLY
A
126
23.261
−17.163
26.489
1.00
25.74
A


ATOM
978
N
ILE
A
127
22.938
−17.344
24.268
1.00
26.99
A


ATOM
979
CA
ILE
A
127
21.605
−16.751
24.287
1.00
25.17
A


ATOM
980
CB
ILE
A
127
21.237
−16.221
22.886
1.00
22.05
A


ATOM
981
CG2
ILE
A
127
19.752
−15.896
22.811
1.00
22.05
A


ATOM
982
CG1
ILE
A
127
22.106
−15.001
22.577
1.00
18.84
A


ATOM
983
CD1
ILE
A
127
21.862
−14.406
21.238
1.00
17.66
A


ATOM
984
C
ILE
A
127
20.610
−17.810
24.754
1.00
24.70
A


ATOM
985
O
ILE
A
127
20.363
−18.790
24.060
1.00
26.26
A


ATOM
986
N
THR
A
128
20.047
−17.594
25.939
1.00
25.26
A


ATOM
987
CA
THR
A
128
19.101
−18.526
26.555
1.00
25.26
A


ATOM
988
CB
THR
A
128
19.418
−18.698
28.053
1.00
27.22
A


ATOM
989
OG1
THR
A
128
19.208
−17.446
28.731
1.00
27.55
A


ATOM
990
CG2
THR
A
128
20.866
−19.134
28.245
1.00
27.17
A


ATOM
991
C
THR
A
128
17.646
−18.090
26.454
1.00
25.40
A


ATOM
992
O
THR
A
128
16.730
−18.854
26.798
1.00
24.68
A


ATOM
993
N
HIS
A
129
17.435
−16.857
26.007
1.00
22.77
A


ATOM
994
CA
HIS
A
129
16.097
−16.303
25.892
1.00
20.64
A


ATOM
995
CB
HIS
A
129
15.762
−15.456
27.122
1.00
18.09
A


ATOM
996
CG
HIS
A
129
15.565
−16.245
28.378
1.00
21.09
A


ATOM
997
CD2
HIS
A
129
14.433
−16.640
29.013
1.00
19.20
A


ATOM
998
ND1
HIS
A
129
16.615
−16.724
29.130
1.00
18.25
A


ATOM
999
CE1
HIS
A
129
16.137
−17.379
30.175
1.00
18.16
A


ATOM
1000
NE2
HIS
A
129
14.817
−17.342
30.128
1.00
17.69
A


ATOM
1001
C
HIS
A
129
15.975
−15.408
24.673
1.00
22.13
A


ATOM
1002
O
HIS
A
129
16.953
−14.800
24.243
1.00
21.06
A


ATOM
1003
N
LEU
A
130
14.762
−15.336
24.129
1.00
22.34
A


ATOM
1004
CA
LEU
A
130
14.463
−14.477
22.993
1.00
22.64
A


ATOM
1005
CB
LEU
A
130
14.471
−15.241
21.672
1.00
24.24
A


ATOM
1006
CG
LEU
A
130
13.867
−14.417
20.522
1.00
22.91
A


ATOM
1007
CD1
LEU
A
130
14.786
−13.246
20.200
1.00
24.49
A


ATOM
1008
CD2
LEU
A
130
13.647
−15.289
19.303
1.00
21.22
A


ATOM
1009
C
LEU
A
130
13.071
−13.894
23.199
1.00
24.28
A


ATOM
1010
O
LEU
A
130
12.117
−14.611
23.505
1.00
22.97
A


ATOM
1011
N
ILE
A
131
12.978
−12.580
23.051
1.00
23.85
A


ATOM
1012
CA
ILE
A
131
11.718
−11.867
23.177
1.00
22.17
A


ATOM
1013
CB
ILE
A
131
11.752
−10.834
24.320
1.00
19.17
A


ATOM
1014
CG2
ILE
A
131
10.523
−9.914
24.219
1.00
17.23
A


ATOM
1015
CG1
ILE
A
131
11.822
−11.557
25.666
1.00
15.59
A


ATOM
1016
CD1
ILE
A
131
11.885
−10.632
26.867
1.00
16.20
A


ATOM
1017
C
ILE
A
131
11.572
−11.139
21.856
1.00
22.74
A


ATOM
1018
O
ILE
A
131
12.378
−10.260
21.537
1.00
24.68
A


ATOM
1019
N
PHE
A
132
10.571
−11.522
21.075
1.00
21.87
A


ATOM
1020
CA
PHE
A
132
10.364
−10.896
19.788
1.00
22.84
A


ATOM
1021
CB
PHE
A
132
10.407
−11.935
18.658
1.00
25.22
A


ATOM
1022
CG
PHE
A
132
10.347
−11.327
17.282
1.00
26.03
A


ATOM
1023
CD1
PHE
A
132
9.126
−11.002
16.699
1.00
27.91
A


ATOM
1024
CD2
PHE
A
132
11.516
−11.014
16.596
1.00
26.87
A


ATOM
1025
CE1
PHE
A
132
9.074
−10.370
15.456
1.00
27.98
A


ATOM
1026
CE2
PHE
A
132
11.469
−10.383
15.356
1.00
26.12
A


ATOM
1027
CZ
PHE
A
132
10.249
−10.061
14.787
1.00
27.33
A


ATOM
1028
C
PHE
A
132
9.054
−10.142
19.757
1.00
23.78
A


ATOM
1029
O
PHE
A
132
8.020
−10.636
20.235
1.00
25.01
A


ATOM
1030
N
CYS
A
133
9.108
−8.948
19.176
1.00
21.79
A


ATOM
1031
CA
CYS
A
133
7.951
−8.082
19.076
1.00
22.75
A


ATOM
1032
CB
CYS
A
133
8.129
−6.891
20.026
1.00
25.53
A


ATOM
1033
SG
CYS
A
133
6.991
−5.537
19.732
1.00
27.54
A


ATOM
1034
C
CYS
A
133
7.676
−7.562
17.669
1.00
21.50
A


ATOM
1035
O
CYS
A
133
8.592
−7.180
16.940
1.00
22.97
A


ATOM
1036
N
SER
A
134
6.399
−7.533
17.309
1.00
21.18
A


ATOM
1037
CA
SER
A
134
5.954
−7.031
16.009
1.00
22.43
A


ATOM
1038
CB
SER
A
134
6.173
−8.095
14.925
1.00
22.07
A


ATOM
1039
OG
SER
A
134
6.351
−7.508
13.641
1.00
21.45
A


ATOM
1040
C
SER
A
134
4.464
−6.733
16.168
1.00
24.43
A


ATOM
1041
O
SER
A
134
3.756
−7.503
16.838
1.00
24.55
A


ATOM
1042
N
THR
A
135
3.977
−5.637
15.580
1.00
24.20
A


ATOM
1043
CA
THR
A
135
2.555
−5.313
15.716
1.00
26.34
A


ATOM
1044
CB
THR
A
135
2.107
−4.107
14.846
1.00
26.54
A


ATOM
1045
OG1
THR
A
135
1.786
−4.562
13.530
1.00
28.93
A


ATOM
1046
CG2
THR
A
135
3.199
−3.045
14.786
1.00
25.74
A


ATOM
1047
C
THR
A
135
1.712
−6.537
15.349
1.00
25.69
A


ATOM
1048
O
THR
A
135
.660
−6.749
15.929
1.00
26.52
A


ATOM
1049
N
THR
A
136
2.168
−7.329
14.379
1.00
25.88
A


ATOM
1050
CA
THR
A
136
1.479
−8.567
14.007
1.00
25.55
A


ATOM
1051
CB
THR
A
136
.460
−8.402
12.834
1.00
24.45
A


ATOM
1052
OG1
THR
A
136
1.149
−8.006
11.648
1.00
22.72
A


ATOM
1053
CG2
THR
A
136
−.625
−7.396
13.173
1.00
25.44
A


ATOM
1054
C
THR
A
136
2.497
−9.623
13.558
1.00
25.00
A


ATOM
1055
O
THR
A
136
3.692
−9.343
13.416
1.00
23.29
A


ATOM
1056
N
THR
A
137
2.004
−10.839
13.360
1.00
24.15
A


ATOM
1057
CA
THR
A
137
2.808
−11.957
12.875
1.00
24.60
A


ATOM
1058
CB
THR
A
137
3.378
−12.819
14.045
1.00
23.38
A


ATOM
1059
OG1
THR
A
137
4.548
−13.503
13.580
1.00
25.80
A


ATOM
1060
CG2
THR
A
137
2.370
−13.837
14.543
1.00
20.20
A


ATOM
1061
C
THR
A
137
1.814
−12.724
11.997
1.00
23.38
A


ATOM
1062
O
THR
A
137
.676
−12.959
12.393
1.00
21.68
A


ATOM
1063
N
PRO
A
138
2.225
−13.099
10.781
1.00
24.14
A


ATOM
1064
CD
PRO
A
138
3.545
−12.846
10.175
1.00
23.44
A


ATOM
1065
CA
PRO
A
138
1.347
−13.816
9.851
1.00
24.04
A


ATOM
1066
CB
PRO
A
138
2.069
−13.657
8.523
1.00
24.17
A


ATOM
1067
CG
PRO
A
138
3.504
−13.700
8.930
1.00
23.06
A


ATOM
1068
C
PRO
A
138
.927
−15.259
10.100
1.00
24.49
A


ATOM
1069
O
PRO
A
138
−.168
−15.662
9.699
1.00
24.01
A


ATOM
1070
N
ASP
A
139
1.765
−16.043
10.757
1.00
24.32
A


ATOM
1071
CA
ASP
A
139
1.427
−17.443
10.959
1.00
26.63
A


ATOM
1072
CB
ASP
A
139
2.227
−18.311
9.970
1.00
30.30
A


ATOM
1073
CG
ASP
A
139
2.354
−17.683
8.582
1.00
34.13
A


ATOM
1074
OD1
ASP
A
139
3.341
−17.999
7.875
1.00
38.40
A


ATOM
1075
OD2
ASP
A
139
1.474
−16.893
8.179
1.00
34.14
A


ATOM
1076
C
ASP
A
139
1.741
−17.938
12.358
1.00
26.12
A


ATOM
1077
O
ASP
A
139
2.041
−17.175
13.270
1.00
25.57
A


ATOM
1078
N
LEU
A
140
1.654
−19.253
12.499
1.00
27.76
A


ATOM
1079
CA
LEU
A
140
2.002
−19.949
13.731
1.00
26.83
A


ATOM
1080
CB
LEU
A
140
.778
−20.555
14.399
1.00
28.40
A


ATOM
1081
CG
LEU
A
140
−.177
−19.538
15.008
1.00
30.52
A


ATOM
1082
CD1
LEU
A
140
−.928
−18.799
13.904
1.00
32.48
A


ATOM
1083
CD2
LEU
A
140
−1.132
−20.254
15.923
1.00
30.95
A


ATOM
1084
C
LEU
A
140
2.929
−21.052
13.244
1.00
27.18
A


ATOM
1085
O
LEU
A
140
2.548
−21.853
12.388
1.00
28.82
A


ATOM
1086
N
PRO
A
141
4.160
−21.104
13.766
1.00
25.78
A


ATOM
1087
CD
PRO
A
141
5.159
−22.037
13.216
1.00
25.32
A


ATOM
1088
CA
PRO
A
141
4.766
−20.228
14.775
1.00
24.99
A


ATOM
1089
CB
PRO
A
141
6.107
−20.898
15.025
1.00
26.03
A


ATOM
1090
CG
PRO
A
141
6.459
−21.422
13.661
1.00
26.03
A


ATOM
1091
C
PRO
A
141
4.924
−18.763
14.344
1.00
24.56
A


ATOM
1092
O
PRO
A
141
4.825
−18.427
13.162
1.00
23.75
A


ATOM
1093
N
GLY
A
142
5.177
−17.894
15.313
1.00
24.62
A


ATOM
1094
CA
GLY
A
142
5.349
−16.490
15.009
1.00
23.80
A


ATOM
1095
C
GLY
A
142
6.792
−16.180
14.679
1.00
26.14
A


ATOM
1096
O
GLY
A
142
7.660
−17.059
14.729
1.00
25.21
A


ATOM
1097
N
ALA
A
143
7.041
−14.917
14.352
1.00
25.92
A


ATOM
1098
CA
ALA
A
143
8.363
−14.426
13.999
1.00
26.94
A


ATOM
1099
CB
ALA
A
143
8.299
−12.909
13.760
1.00
25.13
A


ATOM
1100
C
ALA
A
143
9.471
−14.756
15.008
1.00
26.98
A


ATOM
1101
O
ALA
A
143
10.650
−14.690
14.665
1.00
29.10
A


ATOM
1102
N
ASP
A
144
9.112
−15.085
16.248
1.00
27.97
A


ATOM
1103
CA
ASP
A
144
10.130
−15.435
17.241
1.00
28.11
A


ATOM
1104
CB
ASP
A
144
9.513
−15.650
18.643
1.00
28.84
A


ATOM
1105
CG
ASP
A
144
8.364
−16.668
18.662
1.00
29.51
A


ATOM
1106
OD1
ASP
A
144
7.340
−16.426
17.994
1.00
27.31
A


ATOM
1107
OD2
ASP
A
144
8.480
−17.703
19.364
1.00
30.81
A


ATOM
1108
C
ASP
A
144
10.862
−16.697
16.784
1.00
27.99
A


ATOM
1109
O
ASP
A
144
12.100
−16.747
16.763
1.00
26.30
A


ATOM
1110
N
PHE
A
145
10.086
−17.711
16.406
1.00
26.99
A


ATOM
1111
CA
PHE
A
145
10.648
−18.968
15.930
1.00
27.15
A


ATOM
1112
CB
PHE
A
145
9.536
−19.933
15.544
1.00
27.87
A


ATOM
1113
CG
PHE
A
145
10.027
−21.173
14.858
1.00
28.08
A


ATOM
1114
CD1
PHE
A
145
10.427
−22.280
15.594
1.00
29.08
A


ATOM
1115
CD2
PHE
A
145
10.108
−21.226
13.475
1.00
27.17
A


ATOM
1116
CE1
PHE
A
145
10.902
−23.430
14.960
1.00
28.55
A


ATOM
1117
CE2
PHE
A
145
10.580
−22.362
12.828
1.00
29.72
A


ATOM
1118
CZ
PHE
A
145
10.979
−23.472
13.575
1.00
27.75
A


ATOM
1119
C
PHE
A
145
11.520
−18.711
14.710
1.00
27.78
A


ATOM
1120
O
PHE
A
145
12.690
−19.107
14.663
1.00
25.37
A


ATOM
1121
N
GLU
A
146
10.937
−18.041
13.723
1.00
28.13
A


ATOM
1122
CA
GLU
A
146
11.652
−17.746
12.504
1.00
28.43
A


ATOM
1123
CB
GLU
A
146
10.763
−16.982
11.538
1.00
32.67
A


ATOM
1124
CG
GLU
A
146
10.552
−17.733
10.237
1.00
39.15
A


ATOM
1125
CD
GLU
A
146
10.033
−19.152
10.462
1.00
42.85
A


ATOM
1126
OE1
GLU
A
146
8.847
−19.299
10.847
1.00
43.22
A


ATOM
1127
OE2
GLU
A
146
10.816
−20.113
10.259
1.00
43.47
A


ATOM
1128
C
GLU
A
146
12.932
−16.983
12.730
1.00
27.87
A


ATOM
1129
O
GLU
A
146
13.941
−17.282
12.104
1.00
28.61
A


ATOM
1130
N
VAL
A
147
12.900
−16.004
13.626
1.00
26.97
A


ATOM
1131
CA
VAL
A
147
14.087
−15.210
13.902
1.00
27.33
A


ATOM
1132
CB
VAL
A
147
13.757
−14.038
14.848
1.00
28.53
A


ATOM
1133
CG1
VAL
A
147
15.024
−13.382
15.340
1.00
27.78
A


ATOM
1134
CG2
VAL
A
147
12.912
−13.009
14.102
1.00
28.86
A


ATOM
1135
C
VAL
A
147
15.154
−16.108
14.509
1.00
27.76
A


ATOM
1136
O
VAL
A
147
16.338
−15.976
14.199
1.00
26.81
A


ATOM
1137
N
ALA
A
148
14.721
−17.030
15.365
1.00
27.35
A


ATOM
1138
CA
ALA
A
148
15.630
−17.973
16.001
1.00
27.81
A


ATOM
1139
CB
ALA
A
148
14.878
−18.841
17.011
1.00
26.38
A


ATOM
1140
C
ALA
A
148
16.252
−18.849
14.923
1.00
28.55
A


ATOM
1141
O
ALA
A
148
17.464
−19.061
14.895
1.00
27.16
A


ATOM
1142
N
LYS
A
149
15.409
−19.344
14.028
1.00
28.27
A


ATOM
1143
CA
LYS
A
149
15.865
−20.192
12.940
1.00
30.54
A


ATOM
1144
CB
LYS
A
149
14.655
−20.672
12.125
1.00
30.34
A


ATOM
1145
CG
LYS
A
149
14.879
−21.959
11.344
1.00
33.21
A


ATOM
1146
CD
LYS
A
149
15.675
−21.726
10.077
1.00
35.22
A


ATOM
1147
CE
LYS
A
149
14.855
−20.955
9.054
1.00
36.29
A


ATOM
1148
NZ
LYS
A
149
15.631
−20.646
7.821
1.00
34.92
A


ATOM
1149
C
LYS
A
149
16.885
−19.453
12.052
1.00
31.84
A


ATOM
1150
O
LYS
A
149
17.946
−20.000
11.752
1.00
33.57
A


ATOM
1151
N
LEU
A
150
16.588
−18.223
11.638
1.00
30.97
A


ATOM
1152
CA
LEU
A
150
17.540
−17.480
10.804
1.00
31.42
A


ATOM
1153
CB
LEU
A
150
16.949
−16.151
10.311
1.00
33.16
A


ATOM
1154
CG
LEU
A
150
16.023
−16.098
9.091
1.00
34.92
A


ATOM
1155
CD1
LEU
A
150
14.652
−16.632
9.434
1.00
36.29
A


ATOM
1156
CD2
LEU
A
150
15.904
−14.657
8.623
1.00
36.72
A


ATOM
1157
C
LEU
A
150
18.811
−17.166
11.578
1.00
30.60
A


ATOM
1158
O
LEU
A
150
19.903
−17.155
11.020
1.00
31.87
A


ATOM
1159
N
LEU
A
151
18.665
−16.893
12.866
1.00
29.87
A


ATOM
1160
CA
LEU
A
151
19.809
−16.557
13.698
1.00
29.41
A


ATOM
1161
CB
LEU
A
151
19.340
−15.867
14.980
1.00
27.66
A


ATOM
1162
CG
LEU
A
151
19.013
−14.378
14.886
1.00
29.11
A


ATOM
1163
CD1
LEU
A
151
18.489
−13.880
16.225
1.00
26.30
A


ATOM
1164
CD2
LEU
A
151
20.272
−13.620
14.468
1.00
28.44
A


ATOM
1165
C
LEU
A
151
20.669
−17.763
14.061
1.00
29.68
A


ATOM
1166
O
LEU
A
151
21.799
−17.619
14.539
1.00
29.22
A


ATOM
1167
N
GLY
A
152
20.140
−18.955
13.826
1.00
29.85
A


ATOM
1168
CA
GLY
A
152
20.886
−20.145
14.176
1.00
29.71
A


ATOM
1169
C
GLY
A
152
21.021
−20.159
15.687
1.00
29.47
A


ATOM
1170
O
GLY
A
152
22.076
−20.485
16.231
1.00
31.09
A


ATOM
1171
N
LEU
A
153
19.950
−19.766
16.367
1.00
26.59
A


ATOM
1172
CA
LEU
A
153
19.947
−19.743
17.814
1.00
24.43
A


ATOM
1173
CB
LEU
A
153
18.747
−18.947
18.326
1.00
25.57
A


ATOM
1174
CG
LEU
A
153
19.004
−17.578
18.956
1.00
26.97
A


ATOM
1175
CD1
LEU
A
153
19.894
−16.771
18.055
1.00
26.84
A


ATOM
1176
CD2
LEU
A
153
17.682
−16.865
19.210
1.00
25.05
A


ATOM
1177
C
LEU
A
153
19.844
−21.190
18.241
1.00
23.58
A


ATOM
1178
O
LEU
A
153
19.525
−22.051
17.426
1.00
24.50
A


ATOM
1179
N
HIS
A
154
20.124
−21.458
19.512
1.00
25.47
A


ATOM
1180
CA
HIS
A
154
20.063
−22.818
20.063
1.00
23.90
A


ATOM
1181
CB
HIS
A
154
20.640
−22.827
21.488
1.00
22.82
A


ATOM
1182
CG
HIS
A
154
20.888
−24.199
22.031
1.00
24.68
A


ATOM
1183
CD2
HIS
A
154
20.084
−25.041
22.723
1.00
26.57
A


ATOM
1184
ND1
HIS
A
154
22.080
−24.869
21.855
1.00
25.52
A


ATOM
1185
CE1
HIS
A
154
22.001
−26.064
22.414
1.00
26.84
A


ATOM
1186
NE2
HIS
A
154
20.800
−26.194
22.949
1.00
28.28
A


ATOM
1187
C
HIS
A
154
18.612
−23.318
20.081
1.00
23.62
A


ATOM
1188
O
HIS
A
154
17.693
−22.576
20.407
1.00
21.68
A


ATOM
1189
N
PRO
A
155
18.391
−24.590
19.740
1.00
24.80
A


ATOM
1190
CD
PRO
A
155
19.359
−25.673
19.505
1.00
25.17
A


ATOM
1191
CA
PRO
A
155
17.023
−25.109
19.739
1.00
25.08
A


ATOM
1192
CB
PRO
A
155
17.215
−26.578
19.371
1.00
25.18
A


ATOM
1193
CG
PRO
A
155
18.576
−26.880
19.928
1.00
27.56
A


ATOM
1194
C
PRO
A
155
16.277
−24.932
21.058
1.00
26.29
A


ATOM
1195
O
PRO
A
155
15.053
−24.979
21.088
1.00
26.00
A


ATOM
1196
N
SER
A
156
17.016
−24.729
22.143
1.00
25.49
A


ATOM
1197
CA
SER
A
156
16.392
−24.565
23.452
1.00
23.23
A


ATOM
1198
CB
SER
A
156
17.114
−25.424
24.500
1.00
24.30
A


ATOM
1199
OG
SER
A
156
16.916
−26.801
24.255
1.00
24.44
A


ATOM
1200
C
SER
A
156
16.314
−23.133
23.956
1.00
21.04
A


ATOM
1201
O
SER
A
156
16.185
−22.911
25.147
1.00
19.96
A


ATOM
1202
N
VAL
A
157
16.429
−22.161
23.061
1.00
21.07
A


ATOM
1203
CA
VAL
A
157
16.314
−20.779
23.481
1.00
20.46
A


ATOM
1204
CB
VAL
A
157
16.499
−19.753
22.308
1.00
18.81
A


ATOM
1205
CG1
VAL
A
157
16.244
−18.331
22.828
1.00
19.92
A


ATOM
1206
CG2
VAL
A
157
17.899
−19.826
21.737
1.00
22.14
A


ATOM
1207
C
VAL
A
157
14.875
−20.662
23.963
1.00
21.14
A


ATOM
1208
O
VAL
A
157
13.962
−21.152
23.312
1.00
19.78
A


ATOM
1209
N
LYS
A
158
14.673
−20.035
25.110
1.00
20.85
A


ATOM
1210
CA
LYS
A
158
13.328
−19.855
25.622
1.00
22.35
A


ATOM
1211
CB
LYS
A
158
13.373
−19.711
27.141
1.00
23.13
A


ATOM
1212
CG
LYS
A
158
13.667
−21.030
27.858
1.00
25.41
A


ATOM
1213
CD
LYS
A
158
13.697
−20.828
29.357
1.00
24.19
A


ATOM
1214
CE
LYS
A
158
15.117
−20.708
29.873
1.00
26.45
A


ATOM
1215
NZ
LYS
A
158
15.823
−22.024
29.939
1.00
25.92
A


ATOM
1216
C
LYS
A
158
12.798
−18.596
24.939
1.00
23.09
A


ATOM
1217
O
LYS
A
158
13.164
−17.480
25.291
1.00
21.21
A


ATOM
1218
N
ARG
A
159
11.929
−18.799
23.956
1.00
24.01
A


ATOM
1219
CA
ARG
A
159
11.380
−17.710
23.155
1.00
24.63
A


ATOM
1220
CB
ARG
A
159
11.358
−18.128
21.676
1.00
25.38
A


ATOM
1221
CG
ARG
A
159
12.174
−19.388
21.376
1.00
27.28
A


ATOM
1222
CD
ARG
A
159
12.021
−19.830
19.935
1.00
29.70
A


ATOM
1223
NE
ARG
A
159
10.669
−20.293
19.622
1.00
29.95
A


ATOM
1224
CZ
ARG
A
159
10.282
−21.565
19.619
1.00
29.82
A


ATOM
1225
NH1
ARG
A
159
11.139
−22.533
19.916
1.00
30.94
A


ATOM
1226
NH2
ARG
A
159
9.028
−21.868
19.313
1.00
33.57
A


ATOM
1227
C
ARG
A
159
9.982
−17.289
23.561
1.00
23.52
A


ATOM
1228
O
ARG
A
159
9.217
−18.080
24.097
1.00
25.02
A


ATOM
1229
N
VAL
A
160
9.665
−16.024
23.311
1.00
22.32
A


ATOM
1230
CA
VAL
A
160
8.345
−15.474
23.595
1.00
21.08
A


ATOM
1231
CB
VAL
A
160
8.244
−14.796
24.984
1.00
22.06
A


ATOM
1232
CG1
VAL
A
160
9.252
−13.676
25.105
1.00
21.67
A


ATOM
1233
CG2
VAL
A
160
6.838
−14.249
25.175
1.00
19.10
A


ATOM
1234
C
VAL
A
160
8.035
−14.433
22.540
1.00
21.72
A


ATOM
1235
O
VAL
A
160
8.852
−13.562
22.231
1.00
20.95
A


ATOM
1236
N
GLY
A
161
6.847
−14.528
21.976
1.00
21.41
A


ATOM
1237
CA
GLY
A
161
6.478
−13.560
20.967
1.00
22.25
A


ATOM
1238
C
GLY
A
161
5.433
−12.613
21.509
1.00
20.28
A


ATOM
1239
O
GLY
A
161
4.449
−13.044
22.117
1.00
20.06
A


ATOM
1240
N
VAL
A
162
5.655
−11.322
21.309
1.00
20.58
A


ATOM
1241
CA
VAL
A
162
4.706
−10.314
21.769
1.00
22.29
A


ATOM
1242
CB
VAL
A
162
5.397
−9.253
22.691
1.00
21.30
A


ATOM
1243
CG1
VAL
A
162
6.693
−8.821
22.104
1.00
24.10
A


ATOM
1244
CG2
VAL
A
162
4.501
−8.056
22.885
1.00
21.27
A


ATOM
1245
C
VAL
A
162
4.125
−9.656
20.530
1.00
21.88
A


ATOM
1246
O
VAL
A
162
4.769
−8.818
19.899
1.00
22.52
A


ATOM
1247
N
PHE
A
163
2.904
−10.050
20.179
1.00
21.80
A


ATOM
1248
CA
PHE
A
163
2.258
−9.516
18.989
1.00
20.47
A


ATOM
1249
CB
PHE
A
163
2.004
−10.663
18.012
1.00
21.66
A


ATOM
1250
CG
PHE
A
163
3.212
−11.550
17.792
1.00
22.63
A


ATOM
1251
CD1
PHE
A
163
4.364
−11.052
17.174
1.00
25.88
A


ATOM
1252
CD2
PHE
A
163
3.206
−12.875
18.210
1.00
22.78
A


ATOM
1253
CE1
PHE
A
163
5.495
−11.865
16.975
1.00
24.44
A


ATOM
1254
CE2
PHE
A
163
4.329
−13.695
18.017
1.00
24.67
A


ATOM
1255
CZ
PHE
A
163
5.472
−13.187
17.398
1.00
21.69
A


ATOM
1256
C
PHE
A
163
.960
−8.743
19.261
1.00
20.46
A


ATOM
1257
O
PHE
A
163
.251
−9.001
20.231
1.00
20.17
A


ATOM
1258
N
GLN
A
164
.662
−7.787
18.390
1.00
19.59
A


ATOM
1259
CA
GLN
A
164
−.538
−6.954
18.500
1.00
21.23
A


ATOM
1260
CB
GLN
A
164
−1.798
−7.767
18.156
1.00
20.31
A


ATOM
1261
CG
GLN
A
164
−1.650
−8.597
16.882
1.00
21.02
A


ATOM
1262
CD
GLN
A
164
−2.973
−8.990
16.228
1.00
23.06
A


ATOM
1263
OE1
GLN
A
164
−2.985
−9.831
15.322
1.00
21.66
A


ATOM
1264
NE2
GLN
A
164
−4.085
−8.380
16.666
1.00
19.73
A


ATOM
1265
C
GLN
A
164
−.699
−6.258
19.858
1.00
22.09
A


ATOM
1266
O
GLN
A
164
−1.791
−6.189
20.425
1.00
22.31
A


ATOM
1267
N
HIS
A
165
.405
−5.748
20.382
1.00
22.18
A


ATOM
1268
CA
HIS
A
165
.354
−5.022
21.635
1.00
24.10
A


ATOM
1269
CB
HIS
A
165
1.592
−5.307
22.483
1.00
21.91
A


ATOM
1270
CG
HIS
A
165
1.517
−6.596
23.241
1.00
17.46
A


ATOM
1271
CD2
HIS
A
165
1.334
−6.842
24.559
1.00
15.97
A


ATOM
1272
ND1
HIS
A
165
1.557
−7.827
22.623
1.00
16.67
A


ATOM
1273
CE1
HIS
A
165
1.395
−8.776
23.527
1.00
17.09
A


ATOM
1274
NE2
HIS
A
165
1.255
−8.206
24.710
1.00
15.95
A


ATOM
1275
C
HIS
A
165
.292
−3.556
21.215
1.00
27.28
A


ATOM
1276
O
HIS
A
165
−.587
−2.812
21.642
1.00
26.92
A


ATOM
1277
N
GLY
A
166
1.211
−3.155
20.348
1.00
29.59
A


ATOM
1278
CA
GLY
A
166
1.189
−1.787
19.877
1.00
33.81
A


ATOM
1279
C
GLY
A
166
2.466
−1.002
20.046
1.00
34.98
A


ATOM
1280
O
GLY
A
166
3.506
−1.539
20.436
1.00
36.81
A


ATOM
1281
N
CYS
A
167
2.370
.287
19.748
1.00
35.13
A


ATOM
1282
CA
CYS
A
167
3.490
1.200
19.847
1.00
34.95
A


ATOM
1283
CB
CYS
A
167
3.049
2.604
19.435
1.00
36.37
A


ATOM
1284
SG
CYS
A
167
2.675
2.790
17.682
1.00
38.64
A


ATOM
1285
C
CYS
A
167
4.102
1.257
21.238
1.00
34.59
A


ATOM
1286
O
CYS
A
167
5.198
1.782
21.402
1.00
36.85
A


ATOM
1287
N
PHE
A
168
3.407
.729
22.240
1.00
32.51
A


ATOM
1288
CA
PHE
A
168
3.936
.761
23.603
1.00
31.87
A


ATOM
1289
CB
PHE
A
168
2.781
.885
24.613
1.00
30.03
A


ATOM
1290
CG
PHE
A
168
1.954
−.362
24.758
1.00
30.47
A


ATOM
1291
CD1
PHE
A
168
2.428
−1.451
25.477
1.00
29.65
A


ATOM
1292
CD2
PHE
A
168
.700
−.454
24.165
1.00
30.86
A


ATOM
1293
CE1
PHE
A
168
1.662
−2.619
25.604
1.00
28.73
A


ATOM
1294
CE2
PHE
A
168
−.073
−1.618
24.286
1.00
29.81
A


ATOM
1295
CZ
PHE
A
168
.413
−2.698
25.008
1.00
28.11
A


ATOM
1296
C
PHE
A
168
4.803
−.462
23.932
1.00
31.42
A


ATOM
1297
O
PHE
A
168
5.464
−.502
24.966
1.00
31.40
A


ATOM
1298
N
ALA
A
169
4.797
−1.449
23.039
1.00
29.90
A


ATOM
1299
CA
ALA
A
169
5.554
−2.685
23.227
1.00
27.01
A


ATOM
1300
CB
ALA
A
169
5.299
−3.607
22.053
1.00
26.41
A


ATOM
1301
C
ALA
A
169
7.067
−2.512
23.444
1.00
26.73
A


ATOM
1302
O
ALA
A
169
7.720
−3.369
24.062
1.00
25.79
A


ATOM
1303
N
GLY
A
170
7.623
−1.414
22.941
1.00
24.59
A


ATOM
1304
CA
GLY
A
170
9.047
−1.176
23.100
1.00
24.21
A


ATOM
1305
C
GLY
A
170
9.454
−1.313
24.551
1.00
25.87
A


ATOM
1306
O
GLY
A
170
10.559
−1.776
24.871
1.00
25.12
A


ATOM
1307
N
GLY
A
171
8.540
−.918
25.433
1.00
25.08
A


ATOM
1308
CA
GLY
A
171
8.792
−1.002
26.852
1.00
25.49
A


ATOM
1309
C
GLY
A
171
8.347
−2.307
27.489
1.00
25.76
A


ATOM
1310
O
GLY
A
171
9.017
−2.805
28.390
1.00
24.97
A


ATOM
1311
N
THR
A
172
7.222
−2.869
27.054
1.00
26.67
A


ATOM
1312
CA
THR
A
172
6.768
−4.120
27.666
1.00
26.43
A


ATOM
1313
CB
THR
A
172
5.403
−4.619
27.094
1.00
25.00
A


ATOM
1314
OG1
THR
A
172
5.588
−5.868
26.421
1.00
25.54
A


ATOM
1315
CG2
THR
A
172
4.819
−3.626
26.142
1.00
22.87
A


ATOM
1316
C
THR
A
172
7.841
−5.198
27.459
1.00
27.23
A


ATOM
1317
O
THR
A
172
8.014
−6.091
28.290
1.00
26.37
A


ATOM
1318
N
VAL
A
173
8.580
−5.106
26.360
1.00
27.56
A


ATOM
1319
CA
VAL
A
173
9.623
−6.088
26.122
1.00
29.17
A


ATOM
1320
CB
VAL
A
173
10.179
−5.996
24.693
1.00
29.87
A


ATOM
1321
CG1
VAL
A
173
11.413
−6.834
24.591
1.00
33.23
A


ATOM
1322
CG2
VAL
A
173
9.142
−6.501
23.696
1.00
28.54
A


ATOM
1323
C
VAL
A
173
10.760
−5.914
27.136
1.00
29.10
A


ATOM
1324
O
VAL
A
173
11.349
−6.908
27.581
1.00
29.94
A


ATOM
1325
N
LEU
A
174
11.062
−4.668
27.508
1.00
26.46
A


ATOM
1326
CA
LEU
A
174
12.107
−4.416
28.504
1.00
25.15
A


ATOM
1327
CB
LEU
A
174
12.472
−2.931
28.557
1.00
23.15
A


ATOM
1328
CG
LEU
A
174
13.226
−2.342
27.361
1.00
22.33
A


ATOM
1329
CD1
LEU
A
174
13.316
−.839
27.523
1.00
22.43
A


ATOM
1330
CD2
LEU
A
174
14.612
−2.955
27.254
1.00
23.94
A


ATOM
1331
C
LEU
A
174
11.594
−4.874
29.872
1.00
25.36
A


ATOM
1332
O
LEU
A
174
12.360
−5.370
30.716
1.00
23.86
A


ATOM
1333
N
ARG
A
175
10.288
−4.713
30.071
1.00
23.61
A


ATOM
1334
CA
ARG
A
175
9.635
−5.115
31.304
1.00
26.33
A


ATOM
1335
CB
ARG
A
175
8.184
−4.608
31.310
1.00
26.51
A


ATOM
1336
CG
ARG
A
175
7.329
−5.182
32.409
1.00
29.10
A


ATOM
1337
CD
ARG
A
175
6.139
−4.287
32.726
1.00
31.57
A


ATOM
1338
NE
ARG
A
175
5.198
−4.159
31.620
1.00
34.18
A


ATOM
1339
CZ
ARG
A
175
4.398
−5.132
31.196
1.00
35.28
A


ATOM
1340
NH1
ARG
A
175
4.422
−6.323
31.783
1.00
37.05
A


ATOM
1341
NH2
ARG
A
175
3.554
−4.907
30.198
1.00
35.45
A


ATOM
1342
C
ARG
A
175
9.690
−6.646
31.394
1.00
26.56
A


ATOM
1343
O
ARG
A
175
9.846
−7.222
32.481
1.00
27.45
A


ATOM
1344
N
MET
A
176
9.584
−7.303
30.242
1.00
27.50
A


ATOM
1345
CA
MET
A
176
9.644
−8.764
30.193
1.00
27.64
A


ATOM
1346
CB
MET
A
176
9.029
−9.278
28.879
1.00
26.71
A


ATOM
1347
CG
MET
A
176
7.521
−9.034
28.775
1.00
28.23
A


ATOM
1348
SD
MET
A
176
6.800
−9.487
27.195
1.00
23.55
A


ATOM
1349
CE
MET
A
176
7.101
−8.102
26.259
1.00
28.45
A


ATOM
1350
C
MET
A
176
11.096
−9.221
30.323
1.00
27.94
A


ATOM
1351
O
MET
A
176
11.403
−10.166
31.052
1.00
30.27
A


ATOM
1352
N
ALA
A
177
11.987
−8.532
29.628
1.00
28.25
A


ATOM
1353
CA
ALA
A
177
13.403
−8.868
29.672
1.00
29.84
A


ATOM
1354
CB
ALA
A
177
14.200
−7.954
28.738
1.00
29.86
A


ATOM
1355
C
ALA
A
177
13.961
−8.767
31.075
1.00
30.68
A


ATOM
1356
O
ALA
A
177
14.790
−9.592
31.469
1.00
32.02
A


ATOM
1357
N
LYS
A
178
13.528
−7.759
31.830
1.00
30.79
A


ATOM
1358
CA
LYS
A
178
14.038
−7.588
33.188
1.00
31.72
A


ATOM
1359
CB
LYS
A
178
13.477
−6.310
33.830
1.00
31.12
A


ATOM
1360
CG
LYS
A
178
13.749
−6.197
35.345
1.00
29.02
A


ATOM
1361
CD
LYS
A
178
13.189
−4.903
35.918
1.00
29.04
A


ATOM
1362
CE
LYS
A
178
13.136
−4.914
37.449
1.00
27.26
A


ATOM
1363
NZ
LYS
A
178
14.480
−4.807
38.065
1.00
28.61
A


ATOM
1364
C
LYS
A
178
13.706
−8.795
34.067
1.00
31.60
A


ATOM
1365
O
LYS
A
178
14.581
−9.355
34.733
1.00
31.68
A


ATOM
1366
N
ASP
A
179
12.441
−9.200
34.062
1.00
31.22
A


ATOM
1367
CA
ASP
A
179
12.033
−10.329
34.880
1.00
30.84
A


ATOM
1368
CB
ASP
A
179
10.517
−10.497
34.829
1.00
31.04
A


ATOM
1369
CG
ASP
A
179
9.797
−9.640
35.859
1.00
35.44
A


ATOM
1370
OD1
ASP
A
179
10.435
−8.734
36.452
1.00
30.14
A


ATOM
1371
OD2
ASP
A
179
8.581
−9.875
36.070
1.00
37.43
A


ATOM
1372
C
ASP
A
179
12.733
−11.607
34.446
1.00
29.75
A


ATOM
1373
O
ASP
A
179
13.051
−12.450
35.273
1.00
28.93
A


ATOM
1374
N
LEU
A
180
12.986
−11.744
33.151
1.00
28.74
A


ATOM
1375
CA
LEU
A
180
13.661
−12.936
32.651
1.00
28.44
A


ATOM
1376
CB
LEU
A
180
13.561
−13.009
31.132
1.00
25.80
A


ATOM
1377
CG
LEU
A
180
12.197
−13.379
30.563
1.00
25.86
A


ATOM
1378
CD1
LEU
A
180
12.387
−13.863
29.142
1.00
26.09
A


ATOM
1379
CD2
LEU
A
180
11.575
−14.493
31.379
1.00
26.77
A


ATOM
1380
C
LEU
A
180
15.126
−12.981
33.060
1.00
29.17
A


ATOM
1381
O
LEU
A
180
15.590
−13.971
33.624
1.00
29.96
A


ATOM
1382
N
ALA
A
181
15.852
−11.901
32.787
1.00
29.52
A


ATOM
1383
CA
ALA
A
181
17.273
−11.843
33.116
1.00
28.81
A


ATOM
1384
CB
ALA
A
181
17.909
−10.617
32.473
1.00
27.02
A


ATOM
1385
C
ALA
A
181
17.571
−11.850
34.614
1.00
29.43
A


ATOM
1386
O
ALA
A
181
18.621
−12.323
35.037
1.00
29.28
A


ATOM
1387
N
GLU
A
182
16.654
−11.334
35.418
1.00
28.32
A


ATOM
1388
CA
GLU
A
182
16.903
−11.283
36.845
1.00
28.42
A


ATOM
1389
CB
GLU
A
182
16.206
−10.057
37.446
1.00
28.31
A


ATOM
1390
CG
GLU
A
182
17.074
−8.799
37.425
1.00
28.39
A


ATOM
1391
CD
GLU
A
182
16.286
−7.505
37.641
1.00
30.17
A


ATOM
1392
OE1
GLU
A
182
15.276
−7.535
38.378
1.00
31.81
A


ATOM
1393
OE2
GLU
A
182
16.683
−6.455
37.079
1.00
26.98
A


ATOM
1394
C
GLU
A
182
16.533
−12.545
37.612
1.00
29.49
A


ATOM
1395
O
GLU
A
182
17.124
−12.827
38.657
1.00
29.42
A


ATOM
1396
N
ASN
A
183
15.587
−13.318
37.085
1.00
27.48
A


ATOM
1397
CA
ASN
A
183
15.139
−14.531
37.747
1.00
26.14
A


ATOM
1398
CB
ASN
A
183
13.626
−14.682
37.571
1.00
28.22
A


ATOM
1399
CG
ASN
A
183
13.022
−15.678
38.538
1.00
27.66
A


ATOM
1400
OD1
ASN
A
183
13.287
−15.633
39.740
1.00
26.28
A


ATOM
1401
ND2
ASN
A
183
12.190
−16.571
38.023
1.00
29.55
A


ATOM
1402
C
ASN
A
183
15.844
−15.781
37.236
1.00
26.45
A


ATOM
1403
O
ASN
A
183
15.562
−16.896
37.690
1.00
25.91
A


ATOM
1404
N
ASN
A
184
16.755
−15.595
36.288
1.00
26.39
A


ATOM
1405
CA
ASN
A
184
17.507
−16.710
35.715
1.00
25.21
A


ATOM
1406
CB
ASN
A
184
17.006
−17.015
34.305
1.00
23.95
A


ATOM
1407
CG
ASN
A
184
15.540
−17.407
34.285
1.00
26.13
A


ATOM
1408
OD1
ASN
A
184
15.150
−18.407
34.888
1.00
27.10
A


ATOM
1409
ND2
ASN
A
184
14.719
−16.618
33.595
1.00
24.91
A


ATOM
1410
C
ASN
A
184
18.979
−16.346
35.685
1.00
24.51
A


ATOM
1411
O
ASN
A
184
19.439
−15.657
34.774
1.00
22.61
A


ATOM
1412
N
ARG
A
185
19.713
−16.793
36.701
1.00
25.18
A


ATOM
1413
CA
ARG
A
185
21.135
−16.489
36.792
1.00
26.91
A


ATOM
1414
CB
ARG
A
185
21.757
−17.152
38.027
1.00
27.36
A


ATOM
1415
CG
ARG
A
185
23.194
−16.712
38.326
1.00
27.62
A


ATOM
1416
CD
ARG
A
185
23.915
−17.698
39.265
1.00
29.15
A


ATOM
1417
NE
ARG
A
185
23.236
−17.834
40.554
1.00
32.65
A


ATOM
1418
CZ
ARG
A
185
23.199
−16.886
41.491
1.00
32.73
A


ATOM
1419
NH1
ARG
A
185
23.808
−15.718
41.298
1.00
34.52
A


ATOM
1420
NH2
ARG
A
185
22.543
−17.102
42.623
1.00
32.17
A


ATOM
1421
C
ARG
A
185
21.805
−17.000
35.534
1.00
27.64
A


ATOM
1422
O
ARG
A
185
21.583
−18.142
35.124
1.00
26.90
A


ATOM
1423
N
GLY
A
186
22.593
−16.131
34.907
1.00
29.73
A


ATOM
1424
CA
GLY
A
186
23.301
−16.500
33.694
1.00
29.72
A


ATOM
1425
C
GLY
A
186
22.517
−16.302
32.408
1.00
28.96
A


ATOM
1426
O
GLY
A
186
23.035
−16.517
31.314
1.00
28.86
A


ATOM
1427
N
ALA
A
187
21.267
−15.884
32.533
1.00
27.00
A


ATOM
1428
CA
ALA
A
187
20.423
−15.676
31.369
1.00
27.51
A


ATOM
1429
CB
ALA
A
187
18.968
−15.538
31.800
1.00
27.04
A


ATOM
1430
C
ALA
A
187
20.817
−14.463
30.547
1.00
28.01
A


ATOM
1431
O
ALA
A
187
21.187
−13.416
31.082
1.00
28.40
A


ATOM
1432
N
ARG
A
188
20.724
−14.624
29.236
1.00
27.77
A


ATOM
1433
CA
ARG
A
188
21.006
−13.551
28.300
1.00
27.68
A


ATOM
1434
CB
ARG
A
188
22.331
−13.810
27.581
1.00
26.99
A


ATOM
1435
CG
ARG
A
188
23.572
−13.728
28.492
1.00
27.67
A


ATOM
1436
CD
ARG
A
188
23.868
−12.276
28.890
1.00
31.52
A


ATOM
1437
NE
ARG
A
188
24.994
−12.151
29.820
1.00
30.38
A


ATOM
1438
CZ
ARG
A
188
24.909
−12.292
31.143
1.00
31.58
A


ATOM
1439
NH1
ARG
A
188
23.741
−12.562
31.722
1.00
24.80
A


ATOM
1440
NH2
ARG
A
188
26.002
−12.165
31.891
1.00
31.53
A


ATOM
1441
C
ARG
A
188
19.809
−13.538
27.321
1.00
28.85
A


ATOM
1442
O
ARG
A
188
19.605
−14.459
26.515
1.00
27.23
A


ATOM
1443
N
VAL
A
189
18.993
−12.499
27.436
1.00
27.60
A


ATOM
1444
CA
VAL
A
189
17.819
−12.367
26.597
1.00
26.30
A


ATOM
1445
CB
VAL
A
189
16.676
−11.696
27.375
1.00
25.85
A


ATOM
1446
CG1
VAL
A
189
15.384
−11.786
26.597
1.00
24.31
A


ATOM
1447
CG2
VAL
A
189
16.519
−12.363
28.719
1.00
28.18
A


ATOM
1448
C
VAL
A
189
18.122
−11.539
25.360
1.00
25.71
A


ATOM
1449
O
VAL
A
189
18.738
−10.485
25.438
1.00
25.75
A


ATOM
1450
N
LEU
A
190
17.723
−12.052
24.206
1.00
27.67
A


ATOM
1451
CA
LEU
A
190
17.889
−11.319
22.961
1.00
27.51
A


ATOM
1452
CB
LEU
A
190
18.196
−12.259
21.793
1.00
26.13
A


ATOM
1453
CG
LEU
A
190
18.194
−11.660
20.379
1.00
24.00
A


ATOM
1454
CD1
LEU
A
190
19.134
−10.440
20.284
1.00
16.10
A


ATOM
1455
CD2
LEU
A
190
18.579
−12.758
19.394
1.00
20.62
A


ATOM
1456
C
LEU
A
190
16.519
−10.687
22.781
1.00
27.57
A


ATOM
1457
O
LEU
A
190
15.505
−11.383
22.709
1.00
29.76
A


ATOM
1458
N
VAL
A
191
16.491
−9.365
22.758
1.00
27.48
A


ATOM
1459
CA
VAL
A
191
15.252
−8.632
22.614
1.00
25.21
A


ATOM
1460
CB
VAL
A
191
15.171
−7.544
23.696
1.00
26.45
A


ATOM
1461
CG1
VAL
A
191
14.054
−6.574
23.376
1.00
26.55
A


ATOM
1462
CG2
VAL
A
191
14.953
−8.198
25.072
1.00
23.22
A


ATOM
1463
C
VAL
A
191
15.188
−8.022
21.218
1.00
25.89
A


ATOM
1464
O
VAL
A
191
16.056
−7.243
20.829
1.00
25.61
A


ATOM
1465
N
ILE
A
192
14.162
−8.390
20.460
1.00
25.32
A


ATOM
1466
CA
ILE
A
192
14.026
−7.891
19.102
1.00
25.33
A


ATOM
1467
CB
ILE
A
192
14.340
−9.019
18.074
1.00
23.22
A


ATOM
1468
CG2
ILE
A
192
14.375
−8.447
16.664
1.00
24.09
A


ATOM
1469
CG1
ILE
A
192
15.700
−9.648
18.399
1.00
23.39
A


ATOM
1470
CD1
ILE
A
192
16.041
−10.889
17.601
1.00
21.13
A


ATOM
1471
C
ILE
A
192
12.654
−7.286
18.792
1.00
27.03
A


ATOM
1472
O
ILE
A
192
11.616
−7.857
19.117
1.00
28.27
A


ATOM
1473
N
CYS
A
193
12.676
−6.110
18.176
1.00
27.44
A


ATOM
1474
CA
CYS
A
193
11.459
−5.410
17.777
1.00
29.84
A


ATOM
1475
CB
CYS
A
193
11.286
−4.079
18.524
1.00
29.24
A


ATOM
1476
SG
CYS
A
193
10.748
−4.211
20.241
1.00
33.41
A


ATOM
1477
C
CYS
A
193
11.616
−5.107
16.307
1.00
28.84
A


ATOM
1478
O
CYS
A
193
12.470
−4.301
15.939
1.00
27.97
A


ATOM
1479
N
SER
A
194
10.803
−5.761
15.476
1.00
28.80
A


ATOM
1480
CA
SER
A
194
10.844
−5.541
14.036
1.00
28.93
A


ATOM
1481
CB
SER
A
194
11.290
−6.816
13.304
1.00
28.77
A


ATOM
1482
OG
SER
A
194
11.556
−6.556
11.932
1.00
27.02
A


ATOM
1483
C
SER
A
194
9.462
−5.111
13.552
1.00
28.93
A


ATOM
1484
O
SER
A
194
8.457
−5.766
13.833
1.00
26.74
A


ATOM
1485
N
GLU
A
195
9.425
−4.005
12.816
1.00
29.64
A


ATOM
1486
CA
GLU
A
195
8.172
−3.468
12.311
1.00
30.24
A


ATOM
1487
CB
GLU
A
195
7.737
−2.305
13.200
1.00
31.77
A


ATOM
1488
CG
GLU
A
195
7.727
−2.645
14.686
1.00
36.82
A


ATOM
1489
CD
GLU
A
195
6.410
−3.250
15.148
1.00
39.92
A


ATOM
1490
OE1
GLU
A
195
5.813
−4.031
14.374
1.00
39.88
A


ATOM
1491
OE2
GLU
A
195
5.981
−2.948
16.290
1.00
40.67
A


ATOM
1492
C
GLU
A
195
8.278
−2.994
10.864
1.00
29.61
A


ATOM
1493
O
GLU
A
195
9.326
−2.519
10.426
1.00
28.59
A


ATOM
1494
N
THR
A
196
7.188
−3.141
10.118
1.00
28.84
A


ATOM
1495
CA
THR
A
196
7.151
−2.688
8.733
1.00
28.59
A


ATOM
1496
CB
THR
A
196
7.561
−3.802
7.732
1.00
29.67
A


ATOM
1497
OG1
THR
A
196
7.608
−3.250
6.412
1.00
27.60
A


ATOM
1498
CG2
THR
A
196
6.558
−4.942
7.749
1.00
27.62
A


ATOM
1499
C
THR
A
196
5.741
−2.204
8.394
1.00
28.47
A


ATOM
1500
O
THR
A
196
4.750
−2.732
8.902
1.00
29.71
A


ATOM
1501
N
THR
A
197
5.661
−1.194
7.536
1.00
26.20
A


ATOM
1502
CA
THR
A
197
4.390
−.632
7.139
1.00
23.42
A


ATOM
1503
CB
THR
A
197
4.580
.788
6.587
1.00
24.48
A


ATOM
1504
OG1
THR
A
197
5.705
.797
5.713
1.00
24.80
A


ATOM
1505
CG2
THR
A
197
4.824
1.780
7.713
1.00
22.95
A


ATOM
1506
C
THR
A
197
3.666
−1.475
6.099
1.00
24.32
A


ATOM
1507
O
THR
A
197
2.504
−1.209
5.791
1.00
21.28
A


ATOM
1508
N
ALA
A
198
4.341
−2.490
5.561
1.00
23.32
A


ATOM
1509
CA
ALA
A
198
3.731
−3.347
4.546
1.00
24.83
A


ATOM
1510
CB
ALA
A
198
4.631
−4.554
4.259
1.00
22.22
A


ATOM
1511
C
ALA
A
198
2.327
−3.827
4.944
1.00
27.02
A


ATOM
1512
O
ALA
A
198
1.436
−3.939
4.099
1.00
29.39
A


ATOM
1513
N
VAL
A
199
2.129
−4.110
6.225
1.00
25.63
A


ATOM
1514
CA
VAL
A
199
.834
−4.581
6.697
1.00
25.98
A


ATOM
1515
CB
VAL
A
199
1.001
−5.406
7.999
1.00
27.15
A


ATOM
1516
CG1
VAL
A
199
1.506
−4.512
9.124
1.00
26.01
A


ATOM
1517
CG2
VAL
A
199
−.319
−6.058
8.381
1.00
25.90
A


ATOM
1518
C
VAL
A
199
−.198
−3.459
6.943
1.00
27.11
A


ATOM
1519
O
VAL
A
199
−1.385
−3.736
7.171
1.00
24.23
A


ATOM
1520
N
THR
A
200
.243
−2.203
6.872
1.00
26.28
A


ATOM
1521
CA
THR
A
200
−.649
−1.072
7.127
1.00
28.77
A


ATOM
1522
CB
THR
A
200
−.207
−.306
8.375
1.00
28.69
A


ATOM
1523
OG1
THR
A
200
−1.236
.617
8.745
1.00
34.92
A


ATOM
1524
CG2
THR
A
200
1.082
.468
8.100
1.00
29.34
A


ATOM
1525
C
THR
A
200
−.812
−.046
6.003
1.00
29.04
A


ATOM
1526
O
THR
A
200
−1.803
.686
5.966
1.00
29.83
A


ATOM
1527
N
PHE
A
201
.154
.013
5.093
1.00
29.37
A


ATOM
1528
CA
PHE
A
201
.099
.967
3.993
1.00
27.14
A


ATOM
1529
CB
PHE
A
201
1.390
.900
3.164
1.00
26.36
A


ATOM
1530
CG
PHE
A
201
1.328
1.654
1.853
1.00
23.85
A


ATOM
1531
CD1
PHE
A
201
.634
1.131
.762
1.00
24.10
A


ATOM
1532
CD2
PHE
A
201
1.959
2.889
1.713
1.00
24.80
A


ATOM
1533
CE1
PHE
A
201
.567
1.831
−.447
1.00
24.95
A


ATOM
1534
CE2
PHE
A
201
1.901
3.597
.513
1.00
21.90
A


ATOM
1535
CZ
PHE
A
201
1.205
3.072
−.569
1.00
24.52
A


ATOM
1536
C
PHE
A
201
−1.095
.748
3.089
1.00
26.41
A


ATOM
1537
O
PHE
A
201
−1.278
−.325
2.531
1.00
24.36
A


ATOM
1538
N
ARG
A
202
−1.900
1.789
2.941
1.00
24.97
A


ATOM
1539
CA
ARG
A
202
−3.063
1.730
2.075
1.00
24.55
A


ATOM
1540
CB
ARG
A
202
−4.299
1.327
2.883
1.00
20.28
A


ATOM
1541
CG
ARG
A
202
−4.532
2.183
4.108
1.00
20.71
A


ATOM
1542
CD
ARG
A
202
−5.718
1.693
4.931
1.00
23.12
A


ATOM
1543
NE
ARG
A
202
−5.454
.417
5.588
1.00
24.02
A


ATOM
1544
CZ
ARG
A
202
−5.566
−.771
4.999
1.00
23.58
A


ATOM
1545
NH1
ARG
A
202
−5.942
−.855
3.736
1.00
23.59
A


ATOM
1546
NH2
ARG
A
202
−5.305
−1.883
5.680
1.00
24.60
A


ATOM
1547
C
ARG
A
202
−3.251
3.116
1.448
1.00
24.73
A


ATOM
1548
O
ARG
A
202
−2.648
4.091
1.895
1.00
23.81
A


ATOM
1549
N
GLY
A
203
−4.079
3.192
.411
1.00
26.77
A


ATOM
1550
CA
GLY
A
203
−4.339
4.458
−.251
1.00
27.86
A


ATOM
1551
C
GLY
A
203
−5.000
5.470
.666
1.00
29.95
A


ATOM
1552
O
GLY
A
203
−5.455
5.128
1.757
1.00
30.65
A


ATOM
1553
N
PRO
A
204
−5.086
6.730
.238
1.00
31.00
A


ATOM
1554
CD
PRO
A
204
−4.681
7.238
−1.085
1.00
31.27
A


ATOM
1555
CA
PRO
A
204
−5.693
7.799
1.034
1.00
33.93
A


ATOM
1556
CB
PRO
A
204
−5.127
9.047
.388
1.00
33.92
A


ATOM
1557
CG
PRO
A
204
−5.221
8.670
−1.069
1.00
33.17
A


ATOM
1558
C
PRO
A
204
−7.207
7.780
.961
1.00
35.37
A


ATOM
1559
O
PRO
A
204
−7.784
7.238
.028
1.00
38.01
A


ATOM
1560
N
SER
A
205
−7.846
8.387
1.945
1.00
37.66
A


ATOM
1561
CA
SER
A
205
−9.295
8.452
1.975
1.00
39.54
A


ATOM
1562
CB
SER
A
205
−9.858
7.242
2.722
1.00
40.11
A


ATOM
1563
OG
SER
A
205
−11.271
7.211
2.638
1.00
45.37
A


ATOM
1564
C
SER
A
205
−9.694
9.746
2.675
1.00
39.76
A


ATOM
1565
O
SER
A
205
−9.102
10.119
3.687
1.00
40.03
A


ATOM
1566
N
GLU
A
206
−10.685
10.438
2.129
1.00
41.11
A


ATOM
1567
CA
GLU
A
206
−11.138
11.690
2.723
1.00
43.15
A


ATOM
1568
CB
GLU
A
206
−11.788
12.585
1.660
1.00
44.15
A


ATOM
1569
CG
GLU
A
206
−12.678
11.861
.666
1.00
47.17
A


ATOM
1570
CD
GLU
A
206
−11.906
11.275
−.512
1.00
50.55
A


ATOM
1571
OE1
GLU
A
206
−11.174
10.273
−.332
1.00
50.11
A


ATOM
1572
OE2
GLU
A
206
−12.031
11.830
−1.628
1.00
51.91
A


ATOM
1573
C
GLU
A
206
−12.100
11.481
3.895
1.00
43.15
A


ATOM
1574
O
GLU
A
206
−12.333
12.392
4.690
1.00
44.07
A


ATOM
1575
N
THR
A
207
−12.651
10.281
4.012
1.00
43.47
A


ATOM
1576
CA
THR
A
207
−13.559
9.998
5.109
1.00
43.94
A


ATOM
1577
CB
THR
A
207
−14.742
9.123
4.639
1.00
46.32
A


ATOM
1578
OG1
THR
A
207
−14.258
7.858
4.172
1.00
50.01
A


ATOM
1579
CG2
THR
A
207
−15.494
9.814
3.511
1.00
47.66
A


ATOM
1580
C
THR
A
207
−12.831
9.297
6.260
1.00
42.70
A


ATOM
1581
O
THR
A
207
−13.456
8.884
7.232
1.00
42.48
A


ATOM
1582
N
HIS
A
208
−11.509
9.183
6.155
1.00
41.66
A


ATOM
1583
CA
HIS
A
208
−10.709
8.520
7.185
1.00
40.56
A


ATOM
1584
CB
HIS
A
208
−10.471
7.071
6.761
1.00
40.63
A


ATOM
1585
CG
HIS
A
208
−11.728
6.272
6.641
1.00
41.45
A


ATOM
1586
CD2
HIS
A
208
−12.552
6.060
5.588
1.00
41.71
A


ATOM
1587
ND1
HIS
A
208
−12.306
5.629
7.714
1.00
43.34
A


ATOM
1588
CE1
HIS
A
208
−13.432
5.056
7.327
1.00
42.20
A


ATOM
1589
NE2
HIS
A
208
−13.605
5.303
6.041
1.00
40.79
A


ATOM
1590
C
HIS
A
208
−9.366
9.216
7.468
1.00
40.72
A


ATOM
1591
O
HIS
A
208
−8.305
8.578
7.455
1.00
36.97
A


ATOM
1592
N
LEU
A
209
−9.428
10.519
7.744
1.00
41.16
A


ATOM
1593
CA
LEU
A
209
−8.240
11.328
8.013
1.00
42.25
A


ATOM
1594
CB
LEU
A
209
−8.648
12.766
8.322
1.00
44.19
A


ATOM
1595
CG
LEU
A
209
−9.250
13.521
7.130
1.00
45.60
A


ATOM
1596
CD1
LEU
A
209
−9.688
14.911
7.553
1.00
45.32
A


ATOM
1597
CD2
LEU
A
209
−8.214
13.608
6.016
1.00
45.26
A


ATOM
1598
C
LEU
A
209
−7.326
10.806
9.117
1.00
43.63
A


ATOM
1599
O
LEU
A
209
−6.117
11.059
9.100
1.00
43.18
A


ATOM
1600
N
ASP
A
210
−7.885
10.077
10.077
1.00
44.10
A


ATOM
1601
CA
ASP
A
210
−7.054
9.538
11.144
1.00
43.86
A


ATOM
1602
CB
ASP
A
210
−7.921
8.879
12.224
1.00
44.72
A


ATOM
1603
CG
ASP
A
210
−8.520
7.567
11.781
1.00
46.10
A


ATOM
1604
OD1
ASP
A
210
−8.932
7.454
10.606
1.00
45.79
A


ATOM
1605
OD2
ASP
A
210
−8.595
6.649
12.626
1.00
48.31
A


ATOM
1606
C
ASP
A
210
−6.087
8.539
10.506
1.00
44.25
A


ATOM
1607
O
ASP
A
210
−4.962
8.352
10.985
1.00
44.96
A


ATOM
1608
N
SER
A
211
−6.521
7.928
9.402
1.00
42.15
A


ATOM
1609
CA
SER
A
211
−5.700
6.970
8.671
1.00
40.33
A


ATOM
1610
CB
SER
A
211
−6.570
6.078
7.776
1.00
41.73
A


ATOM
1611
OG
SER
A
211
−5.763
5.245
6.948
1.00
40.95
A


ATOM
1612
C
SER
A
211
−4.659
7.679
7.808
1.00
39.17
A


ATOM
1613
O
SER
A
211
−3.592
7.128
7.550
1.00
37.98
A


ATOM
1614
N
LEU
A
212
−4.979
8.892
7.355
1.00
38.41
A


ATOM
1615
CA
LEU
A
212
−4.049
9.668
6.533
1.00
35.56
A


ATOM
1616
CB
LEU
A
212
−4.622
11.048
6.201
1.00
34.77
A


ATOM
1617
CG
LEU
A
212
−5.091
11.392
4.787
1.00
33.15
A


ATOM
1618
CD1
LEU
A
212
−5.182
12.915
4.668
1.00
32.90
A


ATOM
1619
CD2
LEU
A
212
−4.125
10.855
3.754
1.00
31.17
A


ATOM
1620
C
LEU
A
212
−2.792
9.857
7.358
1.00
35.22
A


ATOM
1621
O
LEU
A
212
−1.701
9.450
6.961
1.00
36.22
A


ATOM
1622
N
VAL
A
213
−2.962
10.499
8.510
1.00
33.04
A


ATOM
1623
CA
VAL
A
213
−1.864
10.745
9.430
1.00
32.51
A


ATOM
1624
CB
VAL
A
213
−2.414
10.985
10.857
1.00
31.66
A


ATOM
1625
CG1
VAL
A
213
−1.275
11.153
11.843
1.00
31.63
A


ATOM
1626
CG2
VAL
A
213
−3.307
12.211
10.860
1.00
29.64
A


ATOM
1627
C
VAL
A
212
−.911
9.539
9.439
1.00
32.48
A


ATOM
1628
O
VAL
A
213
.271
9.660
9.104
1.00
32.59
A


ATOM
1629
N
GLY
A
214
−1.449
8.378
9.809
1.00
31.64
A


ATOM
1630
CA
GLY
A
214
−.666
7.158
9.864
1.00
31.10
A


ATOM
1631
C
GLY
A
214
.185
6.885
8.638
1.00
31.81
A


ATOM
1632
O
GLY
A
214
1.283
6.339
8.760
1.00
31.87
A


ATOM
1633
N
GLN
A
215
−.303
7.249
7.454
1.00
30.01
A


ATOM
1634
CA
GLN
A
215
.470
7.016
6.239
1.00
29.39
A


ATOM
1635
CB
GLN
A
215
−.383
7.249
4.990
1.00
29.12
A


ATOM
1636
CG
GLN
A
215
−1.456
6.213
4.805
1.00
28.36
A


ATOM
1637
CD
GLN
A
215
−.938
4.825
5.120
1.00
29.65
A


ATOM
1638
OE1
GLN
A
215
−1.545
4.095
5.899
1.00
27.40
A


ATOM
1639
NE2
GLN
A
215
.195
4.458
4.523
1.00
29.22
A


ATOM
1640
C
GLN
A
215
1.697
7.908
6.181
1.00
29.72
A


ATOM
1641
O
GLN
A
215
2.644
7.619
5.452
1.00
29.34
A


ATOM
1642
N
ALA
A
215
1.673
8.988
6.957
1.00
29.06
A


ATOM
1643
CA
ALA
A
216
2.781
9.928
6.977
1.00
29.34
A


ATOM
1644
CB
ALA
A
216
2.250
11.358
6.959
1.00
28.98
A


ATOM
1645
C
ALA
A
216
3.711
9.744
8.167
1.00
28.44
A


ATOM
1646
O
ALA
A
216
4.859
10.171
8.119
1.00
28.77
A


ATOM
1647
N
LEU
A
217
3.226
9.105
9.225
1.00
26.41
A


ATOM
1648
CA
LEU
A
217
4.037
8.934
10.417
1.00
26.85
A


ATOM
1649
CB
LEU
A
217
3.159
9.022
11.660
1.00
27.43
A


ATOM
1650
CG
LEU
A
217
2.419
10.340
11.889
1.00
27.77
A


ATOM
1651
CD1
LEU
A
217
1.602
10.236
13.167
1.00
27.93
A


ATOM
1652
CD2
LEU
A
217
3.411
11.495
11.970
1.00
28.42
A


ATOM
1653
C
LEU
A
217
4.860
7.660
10.489
1.00
28.52
A


ATOM
1654
O
LEU
A
217
6.070
7.707
10.703
1.00
29.49
A


ATOM
1655
N
PHE
A
218
4.196
6.524
10.324
1.00
28.61
A


ATOM
1656
CA
PHE
A
218
4.853
5.229
10.409
1.00
28.75
A


ATOM
1657
CB
PHE
A
218
3.794
4.127
10.391
1.00
31.22
A


ATOM
1658
CG
PHE
A
218
2.703
4.324
11.403
1.00
34.00
A


ATOM
1659
CD1
PHE
A
218
3.008
4.645
12.719
1.00
36.79
A


ATOM
1660
CD2
PHE
A
218
1.370
4.170
11.046
1.00
36.49
A


ATOM
1661
CE1
PHE
A
218
2.002
4.811
13.674
1.00
36.73
A


ATOM
1662
CE2
PHE
A
218
.347
4.333
11.993
1.00
38.04
A


ATOM
1663
CZ
PHE
A
218
.667
4.654
13.310
1.00
37.72
A


ATOM
1664
C
PHE
A
218
5.933
4.916
9.368
1.00
27.22
A


ATOM
1665
O
PHE
A
218
5.798
5.219
8.181
1.00
25.21
A


ATOM
1666
N
GLY
A
219
7.011
4.300
9.851
1.00
28.13
A


ATOM
1667
CA
GLY
A
219
8.125
3.894
9.007
1.00
27.30
A


ATOM
1668
C
GLY
A
219
8.561
2.497
9.424
1.00
27.92
A


ATOM
1669
O
GLY
A
219
7.950
1.909
10.311
1.00
27.50
A


ATOM
1670
N
ASP
A
220
9.615
1.968
8.805
1.00
28.69
A


ATOM
1671
CA
ASP
A
220
10.100
.626
9.123
1.00
27.97
A


ATOM
1672
CB
ASP
A
220
10.161
−.243
7.860
1.00
27.48
A


ATOM
1673
CG
ASP
A
220
8.833
−.326
7.138
1.00
28.81
A


ATOM
1674
OD1
ASP
A
220
7.811
.115
7.706
1.00
28.94
A


ATOM
1675
OD2
ASP
A
220
8.810
−.848
6.003
1.00
30.23
A


ATOM
1676
C
ASP
A
220
11.470
.591
9.792
1.00
29.31
A


ATOM
1677
O
ASP
A
220
12.346
1.412
9.503
1.00
28.92
A


ATOM
1678
N
GLY
A
221
11.648
−.388
10.678
1.00
29.62
A


ATOM
1679
CA
GLY
A
221
12.911
−.556
11.378
1.00
27.70
A


ATOM
1680
C
GLY
A
221
12.920
−1.746
12.328
1.00
26.08
A


ATOM
1681
O
GLY
A
221
11.876
−2.273
12.703
1.00
24.58
A


ATOM
1682
N
ALA
A
222
14.114
−2.173
12.711
1.00
26.01
A


ATOM
1683
CA
ALA
A
222
14.270
−3.283
13.634
1.00
25.76
A


ATOM
1684
CB
ALA
A
222
14.657
−4.564
12.885
1.00
23.29
A


ATOM
1685
C
ALA
A
222
15.343
−2.915
14.644
1.00
27.10
A


ATOM
1686
O
ALA
A
222
16.394
−2.365
14.292
1.00
25.67
A


ATOM
1687
N
CYS
A
223
15.071
−3.214
15.906
1.00
27.08
A


ATOM
1688
CA
CYS
A
223
16.016
−2.917
16.960
1.00
28.62
A


ATOM
1689
CB
CYS
A
223
15.413
−1.939
17.942
1.00
33.80
A


ATOM
1690
SG
CYS
A
223
14.226
−2.768
18.964
1.00
42.48
A


ATOM
1691
C
CYS
A
223
16.282
−4.210
17.684
1.00
26.75
A


ATOM
1692
O
CYS
A
223
15.392
−5.058
17.783
1.00
25.04
A


ATOM
1693
N
ALA
A
224
17.494
−4.347
18.212
1.00
24.80
A


ATOM
1694
CA
ALA
A
224
17.872
−5.560
18.923
1.00
26.10
A


ATOM
1695
CB
ALA
A
224
18.578
−6.529
17.975
1.00
21.48
A


ATOM
1696
C
ALA
A
224
18.752
−5.261
20.129
1.00
26.20
A


ATOM
1697
O
ALA
A
224
19.707
−4.487
20.057
1.00
23.62
A


ATOM
1698
N
LEU
A
225
18.408
−5.901
21.240
1.00
28.73
A


ATOM
1699
CA
LEU
A
225
19.117
−5.738
22.499
1.00
29.59
A


ATOM
1700
CB
LEU
A
225
18.213
−5.087
23.547
1.00
28.37
A


ATOM
1701
CG
LEU
A
225
17.447
−3.834
23.171
1.00
30.11
A


ATOM
1702
CD1
LEU
A
225
16.636
−3.373
24.360
1.00
33.00
A


ATOM
1703
CD2
LEU
A
225
18.417
−2.757
22.733
1.00
30.82
A


ATOM
1704
C
LEU
A
225
19.541
−7.077
22.070
1.00
28.64
A


ATOM
1705
O
LEU
A
225
18.892
−8.099
22.837
1.00
26.77
A


ATOM
1706
N
ILE
A
226
20.629
−7.036
23.834
1.00
27.61
A


ATOM
1707
CA
ILE
A
226
21.143
−8.187
24.552
1.00
27.04
A


ATOM
1708
CB
ILE
A
226
22.659
−8.443
24.267
1.00
25.88
A


ATOM
1709
CG2
ILE
A
226
23.243
−9.389
25.305
1.00
27.04
A


ATOM
1710
CG1
ILE
A
226
22.836
−9.095
22.899
1.00
25.32
A


ATOM
1711
CD1
ILE
A
226
22.257
−10.490
22.817
1.00
24.29
A


ATOM
1712
C
ILE
A
226
20.932
−7.744
26.008
1.00
27.60
A


ATOM
1713
O
ILE
A
226
21.506
−6.746
26.463
1.00
26.23
A


ATOM
1714
N
VAL
A
227
20.064
−8.455
26.718
1.00
27.92
A


ATOM
1715
CA
VAL
A
227
19.790
−8.127
28.109
1.00
29.45
A


ATOM
1716
CB
VAL
A
227
18.280
−7.875
28.355
1.00
29.44
A


ATOM
1717
CG1
VAL
A
227
17.995
−7.745
29.851
1.00
27.14
A


ATOM
1718
CG2
VAL
A
227
17.856
−6.602
27.647
1.00
27.64
A


ATOM
1719
C
VAL
A
227
20.274
−9.260
29.004
1.00
30.44
A


ATOM
1720
O
VAL
A
227
20.119
−10.441
28.677
1.00
30.38
A


ATOM
1721
N
GLY
A
228
20.878
−8.891
30.129
1.00
30.00
A


ATOM
1722
CA
GLY
A
228
21.381
−9.893
31.039
1.00
30.18
A


ATOM
1723
C
GLY
A
228
21.795
−9.294
32.354
1.00
31.31
A


ATOM
1724
O
GLY
A
228
22.112
−8.109
32.433
1.00
31.60
A


ATOM
1725
N
ALA
A
229
21.774
−10.126
33.390
1.00
32.55
A


ATOM
1726
CA
ALA
A
229
22.160
−9.710
34.724
1.00
33.95
A


ATOM
1727
CB
ALA
A
229
21.252
−10.367
35.764
1.00
34.17
A


ATOM
1728
C
ALA
A
229
23.619
−10.111
34.961
1.00
35.33
A


ATOM
1729
O
ALA
A
229
24.164
−10.972
34.256
1.00
33.08
A


ATOM
1730
N
ASP
A
230
24.248
−9.465
35.942
1.00
36.86
A


ATOM
1731
CA
ASP
A
230
25.640
−9.740
36.300
1.00
39.56
A


ATOM
1732
CB
ASP
A
230
25.757
−11.083
37.044
1.00
41.40
A


ATOM
1733
CG
ASP
A
230
24.520
−11.413
37.868
1.00
43.35
A


ATOM
1734
OD1
ASP
A
230
24.054
−10.532
38.623
1.00
44.48
A


ATOM
1735
OD2
ASP
A
230
24.022
−12.560
37.767
1.00
44.89
A


ATOM
1736
C
ASP
A
230
26.532
−9.793
35.066
1.00
39.71
A


ATOM
1737
O
ASP
A
230
26.951
−10.873
34.651
1.00
39.33
A


ATOM
1738
N
PRO
A
231
26.831
−8.633
34.456
1.00
39.86
A


ATOM
1739
CD
PRO
A
231
26.381
−7.252
34.717
1.00
40.12
A


ATOM
1740
CA
PRO
A
231
27.692
−8.692
33.271
1.00
40.52
A


ATOM
1741
CB
PRO
A
231
27.573
−7.280
32.687
1.00
39.25
A


ATOM
1742
CG
PRO
A
231
27.353
−6.433
33.884
1.00
38.53
A


ATOM
1743
C
PRO
A
231
29.136
−9.073
33.629
1.00
41.54
A


ATOM
1744
O
PRO
A
231
29.692
−8.570
34.605
1.00
43.36
A


ATOM
1745
N
ILE
A
232
29.723
−9.977
32.850
1.00
41.13
A


ATOM
1746
CA
ILE
A
232
31.099
−10.420
33.062
1.00
40.68
A


ATOM
1747
CB
ILE
A
232
31.474
−11.530
32.070
1.00
40.34
A


ATOM
1748
CG2
ILE
A
232
32.886
−11.998
32.333
1.00
38.27
A


ATOM
1749
CG1
ILE
A
232
30.465
−12.675
32.178
1.00
39.77
A


ATOM
1750
CD1
ILE
A
232
30.197
−13.355
30.861
1.00
41.07
A


ATOM
1751
C
ILE
A
232
32.046
−9.236
32.843
1.00
40.67
A


ATOM
1752
O
ILE
A
232
32.089
−8.660
31.751
1.00
39.36
A


ATOM
1753
N
PRO
A
233
32.836
−8.882
33.872
1.00
41.83
A


ATOM
1754
CD
PRO
A
233
33.100
−9.709
35.064
1.00
41.56
A


ATOM
1755
CA
PRO
A
233
33.782
−7.762
33.803
1.00
42.38
A


ATOM
1756
CB
PRO
A
233
34.560
−7.888
35.108
1.00
42.80
A


ATOM
1757
CG
PRO
A
223
34.539
−9.368
35.365
1.00
42.88
A


ATOM
1758
C
PRO
A
233
34.681
−7.788
32.589
1.00
42.20
A


ATOM
1759
O
PRO
A
233
35.137
−8.844
32.172
1.00
42.50
A


ATOM
1760
N
GLN
A
234
34.914
−6.606
32.032
1.00
43.76
A


ATOM
1761
CA
GLN
A
234
35.764
−6.406
30.860
1.00
45.45
A


ATOM
1762
CB
GLN
A
234
37.245
−6.416
31.262
1.00
46.00
A


ATOM
1763
CG
GLN
A
234
37.726
−7.729
31.838
1.00
48.56
A


ATOM
1764
CD
GLN
A
234
39.175
−7.678
32.263
1.00
49.12
A


ATOM
1765
OE1
GLN
A
234
39.553
−6.892
33.128
1.00
50.98
A


ATOM
1766
NE2
GLN
A
234
39.997
−8.520
31.656
1.00
49.92
A


ATOM
1767
C
GLN
A
234
35.544
−7.394
29.726
1.00
44.87
A


ATOM
1768
O
GLN
A
234
36.397
−7.549
28.849
1.00
45.60
A


ATOM
1769
N
VAL
A
235
34.404
−8.071
29.756
1.00
44.58
A


ATOM
1770
CA
VAL
A
235
34.039
−9.028
28.720
1.00
43.67
A


ATOM
1771
CB
VAL
A
235
33.805
−10.440
29.299
1.00
44.91
A


ATOM
1772
CG1
VAL
A
235
33.227
−11.353
28.218
1.00
45.45
A


ATOM
1773
CG2
VAL
A
235
35.115
−11.010
29.822
1.00
45.12
A


ATOM
1774
C
VAL
A
235
32.743
−8.524
28.108
1.00
42.68
A


ATOM
1775
O
VAL
A
235
32.571
−8.547
26.889
1.00
42.55
A


ATOM
1776
N
GLU
A
236
31.835
−8.076
28.975
1.00
40.47
A


ATOM
1777
CA
GLU
A
236
30.547
−7.527
28.551
1.00
39.21
A


ATOM
1778
CB
GLU
A
236
29.380
−8.321
29.133
1.00
35.88
A


ATOM
1779
CG
GLU
A
236
29.437
−9.787
28.844
1.00
34.44
A


ATOM
1780
CD
GLU
A
236
28.341
−10.545
29.544
1.00
29.35
A


ATOM
1781
OE1
GLU
A
236
28.117
−10.279
30.740
1.00
28.34
A


ATOM
1782
OE2
GLU
A
236
27.718
−11.406
28.900
1.00
29.13
A


ATOM
1783
C
GLU
A
236
30.475
−6.112
29.082
1.00
39.21
A


ATOM
1784
O
GLU
A
236
30.804
−5.863
30.240
1.00
39.77
A


ATOM
1785
N
LYS
A
237
30.041
−5.188
28.236
1.00
40.00
A


ATOM
1786
CA
LYS
A
237
29.946
−3.792
28.630
1.00
38.96
A


ATOM
1787
CB
LYS
A
237
30.721
−2.934
27.631
1.00
38.86
A


ATOM
1788
CG
LYS
A
237
30.876
−1.475
28.023
1.00
41.75
A


ATOM
1789
CD
LYS
A
237
31.777
−.743
27.024
1.00
44.57
A


ATOM
1790
CE
LYS
A
237
31.936
.730
27.385
1.00
45.75
A


ATOM
1791
NZ
LYS
A
237
32.833
1.455
26.432
1.00
46.22
A


ATOM
1792
C
LYS
A
237
28.480
−3.377
28.676
1.00
38.35
A


ATOM
1793
O
LYS
A
237
27.786
−3.403
27.659
1.00
36.98
A


ATOM
1794
N
ALA
A
238
28.006
−3.019
29.865
1.00
37.12
A


ATOM
1795
CA
ALA
A
238
26.625
−2.598
30.031
1.00
35.90
A


ATOM
1796
CB
ALA
A
238
26.131
−2.956
31.421
1.00
34.13
A


ATOM
1797
C
ALA
A
238
26.549
−1.094
29.811
1.00
36.34
A


ATOM
1798
O
ALA
A
238
27.546
−.386
29.977
1.00
37.36
A


ATOM
1799
N
CYS
A
239
25.375
−.608
29.415
1.00
35.65
A


ATOM
1800
CA
CYS
A
239
25.179
.824
29.179
1.00
34.67
A


ATOM
1801
CB
CYS
A
239
25.042
1.096
27.682
1.00
34.03
A


ATOM
1802
SG
CYS
A
239
23.884
.011
26.852
1.00
39.50
A


ATOM
1803
C
CYS
A
239
23.952
1.345
29.928
1.00
32.01
A


ATOM
1804
O
CYS
A
239
23.922
2.488
30.384
1.00
29.97
A


ATOM
1805
N
PHE
A
240
22.952
.489
30.073
1.00
30.69
A


ATOM
1806
CA
PHE
A
240
21.731
.864
30.772
1.00
29.43
A


ATOM
1807
CB
PHE
A
240
20.651
1.222
29.753
1.00
27.09
A


ATOM
1808
CG
PHE
A
240
21.002
2.399
28.886
1.00
26.17
A


ATOM
1809
CD1
PHE
A
240
21.036
3.686
29.415
1.00
25.93
A


ATOM
1810
CD2
PHE
A
240
21.323
2.223
27.544
1.00
28.55
A


ATOM
1811
CE1
PHE
A
240
21.384
4.772
28.623
1.00
25.72
A


ATOM
1812
CE2
PHE
A
240
21.673
3.314
26.743
1.00
23.97
A


ATOM
1813
CZ
PHE
A
240
21.703
4.583
27.285
1.00
23.90
A


ATOM
1814
C
PHE
A
240
21.251
−.288
31.643
1.00
30.74
A


ATOM
1815
O
PHE
A
240
21.413
−1.447
31.277
1.00
32.77
A


ATOM
1816
N
GLU
A
241
20.677
.021
32.802
1.00
31.99
A


ATOM
1817
CA
GLU
A
241
20.147
−1.025
33.678
1.00
34.57
A


ATOM
1818
CB
GLU
A
241
20.852
−1.023
35.046
1.00
35.81
A


ATOM
1819
CG
GLU
A
241
22.360
−1.271
34.997
1.00
37.93
A


ATOM
1820
CD
GLU
A
241
23.006
−1.280
36.381
1.00
40.79
A


ATOM
1821
OE1
GLU
A
241
22.690
−.392
37.211
1.00
42.12
A


ATOM
1822
OE2
GLU
A
241
23.845
−2.170
36.638
1.00
42.83
A


ATOM
1823
C
GLU
A
241
18.648
−.771
33.867
1.00
34.22
A


ATOM
1824
O
GLU
A
241
18.200
.382
33.877
1.00
34.52
A


ATOM
1825
N
ILE
A
242
17.877
−1.846
34.004
1.00
34.06
A


ATOM
1826
CA
ILE
A
242
16.434
−1.733
34.196
1.00
32.84
A


ATOM
1827
CB
ILE
A
242
15.670
−2.830
33.421
1.00
32.65
A


ATOM
1828
CG2
ILE
A
242
14.229
−2.383
33.165
1.00
31.59
A


ATOM
1829
CG1
ILE
A
242
16.359
−3.113
32.089
1.00
32.73
A


ATOM
1830
CD1
ILE
A
242
16.466
−1.903
31.191
1.00
33.02
A


ATOM
1831
C
ILE
A
242
16.124
−1.891
35.683
1.00
32.33
A


ATOM
1832
O
ILE
A
242
16.073
−3.009
36.199
1.00
34.81
A


ATOM
1833
N
VAL
A
243
15.903
−.770
36.362
1.00
30.43
A


ATOM
1834
CA
VAL
A
243
15.624
−.761
37.795
1.00
27.37
A


ATOM
1835
CB
VAL
A
243
16.016
.621
38.394
1.00
28.23
A


ATOM
1836
CG1
VAL
A
243
15.188
.923
39.626
1.00
22.92
A


ATOM
1837
CG2
VAL
A
243
17.499
.632
38.740
1.00
29.02
A


ATOM
1838
C
VAL
A
243
14.196
−1.094
38.247
1.00
26.31
A


ATOM
1839
O
VAL
A
243
14.000
−1.938
39.119
1.00
25.11
A


ATOM
1840
N
TRP
A
244
13.213
−.416
37.659
1.00
26.80
A


ATOM
1841
CA
TRP
A
244
11.806
−.578
38.033
1.00
25.99
A


ATOM
1842
CB
TRP
A
244
11.459
.445
39.123
1.00
24.69
A


ATOM
1843
CG
TRP
A
244
10.085
.344
39.686
1.00
26.65
A


ATOM
1844
CD2
TRP
A
244
8.923
1.064
39.252
1.00
26.94
A


ATOM
1845
CE2
TRP
A
244
7.851
.655
40.071
1.00
28.19
A


ATOM
1846
CE3
TRP
A
244
8.684
2.012
38.249
1.00
30.14
A


ATOM
1847
CD1
TRP
A
244
9.681
−.448
40.715
1.00
27.61
A


ATOM
1848
NE1
TRP
A
244
8.342
−.269
40.956
1.00
27.74
A


ATOM
1849
CZ2
TRP
A
244
6.554
1.163
39.923
1.00
29.62
A


ATOM
1850
CZ3
TRP
A
244
7.387
2.517
38.100
1.00
31.77
A


ATOM
1851
CH2
TRP
A
244
6.344
2.089
38.935
1.00
30.68
A


ATOM
1852
C
TRP
A
244
10.930
−.360
36.803
1.00
25.64
A


ATOM
1853
O
TRP
A
244
11.230
.499
35.968
1.00
24.94
A


ATOM
1854
N
THR
A
245
9.837
−1.117
36.712
1.00
25.35
A


ATOM
1855
CA
THR
A
245
8.946
−1.064
35.554
1.00
25.32
A


ATOM
1856
CB
THR
A
245
9.110
−2.349
34.743
1.00
26.48
A


ATOM
1857
OG1
THR
A
245
8.406
−2.238
33.509
1.00
28.56
A


ATOM
1858
CG2
THR
A
245
8.551
−3.538
35.532
1.00
25.04
A


ATOM
1859
C
THR
A
245
7.455
−.904
35.888
1.00
25.82
A


ATOM
1860
O
THR
A
245
7.029
−1.132
37.024
1.00
24.99
A


ATOM
1861
N
ALA
A
246
6.665
−.524
34.885
1.00
24.85
A


ATOM
1862
CA
ALA
A
246
5.228
−.346
35.067
1.00
23.46
A


ATOM
1863
CB
ALA
A
246
4.957
.788
36.061
1.00
26.77
A


ATOM
1864
C
ALA
A
246
4.493
−.073
33.757
1.00
23.79
A


ATOM
1865
O
ALA
A
246
5.073
.412
32.783
1.00
22.48
A


ATOM
1866
N
GLN
A
247
3.205
−.394
33.754
1.00
23.39
A


ATOM
1867
CA
GLN
A
247
2.326
−.210
32.601
1.00
25.65
A


ATOM
1868
CB
GLN
A
247
2.155
−1.531
31.835
1.00
24.53
A


ATOM
1869
CG
GLN
A
247
1.151
−1.473
30.682
1.00
24.31
A


ATOM
1870
CD
GLN
A
247
.838
−2.843
30.074
1.00
22.11
A


ATOM
1871
OE1
GLN
A
247
.257
−3.709
30.726
1.00
23.16
A


ATOM
1872
NE2
GLN
A
247
1.224
−3.036
28.825
1.00
20.77
A


ATOM
1873
C
GLN
A
247
.984
.220
33.170
1.00
27.26
A


ATOM
1874
O
GLN
A
247
.569
−.263
34.222
1.00
28.63
A


ATOM
1875
N
THR
A
248
.295
1.125
32.494
1.00
28.56
A


ATOM
1876
CA
THR
A
248
−.988
1.567
33.017
1.00
28.92
A


ATOM
1877
CB
THR
A
248
−.797
2.755
33.987
1.00
30.79
A


ATOM
1878
OG1
THR
A
248
−1.944
2.862
34.842
1.00
35.24
A


ATOM
1879
CG2
THR
A
248
−.615
4.060
33.211
1.00
31.01
A


ATOM
1880
C
THR
A
248
−1.953
1.977
31.916
1.00
27.53
A


ATOM
1881
O
THR
A
248
−1.539
2.318
30.812
1.00
25.84
A


ATOM
1882
N
VAL
A
249
−3.241
1.925
32.226
1.00
25.93
A


ATOM
1883
CA
VAL
A
249
−4.272
2.318
31.279
1.00
27.96
A


ATOM
1884
CB
VAL
A
249
−5.407
1.288
31.251
1.00
28.05
A


ATOM
1885
CG1
VAL
A
249
−6.550
1.797
30.397
1.00
27.80
A


ATOM
1886
CG2
VAL
A
249
−4.884
−.038
30.713
1.00
28.94
A


ATOM
1887
C
VAL
A
249
−4.825
3.679
31.713
1.00
27.45
A


ATOM
1888
O
VAL
A
249
−5.378
3.810
32.805
1.00
26.81
A


ATOM
1889
N
VAL
A
250
−4.652
4.700
30.880
1.00
27.86
A


ATOM
1890
CA
VAL
A
250
−5.153
6.018
31.254
1.00
28.83
A


ATOM
1891
CB
VAL
A
250
−4.656
7.129
30.318
1.00
28.90
A


ATOM
1892
CG1
VAL
A
250
−3.192
7.416
30.593
1.00
29.74
A


ATOM
1893
CG2
VAL
A
250
−4.834
6.717
28.889
1.00
30.61
A


ATOM
1894
C
VAL
A
250
−6.670
5.968
31.235
1.00
28.87
A


ATOM
1895
O
VAL
A
250
−7.274
5.444
30.301
1.00
27.18
A


ATOM
1896
N
PRO
A
251
−7.302
6.513
32.283
1.00
28.95
A


ATOM
1897
CD
PRO
A
251
−6.680
7.371
33.302
1.00
27.77
A


ATOM
1898
CA
PRO
A
251
−8.760
6.530
32.405
1.00
30.93
A


ATOM
1899
CB
PRO
A
251
−8.991
7.390
33.643
1.00
28.74
A


ATOM
1900
CG
PRO
A
251
−7.799
8.286
33.662
1.00
30.42
A


ATOM
1901
C
PRO
A
251
−9.479
7.053
31.168
1.00
33.62
A


ATOM
1902
O
PRO
A
251
−8.942
7.863
30.409
1.00
34.58
A


ATOM
1903
N
ASN
A
252
−10.692
6.550
30.970
1.00
36.56
A


ATOM
1904
CA
ASN
A
252
−11.546
6.917
29.851
1.00
38.78
A


ATOM
1905
CB
ASN
A
252
−12.471
8.052
30.291
1.00
40.73
A


ATOM
1906
CG
ASN
A
252
−13.412
8.486
29.198
1.00
44.33
A


ATOM
1907
OD1
ASN
A
252
−13.037
9.262
28.321
1.00
46.53
A


ATOM
1908
ND2
ASN
A
252
−14.642
7.978
29.232
1.00
45.05
A


ATOM
1909
C
ASN
A
252
−10.776
7.295
28.579
1.00
38.09
A


ATOM
1910
O
ASN
A
252
−10.867
8.427
28.106
1.00
38.27
A


ATOM
1911
N
SER
A
253
−10.044
6.331
28.016
1.00
36.57
A


ATOM
1912
CA
SER
A
253
−9.236
6.568
26.816
1.00
36.26
A


ATOM
1913
CB
SER
A
253
−7.775
6.719
27.216
1.00
34.68
A


ATOM
1914
OG
SER
A
253
−7.312
5.503
27.778
1.00
32.19
A


ATOM
1915
C
SER
A
253
−9.329
5.455
25.761
1.00
36.96
A


ATOM
1916
O
SER
A
253
−8.391
5.232
24.998
1.00
36.84
A


ATOM
1917
N
GLU
A
254
−10.455
4.762
25.719
1.00
37.92
A


ATOM
1918
CA
GLU
A
254
−10.658
3.678
24.766
1.00
38.18
A


ATOM
1919
CB
GLU
A
254
−11.874
2.865
25.196
1.00
40.81
A


ATOM
1920
CG
GLU
A
254
−11.709
1.362
25.110
1.00
44.37
A


ATOM
1921
CD
GLU
A
254
−12.993
.637
25.461
1.00
44.94
A


ATOM
1922
OE1
GLU
A
254
−13.494
.833
26.591
1.00
46.54
A


ATOM
1923
OE2
GLU
A
254
−13.507
−.118
24.607
1.00
45.46
A


ATOM
1924
C
GLU
A
254
−10.872
4.196
23.342
1.00
37.96
A


ATOM
1925
O
GLU
A
254
−11.532
5.217
23.127
1.00
34.76
A


ATOM
1926
N
GLY
A
255
−10.319
3.479
22.368
1.00
35.90
A


ATOM
1927
CA
GLY
A
255
−10.487
3.881
20.985
1.00
34.05
A


ATOM
1928
C
GLY
A
255
−9.532
4.966
20.536
1.00
33.62
A


ATOM
1929
O
GLY
A
255
−9.456
5.283
19.348
1.00
34.14
A


ATOM
1930
N
ALA
A
256
−8.806
5.549
21.482
1.00
32.67
A


ATOM
1931
CA
ALA
A
256
−7.844
6.588
21.145
1.00
31.58
A


ATOM
1932
CB
ALA
A
256
−7.138
7.081
22.399
1.00
30.56
A


ATOM
1933
C
ALA
A
256
−6.840
6.001
20.169
1.00
30.51
A


ATOM
1934
O
ALA
A
256
−6.523
6.610
19.155
1.00
32.75
A


ATOM
1935
N
ILE
A
257
−6.348
4.808
20.482
1.00
29.54
A


ATOM
1936
CA
ILE
A
257
−5.383
4.115
19.635
1.00
28.79
A


ATOM
1937
CB
ILE
A
257
−3.971
4.131
20.255
1.00
28.12
A


ATOM
1938
CG2
ILE
A
257
−2.973
3.501
19.300
1.00
28.32
A


ATOM
1939
CG1
ILE
A
257
−3.553
5.567
20.566
1.00
26.99
A


ATOM
1940
CD1
ILE
A
257
−2.172
5.686
21.172
1.00
22.94
A


ATOM
1941
C
ILE
A
257
−5.829
2.662
19.477
1.00
29.98
A


ATOM
1942
O
ILE
A
257
−6.128
1.976
20.457
1.00
31.42
A


ATOM
1943
N
GLY
A
258
−5.882
2.193
18.239
1.00
31.11
A


ATOM
1944
CA
GLY
A
258
−6.300
.826
18.003
1.00
27.25
A


ATOM
1945
C
GLY
A
258
−6.105
.422
16.561
1.00
27.85
A


ATOM
1946
O
GLY
A
258
−5.851
1.259
15.682
1.00
24.88
A


ATOM
1947
N
GLY
A
259
−6.223
−.879
16.324
1.00
26.06
A


ATOM
1948
CA
GLY
A
259
−6.054
−1.401
14.987
1.00
24.94
A


ATOM
1949
C
GLY
A
259
−6.788
−2.709
14.848
1.00
25.74
A


ATOM
1950
O
GLY
A
259
−6.904
−3.474
15.804
1.00
27.81
A


ATOM
1951
N
LYS
A
260
−7.280
−2.972
13.648
1.00
24.91
A


ATOM
1952
CA
LYS
A
260
−8.022
−4.191
13.392
1.00
24.18
A


ATOM
1953
CB
LYS
A
260
−9.468
−3.834
13.058
1.00
23.37
A


ATOM
1954
CG
LYS
A
260
−10.120
−2.976
14.105
1.00
21.02
A


ATOM
1955
CD
LYS
A
260
−11.477
−2.506
13.624
1.00
27.51
A


ATOM
1956
CE
LYS
A
260
−12.267
−1.873
14.757
1.00
27.39
A


ATOM
1957
NZ
LYS
A
260
−12.506
−2.874
15.835
1.00
30.72
A


ATOM
1958
C
LYS
A
260
−7.402
−4.988
12.256
1.00
23.16
A


ATOM
1959
O
LYS
A
260
−7.139
−4.452
11.185
1.00
26.09
A


ATOM
1960
N
VAL
A
261
−7.152
−6.265
12.496
1.00
22.53
A


ATOM
1961
CA
VAL
A
261
−6.581
−7.112
11.458
1.00
22.47
A


ATOM
1962
CB
VAL
A
261
−5.764
−8.275
12.056
1.00
22.44
A


ATOM
1963
CG1
VAL
A
261
−5.339
−9.236
10.954
1.00
24.43
A


ATOM
1964
CG2
VAL
A
261
−4.526
−7.728
12.759
1.00
23.17
A


ATOM
1965
C
VAL
A
261
−7.748
−7.640
10.645
1.00
21.55
A


ATOM
1966
O
VAL
A
261
−8.525
−8.473
11.109
1.00
20.82
A


ATOM
1967
N
ARG
A
262
−7.880
−7.126
9.428
1.00
21.55
A


ATOM
1968
CA
ARG
A
262
−8.982
−7.514
8.564
1.00
22.38
A


ATOM
1969
CB
ARG
A
262
−9.961
−6.344
8.452
1.00
21.69
A


ATOM
1970
CG
ARG
A
262
−10.631
−5.983
9.766
1.00
21.51
A


ATOM
1971
CD
ARG
A
262
−11.517
−7.128
10.288
1.00
22.91
A


ATOM
1972
NE
ARG
A
262
−12.241
−6.748
11.501
1.00
23.25
A


ATOM
1973
CZ
ARG
A
262
−11.766
−6.836
12.740
1.00
24.30
A


ATOM
1974
NH1
ARG
A
262
−10.547
−7.315
12.972
1.00
21.08
A


ATOM
1975
NH2
ARG
A
262
−12.502
−6.398
13.753
1.00
24.59
A


ATOM
1976
C
ARG
A
262
−8.555
−7.997
7.178
1.00
22.47
A


ATOM
1977
O
ARG
A
262
−7.366
−8.019
6.852
1.00
22.56
A


ATOM
1978
N
GLU
A
263
−9.525
−8.392
6.364
1.00
21.88
A


ATOM
1979
CA
GLU
A
263
−9.207
−8.888
5.035
1.00
22.36
A


ATOM
1980
CB
GLU
A
263
−10.481
−9.388
4.355
1.00
22.82
A


ATOM
1981
CG
GLU
A
263
−11.010
−10.653
5.037
1.00
28.67
A


ATOM
1982
CD
GLU
A
263
−12.505
−10.893
4.844
1.00
33.40
A


ATOM
1983
OE1
GLU
A
263
−13.067
−11.739
5.577
1.00
32.78
A


ATOM
1984
OE2
GLU
A
263
−13.120
−10.249
3.961
1.00
37.42
A


ATOM
1985
C
GLU
A
263
−8.486
−7.831
4.203
1.00
22.25
A


ATOM
1986
O
GLU
A
263
−7.881
−8.145
3.173
1.00
18.80
A


ATOM
1987
N
VAL
A
264
−8.530
−6.579
4.661
1.00
21.62
A


ATOM
1988
CA
VAL
A
264
−7.835
−5.508
3.955
1.00
21.09
A


ATOM
1989
CB
VAL
A
264
−8.650
−4.211
3.935
1.00
22.68
A


ATOM
1990
CG1
VAL
A
264
−9.941
−4.419
3.158
1.00
23.99
A


ATOM
1991
CG2
VAL
A
264
−8.929
−3.758
5.355
1.00
21.59
A


ATOM
1992
C
VAL
A
264
−6.500
−5.222
4.630
1.00
20.86
A


ATOM
1993
O
VAL
A
264
−5.816
−4.249
4.292
1.00
19.04
A


ATOM
1994
N
GLY
A
265
−6.135
−6.077
5.583
1.00
20.38
A


ATOM
1995
CA
GLY
A
265
−4.896
−5.897
6.314
1.00
22.57
A


ATOM
1996
C
GLY
A
265
−5.141
−5.198
7.641
1.00
24.13
A


ATOM
1997
O
GLY
A
265
−6.258
−5.210
8.154
1.00
24.25
A


ATOM
1998
N
LEU
A
266
−4.109
−4.575
8.195
1.00
24.55
A


ATOM
1999
CA
LEU
A
266
−4.257
−3.900
9.476
1.00
27.01
A


ATOM
2000
CB
LEU
A
266
−2.935
−3.923
10.259
1.00
26.32
A


ATOM
2001
CG
LEU
A
266
−2.987
−4.172
11.779
1.00
28.57
A


ATOM
2002
CD1
LEU
A
266
−1.872
−3.374
12.425
1.00
25.69
A


ATOM
2003
CD2
LEU
A
266
−4.335
−3.764
12.389
1.00
25.63
A


ATOM
2004
C
LEU
A
266
−4.712
−2.457
9.301
1.00
28.29
A


ATOM
2005
O
LEU
A
266
−3.964
−1.618
8.809
1.00
27.00
A


ATOM
2006
N
THR
A
267
−5.951
−2.182
9.689
1.00
29.50
A


ATOM
2007
CA
THR
A
267
−6.485
−.836
9.608
1.00
30.44
A


ATOM
2008
CB
THR
A
267
−8.022
−.825
9.574
1.00
29.41
A


ATOM
2009
OG1
THR
A
267
−8.541
−1.701
10.579
1.00
28.88
A


ATOM
2010
CG2
THR
A
267
−8.512
−1.271
8.220
1.00
31.59
A


ATOM
2011
C
THR
A
267
−5.990
−.143
10.861
1.00
32.37
A


ATOM
2012
O
THR
A
267
−5.475
−.790
11.762
1.00
32.42
A


ATOM
2013
N
PHE
A
268
−6.153
1.168
10.931
1.00
34.52
A


ATOM
2014
CA
PHE
A
268
−5.646
1.909
12.076
1.00
37.28
A


ATOM
2015
CB
PHE
A
268
−4.208
2.318
11.770
1.00
35.84
A


ATOM
2016
CG
PHE
A
268
−3.713
3.443
12.595
1.00
36.17
A


ATOM
2017
CD1
PHE
A
268
−3.373
3.249
13.927
1.00
38.58
A


ATOM
2018
CD2
PHE
A
268
−3.576
4.709
12.039
1.00
36.83
A


ATOM
2019
CE1
PHE
A
268
−2.895
4.309
14.700
1.00
39.39
A


ATOM
2020
CE2
PHE
A
268
−3.104
5.771
12.798
1.00
37.60
A


ATOM
2021
CZ
PHE
A
268
−2.762
5.573
14.129
1.00
38.49
A


ATOM
2022
C
PHE
A
268
−6.479
3.137
12.430
1.00
38.24
A


ATOM
2023
O
PHE
A
268
−6.645
4.041
11.613
1.00
38.90
A


ATOM
2024
N
GLN
A
269
−7.000
3.157
13.655
1.00
39.85
A


ATOM
2025
CA
GLN
A
269
−7.805
4.274
14.138
1.00
40.66
A


ATOM
2026
CB
GLN
A
269
−9.084
3.760
14.815
1.00
40.42
A


ATOM
2027
CG
GLN
A
269
−8.836
2.678
15.859
1.00
43.55
A


ATOM
2028
CD
GLN
A
269
−8.868
1.271
15.277
1.00
45.56
A


ATOM
2029
OE1
GLN
A
269
−8.456
1.043
14.135
1.00
43.46
A


ATOM
2030
NE2
GLN
A
269
−9.349
.316
16.069
1.00
44.36
A


ATOM
2031
C
GLN
A
269
−6.957
5.068
15.130
1.00
41.21
A


ATOM
2032
O
GLN
A
269
−6.235
4.482
15.938
1.00
41.66
A


ATOM
2033
N
LEU
A
270
−7.041
6.396
15.061
1.00
41.43
A


ATOM
2034
CA
LEU
A
270
−6.263
7.264
15.944
1.00
41.35
A


ATOM
2035
CB
LEU
A
270
−4.927
7.598
15.273
1.00
40.81
A


ATOM
2036
CG
LEU
A
270
−3.927
8.500
15.991
1.00
42.32
A


ATOM
2037
CD1
LEU
A
270
−3.581
7.908
17.338
1.00
43.04
A


ATOM
2038
CD2
LEU
A
270
−2.675
8.642
15.142
1.00
41.53
A


ATOM
2039
C
LEU
A
270
−7.007
8.555
16.283
1.00
41.06
A


ATOM
2040
O
LEU
A
270
−6.881
9.554
15.575
1.00
44.11
A


ATOM
2041
N
LYS
A
271
−7.786
8.540
17.358
1.00
38.77
A


ATOM
2042
CA
LYS
A
271
−8.537
9.730
17.762
1.00
37.60
A


ATOM
2043
CB
LYS
A
271
−9.392
9.420
18.999
1.00
36.95
A


ATOM
2044
CG
LYS
A
271
−10.504
8.407
18.714
1.00
38.43
A


ATOM
2045
CD
LYS
A
271
−11.337
8.048
19.940
1.00
37.75
A


ATOM
2046
CE
LYS
A
271
−12.440
7.055
19.555
1.00
40.27
A


ATOM
2047
NZ
LYS
A
271
−13.165
6.457
20.723
1.00
42.36
A


ATOM
2048
C
LYS
A
271
−7.577
10.888
18.053
1.00
35.81
A


ATOM
2049
O
LYS
A
271
−6.477
10.682
18.557
1.00
34.82
A


ATOM
2050
N
GLY
A
272
−7.998
12.105
17.724
1.00
34.36
A


ATOM
2051
CA
GLY
A
272
−7.159
13.269
17.955
1.00
32.41
A


ATOM
2052
C
GLY
A
272
−6.859
13.596
19.412
1.00
31.39
A


ATOM
2053
O
GLY
A
272
−5.909
14.324
19.701
1.00
30.50
A


ATOM
2054
N
ALA
A
273
−7.646
13.053
20.335
1.00
30.16
A


ATOM
2055
CA
ALA
A
273
−7.442
13.316
21.758
1.00
30.25
A


ATOM
2056
CB
ALA
A
273
−8.680
12.896
22.527
1.00
28.04
A


ATOM
2057
C
ALA
A
273
−6.193
12.667
22.391
1.00
30.52
A


ATOM
2058
O
ALA
A
273
−5.906
12.886
23.572
1.00
31.69
A


ATOM
2059
N
VAL
A
274
−5.449
11.888
21.613
1.00
29.09
A


ATOM
2060
CA
VAL
A
274
−4.255
11.197
22.124
1.00
30.02
A


ATOM
2061
CB
VAL
A
274
−3.574
10.349
20.994
1.00
29.02
A


ATOM
2062
CG1
VAL
A
274
−2.120
10.066
21.328
1.00
26.26
A


ATOM
2063
CG2
VAL
A
274
−4.324
9.029
20.829
1.00
28.14
A


ATOM
2064
C
VAL
A
274
−3.185
12.040
22.832
1.00
29.91
A


ATOM
2065
O
VAL
A
274
−2.706
11.667
23.908
1.00
31.11
A


ATOM
2066
N
PRO
A
275
−2.785
13.174
22.246
1.00
29.31
A


ATOM
2067
CD
PRO
A
275
−3.039
13.717
20.903
1.00
28.93
A


ATOM
2068
CA
PRO
A
275
−1.759
13.959
22.943
1.00
29.97
A


ATOM
2069
CB
PRO
A
275
−1.536
15.141
22.009
1.00
29.08
A


ATOM
2070
CG
PRO
A
275
−1.794
14.543
20.662
1.00
30.30
A


ATOM
2071
C
PRO
A
275
−2.170
14.391
24.348
1.00
30.48
A


ATOM
2072
O
PRO
A
275
−1.355
14.376
25.271
1.00
31.35
A


ATOM
2073
N
ASP
A
276
−3.439
14.752
24.514
1.00
31.00
A


ATOM
2074
CA
ASP
A
276
−3.931
15.197
25.810
1.00
31.59
A


ATOM
2075
CB
ASP
A
276
−5.286
15.885
25.661
1.00
34.05
A


ATOM
2076
CG
ASP
A
276
−5.849
16.327
26.993
1.00
35.35
A


ATOM
2077
OD1
ASP
A
276
−5.196
17.162
27.658
1.00
36.13
A


ATOM
2078
OD2
ASP
A
276
−6.927
15.829
27.384
1.00
36.47
A


ATOM
2079
C
ASP
A
276
−4.060
14.089
26.838
1.00
31.20
A


ATOM
2080
O
ASP
A
276
−3.790
14.299
28.016
1.00
31.91
A


ATOM
2081
N
LEU
A
277
−4.492
12.913
26.400
1.00
32.16
A


ATOM
2082
CA
LEU
A
277
−4.646
11.777
27.303
1.00
31.43
A


ATOM
2083
CB
LEU
A
277
−5.261
10.598
26.547
1.00
30.50
A


ATOM
2084
CG
LEU
A
277
−6.689
10.892
26.089
1.00
30.10
A


ATOM
2085
CD1
LEU
A
277
−7.184
9.828
25.132
1.00
30.66
A


ATOM
2086
CD2
LEU
A
277
−7.582
10.971
27.310
1.00
30.85
A


ATOM
2087
C
LEU
A
277
−3.298
11.381
27.903
1.00
31.68
A


ATOM
2088
O
LEU
A
277
−3.166
11.214
29.114
1.00
31.00
A


ATOM
2089
N
ILE
A
278
−2.294
11.243
27.048
1.00
32.33
A


ATOM
2090
CA
ILE
A
278
−.962
10.887
27.502
1.00
32.96
A


ATOM
2091
CB
ILE
A
278
−.013
10.649
26.300
1.00
30.68
A


ATOM
2092
CG2
ILE
A
278
1.422
10.523
26.777
1.00
28.01
A


ATOM
2093
CG1
ILE
A
278
−.456
9.391
25.547
1.00
29.23
A


ATOM
2094
CD1
ILE
A
278
.283
9.139
24.250
1.00
29.89
A


ATOM
2095
C
ILE
A
278
−.378
11.966
28.406
1.00
34.32
A


ATOM
2096
O
ILE
A
278
.168
11.657
29.455
1.00
34.80
A


ATOM
2097
N
SER
A
279
−.517
13.229
28.011
1.00
36.66
A


ATOM
2098
CA
SER
A
279
.025
14.351
28.790
1.00
37.98
A


ATOM
2099
CB
SER
A
279
−.114
15.663
28.002
1.00
40.15
A


ATOM
2100
OG
SER
A
279
.917
15.792
27.031
1.00
41.42
A


ATOM
2101
C
SER
A
279
−.550
14.562
30.186
1.00
37.84
A


ATOM
2102
O
SER
A
279
.193
14.762
31.151
1.00
38.76
A


ATOM
2103
N
ALA
A
280
−1.870
14.527
30.294
1.00
36.55
A


ATOM
2104
CA
ALA
A
280
−2.530
14.749
31.572
1.00
34.53
A


ATOM
2105
CB
ALA
A
280
−3.977
15.142
31.335
1.00
34.08
A


ATOM
2106
C
ALA
A
280
−2.471
13.547
32.490
1.00
35.22
A


ATOM
2107
O
ALA
A
280
−3.258
13.450
33.432
1.00
35.65
A


ATOM
2108
N
ASN
A
281
−1.551
12.626
32.220
1.00
34.56
A


ATOM
2109
CA
ASN
A
281
−1.418
11.437
33.045
1.00
33.77
A


ATOM
2110
CB
ASN
A
281
−2.257
10.309
32.459
1.00
35.68
A


ATOM
2111
CG
ASN
A
281
−3.730
10.602
32.520
1.00
36.67
A


ATOM
2112
OD1
ASN
A
281
−4.386
10.347
33.529
1.00
37.02
A


ATOM
2113
ND2
ASN
A
281
−4.258
11.169
31.447
1.00
37.77
A


ATOM
2114
C
ASN
A
281
.017
10.963
33.187
1.00
34.57
A


ATOM
2115
O
ASN
A
281
.323
10.141
34.057
1.00
33.59
A


ATOM
2116
N
ILE
A
282
.900
11.476
32.339
1.00
34.05
A


ATOM
2117
CA
ILE
A
282
2.291
11.057
32.383
1.00
36.36
A


ATOM
2118
CB
ILE
A
282
3.060
11.550
31.128
1.00
36.30
A


ATOM
2119
CG2
ILE
A
282
3.278
13.054
31.197
1.00
35.15
A


ATOM
2120
CG1
ILE
A
282
4.388
10.803
31.010
1.00
36.39
A


ATOM
2121
CD1
ILE
A
282
5.063
10.962
29.679
1.00
35.07
A


ATOM
2122
C
ILE
A
282
2.976
11.540
33.661
1.00
39.22
A


ATOM
2123
O
ILE
A
282
3.876
10.874
34.183
1.00
40.83
A


ATOM
2124
N
GLU
A
283
2.534
12.687
34.172
1.00
38.71
A


ATOM
2125
CA
GLU
A
283
3.095
13.251
35.395
1.00
38.20
A


ATOM
2126
CB
GLU
A
283
2.403
14.586
35.710
1.00
39.81
A


ATOM
2127
CG
GLU
A
283
2.918
15.313
36.936
1.00
41.71
A


ATOM
2128
CD
GLU
A
283
4.340
15.821
36.761
1.00
46.24
A


ATOM
2129
OE1
GLU
A
283
4.717
16.782
37.472
1.00
45.68
A


ATOM
2130
OE2
GLU
A
283
5.079
15.260
35.915
1.00
46.93
A


ATOM
2131
C
GLU
A
283
2.868
12.260
36.535
1.00
37.62
A


ATOM
2132
O
GLU
A
283
3.760
11.988
37.340
1.00
37.84
A


ATOM
2133
N
ASN
A
284
1.654
11.726
36.579
1.00
37.45
A


ATOM
2134
CA
ASN
A
284
1.237
10.757
37.584
1.00
36.64
A


ATOM
2135
CB
ASN
A
284
−.211
10.353
37.300
1.00
38.10
A


ATOM
2136
CG
ASN
A
284
−.766
9.388
38.322
1.00
40.96
A


ATOM
2137
OD1
ASN
A
284
−1.919
8.971
38.219
1.00
43.35
A


ATOM
2138
ND2
ASN
A
284
.042
9.028
39.316
1.00
41.64
A


ATOM
2139
C
ASN
A
284
2.138
9.522
37.567
1.00
36.15
A


ATOM
2140
O
ASN
A
284
2.421
8.932
38.606
1.00
34.35
A


ATOM
2141
N
CYS
A
285
2.582
9.136
36.377
1.00
35.52
A


ATOM
2142
CA
CYS
A
285
3.449
7.977
36.232
1.00
37.87
A


ATOM
2143
CB
CYS
A
285
3.511
7.556
34.764
1.00
39.05
A


ATOM
2144
SG
CYS
A
285
1.908
7.052
34.114
1.00
43.04
A


ATOM
2145
C
CYS
A
285
4.858
8.242
36.761
1.00
36.43
A


ATOM
2146
O
CYS
A
285
5.515
7.339
37.268
1.00
36.47
A


ATOM
2147
N
MET
A
286
5.309
9.486
36.649
1.00
35.56
A


ATOM
2148
CA
MET
A
286
6.639
9.860
37.118
1.00
34.53
A


ATOM
2149
CB
MET
A
286
7.033
11.227
36.566
1.00
29.51
A


ATOM
2150
CG
MET
A
286
7.148
11.285
35.060
1.00
27.11
A


ATOM
2151
SD
MET
A
286
8.518
10.331
34.419
1.00
17.52
A


ATOM
2152
CE
MET
A
286
9.910
11.357
34.834
1.00
24.72
A


ATOM
2153
C
MET
A
286
6.725
9.892
38.641
1.00
34.62
A


ATOM
2154
O
MET
A
286
7.770
9.561
39.206
1.00
34.71
A


ATOM
2155
N
VAL
A
287
5.639
10.292
39.305
1.00
34.59
A


ATOM
2156
CA
VAL
A
287
5.648
10.352
40.764
1.00
34.53
A


ATOM
2157
CB
VAL
A
287
4.551
11.294
41.337
1.00
33.53
A


ATOM
2158
CG1
VAL
A
287
4.518
12.594
40.551
1.00
32.05
A


ATOM
2159
CG2
VAL
A
287
3.198
10.602
41.339
1.00
33.56
A


ATOM
2160
C
VAL
A
287
5.448
8.964
41.348
1.00
36.11
A


ATOM
2161
O
VAL
A
287
5.612
8.764
42.551
1.00
38.82
A


ATOM
2162
N
GLU
A
288
5.087
8.011
40.490
1.00
37.10
A


ATOM
2163
CA
GLU
A
288
4.879
6.630
40.912
1.00
36.49
A


ATOM
2164
CB
GLU
A
288
3.735
5.994
40.121
1.00
37.81
A


ATOM
2165
CG
GLU
A
288
2.351
6.394
40.608
1.00
41.70
A


ATOM
2166
CD
GLU
A
288
1.246
5.589
39.945
1.00
43.46
A


ATOM
2167
OE1
GLU
A
288
.071
5.752
40.335
1.00
42.08
A


ATOM
2168
OE2
GLU
A
288
1.555
4.791
39.032
1.00
45.61
A


ATOM
2169
C
GLU
A
288
6.154
5.812
40.724
1.00
34.02
A


ATOM
2170
O
GLU
A
288
6.383
4.826
41.417
1.00
35.06
A


ATOM
2171
N
ALA
A
289
6.988
6.243
39.792
1.00
32.31
A


ATOM
2172
CA
ALA
A
289
8.229
5.553
39.504
1.00
34.35
A


ATOM
2173
CB
ALA
A
289
8.374
5.370
38.005
1.00
32.96
A


ATOM
2174
C
ALA
A
289
9.464
6.259
40.043
1.00
35.81
A


ATOM
2175
O
ALA
A
289
10.570
5.746
39.895
1.00
36.21
A


ATOM
2176
N
PHE
A
290
9.303
7.422
40.672
1.00
37.04
A


ATOM
2177
CA
PHE
A
290
10.480
8.126
41.163
1.00
38.53
A


ATOM
2178
CB
PHE
A
290
10.824
9.258
40.196
1.00
37.84
A


ATOM
2179
CG
PHE
A
290
11.510
8.785
38.945
1.00
37.15
A


ATOM
2180
CD1
PHE
A
290
12.854
8.420
38.971
1.00
35.74
A


ATOM
2181
CD2
PHE
A
290
10.808
8.675
37.746
1.00
36.63
A


ATOM
2182
CE1
PHE
A
290
13.488
7.950
37.822
1.00
35.20
A


ATOM
2183
CE2
PHE
A
290
11.431
8.207
36.592
1.00
34.21
A


ATOM
2184
CZ
PHE
A
290
12.772
7.843
36.631
1.00
35.84
A


ATOM
2185
C
PHE
A
290
10.510
8.643
42.600
1.00
39.68
A


ATOM
2186
O
PHE
A
290
11.593
8.932
43.129
1.00
38.64
A


ATOM
2187
N
SER
A
291
9.352
8.768
43.238
1.00
40.39
A


ATOM
2188
CA
SER
A
291
9.340
9.240
44.615
1.00
41.28
A


ATOM
2189
CB
SER
A
291
7.902
9.336
45.138
1.00
41.61
A


ATOM
2190
OG
SER
A
291
7.321
8.052
45.305
1.00
42.21
A


ATOM
2191
C
SER
A
291
10.153
8.248
45.461
1.00
41.72
A


ATOM
2192
O
SER
A
291
10.838
8.634
46.411
1.00
41.43
A


ATOM
2193
N
GLN
A
292
10.078
6.970
45.088
1.00
41.71
A


ATOM
2194
CA
GLN
A
292
10.798
5.899
45.776
1.00
41.58
A


ATOM
2195
CB
GLN
A
292
10.393
4.537
45.198
1.00
41.30
A


ATOM
2196
CG
GLN
A
292
10.805
4.334
43.744
1.00
43.26
A


ATOM
2197
CD
GLN
A
292
10.166
3.102
43.106
1.00
43.82
A


ATOM
2198
OE1
GLN
A
292
10.242
1.992
43.644
1.00
44.70
A


ATOM
2199
NE2
GLN
A
292
9.538
3.295
41.943
1.00
43.31
A


ATOM
2200
C
GLN
A
292
12.312
6.090
45.642
1.00
41.07
A


ATOM
2201
O
GLN
A
292
13.095
5.469
46.365
1.00
40.68
A


ATOM
2202
N
PHE
A
293
12.717
6.944
44.708
1.00
40.42
A


ATOM
2203
CA
PHE
A
293
14.129
7.232
44.498
1.00
40.51
A


ATOM
2204
CB
PHE
A
293
14.511
7.016
43.033
1.00
39.74
A


ATOM
2205
CG
PHE
A
293
14.218
5.639
42.543
1.00
39.95
A


ATOM
2206
CD1
PHE
A
293
14.845
4.543
43.113
1.00
38.79
A


ATOM
2207
CD2
PHE
A
293
13.273
5.429
41.548
1.00
40.76
A


ATOM
2208
CE1
PHE
A
293
14.533
3.258
42.702
1.00
40.38
A


ATOM
2209
CE2
PHE
A
293
12.955
4.146
41.131
1.00
38.84
A


ATOM
2210
CZ
PHE
A
293
13.584
3.061
41.710
1.00
39.21
A


ATOM
2211
C
PHE
A
293
14.369
8.676
44.900
1.00
40.43
A


ATOM
2212
O
PHE
A
293
15.233
9.353
44.351
1.00
41.10
A


ATOM
2213
N
LYS
A
294
13.589
9.126
45.876
1.00
41.39
A


ATOM
2214
CA
LYS
A
294
13.673
10.482
46.396
1.00
42.03
A


ATOM
2215
CB
LYS
A
294
14.806
10.593
47.425
1.00
42.52
A


ATOM
2216
CG
LYS
A
294
16.217
10.478
46.856
1.00
44.37
A


ATOM
2217
CD
LYS
A
294
17.124
11.572
47.438
1.00
46.80
A


ATOM
2218
CE
LYS
A
294
18.469
11.658
46.725
1.00
46.23
A


ATOM
2219
NZ
LYS
A
294
19.268
12.839
47.195
1.00
46.98
A


ATOM
2220
C
LYS
A
294
13.893
11.502
45.285
1.00
42.25
A


ATOM
2221
O
LYS
A
294
14.693
12.423
45.435
1.00
42.94
A


ATOM
2222
N
ILE
A
295
13.182
11.345
44.171
1.00
42.75
A


ATOM
2223
CA
ILE
A
295
13.318
12.281
43.058
1.00
43.31
A


ATOM
2224
CB
ILE
A
295
13.915
11.616
41.814
1.00
42.40
A


ATOM
2225
CG2
ILE
A
295
13.899
12.598
40.657
1.00
42.02
A


ATOM
2226
CG1
ILE
A
295
15.351
11.165
42.092
1.00
42.85
A


ATOM
2227
CD1
ILE
A
295
16.017
10.483
40.918
1.00
42.43
A


ATOM
2228
C
ILE
A
295
11.995
12.902
42.660
1.00
44.46
A


ATOM
2229
O
ILE
A
295
11.004
12.201
42.444
1.00
44.51
A


ATOM
2230
N
SER
A
296
11.995
14.228
42.564
1.00
46.30
A


ATOM
2231
CA
SER
A
296
10.801
14.978
42.192
1.00
47.21
A


ATOM
2232
CB
SER
A
296
10.308
15.827
43.369
1.00
48.70
A


ATOM
2233
OG
SER
A
296
9.921
15.012
44.463
1.00
52.02
A


ATOM
2234
C
SER
A
296
11.048
15.877
40.989
1.00
46.34
A


ATOM
2235
O
SER
A
296
10.104
16.280
40.314
1.00
47.29
A


ATOM
2236
N
ASP
A
297
12.309
16.203
40.720
1.00
45.60
A


ATOM
2237
CA
ASP
A
297
12.613
17.048
39.574
1.00
44.42
A


ATOM
2238
CB
ASP
A
297
13.785
17.981
39.878
1.00
46.17
A


ATOM
2239
CG
ASP
A
297
14.192
18.825
38.666
1.00
47.06
A


ATOM
2240
OD1
ASP
A
297
13.296
19.317
37.948
1.00
47.00
A


ATOM
2241
OD2
ASP
A
297
15.407
19.000
38.436
1.00
47.36
A


ATOM
2242
C
ASP
A
297
12.920
16.219
38.329
1.00
44.32
A


ATOM
2243
O
ASP
A
297
14.036
15.727
38.135
1.00
44.05
A


ATOM
2244
N
TRP
A
298
11.905
16.079
37.488
1.00
42.80
A


ATOM
2245
CA
TRP
A
298
12.001
15.327
36.253
1.00
40.26
A


ATOM
2246
CB
TRP
A
298
10.742
15.587
35.438
1.00
38.68
A


ATOM
2247
CG
TRP
A
298
9.506
15.431
36.245
1.00
35.51
A


ATOM
2248
CD2
TRP
A
298
9.313
14.553
37.363
1.00
35.36
A


ATOM
2249
CE2
TRP
A
298
7.985
14.735
37.812
1.00
33.05
A


ATOM
2250
CE3
TRP
A
298
10.133
13.631
38.028
1.00
32.97
A


ATOM
2251
CD1
TRP
A
298
8.326
16.087
36.065
1.00
36.11
A


ATOM
2252
NE1
TRP
A
298
7.408
15.675
37.003
1.00
34.29
A


ATOM
2253
CZ2
TRP
A
298
7.456
14.029
38.896
1.00
32.55
A


ATOM
2254
CZ3
TRP
A
298
9.607
12.929
39.105
1.00
33.62
A


ATOM
2255
CH2
TRP
A
298
8.278
13.133
39.529
1.00
33.12
A


ATOM
2256
C
TRP
A
298
13.239
15.674
35.438
1.00
39.63
A


ATOM
2257
O
TRP
A
298
13.873
14.797
34.862
1.00
36.85
A


ATOM
2258
N
ASN
A
299
13.584
16.956
35.399
1.00
40.40
A


ATOM
2259
CA
ASN
A
299
14.744
17.401
34.633
1.00
41.92
A


ATOM
2260
CB
ASN
A
299
14.784
18.925
34.561
1.00
43.62
A


ATOM
2261
CG
ASN
A
299
13.930
19.460
33.447
1.00
46.32
A


ATOM
2262
OD1
ASN
A
299
14.021
18.982
32.312
1.00
46.16
A


ATOM
2263
ND2
ASN
A
299
13.094
20.456
33.752
1.00
45.79
A


ATOM
2264
C
ASN
A
299
16.093
16.889
35.119
1.00
41.44
A


ATOM
2265
O
ASN
A
299
17.114
17.152
34.487
1.00
41.03
A


ATOM
2266
N
LYS
A
300
16.105
16.162
36.233
1.00
41.82
A


ATOM
2267
CA
LYS
A
300
17.355
15.615
36.753
1.00
40.46
A


ATOM
2268
CB
LYS
A
300
17.286
15.495
38.279
1.00
42.21
A


ATOM
2269
CG
LYS
A
300
16.950
16.803
38.973
1.00
42.69
A


ATOM
2270
CD
LYS
A
300
17.123
16.740
40.487
1.00
44.99
A


ATOM
2271
CE
LYS
A
300
16.055
15.890
41.162
1.00
47.76
A


ATOM
2272
NZ
LYS
A
300
16.154
15.946
42.660
1.00
49.25
A


ATOM
2273
C
LYS
A
300
17.583
14.237
36.121
1.00
38.83
A


ATOM
2274
O
LYS
A
300
18.601
13.581
36.370
1.00
38.08
A


ATOM
2275
N
LEU
A
301
16.628
13.827
35.285
1.00
36.04
A


ATOM
2276
CA
LEU
A
301
16.647
12.531
34.601
1.00
34.97
A


ATOM
2277
CB
LEU
A
301
15.353
11.768
34.924
1.00
32.81
A


ATOM
2278
CG
LEU
A
301
15.066
11.287
36.350
1.00
32.28
A


ATOM
2279
CD1
LEU
A
301
15.321
12.393
37.346
1.00
34.57
A


ATOM
2280
CD2
LEU
A
301
13.619
10.856
36.448
1.00
30.89
A


ATOM
2281
C
LEU
A
301
16.766
12.645
33.078
1.00
35.04
A


ATOM
2282
O
LEU
A
301
16.238
13.590
32.484
1.00
36.33
A


ATOM
2283
N
PHE
A
302
17.460
11.697
32.439
1.00
34.85
A


ATOM
2284
CA
PHE
A
302
17.538
11.719
30.973
1.00
33.91
A


ATOM
2285
CB
PHE
A
302
18.796
11.008
30.441
1.00
33.60
A


ATOM
2286
CG
PHE
A
302
18.885
9.555
30.790
1.00
32.97
A


ATOM
2287
CD1
PHE
A
302
19.357
9.150
32.030
1.00
33.68
A


ATOM
2288
CD2
PHE
A
302
18.534
8.585
29.855
1.00
34.78
A


ATOM
2289
CE1
PHE
A
302
19.488
7.788
32.342
1.00
36.33
A


ATOM
2290
CE2
PHE
A
302
18.657
7.221
30.151
1.00
36.72
A


ATOM
2291
CZ
PHE
A
302
19.139
6.822
31.402
1.00
36.20
A


ATOM
2292
C
PHE
A
302
16.256
11.056
30.439
1.00
32.30
A


ATOM
2293
O
PHE
A
302
15.631
10.246
31.137
1.00
29.60
A


ATOM
2294
N
TRP
A
303
15.857
11.402
29.216
1.00
32.29
A


ATOM
2295
CA
TRP
A
303
14.607
10.881
28.660
1.00
31.71
A


ATOM
2296
CB
TRP
A
303
13.634
12.035
28.421
1.00
30.02
A


ATOM
2297
CG
TRP
A
303
13.095
12.620
29.662
1.00
31.30
A


ATOM
2298
CD2
TRP
A
303
11.745
12.559
30.113
1.00
31.48
A


ATOM
2299
CE2
TRP
A
303
11.682
13.259
31.340
1.00
31.80
A


ATOM
2300
CE3
TRP
A
303
10.579
11.981
29.602
1.00
32.51
A


ATOM
2301
CD1
TRP
A
303
13.783
13.325
30.603
1.00
31.26
A


ATOM
2302
NE1
TRP
A
303
12.941
13.714
31.617
1.00
31.13
A


ATOM
2303
CZ2
TRP
A
303
10.496
13.398
32.062
1.00
31.38
A


ATOM
2304
CZ3
TRP
A
303
9.399
12.118
30.321
1.00
32.50
A


ATOM
2305
CH2
TRP
A
303
9.368
12.823
31.538
1.00
32.74
A


ATOM
2306
C
TRP
A
303
14.581
10.016
27.413
1.00
30.99
A


ATOM
2307
O
TRP
A
303
15.311
10.233
26.460
1.00
30.40
A


ATOM
2308
N
VAL
A
304
13.688
9.036
27.443
1.00
31.60
A


ATOM
2309
CA
VAL
A
304
13.469
8.151
26.313
1.00
31.46
A


ATOM
2310
CB
VAL
A
304
14.114
6.774
26.487
1.00
30.67
A


ATOM
2311
CG1
VAL
A
304
13.707
5.886
25.324
1.00
28.82
A


ATOM
2312
CG2
VAL
A
304
15.631
6.909
26.533
1.00
30.09
A


ATOM
2313
C
VAL
A
304
11.970
7.961
26.256
1.00
31.13
A


ATOM
2314
O
VAL
A
304
11.416
7.160
27.002
1.00
32.32
A


ATOM
2315
N
VAL
A
305
11.318
8.713
25.377
1.00
30.86
A


ATOM
2316
CA
VAL
A
305
9.869
8.656
25.224
1.00
30.15
A


ATOM
2317
CB
VAL
A
305
9.240
10.050
25.528
1.00
31.70
A


ATOM
2318
CG1
VAL
A
305
7.786
10.106
25.043
1.00
30.98
A


ATOM
2319
CG2
VAL
A
305
9.308
10.322
27.028
1.00
30.26
A


ATOM
2320
C
VAL
A
305
9.516
8.220
23.805
1.00
29.92
A


ATOM
2321
O
VAL
A
305
10.157
8.637
22.840
1.00
29.78
A


ATOM
2322
N
HIS
A
306
8.510
7.363
23.679
1.00
29.35
A


ATOM
2323
CA
HIS
A
306
8.105
6.899
22.360
1.00
30.96
A


ATOM
2324
CB
HIS
A
306
6.968
5.877
22.474
1.00
31.60
A


ATOM
2325
CG
HIS
A
306
6.353
5.517
21.160
1.00
32.17
A


ATOM
2326
CD2
HIS
A
306
5.099
5.701
20.683
1.00
31.92
A


ATOM
2327
ND1
HIS
A
306
7.063
4.907
20.149
1.00
33.80
A


ATOM
2328
CE1
HIS
A
306
6.271
4.727
19.105
1.00
34.13
A


ATOM
2329
NE2
HIS
A
306
5.074
5.201
19.404
1.00
32.34
A


ATOM
2330
C
HIS
A
306
7.672
8.087
21.487
1.00
30.79
A


ATOM
2331
O
HIS
A
306
6.827
8.909
21.881
1.00
30.02
A


ATOM
2332
N
PRO
A
307
8.253
8.192
20.285
1.00
30.01
A


ATOM
2333
CD
PRO
A
307
9.351
7.348
19.777
1.00
29.05
A


ATOM
2334
CA
PRO
A
307
7.946
9.272
19.346
1.00
29.75
A


ATOM
2335
CB
PRO
A
307
9.168
9.273
18.441
1.00
29.53
A


ATOM
2336
CG
PRO
A
307
9.482
7.804
18.352
1.00
28.95
A


ATOM
2337
C
PRO
A
307
6.642
9.052
18.578
1.00
30.91
A


ATOM
2338
O
PRO
A
307
6.641
8.956
17.347
1.00
30.21
A


ATOM
2339
N
GLY
A
308
5.532
8.984
19.308
1.00
32.39
A


ATOM
2340
CA
GLY
A
308
4.243
8.767
18.671
1.00
34.41
A


ATOM
2341
C
GLY
A
308
3.936
9.818
17.622
1.00
35.01
A


ATOM
2342
O
GLY
A
308
3.438
9.505
16.538
1.00
35.38
A


ATOM
2343
N
GLY
A
309
4.246
11.068
17.952
1.00
34.47
A


ATOM
2344
CA
GLY
A
309
4.010
12.181
17.046
1.00
32.80
A


ATOM
2345
C
GLY
A
309
4.426
13.490
17.695
1.00
32.13
A


ATOM
2346
O
GLY
A
309
4.268
13.647
18.901
1.00
31.23
A


ATOM
2347
N
ARG
A
310
4.954
14.426
16.904
1.00
32.09
A


ATOM
2348
CA
ARG
A
310
5.399
15.717
17.424
1.00
33.38
A


ATOM
2349
CB
ARG
A
310
5.408
16.791
16.323
1.00
35.32
A


ATOM
2350
CG
ARG
A
310
5.632
18.197
16.902
1.00
36.45
A


ATOM
2351
CD
ARG
A
310
5.225
19.329
15.976
1.00
38.46
A


ATOM
2352
NE
ARG
A
310
6.254
19.662
14.998
1.00
40.77
A


ATOM
2353
CZ
ARG
A
310
6.164
20.681
14.147
1.00
42.99
A


ATOM
2354
NH1
ARG
A
310
5.094
21.467
14.156
1.00
44.81
A


ATOM
2355
NH2
ARG
A
310
7.138
20.918
13.280
1.00
44.76
A


ATOM
2356
C
ARG
A
310
4.536
16.227
18.576
1.00
33.42
A


ATOM
2357
O
ARG
A
310
5.048
16.539
19.653
1.00
32.55
A


ATOM
2358
N
ALA
A
311
3.228
16.301
18.330
1.00
34.76
A


ATOM
2359
CA
ALA
A
311
2.251
16.787
19.304
1.00
34.37
A


ATOM
2360
CB
ALA
A
311
.842
16.595
18.766
1.00
34.77
A


ATOM
2361
C
ALA
A
311
2.383
16.133
20.666
1.00
35.11
A


ATOM
2362
O
ALA
A
311
2.488
16.832
21.673
1.00
36.46
A


ATOM
2363
N
ILE
A
312
2.367
14.800
20.705
1.00
34.41
A


ATOM
2364
CA
ILE
A
312
2.514
14.079
21.971
1.00
33.63
A


ATOM
2365
CB
ILE
A
312
2.652
12.553
21.751
1.00
34.10
A


ATOM
2366
CG2
ILE
A
312
3.117
11.869
23.044
1.00
31.59
A


ATOM
2367
CG1
ILE
A
312
1.312
11.965
21.296
1.00
34.90
A


ATOM
2368
CD1
ILE
A
312
1.319
10.436
21.175
1.00
32.76
A


ATOM
2369
C
ILE
A
312
3.760
14.564
22.717
1.00
32.93
A


ATOM
2370
O
ILE
A
312
3.725
14.810
23.924
1.00
33.02
A


ATOM
2371
N
LEU
A
313
4.865
14.693
21.995
1.00
32.22
A


ATOM
2372
CA
LEU
A
313
6.109
15.152
22.602
1.00
32.28
A


ATOM
2373
CB
LEU
A
313
7.268
14.982
21.615
1.00
30.74
A


ATOM
2374
CG
LEU
A
313
7.430
13.580
21.009
1.00
29.06
A


ATOM
2375
CD1
LEU
A
313
8.656
13.542
20.117
1.00
27.85
A


ATOM
2376
CD2
LEU
A
313
7.551
12.544
22.128
1.00
29.06
A


ATOM
2377
C
LEU
A
313
5.988
16.615
23.022
1.00
33.58
A


ATOM
2378
O
LEU
A
313
6.449
17.002
24.095
1.00
31.21
A


ATOM
2379
N
ASP
A
314
5.352
17.428
22.185
1.00
34.88
A


ATOM
2380
CA
ASP
A
314
5.203
18.836
22.512
1.00
37.14
A


ATOM
2381
CB
ASP
A
314
4.623
19.620
21.335
1.00
36.64
A


ATOM
2382
CG
ASP
A
314
5.573
19.681
20.156
1.00
37.32
A


ATOM
2383
OD1
ASP
A
314
6.778
19.406
20.343
1.00
39.89
A


ATOM
2384
OD2
ASP
A
314
5.123
20.013
19.039
1.00
38.32
A


ATOM
2385
C
ASP
A
314
4.337
19.038
23.740
1.00
38.58
A


ATOM
2386
O
ASP
A
314
4.613
19.921
24.554
1.00
41.29
A


ATOM
2387
N
ARG
A
315
3.298
18.226
23.891
1.00
38.56
A


ATOM
2388
CA
ARG
A
315
2.420
18.367
25.051
1.00
39.30
A


ATOM
2389
CB
ARG
A
315
1.076
17.661
24.801
1.00
39.89
A


ATOM
2390
CG
ARG
A
315
−.038
18.094
25.756
1.00
41.38
A


ATOM
2391
CD
ARG
A
315
−.534
19.514
25.461
1.00
39.72
A


ATOM
2392
NE
ARG
A
315
−1.525
19.517
24.391
1.00
39.62
A


ATOM
2393
CZ
ARG
A
315
−2.757
19.034
24.517
1.00
38.98
A


ATOM
2394
NH1
ARG
A
315
−3.151
18.512
25.670
1.00
41.14
A


ATOM
2395
NH2
ARG
A
315
−3.594
19.063
23.491
1.00
40.18
A


ATOM
2396
C
ARG
A
315
3.095
17.816
26.311
1.00
37.88
A


ATOM
2397
O
ARG
A
315
3.120
18.474
27.345
1.00
38.21
A


ATOM
2398
N
VAL
A
316
3.650
16.614
26.220
1.00
38.10
A


ATOM
2399
CA
VAL
A
316
4.341
16.005
27.353
1.00
37.54
A


ATOM
2400
CB
VAL
A
316
5.071
14.695
26.932
1.00
38.03
A


ATOM
2401
CG1
VAL
A
316
6.071
14.282
28.005
1.00
35.70
A


ATOM
2402
CG2
VAL
A
316
4.061
13.579
26.713
1.00
36.09
A


ATOM
2403
C
VAL
A
316
5.379
16.965
27.941
1.00
38.14
A


ATOM
2404
O
VAL
A
316
5.415
17.191
29.145
1.00
37.74
A


ATOM
2405
N
GLU
A
317
6.217
17.520
27.071
1.00
39.36
A


ATOM
2406
CA
GLU
A
317
7.275
18.444
27.462
1.00
40.74
A


ATOM
2407
CB
GLU
A
317
8.078
18.846
26.227
1.00
42.43
A


ATOM
2408
CG
GLU
A
317
9.155
19.873
26.491
1.00
46.61
A


ATOM
2409
CD
GLU
A
317
10.033
20.092
25.280
1.00
49.20
A


ATOM
2410
OE1
GLU
A
317
9.485
20.393
24.197
1.00
50.31
A


ATOM
2411
OE2
GLU
A
317
11.269
19.959
25.409
1.00
51.28
A


ATOM
2412
C
GLU
A
317
6.748
19.691
28.161
1.00
40.41
A


ATOM
2413
O
GLU
A
317
7.250
20.092
29.215
1.00
40.12
A


ATOM
2414
N
ALA
A
318
5.736
20.305
27.568
1.00
40.32
A


ATOM
2415
CA
ALA
A
318
5.148
21.502
28.140
1.00
40.04
A


ATOM
2416
CB
ALA
A
318
4.103
22.067
27.197
1.00
39.47
A


ATOM
2417
C
ALA
A
318
4.517
21.164
29.482
1.00
40.63
A


ATOM
2418
O
ALA
A
318
4.609
21.938
30.436
1.00
40.11
A


ATOM
2419
N
LYS
A
319
3.890
19.996
29.561
1.00
40.54
A


ATOM
2420
CA
LYS
A
319
3.236
19.585
30.793
1.00
43.33
A


ATOM
2421
CB
LYS
A
319
2.442
18.294
30.568
1.00
43.96
A


ATOM
2422
CG
LYS
A
319
1.144
18.225
31.361
1.00
44.46
A


ATOM
2423
CD
LYS
A
319
1.434
18.187
32.849
1.00
45.75
A


ATOM
2424
CE
LYS
A
319
.164
18.197
33.671
1.00
46.68
A


ATOM
2425
NZ
LYS
A
319
.483
18.182
35.128
1.00
48.59
A


ATOM
2426
C
LYS
A
319
4.237
19.405
31.930
1.00
44.12
A


ATOM
2427
O
LYS
A
319
4.156
20.091
32.949
1.00
45.62
A


ATOM
2428
N
LEU
A
320
5.186
18.493
31.757
1.00
44.99
A


ATOM
2429
CA
LEU
A
320
6.200
18.242
32.781
1.00
45.19
A


ATOM
2430
CB
LEU
A
320
6.893
16.903
32.521
1.00
43.92
A


ATOM
2431
CG
LEU
A
320
6.180
15.639
33.016
1.00
43.85
A


ATOM
2432
CD1
LEU
A
320
4.669
15.835
33.062
1.00
43.96
A


ATOM
2433
CD2
LEU
A
320
6.550
14.490
32.106
1.00
41.61
A


ATOM
2434
C
LEU
A
320
7.243
19.346
32.848
1.00
45.43
A


ATOM
2435
O
LEU
A
320
8.073
19.363
33.752
1.00
47.16
A


ATOM
2436
N
ASN
A
321
7.200
20.268
31.892
1.00
45.91
A


ATOM
2437
CA
ASN
A
321
8.156
21.371
31.857
1.00
46.17
A


ATOM
2438
CB
ASN
A
321
7.984
22.276
33.089
1.00
48.27
A


ATOM
2439
CG
ASN
A
321
7.324
23.613
32.757
1.00
50.11
A


ATOM
2440
OD1
ASN
A
321
7.887
24.431
32.016
1.00
51.37
A


ATOM
2441
ND2
ASN
A
321
6.128
23.842
33.306
1.00
47.30
A


ATOM
2442
C
ASN
A
321
9.577
20.826
31.812
1.00
45.21
A


ATOM
2443
O
ASN
A
321
10.381
21.081
32.705
1.00
45.20
A


ATOM
2444
N
LEU
A
322
9.875
20.066
30.766
1.00
43.89
A


ATOM
2445
CA
LEU
A
322
11.195
19.487
30.592
1.00
43.18
A


ATOM
2446
CB
LEU
A
322
11.094
18.173
29.817
1.00
42.20
A


ATOM
2447
CG
LEU
A
322
10.099
17.116
30.300
1.00
41.74
A


ATOM
2448
CD1
LEU
A
322
10.180
15.896
29.386
1.00
40.69
A


ATOM
2449
CD2
LEU
A
322
10.398
16.736
31.741
1.00
39.97
A


ATOM
2450
C
LEU
A
322
12.082
20.455
29.818
1.00
44.00
A


ATOM
2451
O
LEU
A
322
11.597
21.240
29.002
1.00
45.63
A


ATOM
2452
N
ASP
A
323
13.381
20.405
30.077
1.00
44.78
A


ATOM
2453
CA
ASP
A
323
14.317
21.265
29.369
1.00
47.10
A


ATOM
2454
CB
ASP
A
323
15.717
21.187
29.992
1.00
49.02
A


ATOM
2455
CG
ASP
A
323
15.898
22.151
31.147
1.00
51.43
A


ATOM
2456
OD1
ASP
A
323
15.816
23.377
30.911
1.00
52.39
A


ATOM
2457
OD2
ASP
A
323
16.122
21.687
32.287
1.00
52.60
A


ATOM
2458
C
ASP
A
323
14.390
20.801
27.926
1.00
46.91
A


ATOM
2459
O
ASP
A
323
14.444
19.605
27.655
1.00
48.47
A


ATOM
2460
N
PRO
A
324
14.396
21.743
26.978
1.00
46.22
A


ATOM
2461
CD
PRO
A
324
14.387
23.200
27.195
1.00
46.91
A


ATOM
2462
CA
PRO
A
324
14.465
21.436
25.550
1.00
46.06
A


ATOM
2463
CB
PRO
A
324
14.791
22.787
24.930
1.00
45.50
A


ATOM
2464
CG
PRO
A
324
14.066
23.731
25.817
1.00
46.39
A


ATOM
2465
C
PRO
A
324
15.525
20.393
25.216
1.00
45.77
A


ATOM
2466
O
PRO
A
324
15.591
19.916
24.086
1.00
47.09
A


ATOM
2467
N
THR
A
325
16.359
20.049
26.193
1.00
44.47
A


ATOM
2468
CA
THR
A
325
17.424
19.071
25.974
1.00
43.36
A


ATOM
2469
CB
THR
A
325
18.654
19.335
26.885
1.00
42.49
A


ATOM
2470
OG1
THR
A
325
18.310
19.086
28.259
1.00
40.55
A


ATOM
2471
CG2
THR
A
325
19.144
20.768
26.715
1.00
39.78
A


ATOM
2472
C
THR
A
325
16.977
17.635
26.206
1.00
42.40
A


ATOM
2473
O
THR
A
325
17.518
16.716
25.607
1.00
43.43
A


ATOM
2474
N
LYS
A
326
15.994
17.442
27.075
1.00
41.96
A


ATOM
2475
CA
LYS
A
326
15.510
16.104
27.369
1.00
41.14
A


ATOM
2476
CB
LYS
A
326
14.252
16.172
28.233
1.00
40.16
A


ATOM
2477
CG
LYS
A
326
14.337
17.055
29.466
1.00
40.21
A


ATOM
2478
CD
LYS
A
326
15.143
16.444
30.595
1.00
42.29
A


ATOM
2479
CE
LYS
A
326
16.623
16.764
30.488
1.00
42.30
A


ATOM
2480
NZ
LYS
A
326
17.346
16.315
31.715
1.00
42.85
A


ATOM
2481
C
LYS
A
326
15.197
15.314
26.093
1.00
41.72
A


ATOM
2482
O
LYS
A
326
15.702
14.205
25.902
1.00
42.51
A


ATOM
2483
N
LEU
A
327
14.381
15.893
25.214
1.00
42.21
A


ATOM
2484
CA
LEU
A
327
13.976
15.212
23.977
1.00
41.89
A


ATOM
2485
CB
LEU
A
327
12.533
15.590
23.617
1.00
40.14
A


ATOM
2486
CG
LEU
A
327
11.472
15.344
24.689
1.00
40.48
A


ATOM
2487
CD1
LEU
A
327
10.115
15.709
24.124
1.00
40.17
A


ATOM
2488
CD2
LEU
A
327
11.491
13.888
25.138
1.00
40.61
A


ATOM
2489
C
LEU
A
327
14.854
15.410
22.740
1.00
41.12
A


ATOM
2490
O
LEU
A
327
14.371
15.279
21.612
1.00
40.40
A


ATOM
2491
N
ILE
A
328
16.129
15.728
22.930
1.00
38.12
A


ATOM
2492
CA
ILE
A
328
17.003
15.895
21.780
1.00
36.92
A


ATOM
2493
CB
ILE
A
328
18.380
16.460
22.183
1.00
36.66
A


ATOM
2494
CG2
ILE
A
328
19.230
16.700
20.942
1.00
36.52
A


ATOM
2495
CG1
ILE
A
328
18.199
17.772
22.945
1.00
36.61
A


ATOM
2496
CD1
ILE
A
328
17.422
18.817
22.186
1.00
35.30
A


ATOM
2497
C
ILE
A
328
17.174
14.509
21.162
1.00
36.34
A


ATOM
2498
O
ILE
A
328
17.106
14.343
19.939
1.00
37.30
A


ATOM
2499
N
PRO
A
329
17.396
13.488
22.003
1.00
34.69
A


ATOM
2500
CD
PRO
A
329
17.854
13.543
23.400
1.00
32.67
A


ATOM
2501
CA
PRO
A
329
17.559
12.135
21.462
1.00
35.34
A


ATOM
2502
CB
PRO
A
329
17.974
11.329
22.687
1.00
33.96
A


ATOM
2503
CG
PRO
A
329
18.737
12.337
23.491
1.00
33.23
A


ATOM
2504
C
PRO
A
329
16.273
11.610
20.819
1.00
33.93
A


ATOM
2505
O
PRO
A
329
16.307
11.036
19.739
1.00
34.28
A


ATOM
2506
N
THR
A
330
15.142
11.826
21.482
1.00
34.73
A


ATOM
2507
CA
THR
A
330
13.848
11.363
20.978
1.00
34.57
A


ATOM
2508
CB
THR
A
330
12.718
11.627
22.004
1.00
35.22
A


ATOM
2509
OG1
THR
A
330
12.959
10.873
23.200
1.00
36.60
A


ATOM
2510
CG2
THR
A
330
11.376
11.209
21.430
1.00
36.40
A


ATOM
2511
C
THR
A
330
13.448
12.006
19.651
1.00
32.86
A


ATOM
2512
O
THR
A
330
13.133
11.309
18.685
1.00
32.91
A


ATOM
2513
N
ARG
A
331
13.459
13.334
19.614
1.00
32.31
A


ATOM
2514
CA
ARG
A
331
13.088
14.081
18.418
1.00
31.64
A


ATOM
2515
CB
ARG
A
331
13.008
15.586
18.712
1.00
32.71
A


ATOM
2516
CG
ARG
A
331
11.900
16.012
19.676
1.00
31.50
A


ATOM
2517
CD
ARG
A
331
11.844
17.535
19.818
1.00
33.90
A


ATOM
2518
NE
ARG
A
331
10.822
17.981
20.761
1.00
33.69
A


ATOM
2519
CZ
ARG
A
331
9.509
17.953
20.528
1.00
37.09
A


ATOM
2520
NH1
ARG
A
331
9.031
17.506
19.373
1.00
36.82
A


ATOM
2521
NH2
ARG
A
331
8.663
18.357
21.466
1.00
36.77
A


ATOM
2522
C
ARG
A
331
14.065
13.855
17.282
1.00
33.23
A


ATOM
2523
O
ARG
A
331
13.693
13.967
16.116
1.00
36.66
A


ATOM
2524
N
HIS
A
322
15.314
13.540
17.614
1.00
32.09
A


ATOM
2525
CA
HIS
A
332
16.322
13.308
16.588
1.00
32.07
A


ATOM
2526
CB
HIS
A
332
17.720
13.310
17.210
1.00
35.42
A


ATOM
2527
CG
HIS
A
332
18.796
12.893
16.258
1.00
38.11
A


ATOM
2528
CD2
HIS
A
332
19.765
13.608
15.637
1.00
38.88
A


ATOM
2529
ND1
HIS
A
332
18.922
11.597
15.800
1.00
38.66
A


ATOM
2530
CE1
HIS
A
332
19.921
11.534
14.938
1.00
39.10
A


ATOM
2531
NE2
HIS
A
332
20.448
12.740
14.821
1.00
39.79
A


ATOM
2532
C
HIS
A
332
16.093
12.000
15.821
1.00
31.77
A


ATOM
2533
O
HIS
A
332
16.307
11.935
14.605
1.00
32.24
A


ATOM
2534
N
VAL
A
333
15.677
10.959
16.536
1.00
29.94
A


ATOM
2535
CA
VAL
A
333
15.398
9.673
15.912
1.00
28.63
A


ATOM
2536
CB
VAL
A
333
15.344
8.544
16.975
1.00
29.30
A


ATOM
2537
CG1
VAL
A
333
14.872
7.221
16.336
1.00
29.02
A


ATOM
2538
CG2
VAL
A
333
16.731
8.371
17.602
1.00
24.24
A


ATOM
2539
C
VAL
A
333
14.060
9.747
15.156
1.00
28.45
A


ATOM
2540
O
VAL
A
333
13.942
9.263
14.022
1.00
28.50
A


ATOM
2541
N
MET
A
334
13.055
10.363
15.768
1.00
26.42
A


ATOM
2542
CA
MET
A
334
11.771
10.472
15.098
1.00
26.67
A


ATOM
2543
CB
MET
A
334
10.756
11.270
15.937
1.00
23.62
A


ATOM
2544
CG
MET
A
334
9.286
11.001
15.511
1.00
24.33
A


ATOM
2545
SD
MET
A
334
8.068
12.270
15.942
1.00
20.82
A


ATOM
2546
CE
MET
A
334
7.430
11.702
17.373
1.00
19.41
A


ATOM
2547
C
MET
A
334
12.010
11.178
13.774
1.00
27.99
A


ATOM
2548
O
MET
A
334
11.385
10.851
12.767
1.00
29.09
A


ATOM
2549
N
SER
A
335
12.937
12.133
13.776
1.00
29.25
A


ATOM
2550
CA
SER
A
335
13.241
12.888
12.568
1.00
32.40
A


ATOM
2551
CB
SER
A
335
14.107
14.104
12.888
1.00
31.79
A


ATOM
2552
OG
SER
A
335
14.464
14.759
11.683
1.00
32.15
A


ATOM
2553
C
SER
A
335
13.932
12.086
11.475
1.00
32.33
A


ATOM
2554
O
SER
A
335
13.676
12.296
10.288
1.00
34.30
A


ATOM
2555
N
GLU
A
336
14.815
11.181
11.871
1.00
32.37
A


ATOM
2556
CA
GLU
A
336
15.535
10.372
10.901
1.00
31.39
A


ATOM
2557
CB
GLU
A
336
16.951
10.077
11.415
1.00
32.84
A


ATOM
2558
CG
GLU
A
336
17.593
8.849
10.775
1.00
39.41
A


ATOM
2559
CD
GLU
A
336
19.103
8.788
10.950
1.00
42.04
A


ATOM
2560
OE1
GLU
A
336
19.606
9.199
12.022
1.00
44.89
A


ATOM
2561
OE2
GLU
A
336
19.785
8.312
10.013
1.00
42.62
A


ATOM
2562
C
GLU
A
336
14.844
9.061
10.514
1.00
29.79
A


ATOM
2563
O
GLU
A
336
15.141
8.502
9.456
1.00
28.00
A


ATOM
2564
N
TYR
A
337
13.914
8.585
11.345
1.00
28.26
A


ATOM
2565
CA
TYR
A
337
13.235
7.313
11.076
1.00
27.55
A


ATOM
2566
CB
TYR
A
337
13.656
6.273
12.118
1.00
25.68
A


ATOM
2567
CG
TYR
A
337
15.134
6.010
12.148
1.00
22.44
A


ATOM
2568
CD1
TYR
A
337
15.719
5.099
11.272
1.00
21.51
A


ATOM
2569
CE1
TYR
A
337
17.100
4.881
11.279
1.00
22.79
A


ATOM
2570
CD2
TYR
A
337
15.959
6.698
13.031
1.00
21.39
A


ATOM
2571
CE2
TYR
A
337
17.336
6.489
13.046
1.00
23.04
A


ATOM
2572
CZ
TYR
A
337
17.896
5.579
12.170
1.00
22.73
A


ATOM
2573
OH
TYR
A
337
19.244
5.356
12.205
1.00
25.92
A


ATOM
2574
C
TYR
A
337
11.714
7.351
11.047
1.00
28.12
A


ATOM
2575
O
TYR
A
337
11.091
6.623
10.269
1.00
29.61
A


ATOM
2576
N
GLY
A
338
11.122
8.172
11.910
1.00
27.01
A


ATOM
2577
CA
GLY
A
338
9.674
8.261
11.985
1.00
28.08
A


ATOM
2578
C
GLY
A
338
9.171
7.349
13.095
1.00
29.03
A


ATOM
2579
O
GLY
A
338
9.949
6.964
13.973
1.00
30.16
A


ATOM
2580
N
ASN
A
339
7.884
7.003
13.083
1.00
29.06
A


ATOM
2581
CA
ASN
A
339
7.364
6.111
14.112
1.00
28.44
A


ATOM
2582
CB
ASN
A
339
5.871
6.359
14.353
1.00
29.87
A


ATOM
2583
CG
ASN
A
339
5.361
5.702
15.643
1.00
32.77
A


ATOM
2584
OD1
ASN
A
339
5.898
4.682
16.094
1.00
32.86
A


ATOM
2585
ND2
ASN
A
339
4.311
6.280
16.233
1.00
31.79
A


ATOM
2586
C
ASN
A
339
7.577
4.662
13.664
1.00
27.69
A


ATOM
2587
O
ASN
A
339
6.814
4.135
12.864
1.00
26.14
A


ATOM
2588
N
MET
A
340
8.643
4.038
14.156
1.00
28.00
A


ATOM
2589
CA
MET
A
340
8.939
2.646
13.834
1.00
26.29
A


ATOM
2590
CB
MET
A
340
10.443
2.411
13.799
1.00
24.42
A


ATOM
2591
CG
MET
A
340
11.178
3.042
12.626
1.00
21.65
A


ATOM
2592
SD
MET
A
340
12.917
2.677
12.788
1.00
11.19
A


ATOM
2593
CE
MET
A
340
13.287
3.727
14.106
1.00
12.59
A


ATOM
2594
C
MET
A
340
8.311
1.787
14.932
1.00
27.65
A


ATOM
2595
O
MET
A
340
8.795
.706
15.263
1.00
29.01
A


ATOM
2596
N
SER
A
341
7.219
2.300
15.487
1.00
28.65
A


ATOM
2597
CA
SER
A
341
6.481
1.638
16.553
1.00
28.94
A


ATOM
2598
CB
SER
A
341
5.703
.440
16.001
1.00
30.35
A


ATOM
2599
OG
SER
A
341
4.905
−.161
17.013
1.00
33.28
A


ATOM
2600
C
SER
A
341
7.368
1.204
17.716
1.00
28.35
A


ATOM
2601
O
SER
A
341
8.144
2.004
18.247
1.00
27.65
A


ATOM
2602
N
SER
A
342
7.253
−.067
18.097
1.00
28.96
A


ATOM
2603
CA
SER
A
342
7.997
−.622
19.222
1.00
29.52
A


ATOM
2604
CB
SER
A
342
7.624
−2.101
19.419
1.00
29.14
A


ATOM
2605
OG
SER
A
342
7.844
−2.873
18.249
1.00
28.82
A


ATOM
2606
C
SER
A
342
9.516
−.474
19.197
1.00
30.70
A


ATOM
2607
O
SER
A
342
10.142
−.355
20.249
1.00
30.85
A


ATOM
2608
N
ALA
A
343
10.118
−.464
18.016
1.00
31.45
A


ATOM
2609
CA
ALA
A
343
11.570
−.344
17.952
1.00
33.64
A


ATOM
2610
CB
ALA
A
343
12.083
−.983
16.662
1.00
35.55
A


ATOM
2611
C
ALA
A
343
12.136
1.080
18.105
1.00
33.98
A


ATOM
2612
O
ALA
A
343
13.344
1.246
18.233
1.00
34.35
A


ATOM
2613
N
CYS
A
344
11.279
2.098
18.108
1.00
33.68
A


ATOM
2614
CA
CYS
A
344
11.746
3.484
18.244
1.00
33.68
A


ATOM
2615
CB
CYS
A
344
10.566
4.455
18.206
1.00
34.53
A


ATOM
2616
SG
CYS
A
344
9.710
4.519
16.638
1.00
37.50
A


ATOM
2617
C
CYS
A
344
12.547
3.761
19.515
1.00
32.20
A


ATOM
2618
O
CYS
A
344
13.679
4.257
19.455
1.00
30.61
A


ATOM
2619
N
VAL
A
345
11.953
3.438
20.661
1.00
30.76
A


ATOM
2620
CA
VAL
A
345
12.594
3.672
21.950
1.00
30.62
A


ATOM
2621
CB
VAL
A
345
11.700
3.227
23.104
1.00
30.70
A


ATOM
2622
CG1
VAL
A
345
10.457
4.082
23.138
1.00
29.52
A


ATOM
2623
CG2
VAL
A
345
11.339
1.764
22.939
1.00
29.04
A


ATOM
2624
C
VAL
A
345
13.942
2.984
22.091
1.00
30.41
A


ATOM
2625
O
VAL
A
345
14.762
3.389
22.914
1.00
31.73
A


ATOM
2626
N
HIS
A
346
14.177
1.941
21.306
1.00
29.02
A


ATOM
2627
CA
HIS
A
346
15.456
1.254
21.377
1.00
28.83
A


ATOM
2628
CB
HIS
A
346
15.314
−.201
20.924
1.00
29.96
A


ATOM
2629
CG
HIS
A
346
14.336
−.983
21.747
1.00
32.17
A


ATOM
2630
CD2
HIS
A
346
13.228
−1.681
21.400
1.00
32.87
A


ATOM
2631
ND1
HIS
A
346
14.434
−1.083
23.118
1.00
33.79
A


ATOM
2632
CE1
HIS
A
346
13.430
−1.809
23.580
1.00
34.75
A


ATOM
2633
NE2
HIS
A
346
12.684
−2.186
22.557
1.00
34.86
A


ATOM
2634
C
HIS
A
346
16.397
2.045
20.486
1.00
28.71
A


ATOM
2635
O
HIS
A
346
17.579
2.204
20.805
1.00
27.87
A


ATOM
2636
N
PHE
A
347
15.864
2.564
19.381
1.00
27.48
A


ATOM
2637
CA
PHE
A
347
16.660
3.398
18.488
1.00
28.08
A


ATOM
2638
CB
PHE
A
347
15.820
3.906
17.314
1.00
25.80
A


ATOM
2639
CG
PHE
A
347
15.953
3.083
16.070
1.00
26.73
A


ATOM
2640
CD1
PHE
A
347
15.493
1.768
16.031
1.00
24.87
A


ATOM
2641
CD2
PHE
A
347
16.539
3.621
14.927
1.00
24.25
A


ATOM
2642
CE1
PHE
A
347
15.613
1.007
14.862
1.00
25.10
A


ATOM
2643
CE2
PHE
A
347
16.666
2.863
13.758
1.00
23.84
A


ATOM
2644
CZ
PHE
A
347
16.201
1.558
13.727
1.00
25.46
A


ATOM
2645
C
PHE
A
347
17.123
4.595
19.311
1.00
29.17
A


ATOM
2646
O
PHE
A
347
18.265
5.032
19.198
1.00
30.41
A


ATOM
2647
N
ILE
A
348
16.220
5.115
20.144
1.00
29.54
A


ATOM
2648
CA
ILE
A
348
16.519
6.269
20.992
1.00
31.74
A


ATOM
2649
CB
ILE
A
348
15.237
6.805
21.670
1.00
30.12
A


ATOM
2650
CG2
ILE
A
348
15.585
7.905
22.673
1.00
29.86
A


ATOM
2651
CG1
ILE
A
348
14.285
7.351
20.600
1.00
30.80
A


ATOM
2652
CD1
ILE
A
348
12.905
7.697
21.121
1.00
29.48
A


ATOM
2653
C
ILE
A
348
17.564
5.941
22.057
1.00
33.22
A


ATOM
2654
O
ILE
A
348
18.451
6.753
22.331
1.00
32.42
A


ATOM
2655
N
LEU
A
349
17.447
4.756
22.659
1.00
34.52
A


ATOM
2656
CA
LEU
A
349
18.402
4.312
23.673
1.00
33.45
A


ATOM
2657
CB
LEU
A
349
18.131
2.862
24.075
1.00
32.73
A


ATOM
2658
CG
LEU
A
249
17.008
2.663
25.082
1.00
31.86
A


ATOM
2659
CD1
LEU
A
349
16.621
1.218
25.144
1.00
32.57
A


ATOM
2660
CD2
LEU
A
349
17.469
3.159
26.437
1.00
35.89
A


ATOM
2661
C
LEU
A
349
19.783
4.393
23.072
1.00
32.83
A


ATOM
2662
O
LEU
A
349
20.693
4.986
23.642
1.00
33.55
A


ATOM
2663
N
ASP
A
350
19.912
3.791
21.898
1.00
32.31
A


ATOM
2664
CA
ASP
A
350
21.160
3.751
21.163
1.00
32.68
A


ATOM
2665
CB
ASP
A
350
20.953
2.948
19.883
1.00
31.76
A


ATOM
2666
CG
ASP
A
350
22.252
2.579
19.211
1.00
33.89
A


ATOM
2667
OD1
ASP
A
350
23.090
1.926
19.866
1.00
34.37
A


ATOM
2668
OD2
ASP
A
350
22.431
2.936
18.028
1.00
34.98
A


ATOM
2669
C
ASP
A
350
21.662
5.162
20.836
1.00
34.32
A


ATOM
2670
O
ASP
A
350
22.793
5.513
21.161
1.00
33.23
A


ATOM
2671
N
GLN
A
351
20.820
5.971
20.202
1.00
35.14
A


ATOM
2672
CA
GLN
A
351
21.214
7.332
19.853
1.00
36.60
A


ATOM
2673
CB
GLN
A
351
20.072
8.052
19.134
1.00
37.06
A


ATOM
2674
CG
GLN
A
351
20.442
9.464
18.680
1.00
39.34
A


ATOM
2675
CD
GLN
A
351
21.369
9.479
17.472
1.00
40.13
A


ATOM
2676
OE1
GLN
A
351
22.018
10.480
17.198
1.00
40.84
A


ATOM
2677
NE2
GLN
A
351
21.419
8.370
16.736
1.00
41.79
A


ATOM
2678
C
GLN
A
351
21.617
8.128
21.097
1.00
36.53
A


ATOM
2679
O
GLN
A
351
22.511
8.977
21.039
1.00
34.64
A


ATOM
2680
N
THR
A
352
20.945
7.844
22.213
1.00
36.55
A


ATOM
2681
CA
THR
A
352
21.219
8.507
23.481
1.00
37.35
A


ATOM
2682
CB
THR
A
352
20.143
8.164
24.523
1.00
36.83
A


ATOM
2683
OG1
THR
A
352
18.919
8.808
24.159
1.00
36.13
A


ATOM
2684
CG2
THR
A
352
20.559
8.628
25.914
1.00
36.00
A


ATOM
2685
C
THR
A
352
22.600
8.137
24.032
1.00
39.55
A


ATOM
2686
O
THR
A
352
23.302
8.996
24.571
1.00
39.76
A


ATOM
2687
N
ARG
A
353
22.995
6.872
23.902
1.00
38.72
A


ATOM
2688
CA
ARG
A
353
24.308
6.468
24.387
1.00
39.16
A


ATOM
2689
CB
ARG
A
353
24.395
4.949
24.547
1.00
38.70
A


ATOM
2690
CG
ARG
A
353
24.307
4.168
23.270
1.00
38.81
A


ATOM
2691
CD
ARG
A
353
24.503
2.685
23.524
1.00
38.69
A


ATOM
2692
NE
ARG
A
353
24.489
1.938
22.272
1.00
37.26
A


ATOM
2693
CZ
ARG
A
353
24.949
.702
22.131
1.00
36.50
A


ATOM
2694
NH1
ARG
A
353
25.463
.060
23.175
1.00
36.43
A


ATOM
2695
NH2
ARG
A
353
24.910
.114
20.940
1.00
33.66
A


ATOM
2696
C
ARG
A
353
25.402
6.966
23.441
1.00
38.75
A


ATOM
2697
O
ARG
A
353
26.491
7.322
23.889
1.00
38.89
A


ATOM
2698
N
LYS
A
354
25.110
6.999
22.140
1.00
38.70
A


ATOM
2699
CA
LYS
A
354
26.072
7.483
21.141
1.00
38.91
A


ATOM
2700
CB
LYS
A
354
25.530
7.291
19.716
1.00
39.12
A


ATOM
2701
CG
LYS
A
354
25.177
5.870
19.341
1.00
41.11
A


ATOM
2702
CD
LYS
A
354
26.367
4.939
19.472
1.00
41.53
A


ATOM
2703
CE
LYS
A
354
25.948
3.481
19.275
1.00
43.16
A


ATOM
2704
NZ
LYS
A
354
25.334
3.220
17.934
1.00
42.80
A


ATOM
2705
C
LYS
A
354
26.345
8.981
21.355
1.00
39.02
A


ATOM
2706
O
LYS
A
354
27.486
9.438
21.281
1.00
39.72
A


ATOM
2707
N
ALA
A
355
25.284
9.740
21.610
1.00
37.76
A


ATOM
2708
CA
ALA
A
355
25.403
11.168
21.827
1.00
37.38
A


ATOM
2709
CB
ALA
A
355
24.016
11.788
21.926
1.00
35.63
A


ATOM
2710
C
ALA
A
355
26.214
11.460
23.093
1.00
38.06
A


ATOM
2711
O
ALA
A
355
27.016
12.392
23.124
1.00
39.13
A


ATOM
2712
N
SER
A
356
26.003
10.660
24.134
1.00
38.24
A


ATOM
2713
CA
SER
A
356
26.717
10.834
25.396
1.00
38.77
A


ATOM
2714
CB
SER
A
356
26.194
9.849
26.448
1.00
39.74
A


ATOM
2715
OG
SER
A
356
24.828
10.086
26.754
1.00
40.96
A


ATOM
2716
C
SER
A
356
28.200
10.579
25.167
1.00
39.15
A


ATOM
2717
O
SER
A
356
29.061
11.172
25.811
1.00
40.88
A


ATOM
2718
N
LEU
A
357
28.486
9.700
24.224
1.00
37.61
A


ATOM
2719
CA
LEU
A
357
29.847
9.341
23.900
1.00
37.06
A


ATOM
2720
CB
LEU
A
357
29.813
8.048
23.096
1.00
34.46
A


ATOM
2721
CG
LEU
A
357
31.079
7.221
22.966
1.00
35.15
A


ATOM
2722
CD1
LEU
A
357
31.762
7.084
24.316
1.00
33.86
A


ATOM
2723
CD2
LEU
A
357
30.701
5.861
22.387
1.00
35.10
A


ATOM
2724
C
LEU
A
357
30.569
10.455
23.130
1.00
38.07
A


ATOM
2725
O
LEU
A
357
31.624
10.935
23.554
1.00
37.75
A


ATOM
2726
N
GLN
A
358
29.992
10.860
22.003
1.00
39.64
A


ATOM
2727
CA
GLN
A
358
30.555
11.912
21.150
1.00
41.15
A


ATOM
2728
CB
GLN
A
358
29.603
12.218
19.987
1.00
43.94
A


ATOM
2729
CG
GLN
A
358
29.325
11.065
19.026
1.00
46.51
A


ATOM
2730
CD
GLN
A
358
30.239
11.076
17.807
1.00
49.21
A


ATOM
2731
OE1
GLN
A
358
30.413
12.109
17.150
1.00
50.20
A


ATOM
2732
NE2
GLN
A
358
30.817
9.923
17.491
1.00
50.25
A


ATOM
2733
C
GLN
A
358
30.807
13.213
21.901
1.00
41.73
A


ATOM
2734
O
GLN
A
358
31.811
13.894
21.676
1.00
41.83
A


ATOM
2735
N
ASN
A
359
29.885
13.557
22.792
1.00
41.97
A


ATOM
2736
CA
ASN
A
359
29.978
14.795
23.549
1.00
42.02
A


ATOM
2737
CB
ASN
A
359
28.585
15.207
24.022
1.00
42.01
A


ATOM
2738
CG
ASN
A
359
27.546
15.082
22.924
1.00
42.17
A


ATOM
2739
OD1
ASN
A
359
27.892
14.891
21.761
1.00
44.07
A


ATOM
2740
ND2
ASN
A
359
26.269
15.186
23.285
1.00
42.37
A


ATOM
2741
C
ASN
A
359
30.930
14.721
24.728
1.00
43.88
A


ATOM
2742
O
ASN
A
359
31.404
15.755
25.208
1.00
45.52
A


ATOM
2743
N
GLY
A
360
31.207
13.506
25.197
1.00
43.60
A


ATOM
2744
CA
GLY
A
360
32.118
13.332
26.320
1.00
41.65
A


ATOM
2745
C
GLY
A
360
31.478
13.426
27.695
1.00
40.93
A


ATOM
2746
O
GLY
A
360
32.099
13.920
28.641
1.00
39.86
A


ATOM
2747
N
CYS
A
361
30.244
12.938
27.813
1.00
40.23
A


ATOM
2748
CA
CYS
A
361
29.508
12.974
29.071
1.00
39.86
A


ATOM
2749
CB
CYS
A
361
28.021
12.710
28.816
1.00
41.39
A


ATOM
2750
SG
CYS
A
361
27.254
13.841
27.604
1.00
46.32
A


ATOM
2751
C
CYS
A
361
30.043
11.968
30.083
1.00
39.25
A


ATOM
2752
O
CYS
A
361
30.757
11.038
29.730
1.00
39.13
A


ATOM
2753
N
SER
A
362
29.680
12.163
31.344
1.00
39.05
A


ATOM
2754
CA
SER
A
362
30.128
11.303
32.428
1.00
38.13
A


ATOM
2755
CB
SER
A
362
29.856
11.983
33.765
1.00
37.35
A


ATOM
2756
OG
SER
A
362
28.480
12.268
33.906
1.00
37.41
A


ATOM
2757
C
SER
A
362
29.487
9.920
32.432
1.00
39.61
A


ATOM
2758
O
SER
A
362
30.080
8.962
32.926
1.00
39.97
A


ATOM
2759
N
THR
A
363
28.273
9.814
31.902
1.00
39.04
A


ATOM
2760
CA
THR
A
363
27.582
8.527
31.864
1.00
38.14
A


ATOM
2761
CB
THR
A
363
26.482
8.449
32.943
1.00
38.58
A


ATOM
2762
OG1
THR
A
363
25.378
9.284
32.569
1.00
34.35
A


ATOM
2763
CG2
THR
A
363
27.028
8.903
34.289
1.00
38.03
A


ATOM
2764
C
THR
A
363
26.928
8.299
30.507
1.00
37.71
A


ATOM
2765
O
THR
A
363
26.925
9.185
29.652
1.00
38.00
A


ATOM
2766
N
THR
A
364
26.373
7.107
30.312
1.00
36.07
A


ATOM
2767
CA
THR
A
364
25.710
6.779
29.055
1.00
34.36
A


ATOM
2768
CB
THR
A
364
25.442
5.262
28.944
1.00
32.76
A


ATOM
2769
OG1
THR
A
364
25.132
4.734
30.238
1.00
31.72
A


ATOM
2770
CG2
THR
A
364
26.657
4.547
28.389
1.00
33.27
A


ATOM
2771
C
THR
A
364
24.397
7.539
28.917
1.00
34.89
A


ATOM
2772
O
THR
A
364
23.788
7.552
27.855
1.00
33.55
A


ATOM
2773
N
GLY
A
365
23.971
8.174
30.001
1.00
37.02
A


ATOM
2774
CA
GLY
A
365
22.738
8.939
29.985
1.00
39.62
A


ATOM
2775
C
GLY
A
365
23.031
10.424
29.873
1.00
41.66
A


ATOM
2776
O
GLY
A
365
22.526
11.231
30.655
1.00
41.20
A


ATOM
2777
N
GLU
A
366
23.864
10.776
28.899
1.00
42.25
A


ATOM
2778
CA
GLU
A
366
24.248
12.161
28.660
1.00
44.72
A


ATOM
2779
CB
GLU
A
366
23.085
12.903
27.996
1.00
47.19
A


ATOM
2780
CG
GLU
A
366
22.598
12.219
26.721
1.00
52.43
A


ATOM
2781
CD
GLU
A
366
21.451
12.950
26.035
1.00
56.02
A


ATOM
2782
OE1
GLU
A
366
20.404
13.181
26.686
1.00
56.50
A


ATOM
2783
OE2
GLU
A
366
21.600
13.285
24.837
1.00
57.47
A


ATOM
2784
C
GLU
A
366
24.700
12.887
29.933
1.00
44.50
A


ATOM
2785
O
GLU
A
366
24.523
14.100
30.064
1.00
42.81
A


ATOM
2786
N
GLY
A
367
25.279
12.134
30.869
1.00
43.97
A


ATOM
2787
CA
GLY
A
367
25.770
12.721
32.106
1.00
42.81
A


ATOM
2788
C
GLY
A
367
24.962
12.462
33.368
1.00
40.85
A


ATOM
2789
O
GLY
A
367
25.489
12.538
34.478
1.00
40.69
A


ATOM
2790
N
LEU
A
368
22.683
12.158
33.204
1.00
39.07
A


ATOM
2791
CA
LEU
A
368
22.815
11.904
34.340
1.00
37.27
A


ATOM
2792
CB
LEU
A
368
21.374
12.223
33.947
1.00
37.69
A


ATOM
2793
CG
LEU
A
368
21.029
13.698
33.694
1.00
38.92
A


ATOM
2794
CD1
LEU
A
368
22.240
14.489
33.220
1.00
38.52
A


ATOM
2795
CD2
LEU
A
368
19.906
13.766
32.678
1.00
37.84
A


ATOM
2796
C
LEU
A
368
22.942
10.458
34.831
1.00
37.05
A


ATOM
2797
O
LEU
A
368
23.465
9.590
34.127
1.00
36.30
A


ATOM
2798
N
GLU
A
369
22.458
10.206
36.041
1.00
36.23
A


ATOM
2799
CA
GLU
A
369
22.539
8.883
36.641
1.00
37.09
A


ATOM
2800
CB
GLU
A
369
22.701
9.009
38.157
1.00
41.29
A


ATOM
2801
CG
GLU
A
369
23.398
10.294
38.642
1.00
46.01
A


ATOM
2802
CD
GLU
A
369
22.517
11.551
38.547
1.00
47.44
A


ATOM
2803
OE1
GLU
A
369
22.444
12.167
37.454
1.00
44.74
A


ATOM
2804
OE2
GLU
A
369
21.894
11.914
39.578
1.00
49.56
A


ATOM
2805
C
GLU
A
369
21.327
7.999
36.340
1.00
35.30
A


ATOM
2806
O
GLU
A
369
21.481
6.847
35.939
1.00
35.73
A


ATOM
2807
N
MET
A
370
20.130
8.540
36.549
1.00
32.75
A


ATOM
2808
CA
MET
A
370
18.886
7.808
36.308
1.00
31.28
A


ATOM
2809
CB
MET
A
370
18.032
7.785
37.584
1.00
31.18
A


ATOM
2810
CG
MET
A
270
18.348
6.665
38.567
1.00
29.86
A


ATOM
2811
SD
MET
A
270
17.143
6.652
39.910
1.00
28.54
A


ATOM
2812
CE
MET
A
370
17.895
7.805
40.972
1.00
31.46
A


ATOM
2813
C
MET
A
370
18.056
8.413
35.159
1.00
31.15
A


ATOM
2814
O
MET
A
370
18.125
9.615
34.893
1.00
29.39
A


ATOM
2815
N
GLY
A
371
17.268
7.574
34.491
1.00
28.64
A


ATOM
2816
CA
GLY
A
371
16.449
8.051
33.388
1.00
28.20
A


ATOM
2817
C
GLY
A
371
15.117
7.328
33.246
1.00
26.64
A


ATOM
2818
O
GLY
A
371
14.882
6.297
33.879
1.00
24.42
A


ATOM
2819
N
VAL
A
372
14.236
7.861
32.408
1.00
25.98
A


ATOM
2820
CA
VAL
A
372
12.929
7.253
32.223
1.00
25.78
A


ATOM
2821
CB
VAL
A
372
11.784
8.175
32.695
1.00
25.32
A


ATOM
2822
CG1
VAL
A
372
11.584
9.324
31.708
1.00
24.95
A


ATOM
2823
CG2
VAL
A
372
10.496
7.371
32.830
1.00
25.78
A


ATOM
2824
C
VAL
A
372
12.670
6.920
30.776
1.00
26.21
A


ATOM
2825
O
VAL
A
372
13.163
7.587
29.869
1.00
27.38
A


ATOM
2826
N
LEU
A
373
11.892
5.873
30.566
1.00
27.08
A


ATOM
2827
CA
LEU
A
373
11.536
5.466
29.223
1.00
27.81
A


ATOM
2828
CB
LEU
A
373
12.218
4.149
28.866
1.00
29.56
A


ATOM
2829
CG
LEU
A
373
11.907
3.634
27.459
1.00
31.75
A


ATOM
2830
CD1
LEU
A
373
13.171
3.065
26.836
1.00
29.26
A


ATOM
2831
CD2
LEU
A
373
10.791
2.591
27.531
1.00
31.43
A


ATOM
2832
C
LEU
A
373
10.026
5.317
29.194
1.00
27.20
A


ATOM
2833
O
LEU
A
373
9.427
4.811
30.148
1.00
26.34
A


ATOM
2834
N
PHE
A
374
9.418
5.779
28.106
1.00
26.82
A


ATOM
2835
CA
PHE
A
374
7.972
5.712
27.942
1.00
27.12
A


ATOM
2836
CB
PHE
A
374
7.369
7.108
28.029
1.00
28.61
A


ATOM
2837
CG
PHE
A
374
7.242
7.630
29.421
1.00
31.11
A


ATOM
2838
CD1
PHE
A
374
6.239
7.159
30.263
1.00
32.22
A


ATOM
2839
CD2
PHE
A
374
8.110
8.609
29.891
1.00
31.24
A


ATOM
2840
CE1
PHE
A
374
6.093
7.655
31.558
1.00
32.81
A


ATOM
2841
CE2
PHE
A
374
7.977
9.118
31.187
1.00
33.42
A


ATOM
2842
CZ
PHE
A
374
6.960
8.637
32.024
1.00
33.49
A


ATOM
2843
C
PHE
A
374
7.537
5.087
26.622
1.00
28.09
A


ATOM
2844
O
PHE
A
374
8.186
5.247
25.592
1.00
28.61
A


ATOM
2845
N
GLY
A
375
6.423
4.370
26.671
1.00
27.67
A


ATOM
2846
CA
GLY
A
375
5.870
3.765
25.480
1.00
25.79
A


ATOM
2847
C
GLY
A
375
4.377
4.025
25.530
1.00
25.72
A


ATOM
2848
O
GLY
A
375
3.764
3.878
26.583
1.00
26.86
A


ATOM
2849
N
PHE
A
376
3.789
4.430
24.410
1.00
27.30
A


ATOM
2850
CA
PHE
A
376
2.349
4.694
24.363
1.00
26.31
A


ATOM
2851
CB
PHE
A
376
2.061
6.168
24.072
1.00
27.66
A


ATOM
2852
CG
PHE
A
376
2.995
7.120
24.748
1.00
28.81
A


ATOM
2853
CD1
PHE
A
376
3.222
7.044
26.115
1.00
30.56
A


ATOM
2854
CD2
PHE
A
376
3.628
8.117
24.019
1.00
28.26
A


ATOM
2855
CE1
PHE
A
376
4.069
7.949
26.751
1.00
30.43
A


ATOM
2856
CE2
PHE
A
376
4.475
9.026
24.643
1.00
29.11
A


ATOM
2857
CZ
PHE
A
376
4.698
8.943
26.011
1.00
29.04
A


ATOM
2858
C
PHE
A
376
1.708
3.870
23.259
1.00
25.27
A


ATOM
2859
O
PHE
A
376
2.239
3.781
22.156
1.00
25.32
A


ATOM
2860
N
GLY
A
377
.555
3.284
23.552
1.00
25.39
A


ATOM
2861
CA
GLY
A
377
−.127
2.502
22.545
1.00
24.04
A


ATOM
2862
C
GLY
A
377
−1.590
2.234
22.854
1.00
23.88
A


ATOM
2863
O
GLY
A
377
−2.155
2.812
23.785
1.00
20.92
A


ATOM
2864
N
PRO
A
378
−2.225
1.347
22.068
1.00
24.59
A


ATOM
2865
CD
PRO
A
378
−1.538
.702
20.934
1.00
22.15
A


ATOM
2866
CA
PRO
A
378
−3.617
.900
22.134
1.00
26.44
A


ATOM
2867
CB
PRO
A
378
−3.608
−.340
21.259
1.00
23.96
A


ATOM
2868
CG
PRO
A
378
−2.682
.086
20.164
1.00
23.62
A


ATOM
2869
C
PRO
A
378
−4.134
.609
23.529
1.00
28.16
A


ATOM
2870
O
PRO
A
378
−3.376
.220
24.411
1.00
27.70
A


ATOM
2871
N
GLY
A
379
−5.446
.775
23.690
1.00
31.23
A


ATOM
2872
CA
GLY
A
379
−6.111
.572
24.963
1.00
33.70
A


ATOM
2873
C
GLY
A
379
−5.864
1.875
25.669
1.00
36.78
A


ATOM
2874
O
GLY
A
379
−6.661
2.378
26.468
1.00
35.21
A


ATOM
2875
N
LEU
A
380
−4.724
2.421
25.259
1.00
38.76
A


ATOM
2876
CA
LEU
A
380
−4.119
3.652
25.716
1.00
37.20
A


ATOM
2877
CB
LEU
A
380
−5.125
4.780
25.869
1.00
38.70
A


ATOM
2878
CG
LEU
A
380
−4.492
6.083
25.356
1.00
41.13
A


ATOM
2879
CD1
LEU
A
380
−3.071
6.240
25.923
1.00
42.02
A


ATOM
2880
CD2
LEU
A
380
−4.421
6.061
23.837
1.00
40.14
A


ATOM
2881
C
LEU
A
380
−3.443
3.328
27.021
1.00
34.99
A


ATOM
2882
O
LEU
A
380
−3.848
3.763
28.098
1.00
34.48
A


ATOM
2883
N
THR
A
381
−2.406
2.514
26.893
1.00
31.04
A


ATOM
2884
CA
THR
A
381
−1.639
2.088
28.034
1.00
30.02
A


ATOM
2885
CB
THR
A
381
−1.361
.549
28.000
1.00
29.09
A


ATOM
2886
OG1
THR
A
381
−.002
.288
27.613
1.00
28.59
A


ATOM
2887
CG2
THR
A
381
−2.282
−.117
27.011
1.00
26.08
A


ATOM
2888
C
THR
A
381
−.355
2.860
27.933
1.00
29.20
A


ATOM
2889
O
THR
A
381
−.025
3.380
26.874
1.00
29.92
A


ATOM
2890
N
ILE
A
382
.358
2.951
29.042
1.00
29.88
A


ATOM
2891
CA
ILE
A
382
1.622
3.663
29.073
1.00
28.14
A


ATOM
2892
CB
ILE
A
382
1.520
4.957
29.914
1.00
26.61
A


ATOM
2893
CG2
ILE
A
382
2.809
5.750
29.803
1.00
28.80
A


ATOM
2894
CG1
ILE
A
382
.324
5.800
29.461
1.00
29.96
A


ATOM
2895
CD1
ILE
A
382
.455
6.415
28.079
1.00
29.52
A


ATOM
2896
C
ILE
A
382
2.607
2.729
29.759
1.00
27.30
A


ATOM
2897
O
ILE
A
382
2.322
2.189
30.829
1.00
26.16
A


ATOM
2898
N
GLU
A
383
3.747
2.502
29.130
1.00
27.01
A


ATOM
2899
CA
GLU
A
383
4.758
1.667
29.753
1.00
28.35
A


ATOM
2900
CB
GLU
A
383
5.385
.701
28.751
1.00
28.01
A


ATOM
2901
CG
GLU
A
383
4.434
−.408
28.312
1.00
29.73
A


ATOM
2902
CD
GLU
A
383
4.552
−1.679
29.141
1.00
29.55
A


ATOM
2903
OE1
GLU
A
383
5.000
−1.623
30.304
1.00
30.70
A


ATOM
2904
OE2
GLU
A
383
4.179
−2.748
28.626
1.00
31.96
A


ATOM
2905
C
GLU
A
383
5.792
2.644
30.261
1.00
28.17
A


ATOM
2906
O
GLU
A
383
6.263
3.496
29.523
1.00
28.48
A


ATOM
2907
N
THR
A
384
6.098
2.535
31.545
1.00
29.87
A


ATOM
2908
CA
THR
A
384
7.083
3.379
32.192
1.00
29.87
A


ATOM
2909
CB
THR
A
384
6.516
4.060
33.458
1.00
31.48
A


ATOM
2910
OG1
THR
A
384
5.424
4.922
33.099
1.00
35.27
A


ATOM
2911
CG2
THR
A
384
7.617
4.869
34.160
1.00
29.36
A


ATOM
2912
C
THR
A
384
8.240
2.496
32.620
1.00
29.37
A


ATOM
2913
O
THR
A
384
8.040
1.476
33.286
1.00
27.65
A


ATOM
2914
N
VAL
A
385
9.447
2.888
32.230
1.00
28.94
A


ATOM
2915
CA
VAL
A
385
10.632
2.137
32.603
1.00
28.87
A


ATOM
2916
CB
VAL
A
385
11.220
1.386
31.392
1.00
26.12
A


ATOM
2917
CG1
VAL
A
385
12.213
.339
31.862
1.00
28.78
A


ATOM
2918
CG2
VAL
A
385
10.125
.744
30.601
1.00
25.84
A


ATOM
2919
C
VAL
A
385
11.702
3.074
33.177
1.00
30.37
A


ATOM
2920
O
VAL
A
385
12.218
3.957
32.475
1.00
31.40
A


ATOM
2921
N
VAL
A
386
12.014
2.900
34.461
1.00
31.00
A


ATOM
2922
CA
VAL
A
386
13.044
3.709
35.104
1.00
30.62
A


ATOM
2923
CB
VAL
A
386
12.781
3.842
36.636
1.00
30.34
A


ATOM
2924
CG1
VAL
A
386
12.562
2.499
37.232
1.00
31.84
A


ATOM
2925
CG2
VAL
A
386
13.953
4.525
37.332
1.00
31.28
A


ATOM
2926
C
VAL
A
386
14.377
3.012
34.818
1.00
30.23
A


ATOM
2927
O
VAL
A
386
14.593
1.855
35.190
1.00
30.15
A


ATOM
2928
N
LEU
A
387
15.254
3.725
34.120
1.00
30.35
A


ATOM
2929
CA
LEU
A
387
16.556
3.213
33.724
1.00
29.55
A


ATOM
2930
CB
LEU
A
387
16.787
3.490
32.244
1.00
27.05
A


ATOM
2931
CG
LEU
A
387
15.906
2.768
31.236
1.00
24.51
A


ATOM
2932
CD1
LEU
A
387
16.047
3.379
29.854
1.00
23.58
A


ATOM
2933
CD2
LEU
A
387
16.310
1.333
31.215
1.00
23.31
A


ATOM
2934
C
LEU
A
387
17.722
3.801
34.498
1.00
32.46
A


ATOM
2935
O
LEU
A
387
17.719
4.977
34.866
1.00
33.52
A


ATOM
2936
N
LYS
A
388
18.726
2.965
34.724
1.00
34.19
A


ATOM
2937
CA
LYS
A
388
19.938
3.373
35.414
1.00
35.44
A


ATOM
2938
CB
LYS
A
388
20.313
2.348
36.483
1.00
37.24
A


ATOM
2939
CG
LYS
A
388
20.113
2.838
37.904
1.00
37.74
A


ATOM
2940
CD
LYS
A
388
21.123
3.910
38.251
1.00
37.39
A


ATOM
2941
CE
LYS
A
388
22.518
3.331
38.292
1.00
36.28
A


ATOM
2942
NZ
LYS
A
388
22.602
2.295
39.339
1.00
37.97
A


ATOM
2943
C
LYS
A
388
21.056
3.445
34.379
1.00
37.08
A


ATOM
2944
O
LYS
A
388
21.298
2.484
33.633
1.00
36.42
A


ATOM
2945
N
SER
A
389
21.726
4.590
34.320
1.00
36.60
A


ATOM
2946
CA
SER
A
389
22.825
4.769
33.387
1.00
36.00
A


ATOM
2947
CB
SER
A
389
23.022
6.259
33.114
1.00
37.01
A


ATOM
2948
OG
SER
A
389
24.013
6.455
32.130
1.00
38.47
A


ATOM
2949
C
SER
A
389
24.100
4.173
33.995
1.00
35.19
A


ATOM
2950
O
SER
A
389
24.103
3.753
35.152
1.00
32.14
A


ATOM
2951
N
VAL
A
390
25.171
4.125
33.208
1.00
36.45
A


ATOM
2952
CA
VAL
A
390
26.465
3.617
33.677
1.00
38.33
A


ATOM
2953
CB
VAL
A
390
26.885
2.274
32.987
1.00
39.52
A


ATOM
2954
CG1
VAL
A
390
25.856
1.194
33.265
1.00
38.28
A


ATOM
2955
CG2
VAL
A
390
27.069
2.473
31.481
1.00
38.97
A


ATOM
2956
C
VAL
A
390
27.521
4.669
33.355
1.00
39.34
A


ATOM
2957
O
VAL
A
390
27.405
5.399
32.367
1.00
39.68
A


ATOM
2958
N
PRO
A
391
28.567
4.767
34.189
1.00
40.39
A


ATOM
2959
CD
PRO
A
391
28.836
4.016
35.428
1.00
39.55
A


ATOM
2960
CA
PRO
A
391
29.614
5.759
33.937
1.00
40.79
A


ATOM
2961
CB
PRO
A
391
30.398
5.773
35.248
1.00
39.73
A


ATOM
2962
CG
PRO
A
391
30.282
4.369
35.712
1.00
39.36
A


ATOM
2963
C
PRO
A
391
30.473
5.395
32.736
1.00
42.01
A


ATOM
2964
O
PRO
A
391
30.563
4.223
32.354
1.00
42.53
A


ATOM
2965
N
ILE
A
392
31.084
6.414
32.135
1.00
43.00
A


ATOM
2966
CA
ILE
A
392
31.949
6.240
30.978
1.00
43.81
A


ATOM
2967
CB
ILE
A
392
31.547
7.201
29.836
1.00
43.31
A


ATOM
2968
CG2
ILE
A
392
32.465
7.006
28.631
1.00
43.26
A


ATOM
2969
CG1
ILE
A
392
30.100
6.932
29.424
1.00
43.24
A


ATOM
2970
CD1
ILE
A
392
29.649
7.728
28.224
1.00
43.15
A


ATOM
2971
C
ILE
A
392
33.389
6.526
31.391
1.00
46.16
A


ATOM
2972
O
ILE
A
392
33.938
7.571
31.052
1.00
46.65
A


ATOM
2973
N
GLN
A
393
33.978
5.586
32.130
1.00
48.86
A


ATOM
2974
CA
GLN
A
393
35.349
5.683
32.631
1.00
52.16
A


ATOM
2975
CB
GLN
A
393
35.644
7.096
33.149
1.00
54.15
A


ATOM
2976
CG
GLN
A
393
36.288
8.014
32.121
1.00
56.36
A


ATOM
2977
CD
GLN
A
393
37.683
7.566
31.722
1.00
57.85
A


ATOM
2978
OE1
GLN
A
393
37.946
6.370
31.554
1.00
57.70
A


ATOM
2979
NE2
GLN
A
393
38.585
8.529
31.553
1.00
58.57
A


ATOM
2980
C
GLN
A
393
35.601
4.682
33.756
1.00
53.17
A


ATOM
2981
O
GLN
A
393
34.634
4.021
34.186
1.00
54.06
A


ATOM
2982
OXT
GLN
A
393
36.764
4.579
34.205
1.00
54.19
A
















APPENDIX B







Arachis hypogaea STS

















ATOM
#
TYPE
RES

X
Y
Z
OCC
B





















ATOM
1
CB
VAL
A
8
6.075
38.920
83.477
1.00
46.46
A


ATOM
2
CG1
VAL
A
8
5.638
40.112
82.631
1.00
47.07
A


ATOM
3
CG2
VAL
A
8
6.142
37.664
82.618
1.00
46.26
A


ATOM
4
C
VAL
A
8
7.420
40.545
84.830
1.00
43.72
A


ATOM
5
O
VAL
A
8
7.656
41.588
84.215
1.00
43.86
A


ATOM
6
N
VAL
A
8
7.847
38.099
85.052
1.00
45.93
A


ATOM
7
CA
VAL
A
8
7.460
39.195
84.117
1.00
45.01
A


ATOM
8
N
GLN
A
9
7.122
40.527
86.125
1.00
40.46
A


ATOM
9
CA
GLN
A
9
7.067
41.763
86.892
1.00
36.43
A


ATOM
10
CB
GLN
A
9
5.854
41.761
87.831
1.00
38.00
A


ATOM
11
CG
GLN
A
9
5.885
40.706
88.921
1.00
41.02
A


ATOM
12
CD
GLN
A
9
4.619
40.706
89.764
1.00
43.48
A


ATOM
13
OE1
GLN
A
9
3.533
40.370
89.283
1.00
43.47
A


ATOM
14
NE2
GLN
A
9
4.752
41.091
91.029
1.00
46.37
A


ATOM
15
C
GLN
A
9
8.354
41.972
87.688
1.00
32.96
A


ATOM
16
O
GLN
A
9
8.509
42.974
88.380
1.00
30.32
A


ATOM
17
N
ARG
A
10
9.278
41.024
87.575
1.00
29.75
A


ATOM
18
CA
ARG
A
10
10.556
41.114
88.277
1.00
28.77
A


ATOM
19
CB
ARG
A
10
10.931
39.750
88.860
1.00
30.32
A


ATOM
20
CG
ARG
A
10
11.250
38.689
87.819
1.00
31.19
A


ATOM
21
CD
ARG
A
10
11.006
37.297
88.382
1.00
33.88
A


ATOM
22
NE
ARG
A
10
11.685
37.098
89.662
1.00
34.38
A


ATOM
23
CZ
ARG
A
10
11.524
36.031
90.441
1.00
35.70
A


ATOM
24
NH1
ARG
A
10
10.700
35.053
90.078
1.00
34.56
A


ATOM
25
NH2
ARG
A
10
12.189
35.942
91.587
1.00
30.48
A


ATOM
26
C
ARG
A
10
11.643
41.582
87.314
1.00
27.02
A


ATOM
27
O
ARG
A
10
11.532
41.382
86.107
1.00
24.60
A


ATOM
28
N
ALA
A
11
12.686
42.215
87.848
1.00
24.89
A


ATOM
29
CA
ALA
A
11
13.791
42.692
87.023
1.00
23.28
A


ATOM
30
CB
ALA
A
11
14.584
43.761
87.765
1.00
23.85
A


ATOM
31
C
ALA
A
11
14.689
41.510
86.674
1.00
24.68
A


ATOM
32
O
ALA
A
11
14.634
40.467
87.332
1.00
23.55
A


ATOM
33
N
GLU
A
12
15.521
41.674
85.649
1.00
24.82
A


ATOM
34
CA
GLU
A
12
16.402
40.597
85.208
1.00
27.69
A


ATOM
35
CB
GLU
A
12
16.503
40.599
83.682
1.00
29.83
A


ATOM
36
CG
GLU
A
12
15.246
40.125
82.979
1.00
36.49
A


ATOM
37
CD
GLU
A
12
14.809
38.741
83.440
1.00
39.68
A


ATOM
38
OE1
GLU
A
12
14.131
38.637
84.489
1.00
42.41
A


ATOM
39
OE2
GLU
A
12
15.155
37.754
82.756
1.00
42.52
A


ATOM
40
C
GLU
A
12
17.813
40.577
85.783
1.00
27.17
A


ATOM
41
O
GLU
A
12
18.260
39.553
86.306
1.00
28.17
A


ATOM
42
N
GLY
A
13
18.515
41.699
85.673
1.00
23.56
A


ATOM
43
CA
GLY
A
13
19.887
41.758
86.147
1.00
22.50
A


ATOM
44
C
GLY
A
13
20.132
42.174
87.584
1.00
19.30
A


ATOM
45
O
GLY
A
13
19.203
42.469
88.335
1.00
18.70
A


ATOM
46
N
PRO
A
14
21.402
42.203
87.997
1.00
17.89
A


ATOM
47
CD
PRO
A
14
22.595
41.786
87.239
1.00
19.36
A


ATOM
48
CA
PRO
A
14
21.751
42.591
89.366
1.00
17.15
A


ATOM
49
CB
PRO
A
14
23.218
42.177
89.475
1.00
18.61
A


ATOM
50
CG
PRO
A
14
23.721
42.365
88.068
1.00
19.45
A


ATOM
51
C
PRO
A
14
21.546
44.085
89.615
1.00
15.71
A


ATOM
52
O
PRO
A
14
21.722
44.896
88.710
1.00
16.79
A


ATOM
53
N
ALA
A
15
21.153
44.433
90.837
1.00
13.60
A


ATOM
54
CA
ALA
A
15
20.950
45.831
91.205
1.00
13.69
A


ATOM
55
CB
ALA
A
15
20.537
45.933
92.662
1.00
16.43
A


ATOM
56
C
ALA
A
15
22.270
46.562
90.973
1.00
14.74
A


ATOM
57
O
ALA
A
15
23.349
46.064
91.325
1.00
15.66
A


ATOM
58
N
THR
A
16
22.181
47.748
90.391
1.00
14.49
A


ATOM
59
CA
THR
A
16
23.369
48.520
90.063
1.00
14.54
A


ATOM
60
CB
THR
A
16
23.540
48.550
88.540
1.00
16.93
A


ATOM
61
OG1
THR
A
16
23.544
47.204
88.044
1.00
18.63
A


ATOM
62
CG2
THR
A
16
24.837
49.247
88.151
1.00
19.92
A


ATOM
63
C
THR
A
16
23.309
49.957
90.578
1.00
15.11
A


ATOM
64
O
THR
A
16
22.254
50.580
90.570
1.00
13.61
A


ATOM
65
N
VAL
A
17
24.446
50.468
91.039
1.00
14.91
A


ATOM
66
CA
VAL
A
17
24.522
51.846
91.520
1.00
15.45
A


ATOM
67
CB
VAL
A
17
25.762
52.059
92.407
1.00
16.50
A


ATOM
68
CG1
VAL
A
17
25.853
53.524
92.836
1.00
16.06
A


ATOM
69
CG2
VAL
A
17
25.683
51.144
93.628
1.00
16.07
A


ATOM
70
C
VAL
A
17
24.644
52.691
90.249
1.00
14.23
A


ATOM
71
O
VAL
A
17
25.572
52.499
89.462
1.00
14.44
A


ATOM
72
N
LEU
A
18
23.701
53.606
90.052
1.00
13.45
A


ATOM
73
CA
LEU
A
18
23.665
54.443
88.857
1.00
14.26
A


ATOM
74
CB
LEU
A
18
22.253
54.403
88.255
1.00
15.14
A


ATOM
75
CG
LEU
A
18
21.680
52.998
88.049
1.00
16.97
A


ATOM
76
CD1
LEU
A
18
20.242
53.088
87.568
1.00
18.78
A


ATOM
77
CD2
LEU
A
18
22.549
52.235
87.047
1.00
17.90
A


ATOM
78
C
LEU
A
18
24.073
55.898
89.076
1.00
14.73
A


ATOM
79
O
LEU
A
18
24.351
56.613
88.120
1.00
14.38
A


ATOM
80
N
ALA
A
19
24.098
56.340
90.329
1.00
15.35
A


ATOM
81
CA
ALA
A
19
24.475
57.717
90.636
1.00
15.25
A


ATOM
82
CB
ALA
A
19
23.388
58.680
90.168
1.00
14.75
A


ATOM
83
C
ALA
A
19
24.694
57.874
92.133
1.00
14.72
A


ATOM
84
O
ALA
A
19
24.086
57.166
92.942
1.00
14.23
A


ATOM
85
N
ILE
A
20
25.572
58.804
92.484
1.00
12.39
A


ATOM
86
CA
ILE
A
20
25.891
59.091
93.877
1.00
13.68
A


ATOM
87
CB
ILE
A
20
27.221
58.442
94.304
1.00
14.33
A


ATOM
88
CG2
ILE
A
20
27.465
58.691
95.795
1.00
14.65
A


ATOM
89
CG1
ILE
A
20
27.188
56.939
94.044
1.00
13.59
A


ATOM
90
CD1
ILE
A
20
28.534
56.272
94.254
1.00
14.71
A


ATOM
91
C
ILE
A
20
26.066
60.598
94.048
1.00
13.50
A


ATOM
92
O
ILE
A
20
26.766
61.231
93.260
1.00
15.34
A


ATOM
93
N
GLY
A
21
25.433
61.152
95.075
1.00
14.62
A


ATOM
94
CA
GLY
A
21
25.554
62.571
95.373
1.00
14.32
A


ATOM
95
C
GLY
A
21
25.774
62.738
96.872
1.00
15.92
A


ATOM
96
O
GLY
A
21
25.226
61.975
97.667
1.00
15.96
A


ATOM
97
N
THR
A
22
26.573
63.718
97.279
1.00
14.15
A


ATOM
98
CA
THR
A
22
26.816
63.918
98.703
1.00
13.46
A


ATOM
99
CB
THR
A
22
28.236
63.435
99.115
1.00
16.43
A


ATOM
100
OG1
THR
A
22
29.230
64.250
98.474
1.00
14.65
A


ATOM
101
CG2
THR
A
22
28.450
61.966
98.705
1.00
14.38
A


ATOM
102
C
THR
A
22
26.677
65.382
99.094
1.00
13.65
A


ATOM
103
O
THR
A
22
26.700
66.267
98.239
1.00
13.92
A


ATOM
104
N
ALA
A
23
26.555
65.625
100.394
1.00
12.89
A


ATOM
105
CA
ALA
A
23
26.417
66.981
100.911
1.00
13.53
A


ATOM
106
CB
ALA
A
23
24.999
67.467
100.696
1.00
13.62
A


ATOM
107
C
ALA
A
23
26.759
67.018
102.394
1.00
13.65
A


ATOM
108
O
ALA
A
23
26.660
66.007
103.090
1.00
12.16
A


ATOM
109
N
ASN
A
24
27.171
68.186
102.879
1.00
13.77
A


ATOM
110
CA
ASN
A
24
27.510
68.348
104.291
1.00
12.71
A


ATOM
111
CB
ASN
A
24
29.010
68.177
104.559
1.00
15.73
A


ATOM
112
CG
ASN
A
24
29.599
66.941
103.929
1.00
16.23
A


ATOM
113
OD1
ASN
A
24
29.953
66.940
102.747
1.00
16.19
A


ATOM
114
ND2
ASN
A
24
29.726
65.881
104.719
1.00
13.70
A


ATOM
115
C
ASN
A
24
27.199
69.776
104.702
1.00
15.49
A


ATOM
116
O
ASN
A
24
27.161
70.675
103.865
1.00
14.90
A


ATOM
117
N
PRO
A
25
26.965
70.001
105.998
1.00
17.07
A


ATOM
118
CD
PRO
A
25
26.692
69.058
107.094
1.00
16.81
A


ATOM
119
CA
PRO
A
25
26.694
71.381
106.403
1.00
17.11
A


ATOM
120
CB
PRO
A
25
26.360
71.250
107.892
1.00
17.63
A


ATOM
121
CG
PRO
A
25
26.961
69.912
108.300
1.00
19.53
A


ATOM
122
C
PRO
A
25
27.996
72.152
106.118
1.00
20.50
A


ATOM
123
O
PRO
A
25
29.087
71.580
106.161
1.00
18.51
A


ATOM
124
N
PRO
A
26
27.897
73.451
105.805
1.00
20.76
A


ATOM
125
CD
PRO
A
26
26.654
74.240
105.817
1.00
22.95
A


ATOM
126
CA
PRO
A
26
29.053
74.305
105.499
1.00
21.72
A


ATOM
127
CB
PRO
A
26
28.399
75.619
105.080
1.00
24.14
A


ATOM
128
CG
PRO
A
26
27.176
75.660
105.947
1.00
25.19
A


ATOM
129
C
PRO
A
26
30.106
74.512
106.590
1.00
21.55
A


ATOM
130
O
PRO
A
26
31.299
74.601
106.296
1.00
23.48
A


ATOM
131
N
ASN
A
27
29.671
74.598
107.839
1.00
20.95
A


ATOM
132
CA
ASN
A
27
30.589
74.813
108.954
1.00
21.75
A


ATOM
133
CB
ASN
A
27
29.788
74.956
110.245
1.00
20.97
A


ATOM
134
CG
ASN
A
27
30.650
75.307
111.433
1.00
22.82
A


ATOM
135
OD1
ASN
A
27
31.412
76.273
111.396
1.00
21.91
A


ATOM
136
ND2
ASN
A
27
30.524
74.530
112.507
1.00
21.17
A


ATOM
137
C
ASN
A
27
31.620
73.695
109.108
1.00
21.96
A


ATOM
138
O
ASN
A
27
31.258
72.544
109.367
1.00
21.55
A


ATOM
139
N
CYS
A
28
32.898
74.042
108.957
1.00
21.41
A


ATOM
140
CA
CYS
A
28
33.993
73.077
109.082
1.00
24.36
A


ATOM
141
CB
CYS
A
28
34.957
73.194
107.905
1.00
26.72
A


ATOM
142
SG
CYS
A
28
34.296
72.622
106.349
1.00
32.06
A


ATOM
143
C
CYS
A
28
34.793
73.287
110.351
1.00
25.08
A


ATOM
144
O
CYS
A
28
35.100
74.422
110.713
1.00
26.06
A


ATOM
145
N
ILE
A
29
35.143
72.197
111.024
1.00
23.86
A


ATOM
146
CA
ILE
A
29
35.940
72.317
112.233
1.00
23.59
A


ATOM
147
CB
ILE
A
29
35.266
71.650
113.451
1.00
26.59
A


ATOM
148
CG2
ILE
A
29
33.906
72.300
113.715
1.00
26.52
A


ATOM
149
CG1
ILE
A
29
35.128
70.148
113.215
1.00
27.45
A


ATOM
150
CD1
ILE
A
29
34.664
69.387
114.434
1.00
32.28
A


ATOM
151
C
ILE
A
29
37.322
71.711
112.042
1.00
22.44
A


ATOM
152
O
ILE
A
29
37.474
70.597
111.536
1.00
19.22
A


ATOM
153
N
ASP
A
30
38.334
72.476
112.435
1.00
21.63
A


ATOM
154
CA
ASP
A
30
39.718
72.044
112.340
1.00
21.62
A


ATOM
155
CB
ASP
A
30
40.640
73.254
112.432
1.00
25.37
A


ATOM
156
CG
ASP
A
30
42.069
72.915
112.107
1.00
26.61
A


ATOM
157
OD1
ASP
A
30
42.551
71.875
112.595
1.00
29.92
A


ATOM
158
OD2
ASP
A
30
42.713
73.691
111.369
1.00
31.88
A


ATOM
159
C
ASP
A
30
39.978
71.105
113.517
1.00
20.05
A


ATOM
160
O
ASP
A
30
39.899
71.513
114.671
1.00
19.05
A


ATOM
161
N
GLN
A
31
40.292
69.849
113.221
1.00
20.36
A


ATOM
162
CA
GLN
A
31
40.529
68.856
114.265
1.00
19.11
A


ATOM
163
CB
GLN
A
31
40.742
67.480
113.625
1.00
17.44
A


ATOM
164
CG
GLN
A
31
40.787
66.306
114.596
1.00
21.06
A


ATOM
165
CD
GLN
A
31
39.430
65.957
115.189
1.00
21.80
A


ATOM
166
OE1
GLN
A
31
39.207
64.826
115.619
1.00
25.66
A


ATOM
167
NE2
GLN
A
31
38.525
66.926
115.230
1.00
18.69
A


ATOM
168
C
GLN
A
31
41.722
69.200
115.151
1.00
19.87
A


ATOM
169
O
GLN
A
31
41.703
68.931
116.348
1.00
18.46
A


ATOM
170
N
SER
A
32
42.752
69.803
114.564
1.00
20.70
A


ATOM
171
CA
SER
A
32
43.956
70.157
115.311
1.00
22.04
A


ATOM
172
CB
SER
A
32
45.019
70.734
114.363
1.00
22.43
A


ATOM
173
OG
SER
A
32
44.665
72.032
113.906
1.00
24.69
A


ATOM
174
C
SER
A
32
43.694
71.143
116.453
1.00
22.19
A


ATOM
175
O
SER
A
32
44.441
71.178
117.429
1.00
22.11
A


ATOM
176
N
THR
A
33
42.631
71.933
116.342
1.00
21.38
A


ATOM
177
CA
THR
A
33
42.308
72.911
117.379
1.00
20.69
A


ATOM
178
CB
THR
A
33
42.300
74.343
116.801
1.00
22.44
A


ATOM
179
OG1
THR
A
33
41.251
74.459
115.834
1.00
22.63
A


ATOM
180
CG2
THR
A
33
43.635
74.664
116.132
1.00
24.73
A


ATOM
181
C
THR
A
33
40.943
72.663
118.028
1.00
18.62
A


ATOM
182
O
THR
A
33
40.438
73.515
118.754
1.00
18.50
A


ATOM
183
N
TYR
A
34
40.346
71.499
117.787
1.00
16.74
A


ATOM
184
CA
TYR
A
34
39.029
71.226
118.355
1.00
16.94
A


ATOM
185
CB
TYR
A
34
38.451
69.928
117.801
1.00
17.19
A


ATOM
186
CG
TYR
A
34
36.975
69.790
118.083
1.00
17.35
A


ATOM
187
CD1
TYR
A
34
36.058
70.685
117.526
1.00
17.15
A


ATOM
188
CE1
TYR
A
34
34.693
70.575
117.788
1.00
19.47
A


ATOM
189
CD2
TYR
A
34
36.491
68.780
118.911
1.00
16.08
A


ATOM
190
CE2
TYR
A
34
35.133
68.661
119.183
1.00
17.26
A


ATOM
191
CZ
TYR
A
34
34.237
69.562
118.617
1.00
17.18
A


ATOM
192
OH
TYR
A
34
32.891
69.457
118.893
1.00
16.72
A


ATOM
193
C
TYR
A
34
38.992
71.157
119.874
1.00
17.22
A


ATOM
194
O
TYR
A
34
38.015
71.583
120.490
1.00
18.03
A


ATOM
195
N
ALA
A
35
40.043
70.604
120.474
1.00
17.84
A


ATOM
196
CA
ALA
A
35
40.107
70.489
121.926
1.00
18.20
A


ATOM
197
CB
ALA
A
35
41.448
69.913
122.355
1.00
18.99
A


ATOM
198
C
ALA
A
35
39.904
71.867
122.550
1.00
18.82
A


ATOM
199
O
ALA
A
35
39.091
72.028
123.448
1.00
17.85
A


ATOM
200
N
ASP
A
36
40.653
72.858
122.073
1.00
18.76
A


ATOM
201
CA
ASP
A
36
40.516
74.213
122.604
1.00
19.92
A


ATOM
202
CB
ASP
A
36
41.438
75.190
121.864
1.00
22.24
A


ATOM
203
CG
ASP
A
36
42.903
74.972
122.181
1.00
25.34
A


ATOM
204
OD1
ASP
A
36
43.217
74.578
123.324
1.00
25.77
A


ATOM
205
OD2
ASP
A
36
43.745
75.213
121.287
1.00
29.04
A


ATOM
206
C
ASP
A
36
39.078
74.709
122.478
1.00
20.11
A


ATOM
207
O
ASP
A
36
38.477
75.179
123.452
1.00
19.46
A


ATOM
208
N
TYR
A
37
38.538
74.611
121.266
1.00
18.02
A


ATOM
209
CA
TYR
A
37
37.180
75.057
120.991
1.00
17.23
A


ATOM
210
CB
TYR
A
37
36.846
74.817
119.514
1.00
16.64
A


ATOM
211
CG
TYR
A
37
35.399
75.092
119.152
1.00
19.58
A


ATOM
212
CD1
TYR
A
37
34.945
76.396
118.946
1.00
19.88
A


ATOM
213
CE1
TYR
A
37
33.615
76.654
118.611
1.00
21.95
A


ATOM
214
CD2
TYR
A
37
34.482
74.046
119.020
1.00
18.32
A


ATOM
215
CE2
TYR
A
37
33.153
74.290
118.690
1.00
21.26
A


ATOM
216
CZ
TYR
A
37
32.725
75.598
118.483
1.00
22.45
A


ATOM
217
OH
TYR
A
37
31.417
75.846
118.136
1.00
22.04
A


ATOM
218
C
TYR
A
37
36.158
74.342
121.865
1.00
17.32
A


ATOM
219
O
TYR
A
37
35.352
74.977
122.553
1.00
17.84
A


ATOM
220
N
TYR
A
38
36.198
73.013
121.829
1.00
17.92
A


ATOM
221
CA
TYR
A
38
35.270
72.178
122.585
1.00
17.56
A


ATOM
222
CB
TYR
A
38
35.626
70.702
122.369
1.00
16.77
A


ATOM
223
CG
TYR
A
38
34.755
69.726
123.116
1.00
16.04
A


ATOM
224
CD1
TYR
A
38
33.436
69.484
122.724
1.00
17.14
A


ATOM
225
CE1
TYR
A
38
32.635
68.580
123.420
1.00
17.33
A


ATOM
226
CD2
TYR
A
38
35.251
69.039
124.224
1.00
16.93
A


ATOM
227
CE2
TYR
A
38
34.466
68.140
124.923
1.00
17.51
A


ATOM
228
CZ
TYR
A
38
33.161
67.913
124.519
1.00
16.76
A


ATOM
229
OH
TYR
A
38
32.398
67.030
125.234
1.00
17.13
A


ATOM
230
C
TYR
A
38
35.248
72.506
124.076
1.00
18.55
A


ATOM
231
O
TYR
A
38
34.185
72.752
124.646
1.00
18.23
A


ATOM
232
N
PHE
A
39
36.412
72.517
124.714
1.00
19.37
A


ATOM
233
CA
PHE
A
39
36.453
72.813
126.143
1.00
19.56
A


ATOM
234
CB
PHE
A
39
37.816
72.429
126.722
1.00
19.04
A


ATOM
235
CG
PHE
A
39
37.907
70.975
127.108
1.00
20.13
A


ATOM
236
CD1
PHE
A
39
37.759
70.583
128.434
1.00
21.28
A


ATOM
237
CD2
PHE
A
39
38.075
69.993
126.135
1.00
19.97
A


ATOM
238
CE1
PHE
A
39
37.774
69.230
128.788
1.00
21.03
A


ATOM
239
CE2
PHE
A
39
38.091
68.645
126.476
1.00
19.95
A


ATOM
240
CZ
PHE
A
39
37.939
68.262
127.806
1.00
21.19
A


ATOM
241
C
PHE
A
39
36.086
74.255
126.485
1.00
20.19
A


ATOM
242
O
PHE
A
39
35.732
74.553
127.622
1.00
22.34
A


ATOM
243
N
ARG
A
40
36.144
75.143
125.499
1.00
20.54
A


ATOM
244
CA
ARG
A
40
35.773
76.534
125.734
1.00
20.65
A


ATOM
245
CB
ARG
A
40
36.470
77.456
124.726
1.00
19.69
A


ATOM
246
CG
ARG
A
40
36.044
78.918
124.836
1.00
22.28
A


ATOM
247
CD
ARG
A
40
36.875
79.813
123.925
1.00
23.38
A


ATOM
248
NE
ARG
A
40
36.646
79.562
122.503
1.00
23.95
A


ATOM
249
CZ
ARG
A
40
35.519
79.851
121.861
1.00
24.46
A


ATOM
250
NH1
ARG
A
40
34.507
80.404
122.510
1.00
25.71
A


ATOM
251
NH2
ARG
A
40
35.403
79.585
120.567
1.00
26.85
A


ATOM
252
C
ARG
A
40
34.257
76.707
125.627
1.00
20.55
A


ATOM
253
O
ARG
A
40
33.620
77.242
126.540
1.00
18.76
A


ATOM
254
N
VAL
A
41
33.674
76.245
124.522
1.00
20.21
A


ATOM
255
CA
VAL
A
41
32.236
76.385
124.338
1.00
21.46
A


ATOM
256
CB
VAL
A
41
31.790
76.005
122.892
1.00
22.92
A


ATOM
257
CG1
VAL
A
41
32.537
76.875
121.879
1.00
23.74
A


ATOM
258
CG2
VAL
A
41
32.037
74.524
122.619
1.00
21.78
A


ATOM
259
C
VAL
A
41
31.417
75.599
125.350
1.00
21.29
A


ATOM
260
O
VAL
A
41
30.261
75.928
125.588
1.00
20.77
A


ATOM
261
N
THR
A
42
32.001
74.562
125.949
1.00
21.64
A


ATOM
262
CA
THR
A
42
31.274
73.785
126.951
1.00
22.13
A


ATOM
263
CB
THR
A
42
31.532
72.254
126.828
1.00
21.03
A


ATOM
264
OG1
THR
A
42
32.914
71.968
127.082
1.00
19.85
A


ATOM
265
CG2
THR
A
42
31.155
71.758
125.440
1.00
18.84
A


ATOM
266
C
THR
A
42
31.670
74.237
128.360
1.00
24.77
A


ATOM
267
O
THR
A
42
31.365
73.564
129.344
1.00
24.42
A


ATOM
268
N
ASN
A
43
32.357
75.375
128.442
1.00
25.63
A


ATOM
269
CA
ASN
A
43
32.781
75.945
129.722
1.00
27.73
A


ATOM
270
CB
ASN
A
43
31.560
76.502
130.452
1.00
32.42
A


ATOM
271
CG
ASN
A
43
30.721
77.407
129.570
1.00
36.22
A


ATOM
272
OD1
ASN
A
43
31.175
78.472
129.145
1.00
39.75
A


ATOM
273
ND2
ASN
A
43
29.492
76.985
129.285
1.00
38.09
A


ATOM
274
C
ASN
A
43
33.494
74.939
130.624
1.00
27.61
A


ATOM
275
O
ASN
A
43
33.232
74.876
131.829
1.00
26.66
A


ATOM
276
N
SER
A
44
34.405
74.168
130.046
1.00
26.69
A


ATOM
277
CA
SER
A
44
35.125
73.152
130.799
1.00
27.90
A


ATOM
278
CB
SER
A
44
34.892
71.781
130.161
1.00
26.68
A


ATOM
279
OG
SER
A
44
33.509
71.489
130.100
1.00
28.08
A


ATOM
280
C
SER
A
44
36.616
73.438
130.870
1.00
28.33
A


ATOM
281
O
SER
A
44
37.422
72.520
130.989
1.00
28.25
A


ATOM
282
N
GLU
A
45
36.973
74.717
130.803
1.00
30.31
A


ATOM
283
CA
GLU
A
45
38.372
75.137
130.855
1.00
32.52
A


ATOM
284
CB
GLU
A
45
38.460
76.666
130.804
1.00
36.20
A


ATOM
285
CG
GLU
A
45
37.862
77.296
129.556
1.00
40.59
A


ATOM
286
CD
GLU
A
45
38.635
76.954
128.297
1.00
43.46
A


ATOM
287
OE1
GLU
A
45
38.290
77.492
127.224
1.00
44.77
A


ATOM
288
OE2
GLU
A
45
39.589
76.148
128.378
1.00
46.65
A


ATOM
289
C
GLU
A
45
39.082
74.635
132.109
1.00
31.09
A


ATOM
290
O
GLU
A
45
40.261
74.288
132.069
1.00
32.23
A


ATOM
291
N
HIS
A
46
38.356
74.590
133.220
1.00
30.26
A


ATOM
292
CA
HIS
A
46
38.921
74.148
134.489
1.00
30.21
A


ATOM
293
CB
HIS
A
46
37.915
74.373
135.624
1.00
30.18
A


ATOM
294
CG
HIS
A
46
36.608
73.672
135.423
1.00
31.08
A


ATOM
295
CD2
HIS
A
46
36.080
72.580
136.025
1.00
31.68
A


ATOM
296
ND1
HIS
A
46
35.678
74.082
134.491
1.00
31.46
A


ATOM
297
CE1
HIS
A
46
34.635
73.272
134.527
1.00
31.49
A


ATOM
298
NE2
HIS
A
46
34.854
72.352
135.450
1.00
31.69
A


ATOM
299
C
HIS
A
46
39.384
72.691
134.505
1.00
29.90
A


ATOM
300
O
HIS
A
46
40.153
72.301
135.383
1.00
28.22
A


ATOM
301
N
MET
A
47
38.920
71.891
133.544
1.00
29.28
A


ATOM
302
CA
MET
A
47
39.307
70.477
133.471
1.00
28.84
A


ATOM
303
CB
MET
A
47
38.214
69.664
132.771
1.00
28.86
A


ATOM
304
CG
MET
A
47
36.808
69.935
133.286
1.00
30.82
A


ATOM
305
SD
MET
A
47
35.578
68.879
132.493
1.00
31.81
A


ATOM
306
CE
MET
A
47
35.684
67.427
133.551
1.00
33.73
A


ATOM
307
C
MET
A
47
40.621
70.327
132.705
1.00
28.88
A


ATOM
308
O
MET
A
47
40.689
69.627
131.693
1.00
27.03
A


ATOM
309
N
THR
A
48
41.665
70.983
133.199
1.00
29.25
A


ATOM
310
CA
THR
A
48
42.974
70.955
132.554
1.00
29.28
A


ATOM
311
CB
THR
A
48
44.045
71.626
133.450
1.00
30.40
A


ATOM
312
OG1
THR
A
48
44.133
70.932
134.699
1.00
31.38
A


ATOM
313
CG2
THR
A
48
43.681
73.081
133.710
1.00
31.23
A


ATOM
314
C
THR
A
48
43.485
69.575
132.128
1.00
29.36
A


ATOM
315
O
THR
A
48
43.883
69.394
130.977
1.00
30.13
A


ATOM
316
N
ASP
A
49
43.475
68.603
133.036
1.00
28.72
A


ATOM
317
CA
ASP
A
49
43.974
67.271
132.697
1.00
29.59
A


ATOM
318
CB
ASP
A
49
43.992
66.367
133.928
1.00
33.21
A


ATOM
319
CG
ASP
A
49
44.545
64.985
133.621
1.00
36.83
A


ATOM
320
OD1
ASP
A
49
45.679
64.903
133.102
1.00
39.96
A


ATOM
321
OD2
ASP
A
49
43.850
63.981
133.893
1.00
38.97
A


ATOM
322
C
ASP
A
49
43.172
66.588
131.592
1.00
28.05
A


ATOM
323
O
ASP
A
49
43.744
66.023
130.660
1.00
28.22
A


ATOM
324
N
LEU
A
50
41.851
66.637
131.701
1.00
25.60
A


ATOM
325
CA
LEU
A
50
40.991
66.011
130.704
1.00
23.87
A


ATOM
326
CB
LEU
A
50
39.527
66.120
131.131
1.00
21.93
A


ATOM
327
CG
LEU
A
50
38.534
65.261
130.350
1.00
19.98
A


ATOM
328
CD1
LEU
A
50
38.945
63.789
130.429
1.00
19.09
A


ATOM
329
CD2
LEU
A
50
37.146
65.460
130.927
1.00
20.31
A


ATOM
330
C
LEU
A
50
41.189
66.662
129.336
1.00
23.68
A


ATOM
331
O
LEU
A
50
41.215
65.976
128.313
1.00
22.19
A


ATOM
332
N
LYS
A
51
41.332
67.985
129.316
1.00
23.84
A


ATOM
333
CA
LYS
A
51
41.532
68.686
128.052
1.00
25.09
A


ATOM
334
CB
LYS
A
51
41.650
70.199
128.283
1.00
25.49
A


ATOM
335
CG
LYS
A
51
41.828
71.005
126.999
1.00
26.33
A


ATOM
336
CD
LYS
A
51
41.886
72.504
127.280
1.00
28.75
A


ATOM
337
CE
LYS
A
51
42.142
73.288
126.007
1.00
29.76
A


ATOM
338
NZ
LYS
A
51
42.144
74.756
126.260
1.00
30.99
A


ATOM
339
C
LYS
A
51
42.785
68.170
127.344
1.00
26.21
A


ATOM
340
O
LYS
A
51
42.782
67.971
126.130
1.00
24.74
A


ATOM
341
N
LYS
A
52
43.856
67.949
128.103
1.00
27.17
A


ATOM
342
CA
LYS
A
52
45.098
67.449
127.516
1.00
28.10
A


ATOM
343
CB
LYS
A
52
46.194
67.352
128.582
1.00
30.83
A


ATOM
344
CG
LYS
A
52
46.591
68.687
129.190
1.00
34.28
A


ATOM
345
CD
LYS
A
52
47.635
68.497
130.279
1.00
37.20
A


ATOM
346
CE
LYS
A
52
47.985
69.816
130.945
1.00
38.95
A


ATOM
347
NZ
LYS
A
52
48.982
69.624
132.030
1.00
41.28
A


ATOM
348
C
LYS
A
52
44.873
66.076
126.888
1.00
26.97
A


ATOM
349
O
LYS
A
52
45.366
65.792
125.797
1.00
26.02
A


ATOM
350
N
LYS
A
53
44.122
65.228
127.583
1.00
26.21
A


ATOM
351
CA
LYS
A
53
43.831
63.892
127.086
1.00
25.04
A


ATOM
352
CB
LYS
A
53
43.067
63.086
128.140
1.00
24.64
A


ATOM
353
CG
LYS
A
53
43.877
62.781
129.392
1.00
28.22
A


ATOM
354
CD
LYS
A
53
43.065
61.990
130.408
1.00
30.66
A


ATOM
355
CE
LYS
A
53
43.880
61.718
131.666
1.00
33.54
A


ATOM
356
NZ
LYS
A
53
43.126
60.909
132.667
1.00
36.02
A


ATOM
357
C
LYS
A
53
43.012
63.962
125.798
1.00
23.42
A


ATOM
358
O
LYS
A
53
43.226
63.173
124.879
1.00
22.62
A


ATOM
359
N
PHE
A
54
42.086
64.915
125.732
1.00
23.36
A


ATOM
360
CA
PHE
A
54
41.237
65.066
124.550
1.00
22.90
A


ATOM
361
CB
PHE
A
54
40.098
66.055
124.820
1.00
22.20
A


ATOM
362
CG
PHE
A
54
39.044
66.072
123.740
1.00
20.84
A


ATOM
363
CD1
PHE
A
54
38.409
64.897
123.352
1.00
19.63
A


ATOM
364
CD2
PHE
A
54
38.682
67.260
123.115
1.00
20.10
A


ATOM
365
CE1
PHE
A
54
37.432
64.905
122.357
1.00
18.43
A


ATOM
366
CE2
PHE
A
54
37.706
67.276
122.122
1.00
19.37
A


ATOM
367
CZ
PHE
A
54
37.081
66.097
121.742
1.00
18.82
A


ATOM
368
C
PHE
A
54
42.048
65.539
123.354
1.00
23.85
A


ATOM
369
O
PHE
A
54
41.812
65.112
122.219
1.00
23.78
A


ATOM
370
N
GLN
A
55
43.000
66.432
123.603
1.00
24.10
A


ATOM
371
CA
GLN
A
55
43.842
66.930
122.528
1.00
24.91
A


ATOM
372
CB
GLN
A
55
44.832
67.974
123.062
1.00
26.37
A


ATOM
373
CG
GLN
A
55
45.921
68.373
122.072
1.00
28.68
A


ATOM
374
CD
GLN
A
55
45.411
69.175
120.884
1.00
30.30
A


ATOM
375
OE1
GLN
A
55
46.060
69.228
119.839
1.00
31.71
A


ATOM
376
NE2
GLN
A
55
44.259
69.820
121.044
1.00
30.29
A


ATOM
377
C
GLN
A
55
44.586
65.725
121.967
1.00
24.46
A


ATOM
378
O
GLN
A
55
44.767
65.601
120.761
1.00
22.48
A


ATOM
379
N
ARG
A
56
44.997
64.828
122.858
1.00
24.95
A


ATOM
380
CA
ARG
A
56
45.719
63.625
122.468
1.00
25.91
A


ATOM
381
CB
ARG
A
56
46.171
62.866
123.720
1.00
29.99
A


ATOM
382
CG
ARG
A
56
47.559
62.249
123.624
1.00
36.86
A


ATOM
383
CD
ARG
A
56
48.647
63.324
123.571
1.00
40.43
A


ATOM
384
NE
ARG
A
56
48.699
64.137
124.787
1.00
44.69
A


ATOM
385
CZ
ARG
A
56
48.992
63.667
125.998
1.00
46.01
A


ATOM
386
NH1
ARG
A
56
49.263
62.379
126.168
1.00
47.48
A


ATOM
387
NH2
ARG
A
56
49.015
64.485
127.044
1.00
46.66
A


ATOM
388
C
ARG
A
56
44.804
62.739
121.618
1.00
24.27
A


ATOM
389
O
ARG
A
56
45.215
62.221
120.574
1.00
24.04
A


ATOM
390
N
ILE
A
57
43.565
62.572
122.075
1.00
21.82
A


ATOM
391
CA
ILE
A
57
42.579
61.765
121.367
1.00
20.34
A


ATOM
392
CB
ILE
A
57
41.237
61.729
122.129
1.00
20.57
A


ATOM
393
CG2
ILE
A
57
40.154
61.093
121.261
1.00
21.54
A


ATOM
394
CG1
ILE
A
57
41.399
60.948
123.438
1.00
20.21
A


ATOM
395
CD1
ILE
A
57
40.171
60.973
124.315
1.00
19.50
A


ATOM
396
C
ILE
A
57
42.337
62.329
119.968
1.00
20.51
A


ATOM
397
O
ILE
A
57
42.396
61.599
118.986
1.00
20.89
A


ATOM
398
N
CYS
A
58
42.076
63.630
119.879
1.00
19.30
A


ATOM
399
CA
CYS
A
58
41.823
64.251
118.587
1.00
20.99
A


ATOM
400
CB
CYS
A
58
41.533
65.745
118.759
1.00
19.32
A


ATOM
401
SG
CYS
A
58
39.917
66.082
119.509
1.00
18.88
A


ATOM
402
C
CYS
A
58
42.966
64.047
117.601
1.00
22.44
A


ATOM
403
O
CYS
A
58
42.732
63.850
116.412
1.00
23.07
A


ATOM
404
N
GLU
A
59
44.200
64.077
118.092
1.00
24.02
A


ATOM
405
CA
GLU
A
59
45.363
63.892
117.225
1.00
26.24
A


ATOM
406
CB
GLU
A
59
46.644
64.284
117.972
1.00
28.50
A


ATOM
407
CG
GLU
A
59
46.606
65.706
118.527
1.00
33.23
A


ATOM
408
CD
GLU
A
59
47.855
66.085
119.315
1.00
35.09
A


ATOM
409
OE1
GLU
A
59
48.343
65.248
120.109
1.00
36.66
A


ATOM
410
OE2
GLU
A
59
48.338
67.227
119.149
1.00
34.23
A


ATOM
411
C
GLU
A
59
45.455
62.445
116.741
1.00
26.77
A


ATOM
412
O
GLU
A
59
45.872
62.177
115.614
1.00
26.70
A


ATOM
413
N
ARG
A
60
45.046
61.518
117.596
1.00
26.73
A


ATOM
414
CA
ARG
A
60
45.079
60.100
117.264
1.00
28.79
A


ATOM
415
CB
ARG
A
60
44.919
59.274
118.544
1.00
33.01
A


ATOM
416
CG
ARG
A
60
46.132
59.301
119.456
1.00
39.19
A


ATOM
417
CD
ARG
A
60
47.211
58.346
118.956
1.00
45.62
A


ATOM
418
NE
ARG
A
60
47.412
57.224
119.875
1.00
49.49
A


ATOM
419
CZ
ARG
A
60
46.455
56.383
120.261
1.00
51.76
A


ATOM
420
NH1
ARG
A
60
45.215
56.526
119.809
1.00
52.07
A


ATOM
421
NH2
ARG
A
60
46.735
55.399
121.109
1.00
53.18
A


ATOM
422
C
ARG
A
60
44.024
59.664
116.240
1.00
25.81
A


ATOM
423
O
ARG
A
60
44.225
58.686
115.524
1.00
23.81
A


ATOM
424
N
THR
A
61
42.911
60.388
116.160
1.00
23.41
A


ATOM
425
CA
THR
A
61
41.834
60.023
115.235
1.00
22.16
A


ATOM
426
CB
THR
A
61
40.629
60.966
115.359
1.00
19.80
A


ATOM
427
OG1
THR
A
61
41.003
62.269
114.896
1.00
17.03
A


ATOM
428
CG2
THR
A
61
40.150
61.047
116.802
1.00
20.05
A


ATOM
429
C
THR
A
61
42.237
60.045
113.768
1.00
22.06
A


ATOM
430
O
THR
A
61
41.616
59.382
112.942
1.00
20.90
A


ATOM
431
N
GLN
A
62
43.275
60.814
113.457
1.00
21.51
A


ATOM
432
CA
GLN
A
62
43.749
60.979
112.089
1.00
21.94
A


ATOM
433
CB
GLN
A
62
44.232
59.649
111.503
1.00
24.19
A


ATOM
434
CG
GLN
A
62
45.428
59.093
112.270
1.00
25.12
A


ATOM
435
CD
GLN
A
62
46.325
58.218
111.429
1.00
28.57
A


ATOM
436
OE1
GLN
A
62
45.857
57.352
110.687
1.00
28.23
A


ATOM
437
NE2
GLN
A
62
47.633
58.430
111.550
1.00
29.81
A


ATOM
438
C
GLN
A
62
42.654
61.602
111.227
1.00
21.62
A


ATOM
439
O
GLN
A
62
42.545
61.345
110.021
1.00
21.13
A


ATOM
440
N
ILE
A
63
41.829
62.413
111.881
1.00
18.54
A


ATOM
441
CA
ILE
A
63
40.763
63.155
111.220
1.00
16.85
A


ATOM
442
CB
ILE
A
63
39.475
63.188
112.062
1.00
15.18
A


ATOM
443
CG2
ILE
A
63
38.482
64.153
111.446
1.00
17.26
A


ATOM
444
CG1
ILE
A
63
38.854
61.793
112.138
1.00
13.24
A


ATOM
445
CD1
ILE
A
63
37.704
61.705
113.129
1.00
12.22
A


ATOM
446
C
ILE
A
63
41.334
64.572
111.167
1.00
18.36
A


ATOM
447
O
ILE
A
63
41.882
65.053
112.160
1.00
17.80
A


ATOM
448
N
LYS
A
64
41.227
65.231
110.022
1.00
18.39
A


ATOM
449
CA
LYS
A
64
41.757
66.587
109.884
1.00
20.17
A


ATOM
450
CB
LYS
A
64
42.534
66.715
108.568
1.00
21.80
A


ATOM
451
CG
LYS
A
64
43.868
65.976
108.573
1.00
27.09
A


ATOM
452
CD
LYS
A
64
44.813
66.599
109.588
1.00
31.09
A


ATOM
453
CE
LYS
A
64
46.056
65.749
109.806
1.00
33.75
A


ATOM
454
NZ
LYS
A
64
45.731
64.450
110.462
1.00
36.45
A


ATOM
455
C
LYS
A
64
40.661
67.637
109.930
1.00
20.31
A


ATOM
456
O
LYS
A
64
40.845
68.725
110.491
1.00
17.10
A


ATOM
457
N
ASN
A
65
39.520
67.301
109.335
1.00
19.52
A


ATOM
458
CA
ASN
A
65
38.376
68.206
109.273
1.00
19.30
A


ATOM
459
CB
ASN
A
65
38.409
68.985
107.950
1.00
21.83
A


ATOM
460
CG
ASN
A
65
37.084
69.676
107.634
1.00
25.41
A


ATOM
461
OD1
ASN
A
65
36.120
69.041
107.184
1.00
26.40
A


ATOM
462
ND2
ASN
A
65
37.031
70.978
107.871
1.00
24.80
A


ATOM
463
C
ASN
A
65
37.056
67.454
109.391
1.00
18.97
A


ATOM
464
O
ASN
A
65
36.943
66.299
108.969
1.00
17.44
A


ATOM
465
N
ARG
A
66
36.069
68.117
109.986
1.00
18.13
A


ATOM
466
CA
ARG
A
66
34.733
67.553
110.146
1.00
16.96
A


ATOM
467
CB
ARG
A
66
34.529
67.023
111.566
1.00
16.26
A


ATOM
468
CG
ARG
A
66
35.173
65.679
111.852
1.00
16.61
A


ATOM
469
CD
ARG
A
66
34.738
65.183
113.224
1.00
16.24
A


ATOM
470
NE
ARG
A
66
35.405
65.920
114.289
1.00
15.56
A


ATOM
471
CZ
ARG
A
66
34.992
65.947
115.550
1.00
17.32
A


ATOM
472
NH1
ARG
A
66
33.901
65.287
115.908
1.00
17.58
A


ATOM
473
NH2
ARG
A
66
35.685
66.616
116.465
1.00
17.79
A


ATOM
474
C
ARG
A
66
33.701
68.637
109.880
1.00
17.04
A


ATOM
475
O
ARG
A
66
33.912
69.796
110.237
1.00
17.53
A


ATOM
476
N
HIS
A
67
32.602
68.277
109.228
1.00
15.73
A


ATOM
477
CA
HIS
A
67
31.546
69.245
108.984
1.00
17.68
A


ATOM
478
CB
HIS
A
67
30.864
68.997
107.635
1.00
18.72
A


ATOM
479
CG
HIS
A
67
31.713
69.348
106.454
1.00
21.98
A


ATOM
480
CD2
HIS
A
67
31.716
70.441
105.653
1.00
20.76
A


ATOM
481
ND1
HIS
A
67
32.714
68.527
105.982
1.00
21.72
A


ATOM
482
CE1
HIS
A
67
33.295
69.097
104.941
1.00
21.39
A


ATOM
483
NE2
HIS
A
67
32.707
70.259
104.721
1.00
23.60
A


ATOM
484
C
HIS
A
67
30.540
69.069
110.118
1.00
18.33
A


ATOM
485
O
HIS
A
67
30.176
67.941
110.464
1.00
17.18
A


ATOM
486
N
MET
A
68
30.117
70.178
110.713
1.00
16.86
A


ATOM
487
CA
MET
A
68
29.163
70.124
111.807
1.00
20.49
A


ATOM
488
CB
MET
A
68
29.893
70.228
113.155
1.00
23.32
A


ATOM
489
CG
MET
A
68
30.914
69.116
113.386
1.00
28.72
A


ATOM
490
SD
MET
A
68
31.545
69.023
115.086
1.00
37.96
A


ATOM
491
CE
MET
A
68
31.064
67.331
115.520
1.00
34.14
A


ATOM
492
C
MET
A
68
28.106
71.213
111.710
1.00
19.55
A


ATOM
493
O
MET
A
68
28.424
72.397
111.603
1.00
19.23
A


ATOM
494
N
TYR
A
69
26.844
70.800
111.736
1.00
19.71
A


ATOM
495
CA
TYR
A
69
25.733
71.738
111.685
1.00
20.15
A


ATOM
496
CB
TYR
A
69
24.401
70.981
111.659
1.00
20.47
A


ATOM
497
CG
TYR
A
69
23.253
71.748
112.277
1.00
20.28
A


ATOM
498
CD1
TYR
A
69
22.713
72.874
111.650
1.00
22.00
A


ATOM
499
CE1
TYR
A
69
21.668
73.595
112.239
1.00
22.79
A


ATOM
500
CD2
TYR
A
69
22.723
71.363
113.502
1.00
20.81
A


ATOM
501
CE2
TYR
A
69
21.688
72.069
114.094
1.00
21.13
A


ATOM
502
CZ
TYR
A
69
21.163
73.184
113.461
1.00
22.53
A


ATOM
503
OH
TYR
A
69
20.136
73.877
114.063
1.00
22.91
A


ATOM
504
C
TYR
A
69
25.789
72.632
112.918
1.00
19.58
A


ATOM
505
O
TYR
A
69
25.474
73.820
112.853
1.00
18.63
A


ATOM
506
N
LEU
A
70
26.195
72.052
114.044
1.00
17.07
A


ATOM
507
CA
LEU
A
70
26.286
72.799
115.290
1.00
18.70
A


ATOM
508
CB
LEU
A
70
26.548
71.846
116.466
1.00
16.86
A


ATOM
509
CG
LEU
A
70
25.399
70.921
116.867
1.00
17.66
A


ATOM
510
CD1
LEU
A
70
25.866
69.928
117.930
1.00
17.33
A


ATOM
511
CD2
LEU
A
70
24.229
71.755
117.384
1.00
16.30
A


ATOM
512
C
LEU
A
70
27.387
73.842
115.230
1.00
19.34
A


ATOM
513
O
LEU
A
70
28.546
73.515
114.963
1.00
19.14
A


ATOM
514
N
THR
A
71
27.017
75.094
115.483
1.00
19.06
A


ATOM
515
CA
THR
A
71
27.965
76.198
115.478
1.00
19.11
A


ATOM
516
CB
THR
A
71
27.529
77.305
114.514
1.00
20.64
A


ATOM
517
OG1
THR
A
71
26.319
77.892
114.997
1.00
18.72
A


ATOM
518
CG2
THR
A
71
27.288
76.737
113.123
1.00
21.99
A


ATOM
519
C
THR
A
71
28.023
76.794
116.878
1.00
19.23
A


ATOM
520
O
THR
A
71
27.180
76.500
117.727
1.00
17.80
A


ATOM
521
N
GLU
A
72
29.015
77.644
117.118
1.00
19.93
A


ATOM
522
CA
GLU
A
72
29.164
78.269
118.425
1.00
21.10
A


ATOM
523
CB
GLU
A
72
30.386
79.196
118.431
1.00
22.65
A


ATOM
524
CG
GLU
A
72
30.715
79.745
119.814
1.00
25.51
A


ATOM
525
CD
GLU
A
72
32.066
80.436
119.887
1.00
26.76
A


ATOM
526
OE1
GLU
A
72
32.356
81.053
120.939
1.00
29.43
A


ATOM
527
OE2
GLU
A
72
32.835
80.361
118.908
1.00
25.78
A


ATOM
528
C
GLU
A
72
27.908
79.049
118.806
1.00
21.16
A


ATOM
529
O
GLU
A
72
27.479
79.035
119.965
1.00
19.47
A


ATOM
530
N
GLU
A
73
27.315
79.727
117.830
1.00
22.57
A


ATOM
531
CA
GLU
A
73
26.108
80.506
118.082
1.00
23.75
A


ATOM
532
CB
GLU
A
73
25.756
81.340
116.849
1.00
28.49
A


ATOM
533
CG
GLU
A
73
26.548
82.651
116.717
1.00
35.51
A


ATOM
534
CD
GLU
A
73
27.929
82.617
117.382
1.00
41.12
A


ATOM
535
OE1
GLU
A
73
27.995
82.619
118.635
1.00
43.42
A


ATOM
536
OE2
GLU
A
73
28.950
82.594
116.656
1.00
44.19
A


ATOM
537
C
GLU
A
73
24.947
79.594
118.466
1.00
21.96
A


ATOM
538
O
GLU
A
73
24.190
79.895
119.390
1.00
20.37
A


ATOM
539
N
ILE
A
74
24.810
78.470
117.770
1.00
19.89
A


ATOM
540
CA
ILE
A
74
23.738
77.535
118.089
1.00
18.76
A


ATOM
541
CB
ILE
A
74
23.659
76.390
117.043
1.00
18.90
A


ATOM
542
CG2
ILE
A
74
22.714
75.295
117.521
1.00
16.71
A


ATOM
543
CG1
ILE
A
74
23.170
76.954
115.705
1.00
20.30
A


ATOM
544
CD1
ILE
A
74
23.046
75.924
114.596
1.00
18.88
A


ATOM
545
C
ILE
A
74
23.964
76.960
119.493
1.00
18.52
A


ATOM
546
O
ILE
A
74
23.041
76.895
120.306
1.00
20.62
A


ATOM
547
N
LEU
A
75
25.193
76.561
119.788
1.00
18.16
A


ATOM
548
CA
LEU
A
75
25.498
76.010
121.104
1.00
17.27
A


ATOM
549
CB
LEU
A
75
26.954
75.553
121.153
1.00
17.79
A


ATOM
550
CG
LEU
A
75
27.280
74.382
120.222
1.00
14.50
A


ATOM
551
CD1
LEU
A
75
28.761
74.033
120.299
1.00
15.68
A


ATOM
552
CD2
LEU
A
75
26.416
73.189
120.613
1.00
18.83
A


ATOM
553
C
LEU
A
75
25.225
77.028
122.212
1.00
19.75
A


ATOM
554
O
LEU
A
75
24.815
76.666
123.318
1.00
18.99
A


ATOM
555
N
LYS
A
76
25.441
78.303
121.906
1.00
20.65
A


ATOM
556
CA
LYS
A
76
25.212
79.369
122.874
1.00
23.67
A


ATOM
557
CB
LYS
A
76
25.660
80.713
122.294
1.00
25.80
A


ATOM
558
CG
LYS
A
76
25.558
81.874
123.277
1.00
31.54
A


ATOM
559
CD
LYS
A
76
25.830
83.205
122.590
1.00
34.91
A


ATOM
560
CE
LYS
A
76
25.581
84.377
123.528
1.00
36.18
A


ATOM
561
NZ
LYS
A
76
25.622
85.681
122.801
1.00
39.35
A


ATOM
562
C
LYS
A
76
23.734
79.434
123.251
1.00
23.97
A


ATOM
563
O
LYS
A
76
23.389
79.720
124.395
1.00
23.57
A


ATOM
564
N
GLU
A
77
22.865
79.152
122.283
1.00
23.60
A


ATOM
565
CA
GLU
A
77
21.424
79.182
122.516
1.00
25.27
A


ATOM
566
CB
GLU
A
77
20.668
79.378
121.197
1.00
27.47
A


ATOM
567
CG
GLU
A
77
21.266
80.405
120.247
1.00
34.00
A


ATOM
568
CD
GLU
A
77
21.546
81.740
120.909
1.00
36.99
A


ATOM
569
OE1
GLU
A
77
20.633
82.284
121.566
1.00
40.32
A


ATOM
570
OE2
GLU
A
77
22.679
82.250
120.764
1.00
40.16
A


ATOM
571
C
GLU
A
77
20.941
77.886
123.161
1.00
24.62
A


ATOM
572
O
GLU
A
77
19.773
77.770
123.521
1.00
24.54
A


ATOM
573
N
ASN
A
78
21.838
76.913
123.307
1.00
22.72
A


ATOM
574
CA
ASN
A
78
21.468
75.627
123.884
1.00
22.16
A


ATOM
575
CB
ASN
A
78
21.406
74.571
122.782
1.00
20.72
A


ATOM
576
CG
ASN
A
78
20.246
74.789
121.843
1.00
21.61
A


ATOM
577
OD1
ASN
A
78
19.115
74.375
122.123
1.00
19.12
A


ATOM
578
ND2
ASN
A
78
20.512
75.457
120.724
1.00
18.54
A


ATOM
579
C
ASN
A
78
22.402
75.146
124.984
1.00
22.23
A


ATOM
580
O
ASN
A
78
23.104
74.149
124.820
1.00
22.58
A


ATOM
581
N
PRO
A
79
22.412
75.844
126.130
1.00
21.67
A


ATOM
582
CD
PRO
A
79
21.562
76.985
126.514
1.00
21.10
A


ATOM
583
CA
PRO
A
79
23.283
75.441
127.237
1.00
21.96
A


ATOM
584
CB
PRO
A
79
22.958
76.465
128.327
1.00
22.78
A


ATOM
585
CG
PRO
A
79
21.530
76.853
128.023
1.00
23.42
A


ATOM
586
C
PRO
A
79
23.036
74.000
127.689
1.00
22.12
A


ATOM
587
O
PRO
A
79
23.959
73.316
128.119
1.00
20.55
A


ATOM
588
N
ASN
A
80
21.793
73.537
127.594
1.00
21.11
A


ATOM
589
CA
ASN
A
80
21.489
72.173
128.006
1.00
22.35
A


ATOM
590
CB
ASN
A
80
19.982
71.931
128.012
1.00
24.80
A


ATOM
591
CG
ASN
A
80
19.266
72.794
129.026
1.00
27.03
A


ATOM
592
OD1
ASN
A
80
19.790
73.058
130.109
1.00
27.86
A


ATOM
593
ND2
ASN
A
80
18.060
73.233
128.687
1.00
30.50
A


ATOM
594
C
ASN
A
80
22.184
71.144
127.118
1.00
22.01
A


ATOM
595
O
ASN
A
80
22.410
70.009
127.536
1.00
21.27
A


ATOM
596
N
MET
A
81
22.530
71.541
125.898
1.00
20.53
A


ATOM
597
CA
MET
A
81
23.221
70.635
124.986
1.00
21.23
A


ATOM
598
CB
MET
A
81
22.919
70.996
123.523
1.00
20.11
A


ATOM
599
CG
MET
A
81
21.541
70.549
123.044
1.00
17.66
A


ATOM
600
SD
MET
A
81
21.145
71.070
121.348
1.00
20.66
A


ATOM
601
CE
MET
A
81
22.478
70.287
120.420
1.00
19.72
A


ATOM
602
C
MET
A
81
24.728
70.677
125.235
1.00
20.83
A


ATOM
603
O
MET
A
81
25.447
69.745
124.884
1.00
19.87
A


ATOM
604
N
CYS
A
82
25.203
71.758
125.850
1.00
20.43
A


ATOM
605
CA
CYS
A
82
26.625
71.890
126.140
1.00
20.36
A


ATOM
606
CB
CYS
A
82
27.016
73.365
126.252
1.00
19.40
A


ATOM
607
SG
CYS
A
82
26.921
74.261
124.692
1.00
22.96
A


ATOM
608
C
CYS
A
82
26.971
71.159
127.428
1.00
19.46
A


ATOM
609
O
CYS
A
82
28.126
70.807
127.664
1.00
21.85
A


ATOM
610
N
ALA
A
83
25.963
70.932
128.261
1.00
19.79
A


ATOM
611
CA
ALA
A
83
26.167
70.232
129.518
1.00
19.82
A


ATOM
612
CB
ALA
A
83
24.960
70.417
130.414
1.00
20.37
A


ATOM
613
C
ALA
A
83
26.361
68.756
129.207
1.00
21.03
A


ATOM
614
O
ALA
A
83
25.891
68.272
128.175
1.00
18.48
A


ATOM
615
N
TYR
A
84
27.053
68.043
130.091
1.00
20.86
A


ATOM
616
CA
TYR
A
84
27.269
66.615
129.883
1.00
21.75
A


ATOM
617
CB
TYR
A
84
28.207
66.045
130.946
1.00
20.13
A


ATOM
618
CG
TYR
A
84
28.198
64.531
130.988
1.00
20.20
A


ATOM
619
CD1
TYR
A
84
28.805
63.782
129.986
1.00
19.11
A


ATOM
620
CE1
TYR
A
84
28.762
62.387
130.008
1.00
21.15
A


ATOM
621
CD2
TYR
A
84
27.547
63.850
132.017
1.00
19.79
A


ATOM
622
CE2
TYR
A
84
27.495
62.468
132.047
1.00
23.38
A


ATOM
623
CZ
TYR
A
84
28.101
61.740
131.044
1.00
21.82
A


ATOM
624
OH
TYR
A
84
28.027
60.369
131.072
1.00
22.42
A


ATOM
625
C
TYR
A
84
25.936
65.885
129.969
1.00
22.94
A


ATOM
626
O
TYR
A
84
25.678
64.949
129.212
1.00
24.58
A


ATOM
627
N
LYS
A
85
25.091
66.329
130.895
1.00
24.59
A


ATOM
628
CA
LYS
A
85
23.786
65.715
131.116
1.00
27.30
A


ATOM
629
CB
LYS
A
85
23.937
64.572
132.128
1.00
28.97
A


ATOM
630
CG
LYS
A
85
22.680
64.203
132.905
1.00
33.37
A


ATOM
631
CD
LYS
A
85
23.016
63.202
134.011
1.00
35.36
A


ATOM
632
CE
LYS
A
85
21.856
63.001
134.975
1.00
36.29
A


ATOM
633
NZ
LYS
A
85
20.630
62.504
134.289
1.00
37.50
A


ATOM
634
C
LYS
A
85
22.743
66.717
131.613
1.00
26.53
A


ATOM
635
O
LYS
A
85
22.744
67.089
132.786
1.00
28.76
A


ATOM
636
N
ALA
A
86
21.862
67.150
130.713
1.00
23.82
A


ATOM
637
CA
ALA
A
86
20.789
68.089
131.040
1.00
21.57
A


ATOM
638
CB
ALA
A
86
21.283
69.519
130.892
1.00
20.90
A


ATOM
639
C
ALA
A
86
19.638
67.823
130.065
1.00
21.98
A


ATOM
640
O
ALA
A
86
19.885
67.469
128.913
1.00
20.68
A


ATOM
641
N
PRO
A
87
18.374
67.982
130.513
1.00
23.00
A


ATOM
642
CD
PRO
A
87
17.985
68.429
131.864
1.00
25.15
A


ATOM
643
CA
PRO
A
87
17.179
67.756
129.682
1.00
23.11
A


ATOM
644
CB
PRO
A
87
16.046
68.277
130.561
1.00
25.66
A


ATOM
645
CG
PRO
A
87
16.553
67.972
131.951
1.00
26.07
A


ATOM
646
C
PRO
A
87
17.290
68.510
128.368
1.00
23.09
A


ATOM
647
O
PRO
A
87
17.312
69.741
128.363
1.00
20.97
A


ATOM
648
N
SER
A
88
17.342
67.780
127.253
1.00
19.74
A


ATOM
649
CA
SER
A
88
17.517
68.434
125.962
1.00
16.92
A


ATOM
650
CB
SER
A
88
18.992
68.805
125.804
1.00
16.86
A


ATOM
651
OG
SER
A
88
19.797
67.642
125.909
1.00
14.70
A


ATOM
652
C
SER
A
88
17.095
67.626
124.737
1.00
17.40
A


ATOM
653
O
SER
A
88
17.387
68.027
123.613
1.00
17.18
A


ATOM
654
N
LEU
A
89
16.419
66.499
124.931
1.00
16.77
A


ATOM
655
CA
LEU
A
89
16.011
65.691
123.786
1.00
18.16
A


ATOM
656
CB
LEU
A
89
15.315
64.408
124.245
1.00
19.74
A


ATOM
657
CG
LEU
A
89
14.896
63.525
123.066
1.00
20.68
A


ATOM
658
CD1
LEU
A
89
16.117
62.910
122.420
1.00
20.92
A


ATOM
659
CD2
LEU
A
89
13.971
62.457
123.551
1.00
22.54
A


ATOM
660
C
LEU
A
89
15.107
66.441
122.808
1.00
17.08
A


ATOM
661
O
LEU
A
89
15.295
66.344
121.598
1.00
18.35
A


ATOM
662
N
ASP
A
90
14.135
67.191
123.320
1.00
17.39
A


ATOM
663
CA
ASP
A
90
13.222
67.943
122.453
1.00
16.14
A


ATOM
664
CB
ASP
A
90
12.218
68.737
123.294
1.00
19.36
A


ATOM
665
CG
ASP
A
90
11.162
67.858
123.942
1.00
20.42
A


ATOM
666
OD1
ASP
A
90
10.253
68.421
124.581
1.00
22.07
A


ATOM
667
OD2
ASP
A
90
11.234
66.612
123.821
1.00
21.79
A


ATOM
668
C
ASP
A
90
13.959
68.906
121.511
1.00
17.32
A


ATOM
669
O
ASP
A
90
13.725
68.920
120.291
1.00
14.74
A


ATOM
670
N
ALA
A
91
14.833
69.729
122.078
1.00
15.85
A


ATOM
671
CA
ALA
A
91
15.593
70.679
121.273
1.00
16.35
A


ATOM
672
CB
ALA
A
91
16.476
71.533
122.175
1.00
16.94
A


ATOM
673
C
ALA
A
91
16.449
69.951
120.235
1.00
16.25
A


ATOM
674
O
ALA
A
91
16.524
70.369
119.076
1.00
13.95
A


ATOM
675
N
ARG
A
92
17.085
68.855
120.647
1.00
14.79
A


ATOM
676
CA
ARG
A
92
17.937
68.091
119.739
1.00
14.64
A


ATOM
677
CB
ARG
A
92
18.672
66.981
120.499
1.00
14.18
A


ATOM
678
CG
ARG
A
92
19.654
67.461
121.572
1.00
13.74
A


ATOM
679
CD
ARG
A
92
20.045
66.282
122.463
1.00
13.80
A


ATOM
680
NE
ARG
A
92
20.992
66.630
123.523
1.00
13.20
A


ATOM
681
CZ
ARG
A
92
22.310
66.719
123.359
1.00
13.36
A


ATOM
682
NH1
ARG
A
92
22.858
66.491
122.171
1.00
12.28
A


ATOM
683
NH2
ARG
A
92
23.087
67.010
124.398
1.00
15.07
A


ATOM
684
C
ARG
A
92
17.130
67.475
118.598
1.00
14.35
A


ATOM
685
O
ARG
A
92
17.492
67.605
117.432
1.00
13.62
A


ATOM
686
N
GLU
A
93
16.037
66.803
118.939
1.00
14.60
A


ATOM
687
CA
GLU
A
93
15.192
66.178
117.925
1.00
15.88
A


ATOM
688
CB
GLU
A
93
14.073
65.379
118.597
1.00
16.99
A


ATOM
689
CG
GLU
A
93
14.580
64.128
119.313
1.00
20.99
A


ATOM
690
CD
GLU
A
93
15.046
63.032
118.348
1.00
23.76
A


ATOM
691
OE1
GLU
A
93
16.010
62.305
118.675
1.00
23.78
A


ATOM
692
OE2
GLU
A
93
14.442
62.889
117.267
1.00
26.26
A


ATOM
693
C
GLU
A
93
14.614
67.214
116.966
1.00
15.22
A


ATOM
694
O
GLU
A
93
14.458
66.947
115.776
1.00
15.96
A


ATOM
695
N
ASP
A
94
14.309
68.406
117.465
1.00
15.22
A


ATOM
696
CA
ASP
A
94
13.777
69.430
116.576
1.00
14.70
A


ATOM
697
CB
ASP
A
94
13.340
70.673
117.360
1.00
17.50
A


ATOM
698
CG
ASP
A
94
12.052
70.448
118.151
1.00
21.10
A


ATOM
699
OD1
ASP
A
94
11.253
69.564
117.768
1.00
23.41
A


ATOM
700
OD2
ASP
A
94
11.826
71.167
119.150
1.00
23.08
A


ATOM
701
C
ASP
A
94
14.829
69.801
115.530
1.00
15.14
A


ATOM
702
O
ASP
A
94
14.501
70.018
114.364
1.00
14.99
A


ATOM
703
N
MET
A
95
16.094
69.860
115.944
1.00
16.52
A


ATOM
704
CA
MET
A
95
17.183
70.187
115.031
1.00
13.82
A


ATOM
705
CB
MET
A
95
18.507
70.321
115.789
1.00
14.37
A


ATOM
706
CG
MET
A
95
18.598
71.520
116.725
1.00
15.94
A


ATOM
707
SD
MET
A
95
20.178
71.517
117.624
1.00
19.13
A


ATOM
708
CE
MET
A
95
20.074
73.098
118.500
1.00
19.01
A


ATOM
709
C
MET
A
95
17.316
69.071
114.003
1.00
15.95
A


ATOM
710
O
MET
A
95
17.440
69.324
112.806
1.00
15.19
A


ATOM
711
N
MET
A
96
17.313
67.833
114.490
1.00
14.58
A


ATOM
712
CA
MET
A
96
17.428
66.670
113.618
1.00
14.52
A


ATOM
713
CB
MET
A
96
17.341
65.376
114.447
1.00
13.66
A


ATOM
714
CG
MET
A
96
18.498
65.155
115.417
1.00
15.74
A


ATOM
715
SD
MET
A
96
20.095
64.978
114.615
1.00
18.80
A


ATOM
716
CE
MET
A
96
20.010
63.239
114.121
1.00
15.04
A


ATOM
717
C
MET
A
96
16.328
66.673
112.554
1.00
14.12
A


ATOM
718
O
MET
A
96
16.609
66.556
111.366
1.00
17.99
A


ATOM
719
N
ILE
A
97
15.079
66.806
112.983
1.00
14.93
A


ATOM
720
CA
ILE
A
97
13.944
66.804
112.058
1.00
15.15
A


ATOM
721
CB
ILE
A
97
12.615
66.959
112.835
1.00
15.85
A


ATOM
722
CG2
ILE
A
97
11.431
67.096
111.861
1.00
17.38
A


ATOM
723
CG1
ILE
A
97
12.405
65.737
113.735
1.00
13.08
A


ATOM
724
CD1
ILE
A
97
11.277
65.901
114.736
1.00
14.10
A


ATOM
725
C
ILE
A
97
14.062
67.891
110.984
1.00
16.23
A


ATOM
726
O
ILE
A
97
13.664
67.694
109.829
1.00
15.33
A


ATOM
727
N
ARG
A
98
14.624
69.033
111.356
1.00
15.97
A


ATOM
728
CA
ARG
A
98
14.796
70.123
110.400
1.00
18.43
A


ATOM
729
CB
ARG
A
98
15.015
71.435
111.150
1.00
19.15
A


ATOM
730
CG
ARG
A
98
15.092
72.667
110.267
1.00
24.01
A


ATOM
731
CD
ARG
A
98
15.425
73.900
111.093
1.00
25.52
A


ATOM
732
NE
ARG
A
98
14.794
73.866
112.412
1.00
27.90
A


ATOM
733
CZ
ARG
A
98
15.447
73.645
113.548
1.00
27.71
A


ATOM
734
NH1
ARG
A
98
16.758
73.437
113.529
1.00
33.63
A


ATOM
735
NH2
ARG
A
98
14.793
73.635
114.704
1.00
31.02
A


ATOM
736
C
ARG
A
98
15.979
69.889
109.456
1.00
17.85
A


ATOM
737
O
ARG
A
98
15.850
69.980
108.230
1.00
16.62
A


ATOM
738
N
GLU
A
99
17.127
69.561
110.034
1.00
16.61
A


ATOM
739
CA
GLU
A
99
18.352
69.379
109.267
1.00
16.47
A


ATOM
740
CB
GLU
A
99
19.543
69.659
110.181
1.00
17.68
A


ATOM
741
CG
GLU
A
99
19.471
71.041
110.816
1.00
19.11
A


ATOM
742
CD
GLU
A
99
19.564
72.152
109.786
1.00
21.20
A


ATOM
743
OE1
GLU
A
99
19.074
73.271
110.061
1.00
23.07
A


ATOM
744
OE2
GLU
A
99
20.139
71.904
108.705
1.00
21.85
A


ATOM
745
C
GLU
A
99
18.598
68.083
108.514
1.00
16.27
A


ATOM
746
O
GLU
A
99
19.213
68.098
107.449
1.00
16.09
A


ATOM
747
N
VAL
A
100
18.141
66.962
109.053
1.00
15.95
A


ATOM
748
CA
VAL
A
100
18.379
65.681
108.402
1.00
16.57
A


ATOM
749
CB
VAL
A
100
17.809
64.528
109.258
1.00
18.24
A


ATOM
750
CG1
VAL
A
100
17.921
63.197
108.521
1.00
20.43
A


ATOM
751
CG2
VAL
A
100
18.591
64.453
110.562
1.00
19.88
A


ATOM
752
C
VAL
A
100
17.827
65.644
106.980
1.00
16.27
A


ATOM
753
O
VAL
A
100
18.548
65.308
106.041
1.00
14.58
A


ATOM
754
N
PRO
A
101
16.549
66.013
106.792
1.00
18.57
A


ATOM
755
CD
PRO
A
101
15.480
66.240
107.782
1.00
20.19
A


ATOM
756
CA
PRO
A
101
16.013
65.983
105.425
1.00
18.96
A


ATOM
757
CB
PRO
A
101
14.503
66.063
105.646
1.00
20.79
A


ATOM
758
CG
PRO
A
101
14.379
66.821
106.941
1.00
21.86
A


ATOM
759
C
PRO
A
101
16.540
67.100
104.522
1.00
17.94
A


ATOM
760
O
PRO
A
101
16.618
66.945
103.308
1.00
18.12
A


ATOM
761
N
ARG
A
102
16.910
68.222
105.122
1.00
18.08
A


ATOM
762
CA
ARG
A
102
17.411
69.361
104.365
1.00
19.16
A


ATOM
763
CB
ARG
A
102
17.530
70.555
105.314
1.00
22.01
A


ATOM
764
CG
ARG
A
102
18.080
71.815
104.712
1.00
26.94
A


ATOM
765
CD
ARG
A
102
17.796
72.989
105.634
1.00
28.29
A


ATOM
766
NE
ARG
A
102
18.545
74.166
105.225
1.00
30.92
A


ATOM
767
CZ
ARG
A
102
19.826
74.361
105.506
1.00
32.08
A


ATOM
768
NH1
ARG
A
102
20.496
73.459
106.210
1.00
31.02
A


ATOM
769
NH2
ARG
A
102
20.441
75.449
105.059
1.00
33.44
A


ATOM
770
C
ARG
A
102
18.741
69.055
103.664
1.00
18.26
A


ATOM
771
O
ARG
A
102
18.887
69.286
102.464
1.00
18.02
A


ATOM
772
N
VAL
A
103
19.705
68.517
104.402
1.00
15.63
A


ATOM
773
CA
VAL
A
103
20.999
68.175
103.817
1.00
16.43
A


ATOM
774
CB
VAL
A
103
22.037
67.828
104.907
1.00
16.44
A


ATOM
775
CG1
VAL
A
103
23.378
67.471
104.263
1.00
17.24
A


ATOM
776
CG2
VAL
A
103
22.194
69.011
105.856
1.00
19.29
A


ATOM
777
C
VAL
A
103
20.795
66.967
102.911
1.00
15.93
A


ATOM
778
O
VAL
A
103
21.452
66.834
101.881
1.00
14.17
A


ATOM
779
N
GLY
A
104
19.871
66.094
103.302
1.00
16.69
A


ATOM
780
CA
GLY
A
104
19.580
64.918
102.499
1.00
14.99
A


ATOM
781
C
GLY
A
104
19.068
65.333
101.126
1.00
16.35
A


ATOM
782
O
GLY
A
104
19.437
64.745
100.112
1.00
17.10
A


ATOM
783
N
LYS
A
105
18.221
66.356
101.084
1.00
16.15
A


ATOM
784
CA
LYS
A
105
17.702
66.820
99.803
1.00
17.34
A


ATOM
785
CB
LYS
A
105
16.675
67.936
99.990
1.00
17.80
A


ATOM
786
CG
LYS
A
105
16.189
68.486
98.653
1.00
21.22
A


ATOM
787
CD
LYS
A
105
15.789
69.941
98.756
1.00
25.56
A


ATOM
788
CE
LYS
A
105
15.600
70.553
97.374
1.00
28.16
A


ATOM
789
NZ
LYS
A
105
16.888
70.618
96.620
1.00
29.98
A


ATOM
790
C
LYS
A
105
18.818
67.336
98.902
1.00
16.20
A


ATOM
791
O
LYS
A
105
18.807
67.091
97.700
1.00
17.34
A


ATOM
792
N
GLU
A
106
19.773
68.062
99.477
1.00
16.91
A


ATOM
793
CA
GLU
A
106
20.881
68.598
98.696
1.00
19.15
A


ATOM
794
CB
GLU
A
106
21.835
69.387
99.600
1.00
20.83
A


ATOM
795
CG
GLU
A
106
23.047
69.922
98.862
1.00
25.52
A


ATOM
796
CD
GLU
A
106
23.920
70.828
99.716
1.00
26.98
A


ATOM
797
OE1
GLU
A
106
25.035
71.164
99.260
1.00
27.30
A


ATOM
798
OE2
GLU
A
106
23.495
71.204
100.832
1.00
27.96
A


ATOM
799
C
GLU
A
106
21.629
67.450
98.016
1.00
18.67
A


ATOM
800
O
GLU
A
106
21.938
67.504
96.817
1.00
16.99
A


ATOM
801
N
ALA
A
107
21.907
66.401
98.783
1.00
15.83
A


ATOM
802
CA
ALA
A
107
22.610
65.244
98.243
1.00
15.27
A


ATOM
803
CB
ALA
A
107
22.928
64.251
99.359
1.00
14.32
A


ATOM
804
C
ALA
A
107
21.778
64.556
97.162
1.00
13.90
A


ATOM
805
O
ALA
A
107
22.299
64.189
96.105
1.00
13.71
A


ATOM
806
N
ALA
A
108
20.488
64.380
97.431
1.00
14.03
A


ATOM
807
CA
ALA
A
108
19.599
63.720
96.477
1.00
15.72
A


ATOM
808
CB
ALA
A
108
18.219
63.519
97.091
1.00
15.61
A


ATOM
809
C
ALA
A
108
19.480
64.494
95.175
1.00
16.95
A


ATOM
810
O
ALA
A
108
19.442
63.899
94.098
1.00
16.28
A


ATOM
811
N
THR
A
109
19.412
65.820
95.269
1.00
15.93
A


ATOM
812
CA
THR
A
109
19.309
66.642
94.071
1.00
17.23
A


ATOM
813
CB
THR
A
109
19.206
68.148
94.432
1.00
17.73
A


ATOM
814
OG1
THR
A
109
17.994
68.381
95.160
1.00
16.64
A


ATOM
815
CG2
THR
A
109
19.207
69.004
93.176
1.00
21.91
A


ATOM
816
C
THR
A
109
20.538
66.396
93.192
1.00
16.50
A


ATOM
817
O
THR
A
109
20.430
66.291
91.969
1.00
15.20
A


ATOM
818
N
LYS
A
110
21.707
66.286
93.817
1.00
15.38
A


ATOM
819
CA
LYS
A
110
22.940
66.048
93.074
1.00
15.76
A


ATOM
820
CB
LYS
A
110
24.149
66.168
94.002
1.00
16.69
A


ATOM
821
CG
LYS
A
110
24.428
67.571
94.486
1.00
19.70
A


ATOM
822
CD
LYS
A
110
25.648
67.563
95.384
1.00
20.65
A


ATOM
823
CE
LYS
A
110
25.940
68.937
95.931
1.00
22.93
A


ATOM
824
NZ
LYS
A
110
27.124
68.891
96.839
1.00
21.69
A


ATOM
825
C
LYS
A
110
22.957
64.672
92.401
1.00
13.93
A


ATOM
826
O
LYS
A
110
23.397
64.530
91.257
1.00
13.99
A


ATOM
827
N
ALA
A
111
22.482
63.659
93.115
1.00
15.58
A


ATOM
828
CA
ALA
A
111
22.449
62.306
92.561
1.00
14.44
A


ATOM
829
CB
ALA
A
111
22.046
61.318
93.640
1.00
14.66
A


ATOM
830
C
ALA
A
111
21.466
62.245
91.387
1.00
15.71
A


ATOM
831
O
ALA
A
111
21.762
61.673
90.338
1.00
14.80
A


ATOM
832
N
ILE
A
112
20.297
62.851
91.560
1.00
16.78
A


ATOM
833
CA
ILE
A
112
19.298
62.851
90.499
1.00
17.55
A


ATOM
834
CB
ILE
A
112
17.973
63.474
90.993
1.00
17.59
A


ATOM
835
CG2
ILE
A
112
16.986
63.620
89.837
1.00
17.13
A


ATOM
836
CG1
ILE
A
112
17.386
62.580
92.092
1.00
20.85
A


ATOM
837
CD1
ILE
A
112
16.066
63.064
92.660
1.00
22.77
A


ATOM
838
C
ILE
A
112
19.828
63.586
89.268
1.00
18.57
A


ATOM
839
O
ILE
A
112
19.568
63.179
88.139
1.00
16.83
A


ATOM
840
N
LYS
A
113
20.594
64.651
89.484
1.00
19.85
A


ATOM
841
CA
LYS
A
113
21.177
65.401
88.375
1.00
21.93
A


ATOM
842
CB
LYS
A
113
21.924
66.633
88.894
1.00
24.29
A


ATOM
843
CG
LYS
A
113
22.557
67.478
87.785
1.00
26.16
A


ATOM
844
CD
LYS
A
113
23.249
68.717
88.343
1.00
30.15
A


ATOM
845
CE
LYS
A
113
23.865
69.549
87.227
1.00
32.17
A


ATOM
846
NZ
LYS
A
113
22.832
69.994
86.246
1.00
33.78
A


ATOM
847
C
LYS
A
113
22.141
64.515
87.576
1.00
22.24
A


ATOM
848
O
LYS
A
113
22.113
64.514
86.346
1.00
20.23
A


ATOM
849
N
GLU
A
114
22.994
63.763
88.274
1.00
20.31
A


ATOM
850
CA
GLU
A
114
23.941
62.872
87.603
1.00
20.76
A


ATOM
851
CB
GLU
A
114
24.858
62.174
88.615
1.00
20.34
A


ATOM
852
CG
GLU
A
114
25.945
61.318
87.961
1.00
22.36
A


ATOM
853
CD
GLU
A
114
26.594
60.333
88.922
1.00
25.31
A


ATOM
854
OE1
GLU
A
114
26.524
60.562
90.148
1.00
23.40
A


ATOM
855
OE2
GLU
A
114
27.188
59.335
88.449
1.00
27.34
A


ATOM
856
C
GLU
A
114
23.192
61.797
86.825
1.00
20.63
A


ATOM
857
O
GLU
A
114
23.520
61.506
85.677
1.00
20.09
A


ATOM
858
N
TRP
A
115
22.197
61.206
87.483
1.00
19.11
A


ATOM
859
CA
TRP
A
115
21.373
60.148
86.912
1.00
19.80
A


ATOM
860
CB
TRP
A
115
20.271
59.788
87.909
1.00
16.70
A


ATOM
861
CG
TRP
A
115
19.386
58.655
87.513
1.00
17.51
A


ATOM
862
CD2
TRP
A
115
18.002
58.504
87.841
1.00
18.01
A


ATOM
863
CE2
TRP
A
115
17.583
57.255
87.325
1.00
19.36
A


ATOM
864
CE3
TRP
A
115
17.073
59.302
88.520
1.00
18.64
A


ATOM
865
CD1
TRP
A
115
19.744
57.524
86.829
1.00
17.50
A


ATOM
866
NE1
TRP
A
115
18.666
56.679
86.714
1.00
16.73
A


ATOM
867
CZ2
TRP
A
115
16.274
56.788
87.470
1.00
20.10
A


ATOM
868
CZ3
TRP
A
115
15.769
58.837
88.663
1.00
18.36
A


ATOM
869
CH2
TRP
A
115
15.384
57.589
88.139
1.00
19.75
A


ATOM
870
C
TRP
A
115
20.786
60.613
85.581
1.00
20.41
A


ATOM
871
O
TRP
A
115
20.804
59.873
84.598
1.00
20.70
A


ATOM
872
N
GLY
A
116
20.278
61.844
85.560
1.00
20.64
A


ATOM
873
CA
GLY
A
116
19.727
62.414
84.341
1.00
22.03
A


ATOM
874
C
GLY
A
116
18.297
62.044
83.998
1.00
22.10
A


ATOM
875
O
GLY
A
116
17.767
62.487
82.976
1.00
21.00
A


ATOM
876
N
GLN
A
117
17.667
61.237
84.844
1.00
22.18
A


ATOM
877
CA
GLN
A
117
16.295
60.812
84.611
1.00
21.98
A


ATOM
878
CB
GLN
A
117
16.146
59.319
84.916
1.00
22.79
A


ATOM
879
CG
GLN
A
117
16.986
58.429
84.031
1.00
26.38
A


ATOM
880
CD
GLN
A
117
16.533
58.474
82.589
1.00
30.18
A


ATOM
881
OE1
GLN
A
117
15.401
58.104
82.273
1.00
34.37
A


ATOM
882
NE2
GLN
A
117
17.409
58.933
81.708
1.00
31.61
A


ATOM
883
C
GLN
A
117
15.330
61.597
85.482
1.00
22.74
A


ATOM
884
O
GLN
A
117
15.709
62.116
86.538
1.00
20.98
A


ATOM
885
N
PRO
A
118
14.063
61.698
85.049
1.00
22.98
A


ATOM
886
CD
PRO
A
118
13.555
61.274
83.735
1.00
24.02
A


ATOM
887
CA
PRO
A
118
13.028
62.418
85.790
1.00
23.87
A


ATOM
888
CB
PRO
A
118
11.800
62.261
84.903
1.00
24.03
A


ATOM
889
CG
PRO
A
118
12.382
62.200
83.541
1.00
25.61
A


ATOM
890
C
PRO
A
118
12.805
61.816
87.176
1.00
25.25
A


ATOM
891
O
PRO
A
118
12.820
60.595
87.351
1.00
23.22
A


ATOM
892
N
MET
A
119
12.596
62.694
88.145
1.00
24.78
A


ATOM
893
CA
MET
A
119
12.354
62.320
89.530
1.00
26.74
A


ATOM
894
CB
MET
A
119
12.156
63.606
90.334
1.00
29.70
A


ATOM
895
CG
MET
A
119
11.815
63.454
91.789
1.00
32.65
A


ATOM
896
SD
MET
A
119
11.655
65.110
92.524
1.00
35.58
A


ATOM
897
CE
MET
A
119
10.351
65.815
91.532
1.00
38.18
A


ATOM
898
C
MET
A
119
11.131
61.400
89.638
1.00
25.23
A


ATOM
899
O
MET
A
119
11.059
60.538
90.517
1.00
23.60
A


ATOM
900
N
SER
A
120
10.178
61.578
88.727
1.00
24.22
A


ATOM
901
CA
SER
A
120
8.964
60.768
88.712
1.00
23.87
A


ATOM
902
CB
SER
A
120
8.015
61.275
87.618
1.00
25.63
A


ATOM
903
OG
SER
A
120
8.630
61.217
86.343
1.00
26.27
A


ATOM
904
C
SER
A
120
9.247
59.277
88.492
1.00
22.48
A


ATOM
905
O
SER
A
120
8.394
58.432
88.762
1.00
21.93
A


ATOM
906
N
LYS
A
121
10.441
58.946
88.006
1.00
21.07
A


ATOM
907
CA
LYS
A
121
10.770
57.538
87.759
1.00
19.67
A


ATOM
908
CB
LYS
A
121
11.766
57.421
86.606
1.00
20.18
A


ATOM
909
CG
LYS
A
121
11.291
58.113
85.333
1.00
22.53
A


ATOM
910
CD
LYS
A
121
12.096
57.675
84.121
1.00
26.21
A


ATOM
911
CE
LYS
A
121
11.351
56.608
83.328
1.00
29.93
A


ATOM
912
NZ
LYS
A
121
10.074
57.129
82.751
1.00
28.97
A


ATOM
913
C
LYS
A
121
11.307
56.806
88.993
1.00
18.98
A


ATOM
914
O
LYS
A
121
11.593
55.604
88.935
1.00
18.06
A


ATOM
915
N
ILE
A
122
11.451
57.532
90.099
1.00
17.26
A


ATOM
916
CA
ILE
A
122
11.909
56.936
91.352
1.00
15.68
A


ATOM
917
CB
ILE
A
122
12.485
58.015
92.321
1.00
16.42
A


ATOM
918
CG2
ILE
A
122
12.747
57.406
93.690
1.00
16.72
A


ATOM
919
CG1
ILE
A
122
13.789
58.579
91.748
1.00
16.79
A


ATOM
920
CD1
ILE
A
122
14.329
59.777
92.500
1.00
16.88
A


ATOM
921
C
ILE
A
122
10.679
56.263
91.962
1.00
15.84
A


ATOM
922
O
ILE
A
122
9.640
56.900
92.173
1.00
15.43
A


ATOM
923
N
THR
A
123
10.796
54.966
92.226
1.00
14.18
A


ATOM
924
CA
THR
A
123
9.689
54.175
92.752
1.00
14.74
A


ATOM
925
CB
THR
A
123
9.549
52.891
91.934
1.00
16.36
A


ATOM
926
OG1
THR
A
123
10.802
52.199
91.937
1.00
15.10
A


ATOM
927
CG2
THR
A
123
9.198
53.221
90.493
1.00
17.32
A


ATOM
928
C
THR
A
123
9.810
53.785
94.221
1.00
13.87
A


ATOM
929
O
THR
A
123
8.812
53.493
94.884
1.00
12.09
A


ATOM
930
N
HIS
A
124
11.032
53.769
94.725
1.00
12.46
A


ATOM
931
CA
HIS
A
124
11.255
53.404
96.114
1.00
13.52
A


ATOM
932
CB
HIS
A
124
11.896
52.015
96.200
1.00
14.17
A


ATOM
933
CG
HIS
A
124
11.078
50.931
95.567
1.00
14.73
A


ATOM
934
CD2
HIS
A
124
10.806
50.666
94.270
1.00
14.15
A


ATOM
935
ND1
HIS
A
124
10.440
49.951
96.300
1.00
17.98
A


ATOM
936
CE1
HIS
A
124
9.812
49.128
95.479
1.00
13.68
A


ATOM
937
NE2
HIS
A
124
10.019
49.539
94.241
1.00
18.64
A


ATOM
938
C
HIS
A
124
12.168
54.415
96.778
1.00
13.52
A


ATOM
939
O
HIS
A
124
13.081
54.952
96.147
1.00
15.74
A


ATOM
940
N
LEU
A
125
11.921
54.660
98.057
1.00
15.22
A


ATOM
941
CA
LEU
A
125
12.737
55.586
98.826
1.00
13.70
A


ATOM
942
CB
LEU
A
125
11.969
56.874
99.138
1.00
12.90
A


ATOM
943
CG
LEU
A
125
12.658
57.787
100.168
1.00
14.85
A


ATOM
944
CD1
LEU
A
125
13.951
58.355
99.576
1.00
13.04
A


ATOM
945
CD2
LEU
A
125
11.717
58.916
100.575
1.00
13.73
A


ATOM
946
C
LEU
A
125
13.159
54.966
100.143
1.00
11.88
A


ATOM
947
O
LEU
A
125
12.311
54.615
100.960
1.00
12.37
A


ATOM
948
N
ILE
A
126
14.466
54.837
100.340
1.00
11.11
A


ATOM
949
CA
ILE
A
126
15.008
54.328
101.598
1.00
11.89
A


ATOM
950
CB
ILE
A
126
16.074
53.234
101.380
1.00
11.91
A


ATOM
951
CG2
ILE
A
126
16.614
52.751
102.736
1.00
14.16
A


ATOM
952
CG1
ILE
A
126
15.468
52.057
100.615
1.00
11.59
A


ATOM
953
CD1
ILE
A
126
16.504
51.045
100.138
1.00
11.98
A


ATOM
954
C
ILE
A
126
15.691
55.518
102.274
1.00
12.26
A


ATOM
955
O
ILE
A
126
16.632
56.084
101.726
1.00
12.65
A


ATOM
956
N
PHE
A
127
15.211
55.895
103.453
1.00
10.80
A


ATOM
957
CA
PHE
A
127
15.795
57.007
104.188
1.00
12.32
A


ATOM
958
CB
PHE
A
127
14.752
58.082
104.485
1.00
13.70
A


ATOM
959
CG
PHE
A
127
15.353
59.410
104.858
1.00
16.44
A


ATOM
960
CD1
PHE
A
127
16.100
59.550
106.025
1.00
19.42
A


ATOM
961
CD2
PHE
A
127
15.197
60.515
104.025
1.00
18.87
A


ATOM
962
CE1
PHE
A
127
16.689
60.778
106.358
1.00
20.68
A


ATOM
963
CE2
PHE
A
127
15.780
61.744
104.348
1.00
19.48
A


ATOM
964
CZ
PHE
A
127
16.525
61.875
105.514
1.00
19.21
A


ATOM
965
C
PHE
A
127
16.353
56.469
105.497
1.00
12.78
A


ATOM
966
O
PHE
A
127
15.640
55.831
106.278
1.00
14.15
A


ATOM
967
N
CYS
A
128
17.626
56.748
105.737
1.00
13.01
A


ATOM
968
CA
CYS
A
128
18.301
56.259
106.930
1.00
13.64
A


ATOM
969
CB
CYS
A
128
19.359
55.233
106.513
1.00
15.39
A


ATOM
970
SG
CYS
A
128
20.377
54.571
107.831
1.00
20.31
A


ATOM
971
C
CYS
A
128
18.952
57.380
107.714
1.00
15.17
A


ATOM
972
O
CYS
A
128
19.726
58.159
107.161
1.00
14.59
A


ATOM
973
N
THR
A
129
18.622
57.466
108.999
1.00
14.32
A


ATOM
974
CA
THR
A
129
19.205
58.482
109.868
1.00
16.20
A


ATOM
975
CB
THR
A
129
18.473
59.832
109.740
1.00
18.34
A


ATOM
976
OG1
THR
A
129
19.107
60.794
110.596
1.00
18.62
A


ATOM
977
CG2
THR
A
129
17.006
59.692
110.122
1.00
14.76
A


ATOM
978
C
THR
A
129
19.174
58.022
111.324
1.00
16.46
A


ATOM
979
O
THR
A
129
18.273
57.287
111.731
1.00
17.28
A


ATOM
980
N
THR
A
130
20.158
58.463
112.102
1.00
18.56
A


ATOM
981
CA
THR
A
130
20.263
58.082
113.506
1.00
20.61
A


ATOM
982
CB
THR
A
130
21.558
58.633
114.131
1.00
22.58
A


ATOM
983
OG1
THR
A
130
22.683
57.978
113.531
1.00
24.26
A


ATOM
984
CG2
THR
A
130
21.579
58.379
115.635
1.00
24.22
A


ATOM
985
C
THR
A
130
19.074
58.501
114.359
1.00
20.30
A


ATOM
986
O
THR
A
130
18.636
57.741
115.220
1.00
21.48
A


ATOM
987
N
SER
A
131
18.552
59.703
114.140
1.00
20.01
A


ATOM
988
CA
SER
A
131
17.398
60.141
114.911
1.00
22.06
A


ATOM
989
CB
SER
A
131
17.836
60.640
116.290
1.00
23.91
A


ATOM
990
OG
SER
A
131
16.787
60.471
117.229
1.00
24.77
A


ATOM
991
C
SER
A
131
16.578
61.211
114.189
1.00
22.16
A


ATOM
992
O
SER
A
131
16.799
61.476
113.008
1.00
22.30
A


ATOM
993
N
GLY
A
132
15.633
61.817
114.906
1.00
22.15
A


ATOM
994
CA
GLY
A
132
14.761
62.829
114.322
1.00
20.74
A


ATOM
995
C
GLY
A
132
13.403
62.167
114.193
1.00
19.96
A


ATOM
996
O
GLY
A
132
12.845
62.049
113.101
1.00
18.89
A


ATOM
997
N
VAL
A
133
12.868
61.750
115.335
1.00
19.25
A


ATOM
998
CA
VAL
A
133
11.606
61.020
115.401
1.00
18.86
A


ATOM
999
CB
VAL
A
133
11.562
60.138
116.673
1.00
19.36
A


ATOM
1000
CG1
VAL
A
133
10.316
59.272
116.662
1.00
20.48
A


ATOM
1001
CG2
VAL
A
133
12.815
59.288
116.764
1.00
21.42
A


ATOM
1002
C
VAL
A
133
10.307
61.810
115.343
1.00
18.12
A


ATOM
1003
O
VAL
A
133
9.972
62.554
116.257
1.00
15.85
A


ATOM
1004
N
ALA
A
134
9.566
61.603
114.260
1.00
17.33
A


ATOM
1005
CA
ALA
A
134
8.281
62.253
114.054
1.00
18.39
A


ATOM
1006
CB
ALA
A
134
8.480
63.600
113.376
1.00
18.75
A


ATOM
1007
C
ALA
A
134
7.428
61.353
113.170
1.00
20.02
A


ATOM
1008
O
ALA
A
134
7.955
60.526
112.426
1.00
20.00
A


ATOM
1009
N
LEU
A
135
6.112
61.500
113.275
1.00
20.90
A


ATOM
1010
CA
LEU
A
135
5.181
60.740
112.454
1.00
22.04
A


ATOM
1011
CB
LEU
A
135
4.401
59.715
113.284
1.00
22.48
A


ATOM
1012
CG
LEU
A
135
5.190
58.568
113.918
1.00
24.17
A


ATOM
1013
CD1
LEU
A
135
5.842
59.046
115.204
1.00
24.79
A


ATOM
1014
CD2
LEU
A
135
4.254
57.399
114.203
1.00
25.37
A


ATOM
1015
C
LEU
A
135
4.213
61.753
111.849
1.00
21.49
A


ATOM
1016
O
LEU
A
135
3.499
62.446
112.579
1.00
20.88
A


ATOM
1017
N
PRO
A
136
4.212
61.887
110.511
1.00
21.73
A


ATOM
1018
CD
PRO
A
136
3.328
62.816
109.783
1.00
22.31
A


ATOM
1019
CA
PRO
A
136
5.063
61.143
109.576
1.00
22.02
A


ATOM
1020
CB
PRO
A
136
4.528
61.570
108.209
1.00
21.01
A


ATOM
1021
CG
PRO
A
136
4.042
62.958
108.460
1.00
21.68
A


ATOM
1022
C
PRO
A
136
6.541
61.479
109.775
1.00
21.66
A


ATOM
1023
O
PRO
A
136
6.877
62.527
110.326
1.00
20.41
A


ATOM
1024
N
GLY
A
137
7.412
60.582
109.326
1.00
21.85
A


ATOM
1025
CA
GLY
A
137
8.843
60.771
109.499
1.00
22.07
A


ATOM
1026
C
GLY
A
137
9.555
61.689
108.528
1.00
21.47
A


ATOM
1027
O
GLY
A
137
8.929
62.373
107.711
1.00
20.25
A


ATOM
1028
N
VAL
A
138
10.881
61.705
108.627
1.00
21.01
A


ATOM
1029
CA
VAL
A
138
11.693
62.538
107.758
1.00
21.43
A


ATOM
1030
CB
VAL
A
138
13.150
62.616
108.258
1.00
21.99
A


ATOM
1031
CG1
VAL
A
138
13.198
63.423
109.546
1.00
22.78
A


ATOM
1032
CG2
VAL
A
138
13.712
61.223
108.483
1.00
20.43
A


ATOM
1033
C
VAL
A
138
11.655
62.064
106.308
1.00
20.81
A


ATOM
1034
O
VAL
A
138
12.009
62.815
105.396
1.00
20.37
A


ATOM
1035
N
ASP
A
139
11.223
60.824
106.086
1.00
20.30
A


ATOM
1036
CA
ASP
A
139
11.116
60.324
104.719
1.00
20.26
A


ATOM
1037
CB
ASP
A
139
10.771
58.822
104.710
1.00
20.86
A


ATOM
1038
CG
ASP
A
139
9.488
58.497
105.465
1.00
21.95
A


ATOM
1039
OD1
ASP
A
139
9.282
59.048
106.568
1.00
21.43
A


ATOM
1040
OD2
ASP
A
139
8.689
57.673
104.959
1.00
19.82
A


ATOM
1041
C
ASP
A
139
10.019
61.153
104.045
1.00
20.31
A


ATOM
1042
O
ASP
A
139
10.116
61.516
102.870
1.00
19.88
A


ATOM
1043
N
TYR
A
140
8.981
61.465
104.811
1.00
19.31
A


ATOM
1044
CA
TYR
A
140
7.875
62.273
104.311
1.00
20.68
A


ATOM
1045
CB
TYR
A
140
6.746
62.317
105.346
1.00
22.10
A


ATOM
1046
CG
TYR
A
140
5.689
63.360
105.062
1.00
25.72
A


ATOM
1047
CD1
TYR
A
140
4.629
63.093
104.196
1.00
24.85
A


ATOM
1048
CE1
TYR
A
140
3.664
64.058
103.921
1.00
27.16
A


ATOM
1049
CD2
TYR
A
140
5.760
64.624
105.646
1.00
26.43
A


ATOM
1050
CE2
TYR
A
140
4.804
65.596
105.374
1.00
28.31
A


ATOM
1051
CZ
TYR
A
140
3.758
65.306
104.512
1.00
27.72
A


ATOM
1052
OH
TYR
A
140
2.812
66.265
104.241
1.00
30.75
A


ATOM
1053
C
TYR
A
140
8.378
63.692
104.034
1.00
21.06
A


ATOM
1054
O
TYR
A
140
8.059
64.284
103.007
1.00
21.05
A


ATOM
1055
N
GLU
A
141
9.172
64.238
104.950
1.00
22.40
A


ATOM
1056
CA
GLU
A
141
9.697
65.587
104.766
1.00
23.04
A


ATOM
1057
CB
GLU
A
141
10.550
65.990
105.973
1.00
25.22
A


ATOM
1058
CG
GLU
A
141
9.806
65.891
107.310
1.00
29.34
A


ATOM
1059
CD
GLU
A
141
8.717
66.944
107.473
1.00
32.95
A


ATOM
1060
OE1
GLU
A
141
7.895
66.815
108.407
1.00
31.49
A


ATOM
1061
OE2
GLU
A
141
8.687
67.906
106.673
1.00
35.80
A


ATOM
1062
C
GLU
A
141
10.522
65.675
103.480
1.00
22.86
A


ATOM
1063
O
GLU
A
141
10.411
66.643
102.725
1.00
23.57
A


ATOM
1064
N
LEU
A
142
11.344
64.659
103.232
1.00
20.18
A


ATOM
1065
CA
LEU
A
142
12.178
64.628
102.033
1.00
19.91
A


ATOM
1066
CB
LEU
A
142
13.115
63.412
102.057
1.00
18.95
A


ATOM
1067
CG
LEU
A
142
14.028
63.267
100.831
1.00
18.48
A


ATOM
1068
CD1
LEU
A
142
15.022
64.433
100.771
1.00
16.40
A


ATOM
1069
CD2
LEU
A
142
14.770
61.950
100.906
1.00
20.85
A


ATOM
1070
C
LEU
A
142
11.305
64.579
100.779
1.00
19.21
A


ATOM
1071
O
LEU
A
142
11.585
65.260
99.796
1.00
17.35
A


ATOM
1072
N
ILE
A
143
10.246
63.773
100.821
1.00
17.49
A


ATOM
1073
CA
ILE
A
143
9.331
63.648
99.683
1.00
19.30
A


ATOM
1074
CB
ILE
A
143
8.175
62.680
100.010
1.00
19.22
A


ATOM
1075
CG2
ILE
A
143
7.062
62.809
98.972
1.00
18.33
A


ATOM
1076
CG1
ILE
A
143
8.717
61.250
100.077
1.00
19.66
A


ATOM
1077
CD1
ILE
A
143
7.730
60.236
100.615
1.00
22.67
A


ATOM
1078
C
ILE
A
143
8.755
65.019
99.327
1.00
20.59
A


ATOM
1079
O
ILE
A
143
8.663
65.382
98.152
1.00
20.63
A


ATOM
1080
N
VAL
A
144
8.373
65.770
100.353
1.00
21.01
A


ATOM
1081
CA
VAL
A
144
7.818
67.102
100.165
1.00
23.53
A


ATOM
1082
CB
VAL
A
144
7.307
67.679
101.501
1.00
24.60
A


ATOM
1083
CG1
VAL
A
144
6.932
69.145
101.329
1.00
27.88
A


ATOM
1084
CG2
VAL
A
144
6.111
66.883
101.979
1.00
26.36
A


ATOM
1085
C
VAL
A
144
8.860
68.055
99.590
1.00
22.64
A


ATOM
1086
O
VAL
A
144
8.578
68.805
98.660
1.00
21.65
A


ATOM
1087
N
LEU
A
145
10.069
68.015
100.141
1.00
23.18
A


ATOM
1088
CA
LEU
A
145
11.142
68.894
99.685
1.00
24.35
A


ATOM
1089
CB
LEU
A
145
12.331
68.823
100.644
1.00
25.00
A


ATOM
1090
CG
LEU
A
145
12.167
69.569
101.968
1.00
25.62
A


ATOM
1091
CD1
LEU
A
145
13.325
69.229
102.901
1.00
25.97
A


ATOM
1092
CD2
LEU
A
145
12.109
71.071
101.703
1.00
27.80
A


ATOM
1093
C
LEU
A
145
11.624
68.627
98.270
1.00
25.21
A


ATOM
1094
O
LEU
A
145
11.994
69.563
97.562
1.00
25.41
A


ATOM
1095
N
LEU
A
146
11.628
67.360
97.860
1.00
24.69
A


ATOM
1096
CA
LEU
A
146
12.074
66.988
96.519
1.00
23.80
A


ATOM
1097
CB
LEU
A
146
12.652
65.571
96.506
1.00
24.17
A


ATOM
1098
CG
LEU
A
146
14.086
65.321
96.952
1.00
22.03
A


ATOM
1099
CD1
LEU
A
146
14.373
63.824
96.883
1.00
20.90
A


ATOM
1100
CD2
LEU
A
146
15.048
66.100
96.055
1.00
24.88
A


ATOM
1101
C
LEU
A
146
10.958
67.037
95.495
1.00
24.42
A


ATOM
1102
O
LEU
A
146
11.162
67.482
94.366
1.00
26.11
A


ATOM
1103
N
GLY
A
147
9.787
66.550
95.890
1.00
23.14
A


ATOM
1104
CA
GLY
A
147
8.655
66.515
94.985
1.00
22.12
A


ATOM
1105
C
GLY
A
147
8.494
65.121
94.405
1.00
21.57
A


ATOM
1106
O
GLY
A
147
8.049
64.965
93.268
1.00
21.52
A


ATOM
1107
N
LEU
A
148
8.874
64.107
95.183
1.00
20.27
A


ATOM
1108
CA
LEU
A
148
8.757
62.711
94.759
1.00
21.34
A


ATOM
1109
CB
LEU
A
148
9.387
61.777
95.802
1.00
20.35
A


ATOM
1110
CG
LEU
A
148
10.909
61.838
95.961
1.00
22.06
A


ATOM
1111
CD1
LEU
A
148
11.357
60.867
97.037
1.00
21.03
A


ATOM
1112
CD2
LEU
A
148
11.571
61.512
94.625
1.00
21.84
A


ATOM
1113
C
LEU
A
148
7.291
62.336
94.577
1.00
20.24
A


ATOM
1114
O
LEU
A
148
6.408
62.970
95.150
1.00
19.49
A


ATOM
1115
N
ASP
A
149
7.035
61.303
93.779
1.00
21.19
A


ATOM
1116
CA
ASP
A
149
5.669
60.854
93.526
1.00
20.81
A


ATOM
1117
CB
ASP
A
149
5.678
59.672
92.550
1.00
23.34
A


ATOM
1118
CG
ASP
A
149
4.286
59.342
92.019
1.00
25.67
A


ATOM
1119
OD1
ASP
A
149
3.482
58.732
92.757
1.00
23.21
A


ATOM
1120
OD2
ASP
A
149
3.991
59.715
90.863
1.00
28.37
A


ATOM
1121
C
ASP
A
149
5.007
60.436
94.837
1.00
21.87
A


ATOM
1122
O
ASP
A
149
5.628
59.759
95.672
1.00
22.11
A


ATOM
1123
N
PRO
A
150
3.741
60.834
95.044
1.00
19.56
A


ATOM
1124
CD
PRO
A
150
2.883
61.659
94.177
1.00
21.27
A


ATOM
1125
CA
PRO
A
150
3.037
60.472
96.278
1.00
19.66
A


ATOM
1126
CB
PRO
A
150
1.696
61.199
96.141
1.00
20.41
A


ATOM
1127
CG
PRO
A
150
1.498
61.272
94.651
1.00
22.21
A


ATOM
1128
C
PRO
A
150
2.880
58.961
96.448
1.00
18.44
A


ATOM
1129
O
PRO
A
150
2.565
58.480
97.539
1.00
18.21
A


ATOM
1130
N
CYS
A
151
3.110
58.217
95.371
1.00
17.66
A


ATOM
1131
CA
CYS
A
151
3.000
56.762
95.425
1.00
18.31
A


ATOM
1132
CB
CYS
A
151
2.269
56.241
94.190
1.00
19.55
A


ATOM
1133
SG
CYS
A
151
.546
56.775
94.144
1.00
24.40
A


ATOM
1134
C
CYS
A
151
4.349
56.073
95.561
1.00
17.28
A


ATOM
1135
O
CYS
A
151
4.465
54.862
95.353
1.00
16.35
A


ATOM
1136
N
VAL
A
152
5.377
56.837
95.913
1.00
16.24
A


ATOM
1137
CA
VAL
A
152
6.700
56.247
96.086
1.00
15.84
A


ATOM
1138
CB
VAL
A
152
7.764
57.336
96.339
1.00
15.86
A


ATOM
1139
CG1
VAL
A
152
7.489
58.033
97.667
1.00
18.85
A


ATOM
1140
CG2
VAL
A
152
9.159
56.726
96.323
1.00
16.14
A


ATOM
1141
C
VAL
A
152
6.632
55.308
97.302
1.00
16.12
A


ATOM
1142
O
VAL
A
152
5.989
55.630
98.302
1.00
16.07
A


ATOM
1143
N
LYS
A
153
7.264
54.140
97.208
1.00
15.09
A


ATOM
1144
CA
LYS
A
153
7.268
53.196
98.325
1.00
15.78
A


ATOM
1145
CB
LYS
A
153
7.422
51.764
97.810
1.00
15.41
A


ATOM
1146
CG
LYS
A
153
6.190
51.244
97.072
1.00
18.15
A


ATOM
1147
CD
LYS
A
153
6.434
49.827
96.560
1.00
21.61
A


ATOM
1148
CE
LYS
A
153
5.205
49.245
95.886
1.00
24.97
A


ATOM
1149
NZ
LYS
A
153
4.778
50.049
94.708
1.00
28.12
A


ATOM
1150
C
LYS
A
153
8.405
53.551
99.291
1.00
14.03
A


ATOM
1151
O
LYS
A
153
9.573
53.586
98.909
1.00
14.56
A


ATOM
1152
N
ARG
A
154
8.047
53.803
100.546
1.00
14.71
A


ATOM
1153
CA
ARG
A
154
9.014
54.215
101.559
1.00
14.98
A


ATOM
1154
CB
ARG
A
154
8.448
55.402
102.346
1.00
15.82
A


ATOM
1155
CG
ARG
A
154
8.113
56.614
101.492
1.00
16.52
A


ATOM
1156
CD
ARG
A
154
6.666
57.044
101.681
1.00
19.72
A


ATOM
1157
NE
ARG
A
154
6.382
57.386
103.070
1.00
19.17
A


ATOM
1158
CZ
ARG
A
154
5.158
57.536
103.566
1.00
22.61
A


ATOM
1159
NH1
ARG
A
154
4.097
57.379
102.786
1.00
22.37
A


ATOM
1160
NH2
ARG
A
154
4.992
57.826
104.848
1.00
24.78
A


ATOM
1161
C
ARG
A
154
9.493
53.170
102.565
1.00
14.29
A


ATOM
1162
O
ARG
A
154
8.757
52.274
102.961
1.00
12.71
A


ATOM
1163
N
TYR
A
155
10.746
53.329
102.983
1.00
14.99
A


ATOM
1164
CA
TYR
A
155
11.375
52.466
103.972
1.00
15.35
A


ATOM
1165
CB
TYR
A
155
12.312
51.462
103.283
1.00
15.70
A


ATOM
1166
CG
TYR
A
155
11.596
50.631
102.228
1.00
15.84
A


ATOM
1167
CD1
TYR
A
155
11.282
51.176
100.985
1.00
16.66
A


ATOM
1168
CE1
TYR
A
155
10.528
50.467
100.051
1.00
16.19
A


ATOM
1169
CD2
TYR
A
155
11.144
49.338
102.511
1.00
16.71
A


ATOM
1170
CE2
TYR
A
155
10.388
48.613
101.581
1.00
17.09
A


ATOM
1171
CZ
TYR
A
155
10.078
49.189
100.355
1.00
17.25
A


ATOM
1172
OH
TYR
A
155
9.283
48.526
99.447
1.00
15.92
A


ATOM
1173
C
TYR
A
155
12.148
53.425
104.882
1.00
14.71
A


ATOM
1174
O
TYR
A
155
13.241
53.869
104.546
1.00
14.74
A


ATOM
1175
N
MET
A
156
11.550
53.752
106.022
1.00
14.82
A


ATOM
1176
CA
MET
A
156
12.134
54.679
106.992
1.00
17.67
A


ATOM
1177
CB
MET
A
156
10.997
55.466
107.663
1.00
19.67
A


ATOM
1178
CG
MET
A
156
11.412
56.537
108.663
1.00
20.86
A


ATOM
1179
SD
MET
A
156
12.370
57.875
107.942
1.00
19.21
A


ATOM
1180
CE
MET
A
156
13.973
57.560
108.704
1.00
20.63
A


ATOM
1181
C
MET
A
156
12.963
53.915
108.027
1.00
17.40
A


ATOM
1182
O
MET
A
156
12.421
53.225
108.896
1.00
16.91
A


ATOM
1183
N
MET
A
157
14.279
54.050
107.927
1.00
17.80
A


ATOM
1184
CA
MET
A
157
15.199
53.363
108.828
1.00
18.64
A


ATOM
1185
CB
MET
A
157
16.338
52.745
108.008
1.00
18.72
A


ATOM
1186
CG
MET
A
157
15.867
52.052
106.719
1.00
20.59
A


ATOM
1187
SD
MET
A
157
14.560
50.808
106.973
1.00
23.41
A


ATOM
1188
CE
MET
A
157
15.566
49.431
107.583
1.00
23.66
A


ATOM
1189
C
MET
A
157
15.769
54.291
109.911
1.00
20.02
A


ATOM
1190
O
MET
A
157
16.658
55.108
109.647
1.00
17.80
A


ATOM
1191
N
TYR
A
158
15.253
54.156
111.131
1.00
19.95
A


ATOM
1192
CA
TYR
A
158
15.695
54.972
112.256
1.00
19.35
A


ATOM
1193
CB
TYR
A
158
14.483
55.463
113.064
1.00
19.50
A


ATOM
1194
CG
TYR
A
158
13.763
56.698
112.550
1.00
20.57
A


ATOM
1195
CD1
TYR
A
158
14.397
57.942
112.528
1.00
18.96
A


ATOM
1196
CE1
TYR
A
158
13.713
59.097
112.154
1.00
19.96
A


ATOM
1197
CD2
TYR
A
158
12.418
56.641
112.173
1.00
19.97
A


ATOM
1198
CE2
TYR
A
158
11.723
57.801
111.797
1.00
21.41
A


ATOM
1199
CZ
TYR
A
158
12.379
59.024
111.794
1.00
21.79
A


ATOM
1200
OH
TYR
A
158
11.703
60.185
111.455
1.00
21.85
A


ATOM
1201
C
TYR
A
158
16.622
54.198
113.210
1.00
20.02
A


ATOM
1202
O
TYR
A
158
16.527
52.974
113.340
1.00
19.80
A


ATOM
1203
N
HIS
A
159
17.518
54.925
113.872
1.00
19.60
A


ATOM
1204
CA
HIS
A
159
18.422
54.340
114.863
1.00
20.67
A


ATOM
1205
CB
HIS
A
159
17.648
54.094
116.157
1.00
21.27
A


ATOM
1206
CG
HIS
A
159
16.600
55.123
116.445
1.00
22.15
A


ATOM
1207
CD2
HIS
A
159
15.253
55.021
116.534
1.00
21.57
A


ATOM
1208
ND1
HIS
A
159
16.902
56.444
116.699
1.00
22.61
A


ATOM
1209
CE1
HIS
A
159
15.785
57.110
116.934
1.00
22.64
A


ATOM
1210
NE2
HIS
A
159
14.771
56.270
116.841
1.00
24.23
A


ATOM
1211
C
HIS
A
159
19.062
53.023
114.436
1.00
23.07
A


ATOM
1212
O
HIS
A
159
19.092
52.069
115.218
1.00
23.59
A


ATOM
1213
N
GLN
A
160
19.584
52.970
113.218
1.00
22.10
A


ATOM
1214
CA
GLN
A
160
20.190
51.746
112.703
1.00
25.43
A


ATOM
1215
CB
GLN
A
160
20.173
51.759
111.175
1.00
24.14
A


ATOM
1216
CG
GLN
A
160
18.831
52.116
110.568
1.00
26.85
A


ATOM
1217
CD
GLN
A
160
17.869
50.948
110.516
1.00
28.45
A


ATOM
1218
OE1
GLN
A
160
18.111
49.964
109.811
1.00
28.85
A


ATOM
1219
NE2
GLN
A
160
16.767
51.049
111.256
1.00
25.36
A


ATOM
1220
C
GLN
A
160
21.620
51.550
113.181
1.00
26.36
A


ATOM
1221
O
GLN
A
160
22.037
50.431
113.465
1.00
30.01
A


ATOM
1222
N
GLY
A
161
22.377
52.637
113.257
1.00
26.59
A


ATOM
1223
CA
GLY
A
161
23.754
52.524
113.691
1.00
26.91
A


ATOM
1224
C
GLY
A
161
24.746
52.665
112.549
1.00
26.02
A


ATOM
1225
O
GLY
A
161
24.369
52.731
111.374
1.00
25.41
A


ATOM
1226
N
CYS
A
162
26.026
52.682
112.904
1.00
22.86
A


ATOM
1227
CA
CYS
A
162
27.108
52.848
111.942
1.00
21.74
A


ATOM
1228
CB
CYS
A
162
28.428
53.028
112.698
1.00
24.49
A


ATOM
1229
SG
CYS
A
162
28.529
54.618
113.582
1.00
31.19
A


ATOM
1230
C
CYS
A
162
27.282
51.787
110.855
1.00
19.91
A


ATOM
1231
O
CYS
A
162
28.078
51.979
109.941
1.00
19.35
A


ATOM
1232
N
PHE
A
163
26.561
50.673
110.940
1.00
17.83
A


ATOM
1233
CA
PHE
A
163
26.692
49.640
109.914
1.00
19.23
A


ATOM
1234
CB
PHE
A
163
26.621
48.239
110.544
1.00
19.59
A


ATOM
1235
CG
PHE
A
163
25.314
47.939
111.239
1.00
19.53
A


ATOM
1236
CD1
PHE
A
163
24.135
47.796
110.513
1.00
19.57
A


ATOM
1237
CD2
PHE
A
163
25.264
47.817
112.626
1.00
21.14
A


ATOM
1238
CE1
PHE
A
163
22.924
47.539
111.156
1.00
19.62
A


ATOM
1239
CE2
PHE
A
163
24.061
47.559
113.279
1.00
20.54
A


ATOM
1240
CZ
PHE
A
163
22.889
47.421
112.542
1.00
24.00
A


ATOM
1241
C
PHE
A
163
25.606
49.775
108.846
1.00
18.82
A


ATOM
1242
O
PHE
A
163
25.630
49.077
107.829
1.00
19.22
A


ATOM
1243
N
ALA
A
164
24.663
50.679
109.088
1.00
16.89
A


ATOM
1244
CA
ALA
A
164
23.534
50.900
108.186
1.00
17.06
A


ATOM
1245
CB
ALA
A
164
22.663
52.040
108.710
1.00
18.50
A


ATOM
1246
C
ALA
A
164
23.877
51.142
106.724
1.00
16.53
A


ATOM
1247
O
ALA
A
164
23.015
50.985
105.859
1.00
18.01
A


ATOM
1248
N
GLY
A
165
25.115
51.543
106.443
1.00
15.99
A


ATOM
1249
CA
GLY
A
165
25.521
51.758
105.064
1.00
16.79
A


ATOM
1250
C
GLY
A
165
25.337
50.452
104.309
1.00
18.19
A


ATOM
1251
O
GLY
A
165
24.874
50.420
103.160
1.00
19.45
A


ATOM
1252
N
GLY
A
166
25.700
49.358
104.965
1.00
18.25
A


ATOM
1253
CA
GLY
A
166
25.531
48.056
104.352
1.00
17.94
A


ATOM
1254
C
GLY
A
166
24.063
47.644
104.344
1.00
17.15
A


ATOM
1255
O
GLY
A
166
23.597
47.031
103.384
1.00
18.05
A


ATOM
1256
N
THR
A
167
23.339
47.988
105.408
1.00
17.80
A


ATOM
1257
CA
THR
A
167
21.921
47.647
105.545
1.00
17.61
A


ATOM
1258
CB
THR
A
167
21.331
48.188
106.866
1.00
20.13
A


ATOM
1259
OG1
THR
A
167
22.114
47.730
107.978
1.00
22.66
A


ATOM
1260
CG2
THR
A
167
19.896
47.709
107.040
1.00
20.30
A


ATOM
1261
C
THR
A
167
21.076
48.208
104.400
1.00
16.77
A


ATOM
1262
O
THR
A
167
20.233
47.504
103.837
1.00
14.42
A


ATOM
1263
N
VAL
A
168
21.295
49.473
104.050
1.00
14.03
A


ATOM
1264
CA
VAL
A
168
20.512
50.071
102.974
1.00
13.42
A


ATOM
1265
CB
VAL
A
168
20.710
51.608
102.899
1.00
13.78
A


ATOM
1266
CG1
VAL
A
168
20.145
52.250
104.155
1.00
13.71
A


ATOM
1267
CG2
VAL
A
168
22.183
51.955
102.740
1.00
15.67
A


ATOM
1268
C
VAL
A
168
20.804
49.438
101.620
1.00
13.51
A


ATOM
1269
O
VAL
A
168
19.898
49.307
100.800
1.00
15.08
A


ATOM
1270
N
LEU
A
169
22.054
49.037
101.379
1.00
13.10
A


ATOM
1271
CA
LEU
A
169
22.397
48.397
100.107
1.00
14.82
A


ATOM
1272
CB
LEU
A
169
23.920
48.257
99.954
1.00
15.02
A


ATOM
1273
CG
LEU
A
169
24.672
49.559
99.643
1.00
15.90
A


ATOM
1274
CD1
LEU
A
169
26.175
49.323
99.692
1.00
18.49
A


ATOM
1275
CD2
LEU
A
169
24.259
50.063
98.272
1.00
16.52
A


ATOM
1276
C
LEU
A
169
21.731
47.021
100.059
1.00
14.69
A


ATOM
1277
O
LEU
A
169
21.208
46.609
99.019
1.00
14.57
A


ATOM
1278
N
ARG
A
170
21.743
46.323
101.194
1.00
14.14
A


ATOM
1279
CA
ARG
A
170
21.123
45.003
101.309
1.00
13.98
A


ATOM
1280
CB
ARG
A
170
21.363
44.457
102.727
1.00
18.76
A


ATOM
1281
CG
ARG
A
170
20.615
43.185
103.107
1.00
18.37
A


ATOM
1282
CD
ARG
A
170
21.288
42.496
104.306
1.00
18.20
A


ATOM
1283
NE
ARG
A
170
21.420
43.343
105.500
1.00
18.43
A


ATOM
1284
CZ
ARG
A
170
20.434
43.602
106.355
1.00
18.99
A


ATOM
1285
NH1
ARG
A
170
19.231
43.082
106.159
1.00
15.93
A


ATOM
1286
NH2
ARG
A
170
20.650
44.378
107.415
1.00
18.98
A


ATOM
1287
C
ARG
A
170
19.626
45.116
101.006
1.00
15.04
A


ATOM
1288
O
ARG
A
170
19.045
44.266
100.325
1.00
13.87
A


ATOM
1289
N
LEU
A
171
19.010
46.185
101.496
1.00
14.48
A


ATOM
1290
CA
LEU
A
171
17.588
46.412
101.269
1.00
16.01
A


ATOM
1291
CB
LEU
A
171
17.066
47.488
102.229
1.00
16.51
A


ATOM
1292
CG
LEU
A
171
15.657
48.037
101.983
1.00
18.42
A


ATOM
1293
CD1
LEU
A
171
14.644
46.910
101.951
1.00
19.05
A


ATOM
1294
CD2
LEU
A
171
15.305
49.032
103.076
1.00
17.79
A


ATOM
1295
C
LEU
A
171
17.323
46.834
99.823
1.00
15.61
A


ATOM
1296
O
LEU
A
171
16.413
46.313
99.174
1.00
16.14
A


ATOM
1297
N
ALA
A
172
18.116
47.775
99.314
1.00
15.72
A


ATOM
1298
CA
ALA
A
172
17.934
48.241
97.942
1.00
15.52
A


ATOM
1299
CB
ALA
A
172
18.911
49.378
97.636
1.00
17.06
A


ATOM
1300
C
ALA
A
172
18.109
47.115
96.923
1.00
15.78
A


ATOM
1301
O
ALA
A
172
17.430
47.083
95.896
1.00
14.10
A


ATOM
1302
N
LYS
A
173
19.008
46.184
97.211
1.00
15.48
A


ATOM
1303
CA
LYS
A
173
19.251
45.083
96.288
1.00
15.99
A


ATOM
1304
CB
LYS
A
173
20.325
44.148
96.851
1.00
15.75
A


ATOM
1305
CG
LYS
A
173
20.576
42.910
96.001
1.00
16.03
A


ATOM
1306
CD
LYS
A
173
21.788
42.147
96.512
1.00
19.74
A


ATOM
1307
CE
LYS
A
173
21.600
40.640
96.392
1.00
22.75
A


ATOM
1308
NZ
LYS
A
173
21.274
40.183
95.023
1.00
21.00
A


ATOM
1309
C
LYS
A
173
17.985
44.289
95.972
1.00
16.47
A


ATOM
1310
O
LYS
A
173
17.703
44.008
94.804
1.00
16.32
A


ATOM
1311
N
ASP
A
174
17.230
43.924
97.005
1.00
15.20
A


ATOM
1312
CA
ASP
A
174
16.006
43.158
96.804
1.00
17.12
A


ATOM
1313
CB
ASP
A
174
15.496
42.574
98.126
1.00
18.01
A


ATOM
1314
CG
ASP
A
174
16.319
41.378
98.597
1.00
21.22
A


ATOM
1315
OD1
ASP
A
174
16.943
40.698
97.752
1.00
23.11
A


ATOM
1316
OD2
ASP
A
174
16.323
41.103
99.814
1.00
19.95
A


ATOM
1317
C
ASP
A
174
14.909
43.988
96.149
1.00
15.70
A


ATOM
1318
O
ASP
A
174
14.155
43.479
95.318
1.00
14.62
A


ATOM
1319
N
LEU
A
175
14.814
45.263
96.522
1.00
14.64
A


ATOM
1320
CA
LEU
A
175
13.804
46.138
95.936
1.00
16.58
A


ATOM
1321
CB
LEU
A
175
13.841
47.529
96.592
1.00
16.05
A


ATOM
1322
CG
LEU
A
175
13.445
47.613
98.070
1.00
16.89
A


ATOM
1323
CD1
LEU
A
175
13.483
49.061
98.527
1.00
16.97
A


ATOM
1324
CD2
LEU
A
175
12.060
47.041
98.269
1.00
17.52
A


ATOM
1325
C
LEU
A
175
14.015
46.298
94.430
1.00
15.43
A


ATOM
1326
O
LEU
A
175
13.073
46.163
93.642
1.00
17.97
A


ATOM
1327
N
ALA
A
176
15.246
46.589
94.021
1.00
14.64
A


ATOM
1328
CA
ALA
A
176
15.529
46.777
92.601
1.00
14.54
A


ATOM
1329
CB
ALA
A
176
16.918
47.382
92.412
1.00
16.05
A


ATOM
1330
C
ALA
A
176
15.421
45.508
91.764
1.00
15.09
A


ATOM
1331
O
ALA
A
176
14.923
45.536
90.637
1.00
13.49
A


ATOM
1332
N
GLU
A
177
15.899
44.398
92.309
1.00
14.74
A


ATOM
1333
CA
GLU
A
177
15.898
43.143
91.571
1.00
16.33
A


ATOM
1334
CB
GLU
A
177
16.949
42.198
92.170
1.00
16.12
A


ATOM
1335
CG
GLU
A
177
18.370
42.756
92.074
1.00
17.28
A


ATOM
1336
CD
GLU
A
177
19.425
41.845
92.680
1.00
18.83
A


ATOM
1337
OE1
GLU
A
177
19.056
40.938
93.457
1.00
16.57
A


ATOM
1338
OE2
GLU
A
177
20.624
42.051
92.388
1.00
16.51
A


ATOM
1339
C
GLU
A
177
14.568
42.422
91.445
1.00
15.11
A


ATOM
1340
O
GLU
A
177
14.355
41.688
90.479
1.00
16.69
A


ATOM
1341
N
ASN
A
178
13.667
42.633
92.398
1.00
15.01
A


ATOM
1342
CA
ASN
A
178
12.387
41.945
92.370
1.00
16.15
A


ATOM
1343
CB
ASN
A
178
11.944
41.597
93.793
1.00
14.81
A


ATOM
1344
CG
ASN
A
178
10.875
40.519
93.815
1.00
18.14
A


ATOM
1345
OD1
ASN
A
178
11.012
39.493
93.148
1.00
14.61
A


ATOM
1346
ND2
ASN
A
178
9.813
40.743
94.578
1.00
16.87
A


ATOM
1347
C
ASN
A
178
11.279
42.726
91.677
1.00
17.15
A


ATOM
1348
O
ASN
A
178
10.161
42.233
91.550
1.00
15.08
A


ATOM
1349
N
ASN
A
179
11.594
43.932
91.215
1.00
17.66
A


ATOM
1350
CA
ASN
A
179
10.595
44.773
90.568
1.00
18.39
A


ATOM
1351
CB
ASN
A
179
10.162
45.870
91.545
1.00
19.49
A


ATOM
1352
CG
ASN
A
179
9.505
45.303
92.787
1.00
18.74
A


ATOM
1353
OD1
ASN
A
179
8.377
44.818
92.734
1.00
19.10
A


ATOM
1354
ND2
ASN
A
179
10.216
45.341
93.909
1.00
19.12
A


ATOM
1355
C
ASN
A
179
11.069
45.393
89.262
1.00
18.82
A


ATOM
1356
O
ASN
A
179
11.957
46.248
89.251
1.00
18.76
A


ATOM
1357
N
LYS
A
180
10.469
44.960
88.157
1.00
18.18
A


ATOM
1358
CA
LYS
A
180
10.841
45.484
86.856
1.00
17.68
A


ATOM
1359
CB
LYS
A
180
9.980
44.851
85.759
1.00
19.83
A


ATOM
1360
CG
LYS
A
180
10.364
45.309
84.357
1.00
22.78
A


ATOM
1361
CD
LYS
A
180
9.565
44.576
83.284
1.00
28.75
A


ATOM
1362
CE
LYS
A
180
9.922
45.066
81.883
1.00
29.71
A


ATOM
1363
NZ
LYS
A
180
11.333
44.765
81.500
1.00
32.99
A


ATOM
1364
C
LYS
A
180
10.686
47.005
86.833
1.00
16.88
A


ATOM
1365
O
LYS
A
180
9.668
47.541
87.268
1.00
15.93
A


ATOM
1366
N
ASP
A
181
11.725
47.684
86.355
1.00
18.30
A


ATOM
1367
CA
ASP
A
181
11.755
49.144
86.243
1.00
20.40
A


ATOM
1368
CB
ASP
A
181
10.514
49.645
85.496
1.00
22.88
A


ATOM
1369
CG
ASP
A
181
10.441
49.128
84.070
1.00
25.36
A


ATOM
1370
OD1
ASP
A
181
11.469
49.186
83.369
1.00
27.75
A


ATOM
1371
OD2
ASP
A
181
9.354
48.677
83.647
1.00
28.77
A


ATOM
1372
C
ASP
A
181
11.886
49.907
87.561
1.00
19.53
A


ATOM
1373
O
ASP
A
181
11.843
51.140
87.572
1.00
20.09
A


ATOM
1374
N
ALA
A
182
12.055
49.195
88.668
1.00
17.14
A


ATOM
1375
CA
ALA
A
182
12.181
49.873
89.950
1.00
16.34
A


ATOM
1376
CB
ALA
A
182
12.174
48.858
91.094
1.00
16.60
A


ATOM
1377
C
ALA
A
182
13.463
50.694
90.000
1.00
14.49
A


ATOM
1378
O
ALA
A
182
14.517
50.241
89.567
1.00
13.96
A


ATOM
1379
N
ARG
A
183
13.357
51.916
90.510
1.00
14.46
A


ATOM
1380
CA
ARG
A
183
14.516
52.788
90.668
1.00
15.12
A


ATOM
1381
CB
ARG
A
183
14.474
53.953
89.679
1.00
14.27
A


ATOM
1382
CG
ARG
A
183
14.834
53.538
88.266
1.00
14.93
A


ATOM
1383
CD
ARG
A
183
16.287
53.084
88.169
1.00
13.32
A


ATOM
1384
NE
ARG
A
183
16.653
52.650
86.819
1.00
16.28
A


ATOM
1385
CZ
ARG
A
183
16.497
51.413
86.349
1.00
17.08
A


ATOM
1386
NH1
ARG
A
183
15.975
50.459
87.112
1.00
15.62
A


ATOM
1387
NH2
ARG
A
183
16.892
51.118
85.119
1.00
19.64
A


ATOM
1388
C
ARG
A
183
14.446
53.273
92.104
1.00
14.84
A


ATOM
1389
O
ARG
A
183
13.512
53.989
92.495
1.00
13.87
A


ATOM
1390
N
VAL
A
184
15.435
52.851
92.886
1.00
13.98
A


ATOM
1391
CA
VAL
A
184
15.500
53.157
94.313
1.00
13.66
A


ATOM
1392
CB
VAL
A
184
15.984
51.919
95.105
1.00
12.76
A


ATOM
1393
CG1
VAL
A
184
15.823
52.141
96.617
1.00
13.61
A


ATOM
1394
CG2
VAL
A
184
15.224
50.693
94.651
1.00
14.50
A


ATOM
1395
C
VAL
A
184
16.413
54.322
94.663
1.00
13.84
A


ATOM
1396
O
VAL
A
184
17.550
54.395
94.202
1.00
15.51
A


ATOM
1397
N
LEU
A
185
15.894
55.236
95.475
1.00
12.87
A


ATOM
1398
CA
LEU
A
185
16.672
56.375
95.931
1.00
12.68
A


ATOM
1399
CB
LEU
A
185
15.861
57.679
95.834
1.00
11.22
A


ATOM
1400
CG
LEU
A
185
16.532
58.905
96.466
1.00
11.54
A


ATOM
1401
CD1
LEU
A
185
17.866
59.176
95.778
1.00
13.85
A


ATOM
1402
CD2
LEU
A
185
15.612
60.122
96.370
1.00
11.09
A


ATOM
1403
C
LEU
A
185
17.017
56.106
97.394
1.00
11.63
A


ATOM
1404
O
LEU
A
185
16.127
55.958
98.230
1.00
13.09
A


ATOM
1405
N
ILE
A
186
18.305
56.010
97.695
1.00
12.57
A


ATOM
1406
CA
ILE
A
186
18.721
55.803
99.072
1.00
12.90
A


ATOM
1407
CB
ILE
A
186
19.867
54.790
99.209
1.00
12.53
A


ATOM
1408
CG2
ILE
A
186
20.293
54.706
100.672
1.00
15.79
A


ATOM
1409
CG1
ILE
A
186
19.441
53.411
98.703
1.00
17.58
A


ATOM
1410
CD1
ILE
A
186
20.562
52.372
98.791
1.00
15.67
A


ATOM
1411
C
ILE
A
186
19.265
57.126
99.580
1.00
12.87
A


ATOM
1412
O
ILE
A
186
20.041
57.782
98.899
1.00
12.60
A


ATOM
1413
N
VAL
A
187
18.851
57.515
100.776
1.00
13.22
A


ATOM
1414
CA
VAL
A
187
19.359
58.741
101.361
1.00
13.67
A


ATOM
1415
CB
VAL
A
187
18.316
59.866
101.349
1.00
14.26
A


ATOM
1416
CG1
VAL
A
187
18.866
61.083
102.088
1.00
15.07
A


ATOM
1417
CG2
VAL
A
187
17.967
60.228
99.917
1.00
17.12
A


ATOM
1418
C
VAL
A
187
19.763
58.463
102.795
1.00
11.28
A


ATOM
1419
O
VAL
A
187
18.930
58.089
103.618
1.00
12.82
A


ATOM
1420
N
CYS
A
188
21.051
58.621
103.071
1.00
13.30
A


ATOM
1421
CA
CYS
A
188
21.609
58.430
104.410
1.00
13.30
A


ATOM
1422
CB
CYS
A
188
22.816
57.490
104.382
1.00
14.21
A


ATOM
1423
SG
CYS
A
188
22.413
55.739
104.060
1.00
17.94
A


ATOM
1424
C
CYS
A
188
22.058
59.817
104.839
1.00
11.22
A


ATOM
1425
O
CYS
A
188
22.938
60.401
104.220
1.00
13.60
A


ATOM
1426
N
SER
A
189
21.452
60.332
105.899
1.00
12.04
A


ATOM
1427
CA
SER
A
189
21.765
61.675
106.377
1.00
12.31
A


ATOM
1428
CB
SER
A
189
20.612
62.615
106.024
1.00
14.07
A


ATOM
1429
OG
SER
A
189
20.919
63.953
106.369
1.00
13.79
A


ATOM
1430
C
SER
A
189
21.976
61.646
107.882
1.00
11.93
A


ATOM
1431
O
SER
A
189
21.054
61.336
108.638
1.00
13.29
A


ATOM
1432
N
GLU
A
190
23.185
61.993
108.314
1.00
14.10
A


ATOM
1433
CA
GLU
A
190
23.530
61.959
109.734
1.00
13.97
A


ATOM
1434
CB
GLU
A
190
24.692
60.989
109.951
1.00
16.13
A


ATOM
1435
CG
GLU
A
190
24.461
59.577
109.378
1.00
17.69
A


ATOM
1436
CD
GLU
A
190
23.440
58.747
110.160
1.00
20.46
A


ATOM
1437
OE1
GLU
A
190
22.984
59.185
111.237
1.00
17.84
A


ATOM
1438
OE2
GLU
A
190
23.096
57.638
109.692
1.00
22.18
A


ATOM
1439
C
GLU
A
190
23.890
63.345
110.270
1.00
14.72
A


ATOM
1440
O
GLU
A
190
24.438
64.184
109.551
1.00
13.22
A


ATOM
1441
N
ASN
A
191
23.584
63.569
111.542
1.00
14.47
A


ATOM
1442
CA
ASN
A
191
23.826
64.860
112.174
1.00
16.59
A


ATOM
1443
CB
ASN
A
191
22.577
65.726
111.979
1.00
15.33
A


ATOM
1444
CG
ASN
A
191
22.778
67.164
112.405
1.00
16.18
A


ATOM
1445
OD1
ASN
A
191
23.151
67.441
113.540
1.00
16.84
A


ATOM
1446
ND2
ASN
A
191
22.505
68.094
111.492
1.00
16.25
A


ATOM
1447
C
ASN
A
191
24.113
64.643
113.665
1.00
17.21
A


ATOM
1448
O
ASN
A
191
23.396
63.894
114.334
1.00
16.87
A


ATOM
1449
N
THR
A
192
25.141
65.310
114.187
1.00
17.46
A


ATOM
1450
CA
THR
A
192
25.527
65.144
115.594
1.00
17.77
A


ATOM
1451
CB
THR
A
192
27.025
65.466
115.792
1.00
19.46
A


ATOM
1452
OG1
THR
A
192
27.302
66.792
115.326
1.00
21.72
A


ATOM
1453
CG2
THR
A
192
27.885
64.475
115.021
1.00
24.93
A


ATOM
1454
C
THR
A
192
24.719
65.923
116.637
1.00
17.73
A


ATOM
1455
O
THR
A
192
25.014
65.861
117.835
1.00
17.54
A


ATOM
1456
N
ALA
A
193
23.693
66.643
116.199
1.00
16.98
A


ATOM
1457
CA
ALA
A
193
22.872
67.407
117.131
1.00
17.82
A


ATOM
1458
CB
ALA
A
193
21.695
68.043
116.395
1.00
17.73
A


ATOM
1459
C
ALA
A
193
22.357
66.533
118.276
1.00
19.11
A


ATOM
1460
O
ALA
A
193
22.269
66.978
119.420
1.00
17.05
A


ATOM
1461
N
VAL
A
194
22.033
65.279
117.973
1.00
18.73
A


ATOM
1462
CA
VAL
A
194
21.505
64.391
119.000
1.00
18.68
A


ATOM
1463
CB
VAL
A
194
20.586
63.299
118.366
1.00
20.01
A


ATOM
1464
CG1
VAL
A
194
21.429
62.229
117.676
1.00
21.94
A


ATOM
1465
CG2
VAL
A
194
19.681
62.688
119.427
1.00
20.08
A


ATOM
1466
C
VAL
A
194
22.556
63.715
119.894
1.00
18.19
A


ATOM
1467
O
VAL
A
194
22.203
63.188
120.947
1.00
18.53
A


ATOM
1468
N
THR
A
195
23.830
63.737
119.497
1.00
18.59
A


ATOM
1469
CA
THR
A
195
24.892
63.100
120.293
1.00
19.00
A


ATOM
1470
CB
THR
A
195
25.701
62.079
119.456
1.00
19.71
A


ATOM
1471
OG1
THR
A
195
26.401
62.754
118.405
1.00
19.52
A


ATOM
1472
CG2
THR
A
195
24.785
61.028
118.860
1.00
22.73
A


ATOM
1473
C
THR
A
195
25.902
64.061
120.940
1.00
18.87
A


ATOM
1474
O
THR
A
195
26.621
63.692
121.870
1.00
18.50
A


ATOM
1475
N
PHE
A
196
25.971
65.290
120.454
1.00
19.16
A


ATOM
1476
CA
PHE
A
196
26.917
66.244
121.024
1.00
16.16
A


ATOM
1477
CB
PHE
A
196
26.878
67.552
120.230
1.00
17.37
A


ATOM
1478
CG
PHE
A
196
27.756
68.625
120.797
1.00
18.14
A


ATOM
1479
CD1
PHE
A
196
27.339
69.384
121.885
1.00
19.21
A


ATOM
1480
CD2
PHE
A
196
29.030
68.834
120.285
1.00
17.83
A


ATOM
1481
CE1
PHE
A
196
28.185
70.333
122.459
1.00
19.80
A


ATOM
1482
CE2
PHE
A
196
29.878
69.779
120.854
1.00
18.39
A


ATOM
1483
CZ
PHE
A
196
29.455
70.525
121.940
1.00
16.80
A


ATOM
1484
C
PHE
A
196
26.614
66.533
122.497
1.00
15.24
A


ATOM
1485
O
PHE
A
196
25.466
66.703
122.874
1.00
15.60
A


ATOM
1486
N
ARG
A
197
27.645
66.567
123.334
1.00
15.68
A


ATOM
1487
CA
ARG
A
197
27.447
66.885
124.745
1.00
17.09
A


ATOM
1488
CB
ARG
A
197
26.765
65.729
125.500
1.00
16.77
A


ATOM
1489
CG
ARG
A
197
27.647
64.546
125.839
1.00
18.42
A


ATOM
1490
CD
ARG
A
197
26.830
63.452
126.527
1.00
17.90
A


ATOM
1491
NE
ARG
A
197
25.711
63.026
125.689
1.00
18.84
A


ATOM
1492
CZ
ARG
A
197
24.453
63.420
125.855
1.00
17.63
A


ATOM
1493
NH1
ARG
A
197
24.133
64.249
126.843
1.00
16.56
A


ATOM
1494
NH2
ARG
A
197
23.517
63.008
125.012
1.00
16.66
A


ATOM
1495
C
ARG
A
197
28.758
67.250
125.421
1.00
17.09
A


ATOM
1496
O
ARG
A
197
29.842
66.951
124.904
1.00
16.37
A


ATOM
1497
N
GLY
A
198
28.642
67.909
126.572
1.00
16.23
A


ATOM
1498
CA
GLY
A
198
29.806
68.325
127.330
1.00
16.62
A


ATOM
1499
C
GLY
A
198
30.669
67.174
127.809
1.00
16.44
A


ATOM
1500
O
GLY
A
198
30.266
66.010
127.727
1.00
17.18
A


ATOM
1501
N
PRO
A
199
31.866
67.470
128.330
1.00
16.69
A


ATOM
1502
CD
PRO
A
199
32.552
68.775
128.239
1.00
16.86
A


ATOM
1503
CA
PRO
A
199
32.781
66.435
128.814
1.00
16.94
A


ATOM
1504
CB
PRO
A
199
34.146
67.038
128.518
1.00
17.97
A


ATOM
1505
CG
PRO
A
199
33.912
68.487
128.865
1.00
16.67
A


ATOM
1506
C
PRO
A
199
32.643
66.060
130.280
1.00
18.52
A


ATOM
1507
O
PRO
A
199
32.167
66.841
131.097
1.00
17.68
A


ATOM
1508
N
SER
A
200
33.073
64.847
130.598
1.00
19.80
A


ATOM
1509
CA
SER
A
200
33.057
64.349
131.964
1.00
20.75
A


ATOM
1510
CB
SER
A
200
31.718
63.701
132.311
1.00
22.74
A


ATOM
1511
OG
SER
A
200
31.780
63.121
133.608
1.00
23.95
A


ATOM
1512
C
SER
A
200
34.162
63.317
132.105
1.00
21.76
A


ATOM
1513
O
SER
A
200
34.274
62.396
131.287
1.00
18.77
A


ATOM
1514
N
GLU
A
201
34.974
63.480
133.146
1.00
19.44
A


ATOM
1515
CA
GLU
A
201
36.076
62.568
133.425
1.00
22.42
A


ATOM
1516
CB
GLU
A
201
36.836
63.045
134.670
1.00
23.51
A


ATOM
1517
CG
GLU
A
201
37.728
64.257
134.419
1.00
28.88
A


ATOM
1518
CD
GLU
A
201
38.211
64.911
135.704
1.00
32.82
A


ATOM
1519
OE1
GLU
A
201
38.427
64.177
136.694
1.00
32.22
A


ATOM
1520
OE2
GLU
A
201
38.381
66.156
135.717
1.00
32.99
A


ATOM
1521
C
GLU
A
201
35.554
61.152
133.646
1.00
21.15
A


ATOM
1522
O
GLU
A
201
36.291
60.176
133.492
1.00
21.69
A


ATOM
1523
N
THR
A
202
34.276
61.053
133.990
1.00
21.62
A


ATOM
1524
CA
THR
A
202
33.631
59.766
134.249
1.00
23.21
A


ATOM
1525
CB
THR
A
202
32.438
59.943
135.214
1.00
24.29
A


ATOM
1526
OG1
THR
A
202
31.389
60.665
134.550
1.00
25.61
A


ATOM
1527
CG2
THR
A
202
32.870
60.724
136.454
1.00
23.67
A


ATOM
1528
C
THR
A
202
33.111
59.048
132.996
1.00
24.32
A


ATOM
1529
O
THR
A
202
32.641
57.909
133.087
1.00
23.55
A


ATOM
1530
N
ASP
A
203
33.206
59.699
131.837
1.00
24.26
A


ATOM
1531
CA
ASP
A
203
32.706
59.123
130.586
1.00
23.45
A


ATOM
1532
CB
ASP
A
203
31.356
59.772
130.253
1.00
23.20
A


ATOM
1533
CG
ASP
A
203
30.514
58.945
129.295
1.00
24.79
A


ATOM
1534
OD1
ASP
A
203
29.302
59.243
129.174
1.00
25.03
A


ATOM
1535
OD2
ASP
A
203
31.045
58.010
128.664
1.00
23.91
A


ATOM
1536
C
ASP
A
203
33.691
59.328
129.430
1.00
23.07
A


ATOM
1537
O
ASP
A
203
33.483
60.191
128.572
1.00
20.44
A


ATOM
1538
N
MET
A
204
34.761
58.535
129.410
1.00
21.83
A


ATOM
1539
CA
MET
A
204
35.771
58.643
128.362
1.00
21.76
A


ATOM
1540
CB
MET
A
204
37.010
57.808
128.720
1.00
24.97
A


ATOM
1541
CG
MET
A
204
37.825
58.362
129.886
1.00
27.70
A


ATOM
1542
SD
MET
A
204
38.360
60.089
129.663
1.00
29.97
A


ATOM
1543
CE
MET
A
204
37.140
60.917
130.571
1.00
29.70
A


ATOM
1544
C
MET
A
204
35.225
58.200
127.010
1.00
22.24
A


ATOM
1545
O
MET
A
204
35.629
58.722
125.967
1.00
20.89
A


ATOM
1546
N
ASP
A
205
34.309
57.232
127.032
1.00
21.97
A


ATOM
1547
CA
ASP
A
205
33.690
56.736
125.805
1.00
22.89
A


ATOM
1548
CB
ASP
A
205
32.629
55.690
126.133
1.00
25.54
A


ATOM
1549
CG
ASP
A
205
33.214
54.327
126.373
1.00
29.64
A


ATOM
1550
OD1
ASP
A
205
34.441
54.243
126.610
1.00
29.17
A


ATOM
1551
OD2
ASP
A
205
32.441
53.343
126.332
1.00
27.49
A


ATOM
1552
C
ASP
A
205
33.023
57.883
125.071
1.00
21.88
A


ATOM
1553
O
ASP
A
205
33.260
58.105
123.884
1.00
19.23
A


ATOM
1554
N
SER
A
206
32.172
58.606
125.793
1.00
21.39
A


ATOM
1555
CA
SER
A
206
31.452
59.726
125.210
1.00
22.34
A


ATOM
1556
CB
SER
A
206
30.534
60.361
126.260
1.00
24.35
A


ATOM
1557
OG
SER
A
206
29.801
61.441
125.711
1.00
28.36
A


ATOM
1558
C
SER
A
206
32.419
60.765
124.651
1.00
22.11
A


ATOM
1559
O
SER
A
206
32.205
61.294
123.560
1.00
22.41
A


ATOM
1560
N
LEU
A
207
33.489
61.042
125.395
1.00
20.55
A


ATOM
1561
CA
LEU
A
207
34.487
62.018
124.972
1.00
19.96
A


ATOM
1562
CB
LEU
A
207
35.563
62.184
126.055
1.00
19.69
A


ATOM
1563
CG
LEU
A
207
36.586
63.301
125.825
1.00
21.16
A


ATOM
1564
CD1
LEU
A
207
35.909
64.664
125.936
1.00
20.91
A


ATOM
1565
CD2
LEU
A
207
37.712
63.182
126.845
1.00
22.85
A


ATOM
1566
C
LEU
A
207
35.129
61.598
123.648
1.00
18.93
A


ATOM
1567
O
LEU
A
207
35.369
62.430
122.778
1.00
19.49
A


ATOM
1568
N
VAL
A
208
35.402
60.304
123.491
1.00
19.50
A


ATOM
1569
CA
VAL
A
208
35.993
59.811
122.252
1.00
18.09
A


ATOM
1570
CB
VAL
A
208
36.308
58.299
122.351
1.00
19.75
A


ATOM
1571
CG1
VAL
A
208
36.723
57.760
120.995
1.00
22.42
A


ATOM
1572
CG2
VAL
A
208
37.408
58.068
123.378
1.00
22.62
A


ATOM
1573
C
VAL
A
208
35.020
60.059
121.090
1.00
18.11
A


ATOM
1574
O
VAL
A
208
35.428
60.418
119.982
1.00
17.15
A


ATOM
1575
N
GLY
A
209
33.730
59.875
121.349
1.00
17.76
A


ATOM
1576
CA
GLY
A
209
32.744
60.102
120.308
1.00
18.19
A


ATOM
1577
C
GLY
A
209
32.715
61.554
119.858
1.00
19.02
A


ATOM
1578
O
GLY
A
209
32.445
61.843
118.689
1.00
20.34
A


ATOM
1579
N
GLN
A
210
32.993
62.472
120.780
1.00
17.40
A


ATOM
1580
CA
GLN
A
210
32.987
63.901
120.465
1.00
17.84
A


ATOM
1581
CB
GLN
A
210
33.053
64.729
121.754
1.00
16.99
A


ATOM
1582
CG
GLN
A
210
31.942
64.396
122.742
1.00
19.21
A


ATOM
1583
CD
GLN
A
210
30.542
64.568
122.154
1.00
20.53
A


ATOM
1584
OE1
GLN
A
210
29.627
63.805
122.470
1.00
20.22
A


ATOM
1585
NE2
GLN
A
210
30.369
65.578
121.314
1.00
12.91
A


ATOM
1586
C
GLN
A
210
34.133
64.284
119.534
1.00
16.80
A


ATOM
1587
O
GLN
A
210
34.113
65.350
118.921
1.00
18.59
A


ATOM
1588
N
ALA
A
211
35.123
63.405
119.415
1.00
16.27
A


ATOM
1589
CA
ALA
A
211
36.268
63.654
118.546
1.00
16.35
A


ATOM
1590
CB
ALA
A
211
37.552
63.197
119.239
1.00
18.22
A


ATOM
1591
C
ALA
A
211
36.115
62.931
117.207
1.00
15.81
A


ATOM
1592
O
ALA
A
211
36.803
63.251
116.227
1.00
16.08
A


ATOM
1593
N
LEU
A
212
35.192
61.976
117.166
1.00
14.42
A


ATOM
1594
CA
LEU
A
212
34.961
61.172
115.968
1.00
15.87
A


ATOM
1595
CB
LEU
A
212
34.778
59.703
116.370
1.00
15.09
A


ATOM
1596
CG
LEU
A
212
35.978
58.937
116.915
1.00
20.51
A


ATOM
1597
CD1
LEU
A
212
35.522
57.536
117.328
1.00
20.17
A


ATOM
1598
CD2
LEU
A
212
37.067
58.856
115.853
1.00
20.66
A


ATOM
1599
C
LEU
A
212
33.805
61.529
115.040
1.00
15.76
A


ATOM
1600
O
LEU
A
212
33.991
61.646
113.830
1.00
17.03
A


ATOM
1601
N
PHE
A
213
32.609
61.675
115.605
1.00
16.08
A


ATOM
1602
CA
PHE
A
213
31.408
61.918
114.806
1.00
16.97
A


ATOM
1603
CB
PHE
A
213
30.164
61.636
115.651
1.00
17.71
A


ATOM
1604
CG
PHE
A
213
30.186
60.292
116.314
1.00
20.56
A


ATOM
1605
CD1
PHE
A
213
30.512
59.152
115.587
1.00
22.69
A


ATOM
1606
CD2
PHE
A
213
29.923
60.168
117.671
1.00
21.84
A


ATOM
1607
CE1
PHE
A
213
30.583
57.913
116.206
1.00
24.50
A


ATOM
1608
CE2
PHE
A
213
29.992
58.928
118.297
1.00
22.58
A


ATOM
1609
CZ
PHE
A
213
30.323
57.805
117.566
1.00
20.73
A


ATOM
1610
C
PHE
A
213
31.260
63.254
114.101
1.00
15.36
A


ATOM
1611
O
PHE
A
213
31.551
64.304
114.659
1.00
12.76
A


ATOM
1612
N
ALA
A
214
30.771
63.184
112.863
1.00
16.63
A


ATOM
1613
CA
ALA
A
214
30.586
64.363
112.018
1.00
15.40
A


ATOM
1614
CB
ALA
A
214
31.759
64.497
111.050
1.00
16.43
A


ATOM
1615
C
ALA
A
214
29.276
64.260
111.243
1.00
15.29
A


ATOM
1616
O
ALA
A
214
28.595
63.232
111.301
1.00
16.79
A


ATOM
1617
N
ASP
A
215
28.946
65.316
110.502
1.00
16.01
A


ATOM
1618
CA
ASP
A
215
27.700
65.379
109.735
1.00
15.93
A


ATOM
1619
CB
ASP
A
215
26.972
66.703
109.998
1.00
17.66
A


ATOM
1620
CG
ASP
A
215
26.788
66.996
111.474
1.00
22.88
A


ATOM
1621
OD1
ASP
A
215
26.964
66.080
112.302
1.00
22.93
A


ATOM
1622
OD2
ASP
A
215
26.452
68.151
111.805
1.00
21.11
A


ATOM
1623
C
ASP
A
215
27.896
65.251
108.231
1.00
13.47
A


ATOM
1624
O
ASP
A
215
28.892
65.710
107.682
1.00
12.91
A


ATOM
1625
N
GLY
A
216
26.914
64.642
107.571
1.00
14.99
A


ATOM
1626
CA
GLY
A
216
26.969
64.472
106.135
1.00
14.98
A


ATOM
1627
C
GLY
A
216
25.807
63.636
105.626
1.00
15.88
A


ATOM
1628
O
GLY
A
216
25.154
62.929
106.398
1.00
14.93
A


ATOM
1629
N
ALA
A
217
25.537
63.731
104.329
1.00
16.39
A


ATOM
1630
CA
ALA
A
217
24.461
62.961
103.719
1.00
15.08
A


ATOM
1631
CB
ALA
A
217
23.207
63.820
103.543
1.00
14.14
A


ATOM
1632
C
ALA
A
217
24.925
62.454
102.373
1.00
14.86
A


ATOM
1633
O
ALA
A
217
25.679
63.121
101.666
1.00
15.64
A


ATOM
1634
N
ALA
A
218
24.478
61.256
102.027
1.00
13.54
A


ATOM
1635
CA
ALA
A
218
24.828
60.671
100.750
1.00
14.40
A


ATOM
1636
CB
ALA
A
218
25.784
59.499
100.950
1.00
13.37
A


ATOM
1637
C
ALA
A
218
23.521
60.202
100.131
1.00
14.12
A


ATOM
1638
O
ALA
A
218
22.622
59.752
100.845
1.00
15.69
A


ATOM
1639
N
ALA
A
219
23.408
60.336
98.815
1.00
14.03
A


ATOM
1640
CA
ALA
A
219
22.212
59.908
98.103
1.00
15.39
A


ATOM
1641
CB
ALA
A
219
21.447
61.112
97.556
1.00
15.27
A


ATOM
1642
C
ALA
A
219
22.667
59.003
96.971
1.00
14.28
A


ATOM
1643
O
ALA
A
219
23.623
59.315
96.251
1.00
14.99
A


ATOM
1644
N
ILE
A
220
21.974
57.882
96.823
1.00
13.67
A


ATOM
1645
CA
ILE
A
220
22.325
56.893
95.819
1.00
13.44
A


ATOM
1646
CB
ILE
A
220
22.991
55.672
96.495
1.00
14.33
A


ATOM
1647
CG2
ILE
A
220
23.609
54.782
95.461
1.00
14.98
A


ATOM
1648
CG1
ILE
A
220
24.037
56.134
97.515
1.00
14.70
A


ATOM
1649
CD1
ILE
A
220
23.478
56.354
98.914
1.00
16.90
A


ATOM
1650
C
ILE
A
220
21.114
56.389
95.029
1.00
13.38
A


ATOM
1651
O
ILE
A
220
20.061
56.123
95.598
1.00
14.24
A


ATOM
1652
N
ILE
A
221
21.273
56.264
93.717
1.00
13.12
A


ATOM
1653
CA
ILE
A
221
20.207
55.747
92.867
1.00
14.15
A


ATOM
1654
CB
ILE
A
221
20.057
56.561
91.562
1.00
15.24
A


ATOM
1655
CG2
ILE
A
221
18.984
55.924
90.679
1.00
14.91
A


ATOM
1656
CG1
ILE
A
221
19.692
58.013
91.886
1.00
16.31
A


ATOM
1657
CD1
ILE
A
221
18.300
58.187
92.471
1.00
17.99
A


ATOM
1658
C
ILE
A
221
20.623
54.331
92.496
1.00
15.28
A


ATOM
1659
O
ILE
A
221
21.730
54.121
91.989
1.00
14.96
A


ATOM
1660
N
ILE
A
222
19.735
53.372
92.749
1.00
15.38
A


ATOM
1661
CA
ILE
A
222
19.995
51.971
92.443
1.00
15.44
A


ATOM
1662
CB
ILE
A
222
20.102
51.136
93.720
1.00
16.28
A


ATOM
1663
CG2
ILE
A
222
20.159
49.646
93.368
1.00
15.57
A


ATOM
1664
CG1
ILE
A
222
21.346
51.553
94.510
1.00
21.06
A


ATOM
1665
CD1
ILE
A
222
21.400
50.945
95.884
1.00
23.56
A


ATOM
1666
C
ILE
A
222
18.881
51.365
91.595
1.00
15.66
A


ATOM
1667
O
ILE
A
222
17.703
51.641
91.818
1.00
12.27
A


ATOM
1668
N
GLY
A
223
19.263
50.531
90.634
1.00
13.58
A


ATOM
1669
CA
GLY
A
223
18.270
49.885
89.792
1.00
15.55
A


ATOM
1670
C
GLY
A
223
18.839
48.726
88.998
1.00
15.80
A


ATOM
1671
O
GLY
A
223
20.040
48.677
88.737
1.00
15.51
A


ATOM
1672
N
SER
A
224
17.985
47.777
88.630
1.00
15.62
A


ATOM
1673
CA
SER
A
224
18.426
46.645
87.819
1.00
17.60
A


ATOM
1674
CB
SER
A
224
17.697
45.357
88.235
1.00
17.65
A


ATOM
1675
OG
SER
A
224
18.151
44.877
89.495
1.00
15.67
A


ATOM
1676
C
SER
A
224
18.106
46.970
86.352
1.00
18.97
A


ATOM
1677
O
SER
A
224
17.281
47.835
86.074
1.00
16.29
A


ATOM
1678
N
ASP
A
225
18.772
46.288
85.427
1.00
19.29
A


ATOM
1679
CA
ASP
A
225
18.550
46.486
83.996
1.00
20.50
A


ATOM
1680
CB
ASP
A
225
17.159
45.973
83.610
1.00
22.70
A


ATOM
1681
CG
ASP
A
225
16.916
44.546
84.075
1.00
24.43
A


ATOM
1682
OD1
ASP
A
225
17.893
43.773
84.138
1.00
25.70
A


ATOM
1683
OD2
ASP
A
225
15.752
44.198
84.366
1.00
25.65
A


ATOM
1684
C
ASP
A
225
18.695
47.941
83.559
1.00
21.75
A


ATOM
1685
O
ASP
A
225
17.724
48.571
83.124
1.00
19.34
A


ATOM
1686
N
PRO
A
226
19.910
48.499
83.675
1.00
22.11
A


ATOM
1687
CD
PRO
A
226
21.149
47.915
84.216
1.00
22.58
A


ATOM
1688
CA
PRO
A
226
20.113
49.893
83.272
1.00
22.76
A


ATOM
1689
CB
PRO
A
226
21.543
50.183
83.726
1.00
23.77
A


ATOM
1690
CG
PRO
A
226
22.201
48.835
83.655
1.00
24.27
A


ATOM
1691
C
PRO
A
226
19.917
50.108
81.776
1.00
24.18
A


ATOM
1692
O
PRO
A
226
20.359
49.300
80.959
1.00
23.57
A


ATOM
1693
N
VAL
A
227
19.241
51.200
81.433
1.00
25.11
A


ATOM
1694
CA
VAL
A
227
18.983
51.552
80.041
1.00
27.09
A


ATOM
1695
CB
VAL
A
227
18.034
52.766
79.941
1.00
27.14
A


ATOM
1696
CG1
VAL
A
227
17.822
53.145
78.475
1.00
28.54
A


ATOM
1697
CG2
VAL
A
227
16.704
52.444
80.614
1.00
26.13
A


ATOM
1698
C
VAL
A
227
20.309
51.909
79.385
1.00
29.32
A


ATOM
1699
O
VAL
A
227
20.960
52.883
79.762
1.00
30.05
A


ATOM
1700
N
PRO
A
228
20.726
51.127
78.382
1.00
31.26
A


ATOM
1701
CD
PRO
A
228
19.997
50.035
77.714
1.00
31.51
A


ATOM
1702
CA
PRO
A
228
21.994
51.402
77.707
1.00
32.21
A


ATOM
1703
CB
PRO
A
228
22.097
50.258
76.698
1.00
33.57
A


ATOM
1704
CG
PRO
A
228
20.662
49.991
76.358
1.00
33.69
A


ATOM
1705
C
PRO
A
228
22.077
52.779
77.053
1.00
33.32
A


ATOM
1706
O
PRO
A
228
21.109
53.270
76.468
1.00
33.41
A


ATOM
1707
N
GLU
A
229
23.245
53.398
77.180
1.00
35.15
A


ATOM
1708
CA
GLU
A
229
23.510
54.708
76.600
1.00
35.98
A


ATOM
1709
CB
GLU
A
229
23.274
54.662
75.086
1.00
39.82
A


ATOM
1710
CG
GLU
A
229
24.112
55.656
74.289
1.00
44.78
A


ATOM
1711
CD
GLU
A
229
25.586
55.274
74.233
1.00
48.37
A


ATOM
1712
OE1
GLU
A
229
26.221
55.162
75.307
1.00
50.63
A


ATOM
1713
OE2
GLU
A
229
26.111
55.087
73.113
1.00
49.28
A


ATOM
1714
C
GLU
A
229
22.677
55.830
77.221
1.00
34.20
A


ATOM
1715
O
GLU
A
229
22.714
56.969
76.751
1.00
34.48
A


ATOM
1716
N
VAL
A
230
21.926
55.509
78.270
1.00
30.04
A


ATOM
1717
CA
VAL
A
230
21.109
56.508
78.956
1.00
27.19
A


ATOM
1718
CB
VAL
A
230
19.614
56.160
78.878
1.00
28.09
A


ATOM
1719
CG1
VAL
A
230
18.810
57.139
79.712
1.00
26.44
A


ATOM
1720
CG2
VAL
A
230
19.153
56.198
77.428
1.00
29.81
A


ATOM
1721
C
VAL
A
230
21.543
56.580
80.418
1.00
25.17
A


ATOM
1722
O
VAL
A
230
21.904
57.643
80.919
1.00
24.16
A


ATOM
1723
N
GLU
A
231
21.498
55.442
81.099
1.00
20.97
A


ATOM
1724
CA
GLU
A
231
21.929
55.371
82.491
1.00
22.09
A


ATOM
1725
CB
GLU
A
231
21.017
54.425
83.285
1.00
19.51
A


ATOM
1726
CG
GLU
A
231
19.598
54.962
83.442
1.00
20.55
A


ATOM
1727
CD
GLU
A
231
18.638
53.974
84.084
1.00
18.71
A


ATOM
1728
OE1
GLU
A
231
18.623
52.804
83.655
1.00
19.07
A


ATOM
1729
OE2
GLU
A
231
17.890
54.370
85.004
1.00
17.90
A


ATOM
1730
C
GLU
A
231
23.367
54.855
82.460
1.00
22.54
A


ATOM
1731
O
GLU
A
231
23.778
54.217
81.487
1.00
23.20
A


ATOM
1732
N
LYS
A
232
24.136
55.120
83.511
1.00
22.05
A


ATOM
1733
CA
LYS
A
232
25.525
54.684
83.522
1.00
22.17
A


ATOM
1734
CB
LYS
A
232
26.435
55.886
83.249
1.00
25.60
A


ATOM
1735
CG
LYS
A
232
26.106
56.608
81.942
1.00
30.76
A


ATOM
1736
CD
LYS
A
232
26.256
55.672
80.745
1.00
36.23
A


ATOM
1737
CE
LYS
A
232
25.664
56.271
79.471
1.00
38.29
A


ATOM
1738
NZ
LYS
A
232
26.334
57.539
79.069
1.00
37.95
A


ATOM
1739
C
LYS
A
232
25.956
53.989
84.807
1.00
21.43
A


ATOM
1740
O
LYS
A
232
26.191
54.635
85.831
1.00
18.89
A


ATOM
1741
N
PRO
A
233
26.076
52.653
84.762
1.00
20.17
A


ATOM
1742
CD
PRO
A
233
25.704
51.783
83.629
1.00
19.69
A


ATOM
1743
CA
PRO
A
233
26.485
51.853
85.920
1.00
18.06
A


ATOM
1744
CB
PRO
A
233
26.556
50.441
85.348
1.00
17.95
A


ATOM
1745
CG
PRO
A
233
25.475
50.451
84.307
1.00
19.68
A


ATOM
1746
C
PRO
A
233
27.820
52.297
86.523
1.00
17.74
A


ATOM
1747
O
PRO
A
233
28.701
52.797
85.814
1.00
17.95
A


ATOM
1748
N
ILE
A
234
27.955
52.107
87.833
1.00
16.92
A


ATOM
1749
CA
ILE
A
234
29.174
52.449
88.566
1.00
16.46
A


ATOM
1750
CB
ILE
A
234
28.901
53.555
89.610
1.00
17.04
A


ATOM
1751
CG2
ILE
A
234
30.204
53.975
90.274
1.00
17.44
A


ATOM
1752
CG1
ILE
A
234
28.248
54.759
88.926
1.00
16.08
A


ATOM
1753
CD1
ILE
A
234
27.885
55.908
89.868
1.00
15.92
A


ATOM
1754
C
ILE
A
234
29.695
51.194
89.282
1.00
16.04
A


ATOM
1755
O
ILE
A
234
30.876
50.859
89.191
1.00
15.88
A


ATOM
1756
N
PHE
A
235
28.799
50.509
89.987
1.00
14.55
A


ATOM
1757
CA
PHE
A
235
29.125
49.275
90.703
1.00
15.26
A


ATOM
1758
CB
PHE
A
235
29.483
49.545
92.174
1.00
15.43
A


ATOM
1759
CG
PHE
A
235
30.769
50.301
92.372
1.00
16.25
A


ATOM
1760
CD1
PHE
A
235
31.996
49.687
92.154
1.00
15.90
A


ATOM
1761
CD2
PHE
A
235
30.745
51.633
92.788
1.00
17.19
A


ATOM
1762
CE1
PHE
A
235
33.194
50.386
92.346
1.00
17.25
A


ATOM
1763
CE2
PHE
A
235
31.927
52.344
92.983
1.00
14.62
A


ATOM
1764
CZ
PHE
A
235
33.157
51.723
92.762
1.00
15.37
A


ATOM
1765
C
PHE
A
235
27.870
48.414
90.681
1.00
16.08
A


ATOM
1766
O
PHE
A
235
26.763
48.938
90.602
1.00
15.87
A


ATOM
1767
N
GLU
A
236
28.043
47.099
90.739
1.00
15.93
A


ATOM
1768
CA
GLU
A
236
26.907
46.180
90.781
1.00
16.34
A


ATOM
1769
CB
GLU
A
236
27.027
45.090
89.715
1.00
17.35
A


ATOM
1770
CG
GLU
A
236
27.058
45.559
88.291
1.00
20.47
A


ATOM
1771
CD
GLU
A
236
26.908
44.398
87.313
1.00
25.69
A


ATOM
1772
OE1
GLU
A
236
27.460
43.312
87.600
1.00
24.01
A


ATOM
1773
OE2
GLU
A
236
26.248
44.571
86.267
1.00
28.51
A


ATOM
1774
C
GLU
A
236
26.949
45.504
92.149
1.00
16.24
A


ATOM
1775
O
GLU
A
236
28.034
45.240
92.673
1.00
17.59
A


ATOM
1776
N
LEU
A
237
25.781
45.226
92.721
1.00
16.37
A


ATOM
1777
CA
LEU
A
237
25.695
44.558
94.013
1.00
17.59
A


ATOM
1778
CB
LEU
A
237
24.447
45.034
94.764
1.00
18.64
A


ATOM
1779
CG
LEU
A
237
24.363
46.549
95.008
1.00
18.69
A


ATOM
1780
CD1
LEU
A
237
23.085
46.887
95.785
1.00
18.52
A


ATOM
1781
CD2
LEU
A
237
25.589
47.006
95.779
1.00
19.96
A


ATOM
1782
C
LEU
A
237
25.629
43.050
93.746
1.00
18.31
A


ATOM
1783
O
LEU
A
237
24.752
42.586
93.025
1.00
18.78
A


ATOM
1784
N
VAL
A
238
26.557
42.297
94.329
1.00
19.02
A


ATOM
1785
CA
VAL
A
238
26.637
40.849
94.127
1.00
18.34
A


ATOM
1786
CB
VAL
A
238
28.117
40.419
93.976
1.00
19.89
A


ATOM
1787
CG1
VAL
A
238
28.216
38.929
93.689
1.00
20.10
A


ATOM
1788
CG2
VAL
A
238
28.765
41.213
92.855
1.00
19.49
A


ATOM
1789
C
VAL
A
238
25.982
40.027
95.243
1.00
18.89
A


ATOM
1790
O
VAL
A
238
25.114
39.187
94.989
1.00
18.23
A


ATOM
1791
N
SER
A
239
26.410
40.259
96.479
1.00
17.69
A


ATOM
1792
CA
SER
A
239
25.853
39.544
97.621
1.00
18.25
A


ATOM
1793
CB
SER
A
239
26.626
38.252
97.890
1.00
18.69
A


ATOM
1794
OG
SER
A
239
27.964
38.546
98.228
1.00
19.05
A


ATOM
1795
C
SER
A
239
25.935
40.437
98.844
1.00
18.67
A


ATOM
1796
O
SER
A
239
26.749
41.352
98.892
1.00
18.20
A


ATOM
1797
N
THR
A
240
25.079
40.167
99.823
1.00
20.47
A


ATOM
1798
CA
THR
A
240
25.040
40.933
101.061
1.00
21.73
A


ATOM
1799
CB
THR
A
240
23.894
41.977
101.038
1.00
22.77
A


ATOM
1800
OG1
THR
A
240
22.642
41.316
100.814
1.00
23.88
A


ATOM
1801
CG2
THR
A
240
24.115
42.997
99.928
1.00
23.12
A


ATOM
1802
C
THR
A
240
24.819
39.988
102.241
1.00
22.20
A


ATOM
1803
O
THR
A
240
23.843
39.236
102.264
1.00
23.37
A


ATOM
1804
N
ASP
A
241
25.738
40.011
103.203
1.00
19.70
A


ATOM
1805
CA
ASP
A
241
25.636
39.175
104.397
1.00
18.27
A


ATOM
1806
CB
ASP
A
241
26.845
38.232
104.520
1.00
20.13
A


ATOM
1807
CG
ASP
A
241
26.980
37.278
103.344
1.00
21.50
A


ATOM
1808
OD1
ASP
A
241
25.994
36.577
103.024
1.00
21.04
A


ATOM
1809
OD2
ASP
A
241
28.082
37.220
102.746
1.00
20.42
A


ATOM
1810
C
ASP
A
241
25.622
40.096
105.616
1.00
18.38
A


ATOM
1811
O
ASP
A
241
26.094
41.234
105.545
1.00
17.12
A


ATOM
1812
N
GLN
A
242
25.063
39.613
106.722
1.00
14.47
A


ATOM
1813
CA
GLN
A
242
25.039
40.379
107.961
1.00
17.92
A


ATOM
1814
CB
GLN
A
242
23.684
41.068
108.189
1.00
16.66
A


ATOM
1815
CG
GLN
A
242
23.701
42.010
109.410
1.00
18.83
A


ATOM
1816
CD
GLN
A
242
22.334
42.557
109.787
1.00
17.48
A


ATOM
1817
OE1
GLN
A
242
21.344
41.834
109.772
1.00
21.26
A


ATOM
1818
NE2
GLN
A
242
22.281
43.837
110.162
1.00
17.14
A


ATOM
1819
C
GLN
A
242
25.309
39.389
109.083
1.00
17.83
A


ATOM
1820
O
GLN
A
242
24.858
38.244
109.023
1.00
19.34
A


ATOM
1821
N
LYS
A
243
26.047
39.817
110.099
1.00
18.25
A


ATOM
1822
CA
LYS
A
243
26.354
38.927
111.209
1.00
17.86
A


ATOM
1823
CB
LYS
A
243
27.610
38.114
110.910
1.00
18.91
A


ATOM
1824
CG
LYS
A
243
27.935
37.098
112.007
1.00
20.00
A


ATOM
1825
CD
LYS
A
243
29.136
36.244
111.667
1.00
22.37
A


ATOM
1826
CE
LYS
A
243
29.250
35.069
112.631
1.00
26.37
A


ATOM
1827
NZ
LYS
A
243
29.364
35.524
114.037
1.00
25.10
A


ATOM
1828
C
LYS
A
243
26.552
39.623
112.548
1.00
19.29
A


ATOM
1829
O
LYS
A
243
27.176
40.687
112.633
1.00
16.88
A


ATOM
1830
N
LEU
A
244
26.019
38.993
113.589
1.00
18.07
A


ATOM
1831
CA
LEU
A
244
26.151
39.481
114.950
1.00
18.71
A


ATOM
1832
CB
LEU
A
244
24.867
39.232
115.746
1.00
19.92
A


ATOM
1833
CG
LEU
A
244
23.763
40.289
115.745
1.00
21.98
A


ATOM
1834
CD1
LEU
A
244
22.516
39.719
116.407
1.00
21.24
A


ATOM
1835
CD2
LEU
A
244
24.248
41.533
116.491
1.00
22.15
A


ATOM
1836
C
LEU
A
244
27.272
38.675
115.582
1.00
18.89
A


ATOM
1837
O
LEU
A
244
27.307
37.453
115.456
1.00
18.50
A


ATOM
1838
N
VAL
A
245
28.200
39.354
116.241
1.00
19.19
A


ATOM
1839
CA
VAL
A
245
29.286
38.656
116.919
1.00
20.00
A


ATOM
1840
CB
VAL
A
245
30.556
39.522
116.976
1.00
21.57
A


ATOM
1841
CG1
VAL
A
245
31.655
38.800
117.743
1.00
19.12
A


ATOM
1842
CG2
VAL
A
245
31.017
39.838
115.553
1.00
22.63
A


ATOM
1843
C
VAL
A
245
28.783
38.368
118.332
1.00
19.85
A


ATOM
1844
O
VAL
A
245
28.518
39.288
119.114
1.00
17.71
A


ATOM
1845
N
PRO
A
246
28.623
37.081
118.672
1.00
19.89
A


ATOM
1846
CD
PRO
A
246
28.880
35.885
117.856
1.00
21.03
A


ATOM
1847
CA
PRO
A
246
28.142
36.706
120.006
1.00
21.13
A


ATOM
1848
CB
PRO
A
246
28.244
35.182
119.996
1.00
21.02
A


ATOM
1849
CG
PRO
A
246
28.038
34.840
118.561
1.00
21.01
A


ATOM
1850
C
PRO
A
246
28.978
37.320
121.117
1.00
19.52
A


ATOM
1851
O
PRO
A
246
30.173
37.545
120.950
1.00
20.14
A


ATOM
1852
N
GLY
A
247
28.329
37.593
122.243
1.00
21.22
A


ATOM
1853
CA
GLY
A
247
29.006
38.152
123.399
1.00
21.01
A


ATOM
1854
C
GLY
A
247
29.635
39.525
123.242
1.00
22.29
A


ATOM
1855
O
GLY
A
247
30.659
39.802
123.863
1.00
23.76
A


ATOM
1856
N
SER
A
248
29.034
40.396
122.439
1.00
20.11
A


ATOM
1857
CA
SER
A
248
29.607
41.724
122.257
1.00
19.92
A


ATOM
1858
CB
SER
A
248
30.412
41.774
120.952
1.00
19.95
A


ATOM
1859
OG
SER
A
248
29.602
41.489
119.822
1.00
20.22
A


ATOM
1860
C
SER
A
248
28.584
42.854
122.282
1.00
19.40
A


ATOM
1861
O
SER
A
248
28.761
43.870
121.613
1.00
18.71
A


ATOM
1862
N
HIS
A
249
27.524
42.692
123.068
1.00
19.08
A


ATOM
1863
CA
HIS
A
249
26.494
43.729
123.156
1.00
20.12
A


ATOM
1864
CB
HIS
A
249
25.364
43.277
124.088
1.00
21.72
A


ATOM
1865
CG
HIS
A
249
24.341
44.339
124.359
1.00
21.96
A


ATOM
1866
CD2
HIS
A
249
24.221
45.219
125.382
1.00
23.31
A


ATOM
1867
ND1
HIS
A
249
23.290
44.600
123.505
1.00
24.75
A


ATOM
1868
CE1
HIS
A
249
22.566
45.593
123.991
1.00
20.55
A


ATOM
1869
NE2
HIS
A
249
23.110
45.988
125.128
1.00
23.96
A


ATOM
1870
C
HIS
A
249
27.087
45.037
123.682
1.00
20.12
A


ATOM
1871
O
HIS
A
249
26.687
46.133
123.261
1.00
17.34
A


ATOM
1872
N
GLY
A
250
28.045
44.908
124.599
1.00
18.18
A


ATOM
1873
CA
GLY
A
250
28.679
46.074
125.196
1.00
21.10
A


ATOM
1874
C
GLY
A
250
29.815
46.741
124.427
1.00
21.47
A


ATOM
1875
O
GLY
A
250
30.439
47.677
124.938
1.00
21.77
A


ATOM
1876
N
ALA
A
251
30.087
46.286
123.206
1.00
19.97
A


ATOM
1877
CA
ALA
A
251
31.160
46.869
122.407
1.00
20.87
A


ATOM
1878
CB
ALA
A
251
31.528
45.932
121.257
1.00
21.00
A


ATOM
1879
C
ALA
A
251
30.785
48.252
121.858
1.00
21.86
A


ATOM
1880
O
ALA
A
251
31.551
49.209
121.990
1.00
20.74
A


ATOM
1881
N
ILE
A
252
29.611
48.350
121.242
1.00
20.93
A


ATOM
1882
CA
ILE
A
252
29.147
49.615
120.667
1.00
22.07
A


ATOM
1883
CB
ILE
A
252
29.434
49.698
119.155
1.00
24.82
A


ATOM
1884
CG2
ILE
A
252
29.122
51.102
118.649
1.00
25.36
A


ATOM
1885
CG1
ILE
A
252
30.889
49.343
118.861
1.00
26.65
A


ATOM
1886
CD1
ILE
A
252
31.154
49.143
117.378
1.00
29.75
A


ATOM
1887
C
ILE
A
252
27.636
49.709
120.814
1.00
20.47
A


ATOM
1888
O
ILE
A
252
26.922
48.788
120.440
1.00
19.94
A


ATOM
1889
N
GLY
A
253
27.143
50.826
121.336
1.00
18.99
A


ATOM
1890
CA
GLY
A
253
25.709
50.958
121.488
1.00
18.83
A


ATOM
1891
C
GLY
A
253
25.288
52.292
122.059
1.00
18.02
A


ATOM
1892
O
GLY
A
253
26.093
53.220
122.166
1.00
16.78
A


ATOM
1893
N
GLY
A
254
24.019
52.378
122.429
1.00
18.04
A


ATOM
1894
CA
GLY
A
254
23.503
53.610
122.981
1.00
19.32
A


ATOM
1895
C
GLY
A
254
22.028
53.515
123.295
1.00
19.30
A


ATOM
1896
O
GLY
A
254
21.379
52.497
123.029
1.00
18.05
A


ATOM
1897
N
LEU
A
255
21.510
54.587
123.885
1.00
18.15
A


ATOM
1898
CA
LEU
A
255
20.107
54.686
124.251
1.00
17.89
A


ATOM
1899
CB
LEU
A
255
19.909
54.384
125.734
1.00
19.68
A


ATOM
1900
CG
LEU
A
255
20.124
52.976
126.283
1.00
23.45
A


ATOM
1901
CD1
LEU
A
255
19.989
53.011
127.798
1.00
23.78
A


ATOM
1902
CD2
LEU
A
255
19.114
52.020
125.679
1.00
23.72
A


ATOM
1903
C
LEU
A
255
19.653
56.112
124.006
1.00
18.61
A


ATOM
1904
O
LEU
A
255
20.425
57.053
124.198
1.00
18.26
A


ATOM
1905
N
LEU
A
256
18.408
56.275
123.575
1.00
17.55
A


ATOM
1906
CA
LEU
A
256
17.871
57.608
123.367
1.00
17.89
A


ATOM
1907
CB
LEU
A
256
16.779
57.596
122.291
1.00
17.89
A


ATOM
1908
CG
LEC
A
256
16.201
58.956
121.868
1.00
19.06
A


ATOM
1909
CD1
LEU
A
256
17.325
59.921
121.508
1.00
19.37
A


ATOM
1910
CD2
LEU
A
256
15.260
58.763
120.680
1.00
17.30
A


ATOM
1911
C
LEU
A
256
17.297
57.972
124.733
1.00
17.61
A


ATOM
1912
O
LEU
A
256
16.453
57.262
125.276
1.00
17.82
A


ATOM
1913
N
ARG
A
257
17.765
59.076
125.296
1.00
17.36
A


ATOM
1914
CA
ARG
A
257
17.319
59.491
126.617
1.00
16.80
A


ATOM
1915
CB
ARG
A
257
18.474
59.343
127.609
1.00
17.15
A


ATOM
1916
CG
ARG
A
257
19.105
57.958
127.670
1.00
18.55
A


ATOM
1917
CD
ARG
A
257
18.355
57.031
128.616
1.00
17.31
A


ATOM
1918
NE
ARG
A
257
17.311
56.261
127.945
1.00
17.17
A


ATOM
1919
CZ
ARG
A
257
16.626
55.279
128.525
1.00
16.27
A


ATOM
1920
NH1
ARG
A
257
16.871
54.952
129.790
1.00
13.61
A


ATOM
1921
NH2
ARG
A
257
15.722
54.600
127.833
1.00
16.69
A


ATOM
1922
C
ARG
A
257
16.852
60.940
126.624
1.00
17.15
A


ATOM
1923
O
ARG
A
257
16.933
61.637
125.612
1.00
16.73
A


ATOM
1924
N
GLU
A
258
16.381
61.390
127.782
1.00
17.18
A


ATOM
1925
CA
GLU
A
258
15.913
62.757
127.926
1.00
17.36
A


ATOM
1926
CB
GLU
A
258
15.210
62.911
129.283
1.00
20.05
A


ATOM
1927
CG
GLU
A
258
14.011
61.956
129.408
1.00
22.85
A


ATOM
1928
CD
GLU
A
258
13.427
61.842
130.811
1.00
25.37
A


ATOM
1929
OE1
GLU
A
258
12.878
60.761
131.128
1.00
19.60
A


ATOM
1930
OE2
GLU
A
258
13.497
62.819
131.590
1.00
24.69
A


ATOM
1931
C
GLU
A
258
17.074
63.743
127.755
1.00
16.92
A


ATOM
1932
O
GLU
A
258
16.857
64.935
127.509
1.00
17.03
A


ATOM
1933
N
VAL
A
259
18.304
63.238
127.858
1.00
16.14
A


ATOM
1934
CA
VAL
A
259
19.492
64.066
127.679
1.00
16.37
A


ATOM
1935
CB
VAL
A
259
20.598
63.720
128.707
1.00
16.27
A


ATOM
1936
CG1
VAL
A
259
20.035
63.814
130.117
1.00
18.16
A


ATOM
1937
CG2
VAL
A
259
21.158
62.319
128.428
1.00
18.20
A


ATOM
1938
C
VAL
A
259
20.072
63.891
126.276
1.00
15.70
A


ATOM
1939
O
VAL
A
259
21.175
64.360
125.984
1.00
13.21
A


ATOM
1940
N
GLY
A
260
19.323
63.210
125.411
1.00
17.11
A


ATOM
1941
CA
GLY
A
260
19.779
62.983
124.052
1.00
16.11
A


ATOM
1942
C
GLY
A
260
20.218
61.545
123.847
1.00
16.55
A


ATOM
1943
O
GLY
A
260
19.886
60.674
124.644
1.00
17.86
A


ATOM
1944
N
LEU
A
261
20.968
61.294
122.781
1.00
15.96
A


ATOM
1945
CA
LEU
A
261
21.442
59.946
122.485
1.00
18.55
A


ATOM
1946
CB
LEU
A
261
21.558
59.750
120.967
1.00
20.11
A


ATOM
1947
CG
LEU
A
261
22.175
58.437
120.472
1.00
20.59
A


ATOM
1948
CD1
LEU
A
261
21.420
57.265
121.058
1.00
21.27
A


ATOM
1949
CD2
LEU
A
261
22.126
58.391
118.943
1.00
21.87
A


ATOM
1950
C
LEU
A
261
22.794
59.680
123.143
1.00
19.66
A


ATOM
1951
O
LEU
A
261
23.817
60.224
122.730
1.00
21.17
A


ATOM
1952
N
THR
A
262
22.788
58.852
124.176
1.00
19.32
A


ATOM
1953
CA
THR
A
262
24.016
58.513
124.875
1.00
22.73
A


ATOM
1954
CB
THR
A
262
23.734
58.130
126.332
1.00
22.38
A


ATOM
1955
OG1
THR
A
262
22.958
56.927
126.367
1.00
22.08
A


ATOM
1956
CG2
THR
A
262
22.953
59.239
127.022
1.00
22.93
A


ATOM
1957
C
THR
A
262
24.604
57.320
124.143
1.00
23.97
A


ATOM
1958
O
THR
A
262
23.877
56.588
123.464
1.00
24.96
A


ATOM
1959
N
PHE
A
263
25.912
57.122
124.260
1.00
22.66
A


ATOM
1960
CA
PHE
A
263
26.541
56.001
123.580
1.00
23.58
A


ATOM
1961
CB
PHE
A
263
26.870
56.396
122.144
1.00
23.86
A


ATOM
1962
CG
PHE
A
263
27.863
57.515
122.044
1.00
24.17
A


ATOM
1963
CD1
PHE
A
263
29.226
57.249
121.994
1.00
22.87
A


ATOM
1964
CD2
PHE
A
263
27.432
58.840
122.026
1.00
25.32
A


ATOM
1965
CE1
PHE
A
263
30.153
58.290
121.928
1.00
26.00
A


ATOM
1966
CE2
PHE
A
263
28.348
59.888
121.961
1.00
26.02
A


ATOM
1967
CZ
PHE
A
263
29.712
59.613
121.912
1.00
25.32
A


ATOM
1968
C
PHE
A
263
27.801
55.525
124.281
1.00
22.97
A


ATOM
1969
O
PHE
A
263
28.412
56.253
125.067
1.00
21.66
A


ATOM
1970
N
TYR
A
264
28.173
54.283
123.995
1.00
22.70
A


ATOM
1971
CA
TYR
A
264
29.362
53.678
124.565
1.00
21.47
A


ATOM
1972
CB
TYR
A
264
28.998
52.613
125.611
1.00
21.41
A


ATOM
1973
CG
TYR
A
264
28.038
51.534
125.150
1.00
21.74
A


ATOM
1974
CD1
TYR
A
264
26.662
51.666
125.346
1.00
23.63
A


ATOM
1975
CE1
TYR
A
264
25.775
50.647
124.971
1.00
23.76
A


ATOM
1976
CD2
TYR
A
264
28.509
50.358
124.557
1.00
23.02
A


ATOM
1977
CE2
TYR
A
264
27.633
49.337
124.178
1.00
23.26
A


ATOM
1978
CZ
TYR
A
264
26.267
49.488
124.391
1.00
23.52
A


ATOM
1979
OH
TYR
A
264
25.394
48.478
124.041
1.00
21.37
A


ATOM
1980
C
TYR
A
264
30.186
53.060
123.447
1.00
22.11
A


ATOM
1981
O
TYR
A
264
29.648
52.648
122.418
1.00
22.24
A


ATOM
1982
N
LEU
A
265
31.495
53.014
123.652
1.00
23.91
A


ATOM
1983
CA
LEU
A
265
32.421
52.474
122.667
1.00
26.53
A


ATOM
1984
CB
LEU
A
265
32.998
53.610
121.815
1.00
28.16
A


ATOM
1985
CG
LEU
A
265
32.020
54.644
121.236
1.00
32.15
A


ATOM
1986
CD1
LEU
A
265
32.800
55.799
120.631
1.00
33.28
A


ATOM
1987
CD2
LEU
A
265
31.120
54.003
120.189
1.00
34.40
A


ATOM
1988
C
LEU
A
265
33.544
51.788
123.432
1.00
26.95
A


ATOM
1989
O
LEU
A
265
34.476
52.442
123.901
1.00
28.53
A


ATOM
1990
N
ASN
A
266
33.455
50.470
123.566
1.00
26.30
A


ATOM
1991
CA
ASN
A
266
34.473
49.731
124.292
1.00
25.13
A


ATOM
1992
CB
ASN
A
266
34.018
48.296
124.530
1.00
27.85
A


ATOM
1993
CG
ASN
A
266
34.746
47.651
125.683
1.00
30.74
A


ATOM
1994
OD1
ASN
A
266
34.492
47.971
126.845
1.00
33.50
A


ATOM
1995
ND2
ASN
A
266
35.669
46.750
125.374
1.00
31.85
A


ATOM
1996
C
ASN
A
266
35.826
49.712
123.580
1.00
23.31
A


ATOM
1997
O
ASN
A
266
35.900
49.755
122.354
1.00
20.14
A


ATOM
1998
N
LYS
A
267
36.896
49.633
124.366
1.00
22.48
A


ATOM
1999
CA
LYS
A
267
38.254
49.593
123.832
1.00
23.80
A


ATOM
2000
CB
LYS
A
267
39.261
49.664
124.988
1.00
27.81
A


ATOM
2001
CG
LYS
A
267
39.011
50.813
125.958
1.00
32.09
A


ATOM
2002
CD
LYS
A
267
39.933
50.764
127.182
1.00
35.92
A


ATOM
2003
CE
LYS
A
267
39.613
49.595
128.127
1.00
39.38
A


ATOM
2004
NZ
LYS
A
267
40.014
48.253
127.603
1.00
40.18
A


ATOM
2005
C
LYS
A
267
38.505
48.311
123.027
1.00
22.43
A


ATOM
2006
O
LYS
A
267
39.444
48.232
122.234
1.00
20.97
A


ATOM
2007
N
SER
A
268
37.658
47.310
123.228
1.00
21.81
A


ATOM
2008
CA
SER
A
268
37.817
46.029
122.545
1.00
22.21
A


ATOM
2009
CB
SER
A
268
37.109
44.940
123.342
1.00
24.17
A


ATOM
2010
OG
SER
A
268
35.709
45.155
123.318
1.00
27.22
A


ATOM
2011
C
SER
A
268
37.299
45.985
121.107
1.00
21.22
A


ATOM
2012
O
SER
A
268
37.464
44.974
120.421
1.00
20.98
A


ATOM
2013
N
VAL
A
269
36.681
47.067
120.647
1.00
19.08
A


ATOM
2014
CA
VAL
A
269
36.122
47.085
119.301
1.00
19.55
A


ATOM
2015
CB
VAL
A
269
35.463
48.454
118.996
1.00
18.98
A


ATOM
2016
CG1
VAL
A
269
35.028
48.515
117.536
1.00
19.74
A


ATOM
2017
CG2
VAL
A
269
34.260
48.652
119.902
1.00
18.22
A


ATOM
2018
C
VAL
A
269
37.090
46.698
118.180
1.00
19.21
A


ATOM
2019
O
VAL
A
269
36.813
45.774
117.420
1.00
21.42
A


ATOM
2020
N
PRO
A
270
38.235
47.391
118.057
1.00
19.54
A


ATOM
2021
CD
PRO
A
270
38.711
48.550
118.833
1.00
19.24
A


ATOM
2022
CA
PRO
A
270
39.186
47.047
116.995
1.00
18.50
A


ATOM
2023
CB
PRO
A
270
40.388
47.929
117.321
1.00
19.89
A


ATOM
2024
CG
PRO
A
270
39.743
49.149
117.915
1.00
19.70
A


ATOM
2025
C
PRO
A
270
39.538
45.557
116.994
1.00
19.27
A


ATOM
2026
O
PRO
A
270
39.626
44.917
115.938
1.00
16.45
A


ATOM
2027
N
ASP
A
271
39.734
45.007
118.187
1.00
17.58
A


ATOM
2028
CA
ASP
A
271
40.071
43.600
118.332
1.00
19.43
A


ATOM
2029
CB
ASP
A
271
40.500
43.321
119.785
1.00
23.68
A


ATOM
2030
CG
ASP
A
271
39.756
42.157
120.413
1.00
30.76
A


ATOM
2031
OD1
ASP
A
271
38.543
42.298
120.707
1.00
36.55
A


ATOM
2032
OD2
ASP
A
271
40.383
41.092
120.617
1.00
35.24
A


ATOM
2033
C
ASP
A
271
38.924
42.670
117.919
1.00
18.78
A


ATOM
2034
O
ASP
A
271
39.154
41.637
117.279
1.00
18.87
A


ATOM
2035
N
ILE
A
272
37.694
43.035
118.274
1.00
16.19
A


ATOM
2036
CA
ILE
A
272
36.541
42.209
117.935
1.00
16.45
A


ATOM
2037
CB
ILE
A
272
35.247
42.753
118.587
1.00
17.46
A


ATOM
2038
CG2
ILE
A
272
34.056
41.880
118.200
1.00
20.28
A


ATOM
2039
CG1
ILE
A
272
35.403
42.775
120.110
1.00
19.02
A


ATOM
2040
CD1
ILE
A
272
34.200
43.307
120.849
1.00
20.37
A


ATOM
2041
C
ILE
A
272
36.363
42.142
116.426
1.00
17.03
A


ATOM
2042
O
ILE
A
272
36.192
41.060
115.856
1.00
15.04
A


ATOM
2043
N
ILE
A
273
36.412
43.301
115.777
1.00
17.12
A


ATOM
2044
CA
ILE
A
273
36.264
43.369
114.328
1.00
17.75
A


ATOM
2045
CB
ILE
A
273
36.243
44.836
113.845
1.00
19.23
A


ATOM
2046
CG2
ILE
A
273
36.289
44.892
112.329
1.00
18.88
A


ATOM
2047
CG1
ILE
A
273
34.986
45.532
114.361
1.00
19.64
A


ATOM
2048
CD1
ILE
A
273
34.965
47.032
114.095
1.00
19.97
A


ATOM
2049
C
ILE
A
273
37.389
42.636
113.597
1.00
19.28
A


ATOM
2050
O
ILE
A
273
37.137
41.844
112.684
1.00
18.02
A


ATOM
2051
N
SER
A
274
38.631
42.888
113.996
1.00
19.59
A


ATOM
2052
CA
SER
A
274
39.759
42.246
113.328
1.00
21.11
A


ATOM
2053
CB
SER
A
274
41.087
42.873
113.790
1.00
23.23
A


ATOM
2054
OG
SER
A
274
41.285
42.719
115.183
1.00
22.56
A


ATOM
2055
C
SER
A
274
39.783
40.732
113.530
1.00
21.08
A


ATOM
2056
O
SER
A
274
40.322
39.999
112.702
1.00
21.78
A


ATOM
2057
N
GLN
A
275
39.186
40.261
114.617
1.00
21.60
A


ATOM
2058
CA
GLN
A
275
39.147
38.824
114.896
1.00
22.43
A


ATOM
2059
CB
GLN
A
275
39.056
38.583
116.406
1.00
24.09
A


ATOM
2060
CG
GLN
A
275
40.334
38.941
117.162
1.00
28.75
A


ATOM
2061
CD
GLN
A
275
40.235
38.671
118.658
1.00
33.27
A


ATOM
2062
OE1
GLN
A
275
41.170
38.958
119.411
1.00
37.52
A


ATOM
2063
NE2
GLN
A
275
39.105
38.118
119.096
1.00
31.46
A


ATOM
2064
C
GLN
A
275
37.986
38.104
114.196
1.00
21.53
A


ATOM
2065
O
GLN
A
275
37.927
36.872
114.178
1.00
21.17
A


ATOM
2066
N
ASN
A
276
37.068
38.870
113.620
1.00
19.32
A


ATOM
2067
CA
ASN
A
276
35.915
38.279
112.943
1.00
19.41
A


ATOM
2068
CB
ASN
A
276
34.631
38.724
113.641
1.00
20.01
A


ATOM
2069
CG
ASN
A
276
34.423
38.029
114.965
1.00
20.81
A


ATOM
2070
OD1
ASN
A
276
33.911
36.911
115.013
1.00
21.49
A


ATOM
2071
ND2
ASN
A
276
34.839
38.677
116.051
1.00
20.50
A


ATOM
2072
C
ASN
A
276
35.828
38.635
111.468
1.00
19.52
A


ATOM
2073
O
ASN
A
276
34.927
38.170
110.763
1.00
19.26
A


ATOM
2074
N
ILE
A
277
36.763
39.457
111.002
1.00
17.49
A


ATOM
2075
CA
ILE
A
277
36.756
39.895
109.613
1.00
19.10
A


ATOM
2076
CB
ILE
A
277
37.721
41.093
109.429
1.00
20.08
A


ATOM
2077
CG2
ILE
A
277
39.162
40.614
109.402
1.00
21.44
A


ATOM
2078
CG1
ILE
A
277
37.369
41.855
108.147
1.00
20.38
A


ATOM
2079
CD1
ILE
A
277
36.025
42.526
108.204
1.00
20.97
A


ATOM
2080
C
ILE
A
277
37.099
38.775
108.619
1.00
19.93
A


ATOM
2081
O
ILE
A
277
36.548
38.713
107.520
1.00
18.82
A


ATOM
2082
N
ASN
A
278
38.005
37.884
109.002
1.00
19.09
A


ATOM
2083
CA
ASN
A
278
38.374
36.795
108.116
1.00
21.07
A


ATOM
2084
CB
ASN
A
278
39.536
35.994
108.715
1.00
21.91
A


ATOM
2085
CG
ASN
A
278
40.884
36.662
108.491
1.00
25.15
A


ATOM
2086
OD1
ASN
A
278
41.864
36.352
109.172
1.00
29.31
A


ATOM
2087
ND2
ASN
A
278
40.945
37.569
107.525
1.00
24.39
A


ATOM
2088
C
ASN
A
278
37.183
35.883
107.832
1.00
18.75
A


ATOM
2089
O
ASN
A
278
36.996
35.446
106.696
1.00
20.29
A


ATOM
2090
N
ASP
A
279
36.374
35.600
108.848
1.00
18.61
A


ATOM
2091
CA
ASP
A
279
35.198
34.749
108.652
1.00
18.90
A


ATOM
2092
CB
ASP
A
279
34.489
34.482
109.987
1.00
22.33
A


ATOM
2093
CG
ASP
A
279
35.247
33.495
110.874
1.00
25.45
A


ATOM
2094
OD1
ASP
A
279
34.914
33.395
112.074
1.00
25.88
A


ATOM
2095
OD2
ASP
A
279
36.166
32.809
110.369
1.00
26.85
A


ATOM
2096
C
ASP
A
279
34.233
35.426
107.676
1.00
20.29
A


ATOM
2097
O
ASP
A
279
33.655
34.770
106.808
1.00
16.75
A


ATOM
2098
N
ALA
A
280
34.066
36.742
107.813
1.00
17.50
A


ATOM
2099
CA
ALA
A
280
33.175
37.487
106.922
1.00
17.54
A


ATOM
2100
CB
ALA
A
280
33.037
38.933
107.405
1.00
16.55
A


ATOM
2101
C
ALA
A
280
33.674
37.468
105.475
1.00
15.17
A


ATOM
2102
O
ALA
A
280
32.896
37.246
104.545
1.00
16.87
A


ATOM
2103
N
LEU
A
281
34.969
37.707
105.288
1.00
14.58
A


ATOM
2104
CA
LEU
A
281
35.569
37.715
103.953
1.00
14.95
A


ATOM
2105
CB
LEU
A
281
37.049
38.099
104.033
1.00
14.87
A


ATOM
2106
CG
LEU
A
281
37.369
39.579
104.261
1.00
13.37
A


ATOM
2107
CD1
LEU
A
281
38.829
39.744
104.677
1.00
15.16
A


ATOM
2108
CD2
LEU
A
281
37.082
40.346
102.981
1.00
14.81
A


ATOM
2109
C
LEU
A
281
35.445
36.349
103.286
1.00
16.22
A


ATOM
2110
O
LEU
A
281
35.119
36.254
102.104
1.00
16.95
A


ATOM
2111
N
ASN
A
282
35.712
35.301
104.060
1.00
17.34
A


ATOM
2112
CA
ASN
A
282
35.641
33.924
103.582
1.00
18.01
A


ATOM
2113
CB
ASN
A
282
36.099
32.970
104.687
1.00
20.09
A


ATOM
2114
CG
ASN
A
282
37.607
32.909
104.825
1.00
22.43
A


ATOM
2115
OD1
ASN
A
282
38.128
32.318
105.772
1.00
23.93
A


ATOM
2116
ND2
ASN
A
282
38.316
33.506
103.877
1.00
22.40
A


ATOM
2117
C
ASN
A
282
34.233
33.533
103.140
1.00
18.34
A


ATOM
2118
O
ASN
A
282
34.041
32.933
102.078
1.00
17.60
A


ATOM
2119
N
LYS
A
283
33.247
33.861
103.965
1.00
17.04
A


ATOM
2120
CA
LYS
A
283
31.865
33.538
103.641
1.00
17.42
A


ATOM
2121
CB
LYS
A
283
30.956
33.927
104.809
1.00
17.63
A


ATOM
2122
CG
LYS
A
283
29.481
33.667
104.564
1.00
20.90
A


ATOM
2123
CD
LYS
A
283
28.671
33.796
105.848
1.00
22.60
A


ATOM
2124
CE
LYS
A
283
27.207
33.456
105.613
1.00
23.23
A


ATOM
2125
NZ
LYS
A
283
26.396
33.654
106.842
1.00
21.50
A


ATOM
2126
C
LYS
A
283
31.402
34.240
102.361
1.00
16.87
A


ATOM
2127
O
LYS
A
283
30.646
33.681
101.572
1.00
14.25
A


ATOM
2128
N
ALA
A
284
31.874
35.464
102.148
1.00
16.88
A


ATOM
2129
CA
ALA
A
284
31.476
36.232
100.974
1.00
17.52
A


ATOM
2130
CB
ALA
A
284
31.625
37.733
101.263
1.00
17.75
A


ATOM
2131
C
ALA
A
284
32.224
35.879
99.691
1.00
18.24
A


ATOM
2132
O
ALA
A
284
31.629
35.844
98.607
1.00
16.71
A


ATOM
2133
N
PHE
A
285
33.520
35.606
99.811
1.00
17.45
A


ATOM
2134
CA
PHE
A
285
34.338
35.314
98.644
1.00
18.98
A


ATOM
2135
CB
PHE
A
285
35.633
36.116
98.738
1.00
18.50
A


ATOM
2136
CG
PHE
A
285
35.433
37.578
98.496
1.00
16.04
A


ATOM
2137
CD1
PHE
A
285
35.225
38.054
97.206
1.00
17.03
A


ATOM
2138
CD2
PHE
A
285
35.378
38.470
99.559
1.00
16.70
A


ATOM
2139
CE1
PHE
A
285
34.960
39.405
96.976
1.00
15.69
A


ATOM
2140
CE2
PHE
A
285
35.113
39.819
99.341
1.00
15.47
A


ATOM
2141
CZ
PHE
A
285
34.904
40.286
98.053
1.00
15.01
A


ATOM
2142
C
PHE
A
285
34.639
33.860
98.300
1.00
19.52
A


ATOM
2143
O
PHE
A
285
34.928
33.565
97.144
1.00
21.87
A


ATOM
2144
N
ASP
A
286
34.586
32.954
99.273
1.00
21.95
A


ATOM
2145
CA
ASP
A
286
34.837
31.546
98.965
1.00
20.77
A


ATOM
2146
CB
ASP
A
286
34.539
30.646
100.169
1.00
23.34
A


ATOM
2147
CG
ASP
A
286
35.656
30.642
101.204
1.00
24.33
A


ATOM
2148
OD1
ASP
A
286
36.803
31.013
100.871
1.00
27.05
A


ATOM
2149
OD2
ASP
A
286
35.382
30.247
102.359
1.00
28.19
A


ATOM
2150
C
ASP
A
286
33.972
31.093
97.779
1.00
22.10
A


ATOM
2151
O
ASP
A
286
34.462
30.438
96.860
1.00
21.16
A


ATOM
2152
N
PRO
A
287
32.671
31.436
97.786
1.00
22.48
A


ATOM
2153
CD
PRO
A
287
31.932
32.149
98.842
1.00
23.33
A


ATOM
2154
CA
PRO
A
287
31.765
31.049
96.696
1.00
23.96
A


ATOM
2155
CB
PRO
A
287
30.428
31.661
97.120
1.00
24.38
A


ATOM
2156
CG
PRO
A
287
30.520
31.683
98.613
1.00
24.07
A


ATOM
2157
C
PRO
A
287
32.200
31.567
95.329
1.00
22.69
A


ATOM
2158
O
PRO
A
287
31.804
31.030
94.298
1.00
23.56
A


ATOM
2159
N
LEU
A
288
33.012
32.617
95.324
1.00
22.92
A


ATOM
2160
CA
LEU
A
288
33.473
33.217
94.077
1.00
22.67
A


ATOM
2161
CB
LEU
A
288
33.445
34.740
94.201
1.00
23.12
A


ATOM
2162
CG
LEU
A
288
32.092
35.359
94.544
1.00
23.50
A


ATOM
2163
CD1
LEU
A
288
32.286
36.818
94.917
1.00
24.46
A


ATOM
2164
CD2
LEU
A
288
31.147
35.227
93.357
1.00
24.22
A


ATOM
2165
C
LEU
A
288
34.875
32.772
93.682
1.00
22.51
A


ATOM
2166
O
LEU
A
288
35.400
33.203
92.656
1.00
22.48
A


ATOM
2167
N
GLY
A
289
35.483
31.923
94.506
1.00
22.66
A


ATOM
2168
CA
GLY
A
289
36.819
31.445
94.214
1.00
22.32
A


ATOM
2169
C
GLY
A
289
37.894
32.502
94.378
1.00
23.21
A


ATOM
2170
O
GLY
A
289
38.919
32.451
93.701
1.00
25.59
A


ATOM
2171
N
ILE
A
290
37.668
33.454
95.281
1.00
21.89
A


ATOM
2172
CA
ILE
A
290
38.628
34.527
95.536
1.00
21.83
A


ATOM
2173
CB
ILE
A
290
37.950
35.909
95.392
1.00
22.82
A


ATOM
2174
CG2
ILE
A
290
38.870
37.006
95.899
1.00
22.10
A


ATOM
2175
CG1
ILE
A
290
37.565
36.135
93.929
1.00
23.68
A


ATOM
2176
CD1
ILE
A
290
36.795
37.419
93.684
1.00
26.43
A


ATOM
2177
C
ILE
A
290
39.210
34.397
96.944
1.00
22.08
A


ATOM
2178
O
ILE
A
290
38.467
34.401
97.924
1.00
19.27
A


ATOM
2179
N
SER
A
291
40.536
34.297
97.041
1.00
22.84
A


ATOM
2180
CA
SER
A
291
41.196
34.150
98.339
1.00
23.66
A


ATOM
2181
CB
SER
A
291
41.870
32.777
98.430
1.00
23.67
A


ATOM
2182
OG
SER
A
291
42.768
32.582
97.355
1.00
26.92
A


ATOM
2183
C
SER
A
291
42.224
35.241
98.645
1.00
23.75
A


ATOM
2184
O
SER
A
291
42.541
35.491
99.811
1.00
22.93
A


ATOM
2185
N
ASP
A
292
42.749
35.875
97.601
1.00
21.84
A


ATOM
2186
CA
ASP
A
292
43.732
36.946
97.754
1.00
21.38
A


ATOM
2187
CB
ASP
A
292
44.600
37.027
96.499
1.00
23.29
A


ATOM
2188
CG
ASP
A
292
45.573
38.195
96.526
1.00
25.31
A


ATOM
2189
OD1
ASP
A
292
46.344
38.334
95.552
1.00
25.14
A


ATOM
2190
OD2
ASP
A
292
45.568
38.968
97.507
1.00
25.25
A


ATOM
2191
C
ASP
A
292
42.959
38.251
97.944
1.00
21.41
A


ATOM
2192
O
ASP
A
292
42.425
38.807
96.984
1.00
21.93
A


ATOM
2193
N
TYR
A
293
42.905
38.739
99.177
1.00
18.89
A


ATOM
2194
CA
TYR
A
293
42.154
39.956
99.463
1.00
18.84
A


ATOM
2195
CB
TYR
A
293
41.693
39.932
100.924
1.00
19.73
A


ATOM
2196
CG
TYR
A
293
40.867
38.694
101.219
1.00
20.84
A


ATOM
2197
CD1
TYR
A
293
39.776
38.355
100.417
1.00
20.08
A


ATOM
2198
CE1
TYR
A
293
39.041
37.194
100.647
1.00
22.81
A


ATOM
2199
CD2
TYR
A
293
41.199
37.841
102.268
1.00
22.83
A


ATOM
2200
CE2
TYR
A
293
40.472
36.677
102.509
1.00
22.45
A


ATOM
2201
CZ
TYR
A
293
39.398
36.359
101.695
1.00
22.48
A


ATOM
2202
OH
TYR
A
293
38.694
35.198
101.921
1.00
24.63
A


ATOM
2203
C
TYR
A
293
42.842
41.263
99.098
1.00
19.82
A


ATOM
2204
O
TYR
A
293
42.291
42.351
99.306
1.00
17.41
A


ATOM
2205
N
ASN
A
294
44.047
41.166
98.538
1.00
18.72
A


ATOM
2206
CA
ASN
A
294
44.733
42.360
98.075
1.00
20.17
A


ATOM
2207
CB
ASN
A
294
46.251
42.222
98.206
1.00
19.86
A


ATOM
2208
CG
ASN
A
294
46.758
42.686
99.550
1.00
20.29
A


ATOM
2209
OD1
ASN
A
294
46.625
43.860
99.902
1.00
18.17
A


ATOM
2210
ND2
ASN
A
294
47.338
41.767
100.314
1.00
16.51
A


ATOM
2211
C
ASN
A
294
44.364
42.526
96.603
1.00
20.20
A


ATOM
2212
O
ASN
A
294
44.704
43.534
95.983
1.00
22.64
A


ATOM
2213
N
SER
A
295
43.661
41.535
96.052
1.00
18.20
A


ATOM
2214
CA
SER
A
295
43.269
41.568
94.642
1.00
17.41
A


ATOM
2215
CB
SER
A
295
43.334
40.161
94.025
1.00
18.06
A


ATOM
2216
OG
SER
A
295
42.218
39.371
94.403
1.00
19.73
A


ATOM
2217
C
SER
A
295
41.886
42.153
94.401
1.00
15.25
A


ATOM
2218
O
SER
A
295
41.413
42.179
93.263
1.00
16.23
A


ATOM
2219
N
ILE
A
296
41.227
42.609
95.463
1.00
11.98
A


ATOM
2220
CA
ILE
A
296
39.902
43.217
95.328
1.00
13.58
A


ATOM
2221
CB
ILE
A
296
38.838
42.449
96.145
1.00
13.48
A


ATOM
2222
CG2
ILE
A
296
38.699
41.018
95.600
1.00
15.53
A


ATOM
2223
CG1
ILE
A
296
39.233
42.414
97.629
1.00
11.74
A


ATOM
2224
CD1
ILE
A
296
38.169
41.828
98.546
1.00
14.12
A


ATOM
2225
C
ILE
A
296
39.992
44.638
95.867
1.00
13.88
A


ATOM
2226
O
ILE
A
296
40.947
44.959
96.575
1.00
15.39
A


ATOM
2227
N
PHE
A
297
39.029
45.492
95.527
1.00
14.99
A


ATOM
2228
CA
PHE
A
297
39.051
46.849
96.064
1.00
15.65
A


ATOM
2229
CB
PHE
A
297
38.472
47.885
95.081
1.00
14.57
A


ATOM
2230
CG
PHE
A
297
37.069
47.603
94.611
1.00
15.26
A


ATOM
2231
CD1
PHE
A
297
36.843
46.812
93.487
1.00
15.33
A


ATOM
2232
CD2
PHE
A
297
35.979
48.191
95.244
1.00
15.89
A


ATOM
2233
CE1
PHE
A
297
35.554
46.618
92.996
1.00
15.51
A


ATOM
2234
CE2
PHE
A
297
34.684
48.005
94.764
1.00
16.37
A


ATOM
2235
CZ
PHE
A
297
34.469
47.219
93.636
1.00
16.21
A


ATOM
2236
C
PHE
A
297
38.294
46.866
97.383
1.00
15.79
A


ATOM
2237
O
PHE
A
297
37.377
46.063
97.596
1.00
15.96
A


ATOM
2238
N
TRP
A
298
38.672
47.792
98.261
1.00
13.76
A


ATOM
2239
CA
TRP
A
298
38.078
47.891
99.589
1.00
13.84
A


ATOM
2240
CB
TRP
A
298
39.170
47.690
100.652
1.00
15.00
A


ATOM
2241
CG
TRP
A
298
39.590
46.272
100.872
1.00
15.82
A


ATOM
2242
CD2
TRP
A
298
39.394
45.499
102.066
1.00
16.38
A


ATOM
2243
CE2
TRP
A
298
39.943
44.220
101.831
1.00
16.53
A


ATOM
2244
CE3
TRP
A
298
38.805
45.766
103.313
1.00
15.24
A


ATOM
2245
CD1
TRP
A
298
40.232
45.454
99.986
1.00
16.86
A


ATOM
2246
NE1
TRP
A
298
40.448
44.216
100.556
1.00
16.65
A


ATOM
2247
CZ2
TRP
A
298
39.922
43.204
102.799
1.00
16.35
A


ATOM
2248
CZ3
TRP
A
298
38.783
44.756
104.275
1.00
17.36
A


ATOM
2249
CH2
TRP
A
298
39.342
43.489
104.009
1.00
16.55
A


ATOM
2250
C
TRP
A
298
37.343
49.181
99.931
1.00
15.44
A


ATOM
2251
O
TRP
A
298
37.838
50.274
99.674
1.00
15.12
A


ATOM
2252
N
ILE
A
299
36.161
49.033
100.521
1.00
14.10
A


ATOM
2253
CA
ILE
A
299
35.367
50.163
100.984
1.00
14.84
A


ATOM
2254
CB
ILE
A
299
34.126
50.423
100.098
1.00
12.44
A


ATOM
2255
CG2
ILE
A
299
33.252
51.511
100.741
1.00
12.82
A


ATOM
2256
CG1
ILE
A
299
34.584
50.866
98.704
1.00
11.52
A


ATOM
2257
CD1
ILE
A
299
33.463
51.004
97.691
1.00
14.86
A


ATOM
2258
C
ILE
A
299
34.930
49.777
102.390
1.00
15.35
A


ATOM
2259
O
ILE
A
299
34.006
48.991
102.566
1.00
18.17
A


ATOM
2260
N
ALA
A
300
35.613
50.316
103.393
1.00
16.48
A


ATOM
2261
CA
ALA
A
300
35.290
49.991
104.779
1.00
16.75
A


ATOM
2262
CB
ALA
A
300
36.514
49.376
105.460
1.00
17.74
A


ATOM
2263
C
ALA
A
300
34.808
51.191
105.583
1.00
18.52
A


ATOM
2264
O
ALA
A
300
35.309
52.303
105.410
1.00
17.89
A


ATOM
2265
N
HIS
A
301
33.836
50.961
106.464
1.00
16.34
A


ATOM
2266
CA
HIS
A
301
33.325
52.024
107.319
1.00
17.03
A


ATOM
2267
CB
HIS
A
301
32.164
51.524
108.179
1.00
16.06
A


ATOM
2268
CG
HIS
A
301
31.682
52.532
109.179
1.00
17.35
A


ATOM
2269
CD2
HIS
A
301
31.646
52.501
110.533
1.00
18.74
A


ATOM
2270
ND1
HIS
A
301
31.211
53.776
108.813
1.00
18.35
A


ATOM
2271
CE1
HIS
A
301
30.906
54.468
109.897
1.00
18.11
A


ATOM
2272
NE2
HIS
A
301
31.160
53.718
110.955
1.00
18.22
A


ATOM
2273
C
HIS
A
301
34.472
52.467
108.224
1.00
17.49
A


ATOM
2274
O
HIS
A
301
35.043
51.655
108.947
1.00
18.95
A


ATOM
2275
N
PRO
A
302
34.834
53.760
108.184
1.00
18.79
A


ATOM
2276
CD
PRO
A
302
34.297
54.826
107.317
1.00
17.58
A


ATOM
2277
CA
PRO
A
302
35.927
54.261
109.022
1.00
18.96
A


ATOM
2278
CB
PRO
A
302
36.359
55.527
108.287
1.00
19.58
A


ATOM
2279
CG
PRO
A
302
35.052
56.068
107.800
1.00
19.28
A


ATOM
2280
C
PRO
A
302
35.465
54.544
110.453
1.00
19.81
A


ATOM
2281
O
PRO
A
302
35.482
55.691
110.911
1.00
19.60
A


ATOM
2282
N
GLY
A
303
35.044
53.497
111.155
1.00
19.20
A


ATOM
2283
CA
GLY
A
303
34.582
53.671
112.521
1.00
20.12
A


ATOM
2284
C
GLY
A
303
35.644
54.332
113.377
1.00
23.33
A


ATOM
2285
O
GLY
A
303
35.337
55.051
114.333
1.00
23.31
A


ATOM
2286
N
GLY
A
304
36.903
54.092
113.019
1.00
23.07
A


ATOM
2287
CA
GLY
A
304
38.011
54.668
113.757
1.00
23.38
A


ATOM
2288
C
GLY
A
304
39.348
54.218
113.199
1.00
23.14
A


ATOM
2289
O
GLY
A
304
39.438
53.186
112.535
1.00
20.51
A


ATOM
2290
N
ARG
A
305
40.387
54.999
113.467
1.00
22.81
A


ATOM
2291
CA
ARG
A
305
41.737
54.697
112.997
1.00
23.64
A


ATOM
2292
CB
ARG
A
305
42.710
55.725
113.576
1.00
28.06
A


ATOM
2293
CG
ARG
A
305
44.174
55.458
113.274
1.00
32.94
A


ATOM
2294
CD
ARG
A
305
45.033
55.993
114.403
1.00
37.33
A


ATOM
2295
NE
ARG
A
305
46.429
56.179
114.021
1.00
40.67
A


ATOM
2296
CZ
ARG
A
305
47.327
56.795
114.783
1.00
42.66
A


ATOM
2297
NH1
ARG
A
305
46.971
57.280
115.965
1.00
43.64
A


ATOM
2298
NH2
ARG
A
305
48.578
56.938
114.363
1.00
45.35
A


ATOM
2299
C
ARG
A
305
42.197
53.289
113.392
1.00
22.76
A


ATOM
2300
O
ARG
A
305
42.684
52.522
112.556
1.00
20.99
A


ATOM
2301
N
ALA
A
306
42.037
52.968
114.673
1.00
20.50
A


ATOM
2302
CA
ALA
A
306
42.440
51.676
115.224
1.00
20.59
A


ATOM
2303
CB
ALA
A
306
42.125
51.638
116.718
1.00
21.66
A


ATOM
2304
C
ALA
A
306
41.804
50.472
114.527
1.00
19.21
A


ATOM
2305
O
ALA
A
306
42.460
49.452
114.330
1.00
18.90
A


ATOM
2306
N
ILE
A
307
40.523
50.578
114.183
1.00
19.28
A


ATOM
2307
CA
ILE
A
307
39.837
49.488
113.496
1.00
17.80
A


ATOM
2308
CB
ILE
A
307
38.336
49.810
113.287
1.00
19.27
A


ATOM
2309
CG2
ILE
A
307
37.675
48.727
112.429
1.00
18.14
A


ATOM
2310
CG1
ILE
A
307
37.639
49.907
114.644
1.00
20.87
A


ATOM
2311
CD1
ILE
A
307
36.228
50.441
114.578
1.00
22.85
A


ATOM
2312
C
ILE
A
307
40.489
49.241
112.138
1.00
19.21
A


ATOM
2313
O
ILE
A
307
40.796
48.102
111.782
1.00
19.01
A


ATOM
2314
N
LEU
A
308
40.709
50.308
111.376
1.00
17.31
A


ATOM
2315
CA
LEU
A
308
41.326
50.156
110.069
1.00
18.79
A


ATOM
2316
CB
LEU
A
308
41.352
51.503
109.329
1.00
16.84
A


ATOM
2317
CG
LEU
A
308
39.986
52.166
109.093
1.00
16.60
A


ATOM
2318
CD1
LEU
A
308
40.178
53.524
108.421
1.00
15.51
A


ATOM
2319
CD2
LEU
A
308
39.109
51.256
108.237
1.00
17.66
A


ATOM
2320
C
LEU
A
308
42.744
49.588
110.203
1.00
17.81
A


ATOM
2321
O
LEU
A
308
43.110
48.655
109.486
1.00
18.53
A


ATOM
2322
N
ASP
A
309
43.535
50.134
111.124
1.00
18.08
A


ATOM
2323
CA
ASP
A
309
44.900
49.648
111.317
1.00
19.43
A


ATOM
2324
CB
ASP
A
309
45.591
50.381
112.476
1.00
19.58
A


ATOM
2325
CG
ASP
A
309
45.864
51.850
112.176
1.00
22.23
A


ATOM
2326
OD1
ASP
A
309
45.633
52.295
111.032
1.00
20.80
A


ATOM
2327
OD2
ASP
A
309
46.319
52.559
113.100
1.00
21.47
A


ATOM
2328
C
ASP
A
309
44.924
48.147
111.607
1.00
18.66
A


ATOM
2329
O
ASP
A
309
45.695
47.394
110.999
1.00
19.55
A


ATOM
2330
N
GLN
A
310
44.079
47.704
112.530
1.00
19.17
A


ATOM
2331
CA
GLN
A
310
44.063
46.292
112.893
1.00
19.27
A


ATOM
2332
CB
GLN
A
310
43.334
46.107
114.221
1.00
20.83
A


ATOM
2333
CG
GLN
A
310
44.151
46.673
115.379
1.00
24.30
A


ATOM
2334
CD
GLN
A
310
43.560
46.375
116.735
1.00
26.80
A


ATOM
2335
OE1
GLN
A
310
43.182
45.239
117.026
1.00
29.98
A


ATOM
2336
NE2
GLN
A
310
43.486
47.393
117.582
1.00
28.79
A


ATOM
2337
C
GLN
A
310
43.524
45.344
111.825
1.00
19.13
A


ATOM
2338
O
GLN
A
310
43.979
44.207
111.727
1.00
17.24
A


ATOM
2339
N
VAL
A
311
42.576
45.812
111.019
1.00
17.16
A


ATOM
2340
CA
VAL
A
311
42.031
44.990
109.948
1.00
17.35
A


ATOM
2341
CB
VAL
A
311
40.769
45.643
109.330
1.00
17.80
A


ATOM
2342
CG1
VAL
A
311
40.413
44.973
107.995
1.00
19.45
A


ATOM
2343
CG2
VAL
A
311
39.606
45.506
110.299
1.00
16.82
A


ATOM
2344
C
VAL
A
311
43.115
44.799
108.881
1.00
18.13
A


ATOM
2345
O
VAL
A
311
43.300
43.690
108.370
1.00
15.50
A


ATOM
2346
N
GLU
A
312
43.841
45.872
108.559
1.00
18.03
A


ATOM
2347
CA
GLU
A
312
44.923
45.801
107.572
1.00
20.30
A


ATOM
2348
CB
GLU
A
312
45.571
47.176
107.369
1.00
22.51
A


ATOM
2349
CG
GLU
A
312
44.802
48.102
106.456
1.00
27.98
A


ATOM
2350
CD
GLU
A
312
45.431
49.483
106.368
1.00
30.36
A


ATOM
2351
OE1
GLU
A
312
46.632
49.578
106.053
1.00
32.69
A


ATOM
2352
OE2
GLU
A
312
44.721
50.477
106.614
1.00
37.60
A


ATOM
2353
C
GLU
A
312
45.998
44.820
108.034
1.00
19.51
A


ATOM
2354
O
GLU
A
312
46.588
44.095
107.230
1.00
18.40
A


ATOM
2355
N
GLN
A
313
46.261
44.820
109.336
1.00
21.42
A


ATOM
2356
CA
GLN
A
313
47.255
43.932
109.919
1.00
22.77
A


ATOM
2357
CB
GLN
A
313
47.501
44.318
111.378
1.00
24.05
A


ATOM
2358
CG
GLN
A
313
48.585
45.356
111.572
1.00
30.88
A


ATOM
2359
CD
GLN
A
313
49.975
44.748
111.512
1.00
35.25
A


ATOM
2360
OE1
GLN
A
313
50.409
44.255
110.473
1.00
36.85
A


ATOM
2361
NE2
GLN
A
313
50.677
44.769
112.639
1.00
40.09
A


ATOM
2362
C
GLN
A
313
46.818
42.472
109.837
1.00
21.31
A


ATOM
2363
O
GLN
A
313
47.577
41.608
109.399
1.00
22.70
A


ATOM
2364
N
LYS
A
314
45.585
42.208
110.249
1.00
21.15
A


ATOM
2365
CA
LYS
A
314
45.040
40.855
110.236
1.00
20.71
A


ATOM
2366
CB
LYS
A
314
43.665
40.836
110.904
1.00
20.52
A


ATOM
2367
CG
LYS
A
314
43.101
39.443
111.099
1.00
22.86
A


ATOM
2368
CD
LYS
A
314
43.948
38.650
112.092
1.00
26.70
A


ATOM
2369
CE
LYS
A
314
43.390
37.253
112.316
1.00
28.35
A


ATOM
2370
NZ
LYS
A
314
44.240
36.482
113.266
1.00
30.58
A


ATOM
2371
C
LYS
A
314
44.915
40.275
108.834
1.00
21.15
A


ATOM
2372
O
LYS
A
314
45.290
39.132
108.596
1.00
19.91
A


ATOM
2373
N
VAL
A
315
44.388
41.062
107.902
1.00
20.16
A


ATOM
2374
CA
VAL
A
315
44.207
40.589
106.538
1.00
18.60
A


ATOM
2375
CB
VAL
A
315
43.032
41.338
105.847
1.00
17.87
A


ATOM
2376
CG1
VAL
A
315
42.788
40.768
104.465
1.00
16.87
A


ATOM
2377
CG2
VAL
A
315
41.760
41.215
106.693
1.00
16.04
A


ATOM
2378
C
VAL
A
315
45.476
40.736
105.699
1.00
19.02
A


ATOM
2379
O
VAL
A
315
45.562
40.199
104.595
1.00
18.12
A


ATOM
2380
N
ASN
A
316
46.461
41.456
106.235
1.00
19.03
A


ATOM
2381
CA
ASN
A
316
47.733
41.683
105.548
1.00
17.21
A


ATOM
2382
CB
ASN
A
316
48.421
40.338
105.251
1.00
17.36
A


ATOM
2383
CG
ASN
A
316
49.882
40.499
104.883
1.00
18.38
A


ATOM
2384
OD1
ASN
A
316
50.580
41.357
105.430
1.00
16.26
A


ATOM
2385
ND2
ASN
A
316
50.360
39.665
103.964
1.00
20.02
A


ATOM
2386
C
ASN
A
316
47.535
42.481
104.255
1.00
16.62
A


ATOM
2387
O
ASN
A
316
48.041
42.110
103.192
1.00
16.59
A


ATOM
2388
N
LEU
A
317
46.811
43.593
104.362
1.00
15.63
A


ATOM
2389
CA
LEU
A
317
46.522
44.447
103.212
1.00
17.20
A


ATOM
2390
CB
LEU
A
317
45.210
45.212
103.441
1.00
16.66
A


ATOM
2391
CG
LEU
A
317
43.936
44.404
103.701
1.00
18.52
A


ATOM
2392
CD1
LEU
A
317
42.778
45.353
104.044
1.00
17.08
A


ATOM
2393
CD2
LEU
A
317
43.601
43.585
102.470
1.00
17.68
A


ATOM
2394
C
LEU
A
317
47.609
45.467
102.918
1.00
17.33
A


ATOM
2395
O
LEU
A
317
48.164
46.074
103.836
1.00
17.14
A


ATOM
2396
N
LYS
A
318
47.906
45.660
101.637
1.00
16.70
A


ATOM
2397
CA
LYS
A
318
48.881
46.665
101.243
1.00
17.06
A


ATOM
2398
CB
LYS
A
318
49.074
46.657
99.727
1.00
17.35
A


ATOM
2399
CG
LYS
A
318
49.847
45.446
99.211
1.00
18.37
A


ATOM
2400
CD
LYS
A
318
49.921
45.426
97.698
1.00
21.60
A


ATOM
2401
CE
LYS
A
318
48.542
45.255
97.074
1.00
24.87
A


ATOM
2402
NZ
LYS
A
318
48.600
45.204
95.581
1.00
27.70
A


ATOM
2403
C
LYS
A
318
48.261
47.987
101.694
1.00
18.31
A


ATOM
2404
O
LYS
A
318
47.041
48.155
101.637
1.00
18.82
A


ATOM
2405
N
PRO
A
319
49.087
48.939
102.149
1.00
17.96
A


ATOM
2406
CD
PRO
A
319
50.558
48.856
102.225
1.00
19.64
A


ATOM
2407
CA
PRO
A
319
48.625
50.249
102.621
1.00
18.88
A


ATOM
2408
CB
PRO
A
319
49.929
51.020
102.821
1.00
20.93
A


ATOM
2409
CG
PRO
A
319
50.885
49.952
103.210
1.00
19.51
A


ATOM
2410
C
PRO
A
319
47.658
51.003
101.712
1.00
19.97
A


ATOM
2411
O
PRO
A
319
46.757
51.691
102.195
1.00
18.40
A


ATOM
2412
N
GLU
A
320
47.843
50.883
100.401
1.00
21.10
A


ATOM
2413
CA
GLU
A
320
46.979
51.588
99.463
1.00
22.71
A


ATOM
2414
CB
GLU
A
320
47.555
51.508
98.044
1.00
24.81
A


ATOM
2415
CG
GLU
A
320
48.939
52.155
97.890
1.00
33.10
A


ATOM
2416
CD
GLU
A
320
48.985
53.612
98.339
1.00
35.66
A


ATOM
2417
OE1
GLU
A
320
48.827
53.883
99.548
1.00
39.88
A


ATOM
2418
OE2
GLU
A
320
49.184
54.495
97.479
1.00
40.62
A


ATOM
2419
C
GLU
A
320
45.531
51.106
99.464
1.00
20.57
A


ATOM
2420
O
GLU
A
320
44.631
51.859
99.105
1.00
18.61
A


ATOM
2421
N
LYS
A
321
45.300
49.863
99.874
1.00
18.41
A


ATOM
2422
CA
LYS
A
321
43.941
49.318
99.901
1.00
17.42
A


ATOM
2423
CB
LYS
A
321
43.957
47.914
100.525
1.00
18.91
A


ATOM
2424
CG
LYS
A
321
44.603
46.871
99.627
1.00
18.63
A


ATOM
2425
CD
LYS
A
321
43.749
46.700
98.385
1.00
23.06
A


ATOM
2426
CE
LYS
A
321
44.484
46.048
97.247
1.00
25.54
A


ATOM
2427
NZ
LYS
A
321
43.617
46.071
96.032
1.00
22.67
A


ATOM
2428
C
LYS
A
321
42.941
50.216
100.645
1.00
18.06
A


ATOM
2429
O
LYS
A
321
41.819
50.436
100.176
1.00
14.96
A


ATOM
2430
N
MET
A
322
43.352
50.736
101.800
1.00
17.37
A


ATOM
2431
CA
MET
A
322
42.496
51.606
102.613
1.00
16.72
A


ATOM
2432
CB
MET
A
322
42.793
51.380
104.097
1.00
18.06
A


ATOM
2433
CG
MET
A
322
42.387
50.017
104.612
1.00
21.77
A


ATOM
2434
SD
MET
A
322
40.608
49.856
104.615
1.00
26.83
A


ATOM
2435
CE
MET
A
322
40.379
48.447
105.741
1.00
26.99
A


ATOM
2436
C
MET
A
322
42.652
53.099
102.313
1.00
17.42
A


ATOM
2437
O
MET
A
322
42.136
53.940
103.055
1.00
14.58
A


ATOM
2438
N
LYS
A
323
43.353
53.439
101.237
1.00
16.80
A


ATOM
2439
CA
LYS
A
323
43.570
54.846
100.923
1.00
18.31
A


ATOM
2440
CB
LYS
A
323
44.413
54.994
99.654
1.00
20.83
A


ATOM
2441
CG
LYS
A
323
44.660
56.440
99.277
1.00
22.34
A


ATOM
2442
CD
LYS
A
323
45.599
56.576
98.090
1.00
25.20
A


ATOM
2443
CE
LYS
A
323
45.679
58.028
97.661
1.00
27.32
A


ATOM
2444
NZ
LYS
A
323
45.942
58.916
98.833
1.00
27.74
A


ATOM
2445
C
LYS
A
323
42.291
55.668
100.788
1.00
18.02
A


ATOM
2446
O
LYS
A
323
42.161
56.717
101.423
1.00
16.95
A


ATOM
2447
N
ALA
A
324
41.347
55.207
99.970
1.00
17.17
A


ATOM
2448
CA
ALA
A
324
40.094
55.946
99.784
1.00
16.35
A


ATOM
2449
CB
ALA
A
324
39.206
55.241
98.752
1.00
16.45
A


ATOM
2450
C
ALA
A
324
39.359
56.070
101.116
1.00
16.75
A


ATOM
2451
O
ALA
A
324
38.813
57.127
101.456
1.00
14.58
A


ATOM
2452
N
THR
A
325
39.358
54.984
101.876
1.00
14.25
A


ATOM
2453
CA
THR
A
325
38.699
54.969
103.174
1.00
14.58
A


ATOM
2454
CB
THR
A
325
38.752
53.568
103.792
1.00
15.15
A


ATOM
2455
OG1
THR
A
325
37.986
52.670
102.974
1.00
15.01
A


ATOM
2456
CG2
THR
A
325
38.181
53.589
105.205
1.00
13.11
A


ATOM
2457
C
THR
A
325
39.314
55.967
104.162
1.00
14.64
A


ATOM
2458
O
THR
A
325
38.601
56.719
104.820
1.00
14.11
A


ATOM
2459
N
ARG
A
326
40.636
55.977
104.263
1.00
15.97
A


ATOM
2460
CA
ARG
A
326
41.298
56.883
105.194
1.00
14.76
A


ATOM
2461
CB
ARG
A
326
42.766
56.485
105.367
1.00
17.17
A


ATOM
2462
CG
ARG
A
326
42.970
55.120
106.039
1.00
19.48
A


ATOM
2463
CD
ARG
A
326
44.462
54.809
106.181
1.00
21.00
A


ATOM
2464
NE
ARG
A
326
44.729
53.505
106.789
1.00
22.68
A


ATOM
2465
CZ
ARG
A
326
44.655
53.237
108.091
1.00
23.59
A


ATOM
2466
NH1
ARG
A
326
44.314
54.181
108.960
1.00
19.97
A


ATOM
2467
NH2
ARG
A
326
44.947
52.018
108.529
1.00
21.31
A


ATOM
2468
C
ARG
A
326
41.199
58.343
104.763
1.00
15.95
A


ATOM
2469
O
ARG
A
326
41.204
59.244
105.607
1.00
15.73
A


ATOM
2470
N
ASP
A
327
41.116
58.586
103.458
1.00
14.52
A


ATOM
2471
CA
ASP
A
327
41.015
59.965
102.974
1.00
16.76
A


ATOM
2472
CB
ASP
A
327
41.272
60.025
101.463
1.00
17.65
A


ATOM
2473
CG
ASP
A
327
42.758
59.881
101.119
1.00
22.23
A


ATOM
2474
OD1
ASP
A
327
43.584
59.866
102.059
1.00
22.40
A


ATOM
2475
OD2
ASP
A
327
43.105
59.789
99.917
1.00
22.97
A


ATOM
2476
C
ASP
A
327
39.660
60.582
103.331
1.00
15.90
A


ATOM
2477
O
ASP
A
327
39.570
61.782
103.623
1.00
16.46
A


ATOM
2478
N
VAL
A
328
38.610
59.767
103.317
1.00
14.20
A


ATOM
2479
CA
VAL
A
328
37.278
60.247
103.685
1.00
12.95
A


ATOM
2480
CB
VAL
A
328
36.187
59.206
103.338
1.00
11.54
A


ATOM
2481
CG1
VAL
A
328
34.883
59.551
104.045
1.00
13.59
A


ATOM
2482
CG2
VAL
A
328
35.964
59.185
101.824
1.00
12.86
A


ATOM
2483
C
VAL
A
328
37.281
60.513
105.188
1.00
13.33
A


ATOM
2484
O
VAL
A
328
36.744
61.519
105.660
1.00
13.72
A


ATOM
2485
N
LEU
A
329
37.899
59.612
105.942
1.00
13.61
A


ATOM
2486
CA
LEU
A
329
37.980
59.794
107.380
1.00
15.20
A


ATOM
2487
CB
LEU
A
329
38.674
58.594
108.028
1.00
18.20
A


ATOM
2488
CG
LEU
A
329
38.996
58.680
109.524
1.00
20.07
A


ATOM
2489
CD1
LEU
A
329
37.723
58.841
110.346
1.00
20.82
A


ATOM
2490
CD2
LEU
A
329
39.742
57.416
109.938
1.00
21.93
A


ATOM
2491
C
LEU
A
329
38.761
61.081
107.684
1.00
15.58
A


ATOM
2492
O
LEU
A
329
38.367
61.858
108.543
1.00
16.85
A


ATOM
2493
N
SER
A
330
39.859
61.307
106.974
1.00
15.16
A


ATOM
2494
CA
SER
A
330
40.663
62.507
107.208
1.00
18.06
A


ATOM
2495
CB
SER
A
330
41.946
62.489
106.371
1.00
19.28
A


ATOM
2496
OG
SER
A
330
42.770
61.393
106.713
1.00
25.07
A


ATOM
2497
C
SER
A
330
39.933
63.800
106.901
1.00
16.71
A


ATOM
2498
O
SER
A
330
40.085
64.787
107.620
1.00
17.70
A


ATOM
2499
N
ASN
A
331
39.146
63.791
105.832
1.00
17.19
A


ATOM
2500
CA
ASN
A
331
38.434
64.984
105.390
1.00
18.16
A


ATOM
2501
CB
ASN
A
331
38.402
65.014
103.858
1.00
20.73
A


ATOM
2502
CG
ASN
A
331
39.792
65.061
103.251
1.00
28.36
A


ATOM
2503
OD1
ASN
A
331
40.259
64.090
102.651
1.00
30.89
A


ATOM
2504
ND2
ASN
A
331
40.465
66.191
103.413
1.00
27.88
A


ATOM
2505
C
ASN
A
331
37.019
65.203
105.917
1.00
17.12
A


ATOM
2506
O
ASN
A
331
36.514
66.329
105.874
1.00
14.65
A


ATOM
2507
N
TYR
A
332
36.382
64.152
106.422
1.00
14.10
A


ATOM
2508
CA
TYR
A
332
35.011
64.284
106.902
1.00
15.56
A


ATOM
2509
CB
TYR
A
332
34.056
63.599
105.919
1.00
15.57
A


ATOM
2510
CG
TYR
A
332
34.102
64.155
104.522
1.00
16.22
A


ATOM
2511
CD1
TYR
A
332
33.342
65.269
104.165
1.00
17.52
A


ATOM
2512
CE1
TYR
A
332
33.378
65.773
102.865
1.00
19.70
A


ATOM
2513
CD2
TYR
A
332
34.901
63.562
103.547
1.00
17.03
A


ATOM
2514
CE2
TYR
A
332
34.945
64.055
102.254
1.00
18.80
A


ATOM
2515
CZ
TYR
A
332
34.183
65.155
101.919
1.00
20.10
A


ATOM
2516
OH
TYR
A
332
34.234
65.629
100.633
1.00
22.65
A


ATOM
2517
C
TYR
A
332
34.732
63.728
108.285
1.00
14.80
A


ATOM
2518
O
TYR
A
332
33.714
64.056
108.887
1.00
13.27
A


ATOM
2519
N
GLY
A
333
35.618
62.880
108.792
1.00
16.28
A


ATOM
2520
CA
GLY
A
333
35.371
62.290
110.090
1.00
16.15
A


ATOM
2521
C
GLY
A
333
34.397
61.131
109.935
1.00
18.11
A


ATOM
2522
O
GLY
A
333
34.141
60.682
108.819
1.00
17.58
A


ATOM
2523
N
ASN
A
334
33.848
60.660
111.051
1.00
17.54
A


ATOM
2524
CA
ASN
A
334
32.908
59.540
111.053
1.00
18.71
A


ATOM
2525
CB
ASN
A
334
33.058
58.749
112.361
1.00
17.01
A


ATOM
2526
CG
ASN
A
334
32.251
57.462
112.370
1.00
21.08
A


ATOM
2527
OD1
ASN
A
334
31.230
57.342
111.691
1.00
21.26
A


ATOM
2528
ND2
ASN
A
334
32.700
56.493
113.160
1.00
19.04
A


ATOM
2529
C
ASN
A
334
31.459
60.008
110.898
1.00
16.98
A


ATOM
2530
O
ASN
A
334
30.834
60.434
111.867
1.00
16.99
A


ATOM
2531
N
MET
A
335
30.931
59.911
109.678
1.00
16.95
A


ATOM
2532
CA
MET
A
335
29.559
60.317
109.381
1.00
17.01
A


ATOM
2533
CB
MET
A
335
29.506
60.953
107.986
1.00
15.24
A


ATOM
2534
CG
MET
A
335
30.446
62.147
107.832
1.00
13.35
A


ATOM
2535
SD
MET
A
335
30.472
62.793
106.156
1.00
14.73
A


ATOM
2536
CE
MET
A
335
31.510
61.522
105.336
1.00
11.91
A


ATOM
2537
C
MET
A
335
28.552
59.160
109.469
1.00
18.59
A


ATOM
2538
O
MET
A
335
27.514
59.167
108.806
1.00
17.45
A


ATOM
2539
N
SER
A
336
28.860
58.170
110.299
1.00
16.90
A


ATOM
2540
CA
SER
A
336
27.984
57.015
110.470
1.00
17.61
A


ATOM
2541
CB
SER
A
336
26.719
57.421
111.241
1.00
19.09
A


ATOM
2542
OG
SER
A
336
25.946
56.279
111.582
1.00
22.75
A


ATOM
2543
C
SER
A
336
27.602
56.337
109.144
1.00
16.31
A


ATOM
2544
O
SER
A
336
28.465
56.038
108.324
1.00
15.30
A


ATOM
2545
N
SER
A
337
26.313
56.103
108.925
1.00
17.61
A


ATOM
2546
CA
SER
A
337
25.875
55.419
107.708
1.00
18.36
A


ATOM
2547
CB
SER
A
337
24.351
55.237
107.722
1.00
20.03
A


ATOM
2548
OG
SER
A
337
23.682
56.467
107.520
1.00
23.69
A


ATOM
2549
C
SER
A
337
26.295
56.038
106.367
1.00
18.79
A


ATOM
2550
O
SER
A
337
26.441
55.320
105.378
1.00
19.51
A


ATOM
2551
N
ALA
A
338
26.499
57.352
106.319
1.00
16.65
A


ATOM
2552
CA
ALA
A
338
26.879
57.996
105.059
1.00
15.68
A


ATOM
2553
CB
ALA
A
338
26.664
59.499
105.162
1.00
15.38
A


ATOM
2554
C
ALA
A
338
28.313
57.703
104.595
1.00
16.86
A


ATOM
2555
O
ALA
A
338
28.601
57.725
103.396
1.00
14.14
A


ATOM
2556
N
CYS
A
339
29.205
57.409
105.540
1.00
17.12
A


ATOM
2557
CA
CYS
A
339
30.611
57.142
105.222
1.00
18.43
A


ATOM
2558
CB
CYS
A
339
31.313
56.504
106.420
1.00
20.52
A


ATOM
2559
SG
CYS
A
339
31.572
57.633
107.785
1.00
28.72
A


ATOM
2560
C
CYS
A
339
30.936
56.309
103.994
1.00
17.20
A


ATOM
2561
O
CYS
A
339
31.583
56.789
103.068
1.00
16.64
A


ATOM
2562
N
VAL
A
340
30.507
55.052
103.986
1.00
15.01
A


ATOM
2563
CA
VAL
A
340
30.824
54.181
102.865
1.00
15.41
A


ATOM
2564
CB
VAL
A
340
30.187
52.785
103.054
1.00
15.58
A


ATOM
2565
CG1
VAL
A
340
30.751
52.143
104.320
1.00
17.48
A


ATOM
2566
CG2
VAL
A
340
28.678
52.900
103.154
1.00
14.74
A


ATOM
2567
C
VAL
A
340
30.449
54.741
101.493
1.00
13.89
A


ATOM
2568
O
VAL
A
340
31.066
54.385
100.495
1.00
15.42
A


ATOM
2569
N
PHE
A
341
29.456
55.623
101.441
1.00
13.57
A


ATOM
2570
CA
PHE
A
341
29.042
56.194
100.161
1.00
12.42
A


ATOM
2571
CB
PHE
A
341
27.574
56.622
100.232
1.00
12.79
A


ATOM
2572
CG
PHE
A
341
26.655
55.482
100.543
1.00
13.77
A


ATOM
2573
CD1
PHE
A
341
26.541
54.414
99.661
1.00
16.75
A


ATOM
2574
CD2
PHE
A
341
25.992
55.417
101.763
1.00
17.19
A


ATOM
2575
CE1
PHE
A
341
25.788
53.287
99.992
1.00
17.00
A


ATOM
2576
CE2
PHE
A
341
25.234
54.291
102.108
1.00
18.62
A


ATOM
2577
CZ
PHE
A
341
25.137
53.224
101.216
1.00
18.80
A


ATOM
2578
C
PHE
A
341
29.957
57.334
99.732
1.00
13.00
A


ATOM
2579
O
PHE
A
341
30.159
57.550
98.537
1.00
13.53
A


ATOM
2580
N
PHE
A
342
30.524
58.056
100.698
1.00
13.71
A


ATOM
2581
CA
PHE
A
342
31.476
59.116
100.361
1.00
13.53
A


ATOM
2582
CB
PHE
A
342
31.854
59.952
101.592
1.00
13.59
A


ATOM
2583
CG
PHE
A
342
30.880
61.058
101.907
1.00
14.46
A


ATOM
2584
CD1
PHE
A
342
29.606
60.776
102.386
1.00
12.57
A


ATOM
2585
CD2
PHE
A
342
31.254
62.388
101.738
1.00
17.01
A


ATOM
2586
CE1
PHE
A
342
28.708
61.813
102.702
1.00
15.37
A


ATOM
2587
CE2
PHE
A
342
30.369
63.429
102.047
1.00
15.22
A


ATOM
2588
CZ
PHE
A
342
29.097
63.140
102.531
1.00
14.23
A


ATOM
2589
C
PHE
A
342
32.731
58.410
99.836
1.00
12.98
A


ATOM
2590
O
PHE
A
342
33.405
58.895
98.932
1.00
11.91
A


ATOM
2591
N
ILE
A
343
33.033
57.248
100.412
1.00
12.62
A


ATOM
2592
CA
ILE
A
343
34.201
56.473
100.011
1.00
13.59
A


ATOM
2593
CB
ILE
A
343
34.500
55.344
101.038
1.00
12.49
A


ATOM
2594
CG2
ILE
A
343
35.671
54.512
100.561
1.00
12.36
A


ATOM
2595
CG1
ILE
A
343
34.814
55.964
102.412
1.00
14.83
A


ATOM
2596
CD1
ILE
A
343
34.874
54.980
103.572
1.00
13.14
A


ATOM
2597
C
ILE
A
343
33.962
55.868
98.627
1.00
13.20
A


ATOM
2598
O
ILE
A
343
34.832
55.911
97.764
1.00
13.62
A


ATOM
2599
N
MET
A
344
32.782
55.293
98.427
1.00
13.40
A


ATOM
2600
CA
MET
A
344
32.427
54.721
97.131
1.00
13.12
A


ATOM
2601
CB
MET
A
344
31.003
54.157
97.188
1.00
14.23
A


ATOM
2602
CG
MET
A
344
30.511
53.546
95.877
1.00
16.48
A


ATOM
2603
SD
MET
A
344
28.804
52.931
95.975
1.00
17.54
A


ATOM
2604
CE
MET
A
344
29.016
51.477
97.056
1.00
17.01
A


ATOM
2605
C
MET
A
344
32.506
55.817
96.060
1.00
11.32
A


ATOM
2606
O
MET
A
344
33.005
55.599
94.959
1.00
10.54
A


ATOM
2607
N
ASP
A
345
32.025
57.008
96.399
1.00
12.42
A


ATOM
2608
CA
ASP
A
345
32.021
58.121
95.445
1.00
13.38
A


ATOM
2609
CB
ASP
A
345
31.203
59.298
96.006
1.00
11.94
A


ATOM
2610
CG
ASP
A
345
30.908
60.365
94.957
1.00
19.30
A


ATOM
2611
OD1
ASP
A
345
30.675
60.005
93.781
1.00
17.49
A


ATOM
2612
OD2
ASP
A
345
30.896
61.566
95.313
1.00
22.09
A


ATOM
2613
C
ASP
A
345
33.442
58.557
95.108
1.00
12.01
A


ATOM
2614
O
ASP
A
345
33.761
58.776
93.943
1.00
11.34
A


ATOM
2615
N
LEU
A
346
34.291
58.669
96.126
1.00
11.80
A


ATOM
2616
CA
LEU
A
346
35.687
59.055
95.932
1.00
12.85
A


ATOM
2617
CB
LEU
A
346
36.409
59.176
97.274
1.00
12.43
A


ATOM
2618
CG
LEU
A
346
37.879
59.603
97.208
1.00
14.56
A


ATOM
2619
CD1
LEU
A
346
37.981
60.981
96.550
1.00
16.43
A


ATOM
2620
CD2
LEU
A
346
38.462
59.650
98.612
1.00
14.89
A


ATOM
2621
C
LEU
A
346
36.413
58.012
95.097
1.00
12.74
A


ATOM
2622
O
LEU
A
346
37.178
58.348
94.199
1.00
12.63
A


ATOM
2623
N
MET
A
347
36.172
56.741
95.402
1.00
11.90
A


ATOM
2624
CA
MET
A
347
36.832
55.667
94.675
1.00
13.12
A


ATOM
2625
CB
MET
A
347
36.423
54.298
95.223
1.00
15.14
A


ATOM
2626
CG
MET
A
347
37.188
53.175
94.563
1.00
13.55
A


ATOM
2627
SD
MET
A
347
36.836
51.538
95.229
1.00
18.57
A


ATOM
2628
CE
MET
A
347
37.681
51.612
96.825
1.00
16.80
A


ATOM
2629
C
MET
A
347
36.533
55.698
93.185
1.00
13.68
A


ATOM
2630
O
MET
A
347
37.449
55.649
92.371
1.00
13.15
A


ATOM
2631
N
ARG
A
348
35.258
55.767
92.816
1.00
13.41
A


ATOM
2632
CA
ARG
A
348
34.940
55.795
91.398
1.00
13.56
A


ATOM
2633
CB
ARG
A
348
33.434
55.614
91.175
1.00
14.13
A


ATOM
2634
CG
ARG
A
348
32.567
56.688
91.771
1.00
16.43
A


ATOM
2635
CD
ARG
A
348
31.890
57.508
90.683
1.00
15.10
A


ATOM
2636
NE
ARG
A
348
30.971
58.478
91.263
1.00
17.74
A


ATOM
2637
CZ
ARG
A
348
29.944
59.021
90.614
1.00
19.42
A


ATOM
2638
NH1
ARG
A
348
29.692
58.693
89.350
1.00
17.83
A


ATOM
2639
NH2
ARG
A
348
29.161
59.883
91.236
1.00
18.56
A


ATOM
2640
C
ARG
A
348
35.440
57.076
90.733
1.00
13.82
A


ATOM
2641
O
ARG
A
348
35.909
57.042
89.596
1.00
12.96
A


ATOM
2642
N
LYS
A
349
35.352
58.202
91.436
1.00
14.40
A


ATOM
2643
CA
LYS
A
349
35.815
59.463
90.866
1.00
16.03
A


ATOM
2644
CB
LYS
A
349
35.438
60.639
91.779
1.00
19.29
A


ATOM
2645
CG
LYS
A
349
33.987
61.107
91.627
1.00
22.73
A


ATOM
2646
CD
LYS
A
349
33.657
62.225
92.615
1.00
25.81
A


ATOM
2647
CE
LYS
A
349
32.356
62.941
92.264
1.00
28.02
A


ATOM
2648
NZ
LYS
A
349
31.184
62.031
92.147
1.00
29.68
A


ATOM
2649
C
LYS
A
349
37.325
59.441
90.624
1.00
16.60
A


ATOM
2650
O
LYS
A
349
37.803
59.892
89.583
1.00
15.58
A


ATOM
2651
N
ARG
A
350
38.080
58.917
91.582
1.00
16.64
A


ATOM
2652
CA
ARG
A
350
39.527
58.845
91.430
1.00
16.97
A


ATOM
2653
CB
ARG
A
350
40.191
58.429
92.738
1.00
19.36
A


ATOM
2654
CG
ARG
A
350
40.260
59.531
93.768
1.00
23.11
A


ATOM
2655
CD
ARG
A
350
41.012
59.072
95.001
1.00
25.31
A


ATOM
2656
NE
ARG
A
350
41.301
60.187
95.897
1.00
26.05
A


ATOM
2657
CZ
ARG
A
350
41.851
60.050
97.096
1.00
25.60
A


ATOM
2658
NH1
ARG
A
350
42.174
58.842
97.540
1.00
24.33
A


ATOM
2659
NH2
ARG
A
350
42.070
61.118
97.851
1.00
27.53
A


ATOM
2660
C
ARG
A
350
39.921
57.863
90.342
1.00
16.79
A


ATOM
2661
O
ARG
A
350
40.840
58.132
89.574
1.00
15.18
A


ATOM
2662
N
SER
A
351
39.237
56.723
90.276
1.00
15.93
A


ATOM
2663
CA
SER
A
351
39.559
55.731
89.257
1.00
15.20
A


ATOM
2664
CB
SER
A
351
38.727
54.462
89.468
1.00
16.39
A


ATOM
2665
OG
SER
A
351
39.017
53.893
90.735
1.00
14.41
A


ATOM
2666
C
SER
A
351
39.316
56.319
87.863
1.00
15.10
A


ATOM
2667
O
SER
A
351
40.113
56.122
86.946
1.00
13.78
A


ATOM
2668
N
LEU
A
352
38.221
57.056
87.716
1.00
16.59
A


ATOM
2669
CA
LEU
A
352
37.897
57.692
86.444
1.00
18.06
A


ATOM
2670
CB
LEU
A
352
36.540
58.389
86.541
1.00
19.15
A


ATOM
2671
CG
LEU
A
352
35.292
57.505
86.519
1.00
19.76
A


ATOM
2672
CD1
LEU
A
352
34.098
58.301
87.018
1.00
21.28
A


ATOM
2673
CD2
LEU
A
352
35.053
56.988
85.112
1.00
21.19
A


ATOM
2674
C
LEU
A
352
38.969
58.725
86.097
1.00
19.07
A


ATOM
2675
O
LEU
A
352
39.462
58.779
84.968
1.00
17.65
A


ATOM
2676
N
GLU
A
353
39.322
59.540
87.086
1.00
19.59
A


ATOM
2677
CA
GLU
A
353
40.320
60.594
86.921
1.00
20.60
A


ATOM
2678
CB
GLU
A
353
40.422
61.400
88.218
1.00
23.38
A


ATOM
2679
CG
GLU
A
353
41.485
62.485
88.211
1.00
27.60
A


ATOM
2680
CD
GLU
A
353
41.544
63.238
89.530
1.00
29.84
A


ATOM
2681
OE1
GLU
A
353
41.839
62.606
90.570
1.00
31.36
A


ATOM
2682
OE2
GLU
A
353
41.290
64.460
89.525
1.00
32.62
A


ATOM
2683
C
GLU
A
353
41.700
60.070
86.532
1.00
20.58
A


ATOM
2684
O
GLU
A
353
42.410
60.696
85.739
1.00
18.53
A


ATOM
2685
N
GLU
A
354
42.075
58.919
87.089
1.00
19.90
A


ATOM
2686
CA
GLU
A
354
43.379
58.318
86.823
1.00
20.37
A


ATOM
2687
CB
GLU
A
354
43.824
57.507
88.052
1.00
24.66
A


ATOM
2688
CG
GLU
A
354
43.839
58.333
89.339
1.00
27.87
A


ATOM
2689
CD
GLU
A
354
43.942
57.486
90.598
1.00
31.64
A


ATOM
2690
OE1
GLU
A
354
43.427
56.346
90.602
1.00
31.88
A


ATOM
2691
OE2
GLU
A
354
44.518
57.972
91.595
1.00
32.79
A


ATOM
2692
C
GLU
A
354
43.396
57.437
85.574
1.00
21.48
A


ATOM
2693
O
GLU
A
354
44.415
56.819
85.253
1.00
19.63
A


ATOM
2694
N
GLY
A
355
42.268
57.390
84.872
1.00
19.45
A


ATOM
2695
CA
GLY
A
355
42.166
56.588
83.664
1.00
21.36
A


ATOM
2696
C
GLY
A
355
42.349
55.093
83.868
1.00
21.53
A


ATOM
2697
O
GLY
A
355
42.909
54.419
83.010
1.00
21.87
A


ATOM
2698
N
LEU
A
356
41.869
54.569
84.992
1.00
20.13
A


ATOM
2699
CA
LEU
A
356
42.001
53.141
85.289
1.00
20.12
A


ATOM
2700
CB
LEU
A
356
41.774
52.898
86.783
1.00
20.13
A


ATOM
2701
CG
LEU
A
356
42.667
53.735
87.711
1.00
19.29
A


ATOM
2702
CD1
LEU
A
356
42.382
53.378
89.163
1.00
19.65
A


ATOM
2703
CD2
LEU
A
356
44.129
53.492
87.381
1.00
19.63
A


ATOM
2704
C
LEU
A
356
41.042
52.287
84.460
1.00
20.67
A


ATOM
2705
O
LEU
A
356
40.156
52.817
83.785
1.00
18.66
A


ATOM
2706
N
LYS
A
357
41.218
50.966
84.523
1.00
19.35
A


ATOM
2707
CA
LYS
A
357
40.398
50.030
83.754
1.00
19.96
A


ATOM
2708
CB
LYS
A
357
41.085
48.663
83.692
1.00
23.34
A


ATOM
2709
CG
LYS
A
357
42.598
48.754
83.565
1.00
30.70
A


ATOM
2710
CD
LYS
A
357
43.246
47.382
83.544
1.00
33.70
A


ATOM
2711
CE
LYS
A
357
42.888
46.623
82.278
1.00
36.65
A


ATOM
2712
NZ
LYS
A
357
43.583
45.304
82.212
1.00
38.22
A


ATOM
2713
C
LYS
A
357
38.979
49.843
84.276
1.00
18.13
A


ATOM
2714
O
LYS
A
357
38.084
49.476
83.517
1.00
18.43
A


ATOM
2715
N
THR
A
358
38.771
50.068
85.569
1.00
15.16
A


ATOM
2716
CA
THR
A
358
37.442
49.918
86.150
1.00
14.31
A


ATOM
2717
CB
THR
A
358
37.243
48.550
86.838
1.00
14.13
A


ATOM
2718
OG1
THR
A
358
37.870
48.575
88.131
1.00
15.36
A


ATOM
2719
CG2
THR
A
358
37.830
47.424
85.995
1.00
14.35
A


ATOM
2720
C
THR
A
358
37.218
50.970
87.218
1.00
14.15
A


ATOM
2721
O
THR
A
358
38.165
51.593
87.689
1.00
15.99
A


ATOM
2722
N
THR
A
359
35.963
51.132
87.620
1.00
13.93
A


ATOM
2723
CA
THR
A
359
35.594
52.101
88.645
1.00
14.78
A


ATOM
2724
CB
THR
A
359
34.074
52.257
88.732
1.00
17.18
A


ATOM
2725
OG1
THR
A
359
33.472
50.957
88.692
1.00
16.70
A


ATOM
2726
CG2
THR
A
359
33.544
53.102
87.570
1.00
18.46
A


ATOM
2727
C
THR
A
359
36.095
51.664
90.015
1.00
14.99
A


ATOM
2728
O
THR
A
359
36.123
52.459
90.949
1.00
14.02
A


ATOM
2729
N
GLY
A
360
36.478
50.395
90.128
1.00
13.30
A


ATOM
2730
CA
GLY
A
360
36.970
49.879
91.392
1.00
14.14
A


ATOM
2731
C
GLY
A
360
38.486
49.805
91.423
1.00
14.17
A


ATOM
2732
O
GLY
A
360
39.066
48.736
91.628
1.00
13.42
A


ATOM
2733
N
GLU
A
361
39.131
50.947
91.214
1.00
14.93
A


ATOM
2734
CA
GLU
A
361
40.590
51.025
91.214
1.00
16.26
A


ATOM
2735
CB
GLU
A
361
41.131
50.779
92.633
1.00
16.95
A


ATOM
2736
CG
GLU
A
361
40.426
51.624
93.709
1.00
21.62
A


ATOM
2737
CD
GLU
A
361
41.057
51.514
95.098
1.00
23.55
A


ATOM
2738
OE1
GLU
A
361
41.466
50.403
95.497
1.00
24.80
A


ATOM
2739
OE2
GLU
A
361
41.124
52.544
95.804
1.00
24.47
A


ATOM
2740
C
GLU
A
361
41.229
50.052
90.210
1.00
15.01
A


ATOM
2741
O
GLU
A
361
42.313
49.512
90.437
1.00
14.46
A


ATOM
2742
N
GLY
A
362
40.550
49.841
89.089
1.00
13.08
A


ATOM
2743
CA
GLY
A
362
41.071
48.955
88.066
1.00
16.80
A


ATOM
2744
C
GLY
A
362
40.894
47.472
88.342
1.00
17.02
A


ATOM
2745
O
GLY
A
362
41.318
46.641
87.539
1.00
18.60
A


ATOM
2746
N
LEU
A
363
40.281
47.134
89.473
1.00
17.18
A


ATOM
2747
CA
LEU
A
363
40.051
45.740
89.827
1.00
18.00
A


ATOM
2748
CB
LEU
A
363
40.383
45.514
91.307
1.00
19.02
A


ATOM
2749
CG
LEU
A
363
41.826
45.853
91.697
1.00
19.57
A


ATOM
2750
CD1
LEU
A
363
42.048
45.584
93.180
1.00
20.85
A


ATOM
2751
CD2
LEU
A
363
42.781
45.022
90.863
1.00
22.14
A


ATOM
2752
C
LEU
A
363
38.590
45.367
89.541
1.00
17.57
A


ATOM
2753
O
LEU
A
363
37.718
46.238
89.508
1.00
17.19
A


ATOM
2754
N
ASP
A
364
38.323
44.079
89.332
1.00
17.36
A


ATOM
2755
CA
ASP
A
364
36.961
43.629
89.030
1.00
17.54
A


ATOM
2756
CB
ASP
A
364
36.985
42.329
88.214
1.00
21.31
A


ATOM
2757
CG
ASP
A
364
37.599
42.504
86.835
1.00
24.11
A


ATOM
2758
OD1
ASP
A
364
37.602
43.638
86.305
1.00
23.48
A


ATOM
2759
OD2
ASP
A
364
38.064
41.487
86.272
1.00
25.37
A


ATOM
2760
C
ASP
A
364
36.027
43.418
90.226
1.00
17.38
A


ATOM
2761
O
ASP
A
364
34.835
43.728
90.143
1.00
15.70
A


ATOM
2762
N
TRP
A
365
36.542
42.870
91.324
1.00
14.37
A


ATOM
2763
CA
TRP
A
365
35.699
42.634
92.491
1.00
16.23
A


ATOM
2764
CB
TRP
A
365
35.699
41.148
92.877
1.00
19.04
A


ATOM
2765
CG
TRP
A
365
35.319
40.238
91.760
1.00
22.12
A


ATOM
2766
CD2
TRP
A
365
34.027
39.675
91.515
1.00
23.55
A


ATOM
2767
CE2
TRP
A
365
34.123
38.908
90.331
1.00
25.41
A


ATOM
2768
CE3
TRP
A
365
32.795
39.745
92.179
1.00
22.91
A


ATOM
2769
CD1
TRP
A
365
36.126
39.803
90.750
1.00
23.60
A


ATOM
2770
NE1
TRP
A
365
35.415
39.003
89.886
1.00
24.40
A


ATOM
2771
CZ2
TRP
A
365
33.031
38.214
89.794
1.00
25.90
A


ATOM
2772
CZ3
TRP
A
365
31.707
39.054
91.645
1.00
25.49
A


ATOM
2773
CH2
TRP
A
365
31.835
38.299
90.464
1.00
28.06
A


ATOM
2774
C
TRP
A
365
36.131
43.449
93.704
1.00
13.48
A


ATOM
2775
O
TRP
A
365
37.304
43.791
93.849
1.00
16.37
A


ATOM
2776
N
GLY
A
366
35.170
43.735
94.575
1.00
14.49
A


ATOM
2777
CA
GLY
A
366
35.452
44.497
95.774
1.00
15.11
A


ATOM
2778
C
GLY
A
366
34.515
44.126
96.907
1.00
14.59
A


ATOM
2779
O
GLY
A
366
33.565
43.361
96.732
1.00
16.03
A


ATOM
2780
N
VAL
A
367
34.791
44.674
98.082
1.00
14.23
A


ATOM
2781
CA
VAL
A
367
33.981
44.422
99.258
1.00
12.28
A


ATOM
2782
CB
VAL
A
367
34.721
43.482
100.248
1.00
12.07
A


ATOM
2783
CG1
VAL
A
367
35.988
44.156
100.753
1.00
13.16
A


ATOM
2784
CG2
VAL
A
367
33.820
43.111
101.406
1.00
10.94
A


ATOM
2785
C
VAL
A
367
33.705
45.749
99.957
1.00
11.97
A


ATOM
2786
O
VAL
A
367
34.550
46.650
99.961
1.00
13.50
A


ATOM
2787
N
LEU
A
368
32.510
45.864
100.521
1.00
13.10
A


ATOM
2788
CA
LEU
A
368
32.103
47.049
101.273
1.00
14.05
A


ATOM
2789
CB
LEU
A
368
30.920
47.755
100.581
1.00
13.70
A


ATOM
2790
CG
LEU
A
368
30.298
48.978
101.269
1.00
12.89
A


ATOM
2791
CD1
LEU
A
368
29.573
49.875
100.259
1.00
13.87
A


ATOM
2792
CD2
LEU
A
368
29.340
48.498
102.343
1.00
16.70
A


ATOM
2793
C
LEU
A
368
31.710
46.526
102.652
1.00
14.47
A


ATOM
2794
O
LEU
A
368
30.937
45.564
102.760
1.00
15.42
A


ATOM
2795
N
PHE
A
369
32.271
47.136
103.697
1.00
15.36
A


ATOM
2796
CA
PHE
A
369
32.017
46.735
105.081
1.00
15.36
A


ATOM
2797
CB
PHE
A
369
33.328
46.375
105.795
1.00
17.30
A


ATOM
2798
CG
PHE
A
369
33.837
44.996
105.504
1.00
16.57
A


ATOM
2799
CD1
PHE
A
369
33.112
43.875
105.897
1.00
17.75
A


ATOM
2800
CD2
PHE
A
369
35.048
44.817
104.849
1.00
15.72
A


ATOM
2801
CE1
PHE
A
369
33.593
42.587
105.637
1.00
18.32
A


ATOM
2802
CE2
PHE
A
369
35.540
43.533
104.581
1.00
18.65
A


ATOM
2803
CZ
PHE
A
369
34.807
42.415
104.978
1.00
17.23
A


ATOM
2804
C
PHE
A
369
31.337
47.787
105.946
1.00
17.12
A


ATOM
2805
O
PHE
A
369
31.725
48.964
105.952
1.00
15.30
A


ATOM
2806
N
GLY
A
370
30.329
47.345
106.688
1.00
16.03
A


ATOM
2807
CA
GLY
A
370
29.650
48.217
107.623
1.00
15.32
A


ATOM
2808
C
GLY
A
370
29.907
47.618
109.002
1.00
15.98
A


ATOM
2809
O
GLY
A
370
29.788
46.397
109.160
1.00
15.42
A


ATOM
2810
N
PHE
A
371
30.267
48.446
109.986
1.00
15.18
A


ATOM
2811
CA
PHE
A
371
30.519
47.969
111.356
1.00
16.88
A


ATOM
2812
CB
PHE
A
371
31.994
48.167
111.748
1.00
16.02
A


ATOM
2813
CG
PHE
A
371
32.980
47.576
110.776
1.00
18.36
A


ATOM
2814
CD1
PHE
A
371
33.002
46.202
110.522
1.00
19.96
A


ATOM
2815
CD2
PHE
A
371
33.899
48.393
110.122
1.00
19.62
A


ATOM
2816
CE1
PHE
A
371
33.925
45.655
109.631
1.00
20.17
A


ATOM
2817
CE2
PHE
A
371
34.827
47.859
109.229
1.00
20.30
A


ATOM
2818
CZ
PHE
A
371
34.842
46.484
108.982
1.00
21.44
A


ATOM
2819
C
PHE
A
371
29.643
48.749
112.345
1.00
17.73
A


ATOM
2820
O
PHE
A
371
29.607
49.986
112.311
1.00
20.57
A


ATOM
2821
N
GLY
A
372
28.959
48.037
113.235
1.00
17.64
A


ATOM
2822
CA
GLY
A
372
28.095
48.706
114.193
1.00
18.38
A


ATOM
2823
C
GLY
A
372
27.792
47.924
115.461
1.00
18.00
A


ATOM
2824
O
GLY
A
372
28.347
46.860
115.687
1.00
16.36
A


ATOM
2825
N
PRO
A
373
26.887
48.432
116.305
1.00
20.27
A


ATOM
2826
CD
PRO
A
373
26.146
49.670
116.005
1.00
21.14
A


ATOM
2827
CA
PRO
A
373
26.444
47.861
117.588
1.00
22.67
A


ATOM
2828
CB
PRO
A
373
25.456
48.913
118.104
1.00
24.87
A


ATOM
2829
CG
PRO
A
373
25.821
50.173
117.373
1.00
23.22
A


ATOM
2830
C
PRO
A
373
25.753
46.484
117.592
1.00
23.21
A


ATOM
2831
O
PRO
A
373
25.010
46.202
116.641
1.00
22.66
A


ATOM
2832
N
GLY
A
374
26.016
45.617
118.597
1.00
23.17
A


ATOM
2833
CA
GLY
A
374
25.178
44.436
118.666
1.00
25.29
A


ATOM
2834
C
GLY
A
374
26.141
43.404
119.175
1.00
23.83
A


ATOM
2835
O
GLY
A
374
25.862
42.558
120.092
1.00
25.91
A


ATOM
2836
N
LEU
A
375
27.563
43.367
118.304
1.00
24.44
A


ATOM
2837
CA
LEU
A
375
28.323
43.906
117.199
1.00
23.26
A


ATOM
2838
CB
LEU
A
375
29.771
44.208
117.541
1.00
23.81
A


ATOM
2839
CG
LEU
A
375
30.492
44.899
116.384
1.00
25.97
A


ATOM
2840
CD1
LEU
A
375
31.706
45.711
116.830
1.00
27.70
A


ATOM
2841
CD2
LEU
A
375
31.005
43.917
115.329
1.00
25.62
A


ATOM
2842
C
LEU
A
375
28.226
43.150
115.907
1.00
21.89
A


ATOM
2843
O
LEU
A
375
28.728
42.015
115.805
1.00
23.04
A


ATOM
2844
N
THR
A
376
27.598
43.904
115.007
1.00
22.34
A


ATOM
2845
CA
THR
A
376
27.220
43.607
113.645
1.00
19.04
A


ATOM
2846
CB
THR
A
376
25.952
44.396
113.271
1.00
19.55
A


ATOM
2847
OG1
THR
A
376
24.994
44.305
114.330
1.00
18.35
A


ATOM
2848
CG2
THR
A
376
25.352
43.860
111.974
1.00
19.52
A


ATOM
2849
C
THR
A
376
28.241
44.005
112.607
1.00
18.79
A


ATOM
2850
O
THR
A
376
28.837
45.093
112.662
1.00
17.92
A


ATOM
2851
N
ILE
A
377
28.406
43.115
111.641
1.00
17.26
A


ATOM
2852
CA
ILE
A
377
29.277
43.347
110.513
1.00
17.21
A


ATOM
2853
CB
ILE
A
377
30.458
42.354
110.473
1.00
16.53
A


ATOM
2854
CG2
ILE
A
377
31.241
42.543
109.184
1.00
16.65
A


ATOM
2855
CG1
ILE
A
377
31.367
42.561
111.686
1.00
18.63
A


ATOM
2856
CD1
ILE
A
377
32.527
41.576
111.751
1.00
21.55
A


ATOM
2857
C
ILE
A
377
28.400
43.096
109.290
1.00
17.23
A


ATOM
2858
O
ILE
A
377
27.761
42.050
109.189
1.00
17.27
A


ATOM
2859
N
GLU
A
378
28.337
44.072
108.393
1.00
15.61
A


ATOM
2860
CA
GLU
A
378
27.576
43.934
107.155
1.00
16.65
A


ATOM
2861
CB
GLU
A
378
26.732
45.188
106.873
1.00
16.43
A


ATOM
2862
CG
GLU
A
378
25.547
45.389
107.813
1.00
20.23
A


ATOM
2863
CD
GLU
A
378
24.203
44.968
107.214
1.00
21.67
A


ATOM
2864
OE1
GLU
A
378
24.176
44.331
106.137
1.00
21.94
A


ATOM
2865
OE2
GLU
A
378
23.163
45.277
107.834
1.00
23.26
A


ATOM
2866
C
GLU
A
378
28.641
43.785
106.078
1.00
15.61
A


ATOM
2867
O
GLU
A
378
29.575
44.595
106.009
1.00
16.34
A


ATOM
2868
N
THR
A
379
28.523
42.743
105.259
1.00
16.22
A


ATOM
2869
CA
THR
A
379
29.494
42.504
104.194
1.00
15.92
A


ATOM
2870
CB
THR
A
379
30.224
41.159
104.378
1.00
18.24
A


ATOM
2871
OG1
THR
A
379
30.715
41.052
105.720
1.00
18.54
A


ATOM
2872
CG2
THR
A
379
31.390
41.063
103.404
1.00
17.22
A


ATOM
2873
C
THR
A
379
28.817
42.460
102.832
1.00
16.86
A


ATOM
2874
O
THR
A
379
28.045
41.533
102.540
1.00
16.09
A


ATOM
2875
N
VAL
A
380
29.112
43.450
101.997
1.00
12.76
A


ATOM
2876
CA
VAL
A
380
28.534
43.513
100.655
1.00
13.53
A


ATOM
2877
CB
VAL
A
380
27.864
44.885
100.401
1.00
13.13
A


ATOM
2878
CG1
VAL
A
380
27.209
44.906
99.009
1.00
14.37
A


ATOM
2879
CG2
VAL
A
380
26.844
45.171
101.483
1.00
14.22
A


ATOM
2880
C
VAL
A
380
29.620
43.299
99.597
1.00
14.42
A


ATOM
2881
O
VAL
A
380
30.661
43.958
99.619
1.00
13.41
A


ATOM
2882
N
VAL
A
381
29.397
42.362
98.679
1.00
14.62
A


ATOM
2883
CA
VAL
A
381
30.374
42.131
97.618
1.00
12.94
A


ATOM
2884
CB
VAL
A
381
30.424
40.663
97.169
1.00
13.15
A


ATOM
2885
CG1
VAL
A
381
31.315
40.537
95.932
1.00
11.65
A


ATOM
2886
CG2
VAL
A
381
30.962
39.795
98.298
1.00
12.83
A


ATOM
2887
C
VAL
A
381
29.962
42.987
96.439
1.00
15.10
A


ATOM
2888
O
VAL
A
381
28.787
43.033
96.082
1.00
15.48
A


ATOM
2889
N
LEU
A
382
30.935
43.665
95.841
1.00
15.57
A


ATOM
2890
CA
LEU
A
382
30.678
44.540
94.707
1.00
15.16
A


ATOM
2891
CB
LEU
A
382
31.110
45.971
95.047
1.00
14.71
A


ATOM
2892
CG
LEU
A
382
30.478
46.644
96.269
1.00
15.25
A


ATOM
2893
CD1
LEU
A
382
31.191
47.967
96.546
1.00
16.34
A


ATOM
2894
CD2
LEU
A
382
28.999
46.872
96.024
1.00
16.09
A


ATOM
2895
C
LEU
A
382
31.417
44.114
93.445
1.00
16.18
A


ATOM
2896
O
LEU
A
382
32.433
43.423
93.485
1.00
15.42
A


ATOM
2897
N
ARG
A
383
30.893
44.561
92.313
1.00
16.91
A


ATOM
2898
CA
ARG
A
383
31.504
44.283
91.039
1.00
18.58
A


ATOM
2899
CB
ARG
A
383
30.560
43.438
90.187
1.00
23.70
A


ATOM
2900
CG
ARG
A
383
31.212
42.230
89.552
1.00
29.01
A


ATOM
2901
CD
ARG
A
383
32.112
42.639
88.406
1.00
34.91
A


ATOM
2902
NE
ARG
A
383
32.578
41.484
87.646
1.00
38.99
A


ATOM
2903
CZ
ARG
A
383
33.297
41.570
86.532
1.00
41.42
A


ATOM
2904
NH1
ARG
A
383
33.631
42.760
86.047
1.00
42.61
A


ATOM
2905
NH2
ARG
A
383
33.688
40.468
85.906
1.00
42.22
A


ATOM
2906
C
ARG
A
383
31.709
45.663
90.425
1.00
18.51
A


ATOM
2907
O
ARG
A
383
30.798
46.493
90.441
1.00
18.35
A


ATOM
2908
N
SER
A
384
32.908
45.918
89.916
1.00
17.71
A


ATOM
2909
CA
SER
A
384
33.221
47.205
89.305
1.00
17.18
A


ATOM
2910
CB
SER
A
384
34.737
47.429
89.301
1.00
16.78
A


ATOM
2911
OG
SER
A
384
35.377
46.504
88.434
1.00
19.20
A


ATOM
2912
C
SER
A
384
32.704
47.244
87.873
1.00
16.69
A


ATOM
2913
O
SER
A
384
32.259
46.231
87.333
1.00
14.89
A


ATOM
2914
N
VAL
A
385
32.763
48.422
87.266
1.00
16.95
A


ATOM
2915
CA
VAL
A
385
32.318
48.602
85.892
1.00
18.01
A


ATOM
2916
CB
VAL
A
385
31.210
49.679
85.807
1.00
19.03
A


ATOM
2917
CG1
VAL
A
385
30.892
49.986
84.356
1.00
19.61
A


ATOM
2918
CG2
VAL
A
385
29.968
49.200
86.538
1.00
19.12
A


ATOM
2919
C
VAL
A
385
33.503
49.047
85.034
1.00
19.45
A


ATOM
2920
O
VAL
A
385
34.277
49.916
85.437
1.00
18.07
A


ATOM
2921
N
ALA
A
386
33.637
48.448
83.853
1.00
18.41
A


ATOM
2922
CA
ALA
A
386
34.719
48.783
82.937
1.00
19.71
A


ATOM
2923
CB
ALA
A
386
34.692
47.833
81.736
1.00
21.24
A


ATOM
2924
C
ALA
A
386
34.633
50.237
82.459
1.00
20.60
A


ATOM
2925
O
ALA
A
386
33.573
50.698
82.038
1.00
19.64
A


ATOM
2926
N
ILE
A
387
35.757
50.949
82.530
1.00
20.08
A


ATOM
2927
CA
ILE
A
387
35.832
52.344
82.093
1.00
21.90
A


ATOM
2928
CB
ILE
A
387
35.864
53.324
83.293
1.00
20.45
A


ATOM
2929
CG2
ILE
A
387
34.507
53.353
83.977
1.00
20.07
A


ATOM
2930
CG1
ILE
A
387
36.969
52.923
84.274
1.00
20.21
A


ATOM
2931
CD1
ILE
A
387
37.124
53.867
85.451
1.00
17.62
A


ATOM
2932
C
ILE
A
387
37.076
52.591
81.233
1.00
23.48
A


ATOM
2933
O
ILE
A
387
37.190
53.699
80.664
1.00
24.34
A


ATOM
2934
OXT
ILE
A
387
37.929
51.679
81.143
1.00
24.25
A

























APPENDIX C







18× CHS Mutant


ATOM
#
TYPE
RES
X
Y
Z
OCC
B





















ATOM
1
CB
VAL
A
2
−13.230
29.022
69.882
1.00
30.61
A


ATOM
2
CG1
VAL
A
2
−12.890
29.579
71.256
1.00
31.32
A


ATOM
3
CG2
VAL
A
2
−13.703
27.583
69.999
1.00
31.29
A


ATOM
4
C
VAL
A
2
−14.560
29.365
67.801
1.00
29.09
A


ATOM
5
O
VAL
A
2
−15.501
28.610
67.557
1.00
29.96
A


ATOM
6
N
VAL
A
2
−15.591
29.845
70.002
1.00
30.39
A


ATOM
7
CA
VAL
A
2
−14.326
29.883
69.216
1.00
29.93
A


ATOM
8
N
SER
A
3
−13.700
29.774
66.873
1.00
27.49
A


ATOM
9
CA
SER
A
3
−13.814
29.352
65.482
1.00
25.81
A


ATOM
10
CB
SER
A
3
−13.481
30.514
64.548
1.00
25.39
A


ATOM
11
OG
SER
A
3
−12.104
30.840
64.623
1.00
24.75
A


ATOM
12
C
SER
A
3
−12.866
28.195
65.190
1.00
25.08
A


ATOM
13
O
SER
A
3
−11.910
27.961
65.931
1.00
24.70
A


ATOM
14
N
VAL
A
4
−13.134
27.478
64.102
1.00
24.03
A


ATOM
15
CA
VAL
A
4
−12.298
26.352
63.704
1.00
23.31
A


ATOM
16
CB
VAL
A
4
−12.904
25.609
62.491
1.00
23.50
A


ATOM
17
CG1
VAL
A
4
−11.986
24.474
62.058
1.00
23.11
A


ATOM
18
CG2
VAL
A
4
−14.275
25.069
62.848
1.00
23.81
A


ATOM
19
C
VAL
A
4
−10.895
26.833
63.338
1.00
22.89
A


ATOM
20
O
VAL
A
4
−9.910
26.129
63.557
1.00
22.82
A


ATOM
21
N
SER
A
5
−10.813
28.037
62.778
1.00
22.60
A


ATOM
22
CA
SER
A
5
−9.529
28.613
62.383
1.00
22.06
A


ATOM
23
CB
SER
A
5
−9.742
29.969
61.704
1.00
21.99
A


ATOM
24
OG
SER
A
5
−8.505
30.545
61.320
1.00
22.10
A


ATOM
25
C
SER
A
5
−8.610
28.788
63.587
1.00
21.94
A


ATOM
26
O
SER
A
5
−7.435
28.423
63.542
1.00
22.12
A


ATOM
27
N
GLU
A
6
−9.151
29.345
64.665
1.00
21.69
A


ATOM
28
CA
GLU
A
6
−8.372
29.572
65.875
1.00
21.71
A


ATOM
29
CB
GLU
A
6
−9.195
30.387
66.879
1.00
23.91
A


ATOM
30
CG
GLU
A
6
−8.390
30.969
68.040
1.00
28.22
A


ATOM
31
CD
GLU
A
6
−7.384
32.032
67.608
1.00
30.05
A


ATOM
32
OE1
GLU
A
6
−6.670
32.566
68.486
1.00
31.96
A


ATOM
33
OE2
GLU
A
6
−7.302
32.340
66.399
1.00
32.23
A


ATOM
34
C
GLU
A
6
−7.945
28.234
66.488
1.00
20.55
A


ATOM
35
O
GLU
A
6
−6.842
28.109
67.019
1.00
19.81
A


ATOM
36
N
ILE
A
7
−8.820
27.235
66.402
1.00
18.95
A


ATOM
37
CA
ILE
A
7
−8.522
25.909
66.937
1.00
17.56
A


ATOM
38
CB
ILE
A
7
−9.766
24.987
66.864
1.00
17.72
A


ATOM
39
CG2
ILE
A
7
−9.396
23.560
67.269
1.00
17.42
A


ATOM
40
CG1
ILE
A
7
−10.863
25.532
67.784
1.00
17.63
A


ATOM
41
CD1
ILE
A
7
−12.178
24.790
67.693
1.00
17.98
A


ATOM
42
C
ILE
A
7
−7.367
25.263
66.169
1.00
16.69
A


ATOM
43
O
ILE
A
7
−6.415
24.767
66.773
1.00
16.31
A


ATOM
44
N
ARG
A
8
−7.450
25.283
64.839
1.00
15.59
A


ATOM
45
CA
ARG
A
8
−6.411
24.697
63.984
1.00
15.15
A


ATOM
46
CB
ARG
A
8
−6.803
24.836
62.506
1.00
14.73
A


ATOM
47
CG
ARG
A
8
−5.829
24.202
61.507
1.00
13.64
A


ATOM
48
CD
ARG
A
8
−6.090
22.708
61.297
1.00
13.58
A


ATOM
49
NE
ARG
A
8
−5.526
21.844
62.336
1.00
12.35
A


ATOM
50
CZ
ARG
A
8
−4.284
21.358
62.326
1.00
13.34
A


ATOM
51
NH1
ARG
A
8
−3.453
21.644
61.327
1.00
12.64
A


ATOM
52
NH2
ARG
A
8
−3.870
20.578
63.319
1.00
12.49
A


ATOM
53
C
ARG
A
8
−5.048
25.359
64.211
1.00
15.17
A


ATOM
54
O
ARG
A
8
−4.027
24.678
64.286
1.00
14.78
A


ATOM
55
N
LYS
A
9
−5.034
26.687
64.320
1.00
15.05
A


ATOM
56
CA
LYS
A
9
−3.781
27.418
64.528
1.00
15.25
A


ATOM
57
CB
LYS
A
9
−4.039
28.932
64.545
1.00
14.94
A


ATOM
58
CG
LYS
A
9
−4.332
29.532
63.178
1.00
15.21
A


ATOM
59
CD
LYS
A
9
−4.522
31.041
63.280
1.00
16.42
A


ATOM
60
CE
LYS
A
9
−4.697
31.688
61.910
1.00
16.68
A


ATOM
61
NZ
LYS
A
9
−4.801
33.172
62.035
1.00
17.12
A


ATOM
62
C
LYS
A
9
−3.037
27.028
65.799
1.00
15.06
A


ATOM
63
O
LYS
A
9
−1.804
27.007
65.822
1.00
15.26
A


ATOM
64
N
ALA
A
10
−3.789
26.718
66.852
1.00
15.12
A


ATOM
65
CA
ALA
A
10
−3.206
26.349
68.141
1.00
14.75
A


ATOM
66
CB
ALA
A
10
−4.121
26.830
69.267
1.00
15.94
A


ATOM
67
C
ALA
A
10
−2.979
24.848
68.268
1.00
14.60
A


ATOM
68
O
ALA
A
10
−2.392
24.380
69.248
1.00
14.85
A


ATOM
69
N
GLN
A
11
−3.426
24.099
67.267
1.00
13.64
A


ATOM
70
CA
GLN
A
11
−3.308
22.644
67.278
1.00
13.50
A


ATOM
71
CB
GLN
A
11
−4.549
22.038
66.608
1.00
12.91
A


ATOM
72
CG
GLN
A
11
−4.852
20.588
66.973
1.00
13.41
A


ATOM
73
CD
GLN
A
11
−6.114
20.076
66.292
1.00
13.72
A


ATOM
74
OE1
GLN
A
11
−6.101
19.746
65.106
1.00
14.06
A


ATOM
75
NE2
GLN
A
11
−7.214
20.031
67.036
1.00
11.82
A


ATOM
76
C
GLN
A
11
−2.048
22.072
66.611
1.00
13.38
A


ATOM
77
O
GLN
A
11
−1.550
21.025
67.032
1.00
13.66
A


ATOM
78
N
ARG
A
12
−1.531
22.752
65.589
1.00
13.00
A


ATOM
79
CA
ARG
A
12
−0.364
22.256
64.850
1.00
12.85
A


ATOM
80
CB
ARG
A
12
−0.338
22.881
63.442
1.00
12.22
A


ATOM
81
CG
ARG
A
12
−0.209
24.409
63.409
1.00
12.52
A


ATOM
82
CD
ARG
A
12
0.264
24.892
62.036
1.00
13.75
A


ATOM
83
NE
ARG
A
12
−0.672
24.561
60.957
1.00
14.03
A


ATOM
84
CZ
ARG
A
12
−1.757
25.271
60.657
1.00
14.40
A


ATOM
85
NH1
ARG
A
12
−2.052
26.364
61.353
1.00
14.54
A


ATOM
86
NH2
ARG
A
12
−2.549
24.892
59.659
1.00
13.01
A


ATOM
87
C
ARG
A
12
1.022
22.425
65.489
1.00
13.09
A


ATOM
88
O
ARG
A
12
1.246
23.329
66.296
1.00
13.33
A


ATOM
89
N
ALA
A
13
1.950
21.541
65.116
1.00
13.02
A


ATOM
90
CA
ALA
A
13
3.333
21.606
65.607
1.00
13.42
A


ATOM
91
CB
ALA
A
13
3.973
20.214
65.580
1.00
13.07
A


ATOM
92
C
ALA
A
13
4.078
22.552
64.657
1.00
14.07
A


ATOM
93
O
ALA
A
13
3.503
22.988
63.662
1.00
13.68
A


ATOM
94
N
GLU
A
14
5.342
22.870
64.938
1.00
15.31
A


ATOM
95
CA
GLU
A
14
6.072
23.788
64.055
1.00
16.79
A


ATOM
96
CB
GLU
A
14
6.634
24.983
64.844
1.00
19.19
A


ATOM
97
CG
GLU
A
14
7.664
25.800
64.043
1.00
22.25
A


ATOM
98
CD
GLU
A
14
7.866
27.218
64.565
1.00
24.73
A


ATOM
99
OE1
GLU
A
14
8.977
27.766
64.379
1.00
26.12
A


ATOM
100
OE2
GLU
A
14
6.916
27.794
65.144
1.00
25.41
A


ATOM
101
C
GLU
A
14
7.190
23.226
63.180
1.00
16.32
A


ATOM
102
O
GLU
A
14
7.170
23.420
61.964
1.00
16.46
A


ATOM
103
N
GLY
A
15
8.162
22.548
63.787
1.00
15.23
A


ATOM
104
CA
GLY
A
15
9.282
22.024
63.019
1.00
14.11
A


ATOM
105
C
GLY
A
15
9.151
20.637
62.408
1.00
13.41
A


ATOM
106
O
GLY
A
15
8.109
19.999
62.521
1.00
12.54
A


ATOM
107
N
PRO
A
16
10.216
20.142
61.755
1.00
12.96
A


ATOM
108
CD
PRO
A
16
11.490
20.849
61.524
1.00
13.60
A


ATOM
109
CA
PRO
A
16
10.229
18.821
61.116
1.00
13.35
A


ATOM
110
CB
PRO
A
16
11.467
18.892
60.224
1.00
13.76
A


ATOM
111
CG
PRO
A
16
12.407
19.735
61.052
1.00
14.19
A


ATOM
112
C
PRO
A
16
10.298
17.666
62.115
1.00
13.11
A


ATOM
113
O
PRO
A
16
10.893
17.800
63.188
1.00
13.04
A


ATOM
114
N
ALA
A
17
9.685
16.540
61.759
1.00
11.96
A


ATOM
115
CA
ALA
A
17
9.686
15.355
62.614
1.00
12.09
A


ATOM
116
CB
ALA
A
17
8.824
14.262
61.993
1.00
11.81
A


ATOM
117
C
ALA
A
17
11.119
14.862
62.794
1.00
11.94
A


ATOM
118
O
ALA
A
17
11.883
14.766
61.826
1.00
11.18
A


ATOM
119
N
THR
A
18
11.480
14.543
64.035
1.00
11.49
A


ATOM
120
CA
THR
A
18
12.834
14.098
64.338
1.00
11.65
A


ATOM
121
CB
THR
A
18
13.589
15.190
65.134
1.00
13.41
A


ATOM
122
OG1
THR
A
18
13.434
16.457
64.478
1.00
13.74
A


ATOM
123
CG2
THR
A
18
15.072
14.866
65.228
1.00
14.06
A


ATOM
124
C
THR
A
18
12.850
12.803
65.156
1.00
11.14
A


ATOM
125
O
THR
A
18
12.000
12.597
66.023
1.00
11.01
A


ATOM
126
N
ILE
A
19
13.810
11.931
64.860
1.00
10.75
A


ATOM
127
CA
ILE
A
19
13.967
10.680
65.594
1.00
10.47
A


ATOM
128
CB
ILE
A
19
14.722
9.634
64.757
1.00
10.60
A


ATOM
129
CG2
ILE
A
19
14.941
8.371
65.587
1.00
9.37
A


ATOM
130
CG1
ILE
A
19
13.924
9.327
63.483
1.00
10.89
A


ATOM
131
CD1
ILE
A
19
14.571
8.260
62.584
1.00
12.28
A


ATOM
132
C
ILE
A
19
14.776
11.034
66.841
1.00
10.68
A


ATOM
133
O
ILE
A
19
15.866
11.560
66.735
1.00
11.42
A


ATOM
134
N
LEU
A
20
14.218
10.745
68.014
1.00
10.93
A


ATOM
135
CA
LEU
A
20
14.850
11.093
69.287
1.00
11.54
A


ATOM
136
CB
LEU
A
20
13.823
11.805
70.177
1.00
12.05
A


ATOM
137
CG
LEU
A
20
13.140
13.028
69.555
1.00
12.25
A


ATOM
138
CD1
LEU
A
20
11.991
13.478
70.431
1.00
12.71
A


ATOM
139
CD2
LEU
A
20
14.156
14.157
69.371
1.00
13.13
A


ATOM
140
C
LEU
A
20
15.474
9.943
70.072
1.00
11.49
A


ATOM
141
O
LEU
A
20
16.197
10.177
71.044
1.00
12.18
A


ATOM
142
N
ALA
A
21
13.194
8.711
69.659
1.00
10.73
A


ATOM
143
CA
ALA
A
21
15.731
7.532
70.338
1.00
10.18
A


ATOM
144
CB
ALA
A
21
15.087
7.387
71.720
1.00
10.22
A


ATOM
145
C
ALA
A
21
15.456
6.286
69.501
1.00
10.69
A


ATOM
146
O
ALA
A
21
14.472
6.242
68.757
1.00
10.07
A


ATOM
147
N
ILE
A
22
16.329
5.286
69.622
1.00
10.11
A


ATOM
148
CA
ILE
A
22
16.191
4.028
68.885
1.00
10.87
A


ATOM
149
CB
ILE
A
22
17.101
3.990
67.624
1.00
11.25
A


ATOM
150
CG2
ILE
A
22
16.805
2.740
68.807
1.00
10.74
A


ATOM
151
CG1
ILE
A
22
16.889
5.242
66.765
1.00
11.30
A


ATOM
152
CD1
ILE
A
22
17.864
5.344
65.615
1.00
10.46
A


ATOM
153
C
ILE
A
22
16.602
2.850
69.766
1.00
11.38
A


ATOM
154
O
ILE
A
22
17.647
2.898
70.415
1.00
11.77
A


ATOM
155
N
GLY
A
23
15.778
1.802
69.781
1.00
11.30
A


ATOM
156
CA
GLY
A
23
16.072
0.607
70.560
1.00
11.51
A


ATOM
157
C
GLY
A
23
15.733
−0.646
69.760
1.00
12.11
A


ATOM
158
O
GLY
A
23
14.801
−0.614
68.952
1.00
11.93
A


ATOM
159
N
THR
A
24
16.482
−1.734
69.961
1.00
11.78
A


ATOM
160
CA
THR
A
24
16.244
−2.990
69.239
1.00
11.90
A


ATOM
161
CB
THR
A
24
17.278
−3.209
68.094
1.00
12.22
A


ATOM
162
OG1
THR
A
24
18.587
−3.407
68.649
1.00
13.40
A


ATOM
163
CG2
THR
A
24
17.307
−2.010
67.160
1.00
12.77
A


ATOM
164
C
THR
A
24
16.280
−4.234
70.140
1.00
11.99
A


ATOM
165
O
THR
A
24
16.812
−4.199
71.258
1.00
12.20
A


ATOM
166
N
ALA
A
25
15.713
−5.333
69.643
1.00
11.68
A


ATOM
167
CA
ALA
A
25
15.682
−6.596
70.380
1.00
11.37
A


ATOM
168
CB
ALA
A
25
14.534
−6.579
71.390
1.20
11.43
A


ATOM
169
C
ALA
A
25
15.528
−7.799
69.439
1.00
12.04
A


ATOM
170
O
ALA
A
25
14.978
−7.670
68.345
1.00
10.87
A


ATOM
171
N
ASN
A
26
16.020
−8.964
69.868
1.00
12.29
A


ATOM
172
CA
ASN
A
26
15.916
−10.194
69.074
1.00
12.75
A


ATOM
173
CB
ASN
A
26
17.198
−10.467
68.259
1.00
13.20
A


ATOM
174
CG
ASN
A
26
17.652
−9.276
67.425
1.00
13.62
A


ATOM
175
OD1
ASN
A
26
18.349
−8.385
67.919
1.00
13.50
A


ATOM
176
ND2
ASN
A
26
17.272
−9.265
66.145
1.00
11.58
A


ATOM
177
C
ASN
A
26
15.689
−11.396
69.992
1.00
13.37
A


ATOM
178
O
ASN
A
26
16.054
−11.366
71.173
1.00
13.18
A


ATOM
179
N
PRO
A
27
15.084
−12.474
69.465
1.00
14.48
A


ATOM
180
CD
PRO
A
27
14.417
−12.626
68.157
1.00
14.37
A


ATOM
181
CA
PRO
A
27
14.856
−13.652
70.309
1.00
15.55
A


ATOM
182
CB
PRO
A
27
14.166
−14.631
69.355
1.00
15.65
A


ATOM
183
CG
PRO
A
27
13.383
−13.707
68.445
1.00
14.59
A


ATOM
184
C
PRO
A
27
16.203
−14.176
70.820
1.00
16.73
A


ATOM
185
O
PRO
A
27
17.239
−13.968
70.185
1.00
16.65
A


ATOM
186
N
ALA
A
28
16.182
−14.861
71.958
1.00
18.08
A


ATOM
187
CA
ALA
A
28
17.402
−15.387
72.565
1.00
19.92
A


ATOM
188
CB
ALA
A
28
17.091
−15.886
73.983
1.00
20.22
A


ATOM
189
C
ALA
A
28
18.122
−16.483
71.771
1.00
20.71
A


ATOM
190
O
ALA
A
28
19.338
−16.634
71.882
1.00
22.24
A


ATOM
191
N
ASN
A
29
17.384
−17.239
70.965
1.00
21.91
A


ATOM
192
CA
ASN
A
29
17.969
−18.329
70.179
1.00
22.53
A


ATOM
193
CB
ASN
A
29
16.853
−19.300
69.770
1.00
23.29
A


ATOM
194
CG
ASN
A
29
17.360
−20.471
68.954
1.00
24.78
A


ATOM
195
OD1
ASN
A
29
18.351
−21.106
69.311
1.00
25.80
A


ATOM
196
ND2
ASN
A
29
16.669
−20.777
67.857
1.00
24.60
A


ATOM
197
C
ASN
A
29
18.756
−17.870
68.940
1.00
22.49
A


ATOM
198
O
ASN
A
29
18.163
−17.478
67.941
1.00
22.38
A


ATOM
199
N
CYS
A
30
20.088
−17.930
69.013
1.00
22.40
A


ATOM
200
CA
CYS
A
30
20.963
−17.534
67.901
1.00
23.15
A


ATOM
201
CB
CYS
A
30
22.263
−16.912
68.436
1.00
23.31
A


ATOM
202
SG
CYS
A
30
23.478
−16.418
67.155
1.00
25.62
A


ATOM
203
C
CYS
A
30
21.297
−18.737
67.012
1.00
23.29
A


ATOM
204
O
CYS
A
30
21.769
−19.768
67.496
1.00
23.46
A


ATOM
205
N
VAL
A
31
21.068
−18.590
65.709
1.00
22.78
A


ATOM
206
CA
VAL
A
31
21.307
−19.667
64.751
1.00
22.63
A


ATOM
207
CB
VAL
A
31
20.012
−19.961
63.950
1.00
22.87
A


ATOM
208
CG1
VAL
A
31
20.196
−21.191
63.072
1.00
22.78
A


ATOM
209
CG2
VAL
A
31
18.840
−20.144
64.907
1.00
23.17
A


ATOM
210
C
VAL
A
31
22.435
−19.359
63.757
1.00
22.49
A


ATOM
211
O
VAL
A
31
22.312
−18.452
62.932
1.00
21.48
A


ATOM
212
N
GLU
A
32
23.528
−20.121
63.832
1.00
22.05
A


ATOM
213
CA
GLU
A
32
24.663
−19.925
62.925
1.00
22.03
A


ATOM
214
CB
GLU
A
32
25.879
−20.715
63.414
1.00
23.60
A


ATOM
215
CG
GLU
A
32
26.500
−20.173
64.690
1.00
25.06
A


ATOM
216
CD
GLU
A
32
27.024
−18.765
64.517
1.00
26.01
A


ATOM
217
OE1
GLU
A
32
27.738
−18.520
63.521
1.00
27.39
A


ATOM
218
OE2
GLU
A
32
26.732
−17.904
65.375
1.00
26.48
A


ATOM
219
C
GLU
A
32
24.310
−20.366
61.508
1.00
21.46
A


ATOM
220
O
GLU
A
32
23.741
−21.435
61.311
1.00
20.95
A


ATOM
221
N
GLN
A
33
24.672
−19.552
60.521
1.00
20.88
A


ATOM
222
CA
GLN
A
33
24.360
−19.853
59.127
1.00
20.56
A


ATOM
223
CB
GLN
A
33
24.497
−18.589
58.272
1.00
20.04
A


ATOM
224
CG
GLN
A
33
23.983
−18.751
56.845
1.00
18.89
A


ATOM
225
CD
GLN
A
33
22.468
−18.680
56.751
1.00
18.59
A


ATOM
226
OE1
GLN
A
33
21.751
−19.243
57.581
1.00
17.31
A


ATOM
227
NE2
GLN
A
33
21.972
−17.988
55.726
1.00
17.55
A


ATOM
228
C
GLN
A
33
25.184
−20.974
58.488
1.00
20.69
A


ATOM
229
O
GLN
A
33
24.650
−21.768
57.716
1.00
20.26
A


ATOM
230
N
SER
A
34
26.475
−21.044
58.801
1.00
21.34
A


ATOM
231
CA
SER
A
34
27.331
−22.068
58.201
1.00
22.30
A


ATOM
232
CB
SER
A
34
28.770
−21.955
58.732
1.00
21.91
A


ATOM
233
OG
SER
A
34
28.835
−22.155
60.128
1.00
22.81
A


ATOM
234
C
SER
A
34
26.822
−23.497
58.383
1.00
22.37
A


ATOM
235
O
SER
A
34
27.007
−24.340
57.503
1.00
23.51
A


ATOM
236
N
THR
A
35
26.172
−23.772
59.507
1.00
22.43
A


ATOM
237
CA
THR
A
35
25.659
−25.113
59.765
1.00
21.81
A


ATOM
238
CB
THR
A
35
26.132
−25.621
61.136
1.00
22.18
A


ATOM
239
OG1
THR
A
35
25.700
−24.714
62.159
1.00
23.03
A


ATOM
240
CG1
THR
A
35
27.651
−25.725
61.165
1.00
22.82
A


ATOM
241
C
THR
A
35
24.133
−25.229
59.708
1.00
21.18
A


ATOM
242
O
THR
A
35
23.577
−26.273
60.056
1.00
21.01
A


ATOM
243
N
TYR
A
35
23.452
−24.174
59.265
1.00
19.84
A


ATOM
244
CA
TYR
A
36
21.991
−24.210
59.196
1.00
18.75
A


ATOM
245
CB
TYR
A
36
21.429
−22.843
58.775
1.00
17.52
A


ATOM
246
CG
TYR
A
36
19.928
−22.721
58.962
1.00
16.96
A


ATOM
247
CD1
TYR
A
36
19.346
−22.898
60.220
1.00
16.53
A


ATOM
248
CE1
TYR
A
36
17.964
−22.800
60.397
1.00
16.76
A


ATOM
249
CD2
TYR
A
36
19.088
−22.440
57.881
1.00
16.21
A


ATOM
250
CE2
TYR
A
36
17.705
−22.340
58.047
1.00
15.96
A


ATOM
251
CZ
TYR
A
36
17.149
−22.522
59.305
1.00
16.90
A


ATOM
252
OH
TYR
A
36
15.780
−22.438
59.472
1.00
16.69
A


ATOM
253
C
TYR
A
36
21.465
−25.294
58.256
1.00
18.74
A


ATOM
254
O
TYR
A
36
20.475
−25.955
58.566
1.00
19.06
A


ATOM
255
N
PRO
A
37
22.111
−25.489
57.090
1.00
18.99
A


ATOM
256
CD
PRO
A
37
23.208
−24.717
56.474
1.00
18.75
A


ATOM
257
CA
PRO
A
37
21.627
−26.525
56.169
1.00
18.98
A


ATOM
258
CB
PRO
A
37
22.706
−26.551
55.091
1.00
19.26
A


ATOM
259
CG
PRO
A
37
23.097
−25.105
55.005
1.00
18.64
A


ATOM
260
C
PRO
A
37
21.424
−27.887
56.838
1.00
19.27
A


ATOM
261
O
PRO
A
37
20.387
−28.525
56.653
1.00
18.41
A


ATOM
262
N
ASP
A
37
22.406
−28.331
57.617
1.00
19.51
A


ATOM
263
CA
ASP
A
38
22.283
−29.618
58.303
1.00
20.18
A


ATOM
264
CB
ASP
A
38
23.582
−29.976
59.040
1.00
20.94
A


ATOM
265
CG
ASP
A
38
24.691
−30.417
58.097
1.00
22.36
A


ATOM
266
OD1
ASP
A
38
24.381
−31.017
57.043
1.00
22.82
A


ATOM
267
OD2
ASP
A
38
25.877
−30.186
58.417
1.00
23.40
A


ATOM
268
C
ASP
A
38
21.125
−29.599
59.300
1.00
19.89
A


ATOM
269
O
ASP
A
38
20.365
−30.565
59.407
1.00
19.55
A


ATOM
270
N
PHE
A
39
20.991
−28.492
60.022
1.00
19.50
A


ATOM
271
CA
PHE
A
39
19.934
−28.340
61.021
1.00
19.62
A


ATOM
272
CB
PHE
A
39
20.163
−27.057
61.823
1.00
21.89
A


ATOM
273
CG
PHE
A
39
19.139
−26.822
62.892
1.00
24.15
A


ATOM
274
CD1
PHE
A
39
19.106
−27.622
64.031
1.00
25.06
A


ATOM
275
CD2
PHE
A
39
18.193
−25.813
62.753
1.00
25.47
A


ATOM
276
CE1
PHE
A
39
18.145
−27.423
65.019
1.00
26.34
A


ATOM
277
CE2
PHE
A
39
17.221
−25.603
63.737
1.00
26.52
A


ATOM
278
CZ
PHE
A
39
17.198
−26.410
64.871
1.00
27.00
A


ATOM
279
C
PHE
A
39
18.535
−28.307
60.400
1.00
18.72
A


ATOM
280
O
PHE
A
39
17.628
−29.011
60.852
1.00
18.17
A


ATOM
281
N
TYR
A
40
18.365
−27.484
59.371
1.00
17.64
A


ATOM
282
CA
TYR
A
40
17.080
−27.345
58.691
1.00
17.02
A


ATOM
283
CB
TYR
A
40
17.177
−26.240
57.630
1.00
16.06
A


ATOM
284
CG
TYR
A
40
15.923
−26.045
56.794
1.00
14.59
A


ATOM
285
CD1
TYR
A
40
14.742
−25.572
57.361
1.00
14.51
A


ATOM
286
CE1
TYR
A
40
13.595
−25.367
56.585
1.00
14.11
A


ATOM
287
CD2
TYR
A
40
15.933
−26.317
55.430
1.00
14.81
A


ATOM
288
CE2
TYR
A
40
14.799
−26.122
54.646
1.00
14.21
A


ATOM
289
CZ
TYR
A
40
13.635
−25.645
55.227
1.00
14.27
A


ATOM
290
OH
TYR
A
40
12.528
−25.435
54.440
1.00
13.60
A


ATOM
291
C
TYR
A
40
16.591
−28.647
58.050
1.00
17.25
A


ATOM
292
O
TYR
A
40
15.422
−29.004
58.178
1.00
17.01
A


ATOM
293
N
PHE
A
41
17.471
−29.363
57.358
1.00
18.01
A


ATOM
294
CA
PHE
A
41
17.044
−30.607
56.725
1.00
18.83
A


ATOM
295
CB
PHE
A
41
18.051
−31.035
55.654
1.00
18.25
A


ATOM
296
CG
PHE
A
41
17.815
−30.374
54.325
1.00
18.43
A


ATOM
297
CD1
PHE
A
41
18.015
−29.006
54.170
1.00
17.48
A


ATOM
298
CD2
PHE
A
41
17.312
−31.104
53.250
1.00
17.95
A


ATOM
299
CE1
PHE
A
41
17.713
−28.369
52.966
1.00
17.59
A


ATOM
300
CE2
PHE
A
41
17.006
−30.478
52.046
1.00
18.17
A


ATOM
301
CZ
PHE
A
41
17.206
−29.104
51.904
1.00
18.05
A


ATOM
302
C
PHE
A
41
16.766
−31.745
57.705
1.00
19.60
A


ATOM
303
O
PHE
A
41
16.048
−32.690
50.377
1.00
19.06
A


ATOM
304
N
LYS
A
42
17.314
−31.649
58.912
1.00
20.78
A


ATOM
305
CA
LYS
A
42
17.079
−32.678
59.927
1.00
22.23
A


ATOM
306
CB
LYS
A
42
18.174
−32.647
60.996
1.00
23.48
A


ATOM
307
CG
LYS
A
42
17.972
−33.680
62.096
1.00
25.67
A


ATOM
308
CD
LYS
A
42
18.923
−33.467
63.262
1.00
27.51
A


ATOM
309
CE
LYS
A
42
18.621
−32.169
63.993
1.00
29.25
A


ATOM
310
NZ
LYS
A
42
19.511
−31.974
65.173
1.00
30.49
A


ATOM
311
C
LYS
A
42
15.724
−32.465
60.608
1.00
22.35
A


ATOM
312
O
LYS
A
42
14.909
−33.386
60.697
1.00
22.15
A


ATOM
313
N
ILE
A
43
15.485
−31.246
61.085
1.00
22.66
A


ATOM
314
CA
ILE
A
43
14.233
−30.932
61.772
1.00
22.68
A


ATOM
315
CB
ILE
A
43
14.269
−29.502
62.372
1.00
22.71
A


ATOM
316
CG2
ILE
A
43
14.054
−28.462
61.282
1.00
21.97
A


ATOM
317
CG1
ILE
A
43
13.190
−29.364
63.446
1.00
23.48
A


ATOM
318
CD1
ILE
A
43
13.366
−30.310
64.624
1.00
23.50
A


ATOM
319
C
ILE
A
43
12.999
−31.082
60.874
1.00
22.84
A


ATOM
320
O
ILE
A
43
11.891
−31.309
61.366
1.00
22.92
A


ATOM
321
N
THR
A
44
13.184
−30.960
59.562
1.00
22.55
A


ATOM
322
CA
THR
A
44
12.065
−31.104
59.637
1.00
22.54
A


ATOM
323
CB
THR
A
44
12.152
−30.097
57.459
1.00
22.72
A


ATOM
324
OG1
THR
A
44
13.371
−30.303
56.730
1.00
22.37
A


ATOM
325
CG2
THR
A
44
12.098
−28.665
57.977
1.00
22.10
A


ATOM
326
C
THR
A
44
12.014
−32.519
58.071
1.00
23.10
A


ATOM
327
O
THR
A
44
11.202
−32.820
57.191
1.00
23.58
A


ATOM
328
N
ASN
A
45
12.887
−33.383
58.584
1.00
23.35
A


ATOM
329
CA
ASN
A
45
12.960
−34.775
58.147
1.00
23.44
A


ATOM
330
CB
ASN
A
45
11.737
−35.544
58.664
1.00
24.41
A


ATOM
331
CG
ASN
A
45
11.514
−35.346
60.161
1.00
25.94
A


ATOM
332
OD1
ASN
A
45
12.443
−35.452
60.959
1.00
26.60
A


ATOM
333
ND2
ASN
A
45
10.277
−35.062
60.544
1.00
26.55
A


ATOM
334
C
ASN
A
45
13.051
−34.877
56.621
1.00
23.02
A


ATOM
335
O
ASN
A
45
12.304
−35.623
55.990
1.00
22.54
A


ATOM
336
N
SER
A
46
13.990
−34.133
56.041
1.00
22.98
A


ATOM
337
CA
SER
A
46
14.178
−34.115
54.593
1.00
23.29
A


ATOM
338
CB
SER
A
46
13.839
−32.723
54.056
1.00
23.17
A


ATOM
339
OG
SER
A
46
12.593
−32.267
54.556
1.00
23.57
A


ATOM
340
C
SER
A
46
15.606
−34.483
54.164
1.00
23.38
A


ATOM
341
O
SER
A
46
16.051
−34.091
53.086
1.00
22.63
A


ATOM
342
N
GLU
A
47
16.314
−35.241
54.995
1.00
23.79
A


ATOM
343
CA
GLU
A
47
17.693
−35.618
54.687
1.00
24.63
A


ATOM
344
CB
GLU
A
47
18.342
−36.266
55.912
1.00
25.51
A


ATOM
345
CG
GLU
A
47
18.434
−35.310
57.089
1.00
28.07
A


ATOM
346
CD
GLU
A
47
19.244
−35.856
58.236
1.00
29.80
A


ATOM
347
OE1
GLU
A
47
18.831
−36.878
58.824
1.00
31.27
A


ATOM
348
OE2
GLU
A
47
20.297
−35.260
58.550
1.00
30.37
A


ATOM
349
C
GLU
A
47
17.878
−36.510
53.464
1.00
24.72
A


ATOM
350
O
GLU
A
47
18.999
−36.670
52.934
1.00
24.73
A


ATOM
351
N
HIS
A
48
16.792
−37.087
52.963
1.00
24.76
A


ATOM
352
CA
HIS
A
48
16.893
−37.940
51.785
1.00
24.97
A


ATOM
353
CB
HIS
A
48
15.765
−38.978
51.764
1.00
24.66
A


ATOM
354
CG
HIS
A
48
14.401
−38.396
51.952
1.00
24.86
A


ATOM
355
CD2
HIS
A
48
13.382
−38.213
51.079
1.00
24.69
A


ATOM
356
ND1
HIS
A
48
13.956
−37.919
53.166
1.00
25.06
A


ATOM
357
CE1
HIS
A
48
12.721
−37.468
53.033
1.00
24.93
A


ATOM
358
NE2
HIS
A
48
12.350
−37.635
51.777
1.00
24.70
A


ATOM
359
C
HIS
A
48
16.870
−37.111
50.502
1.00
25.02
A


ATOM
360
O
HIS
A
48
17.084
−37.637
49.411
1.00
24.86
A


ATOM
361
N
LYS
A
49
16.609
−35.814
50.634
1.00
25.23
A


ATOM
362
CA
LYS
A
49
16.588
−34.927
49.472
1.00
25.72
A


ATOM
363
CB
LYS
A
49
15.576
−33.800
49.680
1.00
26.92
A


ATOM
364
CG
LYS
A
49
14.147
−34.284
49.886
1.00
28.26
A


ATOM
365
CD
LYS
A
49
13.175
−33.119
49.924
1.00
30.09
A


ATOM
366
CE
LYS
A
49
11.739
−33.597
50.099
1.00
31.30
A


ATOM
367
NZ
LYS
A
49
10.776
−32.457
50.099
1.00
31.83
A


ATOM
368
C
LYS
A
49
17.993
−34.356
49.298
1.00
25.62
A


ATOM
369
O
LYS
A
49
18.215
−33.150
49.423
1.00
25.21
A


ATOM
370
N
THR
A
50
18.936
−35.247
49.005
1.00
25.27
A


ATOM
371
CA
THR
A
50
20.344
−34.901
48.840
1.00
25.11
A


ATOM
372
CB
THR
A
50
21.147
−36.142
48.410
1.00
25.28
A


ATOM
373
OG1
THR
A
50
20.640
−36.633
47.164
1.00
25.79
A


ATOM
374
CG2
THR
A
50
21.018
−37.238
49.459
1.00
25.39
A


ATOM
375
C
THR
A
50
20.662
−33.751
47.882
1.00
25.05
A


ATOM
376
O
THR
A
50
21.462
−32.875
48.211
1.00
24.58
A


ATOM
377
N
GLU
A
51
20.054
−33.758
46.700
1.00
24.67
A


ATOM
378
CA
GLU
A
51
20.294
−32.703
45.721
1.00
24.81
A


ATOM
379
CB
GLU
A
51
19.676
−33.083
44.374
1.00
25.94
A


ATOM
380
CG
GLU
A
51
19.663
−31.964
43.338
1.00
27.31
A


ATOM
381
CD
GLU
A
51
20.991
−31.243
43.233
1.00
28.46
A


ATOM
382
OE1
GLU
A
51
22.039
−31.924
43.231
1.00
29.16
A


ATOM
383
OE2
GLU
A
51
20.986
−29.994
43.145
1.00
28.42
A


ATOM
384
C
GLU
A
51
19.729
−31.365
46.195
1.00
24.29
A


ATOM
385
O
GLU
A
51
20.385
−30.328
46.083
1.00
23.82
A


ATOM
386
N
LEU
A
52
18.511
−31.394
46.725
1.00
23.31
A


ATOM
387
CA
LEU
A
52
17.874
−30.180
47.222
1.00
22.68
A


ATOM
388
CB
LEU
A
52
16.477
−30.508
47.767
1.00
22.59
A


ATOM
389
CG
LEU
A
52
15.576
−29.339
48.178
1.00
22.20
A


ATOM
390
CD1
LEU
A
52
15.415
−28.367
47.016
1.00
22.61
A


ATOM
391
CD2
LEU
A
52
14.221
−29.876
48.612
1.00
22.03
A


ATOM
392
C
LEU
A
52
18.739
−29.559
48.321
1.00
22.60
A


ATOM
393
O
LEU
A
52
18.904
−28.340
48.380
1.00
22.40
A


ATOM
394
N
LYS
A
53
19.299
−30.401
49.185
1.00
22.30
A


ATOM
395
CA
LYS
A
53
20.146
−29.916
50.268
1.00
22.67
A


ATOM
396
CB
LYS
A
53
20.554
−31.067
51.193
1.00
22.70
A


ATOM
397
CG
LYS
A
53
21.340
−30.614
52.422
1.00
23.68
A


ATOM
398
CD
LYS
A
53
21.711
−31.786
53.316
1.00
24.89
A


ATOM
399
CE
LYS
A
53
22.373
−31.312
54.597
1.00
25.28
A


ATOM
400
NZ
LYS
A
53
22.726
−32.448
55.491
1.00
26.32
A


ATOM
401
C
LYS
A
53
21.401
−29.225
49.734
1.00
22.70
A


ATOM
402
O
LYS
A
53
21.884
−28.267
50.336
1.00
22.36
A


ATOM
403
N
GLU
A
54
21.933
−29.716
48.615
1.00
23.17
A


ATOM
404
CA
GLU
A
54
22.129
−29.112
48.025
1.00
23.50
A


ATOM
405
CB
GLU
A
54
22.615
−29.912
46.807
1,00
24.90
A


ATOM
406
CG
GLU
A
54
23.970
−31.367
47.092
1.00
27.49
A


ATOM
407
CD
GLU
A
54
24.723
−32.028
45.943
1.00
28.58
A


ATOM
408
OE1
GLU
A
54
24.314
−31.860
44.773
1.00
29.73
A


ATOM
409
OE2
GLU
A
54
25.723
−32.724
46.214
1.00
29.34
A


ATOM
410
C
GLU
A
54
22.793
−27.691
47.591
1.00
22.71
A


ATOM
411
O
GLU
A
54
23.573
−26.762
47.814
1.00
22.66
A


ATOM
412
N
LYS
A
55
21.629
−27.533
46.964
1.00
21.69
A


ATOM
413
CA
LYS
A
55
21.178
−26.225
46.506
1.00
21.03
A


ATOM
414
CB
LYS
A
55
19.819
−26.330
45.801
1.00
20.58
A


ATOM
415
CG
LYS
A
55
19.849
−26.920
44.399
1.00
21.67
A


ATOM
416
CD
LYS
A
55
18.472
−26.811
43.746
1.00
22.06
A


ATOM
417
CE
LYS
A
55
18.490
−27.256
42.290
1.00
22.95
A


ATOM
418
NZ
LYS
A
55
18.862
−28.692
42.156
1.00
23.21
A


ATOM
419
C
LYS
A
55
21.049
−25.260
47.684
1.00
20.45
A


ATOM
420
O
LYS
A
55
21.441
−24.097
47.588
1.00
19.89
A


ATOM
421
N
PHE
A
56
20.498
−25.748
48.794
1.00
19.90
A


ATOM
422
CA
PHE
A
56
20.309
−24.914
49.976
1.00
19.76
A


ATOM
423
CB
PHE
A
56
19.436
−25.638
51.009
1.00
19.84
A


ATOM
424
CG
PHE
A
56
18.945
−24.743
52.119
1.00
19.88
A


ATOM
425
CD1
PHE
A
56
18.160
−23.628
51.833
1.00
19.11
A


ATOM
426
CD2
PHE
A
56
19.283
−25.003
53.444
1.00
19.71
A


ATOM
427
CE1
PHE
A
56
17.718
−22.782
52.853
1.00
19.68
A


ATOM
428
CE2
PHE
A
56
18.848
−24.165
54.473
1.00
19.76
A


ATOM
429
CZ
PHE
A
56
18.064
−23.052
54.177
1.00
19.57
A


ATOM
430
C
PHE
A
56
21.648
−24.509
50.599
1.00
20.08
A


ATOM
431
O
PHE
A
56
21.786
−23.399
51.114
1.00
19.29
A


ATOM
432
N
GLN
A
57
22.633
−25.404
50.544
1.00
20.33
A


ATOM
433
CA
GLN
A
57
23.957
−25.102
51.084
1.00
21.34
A


ATOM
434
CB
GLN
A
57
24.883
−26.318
50.958
1.00
21.90
A


ATOM
435
CG
GLN
A
57
26.264
−26.129
51.590
1.00
22.72
A


ATOM
436
CD
GLN
A
57
26.206
−25.936
53.094
1.00
23.02
A


ATOM
437
OE1
GLN
A
57
25.666
−26.776
53.818
1.00
23.90
A


ATOM
438
NE2
GLN
A
57
26.766
−24.830
53.573
1.00
22.69
A


ATOM
439
C
GLN
A
57
24.543
−23.924
50.300
1.00
21.43
A


ATOM
440
O
GLN
A
57
25.161
−23.026
50.880
1.00
21.65
A


ATOM
441
N
ARG
A
58
24.344
−23.933
48.982
1.00
21.69
A


ATOM
442
CA
ARG
A
58
24.840
−22.857
48.128
1.00
22.25
A


ATOM
443
CB
ARG
A
58
24.633
−23.184
46.645
1.00
23.45
A


ATOM
444
CG
ARG
A
58
25.478
−24.334
46.108
1.00
27.13
A


ATOM
445
CD
ARG
A
58
25.592
−24.237
44.587
1.00
28.97
A


ATOM
446
NE
ARG
A
58
26.291
−25.374
43.994
1.00
31.10
A


ATOM
447
CZ
ARG
A
58
25.779
−26.596
43.878
1.00
31.73
A


ATOM
448
NH1
ARG
A
58
24.551
−26.851
44.316
1.00
30.89
A


ATOM
449
NH2
ARG
A
58
26.495
−27.563
43.317
1.00
31.70
A


ATOM
450
C
ARG
A
58
24.130
−21.544
48.451
1.00
21.39
A


ATOM
451
O
ARG
A
58
24.758
−20.487
48.489
1.00
21.08
A


ATOM
452
N
MET
A
59
22.820
−21.616
48.667
1.00
20.52
A


ATOM
453
CA
MET
A
59
22.037
−20.433
49.004
1.00
20.06
A


ATOM
454
CB
MET
A
59
20.560
−20.801
49.198
1.00
19.96
A


ATOM
455
CG
MET
A
59
19.825
−21.168
47.908
1.00
20.74
A


ATOM
456
SD
MET
A
59
18.084
−21.605
48.175
1.00
20.50
A


ATOM
457
CE
MET
A
59
17.663
−22.339
46.587
1.00
21.29
A


ATOM
458
C
MET
A
59
22.586
−19.807
50.285
1.00
20.21
A


ATOM
459
O
MET
A
59
22.811
−18.595
50.348
1.00
19.35
A


ATOM
460
N
CYS
A
60
22.814
−20.638
51.298
1.00
19.75
A


ATOM
461
CA
CYS
A
60
23.336
−20.152
52.571
1.00
20.27
A


ATOM
462
CB
CYS
A
60
23.254
−21.254
53.638
1.00
19.75
A


ATOM
463
SG
CYS
A
60
21.564
−21.694
54.177
1.00
19.90
A


ATOM
464
C
CYS
A
60
24.772
−19.627
52.468
1.00
20.80
A


ATOM
465
O
CYS
A
60
25.109
−18.616
53.085
1.00
20.42
A


ATOM
466
N
ASP
A
61
25.618
−20.301
51.689
1.00
21.26
A


ATOM
467
CA
ASP
A
61
27.008
−19.865
51.542
1.00
22.02
A


ATOM
468
CB
ASP
A
61
27.826
−20.878
50.729
1.00
22.21
A


ATOM
469
CG
ASP
A
61
28.014
−22.201
51.445
1.00
23.21
A


ATOM
470
OD1
ASP
A
61
27.908
−22.240
52.692
1.00
21.87
A


ATOM
471
OD2
ASP
A
61
28.290
−23.203
50.747
1.00
23.65
A


ATOM
472
C
ASP
A
61
27.161
−18.498
50.875
1.00
22.10
A


ATOM
473
O
ASP
A
61
28.122
−17.778
51.145
1.00
22.14
A


ATOM
474
N
LYS
A
62
26.224
−18.143
50.004
1.00
22.31
A


ATOM
475
CA
LYS
A
62
26.307
−16.871
49.294
1.00
22.65
A


ATOM
476
CB
LYS
A
62
26.114
−17.110
47.797
1.00
23.96
A


ATOM
477
CG
LYS
A
62
27.022
−18.201
47.241
1.00
25.71
A


ATOM
478
CD
LYS
A
62
27.053
−18.181
45.729
1.00
28.01
A


ATOM
479
CE
LYS
A
62
27.778
−16.951
45.218
1.00
29.31
A


ATOM
480
NZ
LYS
A
62
29.179
−16.906
45.723
1.00
30.60
A


ATOM
481
C
LYS
A
62
25.331
−15.796
49.768
1.00
22.01
A


ATOM
482
O
LYS
A
62
25.206
−14.746
49.135
1.00
21.84
A


ATOM
483
N
SER
A
63
24.660
−16.052
50.886
1.00
20.99
A


ATOM
484
CA
SER
A
63
23.688
−15.112
51.438
1.00
20.43
A


ATOM
485
CB
SER
A
63
22.798
−15.830
52.452
1.00
19.65
A


ATOM
486
OG
SER
A
63
23.572
−16.299
53.544
1.00
19.58
A


ATOM
487
C
SER
A
63
24.326
−13.903
52.118
1.00
20.52
A


ATOM
488
O
SER
A
63
23.685
−12.861
52.274
1.00
20.08
A


ATOM
489
N
MET
A
64
25.584
−14.051
52.523
1.00
20.87
A


ATOM
490
CA
MET
A
64
26.315
−12.990
53.212
1.00
21.59
A


ATOM
491
CB
MET
A
64
26.284
−11.685
52.405
1.00
23.35
A


ATOM
492
CG
MET
A
64
26.926
−11.785
51.024
1.00
25.55
A


ATOM
493
SD
MET
A
64
28.605
−12.454
51.053
1.00
29.17
A


ATOM
494
CE
MET
A
64
28.299
−14.085
50.424
1.00
28.30
A


ATOM
495
C
MET
A
64
25.730
−12.762
54.606
1.00
21.04
A


ATOM
496
O
MET
A
64
25.831
−11.671
55.175
1.30
20.22
A


ATOM
497
N
ILE
A
65
25.114
−13.811
55.144
1.00
20.43
A


ATOM
498
CA
ILE
A
65
24.523
−13.785
56.478
1.00
19.58
A


ATOM
499
CB
ILE
A
65
23.059
−14.294
56.457
1.00
18.89
A


ATOM
500
CG2
ILE
A
65
22.542
−14.457
57.875
1.00
18.15
A


ATOM
501
CG1
ILE
A
65
22.176
−13.322
55.668
1.00
18.42
A


ATOM
502
CD1
ILE
A
65
20.726
−13.775
55.516
1.00
17.96
A


ATOM
503
C
ILE
A
65
25.344
−14.718
57.362
1.00
19.92
A


ATOM
504
O
ILE
A
65
25.572
−15.871
56.999
1.00
20.12
A


ATOM
505
N
LYS
A
66
25.794
−14.225
58.513
1.00
19.96
A


ATOM
506
CA
LYS
A
66
26.584
−15.047
59.426
1.00
20.16
A


ATOM
507
CB
LYS
A
66
27.604
−14.186
60.175
1.00
21.74
A


ATOM
508
CG
LYS
A
66
28.575
−13.467
59.257
1.00
24.36
A


ATOM
509
CD
LYS
A
66
29.645
−12.710
60.029
1.00
25.33
A


ATOM
510
CE
LYS
A
66
30.637
−13.655
60.689
1.00
26.98
A


ATOM
511
NZ
LYS
A
66
31.829
−12.917
61.209
1.00
26.99
A


ATOM
512
C
LYS
A
66
25.696
−15.782
60.431
1.00
19.49
A


ATOM
513
O
LYS
A
66
25.986
−16.918
60.812
1.00
18.64
A


ATOM
514
N
ARG
A
67
24.622
−15.126
60.861
1.00
18.51
A


ATOM
515
CA
ARG
A
67
23.691
−15.726
61.810
1.00
18.88
A


ATOM
516
CB
ARG
A
67
24.349
−15.877
63.187
1.00
20.52
A


ATOM
517
CG
ARG
A
67
25.004
−14.622
63.746
1.00
23.68
A


ATOM
518
CD
ARG
A
67
25.877
−14.994
64.946
1.00
26.21
A


ATOM
519
NE
ARG
A
67
26.647
−13.871
65.476
1.00
28.84
A


ATOM
520
CZ
ARG
A
67
27.641
−13.264
64.833
1.00
29.97
A


ATOM
521
NH1
ARG
A
67
27.999
−13.664
63.621
1.00
30.84
A


ATOM
522
NH2
ARG
A
67
28.286
−12.257
65.410
1.00
30.56
A


ATOM
523
C
ARG
A
67
22.385
−14.950
61.939
1.00
17.34
A


ATOM
524
O
ARG
A
67
22.300
−13.788
61.540
1.00
17.53
A


ATOM
525
N
ARG
A
68
21.373
−15.612
62.494
1.00
15.84
A


ATOM
526
CA
ARG
A
68
20.048
−15.030
62.690
1.00
15.12
A


ATOM
527
CB
ARG
A
68
19.090
−15.512
61.595
1.00
15.02
A


ATOM
528
CG
ARG
A
68
19.435
−15.049
60.182
1.00
15.37
A


ATOM
529
CD
ARG
A
68
18.539
−15.737
59.159
1.00
15.36
A


ATOM
530
NE
ARG
A
68
18.998
−17.087
58.835
1.00
15.15
A


ATOM
531
CZ
ARG
A
68
18.294
−17.961
58.118
1.00
16.53
A


ATOM
532
NH1
ARG
A
68
17.092
−17.632
57.656
1.00
14.86
A


ATOM
533
NH2
ARG
A
68
18.797
−19.160
57.842
1.00
15.79
A


ATOM
534
C
ARG
A
68
19.481
−15.459
64.047
1.00
15.54
A


ATOM
535
O
ARG
A
68
19.968
−16.408
64.661
1.00
15.15
A


ATOM
536
N
TYR
A
69
18.445
−14.762
64.503
1.00
14.96
A


ATOM
537
CA
TYR
A
69
17.798
−15.088
65.770
1.00
15.18
A


ATOM
538
CB
TYR
A
69
17.811
−13.869
66.701
1.00
15.19
A


ATOM
539
CG
TYR
A
69
19.222
−13.407
67.003
1.00
15.86
A


ATOM
540
CD1
TYR
A
69
19.938
−12.641
66.081
1.00
15.86
A


ATOM
541
CE1
TYR
A
69
21.279
−12.307
66.304
1.00
16.29
A


ATOM
542
CD2
TYR
A
69
19.876
−13.821
68.163
1.00
16.01
A


ATOM
543
CE2
TYR
A
69
21.213
−13.498
68.394
1.00
16.51
A


ATOM
544
CZ
TYR
A
69
21.909
−12.745
67.462
1.00
16.56
A


ATOM
545
OH
TYR
A
69
23.243
−12.456
67.670
1.00
17.13
A


ATOM
546
C
TYR
A
69
16.377
−15.533
65.459
1.00
15.75
A


ATOM
547
O
TYR
A
69
15.668
−14.878
64.692
1.00
15.23
A


ATOM
548
N
MET
A
70
15.965
−16.655
66.040
1.00
15.97
A


ATOM
549
CA
MET
A
70
14.631
−17.191
65.775
1.00
17.00
A


ATOM
550
CB
MET
A
70
14.731
−18.369
64.796
1.00
18.13
A


ATOM
551
CG
MET
A
70
15.216
−18.019
63.389
1.00
20.30
A


ATOM
552
SD
MET
A
70
15.414
−19.496
62.341
1.00
23.91
A


ATOM
553
CE
MET
A
70
16.362
−18.809
60.972
1.00
22.14
A


ATOM
554
C
MET
A
70
13.857
−17.654
67.007
1.00
16.77
A


ATOM
555
O
MET
A
70
14.386
−18.385
67.844
1.00
17.33
A


ATOM
556
N
TYR
A
71
12.598
−17.231
67.099
1.00
16.96
A


ATOM
557
CA
TYR
A
71
11.713
−17.629
68.193
1.00
17.37
A


ATOM
558
CB
TYR
A
71
10.377
−16.878
68.096
1.00
17.57
A


ATOM
559
CG
TYR
A
71
9.219
−17.560
68.802
1.00
18.29
A


ATOM
560
CD1
TYR
A
71
9.065
−17.475
70.185
1.00
18.60
A


ATOM
561
CE1
TYR
A
71
8.012
−18.126
70.835
1.00
19.20
A


ATOM
562
CD2
TYR
A
71
8.291
−18.311
68.083
1.00
18.96
A


ATOM
563
CE2
TYR
A
71
7.238
−18.963
68.719
1.00
19.52
A


ATOM
564
CZ
TYR
A
71
7.103
−18.868
70.093
1.00
19.82
A


ATOM
565
OH
TYR
A
71
6.056
−19.511
70.718
1.00
19.82
A


ATOM
566
C
TYR
A
71
11.462
−19.135
68.079
1.00
17.45
A


ATOM
567
O
TYR
A
71
11.358
−19.842
69.085
1.00
16.85
A


ATOM
568
N
LEU
A
72
11.348
−19.613
66.843
1.00
17.94
A


ATOM
569
CA
LEU
A
72
11.124
−21.032
66.586
1.00
18.87
A


ATOM
570
CB
LEU
A
72
10.858
−21.288
65.098
1.00
19.09
A


ATOM
571
CG
LEU
A
72
9.483
−20.991
64.499
1.00
19.52
A


ATOM
572
CD1
LEU
A
72
9.514
−21.350
63.019
1.00
19.49
A


ATOM
573
CD2
LEU
A
72
8.404
−21.791
65.213
1.00
19.42
A


ATOM
574
C
LEU
A
72
12.352
−21.831
66.997
1.00
18.91
A


ATOM
575
O
LEU
A
72
13.458
−21.568
66.528
1.00
19.47
A


ATOM
576
N
THR
A
73
12.152
−22.808
67.871
1.00
19.15
A


ATOM
577
CA
THR
A
73
13.247
−23.651
68.336
1.00
19.69
A


ATOM
578
CB
THR
A
73
13.379
−23.592
69.863
1.00
19.91
A


ATOM
579
OG1
THR
A
73
12.153
−24.037
70.457
1.00
20.02
A


ATOM
580
CG2
THR
A
73
13.679
−22.176
70.321
1.00
19.67
A


ATOM
581
C
THR
A
73
12.955
−25.093
67.946
1.00
20.34
A


ATOM
582
O
THR
A
73
11.850
−25.416
67.509
1.00
19.94
A


ATOM
583
N
GLU
A
74
13.945
−25.963
68.101
1.00
20.84
A


ATOM
584
CA
GLU
A
74
13.747
−27.364
67.775
1.00
21.72
A


ATOM
585
CB
GLU
A
74
15.055
−28.140
67.970
1.00
22.75
A


ATOM
586
CG
GLU
A
74
14.904
−29.649
67.901
1.00
24.21
A


ATOM
587
CD
GLU
A
74
16.228
−30.359
67.729
1.00
25.53
A


ATOM
588
OE1
GLU
A
74
17.232
−29.907
68.322
1.00
25.87
A


ATOM
589
OE2
GLU
A
74
16.263
−31.378
67.003
1.00
26.84
A


ATOM
590
C
GLU
A
74
12.629
−27.968
68.632
1.00
21.92
A


ATOM
591
O
GLU
A
74
11.862
−28.803
68.153
1.00
21.27
A


ATOM
592
N
GLU
A
75
12.520
−27.538
69.888
1.00
22.05
A


ATOM
593
CA
GLU
A
75
11.481
−28.073
70.769
1.00
22.84
A


ATOM
594
CB
GLU
A
75
11.667
−27.583
72.209
1.00
24.92
A


ATOM
595
CG
GLU
A
75
13.096
−27.606
72.704
1.00
27.52
A


ATOM
596
CD
GLU
A
75
13.837
−26.334
72.354
1.00
29.08
A


ATOM
597
OE1
GLU
A
75
13.446
−25.259
72.867
1.00
30.76
A


ATOM
598
OE2
GLU
A
75
14.803
−26.403
71.567
1.00
30.32
A


ATOM
599
C
GLU
A
75
10.086
−27.682
70.296
1.00
22.09
A


ATOM
600
O
GLU
A
75
9.157
−28.493
70.327
1.00
21.65
A


ATOM
601
N
ILE
A
76
9.937
−26.432
69.869
1.00
21.20
A


ATOM
602
CA
ILE
A
76
8.648
−25.953
69.388
1.00
20.72
A


ATOM
603
CB
ILE
A
76
8.677
−24.424
69.138
1.00
20.85
A


ATOM
604
CG2
ILE
A
76
7.408
−23.981
68.404
1.00
20.95
A


ATOM
605
CG1
ILE
A
76
8.814
−23.689
70.476
1.00
21.17
A


ATOM
606
CD1
ILE
A
76
8.900
−22.178
70.356
1.00
21.73
A


ATOM
607
C
ILE
A
76
8.288
−26.677
68.094
1.00
20.27
A


ATOM
608
O
ILE
A
76
7.169
−27.165
67.939
1.00
19.16
A


ATOM
609
N
LEU
A
77
9.243
−26.757
67.173
1.00
20.41
A


ATOM
610
CA
LEU
A
77
8.992
−27.427
65.904
1.00
21.09
A


ATOM
611
CB
LEU
A
77
10.233
−27.365
65.008
1.00
20.90
A


ATOM
612
CG
LEU
A
77
10.516
−25.973
64.424
1.00
20.93
A


ATOM
613
CD1
LEU
A
77
11.852
−25.962
63.711
1.00
21.04
A


ATOM
614
CD2
LEU
A
77
9.395
−25.587
63.467
1.00
20.50
A


ATOM
615
C
LEU
A
77
8.557
−28.872
66.114
1.00
21.87
A


ATOM
616
O
LEU
A
77
7.678
−29.367
65.409
1.00
22.38
A


ATOM
617
N
LYS
A
78
9.150
−29.546
67.095
1.00
22.54
A


ATOM
618
CA
LYS
A
78
8.785
−30.933
67.354
1.00
23.21
A


ATOM
619
CB
LYS
A
78
9.792
−31.577
68.320
1.00
24.36
A


ATOM
620
CG
LYS
A
78
11.206
−31.602
67.746
1.00
26.62
A


ATOM
621
CD
LYS
A
78
12.031
−32.799
68.203
1.00
28.49
A


ATOM
622
CE
LYS
A
78
12.481
−32.672
68.644
1.00
29.78
A


ATOM
623
NZ
LYS
A
78
13.422
−33.776
70.010
1.00
30.83
A


ATOM
624
C
LYS
A
78
7.355
−31.090
67.871
1.00
22.73
A


ATOM
625
O
LYS
A
78
6.767
−32.162
67.753
1.00
23.44
A


ATOM
626
N
GLU
A
79
6.788
−30.017
68.417
1.00
22.50
A


ATOM
627
CA
GLU
A
79
5.418
−30.042
68.940
1.00
22.20
A


ATOM
628
CB
GLU
A
79
5.274
−29.037
70.094
1.00
24.23
A


ATOM
629
CG
GLU
A
79
6.191
−29.276
71.295
1.00
27.11
A


ATOM
630
CD
GLU
A
79
6.244
−28.080
72.247
1.00
29.29
A


ATOM
631
OE1
GLU
A
79
5.173
−27.543
72.598
1.00
31.41
A


ATOM
632
OE2
GLU
A
79
7.357
−27.678
72.655
1.00
30.28
A


ATOM
633
C
GLU
A
79
4.380
−29.695
67.859
1.00
20.87
A


ATOM
634
O
GLU
A
79
3.180
−29.910
68.046
1.00
20.47
A


ATOM
635
N
ASN
A
80
4.843
−29.158
66.734
1.00
18.83
A


ATOM
636
CA
ASN
A
80
3.946
−28.749
65.648
1.00
17.98
A


ATOM
637
CB
ASN
A
80
4.013
−27.229
65.498
1.00
17.92
A


ATOM
638
CG
ASN
A
80
3.591
−26.503
66.761
1.00
18.10
A


ATOM
639
OD1
ASN
A
80
2.407
−26.251
66.978
1.00
17.75
A


ATOM
640
ND2
ASN
A
80
4.562
−26.178
67.612
1.00
17.68
A


ATOM
641
C
ASN
A
80
4.319
−29.421
64.328
1.00
16.94
A


ATOM
642
O
ASN
A
80
4.901
−28.797
63.442
1.00
16.43
A


ATOM
643
N
PRO
A
81
3.961
−30.703
64.172
1.00
16.48
A


ATOM
644
CD
PRO
A
81
3.181
−31.528
65.108
1.00
16.60
A


ATOM
645
CA
PRO
A
81
4.281
−31.448
62.949
1.00
16.06
A


ATOM
646
CB
PRO
A
81
3.647
−32.826
63.200
1.00
16.19
A


ATOM
647
CG
PRO
A
81
2.576
−32.556
64.195
1.00
17.80
A


ATOM
648
C
PRO
A
81
3.895
−30.837
61.598
1.00
15.44
A


ATOM
649
O
PRO
A
81
4.656
−30.956
60.635
1.00
14.88
A


ATOM
650
N
ASN
A
82
2.740
−30.180
61.512
1.00
14.66
A


ATOM
651
CA
ASN
A
82
2.334
−29.578
60.241
1.00
14.83
A


ATOM
652
CB
ASN
A
82
0.833
−29.240
60.252
1.00
14.58
A


ATOM
653
CG
ASN
A
82
−0.039
−30.447
59.932
1.00
15.49
A


ATOM
654
OD1
ASN
A
82
−1.277
−30.345
59.864
1.00
15.62
A


ATOM
655
ND2
ASN
A
82
0.598
−31.595
59.729
1.00
14.09
A


ATOM
656
C
ASN
A
82
3.160
−28.337
59.877
1.00
14.64
A


ATOM
657
O
ASN
A
82
3.217
−27.939
58.714
1.00
14.35
A


ATOM
658
N
VAL
A
83
3.805
−27.728
60.866
1.00
14.89
A


ATOM
659
CA
VAL
A
83
4.637
−26.556
60.596
1.00
15.18
A


ATOM
660
CB
VAL
A
83
5.025
−25.821
61.910
1.00
14.86
A


ATOM
661
CG1
VAL
A
83
6.039
−24.718
61.621
1.00
15.10
A


ATOM
662
CG2
VAL
A
83
3.783
−25.221
62.552
1.00
14.94
A


ATOM
663
C
VAL
A
83
5.909
−26.987
59.857
1.00
15.64
A


ATOM
664
O
VAL
A
83
6.543
−26.183
59.162
1.00
15.69
A


ATOM
665
N
CYS
A
84
6.270
−28.260
59.995
1.00
15.13
A


ATOM
666
CA
CYS
A
84
7.465
−28.790
59.341
1.00
16.08
A


ATOM
667
CB
CYS
A
84
8.022
−29.967
60.147
1.00
16.89
A


ATOM
668
SG
CYS
A
84
8.593
−29.490
61.809
1.00
20.29
A


ATOM
669
C
CYS
A
84
7.242
−29.216
57.889
1.00
15.77
A


ATOM
670
O
CYS
A
84
8.199
−28.479
57.164
1.00
15.77
A


ATOM
671
N
GLU
A
85
5.983
−29.294
57.470
1.00
15.87
A


ATOM
672
CA
GLU
A
85
5.658
−29.675
56.098
1.00
16.07
A


ATOM
673
CB
GLU
A
85
4.262
−30.308
56.032
1.00
16.42
A


ATOM
674
CG
GLU
A
85
4.131
−13.593
56.834
1.00
16.57
A


ATOM
675
CD
GLU
A
85
4.986
−32.721
56.280
1.00
17.93
A


ATOM
676
OE1
GLU
A
85
5.562
−33.478
57.087
1.00
17.45
A


ATOM
677
OE2
GLU
A
85
5.075
−32.860
55.041
1.00
18.39
A


ATOM
678
C
GLU
A
85
5.699
−28.430
55.222
1.00
16.50
A


ATOM
679
O
GLU
A
85
5.616
−27.316
55.727
1.00
15.38
A


ATOM
680
N
TYR
A
86
5.830
−28.612
53.910
1.00
17.34
A


ATOM
681
CA
TYR
A
86
5.874
−27.460
53.018
1.00
18.46
A


ATOM
682
CB
TYR
A
86
6.224
−27.887
51.582
1.00
19.38
A


ATOM
683
CG
TYR
A
86
6.095
−26.761
50.585
1.00
20.22
A


ATOM
684
CD1
TYR
A
86
6.856
−25.597
50.716
1.00
21.14
A


ATOM
685
CE1
TYR
A
86
6.676
−24.519
49.855
1.00
22.27
A


ATOM
686
CD2
TYR
A
86
5.155
−26.821
49.555
1.00
21.48
A


ATOM
687
CE2
TYR
A
86
4.967
−25.748
48.686
1.00
22.12
A


ATOM
688
CZ
TYR
A
86
5.727
−24.600
48.845
1.00
22.64
A


ATOM
689
OH
TYR
A
86
5.517
−23.521
48.020
1.00
23.89
A


ATOM
690
C
TYR
A
86
4.544
−26.712
53.019
1.00
18.72
A


ATOM
691
O
TYR
A
86
4.518
−25.482
53.102
1.00
18.89
A


ATOM
692
N
MET
A
87
3.441
−27.449
52.943
1.00
18.63
A


ATOM
693
CA
MET
A
87
2.128
−26.818
52.912
1.00
19.97
A


ATOM
694
CD
MET
A
87
1.734
−26.542
51.463
1.00
22.09
A


ATOM
695
CG
MET
A
87
0.665
−25.497
51.318
1.00
24.97
A


ATOM
696
SD
MET
A
87
1.405
−23.880
51.450
1.00
30.11
A


ATOM
697
CE
MET
A
87
1.541
−23.463
49.721
1.00
27.15
A


ATOM
698
C
MET
A
87
1.020
−27.639
53.574
1.00
19.37
A


ATOM
699
O
MET
A
87
0.199
−28.245
52.884
1.00
20.41
A


ATOM
700
N
ALA
A
88
0.989
−27.654
54.903
1.00
18.05
A


ATOM
701
CA
ALA
A
88
−0.033
−28.402
55.642
1.00
17.23
A


ATOM
702
CB
ALA
A
88
0.624
−29.521
56.451
1.00
17.03
A


ATOM
703
C
ALA
A
88
−0.797
−27.453
56.576
1.00
16.29
A


ATOM
704
O
ALA
A
88
−0.274
−26.407
56.952
1.00
16.42
A


ATOM
705
N
PRO
A
89
−2.043
−27.808
56.956
1.00
15.67
A


ATOM
706
CD
PRO
A
89
−2.741
−29.042
56.551
1.00
15.28
A


ATOM
707
CA
PRO
A
89
−2.894
−26.998
57.846
1.00
15.05
A


ATOM
708
CB
PRO
A
89
−4.104
−27.900
58.083
1.00
15.61
A


ATOM
709
CG
PRO
A
89
−4.184
−28.687
56.819
1.00
15.58
A


ATOM
710
C
PRO
A
89
−2.178
−26.655
59.154
1.00
14.67
A


ATOM
711
O
PRO
A
89
−1.999
−27.523
60.008
1.00
14.71
A


ATOM
712
N
SER
A
90
−1.792
−25.391
59.321
1.00
13.74
A


ATOM
713
CA
SER
A
90
−1.061
−24.990
60.526
1.00
13.11
A


ATOM
714
CB
SER
A
90
0.427
−25.292
60.326
1.00
13.29
A


ATOM
715
OG
SER
A
90
0.922
−24.652
59.149
1.00
13.45
A


ATOM
716
C
SER
A
90
−1.219
−23.527
60.950
1.00
13.09
A


ATOM
717
O
SER
A
90
−0.528
−23.066
61.866
1.00
12.71
A


ATOM
718
N
LEU
A
91
−2.125
−22.792
60.309
1.00
12.11
A


ATOM
719
CA
LEU
A
91
−2.308
−21.386
60.669
1.00
11.80
A


ATOM
720
CB
LEU
A
91
−3.361
−20.725
59.770
1.00
11.33
A


ATOM
721
CG
LEU
A
91
−3.691
−19.275
60.146
1.00
11.28
A


ATOM
722
CD1
LEU
A
91
−2.489
−18.391
59.860
1.00
10.89
A


ATOM
723
CD2
LEU
A
91
−4.913
−18.792
59.357
1.00
10.27
A


ATOM
724
C
LEU
A
91
−2.697
−21.164
62.131
1.00
11.83
A


ATOM
725
O
LEU
A
91
−2.109
−20.321
62.809
1.00
11.61
A


ATOM
726
N
ASP
A
92
−3.680
−21.917
62.622
1.00
12.12
A


ATOM
727
CA
ASP
A
92
−4.134
−21.745
64.001
1.00
12.34
A


ATOM
728
CB
ASP
A
92
−5.233
−22.771
64.340
1.00
12.99
A


ATOM
729
CG
ASP
A
92
−6.524
−22.550
63.536
1.00
14.23
A


ATOM
730
OD1
ASP
A
92
−6.606
−21.569
62.768
1.00
14.04
A


ATOM
731
OD2
ASP
A
92
−7.468
−23.362
63.677
1.00
15.03
A


ATOM
732
C
ASP
A
92
−2.996
−21.823
65.022
1.00
12.28
A


ATOM
733
O
ASP
A
92
−2.963
−21.045
65.980
1.00
12.39
A


ATOM
734
N
ALA
A
93
−2.060
−22.747
64.820
1.00
11.80
A


ATOM
735
CA
ALA
A
93
−0.931
−22.884
65.737
1.00
11.93
A


ATOM
736
CB
ALA
A
93
−0.177
−24.187
65.462
1.00
12.38
A


ATOM
737
C
ALA
A
93
0.010
−21.685
65.601
1.00
12.01
A


ATOM
738
O
ALA
A
93
0.526
−21.175
66.599
1.00
11.34
A


ATOM
739
N
ARG
A
94
0.234
−21.237
64.366
1.00
11.55
A


ATOM
740
CA
ARG
A
94
1.102
−20.084
64.120
1.00
11.09
A


ATOM
741
CB
ARG
A
94
1.325
−19.893
62.605
1.00
10.46
A


ATOM
742
CG
ARG
A
94
2.047
−21.056
61.875
1.00
10.01
A


ATOM
743
CD
ARG
A
94
1.938
−20.890
60.346
1.00
10.88
A


ATOM
744
NE
ARG
A
94
2.397
−22.036
59.544
1.00
11.13
A


ATOM
745
CZ
ARG
A
94
3.660
−22.262
59.184
1.00
12.04
A


ATOM
746
NH1
ARG
A
94
4.622
−21.427
59.553
1.00
11.41
A


ATOM
747
NH2
ARG
A
94
3.962
−23.309
58.420
1.00
10.17
A


ATOM
748
C
ARG
A
94
0.484
−18.807
64.728
1.00
11.74
A


ATOM
749
O
ARG
A
94
1.201
−17.938
65.236
1.00
12.18
A


ATOM
750
N
GLN
A
95
−0.843
−18.699
64.692
1.00
11.95
A


ATOM
751
CA
GLN
A
95
−1.524
−17.524
65.243
1.00
12.30
A


ATOM
752
CB
GLN
A
95
−3.039
−17.590
64.973
1.00
12.64
A


ATOM
753
CG
GLN
A
95
−3.438
−17.531
63.488
1.00
12.78
A


ATOM
754
CD
GLN
A
95
−3.080
−16.212
62.812
1.00
13.00
A


ATOM
755
OE1
GLN
A
95
−1.934
−15.765
62.861
1.00
11.99
A


ATOM
756
NE2
GLN
A
95
−4.067
−15.587
62.170
1.00
12.04
A


ATOM
757
C
GLN
A
95
−1.275
−17.390
66.745
1.00
12.26
A


ATOM
758
O
GLN
A
95
−1.037
−16.287
67.243
1.00
11.48
A


ATOM
759
N
ALA
A
96
−1.324
−18.511
67.463
1.00
12.75
A


ATOM
760
CA
ALA
A
96
−1.099
−18.502
68.908
1.00
12.75
A


ATOM
761
CB
ALA
A
96
−1.407
−19.883
69.503
1.00
12.71
A


ATOM
762
C
ALA
A
96
0.331
−18.085
69.244
1.00
12.95
A


ATOM
763
O
ALA
A
96
0.563
−17.420
70.260
1.00
13.08
A


ATOM
764
N
MET
A
97
1.284
−18.462
68.389
1.00
12.73
A


ATOM
765
CA
MET
A
97
2.691
−18.112
68.596
1.00
12.42
A


ATOM
766
CB
MET
A
97
3.597
−18.849
67.596
1.00
12.18
A


ATOM
767
CG
MET
A
97
3.612
−20.371
67.718
1.00
11.76
A


ATOM
768
SD
MET
A
97
4.617
−21.149
66.408
1.00
13.63
A


ATOM
769
CE
MET
A
97
4.109
−22.880
66.555
1.00
12.10
A


ATOM
770
C
MET
A
97
2.899
−16.609
68.423
1.00
12.57
A


ATOM
771
O
MET
A
97
3.570
−15.962
69.236
1.00
12.06
A


ATOM
772
N
LEU
A
98
2.328
−16.062
67.354
1.00
11.79
A


ATOM
773
CA
LEU
A
98
2.452
−14.634
67.063
1.00
12.16
A


ATOM
774
CB
LEU
A
98
1.854
−14.324
65.684
1.00
11.36
A


ATOM
775
CG
LEU
A
98
2.512
−15.031
64.496
1.00
12.62
A


ATOM
776
CD1
LEU
A
98
1.679
−14.830
63.227
1.00
12.76
A


ATOM
777
CD2
LEU
A
98
3.921
−14.487
64.305
1.00
12.27
A


ATOM
778
C
LEU
A
98
1.763
−13.770
68.111
1.00
11.92
A


ATOM
779
O
LEU
A
98
2.257
−12.695
68.460
1.00
12.04
A


ATOM
780
N
ALA
A
99
0.621
−14.237
68.606
1.00
12.12
A


ATOM
781
CA
ALA
A
99
−0.144
−13.492
69.602
1.00
12.56
A


ATOM
782
CB
ALA
A
99
−1.389
−14.288
70.020
1.00
12.39
A


ATOM
783
C
ALA
A
99
0.695
−13.155
70.827
1.00
13.30
A


ATOM
784
O
ALA
A
99
0.474
−12.132
71.475
1.00
12.88
A


ATOM
785
N
MET
A
100
1.660
−14.016
71.134
1.00
14.50
A


ATOM
786
CA
MET
A
100
2.537
−13.818
72.285
1.00
15.61
A


ATOM
787
CB
MET
A
100
2.832
−15.168
72.952
1.00
17.98
A


ATOM
788
CG
MET
A
100
3.608
−15.105
74.281
1.00
21.83
A


ATOM
789
SD
MET
A
100
5.365
−14.630
74.196
1.00
26.83
A


ATOM
790
CE
MET
A
100
6.114
−16.169
73.669
1.00
24.50
A


ATOM
791
C
MET
A
100
3.862
−13.135
71.932
1.00
15.20
A


ATOM
792
O
MET
A
100
4.217
−12.113
72.520
1.00
15.12
A


ATOM
793
N
GLU
A
101
4.577
−13.687
70.958
1.00
13.89
A


ATOM
794
CA
GLU
A
101
5.890
−13.163
70.586
1.00
13.45
A


ATOM
795
CB
GLU
A
101
6.616
−14.187
69.713
1.00
13.61
A


ATOM
796
CG
GLU
A
101
8.094
−13.880
69.475
1.00
13.97
A


ATOM
797
CD
GLU
A
101
8.942
−13.936
70.741
1.00
14.80
A


ATOM
798
OE1
GLU
A
101
8.422
−14.335
71.808
1.00
15.03
A


ATOM
799
OE2
GLU
A
101
10.143
−13.584
70.666
1.00
14.42
A


ATOM
800
C
GLU
A
101
5.980
−11.778
69.933
1.00
13.03
A


ATOM
801
O
GLU
A
101
6.860
−10.993
70.286
1.00
11.63
A


ATOM
802
N
VAL
A
102
5.097
−11.469
68.985
1.00
12.32
A


ATOM
803
CA
VAL
A
102
5.160
−10.161
68.340
1.00
12.06
A


ATOM
804
CB
VAL
A
102
4.054
−10.002
67.271
1.00
12.10
A


ATOM
805
CG1
VAL
A
102
4.043
−8.579
66.730
1.00
12.24
A


ATOM
806
CG2
VAL
A
102
4.312
−10.982
66.120
1.00
12.82
A


ATOM
807
C
VAL
A
102
5.071
−9.035
69.378
1.00
12.40
A


ATOM
808
O
VAL
A
102
5.911
−8.135
69.388
1.00
12.03
A


ATOM
809
N
PRO
A
103
4.061
−9.072
70.268
1.00
12.59
A


ATOM
810
CD
PRO
A
103
2.862
−9.928
70.270
1.00
12.42
A


ATOM
811
CA
PRO
A
103
3.942
−8.020
71.284
1.00
12.41
A


ATOM
812
CB
PRO
A
103
2.585
−8.312
71.931
1.00
13.58
A


ATOM
813
CG
PRO
A
103
1.819
−9.000
70.828
1.00
13.22
A


ATOM
814
C
PRO
A
103
5.085
−8.056
72.312
1.00
12.46
A


ATOM
815
O
PRO
A
103
5.570
−7.008
72.748
1.00
11.92
A


ATOM
816
N
ARG
A
104
5.512
−9.256
72.705
1.00
12.35
A


ATOM
817
CA
ARG
A
104
6.593
−9.376
73.691
1.00
12.83
A


ATOM
818
CB
ARG
A
104
6.830
−10.841
74.073
1.00
13.38
A


ATOM
819
CG
ARG
A
104
7.824
−11.005
75.233
1.00
14.51
A


ATOM
820
CD
ARG
A
104
8.463
−12.393
75.252
1.00
15.96
A


ATOM
821
NE
ARG
A
104
9.362
−12.594
74.116
1.00
17.99
A


ATOM
822
CZ
ARG
A
104
10.561
−12.031
73.994
1.00
19.06
A


ATOM
823
NH1
ARG
A
104
11.025
−11.228
74.946
1.00
19.58
A


ATOM
824
NH2
ARG
A
104
11.295
−12.260
72.911
1.00
19.03
A


ATOM
825
C
ARG
A
104
7.907
−8.789
73.179
1.00
12.54
A


ATOM
826
O
ARG
A
104
8.559
−8.002
73.867
1.00
12.97
A


ATOM
827
N
LEU
A
105
8.297
−9.190
71.972
1.00
12.55
A


ATOM
828
CA
LEU
A
105
9.532
−8.722
71.356
1.00
12.96
A


ATOM
829
CB
LEU
A
105
9.768
−9.491
70.047
1.00
13.70
A


ATOM
830
CG
LEU
A
105
11.113
−9.417
69.327
1.00
15.14
A


ATOM
831
CD1
LEU
A
105
12.227
−9.949
70.231
1.00
14.66
A


ATOM
832
CD2
LEU
A
105
11.028
−10.247
68.034
1.00
14.82
A


ATOM
833
C
LEU
A
105
9.454
−7.219
71.094
1.00
12.85
A


ATOM
834
O
LEU
A
105
10.436
−6.494
71.271
1.00
12.86
A


ATOM
835
N
GLY
A
106
8.278
−6.754
70.675
1.00
12.06
A


ATOM
836
CA
GLY
A
106
8.086
−5.337
70.412
1.00
11.77
A


ATOM
837
C
GLY
A
106
8.215
−4.504
71.675
1.00
11.78
A


ATOM
838
O
GLY
A
106
8.767
−3.405
71.648
1.00
11.19
A


ATOM
839
N
LYS
A
107
7.710
−5.025
72.790
1.00
11.65
A


ATOM
840
CA
LYS
A
107
7.800
−4.312
74.060
1.00
12.93
A


ATOM
841
CB
LYS
A
107
6.993
−5.029
75.145
1.00
14.06
A


ATOM
842
CG
LYS
A
107
6.987
−4.280
76.465
1.00
15.87
A


ATOM
843
CD
LYS
A
107
7.048
−5.223
77.649
1.00
17.85
A


ATOM
844
CE
LYS
A
107
7.068
−4.444
78.954
1.00
19.08
A


ATOM
845
NZ
LYS
A
107
7.304
−5.335
80.128
1.00
21.55
A


ATOM
846
C
LYS
A
107
9.255
−4.203
74.520
1.00
13.01
A


ATOM
847
O
LYS
A
107
9.664
−3.180
75.067
1.00
13.04
A


ATOM
848
N
GLU
A
108
10.034
−5.260
74.302
1.00
13.42
A


ATOM
849
CA
GLU
A
108
11.441
−5.264
74.702
1.00
13.99
A


ATOM
850
CB
GLU
A
108
12.081
−6.618
74.360
1.00
15.13
A


ATOM
851
CG
GLU
A
108
13.507
−6.782
74.851
1.00
16.71
A


ATOM
852
CD
GLU
A
108
14.044
−8.195
74.660
1.00
17.86
A


ATOM
853
OE1
GLU
A
108
15.250
−8.408
74.910
1.00
18.93
A


ATOM
854
OE2
GLU
A
108
13.265
−9.088
74.267
1.00
16.99
A


ATOM
855
C
GLU
A
108
12.208
−4.122
74.019
1.00
13.77
A


ATOM
856
O
GLU
A
108
13.015
−3.433
74.651
1.00
13.37
A


ATOM
857
N
ALA
A
109
11.954
−3.922
72.728
1.00
12.99
A


ATOM
858
CA
ALA
A
109
12.618
−2.855
71.981
1.00
12.44
A


ATOM
859
CB
ALA
A
109
12.370
−3.027
70.494
1.00
11.96
A


ATOM
860
C
ALA
A
109
12.105
−1.491
72.440
1.00
12.31
A


ATOM
861
O
ALA
A
109
12.881
−0.543
72.595
1.00
11.79
A


ATOM
862
N
ALA
A
110
10.796
−1.400
72.657
1.00
11.92
A


ATOM
863
CA
ALA
A
110
10.170
−0.154
73.093
1.00
12.92
A


ATOM
864
CB
ALA
A
110
8.655
−0.335
73.173
1.00
12.53
A


ATOM
865
C
ALA
A
110
10.712
0.332
74.440
1.00
13.13
A


ATOM
866
O
ALA
A
110
10.938
1.528
74.632
1.00
13.01
A


ATOM
867
N
VAL
A
111
10.923
−0.592
75.371
1.00
13.59
A


ATOM
868
CA
VAL
A
111
11.442
−0.219
76.683
1.00
14.30
A


ATOM
869
CB
VAL
A
111
11.512
−1.445
77.632
1.00
14.16
A


ATOM
870
CG1
VAL
A
111
12.249
−1.073
78.921
1.00
14.90
A


ATOM
871
CG2
VAL
A
111
10.102
−1.915
77.972
1.00
14.85
A


ATOM
872
C
VAL
A
111
12.830
0.412
76.549
1.00
14.57
A


ATOM
873
O
VAL
A
111
13.140
1.393
77.232
1.00
14.48
A


ATOM
874
N
LYS
A
112
13.655
−0.140
75.660
1.00
14.33
A


ATOM
875
CA
LYS
A
112
15.003
−0.382
75.439
1.00
14.52
A


ATOM
876
CB
LYS
A
112
15.803
−0.550
74.522
1.00
15.84
A


ATOM
877
CG
LYS
A
112
16.113
−1.911
75.118
1.00
17.43
A


ATOM
878
CD
LYS
A
112
16.934
−2.747
74.147
1.00
18.69
A


ATOM
879
CE
LYS
A
112
17.182
−4.137
74.687
1.00
19.96
A


ATOM
880
NZ
LYS
A
112
17.933
−4.976
73.708
1.00
20.59
A


ATOM
881
C
LYS
A
112
14.973
1.783
74.829
1.00
14.19
A


ATOM
882
O
LYS
A
112
15.771
2.645
75.198
1.00
13.66
A


ATOM
883
N
ALA
A
113
14.054
2.008
73.894
1.00
13.82
A


ATOM
884
CA
ALA
A
113
13.935
3.316
73.252
1.00
13.94
A


ATOM
885
CB
ALA
A
113
12.985
3.227
72.039
1.00
13.86
A


ATOM
886
C
ALA
A
113
13.443
4.384
74.235
1.00
13.81
A


ATOM
887
O
ALA
A
113
13.923
5.519
74.228
1.00
13.80
A


ATOM
888
N
ILE
A
114
12.492
4.014
75.085
1.00
13.62
A


ATOM
889
CA
ILE
A
114
11.939
4.938
76.067
1.00
14.81
A


ATOM
890
CB
ILE
A
114
10.690
4.325
76.751
1.00
14.96
A


ATOM
891
CG2
ILE
A
114
10.205
5.229
77.874
1.00
15.35
A


ATOM
892
CG1
ILE
A
114
9.592
4.106
75.702
1.00
15.11
A


ATOM
893
CD1
ILE
A
114
8.359
3.358
76.211
1.00
14.83
A


ATOM
894
C
ILE
A
114
12.993
5.301
77.118
1.00
15.14
A


ATOM
895
O
ILE
A
114
13.031
6.430
77.607
1.00
14.81
A


ATOM
896
N
LYS
A
115
13.851
4.341
77.452
1.00
15.95
A


ATOM
897
CA
LYS
A
115
14.915
4.572
78.427
1.00
17.10
A


ATOM
898
CB
LYS
A
115
15.664
3.264
78.723
1.00
18.03
A


ATOM
899
CG
LYS
A
115
16.793
3.422
79.732
1.00
20.46
A


ATOM
900
CD
LYS
A
115
17.665
2.176
79.815
1.00
22.06
A


ATOM
901
CE
LYS
A
115
18.867
2.413
80.730
1.00
24.19
A


ATOM
902
NZ
LYS
A
115
19.768
1.230
80.814
1.00
24.53
A


ATOM
903
C
LYS
A
115
15.896
5.615
77.882
1.00
16.58
A


ATOM
904
O
LYS
A
115
16.293
6.536
78.596
1.00
16.08
A


ATOM
905
N
GLU
A
116
16.282
5.470
76.615
1.00
15.74
A


ATOM
906
CA
GLU
A
116
17.209
6.413
75.989
1.00
15.99
A


ATOM
907
CB
GLU
A
116
17.559
5.973
74.563
1.00
15.39
A


ATOM
908
CG
GLU
A
116
18.606
6.860
73.895
1.00
16.97
A


ATOM
909
CD
GLU
A
116
18.736
6.634
72.392
1.00
17.20
A


ATOM
910
OE1
GLU
A
116
18.375
5.542
71.907
1.00
16.77
A


ATOM
911
OE2
CLU
A
116
19.219
7.553
71.694
1.00
17.90
A


ATOM
912
C
GLU
A
116
16.576
7.807
75.935
1.00
16.26
A


ATOM
913
O
GLU
A
116
17.223
8.811
76.250
1.00
15.55
A


ATOM
914
N
TRP
A
117
15.312
7.853
75.520
1.00
16.06
A


ATOM
915
CA
TRP
A
117
14.561
9.102
75.424
1.00
16.63
A


ATOM
916
CB
TRP
A
117
13.113
8.792
75.026
1.00
15.45
A


ATOM
917
CG
TRP
A
117
12.222
9.992
74.851
1.00
15.18
A


ATOM
918
CD2
TRP
A
117
10.815
10.061
75.130
1.00
14.59
A


ATOM
919
CE2
TRP
A
117
10.372
11.344
74.735
1.00
14.57
A


ATOM
920
CE3
TRP
A
117
9.885
9.162
75.672
1.00
14.93
A


ATOM
921
CD1
TRP
A
117
12.565
11.204
74.320
1.00
14.39
A


ATOM
922
NE1
TRP
A
117
11.459
12.019
74.246
1.00
14.28
A


ATOM
923
CZ2
TRP
A
117
9.038
11.752
74.864
1.00
14.45
A


ATOM
924
CZ3
TRP
A
117
8.555
9.569
75.801
1.00
14.58
A


ATOM
925
CH2
TRP
A
117
8.147
10.852
75.397
1.00
14.55
A


ATOM
926
C
TRP
A
117
14.615
9.836
76.765
1.00
17.46
A


ATOM
927
O
TRP
A
117
14.919
11.026
76.812
1.00
17.93
A


ATOM
928
N
GLY
A
118
14.322
9.120
77.848
1.00
18.47
A


ATOM
929
CA
GLY
A
118
14.375
9.713
79.175
1.00
19.45
A


ATOM
930
C
GLY
A
118
13.121
10.377
79.724
1.00
20.29
A


ATOM
931
O
GLY
A
118
13.110
10.800
80.883
1.00
20.22
A


ATOM
932
N
GLN
A
119
12.066
10.489
78.918
1.00
20.22
A


ATOM
933
CA
GLN
A
119
10.825
11.100
79.363
1.00
20.78
A


ATOM
934
CB
GLN
A
119
10.282
12.014
78.257
1.00
21.39
A


ATOM
935
CG
GLN
A
119
11.219
13.173
77.913
1.00
23.09
A


ATOM
936
CD
GLN
A
119
11.655
13.958
79.146
1.00
23.77
A


ATOM
937
OE1
GLN
A
119
10.824
14.468
79.899
1.00
24.98
A


ATOM
938
NE2
GLN
A
119
12.962
14.050
79.357
1.00
24.40
A


ATOM
939
C
GLN
A
119
9.763
10.079
79.782
1.00
20.88
A


ATOM
940
O
GLN
A
119
9.859
8.903
79.443
1.00
20.86
A


ATOM
941
N
PRO
A
120
8.733
10.524
80.525
1.00
21.16
A


ATOM
942
CD
PRO
A
120
8.517
11.921
80.939
1.00
21.29
A


ATOM
943
CA
PRO
A
120
7.641
9.667
81.008
1.00
21.57
A


ATOM
944
CB
PRO
A
120
6.746
10.643
81.772
1.00
21.80
A


ATOM
945
CG
PRO
A
120
7.677
11.753
82.165
1.00
22.42
A


ATOM
946
C
PRO
A
120
6.877
8.983
79.873
1.00
21.27
A


ATOM
947
O
PRO
A
120
6.608
9.607
78.851
1.00
21.61
A


ATOM
948
N
LYS
A
121
6.519
7.714
80.056
1.00
21.35
A


ATOM
949
CA
LYS
A
121
5.777
6.977
79.029
1.00
21.42
A


ATOM
950
CB
LYS
A
121
5.623
5.501
79.421
1.00
22.56
A


ATOM
951
CG
LYS
A
121
4.759
5.288
80.654
1.00
25.13
A


ATOM
952
CD
LYS
A
121
4.399
3.822
80.900
1.00
26.18
A


ATOM
953
CE
LYS
A
121
5.619
2.984
81.222
1.00
27.36
A


ATOM
954
NZ
LYS
A
121
5.225
1.655
81.786
1.00
28.12
A


ATOM
955
C
LYS
A
121
4.392
7.595
78.840
1.02
20.94
A


ATOM
956
O
LYS
A
121
3.762
7.429
77.791
1.00
20.02
A


ATOM
957
N
SER
A
122
3.928
8.309
79.863
1.00
19.98
A


ATOM
958
CA
SER
A
122
2.621
8.956
79.836
1.00
19.81
A


ATOM
959
CB
SER
A
122
2.252
9.457
81.236
1.00
20.86
A


ATOM
960
OG
SER
A
122
3.131
10.488
81.656
1.00
20.86
A


ATOM
961
C
SER
A
122
2.580
10.121
78.856
1.00
19.21
A


ATOM
962
O
SER
A
122
1.508
10.633
78.533
1.00
19.72
A


ATOM
963
N
LYS
A
123
3.748
10.540
78.380
1.00
18.76
A


ATOM
964
CA
LYS
A
123
3.819
11.646
77.435
1.00
17.51
A


ATOM
965
CB
LYS
A
123
5.069
12.486
77.715
1.00
19.70
A


ATOM
966
CG
LYS
A
123
5.096
13.004
79.157
1.00
21.88
A


ATOM
967
CD
LYS
A
123
6.289
13.894
79.465
1.00
24.26
A


ATOM
968
CE
LYS
A
123
6.204
15.233
78.751
1.00
25.53
A


ATOM
969
NZ
LYS
A
123
7.195
16.202
79.318
1.00
26.85
A


ATOM
970
C
LYS
A
123
3.782
11.179
75.975
1.00
16.02
A


ATOM
971
O
LYS
A
123
3.874
11.990
75.056
1.00
15.29
A


ATOM
972
N
ILE
A
124
3.649
9.871
75.767
1.00
14.24
A


ATOM
973
CA
ILE
A
124
3.551
9.326
74.413
1.00
13.14
A


ATOM
974
CB
ILE
A
124
3.949
7.828
74.370
1.00
13.63
A


ATOM
975
CG2
ILE
A
124
3.612
7.235
73.000
1.00
13.42
A


ATOM
976
CG1
ILE
A
124
5.451
7.685
74.668
1.00
13.73
A


ATOM
977
CD1
ILE
A
124
5.932
6.250
74.850
1.00
14.46
A


ATOM
978
C
ILE
A
124
2.084
9.503
74.016
1.00
12.41
A


ATOM
979
O
ILE
A
124
1.184
9.010
74.695
1.00
12.34
A


ATOM
980
N
THR
A
125
1.853
10.219
72.922
1.00
11.64
A


ATOM
981
CA
THR
A
125
0.499
10.515
72.451
1.00
10.75
A


ATOM
982
CB
THR
A
125
0.409
11.975
71.989
1.00
9.91
A


ATOM
983
OG1
THR
A
125
1.357
12.196
70.937
1.00
10.98
A


ATOM
984
CG2
THR
A
125
0.714
12.921
73.147
1.00
10.30
A


ATOM
985
C
THR
A
125
−0.030
9.639
71.313
1.00
10.65
A


ATOM
986
O
THR
A
125
−1.249
9.502
71.150
1.00
10.36
A


ATOM
987
N
HIS
A
126
0.877
9.078
70.516
1.00
10.15
A


ATOM
988
CA
HIS
A
126
0.494
8.223
69.389
1.00
9.76
A


ATOM
989
CB
HIS
A
126
0.735
8.936
68.047
1.00
9.29
A


ATOM
990
CG
HIS
A
126
−0.054
10.195
67.858
1.00
9.51
A


ATOM
991
CD2
HIS
A
126
−1.047
10.498
66.987
1.00
10.73
A


ATOM
992
ND1
HIS
A
126
0.185
11.346
68.580
1.00
9.94
A


ATOM
993
CE1
HIS
A
126
−0.624
12.303
68.159
1.00
10.59
A


ATOM
994
NE2
HIS
A
126
−1.381
11.815
67.193
1.00
10.64
A


ATOM
995
C
HIS
A
126
1.329
6.935
69.390
1.00
9.52
A


ATOM
996
O
HIS
A
126
2.463
6.926
69.870
1.00
9.39
A


ATOM
997
N
LEU
A
127
0.770
5.865
68.826
1.00
8.68
A


ATOM
998
CA
LEU
A
127
1.457
4.577
68.741
1.00
8.66
A


ATOM
999
CB
LEU
A
127
0.943
3.615
69.820
1.00
8.64
A


ATOM
1000
CG
LEU
A
127
1.448
2.167
69.722
1.00
9.47
A


ATOM
1001
CD1
LEU
A
127
2.954
2.119
69.949
1.00
9.18
A


ATOM
1002
CD2
LEU
A
127
0.728
1.298
70.748
1.00
9.28
A


ATOM
1003
C
LEU
A
127
1.243
3.927
67.379
1.00
8.85
A


ATOM
1004
O
LEU
A
127
0.107
3.737
66.956
1.00
7.92
A


ATOM
1005
N
ILE
A
128
2.339
3.580
66.710
1.00
8.63
A


ATOM
1006
CA
ILE
A
128
2.280
2.921
65.407
1.00
8.91
A


ATOM
1007
CB
ILE
A
128
3.054
3.717
64.324
1.00
8.76
A


ATOM
1008
CG2
ILE
A
128
3.053
2.942
63.007
1.00
9.37
A


ATOM
1009
CG1
ILE
A
128
2.436
5.110
64.144
1.00
8.68
A


ATOM
1010
CD1
ILE
A
128
3.161
5.984
63.137
1.00
8.20
A


ATOM
1011
C
ILE
A
128
2.950
1.551
65.541
1.00
9.26
A


ATOM
1012
O
ILE
A
128
4.142
1.477
65.847
1.00
9.52
A


ATOM
1013
N
VAL
A
129
2.195
0.475
65.329
1.00
9.33
A


ATOM
1014
CA
VAL
A
129
2.768
−0.872
65.408
1.00
9.83
A


ATOM
1015
CB
VAL
A
129
2.095
−1.728
66.500
1.00
9.91
A


ATOM
1016
CG1
VAL
A
129
2.655
−3.151
66.465
1.00
9.78
A


ATOM
1017
CG2
VAL
A
129
2.342
−1.099
67.873
1.00
8.95
A


ATOM
1018
C
VAL
A
129
2.621
−1.571
64.063
1.00
10.19
A


ATOM
1019
O
VAL
A
129
1.524
−1.638
63.504
1.00
10.94
A


ATOM
1020
N
CYS
A
130
3.739
−2.089
63.561
1.00
10.12
A


ATOM
1021
CA
CYS
A
130
3.803
−2.765
62.268
1.00
10.10
A


ATOM
1022
CB
CYS
A
130
4.696
−1.946
61.328
1.00
10.57
A


ATOM
1023
SG
CYS
A
130
5.174
−2.737
59.758
1.00
12.03
A


ATOM
1024
C
CYS
A
130
4.343
−4.194
62.363
1.00
9.44
A


ATOM
1025
O
CYS
A
130
5.309
−4.455
63.078
1.00
9.20
A


ATOM
1026
N
SER
A
131
3.702
−5.109
61.641
1.00
8.71
A


ATOM
1027
CA
SER
A
131
4.117
−6.516
61.579
1.00
9.13
A


ATOM
1028
CB
SER
A
131
3.590
−7.297
62.788
1.00
9.14
A


ATOM
1029
OG
SER
A
131
4.170
−8.592
62.834
1.00
8.81
A


ATOM
1030
C
SER
A
131
3.535
−7.098
60.293
1.00
9.18
A


ATOM
1031
O
SER
A
131
2.451
−6.699
59.878
1.00
9.08
A


ATOM
1032
N
THR
A
132
4.246
−8.028
59.655
1.00
10.48
A


ATOM
1033
CA
THR
A
132
3.754
−8.620
58.411
1.00
10.93
A


ATOM
1034
CB
THR
A
132
4.689
−9.774
57.941
1.00
11.08
A


ATOM
1035
OG1
THR
A
132
5.988
−9.232
57.654
1.00
10.58
A


ATOM
1036
CG2
THR
A
132
4.150
−10.437
56.675
1.00
11.82
A


ATOM
1037
C
THR
A
132
2.294
−9.089
58.544
1.00
11.41
A


ATOM
1038
O
THR
A
132
1.505
−8.928
57.607
1.00
11.93
A


ATOM
1039
N
THR
A
133
1.928
−9.647
59.701
1.00
11.44
A


ATOM
1040
CA
THR
A
133
0.541
−10.075
59.960
1.00
11.06
A


ATOM
1041
CB
THR
A
133
0.301
−11.586
59.681
1.00
12.44
A


ATOM
1042
OG1
THR
A
133
0.982
−12.371
60.675
1.00
12.81
A


ATOM
1043
CG2
THR
A
133
0.798
−11.975
58.292
1.00
12.09
A


ATOM
1044
C
THR
A
133
0.171
−9.867
61.432
1.00
11.34
A


ATOM
1045
O
THR
A
133
1.038
−9.591
62.262
1.00
10.26
A


ATOM
1046
N
THR
A
134
−1.121
−9.972
61.741
1.00
10.39
A


ATOM
1047
CA
THR
A
134
−1.599
−9.886
63.127
1.00
10.86
A


ATOM
1048
CB
THR
A
134
−2.151
−8.478
63.490
1.00
10.72
A


ATOM
1049
OG1
THR
A
134
−2.068
−8.297
64.913
1.00
10.97
A


ATOM
1050
CG2
THR
A
134
−3.595
−8.310
63.049
1.00
9.79
A


ATOM
1051
C
THR
A
134
−2.681
−10.973
63.214
1.00
10.76
A


ATOM
1052
O
THR
A
134
−3.493
−11.124
62.307
1.00
10.88
A


ATOM
1053
N
PRO
A
135
−2.696
−11.753
64.305
1.00
10.68
A


ATOM
1054
CD
PRO
A
135
−1.766
−11.689
65.450
1.00
10.93
A


ATOM
1055
CA
PRO
A
135
−3.665
−12.840
64.483
1.00
11.06
A


ATOM
1056
CB
PRO
A
135
−2.969
−13.736
65.502
1.00
10.76
A


ATOM
1057
CG
PRO
A
135
−2.338
−12.722
66.415
1.00
10.45
A


ATOM
1058
C
PRO
A
135
−5.105
−12.568
64.890
1.00
11.42
A


ATOM
1059
O
PRO
A
135
−5.999
−13.341
64.538
1.00
11.28
A


ATOM
1060
N
ASP
A
136
−5.352
−11.481
65.608
1.00
11.37
A


ATOM
1061
CA
ASP
A
136
−6.704
−11.235
66.091
1.00
12.18
A


ATOM
1062
CB
ASP
A
136
−6.774
−11.593
67.587
1.00
13.43
A


ATOM
1063
CG
ASP
A
136
−6.122
−12.935
67.916
1.00
14.45
A


ATOM
1064
OD1
ASP
A
136
−5.193
−12.973
68.762
1.00
13.87
A


ATOM
1065
OD2
ASP
A
136
−6.544
−13.955
67.343
1.00
14.97
A


ATOM
1066
C
ASP
A
136
−7.199
−9.802
65.942
1.00
12.49
A


ATOM
1067
O
ASP
A
136
−6.625
−8.983
65.225
1.00
12.60
A


ATOM
1068
N
LEU
A
137
−8.310
−9.546
66.627
1.00
12.88
A


ATOM
1069
CA
LEU
A
137
−8.924
−8.230
66.740
1.00
13.15
A


ATOM
1070
CB
LEU
A
137
−10.244
−8.126
65.967
1.00
13.24
A


ATOM
1071
CG
LEU
A
137
−10.145
−7.967
64.450
1.00
13.68
A


ATOM
1072
CD1
LEU
A
137
−10.283
−9.326
63.798
1.00
14.40
A


ATOM
1073
CD2
LEU
A
137
−11.235
−7.023
63.957
1.00
14.51
A


ATOM
1074
C
LEU
A
137
−9.212
−8.202
68.231
1.00
13.21
A


ATOM
1075
O
LEU
A
137
−9.906
−9.080
68.741
1.00
13.93
A


ATOM
1076
N
PRO
A
138
−8.660
−7.225
66.963
1.00
13.99
A


ATOM
1077
CD
PRO
A
138
−8.996
−7.174
70.396
1.00
14.42
A


ATOM
1078
CA
PRO
A
138
−7.780
−6.107
68.602
1.00
13.83
A


ATOM
1079
CB
PRO
A
138
−7.565
−5.401
69.941
1.00
14.52
A


ATOM
1080
CG
PRO
A
138
−8.802
−5.728
70.705
1.00
14.81
A


ATOM
1081
C
PRO
A
138
−6.444
−6.511
67.956
1.00
14.18
A


ATOM
1082
O
PRO
A
138
−5.955
−7.621
68.166
1.00
13.48
A


ATOM
1083
N
GLY
A
139
−5.872
−5.598
67.170
1.00
13.47
A


ATOM
1084
CA
GLY
A
139
−4.596
−5.841
66.515
1.00
13.68
A


ATOM
1085
C
GLY
A
139
−3.441
−5.742
67.504
1.00
13.10
A


ATOM
1086
O
GLY
A
139
−3.664
−5.427
68.668
1.00
13.23
A


ATOM
1087
N
ALA
A
140
−2.212
−5.995
67.056
1.00
12.38
A


ATOM
1088
CA
ALA
A
140
−1.056
−5.938
67.961
1.00
12.40
A


ATOM
1089
CB
ALA
A
140
0.216
−6.393
67.236
1.00
10.91
A


ATOM
1090
C
ALA
A
140
−0.823
−4.568
68.611
1.00
12.51
A


ATOM
1091
O
ALA
A
140
−0.152
−4.483
69.643
1.00
12.15
A


ATOM
1092
N
ASP
A
141
−1.359
−3.499
68.024
1.00
12.33
A


ATOM
1093
CA
ASP
A
141
−1.191
−2.173
68.622
1.00
12.63
A


ATOM
1094
CB
ASP
A
141
−1.785
−1.081
67.724
1.00
13.06
A


ATOM
1095
CG
ASP
A
141
−3.207
−1.384
67.287
1.00
13.39
A


ATOM
1096
OD1
ASP
A
141
−3.413
−2.385
66.564
1.00
13.50
A


ATOM
1097
OD2
ASP
A
141
−4.119
−0.618
67.661
1.00
13.61
A


ATOM
1098
C
ASP
A
141
−1.856
−2.140
70.000
1.00
12.86
A


ATOM
1099
O
ASP
A
141
−1.319
−1.562
70.948
1.00
12.35
A


ATOM
1100
N
TYR
A
142
−3.022
−2.774
70.110
1.00
13.35
A


ATOM
1101
CA
TYR
A
142
−3.747
−2.836
71.377
1.00
13.60
A


ATOM
1102
CB
TYR
A
142
−5.090
−3.549
71.182
1.00
14.21
A


ATOM
1103
CG
TYR
A
142
−5.781
−3.900
72.478
1.00
15.51
A


ATOM
1104
CD1
TYR
A
142
−6.503
−2.943
73.193
1.00
15.93
A


ATOM
1105
CE1
TYR
A
142
−7.110
−3.262
74.411
1.00
17.60
A


ATOM
1106
CD2
TYR
A
142
−5.680
−5.184
73.012
1.00
16.59
A


ATOM
1107
CE2
TYR
A
142
−6.275
−5.509
74.224
1.00
17.58
A


ATOM
1108
CZ
TYR
A
142
−6.988
−4.549
74.917
1.00
18.62
A


ATOM
1109
OH
TYR
A
142
−7.587
−4.890
76.112
1.00
20.44
A


ATOM
1110
C
TYR
A
142
−2.932
−3.584
72.441
1.00
13.98
A


ATOM
1111
O
TYR
A
142
−2.773
−3.108
73.572
1.00
13.20
A


ATOM
1112
N
GLN
A
143
−2.420
−4.757
72.080
1.00
14.49
A


ATOM
1113
CA
GLN
A
143
−1.635
−5.551
73.023
1.00
15.02
A


ATOM
1114
CB
GLN
A
143
−1.239
−6.896
72.403
1.00
16.02
A


ATOM
1115
CG
GLN
A
143
−2.406
−7.861
72.183
1.00
17.48
A


ATOM
1116
CD
GLN
A
143
−3.193
−8.148
73.455
1.00
18.91
A


ATOM
1117
OE1
GLN
A
143
−2.621
−8.294
74.539
1.00
18.85
A


ATOM
1118
NE2
GLN
A
143
−4.515
−8.246
73.324
1.00
20.56
A


ATOM
1119
C
GLN
A
143
−0.385
−4.824
73.518
1.00
15.31
A


ATOM
1120
O
GLN
A
143
−0.047
−4.908
74.703
1.00
15.22
A


ATOM
1121
N
LEU
A
144
0.303
−4.113
72.626
1.00
14.97
A


ATOM
1122
CA
LEU
A
144
1.506
−3.385
73.032
1.00
15.35
A


ATOM
1123
CB
LEU
A
144
2.189
−2.716
71.832
1.00
16.16
A


ATOM
1124
CG
LEU
A
144
3.669
−3.050
71.600
1.00
17.50
A


ATOM
1125
CD1
LEU
A
144
4.321
−1.918
70.822
1.00
18.53
A


ATOM
1126
CD2
LEU
A
144
4.399
−3.242
72.926
1.00
18.13
A


ATOM
1127
C
LEU
A
144
1.150
−2.317
74.061
1.00
15.11
A


ATOM
1128
O
LEU
A
144
1.880
−2.110
75.030
1.00
14.55
A


ATOM
1129
N
THR
A
145
0.030
−1.635
73.838
1.00
14.64
A


ATOM
1130
CA
THR
A
145
−0.442
−0.599
74.752
1.00
15.04
A


ATOM
1131
CB
THR
A
145
−1.769
0.018
74.258
1.00
15.52
A


ATOM
1132
OG1
THR
A
145
−1.544
0.707
73.023
1.00
15.30
A


ATOM
1133
CG2
THR
A
145
−2.325
0.993
75.288
1.00
15.63
A


ATOM
1134
C
THR
A
145
−0.678
−1.215
76.130
1.00
15.20
A


ATOM
1135
O
THR
A
145
−0.310
−0.640
77.156
1.00
14.90
A


ATOM
1136
N
LYS
A
146
−1.296
−2.392
76.138
1.00
15.71
A


ATOM
1137
CA
LYS
A
146
−1.587
−3.116
77.374
1.00
16.56
A


ATOM
1138
CB
LYS
A
146
−2.469
−4.325
77.054
1.00
17.61
A


ATOM
1139
CG
LYS
A
146
−2.785
−5.242
78.232
1.00
19.39
A


ATOM
1140
CD
LYS
A
146
−3.567
−6.463
77.745
1.00
21.39
A


ATOM
1141
CE
LYS
A
146
−3.488
−7.618
78.725
1.00
22.15
A


ATOM
1142
NZ
LYS
A
146
−4.011
−8.877
78.116
1.00
23.90
A


ATOM
1143
C
LYS
A
146
−0.302
−3.569
78.083
1.00
16.40
A


ATOM
1144
O
LYS
A
146
−0.176
−3.421
79.302
1.00
16.41
A


ATOM
1145
N
LEU
A
147
0.654
−4.102
77.322
1.00
16.28
A


ATOM
1146
CA
LEU
A
147
1.912
−4.579
77.901
1.00
16.03
A


ATOM
1147
CB
LEU
A
147
2.717
−5.387
76.872
1.00
16.79
A


ATOM
1148
CG
LEU
A
147
2.089
−6.628
76.224
1.00
17.91
A


ATOM
1149
CD1
LEU
A
147
3.145
−7.359
75.409
1.00
18.58
A


ATOM
1150
CD2
LEU
A
147
1.520
−7.551
77.277
1.00
19.05
A


ATOM
1151
C
LEU
A
147
2.789
−3.449
78.446
1.00
15.74
A


ATOM
1152
O
LEU
A
147
3.477
−3.622
79.456
1.00
15.01
A


ATOM
1153
N
LEU
A
148
2.765
−2.297
77.780
1.00
14.59
A


ATOM
1154
CA
LEU
A
148
3.567
−1.149
78.202
1.00
14.85
A


ATOM
1155
CB
LEU
A
148
3.913
−0.261
76.998
1.00
14.25
A


ATOM
1156
CG
LEU
A
148
4.991
−0.710
76.017
1.00
14.59
A


ATOM
1157
CD1
LEU
A
148
4.989
0.201
74.790
1.00
14.37
A


ATOM
1158
CD2
LEU
A
148
6.349
−0.680
76.712
1.00
15.53
A


ATOM
1159
C
LEU
A
148
2.877
−0.289
79.257
1.00
14.60
A


ATOM
1160
O
LEU
A
148
3.535
0.459
79.991
1.00
14.89
A


ATOM
1161
N
GLY
A
149
1.554
−0.381
79.336
1.00
14.31
A


ATOM
1162
CA
GLY
A
149
0.822
0.426
80.295
1.00
14.76
A


ATOM
1163
C
GLY
A
149
0.754
1.885
79.867
1.00
15.29
A


ATOM
1164
O
GLY
A
149
0.838
2.792
80.696
1.00
15.01
A


ATOM
1165
N
LEU
A
150
0.618
2.123
78.565
1.00
15.01
A


ATOM
1166
CA
LEU
A
150
0.522
3.490
78.058
1.00
14.43
A


ATOM
1167
CB
LEU
A
150
0.665
3.500
76.530
1.00
14.29
A


ATOM
1168
CG
LEU
A
150
1.962
2.940
75.928
1.00
14.95
A


ATOM
1169
CD1
LEU
A
150
1.852
2.932
74.401
1.00
15.08
A


ATOM
1170
CD2
LEU
A
150
3.157
3.773
76.374
1.00
14.06
A


ATOM
1171
C
LEU
A
150
−0.851
4.041
78.451
1.00
14.48
A


ATOM
1172
O
LEU
A
150
−1.729
3.278
78.853
1.00
24.49
A


ATOM
1173
N
ARG
A
151
−1.043
5.356
78.348
1.00
14.75
A


ATOM
1174
CA
ARG
A
151
−2.343
5.942
78.686
1.00
15.18
A


ATOM
1175
CB
ARG
A
151
−2.363
7.447
78.418
1.00
16.74
A


ATOM
1176
CG
ARG
A
151
−1.317
8.281
79.141
1.00
20.10
A


ATOM
1177
CD
ARG
A
151
−1.614
8.453
80.619
1.00
22.50
A


ATOM
1178
NE
ARG
A
151
−1.242
7.285
81.409
1.00
25.48
A


ATOM
1179
CZ
ARG
A
151
−0.889
7.345
82.690
1.00
26.63
A


ATOM
1180
NH1
ARG
A
151
−0.863
8.517
83.315
1.00
27.54
A


ATOM
1181
NH2
ARG
A
151
−0.554
6.240
83.345
1.00
27.39
A


ATOM
1182
C
ARG
A
151
−3.376
5.285
77.767
1.00
14.81
A


ATOM
1183
O
ARG
A
151
−3.086
5.017
76.597
1.00
14.19
A


ATOM
1184
N
PRO
A
152
−4.594
5.026
78.276
1.00
14.13
A


ATOM
1185
CD
PRO
A
152
−5.080
5.236
79.652
1.00
14.92
A


ATOM
1186
CA
PRO
A
152
−5.626
4.397
77.440
1.00
13.82
A


ATOM
1187
CB
PRO
A
152
−6.768
4.139
78.427
1.00
14.60
A


ATOM
1188
CG
PRO
A
152
−6.581
5.212
79.469
1.00
15.28
A


ATOM
1189
C
PRO
A
152
−6.063
5.243
76.244
1.00
13.54
A


ATOM
1190
O
PRO
A
152
−6.637
4.718
75.285
1.00
13.02
A


ATOM
1191
N
TYR
A
153
−5.782
6.543
76.296
1.00
12.81
A


ATOM
1192
CA
TYR
A
153
−6.160
7.447
75.215
1.00
12.98
A


ATOM
1193
CB
TYR
A
153
−6.697
8.760
75.799
1.00
13.85
A


ATOM
1194
CG
TYR
A
153
−5.834
9.362
76.879
1.00
15.46
A


ATOM
1195
CD1
TYR
A
153
−4.728
10.150
76.559
1.00
15.67
A


ATOM
1196
CE1
TYR
A
153
−3.933
10.713
77.558
1.00
16.87
A


ATOM
1197
CD2
TYR
A
153
−6.124
9.145
78.228
1.00
15.87
A


ATOM
1198
CE2
TYR
A
153
−5.335
9.700
79.233
1.00
16.78
A


ATOM
1199
CZ
TYR
A
153
−4.243
10.484
78.892
1.00
16.94
A


ATOM
1200
OH
TYR
A
153
−3.466
11.045
79.887
1.00
18.20
A


ATOM
1201
C
TYR
A
153
−5.046
7.714
74.198
1.00
12.40
A


ATOM
1202
O
TYR
A
153
−5.072
8.707
73.471
1.00
11.41
A


ATOM
1203
N
VAL
A
154
−4.061
6.822
74.157
1.00
11.87
A


ATOM
1204
CA
VAL
A
154
−2.980
6.940
73.185
1.00
11.77
A


ATOM
1205
CB
VAL
A
154
−1.853
5.908
73.489
1.00
11.94
A


ATOM
1206
CG1
VAL
A
154
−2.405
4.491
73.415
1.00
11.75
A


ATOM
1207
CG2
VAL
A
154
−0.689
6.092
72.525
1.00
11.07
A


ATOM
1208
C
VAL
A
154
−3.648
6.625
71.837
1.00
11.61
A


ATOM
1209
O
VAL
A
154
−4.427
5.677
71.746
1.00
11.48
A


ATOM
1210
N
LYS
A
155
−3.372
7.434
70.815
1.00
11.04
A


ATOM
1211
CA
LYS
A
155
−3.958
7.240
69.488
1.00
11.52
A


ATOM
1212
CB
LYS
A
155
−4.021
8.579
68.744
1.00
12.00
A


ATOM
1213
CG
LYS
A
155
−5.109
9.511
69.281
1.00
13.78
A


ATOM
1214
CD
LYS
A
155
−5.049
10.889
68.638
1.00
14.84
A


ATOM
1215
CE
LYS
A
155
−4.098
11.811
69.373
1.00
16.12
A


ATOM
1216
NZ
LYS
A
155
−4.651
12.234
70.700
1.00
17.06
A


ATOM
1217
C
LYS
A
155
−3.144
6.219
68.705
1.00
10.94
A


ATOM
1218
O
LYS
A
155
−1.993
6.472
68.349
1.00
10.07
A


ATOM
1219
N
ARG
A
156
−3.771
5.077
68.422
1.00
10.42
A


ATOM
1220
CA
ARG
A
156
−3.118
3.956
67.748
1.00
10.30
A


ATOM
1221
CB
ARG
A
156
−3.463
2.660
68.492
1.00
10.46
A


ATOM
1222
CG
ARG
A
156
−3.114
2.635
69.984
1.00
12.15
A


ATOM
1223
CD
ARG
A
156
−3.773
1.430
70.673
1.00
11.65
A


ATOM
1224
NE
ARG
A
156
−5.153
1.718
71.061
1.00
13.59
A


ATOM
1225
CZ
ARG
A
156
−6.222
1.026
70.670
1.00
13.73
A


ATOM
1226
NH1
ARG
A
156
−6.092
−0.017
69.860
1.00
13.14
A


ATOM
1227
NH2
ARG
A
156
−7.429
1.377
71.101
1.00
12.93
A


ATOM
1228
C
ARG
A
156
−3.435
3.718
66.271
1.00
10.47
A


ATOM
1229
O
ARG
A
156
−4.520
4.034
65.794
1.00
10.65
A


ATOM
1230
N
VAL
A
157
−2.470
3.128
65.569
1.00
10.08
A


ATOM
1231
CA
VAL
A
157
−2.629
2.742
64.166
1.00
10.38
A


ATOM
1232
CB
VAL
A
157
−2.160
3.834
63.181
1.00
10.90
A


ATOM
1233
CG1
VAL
A
157
−0.714
4.156
63.410
1.00
13.08
A


ATOM
1234
CG2
VAL
A
157
−2.374
3.352
61.739
1.00
12.71
A


ATOM
1235
C
VAL
A
157
−1.793
1.484
63.939
1.00
9.54
A


ATOM
1236
O
VAL
A
157
−0.603
1.456
64.257
1.00
8.67
A


ATOM
1237
N
GLY
A
158
−2.431
0.440
63.414
1.00
8.62
A


ATOM
1238
CA
GLY
A
158
−1.725
−0.801
63.145
1.00
8.95
A


ATOM
1239
C
GLY
A
158
−1.474
−0.920
61.655
1.00
9.11
A


ATOM
1240
O
GLY
A
158
−2.377
−0.660
60.861
1.00
9.18
A


ATOM
1241
N
VAL
A
159
−0.252
−1.297
61.280
1.00
8.82
A


ATOM
1242
CA
VAL
A
159
0.139
−1.446
59.876
1.00
9.27
A


ATOM
1243
CB
VAL
A
159
1.383
−0.578
59.566
1.00
10.03
A


ATOM
1244
CG1
VAL
A
159
1.821
−0.763
58.120
1.00
9.90
A


ATOM
1245
CG2
VAL
A
159
1.060
0.890
59.848
1.00
8.75
A


ATOM
1246
C
VAL
A
159
0.449
−2.918
59.622
1.00
9.42
A


ATOM
1247
O
VAL
A
159
1.541
−3.403
59.937
1.00
8.94
A


ATOM
1248
N
PHE
A
160
−0.523
−3.620
59.048
1.00
9.07
A


ATOM
1249
CA
PHE
A
160
−0.401
−5.049
58.793
1.00
9.95
A


ATOM
1250
CB
PHE
A
160
−1.476
−5.787
59.607
1.00
9.65
A


ATOM
1251
CG
PHE
A
160
−1.534
−5.354
61.057
1.00
10.47
A


ATOM
1252
CD1
PHE
A
160
−0.428
−5.519
61.889
1.00
10.51
A


ATOM
1253
CD2
PHE
A
160
−2.679
−4.757
61.577
1.00
10.31
A


ATOM
1254
CE1
PHE
A
160
−0.462
−5.091
63.226
1.00
10.88
A


ATOM
1255
CE2
PHE
A
160
−2.726
−4.325
62.913
1.00
11.26
A


ATOM
1256
CZ
PHE
A
160
−1.618
−4.491
63.735
1.00
10.62
A


ATOM
1257
C
PHE
A
160
−0.506
−5.439
57.320
1.00
10.38
A


ATOM
1258
O
PHE
A
160
−1.192
−4.787
56.530
1.00
10.36
A


ATOM
1259
N
GLN
A
161
0.179
−6.527
56.981
1.00
10.62
A


ATOM
1260
CA
GLN
A
161
0.230
−7.076
55.634
1.00
11.79
A


ATOM
1261
CB
GLN
A
161
−1.117
−7.743
55.272
1.00
11.33
A


ATOM
1262
CG
GLN
A
161
−1.311
−9.055
56.058
1.00
12.18
A


ATOM
1263
CD
GLN
A
161
−2.598
−9.818
55.754
1.00
12.20
A


ATOM
1264
OE1
GLN
A
161
−3.381
−10.113
56.662
1.00
11.95
A


ATOM
1265
NE2
GLN
A
161
−2.810
−10.161
54.487
1.00
12.09
A


ATOM
1266
C
GLN
A
161
0.704
−6.102
54.554
1.00
12.04
A


ATOM
1267
O
GLN
A
161
0.215
−6.114
53.421
1.00
13.06
A


ATOM
1268
N
HIS
A
162
1.667
−5.256
54.922
1.00
11.82
A


ATOM
1269
CA
HIS
A
162
2.279
−4.330
53.975
1.00
12.08
A


ATOM
1270
CB
HIS
A
162
2.552
−2.962
54.619
1.00
11.69
A


ATOM
1271
CG
HIS
A
162
1.307
−2.154
54.852
1.00
10.82
A


ATOM
1272
CD2
HIS
A
162
0.161
−2.456
55.507
1.00
9.91
A


ATOM
1273
ND1
HIS
A
162
1.142
−0.874
54.366
1.00
12.15
A


ATOM
1274
CE1
HIS
A
162
−0.051
−0.422
54.711
1.00
9.94
A


ATOM
1275
NE2
HIS
A
162
−0.667
−1.363
55.405
1.00
11.67
A


ATOM
1276
C
HIS
A
162
3.575
−5.021
53.539
1.00
12.51
A


ATOM
1277
O
HIS
A
162
3.854
−5.127
52.348
1.00
14.03
A


ATOM
1278
N
GLY
A
163
4.361
−5.507
54.497
1.00
12.09
A


ATOM
1279
CA
GLY
A
163
5.570
−6.229
54.130
1.00
12.81
A


ATOM
1280
C
GLY
A
163
6.937
−5.602
54.325
1.00
12.93
A


ATOM
1281
O
GLY
A
163
7.122
−4.713
53.159
1.00
13.11
A


ATOM
1282
N
CYS
A
164
7.898
−6.079
53.553
1.00
12.87
A


ATOM
1283
CA
CYS
A
164
9.285
−5.630
53.608
1.00
12.88
A


ATOM
1284
CB
CYS
A
164
10.145
−6.435
52.621
1.00
14.32
A


ATOM
1285
SG
CYS
A
164
10.567
−8.126
53.171
1.00
18.21
A


ATOM
1286
C
CYS
A
164
9.565
−4.137
53.419
1.00
12.07
A


ATOM
1287
O
CYS
A
164
10.611
−3.655
53.851
1.00
12.09
A


ATOM
1288
N
PHE
A
165
8.656
−3.402
52.787
1.00
11.32
A


ATOM
1289
CA
PHE
A
165
8.881
−1.970
52.579
1.00
11.97
A


ATOM
1290
CB
PHE
A
165
8.268
−1.529
51.239
1.00
12.38
A


ATOM
1291
CG
PHE
A
165
6.761
−1.608
51.194
1.00
12.73
A


ATOM
1292
CD1
PHE
A
165
5.977
−0.679
51.878
1.00
12.91
A


ATOM
1293
CD2
PHE
A
165
6.126
−2.624
50.487
1.00
12.52
A


ATOM
1294
CE1
PHE
A
165
4.582
−0.763
51.865
1.00
12.61
A


ATOM
1295
CE2
PHE
A
165
4.727
−2.719
50.466
1.00
12.91
A


ATOM
1296
CZ
PHE
A
165
3.955
−1.785
51.160
1.00
12.54
A


ATOM
1297
C
PHE
A
165
8.327
−1.090
53.711
1.00
11.55
A


ATOM
1298
O
PHE
A
165
8.591
0.116
53.755
1.00
10.90
A


ATOM
1299
N
ALA
A
166
7.597
−1.705
54.640
1.00
11.47
A


ATOM
1300
CA
ALA
A
166
6.951
−0.987
55.742
1.00
10.36
A


ATOM
1301
CB
ALA
A
166
6.055
−1.944
56.520
1.00
10.05
A


ATOM
1302
C
ALA
A
166
7.832
−0.201
56.716
1.00
10.76
A


ATOM
1303
O
ALA
A
166
7.311
0.568
57.541
1.00
10.61
A


ATOM
1304
N
GLY
A
167
9.142
−0.404
56.660
1.00
10.33
A


ATOM
1305
CA
GLY
A
167
10.025
0.363
57.525
1.00
10.23
A


ATOM
1306
C
GLY
A
167
9.945
1.808
57.056
1.00
10.55
A


ATOM
1307
O
GLY
A
167
10.031
2.757
57.844
1.00
9.84
A


ATOM
1308
N
GLY
A
168
9.779
1.982
55.749
1.00
9.79
A


ATOM
1309
CA
GLY
A
168
9.650
3.319
55.205
1.00
10.50
A


ATOM
1310
C
GLY
A
168
8.246
3.849
55.466
1.00
9.99
A


ATOM
1311
O
GLY
A
168
8.057
5.036
55.733
1.00
10.63
A


ATOM
1312
N
THR
A
169
7.260
2.957
55.392
1.00
9.91
A


ATOM
1313
CA
THR
A
169
5.853
3.307
55.615
1.00
8.80
A


ATOM
1314
CB
THR
A
169
4.939
2.060
55.439
1.00
9.40
A


ATOM
1315
OG1
THR
A
169
5.186
1.457
54.163
1.00
10.04
A


ATOM
1316
CG2
THR
A
169
3.468
2.454
55.521
1.00
9.30
A


ATOM
1317
C
THR
A
169
5.590
3.898
57.006
1.00
8.76
A


ATOM
1318
O
THR
A
169
4.865
4.896
57.144
1.00
7.14
A


ATOM
1319
N
VAL
A
170
6.157
3.288
58.046
1.00
7.94
A


ATOM
1320
CA
VAL
A
170
5.925
3.804
59.391
1.00
7.96
A


ATOM
1321
CB
VAL
A
170
6.391
2.818
60.492
1.00
8.12
A


ATOM
1322
CG1
VAL
A
170
5.595
1.516
60.377
1.00
8.51
A


ATOM
1323
CG2
VAL
A
170
7.894
2.571
60.387
1.00
8.83
A


ATOM
1324
C
VAL
A
170
6.599
5.153
59.615
1.00
8.27
A


ATOM
1325
O
VAL
A
170
6.121
5.958
60.411
1.00
8.24
A


ATOM
1326
N
LEU
A
171
7.706
5.401
58.919
1.00
8.82
A


ATOM
1327
CA
LEU
A
171
8.398
6.680
59.059
1.00
9.31
A


ATOM
1328
CB
LEU
A
171
9.798
6.610
58.438
1.00
9.00
A


ATOM
1329
CG
LEU
A
171
10.849
5.863
59.275
1.00
9.38
A


ATOM
1330
CG1
LEU
A
171
12.115
5.666
58.461
1.00
10.01
A


ATOM
1331
CG2
LEU
A
171
11.155
6.668
60.549
1.00
10.13
A


ATOM
1332
C
LEU
A
171
7.559
7.756
58.371
1.00
9.34
A


ATOM
1333
O
LEU
A
171
7.412
8.868
58.886
1.00
9.70
A


ATOM
1334
N
ARG
A
172
7.006
7.411
57.208
1.00
9.62
A


ATOM
1335
CA
ARG
A
172
6.155
8.319
56.435
1.00
9.46
A


ATOM
1336
CB
ARG
A
172
5.757
7.647
55.106
1.00
10.16
A


ATOM
1337
CG
ARG
A
172
4.732
8.408
54.269
1.00
10.70
A


ATOM
1338
CD
ARG
A
172
4.768
7.971
52.792
1.00
10.81
A


ATOM
1339
NE
ARG
A
172
4.534
6.538
52.581
1.00
10.35
A


ATOM
1340
CZ
ARG
A
172
3.341
5.948
52.574
1.00
10.72
A


ATOM
1341
NH1
ARG
A
172
2.232
6.652
52.772
1.00
10.58
A


ATOM
1342
NH2
ARG
A
172
3.251
4.641
52.336
1.00
10.24
A


ATOM
1343
C
ARG
A
172
4.906
8.703
57.246
1.00
9.67
A


ATOM
1344
O
ARG
A
172
4.491
9.864
57.251
1.00
8.96
A


ATOM
1345
N
LEU
A
173
4.315
7.735
57.943
1.00
9.66
A


ATOM
1346
CA
LEU
A
173
3.135
8.015
58.759
1.00
9.61
A


ATOM
1347
CB
LEU
A
173
2.469
6.714
59.221
1.00
10.65
A


ATOM
1348
CG
LEU
A
173
1.700
5.893
58.180
1.00
10.70
A


ATOM
1349
CD1
LEU
A
173
1.374
4.522
58.764
1.00
10.48
A


ATOM
1350
CD2
LEU
A
173
0.422
6.630
57.766
1.00
10.97
A


ATOM
1351
C
LEU
A
173
3.514
8.846
59.985
1.00
10.02
A


ATOM
1352
O
LEU
A
173
2.838
9.819
60.314
1.00
8.14
A


ATOM
1353
N
ALA
A
174
4.589
8.452
60.667
1.00
9.18
A


ATOM
1354
CA
ALA
A
174
5.031
9.177
61.858
1.00
9.26
A


ATOM
1355
CB
ALA
A
174
6.273
8.507
62.453
1.00
8.76
A


ATOM
1356
C
ALA
A
174
5.331
10.640
61.533
1.00
9.47
A


ATOM
1357
O
ALA
A
174
5.117
11.530
62.362
1.00
9.93
A


ATOM
1358
N
LYS
A
175
5.833
10.889
60.330
1.00
9.17
A


ATOM
1359
CA
LYS
A
175
6.160
12.252
59.925
1.00
9.55
A


ATOM
1360
CB
LYS
A
175
6.749
12.262
58.509
1.00
9.91
A


ATOM
1361
CG
LYS
A
175
7.144
13.652
58.009
1.00
10.71
A


ATOM
1362
CD
LYS
A
175
7.661
13.602
56.573
1.00
11.77
A


ATOM
1363
CE
LYS
A
175
8.152
14.967
56.104
1.00
11.36
A


ATOM
1364
NZ
LYS
A
175
7.064
15.983
56.022
1.00
12.68
A


ATOM
1365
C
LYS
A
175
4.932
13.167
59.986
1.00
9.54
A


ATOM
1366
O
LYS
A
175
4.990
14.252
60.561
1.00
9.61
A


ATOM
1367
N
ASP
A
176
3.816
12.733
59.409
1.00
9.94
A


ATOM
1368
CA
ASP
A
176
2.611
13.563
59.437
1.00
10.35
A


ATOM
1369
CB
ASP
A
176
1.577
13.062
58.422
1.00
10.89
A


ATOM
1370
CG
ASP
A
176
1.986
13.336
56.984
1.00
11.89
A


ATOM
1371
OD1
ASP
A
176
2.750
14.301
56.755
1.00
12.55
A


ATOM
1372
OD2
ASP
A
176
1.526
12.600
56.084
1.00
12.25
A


ATOM
1373
C
ASP
A
176
1.953
13.658
60.816
1.00
10.80
A


ATOM
1374
O
ASP
A
176
1.484
14.729
61.206
1.00
11.51
A


ATOM
1375
N
LEU
A
177
1.913
12.558
61.563
1.00
10.38
A


ATOM
1376
CA
LEU
A
177
1.278
12.595
62.882
1.00
10.56
A


ATOM
1377
CB
LEU
A
177
1.206
11.190
63.502
1.00
11.79
A


ATOM
1378
CG
LEU
A
177
0.639
9.991
62.725
1.00
14.19
A


ATOM
1379
CD1
LEU
A
177
0.109
8.979
63.738
1.00
13.55
A


ATOM
1380
CD2
LEU
A
177
−0.469
10.405
61.769
1.00
13.39
A


ATOM
1381
C
LEU
A
177
2.012
13.535
63.845
1.00
10.13
A


ATOM
1382
O
LEU
A
177
1.381
14.256
64.613
1.00
10.07
A


ATOM
1383
N
ALA
A
178
3.343
13.532
63.798
1.00
9.17
A


ATOM
1384
CA
ALA
A
178
4.132
14.387
64.684
1.00
9.84
A


ATOM
1385
CB
ALA
A
178
5.565
13.867
64.768
1.00
9.65
A


ATOM
1386
C
ALA
A
178
4.144
15.860
64.261
1.00
9.88
A


ATOM
1387
O
ALA
A
178
4.064
16.756
65.108
1.00
10.05
A


ATOM
1388
N
GLU
A
179
4.243
16.111
62.958
1.00
8.91
A


ATOM
1389
CA
GLU
A
179
4.286
17.479
62.447
1.00
10.22
A


ATOM
1390
CB
GLU
A
179
4.834
17.488
61.005
1.00
10.39
A


ATOM
1391
CG
GLU
A
179
6.363
17.310
60.920
1.00
12.08
A


ATOM
1392
CD
GLU
A
179
6.887
17.099
59.495
1.00
12.59
A


ATOM
1393
OE1
GLU
A
179
6.109
17.252
58.527
1.00
13.52
A


ATOM
1394
OE2
GLU
A
179
8.090
16.781
59.344
1.00
11.85
A


ATOM
1395
C
GLU
A
179
2.954
18.241
62.507
1.00
10.38
A


ATOM
1396
O
GLU
A
179
2.953
19.465
62.644
1.00
10.28
A


ATOM
1397
N
ASN
A
180
1.828
17.534
62.426
1.00
10.18
A


ATOM
1398
CA
ASN
A
180
0.522
18.204
62.453
1.00
10.49
A


ATOM
1399
CB
ASN
A
180
−0.468
17.472
61.534
1.00
10.37
A


ATOM
1400
CG
ASN
A
180
−1.703
18.304
61.229
1.00
10.46
A


ATOM
1401
OD1
ASN
A
180
−1.591
19.448
60.787
1.00
11.09
A


ATOM
1402
ND2
ASN
A
180
−2.888
17.733
61.457
1.00
10.21
A


ATOM
1403
C
ASN
A
180
−0.121
18.362
63.834
1.00
10.50
A


ATOM
1404
O
ASN
A
180
−1.202
18.945
63.944
1.00
10.62
A


ATOM
1405
N
ASN
A
181
0.535
17.860
64.880
1.00
10.99
A


ATOM
1406
CA
ASN
A
181
−0.016
17.927
66.238
1.00
11.61
A


ATOM
1407
CB
ASN
A
181
−0.564
16.549
66.625
1.00
10.99
A


ATOM
1408
CG
ASN
A
181
−1.740
16.127
65.759
1.00
11.32
A


ATOM
1409
OD1
ASN
A
181
−2.859
16.615
65.934
1.00
10.59
A


ATOM
1410
ND2
ASN
A
181
−1.489
15.227
64.808
1.00
9.52
A


ATOM
1411
C
ASN
A
181
0.998
18.401
67.292
1.00
11.97
A


ATOM
1412
O
ASN
A
181
1.937
17.679
67.643
1.00
12.00
A


ATOM
1413
N
LYS
A
182
0.795
19.614
67.798
1.00
12.75
A


ATOM
1414
CA
LYS
A
182
1.696
20.206
68.789
1.00
13.47
A


ATOM
1415
CB
LYS
A
182
1.196
21.599
69.184
1.00
14.26
A


ATOM
1416
CG
LYS
A
182
2.079
22.332
70.192
1.00
15.00
A


ATOM
1417
CD
LYS
A
182
1.552
23.747
70.417
1.00
16.14
A


ATOM
1418
CE
LYS
A
182
2.521
24.601
71.221
1.00
16.60
A


ATOM
1419
NZ
LYS
A
182
1.974
25.979
71.402
1.00
18.49
A


ATOM
1420
C
LYS
A
182
1.856
19.357
70.044
1.00
13.44
A


ATOM
1421
O
LYS
A
182
0.872
18.987
70.684
1.00
13.52
A


ATOM
1422
N
GLY
A
183
3.105
19.060
70.391
1.00
13.68
A


ATOM
1423
CA
GLY
A
183
3.383
18.262
71.574
1.00
13.42
A


ATOM
1424
C
GLY
A
183
3.351
16.758
71.360
1.00
12.95
A


ATOM
1425
O
GLY
A
183
3.689
15.993
72.259
1.00
13.54
A


ATOM
1426
N
ALA
A
184
2.963
16.320
70.169
1.00
13.05
A


ATOM
1427
CA
ALA
A
184
2.875
14.891
69.893
1.00
11.73
A


ATOM
1428
CB
ALA
A
184
2.194
14.659
68.537
1.00
11.31
A


ATOM
1429
C
ALA
A
184
4.218
14.187
69.930
1.00
11.28
A


ATOM
1430
O
ALA
A
184
5.223
14.664
59.426
1.00
11.97
A


ATOM
1431
N
ARG
A
185
4.216
12.990
70.547
1.00
10.77
A


ATOM
1432
CA
ARG
A
185
5.402
12.145
70.650
1.00
10.15
A


ATOM
1433
CB
ARG
A
185
5.943
12.158
72.085
1.30
10.47
A


ATOM
1434
CG
ARG
A
185
6.661
13.478
72.457
1.00
10.37
A


ATOM
1435
CD
ARG
A
185
7.966
13.635
71.667
1.00
11.21
A


ATOM
1436
NE
ARG
A
185
8.724
14.859
71.958
1.00
11.36
A


ATOM
1437
CZ
ARG
A
185
8.514
16.039
71.375
1.00
11.90
A


ATOM
1438
NH1
ARG
A
185
7.557
16.180
70.462
1.00
11.35
A


ATOM
1439
NH2
ARG
A
185
9.287
17.078
71.676
1.00
12.08
A


ATOM
1440
C
ARG
A
185
4.937
10.754
70.219
1.00
9.96
A


ATOM
1441
O
ARG
A
185
4.102
10.121
70.878
1.00
8.97
A


ATOM
1442
N
VAL
A
186
5.477
10.297
69.093
1.00
9.29
A


ATOM
1443
CA
VAL
A
186
5.083
9.024
68.499
1.00
9.31
A


ATOM
1444
CB
VAL
A
186
4.918
9.190
66.966
1.00
9.15
A


ATOM
1445
CG1
VAL
A
186
4.292
7.933
66.360
1.00
9.74
A


ATOM
1446
CG2
VAL
A
188
4.063
10.423
66.659
1.00
9.08
A


ATOM
1447
C
VAL
A
186
6.026
7.852
68.742
1.00
9.11
A


ATOM
1448
O
VAL
A
186
7.213
7.930
68.423
1.00
8.24
A


ATOM
1449
N
LEU
A
187
5.496
6.774
69.325
1.00
9.01
A


ATOM
1450
CA
LEU
A
187
6.293
5.570
69.547
1.00
8.10
A


ATOM
1451
CB
LEU
A
187
5.856
4.829
70.819
1.00
8.38
A


ATOM
1452
CG
LEU
A
187
6.458
3.432
71.043
1.00
7.38
A


ATOM
1453
CD1
LEU
A
187
7.982
3.520
71.124
1.00
7.26
A


ATOM
1454
CD2
LEU
A
187
5.901
2.821
72.327
1.00
6.64
A


ATOM
1455
C
LEU
A
187
6.011
4.703
68.319
1.00
8.64
A


ATOM
1456
O
LEU
A
187
4.852
4.408
68.021
1.00
8.42
A


ATOM
1457
N
VAL
A
188
7.069
4.320
67.610
1.00
8.34
A


ATOM
1458
CA
VAL
A
188
6.954
3.497
66.406
1.00
8.95
A


ATOM
1459
CB
VAL
A
188
7.675
4.163
65.208
1.00
8.81
A


ATOM
1460
CG1
VAL
A
188
7.505
3.307
63.952
1.00
9.57
A


ATOM
1461
CG2
VAL
A
188
7.127
5.563
64.983
1.00
8.73
A


ATOM
1462
C
VAL
A
188
7.603
2.144
66.665
1.00
9.22
A


ATOM
1463
O
VAL
A
188
8.750
2.089
67.109
1.00
9.45
A


ATOM
1464
N
VAL
A
189
6.876
1.059
66.389
1.00
9.29
A


ATOM
1465
CA
VAL
A
189
7.403
−0.286
66.609
1.00
9.54
A


ATOM
1466
CB
VAL
A
189
6.771
−0.938
67.876
1.00
9.93
A


ATOM
1467
CG1
VAL
A
189
7.359
−2.339
68.101
1.00
10.83
A


ATOM
1468
CG2
VAL
A
189
7.006
−0.060
69.103
1.00
10.08
A


ATOM
1469
C
VAL
A
189
7.180
−1.250
65.437
1.00
9.89
A


ATOM
1470
O
VAL
A
189
6.044
−1.446
64.985
1.00
9.62
A


ATOM
1471
N
CYS
A
190
8.267
−1.838
64.944
1.00
10.01
A


ATOM
1472
CA
CYS
A
190
8.194
−2.838
63.875
1.00
10.09
A


ATOM
1473
CB
CYS
A
190
9.120
−2.495
62.703
1.00
11.33
A


ATOM
1474
SG
CYS
A
190
8.653
−1.059
61.716
1.00
12.55
A


ATOM
1475
C
CYS
A
190
8.680
−4.130
64.530
1.00
10.56
A


ATOM
1476
O
CYS
A
190
9.794
−4.182
65.062
1.00
9.40
A


ATOM
1477
N
SER
A
191
7.847
−5.165
64.498
1.00
10.19
A


ATOM
1478
CA
SER
A
191
8.193
−6.448
65.106
1.00
10.68
A


ATOM
1479
CB
SER
A
191
7.402
−6.629
66.405
1.00
10.50
A


ATOM
1480
OG
SER
A
191
7.696
−7.867
67.016
1.00
10.11
A


ATOM
1481
C
SER
A
191
7.863
−7.573
64.137
1.00
10.91
A


ATOM
1482
O
SER
A
191
6.706
−7.740
63.750
1.00
10.99
A


ATOM
1483
N
GLU
A
192
8.876
−8.351
63.760
1.00
11.05
A


ATOM
1484
CA
GLU
A
192
8.699
−9.442
62.800
1.00
10.62
A


ATOM
1485
CB
GLU
A
192
9.462
−9.107
61.512
1.00
10.66
A


ATOM
1486
CG
GLU
A
192
9.135
−7.721
60.914
1.00
10.64
A


ATOM
1487
CD
GLU
A
192
7.802
−7.684
60.166
1.00
10.87
A


ATOM
1488
OE1
GLU
A
192
7.109
−8.719
60.125
1.00
11.53
A


ATOM
1489
OE2
GLU
A
192
7.446
−6.618
59.618
1.00
10.92
A


ATOM
1490
C
GLU
A
192
9.170
−10.796
63.347
1.00
10.89
A


ATOM
1491
O
GLU
A
192
10.285
−10.917
63.847
1.00
9.91
A


ATOM
1492
N
VAL
A
192
8.316
−11.811
63.221
1.00
11.07
A


ATOM
1493
CA
VAL
A
193
8.602
−13.162
63.711
1.00
11.62
A


ATOM
1494
CB
VAL
A
193
7.725
−13.468
64.953
1.00
11.44
A


ATOM
1495
CG1
VAL
A
193
7.933
−14.908
65.420
1.00
11.03
A


ATOM
1496
CG2
VAL
A
193
8.074
−12.489
66.077
1.00
11.56
A


ATOM
1497
C
VAL
A
193
8.328
−14.197
62.614
1.00
12.46
A


ATOM
1498
O
VAL
A
193
7.192
−14.331
62.151
1.00
12.86
A


ATOM
1499
N
THR
A
194
9.366
−14.933
62.216
1.00
12.81
A


ATOM
1500
CA
THR
A
194
9.260
−15.931
61.148
1.00
12.86
A


ATOM
1501
CB
THR
A
194
10.664
−16.424
60.702
1.00
13.15
A


ATOM
1502
OG1
THR
A
194
11.370
−16.975
61.822
1.00
12.89
A


ATOM
1503
CG2
THR
A
194
11.472
−15.264
60.112
1.00
13.13
A


ATOM
1504
C
THR
A
194
8.381
−17.160
61.395
1.00
13.30
A


ATOM
1505
O
THR
A
194
8.258
−18.017
60.519
1.00
12.89
A


ATOM
1506
N
ALA
A
195
7.775
−17.256
62.571
1.00
13.76
A


ATOM
1507
CA
ALA
A
195
6.897
−18.384
62.872
1.00
14.53
A


ATOM
1508
CB
ALA
A
195
6.322
−18.242
64.278
1.00
15.45
A


ATOM
1509
C
ALA
A
195
5.758
−18.440
61.855
1.00
14.54
A


ATOM
1510
O
ALA
A
195
5.173
−19.498
61.612
1.00
14.97
A


ATOM
1511
N
VAL
A
196
5.445
−17.296
61.260
1.00
14.30
A


ATOM
1512
CA
VAL
A
196
4.363
−17.231
60.289
1.00
14.81
A


ATOM
1513
CB
VAL
A
196
3.774
−15.792
60.215
1.00
14.74
A


ATOM
1514
CG1
VAL
A
196
4.742
−14.859
59.494
1.00
15.82
A


ATOM
1515
CG2
VAL
A
196
2.412
−15.816
59.525
1.00
15.91
A


ATOM
1516
C
VAL
A
196
4.770
−17.696
58.884
1.00
14.53
A


ATOM
1517
O
VAL
A
196
3.914
−18.082
58.088
1.00
14.83
A


ATOM
1518
N
THR
A
197
6.069
−17.694
58.589
1.00
14.33
A


ATOM
1519
CA
THR
A
197
6.542
−18.097
57.263
1.00
14.12
A


ATOM
1520
CB
THR
A
197
7.393
−16.975
56.603
1.00
14.84
A


ATOM
1521
OG1
THR
A
197
8.492
−16.640
57.460
1.00
14.20
A


ATOM
1522
CG2
THR
A
197
6.548
−15.736
56.346
1.00
14.92
A


ATOM
1523
C
THR
A
197
7.361
−19.392
57.184
1.00
13.95
A


ATOM
1524
O
THR
A
197
7.515
−19.951
56.099
1.00
14.12
A


ATOM
1525
N
PHE
A
198
7.891
−19.868
58.309
1.00
13.34
A


ATOM
1526
CA
PHE
A
198
8.705
−21.089
58.295
1.00
13.23
A


ATOM
1527
CB
PHE
A
198
9.239
−21.393
59.706
1.00
12.64
A


ATOM
1528
CG
PHE
A
198
10.107
−22.633
59.782
1.00
12.39
A


ATOM
1529
CD1
PHE
A
199
9.538
−23.904
59.752
1.00
12.24
A


ATOM
1530
CD2
PHE
A
198
11.495
−22.524
59.849
1.00
12.72
A


ATOM
1531
CE1
PHE
A
198
10.336
−25.054
59.783
1.00
12.32
A


ATOM
1532
CE2
PHE
A
198
12.306
−23.668
59.880
1.00
12.12
A


ATOM
1533
CZ
PHE
A
198
11.720
−24.936
59.846
1.00
12.30
A


ATOM
1534
C
PHE
A
198
7.958
−22.310
57.764
1.00
13.09
A


ATOM
1535
O
PHE
A
198
6.816
−22.572
58.152
1.00
12.80
A


ATOM
1536
N
ARG
A
199
8.609
−23.060
56.877
1.00
13.29
A


ATOM
1537
CA
ARG
A
199
8.012
−24.275
56.323
1.00
13.07
A


ATOM
1538
CB
ARG
A
199
6.925
−23.922
55.293
1.00
13.33
A


ATOM
1539
CG
ARG
A
199
7.405
−23.140
54.078
1.00
12.99
A


ATOM
1540
CD
ARG
A
199
6.224
−22.551
53.305
1.00
13.81
A


ATOM
1541
NE
ARG
A
199
5.473
−21.575
54.101
1.00
13.90
A


ATOM
1542
CZ
ARG
A
199
4.324
−21.820
54.734
1.00
13.37
A


ATOM
1543
NH1
ARG
A
199
3.757
−23.020
54.682
1.00
12.59
A


ATOM
1544
NH2
ARG
A
199
3.735
−20.854
55.424
1.00
12.86
A


ATOM
1545
C
ARG
A
199
9.076
−25.183
55.702
1.00
13.44
A


ATOM
1546
O
ARG
A
199
10.198
−24.749
55.446
1.00
12.86
A


ATOM
1547
N
GLY
A
200
8.717
−26.447
55.479
1.00
14.16
A


ATOM
1548
CA
GLY
A
200
9.647
−27.412
54.908
1.00
14.89
A


ATOM
1549
C
GLY
A
200
10.055
−27.114
53.476
1.00
15.67
A


ATOM
1550
O
GLY
A
200
9.433
−26.282
52.820
1.00
15.33
A


ATOM
1551
N
PRO
A
201
11.101
−27.789
52.962
1.00
16.65
A


ATOM
1552
CD
PRO
A
201
11.997
−28.662
53.747
1.00
16.48
A


ATOM
1553
CA
PRO
A
201
11.616
−27.610
51.600
1.00
17.08
A


ATOM
1554
CB
PRO
A
201
13.059
−28.084
51.724
1.00
16.70
A


ATOM
1555
CG
PRO
A
201
12.923
−29.231
52.681
1.00
17.23
A


ATOM
1556
C
PRO
A
201
10.861
−28.372
50.514
1.00
18.19
A


ATOM
1557
O
PRO
A
201
10.369
−29.475
50.748
1.00
18.52
A


ATOM
1558
N
SER
A
202
10.788
−27.777
49.325
1.00
19.20
A


ATOM
1559
CA
SER
A
202
10.112
−28.381
48.171
1.00
20.83
A


ATOM
1560
CB
SER
A
202
8.714
−27.777
48.003
1.00
20.75
A


ATOM
1561
OG
SER
A
202
8.080
−28.273
46.833
1.00
22.13
A


ATOM
1562
C
SER
A
202
10.939
−28.131
46.906
1.00
21.36
A


ATOM
1563
O
SER
A
202
11.276
−26.988
46.601
1.00
21.26
A


ATOM
1564
N
ASP
A
203
11.259
−29.188
46.162
1.00
22.79
A


ATOM
1565
CA
ASP
A
203
12.071
−29.018
44.958
1.00
24.44
A


ATOM
1566
CB
ASP
A
203
12.717
−30.349
44.543
1.00
25.63
A


ATOM
1567
CG
ASP
A
203
11.705
−31.429
44.235
1.00
27.41
A


ATOM
1568
OD1
ASP
A
203
12.134
−32.575
43.975
1.00
29.04
A


ATOM
1569
OD2
ASP
A
203
10.490
−31.143
44.249
1.00
28.72
A


ATOM
1570
C
ASP
A
203
11.345
−28.383
43.774
1.00
24.57
A


ATOM
1571
O
ASP
A
203
11.938
−28.183
42.714
1.00
25.13
A


ATOM
1572
N
THR
A
204
10.070
−28.055
43.952
1.00
24.84
A


ATOM
1573
CA
THR
A
204
9.307
−27.406
42.892
1.00
25.35
A


ATOM
1574
CB
THR
A
204
7.995
−28.171
42.574
1.00
25.57
A


ATOM
1575
OG1
THR
A
204
7.270
−28.430
43.784
1.00
26.36
A


ATOM
1576
CG2
THR
A
204
8.309
−29.491
41.878
1.00
25.89
A


ATOM
1577
C
THR
A
204
8.980
−25.962
43.290
1.00
25.30
A


ATOM
1578
O
THR
A
204
8.263
−25.253
42.579
1.00
24.92
A


ATOM
1579
N
HIS
A
205
9.520
−25.533
44.429
1.00
25.03
A


ATOM
1580
CA
HIS
A
205
9.308
−24.175
44.924
1.00
25.38
A


ATOM
1581
CB
HIS
A
205
8.244
−24.166
46.026
1.00
26.03
A


ATOM
1582
CG
HIS
A
205
6.916
−24.699
45.585
1.00
26.52
A


ATOM
1583
CD2
HIS
A
205
5.865
−24.087
44.989
1.00
27.09
A


ATOM
1584
ND1
HIS
A
205
6.571
−26.029
45.698
1.00
26.88
A


ATOM
1585
CE1
HIS
A
205
5.366
−26.214
45.189
1.00
26.94
A


ATOM
1586
NE2
HIS
A
205
4.915
−25.051
44.751
1.00
27.31
A


ATOM
1587
C
HIS
A
205
10.609
−23.584
45.461
1.00
25.22
A


ATOM
1588
O
HIS
A
205
10.719
−23.267
46.643
1.00
25.50
A


ATOM
1589
N
LEU
A
206
11.591
−23.425
44.579
1.00
24.95
A


ATOM
1590
CA
LEU
A
206
12.892
−22.890
44.963
1.00
24.94
A


ATOM
1591
CB
LEU
A
206
13.863
−22.992
43.781
1.00
24.92
A


ATOM
1592
CG
LEU
A
206
14.102
−24.420
43.264
1.00
25.37
A


ATOM
1593
CD1
LEU
A
206
15.120
−24.397
42.129
1.00
25.23
A


ATOM
1594
CD2
LEU
A
206
14.591
−25.313
44.404
1.00
24.70
A


ATOM
1595
C
LEU
A
206
12.850
−21.455
45.495
1.00
25.23
A


ATOM
1596
O
LEU
A
206
13.729
−21.047
46.257
1.00
24.95
A


ATOM
1597
N
ASP
A
207
11.832
−20.690
45.104
1.00
25.29
A


ATOM
1598
CA
ASP
A
207
11.709
−19.317
45.583
1.00
25.66
A


ATOM
1599
CB
ASP
A
207
10.656
−18.548
44.775
1.00
27.12
A


ATOM
1600
CG
ASP
A
207
9.299
−19.231
44.768
1.00
28.64
A


ATOM
1601
OD1
ASP
A
207
8.347
−18.634
44.222
1.00
29.73
A


ATOM
1602
OD2
ASP
A
207
9.178
−20.360
45.294
1.00
29.96
A


ATOM
1603
C
ASP
A
207
11.341
−19.309
47.065
1.00
25.27
A


ATOM
1604
O
ASP
A
207
11.753
−18.426
47.817
1.00
25.41
A


ATOM
1605
N
SER
A
208
10.567
−20.301
47.486
1.00
24.29
A


ATOM
1606
CA
SER
A
208
10.173
−20.399
48.881
1.00
23.76
A


ATOM
1607
CB
SER
A
208
9.090
−21.473
49.048
1.00
24.07
A


ATOM
1608
OG
SER
A
206
8.686
−21.592
50.400
1.00
25.22
A


ATOM
1609
C
SER
A
208
11.409
−20.761
49.704
1.00
22.63
A


ATOM
1610
O
SER
A
208
11.607
−20.258
50.809
1.00
22.30
A


ATOM
1611
N
LEU
A
209
12.251
−21.620
49.138
1.00
21.70
A


ATOM
1612
CA
LEU
A
209
13.464
−22.075
49.802
1.00
20.71
A


ATOM
1613
CB
LEU
A
209
14.136
−23.165
48.957
1.00
20.77
A


ATOM
1614
CG
LEU
A
209
15.193
−24.039
49.629
1.00
20.98
A


ATOM
1615
CD1
LEU
A
209
14.554
−24.802
50.786
1.00
20.75
A


ATOM
1616
CD2
LEU
A
209
15.786
−25.009
48.608
1.00
20.81
A


ATOM
1617
C
LEU
A
209
14.461
−20.950
50.078
1.00
20.48
A


ATOM
1618
O
LEU
A
209
15.090
−20.924
51.139
1.00
20.50
A


ATOM
1619
N
VAL
A
210
14.621
−20.029
49.131
1.00
19.42
A


ATOM
1620
CA
VAL
A
210
15.560
−18.929
49.329
1.00
19.15
A


ATOM
1621
CB
VAL
A
210
15.658
−18.009
48.080
1.00
19.36
A


ATOM
1622
CG1
VAL
A
210
14.353
−17.264
47.857
1.00
20.36
A


ATOM
1623
CG2
VAL
A
210
16.806
−17.025
48.251
1.00
20.35
A


ATOM
1624
C
VAL
A
210
15.123
−18.119
50.545
1.00
18.35
A


ATOM
1625
O
VAL
A
210
15.954
−17.608
51.289
1.00
18.00
A


ATOM
1626
N
GLY
A
211
13.812
−18.016
50.742
1.00
17.76
A


ATOM
1627
CA
GLY
A
211
13.288
−17.295
51.888
1.00
17.42
A


ATOM
1628
C
GLY
A
211
13.710
−17.941
53.202
1.00
16.84
A


ATOM
1629
O
GLY
A
211
13.903
−17.249
54.201
1.00
17.07
A


ATOM
1630
N
GLN
A
212
13.855
−19.265
53.207
1.00
16.19
A


ATOM
1631
CA
GLN
A
212
14.267
−19.979
54.415
1.00
16.19
A


ATOM
1632
CB
GLN
A
212
14.053
−21.491
54.250
1.00
16.68
A


ATOM
1633
CG
GLN
A
212
12.614
−21.917
53.927
1.00
18.07
A


ATOM
1634
CD
GLN
A
212
11.600
−21.436
54.954
1.00
18.95
A


ATOM
1635
OE1
GLN
A
212
11.761
−21.657
56.152
1.00
19.82
A


ATOM
1636
NE2
GLN
A
212
10.547
−20.779
54.485
1.00
19.27
A


ATOM
1637
C
GLN
A
212
15.741
−19.702
54.741
1.00
15.86
A


ATOM
1638
O
GLN
A
212
16.191
−19.908
55.869
1.00
15.74
A


ATOM
1639
N
ALA
A
213
16.492
−19.231
53.751
1.00
15.43
A


ATOM
1640
CA
ALA
A
213
17.904
−18.922
53.953
1.00
15.06
A


ATOM
1641
CB
ALA
A
213
18.686
−19.225
52.674
1.00
15.32
A


ATOM
1642
C
ALA
A
213
18.137
−17.463
54.365
1.00
14.68
A


ATOM
1643
O
ALA
A
213
19.204
−17.117
54.886
1.00
14.33
A


ATOM
1644
N
LEU
A
214
17.135
−16.616
54.154
1.00
14.29
A


ATOM
1645
CA
LEU
A
214
17.275
−15.192
54.455
1.00
14.48
A


ATOM
1646
CB
LEU
A
214
16.924
−14.378
53.205
1.00
14.91
A


ATOM
1647
CG
LEU
A
214
17.668
−14.670
51.901
1.00
15.41
A


ATOM
1648
CD1
LEU
A
214
17.042
−13.844
50.774
1.00
16.41
A


ATOM
1649
CD2
LEU
A
214
19.146
−14.341
52.058
1.00
16.05
A


ATOM
1650
C
LEU
A
214
16.520
−14.576
55.640
1.00
14.29
A


ATOM
1651
O
LEU
A
214
17.082
−13.739
56.351
1.00
14.63
A


ATOM
1652
N
PHE
A
215
15.264
−14.965
55.844
1.00
13.93
A


ATOM
1653
CA
PHE
A
215
14.440
−14.377
56.907
1.00
13.96
A


ATOM
1654
CB
PHE
A
215
12.961
−14.752
56.718
1.00
15.54
A


ATOM
1655
CG
PHE
A
215
12.433
−14.517
55.324
1.00
17.87
A


ATOM
1656
CD1
PHE
A
215
12.952
−13.507
54.519
1.00
18.86
A


ATOM
1657
CD2
PHE
A
215
11.395
−15.302
54.826
1.00
18.79
A


ATOM
1658
CE1
PHE
A
215
12.445
−13.283
53.234
1.00
19.31
A


ATOM
1659
CE2
PHE
A
215
10.882
−15.086
53.547
1.00
19.39
A


ATOM
1660
CZ
PHE
A
215
11.409
−14.074
52.750
1.00
19.43
A


ATOM
1661
C
PHE
A
215
14.826
−14.689
58.349
1.00
13.33
A


ATOM
1662
O
PHE
A
215
15.054
−15.847
58.704
1.00
12.97
A


ATOM
1663
N
GLY
A
216
14.859
−13.637
59.170
1.00
12.63
A


ATOM
1664
CA
GLY
A
216
15.195
−13.751
60.585
1.00
12.55
A


ATOM
1665
C
GLY
A
216
14.239
−12.912
61.429
1.00
12.18
A


ATOM
1666
O
GLY
A
216
13.452
−12.136
60.873
1.00
11.45
A


ATOM
1667
N
ASP
A
217
14.313
−13.050
62.757
1.00
11.54
A


ATOM
1668
CA
ASP
A
217
13.430
−12.325
63.687
1.00
11.59
A


ATOM
1669
CB
ASP
A
217
12.952
−13.267
64.798
1.00
11.47
A


ATOM
1670
CG
ASP
A
217
12.188
−14.469
64.275
1.00
12.37
A


ATOM
1671
OD1
ASP
A
217
12.114
−14.667
63.043
1.00
12.95
A


ATOM
1672
OD2
ASP
A
217
11.665
−15.227
65.112
1.00
13.04
A


ATOM
1673
C
ASP
A
217
14.046
−11.089
64.362
1.00
11.79
A


ATOM
1674
O
ASP
A
217
15.253
−11.040
64.619
1.00
11.06
A


ATOM
1675
N
GLY
A
218
13.196
−10.109
64.681
1.00
11.39
A


ATOM
1676
CA
GLY
A
218
13.666
−8.899
65.338
1.00
10.97
A


ATOM
1677
C
GLY
A
218
12.637
−7.786
65.469
1.00
11.12
A


ATOM
1678
O
GLY
A
218
11.619
−7.780
64.774
1.00
11.86
A


ATOM
1679
N
ALA
A
219
12.894
−6.850
66.379
1.00
10.90
A


ATOM
1680
CA
ALA
A
219
12.010
−5.702
66.587
1.00
10.79
A


ATOM
1681
CB
ALA
A
219
11.083
−5.943
67.792
1.00
10.28
A


ATOM
1682
C
ALA
A
219
12.848
−4.439
66.811
1.00
10.65
A


ATOM
1683
O
ALA
A
219
13.940
−4.496
67.388
1.00
10.66
A


ATOM
1684
N
ALA
A
220
12.333
−3.309
66.337
1.00
9.85
A


ATOM
1685
CA
ALA
A
220
13.002
−2.019
66.486
1.00
10.37
A


ATOM
1686
CB
ALA
A
220
13.677
−1.616
65.172
1.00
9.86
A


ATOM
1687
C
ALA
A
220
11.959
−0.979
66.887
1.00
10.57
A


ATOM
1688
O
ALA
A
220
10.824
−1.007
66.399
1.00
10.66
A


ATOM
1689
N
ALA
A
221
12.339
−0.068
67.781
1.00
9.94
A


ATOM
1690
CA
ALA
A
221
11.419
0.963
68.246
1.00
10.32
A


ATOM
1691
CB
ALA
A
221
10.959
0.653
69.680
1.00
10.35
A


ATOM
1692
C
ALA
A
221
12.045
2.352
68.192
1.00
10.54
A


ATOM
1693
O
ALA
A
221
13.237
2.518
68.475
1.00
9.74
A


ATOM
1694
N
LEU
A
222
11.223
3.341
67.840
1.00
10.56
A


ATOM
1695
CA
LEU
A
222
11.664
4.731
67.735
1.00
11.43
A


ATOM
1696
CB
LEU
A
222
11.676
5.180
66.269
1.00
12.57
A


ATOM
1697
CG
LEU
A
222
12.161
4.265
65.151
1.00
13.60
A


ATOM
1698
CD1
LEU
A
222
11.614
4.787
63.819
1.00
13.87
A


ATOM
1699
CD2
LEU
A
222
13.681
4.204
65.138
1.00
12.89
A


ATOM
1700
C
LEU
A
222
10.704
5.672
68.459
1.00
11.56
A


ATOM
1701
O
LEU
A
222
9.532
5.341
68.669
1.00
12.07
A


ATOM
1702
N
ILE
A
223
11.216
6.838
68.848
1.00
11.46
A


ATOM
1703
CA
ILE
A
223
10.393
7.887
69.447
1.00
11.36
A


ATOM
1704
CB
ILE
A
223
10.904
8.370
70.829
1.00
11.65
A


ATOM
1705
CG2
ILE
A
223
10.178
9.655
71.223
1.00
10.99
A


ATOM
1706
CG1
ILE
A
223
10.687
7.289
71.893
1.00
11.08
A


ATOM
1707
CD1
ILE
A
223
9.227
6.989
72.214
1.00
12.35
A


ATOM
1708
C
ILE
A
223
10.588
9.011
68.435
1.00
11.23
A


ATOM
1709
O
ILE
A
223
11.726
9.402
68.149
1.00
11.56
A


ATOM
1710
N
VAL
A
224
9.486
9.509
67.879
1.00
10.50
A


ATOM
1711
CA
VAL
A
224
9.522
10.570
66.876
1.00
10.56
A


ATOM
1712
CB
VAL
A
224
8.947
10.078
65.519
1.00
9.92
A


ATOM
1713
CG1
VAL
A
224
8.933
11.223
64.499
1.00
9.91
A


ATOM
1714
CG2
VAL
A
224
9.770
8.915
64.999
1.00
9.84
A


ATOM
1715
C
VAL
A
224
8.705
11.782
67.310
1.00
10.99
A


ATOM
1716
O
VAL
A
224
7.578
11.644
67.789
1.00
10.91
A


ATOM
1717
N
GLY
A
225
9.276
12.970
67.135
1.00
11.59
A


ATOM
1718
CA
GLY
A
225
8.567
14.181
67.499
1.00
11.11
A


ATOM
1719
C
GLY
A
225
9.126
15.444
66.874
1.00
11.82
A


ATOM
1720
O
GLY
A
225
10.297
15.500
66.488
1.00
10.35
A


ATOM
1721
N
SER
A
226
8.273
16.457
66.761
1.00
12.29
A


ATOM
1722
CA
SER
A
226
8.676
17.755
66.230
1.00
13.04
A


ATOM
1723
CB
SER
A
226
7.557
18.364
65.376
1.00
13.32
A


ATOM
1724
OG
SER
A
226
7.422
17.697
64.133
1.00
14.87
A


ATOM
1725
C
SER
A
226
8.940
18.661
67.437
1.00
13.71
A


ATOM
1726
O
SER
A
226
8.429
18.406
65.533
1.00
13.89
A


ATOM
1727
N
ASP
A
227
9.746
19.701
67.240
1.00
13.96
A


ATOM
1728
CA
ASP
A
227
10.056
20.659
68.304
1.00
14.97
A


ATOM
1729
CB
ASP
A
227
8.775
21.400
68.711
1.00
15.35
A


ATOM
1730
CG
ASP
A
227
7.974
21.886
67.512
1.00
15.96
A


ATOM
1731
OD1
ASP
A
227
8.588
22.393
66.551
1.00
16.70
A


ATOM
1732
OD2
ASP
A
227
6.729
21.766
67.536
1.00
17.02
A


ATOM
1733
C
ASP
A
227
10.705
20.040
69.549
1.00
15.00
A


ATOM
1734
O
ASP
A
227
10.144
20.093
70.646
1.00
14.00
A


ATOM
1735
N
PRO
A
228
11.906
19.458
69.398
1.00
15.76
A


ATOM
1736
CD
PRO
A
228
12.704
19.370
68.165
1.00
16.05
A


ATOM
1737
CA
PRO
A
228
12.614
18.832
70.524
1.00
16.49
A


ATOM
1738
CB
PRO
A
228
13.862
18.230
69.868
1.00
16.50
A


ATOM
1739
CG
PRO
A
228
13.500
18.124
68.405
1.00
17.67
A


ATOM
1740
C
PRO
A
228
12.996
19.845
71.605
1.00
16.81
A


ATOM
1741
O
PRO
A
228
13.345
20.982
71.296
1.00
16.80
A


ATOM
1742
N
VAL
A
229
12.936
19.432
72.868
1.00
17.75
A


ATOM
1743
CA
VAL
A
229
13.307
20.311
73.972
1.00
18.66
A


ATOM
1744
CB
VAL
A
229
12.759
19.777
75.319
1.00
18.87
A


ATOM
1745
CG1
VAL
A
229
13.106
20.735
76.442
1.00
18.50
A


ATOM
1746
CG2
VAL
A
229
11.252
19.587
75.231
1.00
19.24
A


ATOM
1747
C
VAL
A
229
14.842
20.357
74.024
1.00
19.25
A


ATOM
1748
O
VAL
A
229
15.490
19.361
74.338
1.00
19.01
A


ATOM
1749
N
PRO
A
230
15.440
21.516
73.703
1.00
19.93
A


ATOM
1750
CD
PRO
A
230
14.785
22.779
73.322
1.00
20.33
A


ATOM
1751
CA
PRO
A
230
16.898
21.673
73.713
1.00
20.52
A


ATOM
1752
CB
PRO
A
230
17.082
23.173
73.500
1.00
20.70
A


ATOM
1753
CG
PRO
A
230
15.912
23.527
72.641
1.00
20.85
A


ATOM
1754
C
PRO
A
230
17.585
21.188
74.986
1.00
21.15
A


ATOM
1755
O
PRO
A
230
17.133
21.471
76.092
1.00
20.91
A


ATOM
1756
N
GLU
A
231
18.677
20.450
74.807
1.00
21.72
A


ATOM
1757
CA
GLU
A
231
19.474
19.921
75.914
1.00
22.87
A


ATOM
1758
CB
GLU
A
231
19.977
21.072
76.790
1.00
24.06
A


ATOM
1759
CG
GLU
A
231
20.632
22.204
76.014
1.00
26.41
A


ATOM
1760
CD
GLU
A
231
21.929
21.795
75.342
1.00
28.22
A


ATOM
1761
OE1
GLU
A
231
22.428
22.575
74.502
1.00
29.91
A


ATOM
1762
OE2
GLU
A
231
22.458
20.705
75.654
1.00
29.36
A


ATOM
1763
C
GLU
A
231
18.778
18.879
76.792
1.00
22.51
A


ATOM
1764
O
GLU
A
231
19.405
18.321
77.693
1.00
23.39
A


ATOM
1765
N
ILE
A
232
17.492
18.626
76.548
1.00
21.33
A


ATOM
1766
CA
ILE
A
232
16.744
17.622
77.314
1.00
20.10
A


ATOM
1767
CB
ILE
A
232
15.372
18.165
77.808
1.00
20.35
A


ATOM
1768
CG2
ILE
A
232
14.505
17.021
78.323
1.00
20.81
A


ATOM
1769
CG1
ILE
A
232
15.588
19.189
78.927
1.00
20.76
A


ATOM
1770
CD1
ILE
A
232
16.381
18.652
80.107
1.00
20.81
A


ATOM
1771
C
ILE
A
232
16.511
16.406
78.418
1.00
19.24
A


ATOM
1772
O
ILE
A
232
16.779
15.270
76.808
1.00
18.76
A


ATOM
1773
N
GLU
A
233
15.998
16.654
75.218
1.00
18.19
A


ATOM
1774
CA
GLU
A
233
15.773
15.588
74.248
1.00
17.68
A


ATOM
1775
CB
GLU
A
233
14.435
15.796
73.516
1.00
16.61
A


ATOM
1776
CG
GLU
A
233
13.225
15.614
74.442
1.00
15.77
A


ATOM
1777
CD
GLU
A
233
11.878
15.811
73.763
1.00
15.66
A


ATOM
1778
OE1
GLU
A
233
11.663
16.888
73.164
1.00
14.98
A


ATOM
1779
OE2
GLU
A
233
11.024
14.894
73.846
1.00
13.88
A


ATOM
1780
C
GLU
A
233
16.969
15.696
73.304
1.00
18.08
A


ATOM
1781
O
GLU
A
233
17.581
16.763
73.202
1.00
18.12
A


ATOM
1782
N
LYS
A
234
17.316
14.606
72.626
1.00
18.13
A


ATOM
1783
CA
LYS
A
234
18.479
14.620
71.743
1.00
18.28
A


ATOM
1784
CB
LYS
A
234
19.609
13.818
72.391
1.00
19.97
A


ATOM
1785
CG
LYS
A
234
20.833
13.658
71.517
1.00
22.36
A


ATOM
1786
CD
LYS
A
234
21.912
12.864
72.228
1.00
24.07
A


ATOM
1787
CE
LYS
A
234
23.161
12.748
71.377
1.00
24.43
A


ATOM
1788
NZ
LYS
A
234
24.241
12.063
72.132
1.00
26.13
A


ATOM
1789
C
LYS
A
234
18.226
14.088
70.332
1.00
17.50
A


ATOM
1790
O
LYS
A
234
18.151
12.879
70.117
1.00
17.33
A


ATOM
1791
N
PRO
A
235
18.103
14.995
69.349
1.00
16.44
A


ATOM
1792
CD
PRO
A
235
18.018
16.454
69.532
1.00
16.79
A


ATOM
1793
CA
PRO
A
235
17.861
14.628
67.948
1.00
15.90
A


ATOM
1794
CB
PRO
A
235
17.822
15.983
67.244
1.00
16.17
A


ATOM
1795
CG
PRO
A
235
17.250
16.890
68.297
1.00
17.19
A


ATOM
1796
C
PRO
A
235
18.948
13.719
67.365
1.00
15.14
A


ATOM
1797
O
PRO
A
235
20.133
13.916
67.642
1.00
15.33
A


ATOM
1798
N
ILE
A
236
18.540
12.739
66.559
1.00
13.84
A


ATOM
1799
CA
ILE
A
236
19.475
11.815
65.914
1.00
13.10
A


ATOM
1800
CB
ILE
A
236
19.117
10.335
66.217
1.00
12.82
A


ATOM
1801
CG2
ILE
A
236
20.170
9.416
65.618
1.00
13.36
A


ATOM
1802
CG1
ILE
A
236
19.028
10.104
67.727
1.00
12.98
A


ATOM
1803
CD1
ILE
A
236
18.623
8.689
68.107
1.00
13.32
A


ATOM
1804
C
ILE
A
236
19.454
12.029
64.389
1.00
12.89
A


ATOM
1805
O
ILE
A
236
20.503
12.188
63.760
1.00
12.73
A


ATOM
1806
N
PHE
A
237
18.254
12.019
63.808
1.00
12.93
A


ATOM
1807
CA
PHE
A
237
18.052
12.233
62.372
1.00
13.23
A


ATOM
1808
CB
PHE
A
237
17.878
10.894
61.631
1.00
13.29
A


ATOM
1809
CG
PHE
A
237
19.118
10.037
61.594
1.00
13.07
A


ATOM
1810
CD1
PHE
A
237
20.214
10.398
60.812
1.00
13.37
A


ATOM
1811
CD2
PHE
A
237
19.183
8.860
62.334
1.00
13.32
A


ATOM
1812
CE1
PHE
A
237
21.359
9.594
60.769
1.00
13.12
A


ATOM
1813
CE2
PHE
A
237
20.321
8.050
62.300
1.00
13.01
A


ATOM
1814
CZ
PHE
A
237
21.411
8.418
61.515
1.00
13.20
A


ATOM
1815
C
PHE
A
237
16.769
13.057
62.185
1.00
13.74
A


ATOM
1816
O
PHE
A
237
15.818
12.909
62.953
1.00
14.05
A


ATOM
1817
N
GLU
A
238
16.744
13.917
61.170
1.00
14.11
A


ATOM
1818
CA
GLU
A
238
15.558
14.728
60.873
1.00
14.73
A


ATOM
1819
CB
GLU
A
238
15.917
16.213
60.718
1.00
15.82
A


ATOM
1820
CG
GLU
A
238
16.429
16.918
61.958
1.00
18.71
A


ATOM
1821
CD
GLU
A
238
16.434
18.438
61.794
1.00
21.33
A


ATOM
1822
OE1
GLU
A
238
17.008
18.939
60.803
1.00
22.01
A


ATOM
1823
OE2
GLU
A
238
15.856
19.135
62.657
1.00
22.77
A


ATOM
1824
C
GLU
A
238
14.963
14.251
59.548
1.00
14.20
A


ATOM
1825
O
GLU
A
238
15.707
13.948
58.614
1.00
13.90
A


ATOM
1826
N
MET
A
239
13.638
14.180
59.456
1.00
13.86
A


ATOM
1827
CA
MET
A
239
13.008
13.766
58.205
1.00
14.51
A


ATOM
1828
CB
MET
A
239
11.702
13.006
58.468
1.00
15.35
A


ATOM
1829
CG
MET
A
239
11.940
11.583
58.970
1.00
17.08
A


ATOM
1830
SD
MET
A
239
10.448
10.564
59.044
1.00
19.48
A


ATOM
1831
CE
MET
A
239
9.981
10.786
60.745
1.00
18.17
A


ATOM
1832
C
MET
A
239
12.757
15.011
57.363
1.00
14.60
A


ATOM
1833
O
MET
A
239
12.329
16.047
57.884
1.00
13.98
A


ATOM
1834
N
VAL
A
240
13.041
14.905
56.067
1.00
14.28
A


ATOM
1835
CA
VAL
A
240
12.893
16.025
55.141
1.00
15.20
A


ATOM
1836
CB
VAL
A
240
14.224
16.271
54.375
1.00
15.56
A


ATOM
1837
CG1
VAL
A
240
14.091
17.470
53.452
1.00
15.90
A


ATOM
1838
CG2
VAL
A
240
15.366
16.479
55.363
1.00
16.93
A


ATOM
1839
C
VAL
A
240
11.784
15.875
54.096
1.00
15.14
A


ATOM
1840
O
VAL
A
240
11.009
16.803
53.865
1.00
14.78
A


ATOM
1841
N
TRP
A
241
11.715
14.706
53.466
1.00
15.48
A


ATOM
1842
CA
TRP
A
241
10.740
14.462
52.405
1.00
15.48
A


ATOM
1843
CB
TRP
A
241
11.309
15.035
51.104
1.00
17.25
A


ATOM
1844
CG
TRP
A
241
10.446
14.908
49.891
1.00
18.55
A


ATOM
1845
CD2
TRP
A
241
10.627
13.993
48.802
1.00
19.60
A


ATOM
1846
CE2
TRP
A
241
9.618
14.267
47.851
1.00
20.24
A


ATOM
1847
CE3
TRP
A
241
11.544
12.968
48.536
1.00
19.96
A


ATOM
1848
CD1
TRP
A
241
9.363
15.674
49.571
1.00
19.19
A


ATOM
1849
NE1
TRP
A
241
8.860
15.296
48.345
1.00
20.36
A


ATOM
1850
CZ2
TRP
A
241
9.503
13.554
46.652
1.00
20.07
A


ATOM
1851
CZ3
TRP
A
241
11.428
12.259
47.344
1.00
20.26
A


ATOM
1852
CH2
TRP
A
241
10.414
12.559
46.417
1.00
20.45
A


ATOM
1853
C
TRP
A
241
10.500
12.958
52.252
1.00
15.29
A


ATOM
1854
O
TRP
A
241
11.399
12.162
52.516
1.00
15.20
A


ATOM
1855
N
THR
A
242
9.297
12.570
51.827
1.00
14.37
A


ATOM
1856
CA
THR
A
242
8.984
11.149
51.636
1.00
13.75
A


ATOM
1857
CB
THR
A
242
8.150
10.563
52.815
1.00
14.23
A


ATOM
1858
OG1
THR
A
242
6.860
11.188
52.853
1.00
15.91
A


ATOM
1859
CG2
THR
A
242
8.863
10.780
54.144
1.00
13.74
A


ATOM
1860
C
THR
A
242
8.207
10.878
50.350
1.00
13.35
A


ATOM
1861
O
THR
A
242
7.526
11.757
49.820
1.00
13.22
A


ATOM
1862
N
ALA
A
243
8.310
9.648
49.856
1.00
12.74
A


ATOM
1863
CA
ALA
A
243
7.607
9.244
48.646
1.00
12.52
A


ATOM
1864
CB
ALA
A
243
8.379
9.702
47.410
1.00
12.73
A


ATOM
1865
C
ALA
A
243
7.422
7.726
48.611
1.00
12.56
A


ATOM
1866
O
ALA
A
243
8.142
6.988
49.285
1.00
12.38
A


ATOM
1867
N
GLN
A
244
6.430
7.276
47.848
1.00
12.33
A


ATOM
1868
CA
GLN
A
244
6.158
5.850
47.681
1.00
13.23
A


ATOM
1869
CB
GLN
A
244
5.005
5.372
48.581
1.00
13.07
A


ATOM
1870
CG
GLN
A
244
4.761
3.860
48.475
1.00
12.26
A


ATOM
1871
CD
GLN
A
244
3.457
3.383
49.114
1.00
12.34
A


ATOM
1872
OE1
GLN
A
244
2.378
3.893
48.811
1.00
12.05
A


ATOM
1873
NE2
GLN
A
244
3.556
2.379
49.989
1.00
10.52
A


ATOM
1874
C
GLN
A
244
5.753
5.660
46.225
1.00
13.65
A


ATOM
1875
O
GLN
A
244
4.996
6.466
45.681
1.00
13.54
A


ATOM
1876
N
THR
A
245
6.260
4.611
45.588
1.00
14.00
A


ATOM
1877
CA
THR
A
245
5.903
4.361
44.200
1.00
14.97
A


ATOM
1878
CB
THR
A
245
6.862
5.104
43.240
1.00
15.16
A


ATOM
1879
OG1
THR
A
245
6.295
5.121
41.922
1.00
16.09
A


ATOM
1880
CG2
THR
A
245
8.222
4.418
43.201
1.00
16.31
A


ATOM
1881
C
THR
A
245
5.908
2.872
43.875
1.00
15.50
A


ATOM
1882
O
THR
A
245
6.472
2.069
44.616
1.00
15.47
A


ATOM
1883
N
ILE
A
246
5.257
2.516
42.770
1.00
16.25
A


ATOM
1884
CA
ILE
A
246
5.174
1.136
42.309
1.00
16.49
A


ATOM
1885
CD
ILE
A
246
3.698
0.719
42.056
1.00
16.23
A


ATOM
1886
CG2
ILE
A
246
3.636
−0.679
41.456
1.00
15.84
A


ATOM
1887
CG1
ILE
A
246
2.915
0.748
43.376
1.00
15.94
A


ATOM
1888
CD1
ILE
A
246
1.417
0.555
43.212
1.00
15.61
A


ATOM
1889
C
ILE
A
246
5.960
1.046
41.001
1.00
18.27
A


ATOM
1890
O
ILE
A
246
5.689
1.790
40.058
1.00
17.51
A


ATOM
1891
N
ALA
A
247
6.937
0.145
40.956
1.00
19.38
A


ATOM
1892
CA
ALA
A
247
7.770
−0.025
39.768
1.00
21.64
A


ATOM
1893
CB
ALA
A
247
8.938
−0.960
40.080
1.00
21.46
A


ATOM
1894
C
ALA
A
247
6.971
−0.566
38.584
1.00
23.14
A


ATOM
1895
O
ALA
A
247
6.131
−1.451
38.743
1.00
23.05
A


ATOM
1896
N
PRO
A
248
7.223
−0.033
37.378
1.00
24.93
A


ATOM
1897
CD
PRO
A
248
8.193
1.027
37.042
1.00
25.33
A


ATOM
1898
CA
PRO
A
248
6.510
−0.488
36.183
1.00
26.41
A


ATOM
1899
CB
PRO
A
248
6.983
0.490
35.107
1.00
26.16
A


ATOM
1900
CG
PRO
A
248
8.370
0.834
35.554
1.00
26.28
A


ATOM
1901
C
PRO
A
248
6.835
−1.945
35.847
1.00
28.02
A


ATOM
1902
O
PRO
A
248
7.964
−2.401
36.040
1.00
28.21
A


ATOM
1903
N
ASP
A
249
5.832
−2.667
35.354
1.00
29.84
A


ATOM
1904
CA
ASP
A
249
5.982
−4.077
34.997
1.00
31.50
A


ATOM
1905
CB
ASP
A
249
6.744
−4.214
33.680
1.00
32.96
A


ATOM
1906
CG
ASP
A
249
5.969
−3.663
32.506
1.00
34.22
A


ATOM
1907
OD1
ASP
A
249
4.816
−4.104
32.299
1.00
35.29
A


ATOM
1908
OD2
ASP
A
249
6.512
−2.794
31.792
1.00
35.24
A


ATOM
1909
C
ASP
A
249
6.691
−4.878
36.077
1.00
31.86
A


ATOM
1910
O
ASP
A
249
7.796
−5.379
35.867
1.00
32.42
A


ATOM
1911
N
SER
A
250
6.049
−5.004
37.232
1.00
31.79
A


ATOM
1912
CA
SER
A
250
6.629
−5.747
38.338
1.00
31.71
A


ATOM
1913
CB
SER
A
250
7.363
−4.793
39.281
1.00
31.24
A


ATOM
1914
OG
SER
A
250
6.458
−3.890
39.883
1.00
30.46
A


ATOM
1915
C
SER
A
250
5.556
−6.506
39.111
1.00
31.85
A


ATOM
1916
O
SER
A
250
5.839
−7.133
40.129
1.00
31.15
A


ATOM
1917
N
GLU
A
251
4.321
−6.441
38.624
1.00
32.41
A


ATOM
1918
CA
GLU
A
251
3.219
−7.135
39.275
1.00
32.93
A


ATOM
1919
CB
GLU
A
251
1.915
−6.885
38.510
1.00
34.41
A


ATOM
1920
CG
GLU
A
251
0.667
−7.443
39.186
1.00
36.20
A


ATOM
1921
CD
GLU
A
251
−0.612
−7.063
38.459
1.00
37.28
A


ATOM
1922
OE1
GLU
A
251
−1.705
−7.458
38.925
1.00
37.89
A


ATOM
1923
OE2
GLU
A
251
−0.525
−6.368
37.421
1.00
38.05
A


ATOM
1924
C
GLU
A
251
3.542
−8.625
39.301
1.00
32.68
A


ATOM
1925
O
GLU
A
251
3.762
−9.240
38.254
1.00
32.66
A


ATOM
1926
N
GLY
A
252
3.595
−9.196
40.501
1.00
32.04
A


ATOM
1927
CA
GLY
A
252
3.901
−10.609
40.637
1.00
30.95
A


ATOM
1928
C
GLY
A
252
5.326
−10.861
41.093
1.00
30.57
A


ATOM
1929
O
GLY
A
252
5.672
−11.974
41.488
1.00
30.50
A


ATOM
1930
N
ALA
A
253
6.159
−9.827
41.045
1.00
29.95
A


ATOM
1931
CA
ALA
A
253
7.553
−9.955
41.454
1.00
29.30
A


ATOM
1932
CB
ALA
A
253
8.253
−8.608
41.344
1.00
29.04
A


ATOM
1933
C
ALA
A
253
7.670
−10.494
42.876
1.00
29.10
A


ATOM
1934
O
ALA
A
253
8.502
−11.358
43.153
1.00
28.97
A


ATOM
1935
N
ILE
A
254
6.833
−9.977
43.772
1.00
29.05
A


ATOM
1936
CA
ILE
A
254
6.827
−10.404
45.169
1.00
28.75
A


ATOM
1937
CB
ILE
A
254
7.611
−9.424
46.070
1.00
28.87
A


ATOM
1938
CG2
ILE
A
254
7.593
−9.922
47.511
1.00
29.14
A


ATOM
1939
CG1
ILE
A
254
9.055
−9.287
45.584
1.00
29.03
A


ATOM
1940
CD1
ILE
A
254
9.901
−10.528
45.803
1.00
30.14
A


ATOM
1941
C
ILE
A
254
5.387
−10.447
45.670
1.00
28.64
A


ATOM
1942
O
ILE
A
254
4.730
−9.411
45.773
1.00
28.64
A


ATOM
1943
N
ASP
A
255
4.895
−11.639
45.989
1.00
28.26
A


ATOM
1944
CA
ASP
A
255
3.525
−11.762
46.471
1.00
27.70
A


ATOM
1945
CB
ASP
A
255
2.598
−12.163
45.322
1.00
29.83
A


ATOM
1946
CG
ASP
A
255
2.660
−13.643
45.016
1.00
32.19
A


ATOM
1947
OD1
ASP
A
255
2.153
−14.443
45.835
1.00
33.88
A


ATOM
1948
OD2
ASP
A
255
3.222
−14.012
43.964
1.00
33.72
A


ATOM
1949
C
ASP
A
255
3.401
−12.778
47.600
1.00
26.17
A


ATOM
1950
O
ASP
A
255
4.086
−13.803
47.612
1.00
26.56
A


ATOM
1951
N
GLY
A
256
2.519
−12.483
48.548
1.00
23.34
A


ATOM
1952
CA
GLY
A
256
2.304
−13.379
49.664
1.00
20.65
A


ATOM
1953
C
GLY
A
256
0.831
−13.708
49.807
1.00
18.54
A


ATOM
1954
O
GLY
A
256
−0.030
−12.931
49.389
1.00
17.67
A


ATOM
1955
N
HIS
A
257
0.537
−14.862
50.395
1.00
17.10
A


ATOM
1956
CA
HIS
A
257
−0.844
−15.289
50.586
1.00
16.09
A


ATOM
1957
CB
HIS
A
257
−1.205
−16.374
49.567
1.00
17.01
A


ATOM
1958
CG
HIS
A
257
−0.976
−15.973
48.141
1.00
17.98
A


ATOM
1959
CD2
HIS
A
257
−0.126
−16.458
47.204
1.00
18.47
A


ATOM
1960
ND1
HIS
A
257
−1.680
−14.957
47.529
1.00
18.29
A


ATOM
1961
CE1
HIS
A
257
−1.275
−14.836
46.276
1.00
18.53
A


ATOM
1962
NE2
HIS
A
257
−0.332
−15.734
46.054
1.00
18.65
A


ATOM
1963
C
HIS
A
257
−1.034
−15.842
51.997
1.00
15.08
A


ATOM
1964
O
HIS
A
257
−0.328
−16.771
52.400
1.00
14.51
A


ATOM
1965
N
LEU
A
258
−1.981
−15.274
52.744
1.00
13.67
A


ATOM
1966
CA
LEU
A
258
−2.269
−15.735
54.104
1.00
12.94
A


ATOM
1967
CB
LEU
A
258
−2.743
−14.565
54.973
1.00
13.79
A


ATOM
1968
CG
LEU
A
258
−2.864
−14.775
56.490
1.00
14.04
A


ATOM
1969
CD1
LEU
A
258
−3.994
−15.736
56.802
1.00
15.09
A


ATOM
1970
CD2
LEU
A
258
−1.542
−15.300
57.035
1.00
13.98
A


ATOM
1971
C
LEU
A
258
−3.369
−16.789
53.972
1.00
12.65
A


ATOM
1972
O
LEU
A
258
−4.527
−16.484
53.684
1.00
11.92
A


ATOM
1973
N
ARG
A
259
−2.998
−18.047
54.185
1.00
11.51
A


ATOM
1974
CA
ARG
A
259
−3.927
−19.162
54.033
1.00
12.09
A


ATOM
1975
CB
ARG
A
259
−3.614
−19.896
52.723
1.00
12.33
A


ATOM
1976
CG
ARG
A
259
−3.690
−19.023
51.473
1.00
12.60
A


ATOM
1977
CD
ARG
A
259
−5.127
−18.640
51.129
1.00
13.20
A


ATOM
1978
NE
ARG
A
259
−5.220
−17.892
49.874
1.00
13.86
A


ATOM
1979
CZ
ARG
A
259
−5.066
−16.575
49.767
1.00
14.56
A


ATOM
1980
NH1
ARG
A
259
−4.814
−15.846
50.843
1.00
13.37
A


ATOM
1981
NH2
ARG
A
259
−5.163
−15.987
48.580
1.00
14.20
A


ATOM
1982
C
ARG
A
259
−3.892
−20.155
55.194
1.00
12.02
A


ATOM
1983
O
ARG
A
259
−3.224
−19.925
56.208
1.00
11.93
A


ATOM
1984
N
GLU
A
260
−4.608
−21.266
55.032
1.00
12.07
A


ATOM
1985
CA
GLU
A
260
−4.677
−22.293
56.067
1.00
11.81
A


ATOM
1986
CB
GLU
A
260
−5.658
−23.401
55.638
1.00
12.66
A


ATOM
1987
CG
GLU
A
260
−7.136
−22.962
55.733
1.00
12.50
A


ATOM
1988
CD
GLU
A
260
−8.119
−23.909
55.037
1.00
13.49
A


ATOM
1989
OE1
GLU
A
260
−8.009
−25.138
55.209
1.00
13.25
A


ATOM
1990
OE2
GLU
A
260
−9.020
−23.414
54.323
1.00
13.98
A


ATOM
1991
C
GLU
A
260
−3.314
−22.877
56.433
1.00
12.29
A


ATOM
1992
O
GLU
A
260
−3.138
−23.412
57.531
1.00
12.18
A


ATOM
1993
N
ALA
A
261
−2.344
−22.760
55.530
1.00
12.23
A


ATOM
1994
CA
ALA
A
261
−1.006
−23.282
55.789
1.00
12.39
A


ATOM
1995
CB
ALA
A
261
−0.454
−23.962
54.531
1.00
13.04
A


ATOM
1996
C
ALA
A
261
−0.047
−22.180
56.255
1.00
12.98
A


ATOM
1997
O
ALA
A
261
1.165
−22.383
56.308
1.00
12.59
A


ATOM
1998
N
GLY
A
262
−0.591
−21.016
56.596
1.00
13.18
A


ATOM
1999
CA
GLY
A
262
0.249
−19.916
57.033
1.00
13.93
A


ATOM
2000
C
GLY
A
262
0.495
−18.934
55.902
1.00
14.52
A


ATOM
2001
O
GLY
A
262
−0.305
−18.850
54.965
1.00
14.28
A


ATOM
2002
N
LEU
A
263
1.598
−18.193
59.981
1.00
15.26
A


ATOM
2003
CA
LEU
A
283
1.944
−17.210
54.954
1.00
16.05
A


ATOM
2004
CB
LEU
A
263
2.466
−15.924
55.609
1.00
15.77
A


ATOM
2005
CG
LEU
A
263
2.933
−14.826
54.646
1.00
15.80
A


ATOM
2006
CD1
LEU
A
263
1.737
−14.294
53.861
1.00
16.55
A


ATOM
2007
CD2
LEU
A
263
3.604
−13.700
55.424
1.00
15.82
A


ATOM
2008
C
LEU
A
263
2.997
−17.737
53.976
1.00
17.41
A


ATOM
2009
O
LEU
A
263
4.087
−18.131
54.388
1.00
15.70
A


ATOM
2010
N
THR
A
264
2.669
−17.745
52.683
1.00
19.51
A


ATOM
2011
CA
THR
A
264
3.604
−18.203
51.652
1.00
22.55
A


ATOM
2012
CB
THR
A
264
3.032
−19.396
50.841
1.00
22.62
A


ATOM
2013
OG1
THR
A
264
1.814
−19.005
50.193
1.00
22.53
A


ATOM
2014
CG2
THR
A
264
2.758
−20.578
51.759
1.00
22.97
A


ATOM
2015
C
THR
A
264
3.930
−17.061
50.684
1.00
25.08
A


ATOM
2016
O
THR
A
264
3.152
−16.116
50.553
1.00
24.86
A


ATOM
2017
N
PHE
A
285
5.080
−17.150
50.014
1.00
27.68
A


ATOM
2018
CA
PHE
A
265
5.520
−16.124
49.059
1.00
30.90
A


ATOM
2019
CB
PHE
A
265
6.761
−15.399
49.590
1.00
31.48
A


ATOM
2020
CG
PHE
A
265
6.458
−14.282
50.550
1.00
31.83
A


ATOM
2021
CD1
PHE
A
265
5.800
−13.133
50.116
1.00
32.13
A


ATOM
2022
CD2
PHE
A
265
6.851
−14.364
51.882
1.00
31.97
A


ATOM
2023
CE1
PHE
A
265
5.541
−12.080
50.997
1.00
31.84
A


ATOM
2024
CE2
PHE
A
265
6.595
−13.316
52.770
1.00
32.16
A


ATOM
2025
CZ
PHE
A
265
5.941
−12.174
52.325
1.00
31.81
A


ATOM
2026
C
PHE
A
265
5.844
−16.701
47.679
1.00
33.06
A


ATOM
2027
O
PHE
A
265
6.356
−17.817
47.572
1.00
33.32
A


ATOM
2028
N
HIS
A
266
5.552
−15.931
46.630
1.00
35.28
A


ATOM
2029
CA
HIS
A
266
5.803
−16.354
45.249
1.00
37.58
A


ATOM
2030
CB
HIS
A
266
4.495
−16.800
44.589
1.00
38.61
A


ATOM
2031
CG
HIS
A
266
3.760
−17.857
45.355
1.00
40.09
A


ATOM
2032
CD2
HIS
A
266
3.407
−19.120
45.018
1.00
40.75
A


ATOM
2033
ND1
HIS
A
266
3.288
−17.657
46.635
1.00
40.98
A


ATOM
2034
CE1
HIS
A
266
2.674
−18.750
47.053
1.00
41.00
A


ATOM
2035
NE2
HIS
A
266
2.732
−19.653
46.090
1.00
41.36
A


ATOM
2036
C
HIS
A
266
6.427
−15.224
44.421
1.00
38.52
A


ATOM
2037
O
HIS
A
266
5.931
−14.096
44.426
1.00
38.95
A


ATOM
2038
N
LEU
A
267
7.503
−15.533
43.699
1.00
39.31
A


ATOM
2039
CA
LEU
A
267
8.197
−14.531
42.889
1.70
39.61
A


ATOM
2040
CB
LEU
A
267
9.705
−14.576
43.174
1.00
39.95
A


ATOM
2041
CG
LEU
A
267
10.194
−14.308
44.603
1.00
40.58
A


ATOM
2042
CD1
LEU
A
267
9.725
−15.410
45.541
1.00
40.74
A


ATOM
2043
CD2
LEU
A
267
11.711
−14.243
44.608
1.00
40.64
A


ATOM
2044
C
LEU
A
267
7.975
−14.660
41.381
1.00
39.65
A


ATOM
2045
O
LEU
A
267
7.598
−15.719
40.878
1.00
39.80
A


ATOM
2046
N
ALA
A
268
8.217
−13.562
40.670
1.00
39.52
A


ATOM
2047
CA
ALA
A
268
8.069
−13.510
39.218
1.00
39.27
A


ATOM
2048
CB
ALA
A
268
6.646
−13.114
38.846
1.00
39.26
A


ATOM
2049
C
ALA
A
268
9.062
−12.486
30.673
1.00
39.03
A


ATOM
2050
O
ALA
A
268
8.990
−11.303
39.004
1.00
39.11
A


ATOM
2051
N
GLY
A
269
9.988
−12.942
37.837
1.00
38.84
A


ATOM
2052
CA
GLY
A
269
10.985
−12.040
37.288
1.00
38.15
A


ATOM
2053
C
GLY
A
269
12.158
−11.931
38.247
1.00
37.50
A


ATOM
2054
O
GLY
A
269
12.241
−12.699
39.206
1.00
37.96
A


ATOM
2055
N
ALA
A
270
13.058
−10.983
38.003
1.00
36.27
A


ATOM
2056
CA
ALA
A
270
14.223
−10.808
38.865
1.00
34.83
A


ATOM
2057
CB
ALA
A
270
15.486
−10.771
38.019
1.00
35.40
A


ATOM
2058
C
ALA
A
270
14.130
−9.547
39.724
1.00
33.76
A


ATOM
2059
O
ALA
A
270
14.279
−8.431
39.224
1.00
33.47
A


ATOM
2060
N
VAL
A
271
13.892
−9.737
41.019
1.00
32.23
A


ATOM
2061
CA
VAL
A
271
13.773
−8.626
41.961
1.00
31.04
A


ATOM
2062
CB
VAL
A
271
13.521
−9.145
43.402
1.00
31.01
A


ATOM
2063
CG1
VAL
A
271
13.626
−8.003
44.404
1.00
30.77
A


ATOM
2064
CG2
VAL
A
271
12.151
−9.783
43.484
1.00
31.12
A


ATOM
2065
C
VAL
A
271
14.989
−7.697
41.972
1.00
29.97
A


ATOM
2066
O
VAL
A
271
14.841
−6.479
41.883
1.00
30.03
A


ATOM
2067
N
PRO
A
272
16.206
−8.256
42.086
1.00
29.22
A


ATOM
2068
CD
PRO
A
272
16.559
−9.677
42.254
1.00
28.94
A


ATOM
2069
CA
PRO
A
272
17.410
−7.417
42.104
1.00
28.46
A


ATOM
2070
CB
PRO
A
272
18.542
−8.442
42.131
1.00
28.41
A


ATOM
2071
CG
PRO
A
272
17.932
−9.590
42.878
1.00
28.73
A


ATOM
2072
C
PRO
A
272
17.509
−6.479
40.897
1.00
27.94
A


ATOM
2073
O
PRO
A
272
17.907
−5.323
41.032
1.00
27.50
A


ATOM
2074
N
ASP
A
273
17.147
−6.986
39.722
1.00
27.25
A


ATOM
2075
CA
ASP
A
273
17.193
−6.196
38.496
1.00
26.96
A


ATOM
2076
CB
ASP
A
273
16.970
−7.099
37.281
1.00
27.99
A


ATOM
2077
CG
ASP
A
273
18.228
−7.831
36.859
1.00
29.35
A


ATOM
2078
OD1
ASP
A
273
18.956
−8.347
37.734
1.00
30.19
A


ATOM
2079
OD2
ASP
A
273
18.488
−7.899
35.642
1.00
31.21
A


ATOM
2080
C
ASP
A
273
16.164
−5.070
38.494
1.00
26.29
A


ATOM
2081
O
ASP
A
273
16.457
−3.951
38.082
1.00
25.72
A


ATOM
2082
N
ILE
A
274
14.954
−5.368
38.952
1.00
26.11
A


ATOM
2083
CA
ILE
A
274
13.899
−4.363
38.990
1.00
25.68
A


ATOM
2084
CB
ILE
A
274
12.561
−4.987
39.440
1.00
25.78
A


ATOM
2085
CG2
ILE
A
274
11.480
−3.915
39.498
1.00
23.49
A


ATOM
2086
CG1
ILE
A
274
12.169
−6.103
38.465
1.00
26.11
A


ATOM
2087
CD1
ILE
A
274
10.946
−6.901
38.866
1.00
26.62
A


ATOM
2088
C
ILE
A
274
14.281
−3.215
39.925
1.00
25.55
A


ATOM
2089
O
ILE
A
274
14.087
−2.045
39.594
1.00
24.97
A


ATOM
2090
N
VAL
A
275
14.838
−3.350
41.086
1.00
25.89
A


ATOM
2091
CA
VAL
A
275
15.249
−2.530
42.048
1.00
26.31
A


ATOM
2092
CB
VAL
A
275
15.736
−3.164
43.380
1.00
26.56
A


ATOM
2093
CG1
VAL
A
275
16.295
−2.087
44.301
1.00
26.70
A


ATOM
2094
CG2
VAL
A
275
14.586
−3.886
44.068
1.00
26.15
A


ATOM
2095
C
VAL
A
275
16.371
−1.657
41.482
1.00
26.97
A


ATOM
2096
O
VAL
A
275
16.257
−0.433
41.458
1.00
27.12
A


ATOM
2097
N
SER
A
276
17.442
−2.289
41.006
1.00
27.37
A


ATOM
2098
CA
SER
A
276
18.587
−1.559
40.465
1.00
28.02
A


ATOM
2099
CB
SER
A
276
19.741
−2.526
40.173
1.00
28.39
A


ATOM
2100
OG
SER
A
276
19.374
−3.502
39.214
1.00
28.82
A


ATOM
2101
C
SER
A
276
18.286
−0.729
39.218
1.00
28.31
A


ATOM
2102
O
SER
A
276
18.977
−0.254
38.947
1.00
28.51
A


ATOM
2103
N
LYS
A
277
17.265
−1.116
38.461
1.00
28.38
A


ATOM
2104
CA
LYS
A
277
16.901
−0.379
37.255
1.00
28.77
A


ATOM
2105
CB
LYS
A
277
16.196
−1.298
36.255
1.00
30.10
A


ATOM
2106
CG
LYS
A
277
17.077
−2.408
35.702
1.00
32.06
A


ATOM
2107
CD
LYS
A
277
16.333
−3.237
34.667
1.00
33.51
A


ATOM
2108
CE
LYS
A
277
17.151
−4.443
34.229
1.00
34.41
A


ATOM
2109
NZ
LYS
A
277
18.471
−4.060
33.652
1.00
34.50
A


ATOM
2110
C
LYS
A
277
15.998
0.814
37.556
1.00
28.23
A


ATOM
2111
O
LYS
A
277
15.910
1.745
36.756
1.00
28.03
A


ATOM
2112
N
ASN
A
278
15.339
0.784
38.712
1.00
27.01
A


ATOM
2113
CA
ASN
A
278
14.427
1.853
39.115
1.00
26.27
A


ATOM
2114
CB
ASN
A
278
13.103
1.253
39.591
1.00
26.13
A


ATOM
2115
CG
ASN
A
278
12.247
0.739
38.447
1.00
26.09
A


ATOM
2116
OD1
ASN
A
278
11.588
1.516
37.752
1.00
26.66
A


ATOM
2117
ND2
ASN
A
278
12.261
−0.572
38.240
1.00
25.15
A


ATOM
2118
C
ASN
A
278
14.989
2.735
40.221
1.00
26.25
A


ATOM
2119
O
ASN
A
278
14.376
3.738
40.591
1.00
26.18
A


ATOM
2120
N
ILE
A
279
16.155
2.370
40.743
1.00
25.52
A


ATOM
2121
CA
ILE
A
279
16.762
3.123
41.830
1.00
25.04
A


ATOM
2122
CB
ILE
A
279
17.921
2.327
42.474
1.00
25.04
A


ATOM
2123
CG2
ILE
A
279
19.131
2.299
41.548
1.00
25.43
A


ATOM
2124
CG1
ILE
A
279
18.284
2.951
43.820
1.00
24.74
A


ATOM
2125
CD1
ILE
A
279
17.153
2.907
44.818
1.00
24.79
A


ATOM
2126
C
ILE
A
279
17.265
4.513
41.446
1.00
24.99
A


ATOM
2127
O
ILE
A
279
17.085
5.468
42.204
1.00
24.98
A


ATOM
2128
N
THR
A
280
17.887
4.636
40.276
1.00
24.16
A


ATOM
2129
CA
THR
A
280
18.406
5.927
39.846
1.00
23.97
A


ATOM
2130
CB
THR
A
280
19.122
5.831
38.480
1.00
23.59
A


ATOM
2131
OG1
THR
A
280
20.213
4.907
38.573
1.00
23.27
A


ATOM
2132
CG2
THR
A
280
19.661
7.195
38.069
1.00
23.09
A


ATOM
2133
C
THR
A
280
17.309
6.978
39.745
1.00
24.11
A


ATOM
2134
O
THR
A
280
17.489
8.109
40.197
1.00
23.96
A


ATOM
2135
N
LYS
A
281
16.172
6.608
39.161
1.00
24.39
A


ATOM
2136
CA
LYS
A
281
15.069
7.550
39.010
1.00
24.90
A


ATOM
2137
CB
LYS
A
281
13.962
6.949
38.140
1.00
26.58
A


ATOM
2138
CG
LYS
A
281
13.414
5.626
38.631
1.00
28.54
A


ATOM
2139
CD
LYS
A
281
12.272
5.129
37.750
1.00
30.15
A


ATOM
2140
CE
LYS
A
281
11.047
6.036
37.837
1.00
31.02
A


ATOM
2141
NZ
LYS
A
281
11.308
7.427
37.359
1.00
32.08
A


ATOM
2142
C
LYS
A
281
14.501
7.990
40.353
1.00
24.09
A


ATOM
2143
O
LYS
A
281
14.058
9.128
40.502
1.00
24.02
A


ATOM
2144
N
ALA
A
282
14.509
7.092
41.331
1.00
23.31
A


ATOM
2145
CA
ALA
A
282
14.004
7.434
42.658
1.00
22.44
A


ATOM
2146
CB
ALA
A
282
13.877
6.176
43.517
1.00
22.10
A


ATOM
2147
C
ALA
A
282
14.967
8.432
43.309
1.00
22.14
A


ATOM
2148
O
ALA
A
282
14.544
9.360
43.999
1.00
21.76
A


ATOM
2149
N
LEU
A
283
16.264
8.240
43.074
1.00
21.91
A


ATOM
2150
CA
LEU
A
283
17.298
9.119
43.627
1.00
22.25
A


ATOM
2151
CB
LEU
A
283
18.681
8.487
43.466
1.00
21.95
A


ATOM
2152
CG
LEU
A
283
19.137
7.434
44.471
1.00
21.65
A


ATOM
2153
CD1
LEU
A
283
20.407
6.781
43.954
1.00
21.52
A


ATOM
2154
CD2
LEU
A
283
19.372
8.078
45.837
1.00
20.87
A


ATOM
2155
C
LEU
A
283
17.324
10.498
42.977
1.00
22.77
A


ATOM
2156
O
LEU
A
283
17.448
11.513
43.667
1.00
22.46
A


ATOM
2157
N
VAL
A
284
17.235
10.535
41.651
1.00
23.26
A


ATOM
2158
CA
VAL
A
284
17.258
11.810
40.942
1.00
24.56
A


ATOM
2159
CB
VAL
A
284
17.197
11.617
39.402
1.00
24.60
A


ATOM
2160
CG1
VAL
A
204
18.434
10.888
38.922
1.00
24.22
A


ATOM
2161
CG2
VAL
A
284
15.948
10.847
39.018
1.00
25.47
A


ATOM
2162
C
VAL
A
284
16.099
12.696
41.371
1.00
25.10
A


ATOM
2163
O
VAL
A
284
16.268
13.896
41.576
1.00
26.07
A


ATOM
2164
N
GLU
A
285
14.924
12.097
41.520
1.00
25.93
A


ATOM
2165
CA
GLU
A
285
13.732
12.832
41.915
1.00
26.80
A


ATOM
2166
CB
GLU
A
285
12.500
11.947
41.715
1.00
28.36
A


ATOM
2167
CG
GLU
A
285
11.241
12.450
42.384
1.00
31.15
A


ATOM
2168
CD
GLU
A
285
10.001
11.815
41.809
1.00
32.58
A


ATOM
2169
OE1
GLU
A
285
10.025
10.588
41.569
1.00
34.38
A


ATOM
2170
OE2
GLU
A
285
9.000
12.538
41.599
1.00
34.22
A


ATOM
2171
C
GLU
A
285
13.788
13.347
43.351
1.00
26.74
A


ATOM
2172
O
GLU
A
285
13.174
14.363
43.676
1.00
26.52
A


ATOM
2173
N
ALA
A
286
14.534
12.655
44.205
1.00
26.28
A


ATOM
2174
CA
ALA
A
286
14.651
13.057
45.602
1.00
26.53
A


ATOM
2175
CB
ALA
A
286
14.821
11.821
46.477
1.00
25.97
A


ATOM
2176
C
ALA
A
286
15.797
14.035
45.864
1.00
26.80
A


ATOM
2177
O
ALA
A
286
15.683
14.921
46.713
1.00
26.76
A


ATOM
2178
N
PHE
A
287
16.894
13.884
45.127
1.00
27.08
A


ATOM
2179
CA
PHE
A
287
18.062
14.733
45.329
1.00
27.56
A


ATOM
2180
CB
PHE
A
287
19.294
13.848
45.536
1.00
26.16
A


ATOM
2181
CG
PHE
A
287
19.300
13.142
46.860
1.00
25.16
A


ATOM
2182
CD1
PHE
A
287
19.599
13.837
48.027
1.00
24.31
A


ATOM
2183
CD2
PHE
A
287
18.941
11.802
46.952
1.00
24.68
A


ATOM
2184
CE1
PHE
A
287
19.538
13.210
49.270
1.00
24.57
A


ATOM
2185
CE2
PHE
A
287
18.876
11.164
48.191
1.00
24.72
A


ATOM
2186
CZ
PHE
A
287
19.174
11.872
49.353
1.00
24.05
A


ATOM
2187
C
PHE
A
287
18.354
15.805
44.282
1.00
29.00
A


ATOM
2188
O
PHE
A
287
19.231
16.646
44.487
1.00
28.79
A


ATOM
2189
N
GLN
A
288
17.636
15.781
43.164
1.00
30.59
A


ATOM
2190
CA
GLN
A
288
17.845
16.801
42.138
1.00
32.44
A


ATOM
2191
CB
GLN
A
288
16.899
16.581
40.954
1.00
33.45
A


ATOM
2192
CG
GLN
A
288
17.114
17.546
39.799
1.00
35.64
A


ATOM
2193
CD
GLN
A
288
16.158
17.296
38.646
1.00
36.73
A


ATOM
2194
OE1
GLN
A
288
14.950
17.577
38.796
1.00
37.57
A


ATOM
2195
OE2
GLN
A
288
16.616
16.808
37.592
1.00
37.77
A


ATOM
2196
C
GLN
A
288
17.588
18.176
42.761
1.00
32.65
A


ATOM
2197
O
GLN
A
288
18.391
19.095
42.608
1.00
33.11
A


ATOM
2198
N
PRO
A
289
16.463
18.329
43.482
1.00
33.05
A


ATOM
2199
CD
PRO
A
289
15.364
17.358
43.650
1.00
33.26
A


ATOM
2200
CA
PRO
A
289
16.121
19.602
44.125
1.00
33.05
A


ATOM
2201
CB
PRO
A
289
14.818
19.279
44.851
1.00
33.14
A


ATOM
2202
CG
PRO
A
289
14.192
18.256
43.966
1.00
33.18
A


ATOM
2203
C
PRO
A
289
17.196
20.118
45.083
1.00
33.10
A


ATOM
2204
O
PRO
A
289
17.298
21.324
45.315
1.00
33.32
A


ATOM
2205
N
LEU
A
290
17.988
19.206
45.641
1.00
32.89
A


ATOM
2206
CA
LEU
A
290
19.047
19.580
46.577
1.00
32.40
A


ATOM
2207
CB
LEU
A
290
19.289
18.457
47.596
1.00
32.52
A


ATOM
2208
CG
LEU
A
290
18.136
18.060
48.524
1.00
32.73
A


ATOM
2209
CD1
LEU
A
290
18.595
16.961
49.469
1.00
32.65
A


ATOM
2210
CD2
LEU
A
290
17.672
19.267
49.313
1.00
32.85
A


ATOM
2211
C
LEU
A
290
20.351
19.887
45.852
1.00
32.01
A


ATOM
2212
O
LEU
A
290
21.323
20.330
46.468
1.00
31.92
A


ATOM
2213
N
GLY
A
291
20.363
19.640
44.545
1.00
31.46
A


ATOM
2214
CA
GLY
A
291
21.559
19.898
43.753
1.00
30.99
A


ATOM
2215
C
GLY
A
291
22.663
18.874
43.948
1.00
30.50
A


ATOM
2216
O
GLY
A
291
23.839
19.169
43.726
1.00
30.55
A


ATOM
2217
N
ILE
A
292
22.290
17.665
44.355
1.00
29.69
A


ATOM
2218
CA
ILE
A
292
23.261
16.601
44.583
1.00
29.08
A


ATOM
2219
CB
ILE
A
292
23.031
15.937
45.953
1.00
29.06
A


ATOM
2220
CG2
ILE
A
292
23.989
14.764
46.135
1.00
28.81
A


ATOM
2221
CG1
ILE
A
292
23.224
16.973
47.066
1.00
28.76
A


ATOM
2222
CD1
ILE
A
292
22.920
16.455
48.454
1.00
28.39
A


ATOM
2223
C
ILE
A
292
23.189
15.530
43.499
1.00
28.90
A


ATOM
2224
O
ILE
A
292
22.140
14.926
43.282
1.00
28.79
A


ATOM
2225
N
SER
A
293
24.312
15.302
42.821
1.00
28.59
A


ATOM
2226
CA
SER
A
293
24.381
14.304
41.756
1.00
28.30
A


ATOM
2227
CB
SER
A
293
24.792
14.969
40.440
1.00
28.20
A


ATOM
2228
OG
SER
A
293
26.091
15.529
40.548
1.00
28.70
A


ATOM
2229
C
SER
A
293
25.373
13.188
42.087
1.00
27.62
A


ATOM
2230
O
SER
A
293
25.332
12.119
41.485
1.00
27.89
A


ATOM
2231
N
ASP
A
294
26.265
13.446
43.039
1.00
27.00
A


ATOM
2232
CA
ASP
A
294
27.266
12.463
43.450
1.00
26.30
A


ATOM
2233
CB
ASP
A
294
28.587
13.173
43.769
1.00
27.80
A


ATOM
2234
CG
ASP
A
294
29.621
12.246
44.379
1.00
28.79
A


ATOM
2235
OD1
ASP
A
294
29.606
11.037
44.063
1.00
28.85
A


ATOM
2236
OD2
ASP
A
294
30.459
12.735
45.168
1.00
30.27
A


ATOM
2237
C
ASP
A
294
26.770
11.676
44.667
1.00
25.13
A


ATOM
2238
O
ASP
A
294
26.850
12.151
45.797
1.00
24.51
A


ATOM
2239
N
TYR
A
295
26.276
10.465
44.424
1.00
23.98
A


ATOM
2240
CA
TYR
A
295
25.727
9.628
45.487
1.00
22.92
A


ATOM
2241
CB
TYR
A
295
24.901
8.504
44.861
1.00
23.20
A


ATOM
2242
CG
TYR
A
235
23.850
9.050
43.922
1.00
23.56
A


ATOM
2243
CD1
TYR
A
295
22.910
9.985
44.366
1.00
24.31
A


ATOM
2244
CE1
TYR
A
295
21.984
10.552
43.491
1.00
24.25
A


ATOM
2245
CD2
TYR
A
295
23.833
8.690
42.573
1.00
24.63
A


ATOM
2246
CE2
TYR
A
295
22.911
9.251
41.688
1.00
24.54
A


ATOM
2247
CB
TYR
A
295
21.992
10.182
42.153
1.00
24.93
A


ATOM
2248
OH
TYR
A
295
21.095
10.752
41.279
1.00
24.87
A


ATOM
2249
C
TYR
A
295
26.723
9.088
46.514
1.00
22.33
A


ATOM
2250
O
TYR
A
295
26.338
8.392
47.455
1.00
21.89
A


AToM
2251
N
ASN
A
296
28.001
9.407
46.339
1.00
21.23
A


ATOM
2252
CA
ASN
A
296
29.011
8.999
47.306
1.00
20.36
A


ATOM
2253
CB
ASN
A
296
30.383
8.844
49.641
1.00
21.14
A


ATOM
2254
CG
ASN
A
296
30.596
7.460
46.052
1.00
20.97
A


ATOM
2255
OD1
ASN
A
296
30.624
6.464
46.776
1.00
21.95
A


ATOM
2256
ND2
ASN
A
296
30.749
7.392
44.735
1.00
20.64
A


ATOM
2257
C
ASN
A
296
29.073
10.104
48.359
1.00
19.68
A


ATOM
2258
O
ASN
A
296
29.722
9.959
49.395
1.00
19.26
A


ATOM
2259
N
SER
A
297
28.373
11.206
48.089
1.00
19.05
A


ATOM
2260
CA
SER
A
297
28.354
12.345
49.003
1.00
18.66
A


ATOM
2261
CB
SER
A
297
28.379
13.659
48.209
1.00
18.96
A


ATOM
2262
OG
SER
A
297
27.200
13.833
47.438
1.00
20.75
A


ATOM
2263
C
SER
A
297
27.196
12.379
50.006
1.00
18.07
A


ATOM
2264
O
SER
A
297
26.998
13.387
50.687
1.00
17.98
A


ATOM
2265
N
ILE
A
298
26.435
11.292
50.101
1.00
17.31
A


ATOM
2266
CA
ILE
A
298
25.312
11.216
51.046
1.00
16.71
A


ATOM
2267
CB
ILE
A
298
23.949
11.279
50.305
1.00
16.38
A


ATOM
2268
CG2
ILE
A
298
23.849
12.575
49.504
1.00
16.94
A


ATOM
2269
CG1
ILE
A
288
23.797
10.070
49.375
1.00
16.73
A


ATOM
2270
CD1
ILE
A
298
22.459
10.005
48.652
1.00
16.32
A


ATOM
2271
C
ILE
A
298
25.392
9.891
51.814
1.00
16.04
A


ATOM
2272
O
ILE
A
298
26.006
8.943
51.317
1.00
16.33
A


ATOM
2273
N
PHE
A
299
24.810
9.819
53.018
1.00
15.01
A


ATOM
2274
CA
PHE
A
299
24.843
8.556
53.759
1.00
14.11
A


ATOM
2275
CB
PHE
A
299
24.851
8.754
55.292
1.00
13.75
A


ATOM
2276
CG
PHE
A
299
23.689
9.547
55.850
1.00
12.78
A


ATOM
2277
CD1
PHE
A
299
23.713
10.939
55.852
1.00
12.57
A


ATOM
2278
CD2
PHE
A
299
22.616
8.897
56.455
1.00
12.47
A


ATOM
2279
CE1
PHE
A
299
22.687
11.674
56.458
1.00
12.78
A


ATOM
2280
CE2
PHE
A
299
21.583
9.620
57.064
1.00
12.49
A


ATOM
2281
CZ
PHE
A
299
21.620
11.012
57.066
1.00
12.45
A


ATOM
2282
C
PHE
A
299
23.698
7.645
53.311
1.00
14.17
A


ATOM
2283
O
PHE
A
299
22.620
8.119
52.932
1.00
14.13
A


ATOM
2284
N
TRP
A
300
23.953
6.338
53.347
1.00
13.43
A


ATOM
2285
CA
TRP
A
300
23.012
5.330
52.863
1.00
13.55
A


ATOM
2286
CB
TRP
A
300
23.689
4.499
51.756
1.00
13.64
A


ATOM
2287
CG
TRP
A
300
23.741
5.128
50.398
1.00
14.19
A


ATOM
2288
CD2
TRP
A
300
22.917
4.794
49.275
1.00
14.07
A


ATOM
2289
CE2
TRP
A
300
23.295
5.642
48.212
1.00
14.33
A


ATOM
2290
CE3
TRP
A
300
21.888
3.861
49.067
1.00
14.36
A


ATOM
2291
CD1
TRP
A
300
24.568
6.134
49.981
1.00
14.12
A


ATOM
2292
NE1
TRP
A
300
24.305
6.447
48.669
1.00
14.30
A


ATOM
2293
CZ2
TRP
A
300
22.683
5.585
46.953
1.00
14.52
A


ATOM
2294
CZ3
TRP
A
300
21.278
3.805
47.813
1.00
14.75
A


ATOM
2295
CH2
TRP
A
300
21.679
4.665
46.774
1.00
14.61
A


ATOM
2296
C
TRP
A
300
22.394
4.327
53.840
1.00
12.97
A


ATOM
2297
O
TRP
A
300
23.067
3.808
54.733
1.00
13.38
A


ATOM
2298
N
ILE
A
301
21.109
4.050
53.631
1.00
12.82
A


ATOM
2299
CA
ILE
A
301
20.370
3.041
54.389
1.00
12.85
A


ATOM
2300
CB
ILE
A
301
19.465
3.629
55.510
1.00
12.55
A


ATOM
2301
CG2
ILE
A
301
18.614
2.508
56.122
1.00
12.29
A


ATOM
2302
CG1
ILE
A
301
20.311
4.266
56.620
1.00
12.45
A


ATOM
2303
CD1
ILE
A
301
20.591
5.741
56.412
1.00
11.84
A


ATOM
2304
C
ILE
A
301
19.471
2.341
53.356
1.00
13.12
A


ATOM
2305
O
ILE
A
301
18.549
2.951
52.806
1.00
13.40
A


ATOM
2306
N
ALA
A
302
19.754
1.072
53.073
1.00
13.05
A


ATOM
2307
CA
ALA
A
302
18.965
0.321
52.093
1.00
13.27
A


ATOM
2308
CB
ALA
A
302
19.806
0.064
50.836
1.00
13.42
A


ATOM
2309
C
ALA
A
302
18.462
−1.006
52.658
1.00
13.08
A


ATOM
2310
O
ALA
A
302
19.217
−1.741
53.295
1.00
13.86
A


ATOM
2311
N
HIS
A
303
17.188
−1.313
52.425
1.00
12.38
A


ATOM
2312
CA
HIS
A
303
16.613
−2.566
52.905
1.00
12.20
A


ATOM
2313
CB
HIS
A
303
15.131
−2.673
52.516
1.00
11.11
A


ATOM
2314
CG
HIS
A
303
14.535
−4.016
52.809
1.00
10.71
A


ATOM
2315
CD2
HIS
A
302
14.074
−4.986
51.983
1.00
10.88
A


ATOM
2316
ND1
HIS
A
303
14.422
−4.518
54.088
1.00
11.15
A


ATOM
2317
CE1
HIS
A
303
13.918
−5.739
54.039
1.00
10.53
A


ATOM
2318
NE2
HIS
A
303
13.699
−6.047
52.773
1.00
10.34
A


ATOM
2319
C
HIS
A
303
17.390
−3.732
52.295
1.00
12.67
A


ATOM
2320
O
HIS
A
303
17.415
−3.901
51.076
1.00
12.89
A


ATOM
2321
N
PRO
A
304
18.033
−4.558
53.137
1.00
13.61
A


ATOM
2322
CD
PRO
A
304
18.161
−4.439
54.602
1.00
14.16
A


ATOM
2323
CA
PRO
A
304
18.808
−5.698
52.638
1.00
14.34
A


ATOM
2324
CB
PRO
A
304
19.786
−5.950
53.774
1.00
14.36
A


ATOM
2325
CG
PRO
A
304
18.916
−5.711
54.973
1.00
14.60
A


ATOM
2326
C
PRO
A
304
17.956
−6.929
52.324
1.00
14.55
A


ATOM
2327
O
PRO
A
304
18.096
−7.965
52.972
1.00
15.04
A


ATOM
2328
N
GLY
A
305
17.077
−6.809
51.331
1.00
14.61
A


ATOM
2329
CA
GLY
A
305
16.224
−7.925
50.966
1.00
14.76
A


ATOM
2330
C
GLY
A
305
17.055
−9.156
50.666
1.00
15.27
A


ATOM
2331
O
GLY
A
305
16.671
−10.275
51.006
1.00
15.14
A


ATOM
2332
N
GLY
A
306
18.199
−8.938
50.027
1.00
15.34
A


ATOM
2333
CA
GLY
A
306
19.102
−10.025
49.678
1.00
16.49
A


ATOM
2334
C
GLY
A
306
20.457
−9.455
49.307
1.00
16.93
A


ATOM
2335
O
GLY
A
306
20.564
−8.249
49.082
1.00
17.30
A


ATOM
2336
N
PRO
A
307
21.515
−10.278
49.228
1.00
17.46
A


ATOM
2337
CD
PRO
A
307
21.579
−11.730
49.472
1.00
18.01
A


ATOM
2338
CA
PRO
A
307
22.836
−9.748
48.874
1.00
18.03
A


ATOM
2339
CB
PRO
A
307
22.761
−10.938
49.126
1.00
18.12
A


ATOM
2340
CG
PRO
A
307
22.891
−12.109
48.814
1.00
18.51
A


ATOM
2341
C
PRO
A
307
22.949
−9.212
47.444
1.00
18.05
A


ATOM
2342
O
PRO
A
307
23.710
−8.272
47.184
1.00
17.85
A


ATOM
2343
N
ALA
A
308
22.191
−9.803
46.524
1.00
17.71
A


ATOM
2344
CA
ALA
A
308
22.224
−9.383
45.126
1.00
18.01
A


ATOM
2345
CB
ALA
A
308
21.413
−10.347
44.269
1.00
18.21
A


ATOM
2346
C
ALA
A
308
21.715
−7.956
44.926
1.00
18.23
A


ATOM
2347
O
ALA
A
308
22.236
−7.219
44.085
1.00
18.16
A


ATOM
2348
N
ILE
A
309
20.691
−7.569
45.681
1.00
17.84
A


ATOM
2349
CA
ILE
A
309
20.155
−6.217
45.561
1.00
17.99
A


ATOM
2350
CB
ILE
A
309
18.928
−6.011
46.480
1.00
18.26
A


ATOM
2351
CG2
ILE
A
309
18.527
−4.541
46.488
1.00
18.23
A


ATOM
2352
CG1
ILE
A
309
17.771
−6.893
45.999
1.00
18.73
A


ATOM
2353
CD1
ILE
A
309
16.508
−6.785
46.833
1.00
19.58
A


ATOM
2354
C
ILE
A
309
21.238
−5.204
45.925
1.00
17.80
A


ATOM
2355
O
ILE
A
309
21.412
−4.191
45.243
1.00
17.95
A


ATOM
2356
N
LEU
A
310
21.978
−5.488
46.992
1.00
17.66
A


ATOM
2357
CA
LEU
A
310
23.051
−4.600
47.428
1.00
17.75
A


ATOM
2358
CB
LEU
A
310
22.611
−5.070
48.774
1.00
17.50
A


ATOM
2359
CG
LEU
A
310
22.609
−5.217
49.926
1.00
17.03
A


ATOM
2360
CD1
LEU
A
310
23.348
−5.610
51.199
1.00
16.69
A


ATOM
2361
CD2
LEU
A
310
21.863
−3.908
50.138
1.00
17.12
A


ATOM
2362
C
LEU
A
310
24.182
−4.513
46.392
1.00
18.34
A


ATOM
2363
O
LEU
A
310
24.685
−3.422
46.102
1.00
17.54
A


ATOM
2364
N
ASP
A
311
24.578
−5.655
45.832
1.00
18.40
A


ATOM
2365
CA
ASP
A
311
25.645
−5.673
44.829
1.00
19.39
A


ATOM
2366
CB
ASP
A
311
25.973
−7.107
44.384
1.00
19.51
A


ATOM
2367
CG
ASP
A
311
26.604
−7.945
45.483
1.00
20.61
A


ATOM
2368
OD1
ASP
A
311
27.210
−7.374
46.416
1.00
20.57
A


ATOM
2369
OD2
ASP
A
311
26.509
−9.189
45.395
1.00
21.12
A


ATOM
2370
C
ASP
A
311
25.273
−4.860
43.588
1.00
19.57
A


ATOM
2371
O
ASP
A
311
26.079
−4.072
43.090
1.00
19.38
A


ATOM
2372
N
GLN
A
312
24.057
−5.059
43.086
1.00
20.06
A


ATOM
2373
CA
GLN
A
312
23.604
−4.351
41.890
1.00
20.92
A


ATOM
2374
CB
GLN
A
312
22.336
−5.011
41.331
1.00
21.67
A


ATOM
2375
CG
GLN
A
312
22.644
−6.263
40.511
1.00
22.92
A


ATOM
2376
CD
GLN
A
312
21.408
−6.980
40.001
1.00
23.83
A


ATOM
2377
OE1
GLN
A
312
20.503
−6.365
39.435
1.00
24.46
A


ATOM
2378
NE2
GLN
A
312
21.372
−8.297
40.187
1.00
24.27
A


ATOM
2379
C
GLN
A
312
23.389
−2.856
42.106
1.00
21.43
A


ATOM
2380
O
GLN
A
312
23.610
−2.054
41.193
1.00
21.12
A


ATOM
2381
N
VAL
A
313
22.964
−2.472
43.304
1.00
21.36
A


ATOM
2382
CA
VAL
A
313
22.772
−1.056
43.593
1.00
22.26
A


ATOM
2383
CB
VAL
A
313
22.064
−0.847
44.958
1.00
21.61
A


ATOM
2384
CG1
VAL
A
313
22.126
0.618
45.368
1.00
21.70
A


ATOM
2385
CG2
VAL
A
313
20.610
−1.280
44.856
1.00
21.27
A


ATOM
2386
C
VAL
A
313
24.152
−0.399
43.620
1.00
22.76
A


ATOM
2387
O
VAL
A
313
24.365
0.652
43.016
1.00
22.83
A


ATOM
2388
N
GLU
A
314
25.090
−1.044
44.306
1.00
23.89
A


ATOM
2389
CA
GLU
A
314
26.452
−0.539
44.423
1.00
24.82
A


ATOM
2390
CB
GLU
A
314
27.285
−1.490
45.290
1.00
26.33
A


ATOM
2391
CG
GLU
A
314
28.633
−0.930
45.720
1.00
28.97
A


ATOM
2392
CD
GLU
A
314
29.345
−1.809
46.737
1.00
30.11
A


ATOM
2393
OE1
GLU
A
314
28.730
−2.158
47.768
1.00
30.61
A


ATOM
2394
OE2
GLU
A
314
30.528
−2.141
46.511
1.00
31.99
A


ATOM
2395
C
GLU
A
314
27.107
−0.370
43.046
1.00
25.07
A


ATOM
2396
O
GLU
A
314
27.788
0.627
42.790
1.00
24.35
A


ATOM
2397
N
GLN
A
315
26.893
−1.339
42.162
1.00
24.83
A


ATOM
2398
CA
GLN
A
315
27.472
−1.280
40.823
1.00
25.91
A


ATOM
2399
CB
GLN
A
315
27.421
−2.664
40.165
1.00
26.90
A


ATOM
2400
CG
GLN
A
315
28.328
−3.678
40.846
1.00
29.10
A


ATOM
2401
CD
GLN
A
315
28.375
−5.012
40.128
1.00
31.04
A


ATOM
2402
OE1
GLN
A
315
28.733
−5.083
38.949
1.00
32.27
A


ATOM
2403
NE2
GLN
A
315
28.019
−6.083
40.838
1.00
31.39
A


ATOM
2404
C
GLN
A
315
26.787
−0.250
39.928
1.00
25.61
A


ATOM
2405
O
GLN
A
315
27.448
0.453
39.166
1.00
25.64
A


ATOM
2406
N
LYS
A
316
25.464
−0.161
40.030
1.00
25.14
A


ATOM
2407
CA
LYS
A
316
24.683
0.781
39.232
1.00
25.04
A


ATOM
2408
CB
LYS
A
316
23.187
0.591
39.524
1.00
26.09
A


ATOM
2409
CG
LYS
A
316
22.251
1.622
38.882
1.00
26.89
A


ATOM
2410
CD
LYS
A
316
21.711
1.164
37.528
1.00
27.90
A


ATOM
2411
CE
LYS
A
316
22.772
1.182
36.447
1.00
28.93
A


ATOM
2412
NZ
LYS
A
316
22.266
0.658
35.140
1.00
27.99
A


ATOM
2413
C
LYS
A
316
25.069
2.238
39.489
1.00
24.49
A


ATOM
2414
O
LYS
A
316
25.110
3.046
38.561
1.00
24.40
A


ATOM
2415
N
LEU
A
317
25.361
2.571
40.744
1.00
23.79
A


ATOM
2416
CA
LEU
A
317
25.712
3.941
41.112
1.00
23.24
A


ATOM
2417
CB
LEU
A
317
24.917
4.344
42.356
1.00
23.11
A


ATOM
2418
CG
LEU
A
317
23.407
4.110
42.247
1.00
22.79
A


ATOM
2419
CD1
LEU
A
317
22.780
4.131
43.631
1.00
22.84
A


ATOM
2420
CD2
LEU
A
317
22.786
5.164
41.335
1.00
22.52
A


ATOM
2421
C
LEU
A
317
27.204
4.175
41.361
1.00
23.10
A


ATOM
2422
O
LEU
A
317
27.602
5.265
41.773
1.00
23.32
A


ATOM
2423
N
ALA
A
318
28.021
3.156
41.115
1.00
22.49
A


ATOM
2424
CA
ALA
A
318
29.466
3.253
41.314
1.00
22.25
A


ATOM
2425
CB
ALA
A
318
30.080
4.152
40.238
1.00
22.73
A


ATOM
2426
C
ALA
A
318
29.823
3.781
42.705
1.00
22.10
A


ATOM
2427
O
ALA
A
318
30.592
4.735
42.837
1.00
21.67
A


ATOM
2428
N
LEU
A
319
29.271
3.148
43.738
1.00
21.00
A


ATOM
2429
CA
LEU
A
319
29.519
3.546
45.122
1.00
20.63
A


ATOM
2430
CB
LEU
A
319
28.350
3.104
46.010
1.00
20.00
A


ATOM
2431
CG
LEU
A
319
26.936
3.586
45.666
1.00
19.28
A


ATOM
2432
CD1
LEU
A
319
25.935
2.999
46.661
1.00
19.38
A


ATOM
2433
CD2
LEU
A
319
26.888
5.099
45.699
1.00
18.96
A


ATOM
2434
C
LEU
A
319
30.808
2.944
45.688
1.00
21.45
A


ATOM
2435
O
LEU
A
319
31.163
1.814
45.366
1.00
20.80
A


ATOM
2436
N
LYS
A
320
31.498
3.699
46.541
1.00
21.99
A


ATOM
2437
CA
LYS
A
320
32.717
3.203
47.173
1.00
23.22
A


ATOM
2438
CB
LYS
A
320
33.413
4.315
47.966
1.00
24.04
A


ATOM
2439
CG
LYS
A
320
33.695
5.585
47.170
1.00
26.42
A


ATOM
2440
CD
LYS
A
320
34.439
6.616
48.014
1.00
27.32
A


ATOM
2441
CE
LYS
A
320
34.260
8.023
47.455
1.00
28.64
A


ATOM
2442
NZ
LYS
A
320
34.606
8.111
46.002
1.00
29.29
A


ATOM
2443
C
LYS
A
320
32.283
2.086
48.128
1.00
23.17
A


ATOM
2444
O
LYS
A
320
31.162
2.097
48.634
1.00
23.14
A


ATOM
2445
N
PRO
A
321
33.167
1.114
48.392
1.00
23.18
A


ATOM
2446
CD
PRO
A
321
34.535
0.975
47.858
1.00
23.17
A


ATOM
2447
CA
PRO
A
221
32.842
−0.001
49.291
1.00
23.00
A


ATOM
2448
CB
PRO
A
321
31.174
−0.738
49.416
1.00
23.25
A


ATOM
2449
CG
PRO
A
321
34.812
−0.495
48.077
1.00
23.67
A


ATOM
2450
C
PRO
A
321
32.280
0.405
50.655
1.00
22.40
A


ATOM
2451
O
PRO
A
321
31.373
−0.239
51.182
1.00
21.92
A


ATOM
2452
N
GLU
A
322
32.813
1.482
51.214
1.00
22.04
A


ATOM
2453
CA
GLU
A
322
32.391
1.954
52.528
1.00
21.71
A


ATOM
2454
CB
GLU
A
322
33.316
3.088
52.988
1.00
23.36
A


ATOM
2455
CG
GLU
A
322
34.795
2.845
52.720
1.00
26.98
A


ATOM
2456
CD
GLU
A
322
35.132
2.879
51.241
1.00
28.13
A


ATOM
2457
OE1
GLU
A
322
34.883
3.918
50.596
1.00
30.36
A


ATOM
2458
OE2
GLU
A
322
35.640
1.867
50.720
1.00
30.37
A


ATOM
2459
C
GLU
A
322
30.934
2.429
52.631
1.00
20.23
A


ATOM
2460
O
GLU
A
322
30.368
2.439
53.720
1.00
19.87
A


ATOM
2461
N
LYS
A
323
30.326
2.821
51.515
1.00
19.09
A


ATOM
2462
CA
LYS
A
323
28.946
3.314
51.555
1.00
18.24
A


ATOM
2463
CB
LYS
A
323
28.468
3.697
50.148
1.00
17.68
A


ATOM
2464
CG
LYS
A
323
29.359
4.719
49.423
1.00
17.88
A


ATOM
2465
CD
LYS
A
323
29.670
5.951
50.275
1.00
18.08
A


ATOM
2466
CE
LYS
A
323
28.407
6.688
50.708
1.00
17.75
A


ATOM
2467
NZ
LYS
A
323
28.711
7.892
51.538
1.00
18.08
A


ATOM
2468
C
LYS
A
323
27.949
2.330
52.186
1.00
18.18
A


ATOM
2469
O
LYS
A
323
27.091
2.727
52.980
1.00
17.44
A


ATOM
2470
N
MET
A
324
28.072
1.050
51.843
1.00
17.79
A


ATOM
2471
CA
MET
A
324
27.168
0.022
52.362
1.00
17.73
A


ATOM
2472
CB
MET
A
324
26.926
−1.049
51.290
1.00
17.86
A


ATOM
2473
CG
MET
A
324
26.067
−0.601
50.116
1.00
18.32
A


ATOM
2474
SD
MET
A
324
24.323
−0.405
50.580
1.00
19.61
A


ATOM
2475
CE
MET
A
324
23.587
0.034
48.988
1.00
18.17
A


ATOM
2476
C
MET
A
324
27.619
−0.658
53.657
1.00
17.26
A


ATOM
2477
O
MET
A
324
27.054
−1.685
54.044
1.00
17.39
A


ATOM
2478
N
ASN
A
325
28.620
−0.099
54.332
1.00
17.04
A


ATOM
2479
CA
ASN
A
325
29.105
−0.689
55.578
1.00
16.26
A


ATOM
2480
CB
ASN
A
325
30.138
0.227
56.249
1.00
16.89
A


ATOM
2481
CG
ASN
A
325
31.544
0.043
55.694
1.00
17.31
A


ATOM
2482
OD1
ASN
A
325
31.792
−0.825
54.856
1.00
17.48
A


ATOM
2483
ND2
ASN
A
325
32.475
0.865
56.170
1.00
16.86
A


ATOM
2484
C
ASN
A
325
27.996
−1.000
56.592
1.00
15.84
A


ATOM
2485
O
ASN
A
325
27.873
−2.134
57.061
1.00
15.57
A


ATOM
2486
N
ALA
A
326
27.194
0.006
56.931
1.00
14.81
A


ATOM
2487
CA
ALA
A
326
26.127
−0.162
57.918
1.00
14.14
A


ATOM
2488
CB
ALA
A
326
25.499
1.199
58.243
1.00
14.41
A


ATOM
2489
C
ALA
A
326
25.043
−1.152
57.501
1.00
14.35
A


ATOM
2490
O
ALA
A
326
24.589
−1.967
58.313
1.00
14.78
A


ATOM
2491
N
THR
A
327
24.635
−1.079
56.241
1.00
13.41
A


ATOM
2492
CA
THR
A
327
23.605
−1.962
55.713
1.00
13.87
A


ATOM
2493
CB
THR
A
327
23.242
−1.569
54.259
1.00
13.38
A


ATOM
2494
OG1
THR
A
327
22.655
−0.256
54.253
1.00
13.83
A


ATOM
2495
CG2
THR
A
327
22.253
−2.570
53.657
1.00
13.68
A


ATOM
2496
C
THR
A
327
24.072
−3.421
55.753
1.00
14.01
A


ATOM
2497
O
THR
A
327
23.371
−4.288
56.279
1.00
13.75
A


ATOM
2498
N
ARG
A
328
25.259
−3.682
55.211
1.00
14.33
A


ATOM
2499
CA
ARG
A
328
25.814
−5.040
55.182
1.00
14.77
A


ATOM
2500
CB
ARG
A
328
27.082
−5.080
54.316
1.00
15.22
A


ATOM
2501
CG
ARG
A
328
26.835
−4.886
52.812
1.00
16.37
A


ATOM
2502
CD
ARG
A
328
28.148
−4.913
52.021
1.00
18.14
A


ATOM
2503
NE
ARG
A
328
27.969
−4.631
50.597
1.00
19.53
A


ATOM
2504
CZ
ARG
A
328
27.457
−5.483
49.715
1.00
20.66
A


ATOM
2505
NH1
ARG
A
328
27.064
−6.689
50.102
1.00
22.08
A


ATOM
2506
NH2
ARG
A
328
27.345
−5.136
48.439
1.00
21.33
A


ATOM
2507
C
ARG
A
328
26.116
−5.620
56.573
1.00
15.06
A


ATOM
2508
O
ARG
A
328
26.114
−6.836
56.748
1.00
15.82
A


ATOM
2509
N
GLU
A
329
26.381
−4.762
57.555
1.00
14.77
A


ATOM
2510
CA
GLU
A
329
26.651
−5.229
58.918
1.00
14.81
A


ATOM
2511
CB
GLU
A
329
27.125
−4.067
59.799
1.00
15.53
A


ATOM
2512
CG
GLU
A
329
27.244
−4.379
61.293
1.00
17.33
A


ATOM
2513
CD
GLU
A
329
28.431
−5.268
61.645
1.00
18.89
A


ATOM
2514
OE1
GLU
A
329
29.282
−5.523
60.764
1.00
18.54
A


ATOM
2515
OE2
GLU
A
329
28.519
−5.702
62.818
1.00
20.32
A


ATOM
2516
C
GLU
A
329
25.378
−5.840
59.509
1.00
14.36
A


ATOM
2517
O
GLU
A
329
25.425
−6.885
60.163
1.00
13.91
A


ATOM
2518
N
VAL
A
330
24.243
−5.185
59.278
1.00
13.59
A


ATOM
2519
CA
VAL
A
330
22.965
−5.676
59.785
1.00
14.02
A


ATOM
2520
CD
VAL
A
330
21.856
−4.604
59.629
1.00
13.99
A


ATOM
2521
CG1
VAL
A
330
20.484
−5.196
59.968
1.00
13.58
A


ATOM
2522
CG2
VAL
A
330
22.157
−3.425
60.556
1.00
14.00
A


ATOM
2523
C
VAL
A
330
22.549
−6.968
59.077
1.00
14.02
A


ATOM
2524
O
VAL
A
330
22.062
−7.899
59.721
1.00
13.94
A


ATOM
2525
N
LEU
A
331
22.738
−7.029
57.759
1.00
13.64
A


ATOM
2526
CA
LEU
A
331
22.399
−8.237
57.005
1.00
13.71
A


ATOM
2527
CB
LEU
A
331
22.655
−8.037
55.502
1.00
14.19
A


ATOM
2528
CG
LEU
A
331
22.547
−9.303
54.637
1.00
13.98
A


ATOM
2529
CD1
LEU
A
331
21.135
−9.876
54.726
1.00
13.96
A


ATOM
2530
CD2
LEU
A
331
22.894
−8.988
53.189
1.00
14.69
A


ATOM
2531
C
LEU
A
331
23.262
−9.397
57.501
1.00
14.26
A


ATOM
2532
O
LEU
A
331
22.792
−10.527
57.647
1.00
13.37
A


ATOM
2533
N
SER
A
332
24.531
−9.099
57.760
1.00
15.11
A


ACOM
2534
CA
SER
A
332
25.485
−10.097
58.225
1.00
16.35
A


ATOM
2535
CB
SER
A
332
26.903
−9.509
58.174
1.00
17.12
A


ATOM
2536
OG
SER
A
332
27.870
−10.444
58.619
1.00
19.44
A


ATOM
2537
C
SER
A
332
25.180
−10.602
59.638
1.00
16.20
A


ATOM
2538
O
SER
A
332
25.254
−11.799
59.902
1.00
16.47
A


ATOM
2539
N
GLU
A
333
24.821
−9.689
60.536
1.00
15.96
A


ATOM
2540
CA
GLU
A
333
24.537
−10.040
61.929
1.00
15.99
A


ATOM
2541
CB
GLU
A
333
24.922
−8.872
62.848
1.00
17.32
A


ATOM
2542
CG
GLU
A
333
26.411
−8.541
62.897
1.00
20.64
A


ATOM
2543
CD
GLU
A
333
27.242
−9.659
63.496
1.00
22.34
A


ATOM
2544
OE1
GLU
A
333
26.931
−10.096
64.625
1.00
23.49
A


ATOM
2545
OE2
GLU
A
333
28.211
−10.096
62.843
1.00
23.53
A


ATOM
2546
C
GLU
A
333
23.105
−10.454
62.279
1.00
14.90
A


ATOM
2547
O
GLU
A
333
22.887
−11.062
63.328
1.00
14.01
A


ATOM
2548
N
TYR
A
334
22.135
−10.144
61.421
1.00
13.81
A


ATOM
2549
CA
TYR
A
334
20.735
−10.455
61.740
1.00
13.26
A


ATOM
2550
CB
TYR
A
334
20.031
−9.174
62.216
1.00
13.56
A


ATOM
2551
CG
TYR
A
334
20.683
−8.494
63.398
1.00
14.44
A


ATOM
2552
CD1
TYR
A
334
20.558
−9.018
64.686
1.00
15.41
A


ATOM
2553
CE1
TYR
A
334
21.191
−8.413
65.774
1.00
16.14
A


ATOM
2554
CD2
TYR
A
334
21.455
−7.342
63.225
1.00
14.72
A


ATOM
2555
CE2
TYR
A
334
22.088
−6.729
64.303
1.00
15.69
A


ATOM
2556
CZ
TYR
A
334
21.954
−7.270
65.572
1.00
16.75
A


ATOM
2557
OH
TYR
A
334
22.584
−6.668
66.639
1.00
17.76
A


ATOM
2558
C
TYR
A
334
19.878
−11.071
60.631
1.00
12.57
A


ATOM
2559
O
TYR
A
334
18.802
−11.600
60.907
1.00
12.41
A


ATOM
2560
N
GLY
A
335
20.333
−10.993
59.387
1.00
12.22
A


ATOM
2561
CA
GLY
A
335
19.537
−11.522
58.287
1.00
11.80
A


ATOM
2562
C
GLY
A
335
18.447
−10.524
57.912
1.00
11.96
A


ATOM
2563
O
GLY
A
335
18.430
−9.404
58.429
1.00
11.44
A


ATOM
2564
N
ASN
A
336
17.535
−10.928
57.028
1.00
11.66
A


ATOM
2565
CA
ASN
A
336
16.433
−10.071
56.577
1.00
11.70
A


ATOM
2566
CB
ASN
A
336
15.957
−10.540
55.189
1.00
11.42
A


ATOM
2567
CG
ASN
A
336
14.806
−9.710
54.638
1.00
12.51
A


ATOM
2568
OD1
ASN
A
336
14.090
−9.039
55.382
1.00
13.12
A


ATOM
2569
ND2
ASN
A
336
14.610
−9.770
53.318
1.00
12.55
A


ATOM
2570
C
ASN
A
336
15.272
−10.144
57.573
1.00
11.85
A


ATOM
2571
O
ASN
A
336
14.529
−11.132
57.589
1.00
11.61
A


ATOM
2572
N
MET
A
337
15.125
−9.103
58.396
1.00
11.75
A


ATOM
2573
CA
MET
A
337
14.066
−9.023
59.406
1.00
11.30
A


ATOM
2574
CB
MET
A
337
14.616
−8.402
60.702
1.00
11.74
A


ATOM
2575
CG
MET
A
337
15.776
−9.162
61.347
1.00
11.23
A


ATOM
2576
SD
MET
A
337
16.500
−8.267
62.775
1.00
12.05
A


ATOM
2577
CE
MET
A
337
17.454
−7.023
61.918
1.00
10.68
A


ATOM
2578
C
MET
A
337
12.872
−8.185
58.912
1.00
11.73
A


ATOM
2579
O
MET
A
337
12.185
−7.521
59.705
1.00
11.01
A


ATOM
2580
N
SER
A
338
12.636
−8.220
57.606
1.00
10.58
A


ATOM
2581
CA
SER
A
338
11.540
−7.480
56.987
1.00
11.13
A


ATOM
2582
CB
SER
A
338
10.194
−8.129
57.344
1.00
11.47
A


ATOM
2583
OG
SER
A
338
9.133
−7.611
56.541
1.00
11.75
A


ATOM
2584
C
SER
A
338
11.539
−5.995
57.365
1.00
10.94
A


ATOM
2585
O
SER
A
338
12.580
−5.341
57.318
1.00
10.10
A


ATOM
2586
N
SER
A
339
10.380
−5.466
57.753
1.00
10.98
A


ATOM
2587
CA
SER
A
339
10.266
−4.044
58.084
1.00
10.99
A


ATOM
2588
CB
SER
A
339
8.838
−3.709
58.543
1.00
11.08
A


ATOM
2589
OG
SER
A
339
8.561
−4.237
59.829
1.00
10.91
A


ATOM
2590
C
SER
A
339
11.259
−3.494
59.107
1.00
10.72
A


ATOM
2591
O
SER
A
339
11.591
−2.311
59.059
1.00
10.36
A


ATOM
2592
N
ALA
A
340
11.743
−4.338
60.015
1.00
10.25
A


ATOM
2593
CA
ALA
A
340
12.678
−3.877
61.048
1.00
10.47
A


ATOM
2594
CB
ALA
A
340
12.734
−4.900
62.192
1.00
10.31
A


ATOM
2595
C
ALA
A
340
14.102
−3.553
60.584
1.00
10.95
A


ATOM
2596
O
ALA
A
340
14.793
−2.763
61.230
1.00
10.69
A


ATOM
2597
N
CYS
A
341
14.542
−4.153
59.480
1.00
11.51
A


ATOM
2598
CA
CYS
A
341
15.907
−3.939
58.978
1.00
12.12
A


ATOM
2599
CB
CYS
A
341
16.080
−4.551
57.582
1.00
13.41
A


ATOM
2600
SG
CYS
A
341
16.004
−6.345
57.497
1.00
15.80
A


ATOM
2601
C
CYS
A
341
16.407
−2.501
58.911
1.00
11.76
A


ATOM
2602
O
CYS
A
341
17.434
−2.167
59.511
1.00
11.11
A


ATOM
2603
N
VAL
A
342
15.704
−1.653
58.165
1.00
11.06
A


ATOM
2604
CA
VAL
A
342
16.152
−0.274
58.010
1.00
11.17
A


ATOM
2605
CB
VAL
A
342
15.254
0.506
57.021
1.00
10.53
A


ATOM
2606
CG1
VAL
A
342
15.371
−0.118
55.637
1.00
10.75
A


ATOM
2607
CG2
VAL
A
342
13.812
0.501
57.493
1.00
10.96
A


ATOM
2608
C
VAL
A
342
16.266
0.487
59.321
1.00
10.94
A


ATOM
2609
O
VAL
A
342
17.048
1.436
59.423
1.00
11.24
A


ATOM
2610
N
LEU
A
343
15.501
0.073
60.328
1.00
10.28
A


ATOM
2611
CA
LEU
A
343
15.576
0.736
61.623
1.00
9.58
A


ATOM
2612
CB
LEU
A
343
14.298
0.479
62.435
1.00
9.47
A


ATOM
2613
CG
LEU
A
343
13.005
0.940
61.735
1.00
9.16
A


ATOM
2614
CD1
LEU
A
343
11.828
0.841
62.708
1.00
9.75
A


ATOM
2615
CD2
LEU
A
343
13.160
2.381
61.236
1.00
10.29
A


ATOM
2616
C
LEU
A
343
16.832
0.261
62.374
1.00
9.66
A


ATOM
2617
O
LEU
A
343
17.470
1.051
63.073
1.00
9.55
A


ATOM
2618
N
PHE
A
344
17.197
−1.014
62.223
1.00
10.11
A


ATOM
2619
CA
PHE
A
344
18.417
−1.525
62.858
1.00
10.35
A


ATOM
2620
CB
PHE
A
344
18.593
−3.040
62.626
1.00
10.60
A


ATOM
2621
CG
PHE
A
344
17.946
−3.924
63.674
1.00
11.60
A


ATOM
2622
CD1
PHE
A
344
16.560
−4.063
63.743
1.00
11.33
A


ATOM
2623
CD2
PHE
A
344
18.737
−4.673
64.551
1.00
12.06
A


ATOM
2624
CE1
PHE
A
344
15.970
−4.939
64.664
1.00
12.07
A


ATOM
2625
CE2
PHE
A
344
18.162
−5.551
65.477
1.00
12.12
A


ATOM
2626
CZ
PHE
A
344
16.773
−5.686
65.533
1.00
12.33
A


ATOM
2627
C
PHE
A
344
19.605
−0.804
62.204
1.00
10.33
A


ATOM
2628
O
PHE
A
344
20.588
−0.460
62.870
1.00
9.78
A


ATOM
2629
N
ILE
A
345
19.514
−0.574
60.895
1.00
9.91
A


ATOM
2630
CA
ILE
A
345
20.598
0.092
60.168
1.00
10.19
A


ATOM
2631
CB
ILE
A
345
20.360
0.029
58.632
1.00
9.96
A


ATOM
2632
CG2
ILE
A
345
21.463
0.791
57.893
1.00
9.91
A


ATOM
2633
CG1
ILE
A
345
20.345
−1.438
58.180
1.00
10.15
A


ATOM
2634
CD1
ILE
A
345
19.967
−1.653
56.722
1.00
9.55
A


ATOM
2635
C
ILE
A
345
20.798
1.539
60.624
1.00
10.60
A


ATOM
2636
O
ILE
A
345
21.938
2.006
60.728
1.00
11.29
A


ATOM
2637
N
LEU
A
346
19.706
2.254
60.889
1.00
10.89
A


ATOM
2638
CA
LEU
A
346
19.809
3.633
61.375
1.00
11.20
A


ATOM
2639
CB
LEU
A
346
18.414
4.251
61.580
1.00
10.69
A


ATOM
2640
CG
LEU
A
346
17.624
4.627
60.321
1.00
10.61
A


ATOM
2641
CD1
LEU
A
346
16.187
4.996
60.695
1.00
11.25
A


ATOM
2642
CD2
LEU
A
346
18.313
5.790
59.617
1.00
11.23
A


ATOM
2643
C
LEU
A
346
20.561
3.627
62.707
1.00
11.84
A


ATOM
2644
O
LEU
A
346
21.406
4.492
62.965
1.00
12.64
A


ATOM
2645
N
ASP
A
347
20.258
2.644
63.550
1.00
12.06
A


ATOM
2646
CA
ASP
A
347
20.908
2.537
64.857
1.00
13.39
A


ATOM
2647
CB
ASP
A
347
20.217
1.450
65.690
1.00
13.78
A


ATOM
2648
CG
ASP
A
347
20.591
1.508
67.163
1.00
15.67
A


ATOM
2649
OD1
ASP
A
347
20.710
2.629
67.706
1.00
14.75
A


ATOM
2650
OD2
ASP
A
347
20.746
0.432
67.783
1.00
15.69
A


ATOM
2651
C
ASP
A
347
22.408
2.245
64.710
1.00
13.67
A


ATOM
2652
O
ASP
A
347
23.239
2.873
65.367
1.00
13.64
A


ATOM
2653
N
GLU
A
348
22.751
1.301
63.838
1.00
14.56
A


ATOM
2654
CA
GLU
A
348
24.147
0.938
63.592
1.00
15.36
A


ATOM
2655
CB
GLU
A
348
24.215
−0.210
62.579
1.00
16.27
A


ATOM
2656
CG
GLU
A
348
25.617
−0.592
62.092
1.00
17.76
A


ATOM
2657
CD
GLU
A
348
26.541
−1.082
63.200
1.00
18.78
A


ATOM
2658
OE1
GLU
A
348
26.047
−1.562
64.242
1.00
19.58
A


ATOM
2659
OE2
GLU
A
348
27.773
−1.002
63.019
1.00
19.89
A


ATOM
2660
C
GLU
A
348
24.946
2.134
63.071
1.00
15.06
A


ATOM
2661
O
GLU
A
348
26.049
2.405
63.541
1.00
14.81
A


ATOM
2662
N
MET
A
349
24.388
2.853
62.104
1.00
14.78
A


ATOM
2663
CA
MET
A
343
25.079
4.008
61.540
1.00
15.19
A


ATOM
2664
CB
MET
A
349
24.265
4.625
60.401
1.00
15.22
A


ATOM
2665
CG
MET
A
349
24.931
5.857
59.811
1.00
17.23
A


ATOM
2666
SD
MET
A
349
24.032
6.538
58.421
1.00
18.52
A


ATOM
2667
CE
MET
A
349
24.320
5.238
57.186
1.00
16.39
A


ATOM
2668
C
MET
A
349
25.390
5.100
62.563
1.00
14.73
A


ATOM
2669
O
MET
A
349
26.503
5.624
62.599
1.00
14.30
A


ATOM
2670
N
ARG
A
350
24.409
5.453
63.384
1.00
14.34
A


ATOM
2671
CA
ARG
A
350
24.615
6.498
64.379
1.00
15.08
A


ATOM
2672
CB
ARG
A
350
23.272
6.950
64.962
1.00
14.45
A


ATOM
2673
CG
ARG
A
350
22.518
5.897
65.756
1.00
14.44
A


ATOM
2674
CD
ARG
A
350
22.510
6.236
67.247
1.00
14.54
A


ATOM
2675
NE
ARG
A
350
21.567
5.396
67.984
1.00
14.41
A


ATOM
2676
CZ
ARG
A
350
21.013
5.735
69.144
1.00
14.88
A


ATOM
2677
NH1
ARG
A
350
21.308
6.902
69.701
1.00
14.87
A


ATOM
2678
NH2
ARG
A
350
20.159
4.912
69.745
1.00
14.52
A


ATOM
2679
C
ARG
A
350
25.571
6.066
65.492
1.00
15.83
A


ATOM
2680
O
ARG
A
350
26.360
6.873
65.987
1.00
15.01
A


ATOM
2681
N
LYS
A
351
25.514
4.795
65.880
1.00
16.14
A


ATOM
2682
CA
LYS
A
351
26.411
4.305
68.921
1.00
17.27
A


ATOM
2683
CB
LYS
A
351
25.998
2.909
67.382
1.00
18.64
A


ATOM
2684
CG
LYS
A
351
24.844
2.916
68.386
1.00
20.60
A


ATOM
2685
CD
LYS
A
351
24.438
1.494
68.767
1.00
22.37
A


ATOM
2686
CE
LYS
A
351
23.636
1.480
70.061
1.00
23.69
A


ATOM
2687
NZ
LYS
A
351
22.393
2.293
69.986
1.00
24.80
A


ATOM
2688
C
LYS
A
351
27.860
4.286
66.430
1.00
17.14
A


ATOM
2689
O
LYS
A
351
28.771
4.696
67.152
1.00
16.83
A


ATOM
2690
N
LYS
A
352
28.073
3.817
65.203
1.00
16.98
A


ATOM
2691
CA
LYS
A
352
29.419
3.767
64.627
1.00
17.64
A


ATOM
2692
CB
LYS
A
352
29.416
2.966
63.323
1.00
18.76
A


ATOM
2693
CG
LYS
A
352
29.490
1.470
63.526
1.00
21.91
A


ATOM
2694
CD
LYS
A
352
30.857
1.068
64.077
1.00
23.41
A


ATOM
2695
CE
LYS
A
352
30.896
−0.405
64.432
1.00
24.84
A


ATOM
2696
NZ
LYS
A
352
29.886
−0.731
65.483
1.00
26.79
A


ATOM
2697
C
LYS
A
352
29.995
5.156
64.363
1.00
17.19
A


ATOM
2698
O
LYS
A
352
31.204
5.369
64.500
1.00
16.04
A


ATOM
2699
N
SER
A
353
29.138
6.094
63.970
1.00
16.74
A


ATOM
2700
CA
SER
A
353
29.583
7.460
63.710
1.00
17.39
A


ATOM
2701
CB
SER
A
353
28.435
8.297
63.138
1.00
17.32
A


ATOM
2702
OG
SER
A
353
28.067
7.843
61.848
1.00
16.97
A


ATOM
2703
C
SER
A
353
30.073
8.088
65.012
1.00
18.27
A


ATOM
2704
O
SER
A
353
31.043
8.850
65.025
1.00
18.81
A


ATOM
2705
N
THR
A
354
29.391
7.768
66.106
1.00
18.39
A


ATOM
2706
CA
THR
A
354
29.749
8.290
67.420
1.00
19.76
A


ATOM
2707
CB
THR
A
354
28.618
8.011
68.435
1.00
20.00
A


ATOM
2708
OG1
THR
A
354
27.443
8.729
68.043
1.00
20.37
A


ATOM
2709
CG2
THR
A
354
29.027
8.435
69.839
1.00
20.74
A


ATOM
2710
C
THR
A
354
31.036
7.618
67.899
1.00
20.00
A


ATOM
2711
O
THR
A
354
31.959
8.272
68.399
1.00
19.48
A


ATOM
2712
N
GLN
A
355
31.080
6.303
67.730
1.00
20.15
A


ATOM
2713
CA
GLN
A
355
32.222
5.493
68.128
1.00
21.65
A


ATOM
2714
CB
GLN
A
355
31.913
4.019
67.837
1.00
22.91
A


ATOM
2715
CG
GLN
A
355
33.095
3.066
67.958
1.00
25.78
A


ATOM
2716
CD
GLN
A
355
32.778
1.685
67.405
1.00
27.34
A


ATOM
2717
OE1
GLN
A
355
31.862
1.009
67.874
1.00
29.12
A


ATOM
2718
NE2
GLN
A
355
33.532
1.264
66.398
1.00
28.38
A


ATOM
2719
C
GLN
A
355
33.530
5.889
67.432
1.00
21.31
A


ATOM
2720
O
GLN
A
355
34.562
6.071
68.086
1.00
21.87
A


ATOM
2721
N
ASN
A
356
33.488
6.027
66.111
1.00
20.41
A


ATOM
2722
CA
ASN
A
356
34.692
6.352
65.356
1.00
20.53
A


ATOM
2723
CB
ASN
A
356
34.655
5.657
63.992
1.00
21.37
A


ATOM
2724
CG
ASN
A
356
34.710
4.143
64.116
1.00
22.05
A


ATOM
2725
OD1
ASN
A
356
35.340
3.608
65.029
1.00
22.39
A


ATOM
2726
ND2
ASN
A
356
34.060
3.447
63.193
1.00
23.15
A


ATOM
2727
C
ASN
A
356
35.027
7.829
65.182
1.00
19.88
A


ATOM
2728
O
ASN
A
356
35.927
8.179
64.413
1.00
19.58
A


ATOM
2729
N
GLY
A
357
34.301
8.687
65.894
1.00
19.15
A


ATOM
2730
CA
GLY
A
357
34.563
10.117
65.848
1.00
18.39
A


ATOM
2731
C
GLY
A
357
34.155
10.930
64.634
1.00
18.00
A


ATOM
2732
O
GLY
A
357
34.839
11.896
64.289
1.00
17.19
A


ATOM
2733
N
LEU
A
358
33.056
10.564
63.982
1.00
17.83
A


ATOM
2734
CA
LEU
A
358
32.599
11.325
62.819
1.00
18.37
A


ATOM
2735
CB
LEU
A
358
31.641
10.487
61.960
1.00
18.29
A


ATOM
2736
CG
LEU
A
358
32.261
9.431
61.033
1.00
18.70
A


ATOM
2737
CD1
LEU
A
358
33.183
10.113
60.032
1.00
18.64
A


ATOM
2738
CD2
LEU
A
358
33.028
8.392
61.841
1.00
18.14
A


ATOM
2739
C
LEU
A
358
31.905
12.589
63.329
1.00
18.28
A


ATOM
2740
O
LEU
A
358
31.430
12.621
64.465
1.00
19.60
A


ATOM
2741
N
LYS
A
359
31.847
13.625
62.497
1.00
18.13
A


ATOM
2742
CA
LYS
A
359
31.245
14.894
62.902
1.00
18.17
A


ATOM
2743
CB
LYS
A
359
31.862
16.033
62.085
1.00
19.78
A


ATOM
2744
CG
LYS
A
359
33.378
16.146
62.242
1.00
22.00
A


ATOM
2745
CD
LYS
A
359
33.773
16.502
63.672
1.00
24.21
A


ATOM
2746
CE
LYS
A
359
33.331
17.915
64.027
1.00
26.14
A


ATOM
2747
NZ
LYS
A
359
33.637
18.270
65.443
1.00
27.55
A


ATOM
2748
C
LYS
A
359
29.713
14.990
62.861
1.00
17.59
A


ATOM
2749
O
LYS
A
359
29.147
15.972
63.337
1.00
17.60
A


ATOM
2750
N
THR
A
360
29.046
13.992
62.286
1.00
16.40
A


ATOM
2751
CA
THR
A
360
27.577
13.975
62.247
1.00
15.45
A


ATOM
2752
CB
THR
A
360
26.992
14.499
60.911
1.00
15.82
A


ATOM
2753
OG1
THR
A
360
27.231
13.539
59.877
1.00
15.65
A


ATOM
2754
CG2
THR
A
360
27.613
15.840
60.524
1.00
16.52
A


ATOM
2755
C
THR
A
360
27.116
12.532
62.413
1.00
14.68
A


ATOM
2756
O
THR
A
360
27.897
11.598
62.215
1.00
14.27
A


ATOM
2757
N
THR
A
361
25.852
12.348
62.777
1.00
13.61
A


ATOM
2758
CA
THR
A
361
25.307
11.008
62.965
1.00
13.33
A


ATOM
2759
CB
THR
A
361
23.919
11.066
63.629
1.00
13.09
A


ATOM
2760
OG1
THR
A
361
23.093
11.988
62.915
1.00
12.47
A


ATOM
2761
CG2
THR
A
361
24.043
11.529
65.081
1.00
13.05
A


ATOM
2762
C
THR
A
361
25.194
10.256
61.645
1.00
13.18
A


ATOM
2763
O
THR
A
361
24.936
9.050
61.633
1.00
13.52
A


ATOM
2764
N
GLY
A
362
25.394
10.973
60.542
1.00
13.05
A


ATOM
2765
CA
GLY
A
362
25.325
10.368
59.222
1.00
13.54
A


ATOM
2766
C
GLY
A
362
26.693
10.220
58.572
1.00
13.80
A


ATOM
2767
O
GLY
A
362
26.921
10.676
57.447
1.00
13.72
A


ATOM
2768
N
GLU
A
363
27.606
9.578
59.292
1.00
14.30
A


ATOM
2769
CA
GLU
A
363
28.969
9.342
58.823
1.00
14.87
A


ATOM
2770
CB
GLU
A
363
28.951
8.326
57.672
1.00
15.38
A


ATOM
2771
CG
GLU
A
363
28.092
7.101
58.010
1.00
16.94
A


ATOM
2772
CD
GLU
A
363
28.216
5.954
57.023
1.00
17.95
A


ATOM
2773
OE1
GLU
A
363
28.357
6.202
55.808
1.00
18.60
A


ATOM
2774
OE2
GLU
A
363
28.144
4.789
57.472
1.00
19.19
A


ATOM
2775
C
GLU
A
363
29.682
10.634
58.414
1.00
15.17
A


ATOM
2776
O
GLU
A
363
30.481
10.655
57.475
1.00
14.88
A


ATOM
2777
N
GLY
A
364
29.388
11.711
59.136
1.00
15.36
A


ATOM
2778
CA
GLY
A
364
30.023
12.986
58.851
1.00
16.19
A


ATOM
2779
C
GLY
A
364
29.429
13.764
57.693
1.00
16.44
A


ATOM
2780
O
GLY
A
364
29.856
14.884
57.418
1.00
16.69
A


ATOM
2781
N
LEU
A
365
28.445
13.184
57.012
1.00
16.46
A


ATOM
2782
CA
LEU
A
365
27.813
13.853
55.880
1.00
16.91
A


ATOM
2783
CB
LEU
A
365
27.494
12.831
54.786
1.00
16.94
A


ATOM
2784
CG
LEU
A
365
28.696
11.997
54.320
1.00
17.07
A


ATOM
2785
CD1
LEU
A
365
28.228
10.876
53.405
1.00
17.97
A


ATOM
2786
CD2
LEU
A
365
29.703
12.889
53.610
1.00
16.75
A


ATOM
2787
C
LEU
A
365
26.544
14.587
56.323
1.00
16.99
A


ATOM
2788
O
GLU
A
366
26.039
14.354
57.421
1.00
17.16
A


ATOM
2789
N
GLU
A
366
26.034
15.469
55.467
1.00
16.87
A


ATOM
2790
CA
GLU
A
366
24.838
16.252
55.787
1.00
17.25
A


ATOM
2791
CB
GLU
A
366
24.941
17.644
55.144
1.00
19.11
A


ATOM
2792
CG
GLU
A
366
23.629
18.432
55.109
1.00
21.19
A


ATOM
2793
CD
GLU
A
366
23.828
19.896
54.758
1.00
22.96
A


ATOM
2794
OE1
GLU
A
366
24.687
20.198
53.905
1.00
23.65
A


ATOM
2795
OE2
GLU
A
366
23.111
20.748
55.328
1.00
24.80
A


ATOM
2796
C
GLU
A
366
23.499
15.611
55.410
1.00
16.91
A


ATOM
2797
O
GLU
A
366
22.589
15.540
56.244
1.00
16.56
A


ATOM
2798
N
TRP
A
367
23.374
15.153
54.168
1.00
15.76
A


ATOM
2799
CA
TRP
A
367
22.127
14.535
53.703
1.00
15.43
A


ATOM
2800
CB
TRP
A
367
21.699
15.136
52.358
1.00
15.92
A


ATOM
2801
CG
TRP
A
367
21.584
16.640
52.362
1.00
17.29
A


ATOM
2802
CD2
TRP
A
367
20.521
17.420
52.924
1.00
17.28
A


ATOM
2803
CE2
TRP
A
367
20.843
18.781
52.714
1.00
17.73
A


ATOM
2804
CE3
TRP
A
367
19.327
17.101
53.587
1.00
17.91
A


ATOM
2805
CD1
TRP
A
367
22.483
17.535
51.848
1.00
17.11
A


ATOM
2806
NE1
TRP
A
367
22.043
18.823
52.054
1.00
17.26
A


ATOM
2807
CZ2
TRP
A
367
20.014
19.823
53.142
1.00
18.10
A


ATOM
2808
CZ3
TRP
A
367
18.500
18.139
54.014
1.00
17.80
A


ATOM
2809
CH2
TRP
A
367
18.849
19.483
53.789
1.00
18.48
A


ATOM
2810
C
TRP
A
367
22.243
13.021
53.551
1.00
14.85
A


ATOM
2811
O
TRP
A
367
23.335
12.493
53.340
1.00
14.03
A


ATOM
2812
N
GLY
A
368
21.105
12.333
53.643
1.00
13.90
A


ATOM
2813
CA
GLY
A
368
21.093
10.883
53.510
1.00
13.64
A


ATOM
2814
C
GLY
A
368
19.786
10.357
52.939
1.00
12.46
A


ATOM
2815
O
GLY
A
368
18.826
11.110
52.773
1.00
13.28
A


ATOM
2816
N
VAL
A
369
19.739
9.064
52.633
1.00
12.00
A


ATOM
2817
CA
VAL
A
369
18.530
8.470
52.077
1.00
11.30
A


ATOM
2818
CB
VAL
A
369
18.634
8.356
50.533
1.00
11.23
A


ATOM
2819
CG1
VAL
A
369
19.762
7.405
50.155
1.00
10.95
A


ATOM
2820
CG2
VAL
A
369
17.316
7.871
49.952
1.00
11.34
A


ATOM
2821
C
VAL
A
369
18.265
7.083
52.656
1.00
11.73
A


ATOM
2822
O
VAL
A
369
19.198
6.334
52.936
1.00
11.94
A


ATOM
2823
N
VAL
A
369
16.989
6.759
52.848
1.00
11.77
A


ATOM
2824
CA
LEU
A
370
16.580
5.456
53.371
1.00
11.76
A


ATOM
2825
CB
LEU
A
370
15.911
5.606
54.749
1.00
11.28
A


ATOM
2826
CG
LEU
A
370
15.397
4.333
55.445
1.00
11.66
A


ATOM
2827
CD1
LEU
A
370
15.368
4.547
56.960
1.00
11.65
A


ATOM
2828
CD2
LEU
A
370
14.015
3.962
54.918
1.00
12.29
A


ATOM
2829
C
LEU
A
370
15.595
4.857
52.376
1.00
11.86
A


ATOM
2830
O
LEU
A
370
14.646
5.527
51.971
1.00
11.90
A


ATOM
2831
N
PHE
A
371
15.828
3.604
51.984
1.00
11.79
A


ATOM
2832
CA
PHE
A
371
14.968
2.912
51.027
1.00
11.80
A


ATOM
2833
CB
PHE
A
371
15.755
2.528
49.761
1.00
12.26
A


ATOM
2834
CG
PHE
A
371
16.049
3.680
48.835
1.00
13.18
A


ATOM
2835
CD1
PHE
A
371
15.017
4.364
48.199
1.00
13.53
A


ATOM
2836
CD2
PHE
A
371
17.364
4.053
48.569
1.00
13.39
A


ATOM
2837
CE1
PHE
A
371
15.291
5.401
47.309
1.00
14.13
A


ATOM
2838
CE2
PHE
A
371
17.650
5.090
47.680
1.00
14.61
A


ATOM
2839
CZ
PHE
A
371
16.612
5.765
47.049
1.00
14.39
A


ATOM
2840
C
PHE
A
371
14.350
1.633
51.580
1.00
11.83
A


ATOM
2841
O
PHE
A
371
15.024
0.837
52.242
1.00
11.89
A


ATOM
2842
N
GLY
A
372
13.069
1.442
51.278
1.00
11.66
A


ATOM
2843
CA
GLY
A
372
12.357
0.238
51.677
1.00
11.23
A


ATOM
2844
C
GLY
A
372
11.875
−0.413
50.386
1.00
12.03
A


ATOM
2845
O
GLY
A
372
11.381
0.290
49.504
1.00
11.11
A


ATOM
2846
N
PHE
A
373
12.034
−1.732
50.254
1.00
12.31
A


ATOM
2847
CA
PHE
A
373
11.604
−2.446
49.043
1.00
12.91
A


ATOM
2848
CB
PHE
A
373
12.815
−3.026
48.281
1.00
13.68
A


ATOM
2849
CG
PHE
A
373
13.966
−2.063
48.107
1.00
14.91
A


ATOM
2850
CD1
PHE
A
373
13.784
−0.832
47.485
1.00
15.93
A


ATOM
2851
CD2
PHE
A
373
15.245
−2.406
48.547
1.00
15.06
A


ATOM
2852
CE1
PHE
A
373
14.859
0.046
47.303
1.00
16.22
A


ATOM
2853
CE2
PHE
A
373
16.327
−1.538
48.372
1.00
15.66
A


ATOM
2354
CZ
PHE
A
373
16.133
−0.309
47.749
1.00
15.82
A


ATOM
2855
C
PHE
A
373
10.698
−3.609
43.450
1.00
12.82
A


ATOM
2856
O
PHE
A
373
10.962
−4.269
50.455
1.00
11.69
A


ATOM
2857
N
GLY
A
374
9.650
−3.879
48.672
1.00
13.46
A


ATOM
2858
CA
GLY
A
374
8.756
−4.979
49.019
1.00
14.44
A


ATOM
2859
C
GLY
A
374
7.629
−5.288
48.041
1.00
15.41
A


ATOM
2860
O
GLY
A
374
7.630
−4.787
46.916
1.00
15.04
A


ATOM
2861
N
PRO
A
375
6.639
−6.108
48.457
1.00
16.00
A


ATOM
2862
CD
PRO
A
375
6.560
−6.647
48.828
1.00
16.19
A


ATOM
2863
CA
PRO
A
375
5.467
−6.538
47.680
1.00
16.73
A


ATOM
2864
CB
PRO
A
375
4.529
−7.081
48.751
1.00
16.44
A


ATOM
2865
CG
PRO
A
375
5.475
−7.711
49.703
1.00
16.06
A


ATOM
2866
C
PRO
A
375
4.799
−5.474
46.820
1.00
18.46
A


ATOM
2867
O
PRO
A
375
4.691
−4.298
47.206
1.00
17.70
A


ATOM
2868
N
GLY
A
376
4.319
−5.915
45.660
1.00
20.24
A


ATOM
2869
CA
GLY
A
376
3.682
−5.010
44.731
1.00
21.94
A


ATOM
2870
C
GLY
A
376
4.800
−4.070
44.412
1.00
23.04
A


ATOM
2871
O
GLY
A
376
4.606
−2.851
44.335
1.00
24.98
A


ATOM
2872
N
LEU
A
377
5.977
−4.666
44.214
1.00
22.83
A


ATOM
2873
CA
LEU
A
377
7.203
−3.935
43.963
1.00
20.77
A


ATOM
2874
CB
LEU
A
377
7.742
−4.194
42.562
1.00
22.54
A


ATOM
2875
CG
LEU
A
377
8.891
−5.198
42.724
1.00
23.55
A


ATOM
2876
CD1
LEU
A
377
9.542
−5.485
41.399
1.00
24.83
A


ATOM
2877
CD2
LEU
A
377
9.919
−4.634
43.709
1.00
23.91
A


ATOM
2878
C
LEU
A
377
7.042
−2.465
44.240
1.00
19.02
A


ATOM
2879
O
LEU
A
377
6.897
−1.629
43.344
1.00
17.12
A


ATOM
2880
N
THR
A
378
7.057
−2.194
45.537
1.00
16.80
A


ATOM
2881
CA
THR
A
378
6.910
−0.873
46.096
1.00
14.86
A


ATOM
2882
CB
THR
A
378
5.954
−0.918
47.319
1.00
14.08
A


ATOM
2883
OG1
THR
A
378
4.660
−1.385
46.905
1.00
15.17
A


ATOM
2884
CG2
THR
A
378
5.825
0.455
47.954
1.00
13.38
A


ATOM
2885
C
THR
A
378
8.279
−0.393
46.565
1.00
14.33
A


ATOM
2886
O
THR
A
378
9.075
−1.172
47.104
1.00
13.55
A


ATOM
2887
N
ILE
A
379
8.553
0.885
46.339
1:00
13.27
A


ATOM
2888
CA
ILE
A
379
9.803
1.500
46.772
1.00
12.71
A


ATOM
2889
CB
ILE
A
379
10.649
2.010
45.570
1.00
13.23
A


ATOM
2890
CG2
ILE
A
379
11.892
2.740
46.078
1.00
13.06
A


ATOM
2891
CG1
ILE
A
379
11.066
0.837
44.678
1.00
14.08
A


ATOM
2892
CD1
ILE
A
379
11.854
1.247
43.439
1.00
15.36
A


ATOM
2893
C
ILE
A
379
9.425
2.703
47.633
1.00
12.32
A


ATOM
2894
O
ILE
A
379
8.763
3.615
47.151
1.00
12.02
A


ATOM
2895
N
GLU
A
380
9.804
2.682
48.911
1.00
11.67
A


ATOM
2896
CA
GLU
A
380
9.532
3.803
49.808
1.00
11.50
A


ATOM
2897
CB
GLU
A
380
9.123
3.317
51.212
1.00
11.02
A


ATOM
2898
CG
GLU
A
380
7.764
2.601
51.299
1.00
11.78
A


ATOM
2899
CD
GLU
A
380
6.607
3.522
51.695
1.00
11.77
A


ATOM
2900
OE1
GLU
A
380
6.819
4.747
51.805
1.00
11.99
A


ATOM
2901
OE2
GLU
A
380
5.479
3.019
51.897
1.00
11.77
A


ATOM
2902
C
GLU
A
380
10.848
4.576
49.907
1.00
11.95
A


ATOM
2903
O
GLU
A
380
11.912
3.971
50.076
1.00
11.95
A


ATOM
2904
N
THR
A
381
10.773
5.900
49.783
1.00
12.03
A


ATOM
2905
CA
THR
A
381
11.951
6.763
49.867
1.00
12.38
A


ATOM
2906
CB
THR
A
381
12.186
7.570
48.552
1.00
13.41
A


ATOM
2907
OG1
THR
A
381
12.202
6.690
47.422
1.00
14.31
A


ATOM
2908
CG2
THR
A
381
13.522
8.311
48.613
1.00
13.86
A


ATOM
2909
C
THR
A
381
11.777
7.791
50.987
1.00
12.43
A


ATOM
2910
O
THR
A
381
10.747
8.466
51.062
1.00
12.02
A


ATOM
2911
N
VAL
A
382
12.778
7.900
51.860
1.00
12.62
A


ATOM
2912
CA
VAL
A
382
12.754
8.882
52.942
1.00
13.01
A


ATOM
2913
CB
VAL
A
382
12.626
8.229
54.346
1.00
12.57
A


ATOM
2914
CG1
VAL
A
382
12.612
9.321
55.414
1.00
12.79
A


ATOM
2915
CG2
VAL
A
382
11.362
7.380
54.433
1.00
12.77
A


ATOM
2916
C
VAL
A
382
14.062
9.678
52.933
1.00
13.29
A


ATOM
2917
O
VAL
A
382
15.140
9.109
53.128
1.00
13.54
A


ATOM
2918
N
VAL
A
383
13.977
10.984
52.692
1.00
13.17
A


ATOM
2919
CA
VAL
A
383
15.178
11.819
52.698
1.00
13.33
A


ATOM
2920
CB
VAL
A
383
15.024
13.063
51.793
1.00
13.72
A


ATOM
2921
CG1
VAL
A
383
16.291
13.928
51.870
1.00
13.77
A


ATOM
2922
CG2
VAL
A
383
14.782
12.628
50.356
1.00
14.43
A


ATOM
2923
C
VAL
A
383
15.438
12.264
54.136
1.00
12.88
A


ATOM
2924
O
VAL
A
383
14.522
12.687
54.845
1.00
12.31
A


ATOM
2925
N
LEU
A
384
16.694
12.168
54.559
1.00
13.47
A


ATOM
2926
CA
LEU
A
384
17.083
12.520
55.922
1.00
13.63
A


ATOM
2927
CB
LEU
A
384
17.542
11.257
56.662
1.00
13.93
A


ATOM
2928
CG
LEU
A
384
16.574
10.078
56.767
1.00
12.86
A


ATOM
2929
CD1
LEU
A
384
17.339
8.831
57.206
1.00
12.88
A


ATOM
2930
CD2
LEU
A
384
15.465
10.406
57.752
1.00
12.99
A


ATOM
2931
C
LEU
A
384
18.214
13.543
55.988
1.00
14.36
A


ATOM
2932
O
LEU
A
384
18.951
13.734
55.022
1.00
14.08
A


ATOM
2933
N
ARG
A
385
18.330
14.199
57.140
1.00
14.44
A


ATOM
2934
CA
ARG
A
385
19.402
15.163
57.400
1.00
15.65
A


ATOM
2935
CB
ARG
A
385
18.858
16.594
57.540
1.00
16.91
A


ATOM
2936
CG
ARG
A
385
19.954
17.674
57.630
1.00
19.02
A


ATOM
2937
CD
ARG
A
385
19.381
19.100
57.574
1.00
20.86
A


ATOM
2938
NE
ARG
A
385
20.430
20.114
57.422
1.00
23.18
A


ATOM
2939
CZ
ARG
A
385
21.158
20.611
58.419
1.00
24.39
A


ATOM
2940
NH1
ARG
A
385
20.960
20.202
59.663
1.00
25.40
A


ATOM
2941
NH2
ARG
A
385
22.096
21.518
58.171
1.00
25.36
A


ATOM
2942
C
ARG
A
385
20.001
14.701
58.731
1.00
15.04
A


ATOM
2943
O
ARG
A
385
19.268
14.342
59.653
1.00
14.72
A


ATOM
2944
N
SER
A
386
21.326
14.683
58.823
1.00
14.39
A


ATOM
2945
CA
SER
A
386
21.992
14.242
60.043
1.00
14.75
A


ATOM
2946
CB
SER
A
386
23.422
13.803
59.732
1.00
14.25
A


ATOM
2947
OG
SER
A
386
24.170
14.898
59.235
1.00
14.91
A


ATOM
2948
C
SER
A
386
22.030
15.347
61.093
1.00
14.95
A


ATOM
2949
O
SER
A
386
21.565
16.465
60.855
1.00
14.63
A


ATOM
2950
N
VAL
A
387
22.592
15.014
62.252
1.00
15.31
A


ATOM
2951
CA
VAL
A
387
22.734
15.943
63.369
1.00
16.50
A


ATOM
2952
CB
VAL
A
387
21.947
15.452
64.606
1.00
16.07
A


ATOM
2953
CG1
VAL
A
387
22.214
16.364
65.796
1.00
15.48
A


ATOM
2954
CG2
VAL
A
387
20.457
15.408
64.287
1.00
15.50
A


ATOM
2955
C
VAL
A
387
24.218
16.025
63.735
1.00
18.05
A


ATOM
2956
O
VAL
A
387
24.912
15.006
63.750
1.00
17.63
A


ATOM
2957
N
ALA
A
388
24.693
17.233
64.030
1.00
19.63
A


ATOM
2958
CA
ALA
A
388
26.095
17.455
64.389
1.00
22.13
A


ATOM
2959
CB
ALA
A
388
26.325
18.931
64.711
1.00
22.23
A


ATOM
2960
C
ALA
A
388
26.548
16.588
65.560
1.00
23.82
A


ATOM
2961
O
ALA
A
388
25.890
16.540
66.601
1.00
24.03
A


ATOM
2962
N
ILE
A
389
27.689
15.926
65.366
1.00
25.95
A


ATOM
2963
CA
ILE
A
389
28.306
15.023
66.338
1.00
27.95
A


ATOM
2964
CB
ILE
A
389
28.605
15.734
67.679
1.00
28.69
A


ATOM
2965
CG2
ILE
A
389
28.958
14.707
68.752
1.00
29.02
A


ATOM
2966
CG1
ILE
A
389
29.788
16.693
67.521
1.00
28.93
A


ATOM
2967
CD1
ILE
A
389
29.524
17.871
66.590
1.00
29.88
A


ATOM
2968
C
ILE
A
389
27.470
13.775
66.607
1.00
28.74
A


ATOM
2969
OT1
ILE
A
389
27.939
12.668
66.256
1.00
28.79
A


ATOM
2970
OT2
ILE
A
389
26.354
13.915
67.157
1.00
29.65
A









Table 9. PDB Accession No. 1EE0. The content of Table 9 is hereby incorporated by reference under 37 C.F.R. §1.52(e)(1)(iii) to file “1EE0.txt” of CD-R disk “S2370-3”, created Mar. 8, 2007, with size XXX,XXX bytes.
Table 10. PDB Accession No, 1BI5. The content of Table 10 is hereby incorporated by reference under 37 C.F.R. §1.52(e)(1)(iii) to file “1BI5.txt” of CD-R disk “ S2370-3”, created Mar. 8, 2007, with size XXX,XXX bytes.
Table 11. PDB Accession No. 1D6F. The content of Table 11 is hereby incorporated by reference under 37 C.F.R. §1.52(e)(1)(iii) to file “1D6F.txt” of CD-R disk “ S2370-3”, created Mar. 8, 2007, with size XXX,XXX bytes.
Table 12. PDB Accession No. 1D6I. The content of Table 12 is hereby incorporated by reference under 37 C.F.R. §1.52(e)(1)(iii) to file “1D6I.txt” of CD-R disk “ S2370-3”, created Mar. 8, 2007, with size XXX,XXX bytes.
Table 13. PDB Accession No. 1D6H. The content of Table 13 is hereby incorporated by reference under 37 C.F.R. §1.52(e)(1)(iii) to file “1D6H.txt” of CD-R disk “ S2370-3”, created Mar. 8, 2007, with size XXX,XXX bytes.
Table 14. PDB Accession No. 1BQ6. The content of Table 14 is hereby incorporated by reference under 37 C.F.R. §1.52(e)(1)(iii) to file “1BQ6.txt” of CD-R disk “ S2370-3”, created Mar. 8, 2007, with size XXX,XXX bytes.
Table 15. PDB Accession No. 1CML. The content of Table 15 is hereby incorporated by reference under 37 C.F.R. §1.52(e)(1)(iii) to file “1CML.txt” of CD-R disk “S2370-3”, created Mar. 8, 2007, with size XXX,XXX bytes.
Table 16. PDB Accession No. 1CHW. The content of Table 16 is hereby incorporated by reference under 37 C.F.R. §1.52(e)(1)(iii) to file “1CHW.txt” of CD-R disk “ S2370-3”, created Mar. 8, 2007, with size XXX,XXX bytes.
Table 17. PDB Accession No. 1CGK. The content of Table 17 is hereby incorporated by reference under 37 C.F.R. §1.52(e)(1)(iii) to file “1CGK.txt” of CD-R disk “ S2370-3”, created Mar. 8, 2007, with size XXX,XXX bytes.
Table 18. PDB Accession No. 1CGZ. The content of Table 18 is hereby incorporated by reference under 37 C.F.R. §1.52(e)(1)(iii) to file “1CGZ.txt” of CD-R disk “ S2370-3”, created Mar. 8, 2007, with size XXX,XXX bytes.

## Claims

1. An isolated polyketide synthase comprising an amino acid sequence having at least 95% sequence homology with respect to the chalcone synthase of SEQ ID NO:1, wherein one or more amino acid residues are modified at one or more positions corresponding to residues selected from the group consisting of positions 96, 98, 99, 100, 131, 133, 134, 135, 137, 157, 158, 159, 160, 165, 255, 257, 258, 266, 268, 269 and 270 of SEQ ID NO:1.

2. The isolated polyketide synthase of claim 1, wherein the amino acid sequence thereof has the same sequence as set forth in SEQ ID NO:1.

3. The isolated polyketide synthase of claim 1, wherein said polyketide synthase is further modified at the position corresponding to residue 273 of SEQ ID NO: 1.

4. The isolated polyketide synthase of claim 2, wherein said polyketide synthase is further modified at the position corresponding to residue 273 of SEQ ID NO: 1.

5. A method for producing anthocyanins, said method comprising contacting p-coumaroyl Co-enzyme-A and/or malonyl Co-enzyme-A with a polyketide synthase of claim 1.

6. A method for producing anthocyanins, said method comprising contacting p-coumaroyl Co-enzyme-A and/or malonyl Co-enzyme-A with a polyketide synthase of claim 2.

7. A method for producing anthocyanins, said method comprising contacting p-coumaroyl Co-enzyme-A and/or malonyl Co-enzyme-A with a polyketide synthase of claim 3.

8. A method for producing anthocyanins, said method comprising contacting p-coumaroyl Co-enzyme-A and/or malonyl Co-enzyme-A with a polyketide synthase of claim 4.