ANTIMICROBIAL TARGET Field of the Invention The present invention relates to a crystal of CDP-ME kinase complexed with its substrate CDP-ME and AMP-PNP and obtaining the crystal data relating to this and uses of the crystal data information for example to identify inhibitors of CDP-ME kinase.
Background to the Invention The ATP-dependent 4-diphosphocytidyl-2C-methyl-D- erythritol kinase (EC 2.7.1.148, CDP-ME kinase) participates in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) . These isomeric compounds are the universal five-carbon precursors of isoprenoids, a diverse and important family of natural products which includes sterols, dolichols, triterpenes and ubiquinones, and also components of macromolecules such as the prenyl groups of prenylated proteins and isopentenylated tRNAs (1-3) . Isoprenoids contribute to many biological functions including electron transport in respiration and photosynthesis, hormonebased signaling, apoptosis, meiosis, protein cleavage and degradation (4) . In addition, they provide important structural components of cell membranes (1) . Two biosynthetic routes to IPP and DMAPP have evolved. In eukaryotes, archaebacteria and a few eubacteria, the precursor biosynthesis is through the mevalonate pathway (3-7) . This begins with the conversion of three molecules of acetyl-CoA to 3-hydroxy-3-
methylglutaryl-CoA followed by reduction, phosphorylation and decarboxylation to generate IPP, some of which is isomerized to DMAPP. The last three steps in this pathway are ATP-dependent and catalyzed by the structurally related mevalonate kinase (MVK) , phosphomevalonate kinase (PMVK) , and mevalonate 5- diphosphate decarboxylase (MDD) . In chloroplasts, algae, cyanobacteria, most eubacteria and the apicomplexa, IPP and DMAPP synthesis is accomplished by seven enzymes in a pathway named after one of the intermediates, the l-deoxy-D-xylulose-5- phosphate (DOXP) pathway (5-8) . The first stage in the non-mevalonate route is the condensation of pyruvate and D-glyceraldehyde 3-phosphate to produce DOXP (9, 10). The second and third stages convert DOXP to MEP (11, 12) and transfer the erythritol derivative onto a nucleotide resulting in 4-diphosphocytidyl-2C-methyl-Derythritol (CDP-ME, 13-15) . Stage four, the only ATP-dependent step in the pathway, is catalysed by CDP-ME kinase (16, 17) , the subject of the present study. Here, CDP-ME kinase catalyzes the transfer of the γ-phosphoryl moiety of ATP to CDP-ME forming 4-diphosphocytidyl-2C-methyl-D- erythritol-2 -phosphate (CDP-ME2P) and ADP (Fig. 1) . Next, CDP-ME2P is converted to 2C-methyl-D-erythritol-2 , 4-cyclodiphosphate and CMP (18, 19) . The cyclodiphosphate then, in two enzyme-catalyzed stages, undergoes reduction and elimination to l-hydroxy-2- methyl-2- {E) -butenyl- -diphosphate and on to IPP and DMAPP (20-23) .
The species that utilize the DOXP pathway include the causal agents for diverse and serious human diseases including leprosy, malaria, bacterial meningitis, various gastrointestinal and sexually transmitted infections, trachoma, tuberculosis and certain types of pneumonia (5) . The enzymes of the DOXP pathway have no orthologs in humans and have attracted interest as potential targets for structure-based antimicrobial drug development. DOXP reductoisomerase, the enzyme which catalyses the second reaction in the pathway, is inhibited by the antibiotic fosmidomycin (24, 25); a compound which has performed well in recent clinical trials against malaria (26) . Such chemical validation of the reductoisomerase is complemented by genetic studies, which have proven that the enzymes responsible for stages three to five of the pathway are essential in eubacteria (27-31) . The crystallographic studies necessary to support structure-based drug discovery have produced models for DOXP reductoisomerase (32-34) , MEP cytidylyltransferase (15, 35) and 2C-methyl-D-erythritol- 2, 4-ayclodiphosphate (MECP) synthase (36-39). On the basis of sequence comparisons, CDP-ME kinase has been recognized as a member of the GHMP kinase superfamily (40) , so called after the four founding members namely galacto, homoserine, mevalonate and phosphomevalonate kinases (41) . The GHMP family now also includes MDD (42) , and archaeal shikimate kinase (43) . Crystal structures are available for several GHMP kinases (40, 42, 44-47) although only homoserine kinase (HSK, 38)
has provided experimental details for a ternary complex. In other cases modeling has been used to support mechanistic studies (45, 46) . A recent publication (Wada et al, JBC Papers in Press, 2003 Manuscript M304339200) discloses the crystal structure of 4- (cytidine 5 ' -diphospho) -2C-methyl-D- erythritol kinase, but does so in the absence of its substrate and co-factor. Thus, the authors merely hypothesis how the substrate and co-factor may bind to the CDP-ME kinase molecule.
Summary of the Invention The present invention is at least based on (i) production of CDP-ME kinase crystals incorporating its substrate and non-hydrolysable ATP analogue of suitable quality for performing X-ray diffraction analyses, (ii) collected X-ray diffraction data from the crystals, (iii) determination of the three-dimensional structure of CDP- ME kinase, and (iv) identification of the binding sites on the enzyme for the substrate and ATP analogue which are likely to be involved in the enzymatic reaction. The inventors have succeeded in the expression, purification, crystallisation and structure determination of CDP-ME kinase bound to its substrate and an ATP analogue . The crystal has been found to occur as a dimmer of the enzyme . In general aspects, the present invention is concerned with identifying or obtaining agent compounds for modulating CDP-ME kinase activity, and in preferred
embodiments identifying or obtaining actual agent compounds which are inhibitors or activators. Where methods of identifying or modelling inhibitors are described hereinafter, the skilled person will appreciate that the processes may be applied analogously to other modulators such as activators. Crystal structure information presented herein is useful in designing potential modulators and modelling them or their potential interaction with CDP-ME kinase binding cavities, for example, the CDP-ME kinase substrate binding cavity, ATP binding site, or other region or regions of interest (e.g. dimmer interface) . Potential modulators may be brought into contact with CDP-ME kinase to test for ability to interact with the CDP-ME kinase active site. Actual modulators may be identified from among potential modulators synthesized following design and model work performed in silico. A modulator identified using the present invention may be formulated into a composition, for instance a composition comprising a pharmaceutically acceptable excipient, and may be used in the manufacture of a medicament for use in a method of treatment . These and other aspects and embodiments of the present invention are discussed below. The present invention provides a crystal of CDP-ME kinase in combination with its substrate, CDP-ME and the ATP analogue, AMP-PNP having a space group P2., and unit cell dimensions of a = 61.0 A, b = 76.3 A, c = 68.6 A and
B = 107.8 degrees and more generally these figures ± 0.5, preferably ± 0.2. The asymmetric unit consists of two
subunits A and B of approx mass 62 KDa, which assemble with C2 symmetry to form an extended homodimer of approx dimensions 90 x 50 x 33 A ± 0.5 A, preferably ± 0.2 A. Alternatively, or additionally, the crystal may have the three dimensional atomic coordinates of Table 1. A further aspect of the invention includes within its scope a crystal of CDP-ME kinase defined by structural data having a resolution of about 2 A. The crystal comprises the relevant enzyme molecules complexed with either a substrate or substrate analogue, or a nucleotide or nucleotide analogue, or both. The substrate or substrate analogue may be CDP-ME. The nucleotide or analogue thereof will typically be ATP, or preferably a non-hydrolysable analogue thereof, such as AMP-PNP or ATP-gammaS. The coordinates of Table 1 provide a measure of atomic location in Angstroms. The coordinates are a relative set of positions that define a shape in three dimensions, so the skilled person would understand that an entirely different set of coordinates having a different origin and/or axes could define a similar or identical shape. Furthermore, the skilled person would understand that varying the relative atomic positions of the atoms of the structure so that the root mean square deviation of the residue backbone atoms (i.e. the nitrogen-carbon-carbon backbone atoms of the protein amino acid residues) is less than 1.5 A (preferably less than 1.0 A and more preferably less than 0.5 A) when superimposed on the coordinates provided for the residue
backbone atoms, will generally result in a structure which is substantially the same as the structure of Table 1 in terms of both its structural characteristics and usefulness for structure-based analysis, including design of CDP-ME kinase modulators. Likewise the skilled person would understand that changing the number and/or positions of the water molecules in these structures (where shown) will not generally affect the usefulness of the structure for structure-based analysis. Thus for the purposes described herein as being aspects of the present invention, it is within the scope of the invention if: the coordinates are transposed to a different origin and/or axes; the relative atomic positions of the atoms of the structure are varied so that the root mean square deviation of residue backbone atoms is less than 1.5 (preferably less than 1.0 A and more preferably less than
0.5 A) when superimposed on the coordinates provide in
Table 1 for the residue backbone atoms. Reference herein to the coordinate data of Table 1 thus includes the coordinate data in which one or more individual values of the Tables are varied in this way. Modifications in the native CDP-ME kinase crystal structure due to e.g. mutations, additions, substitutions, and/or deletions of amino acid residues could lead to variations in the CDP-ME kinase atomic coordinates and where such modified forms of CDP-ME kinase are being investigated, atomic coordinate data of CDP-ME kinase modified so that a ligand that bound to one
or more binding sites of CDP-ME kinase would be expected to bind to the corresponding binding sites of the modified CDP-ME kinase are, for the purposes described herein as being aspects of the present invention, also within the scope of the invention. Reference herein to the coordinates of Table 1 thus includes the coordinates modified in this way. Preferably, the modified coordinate data define at least one CDP-ME kinase binding site . In a further aspect, the invention provides a method for crystallising CDP-ME kinase with its substrate and nucleotide phosphate or analogue, comprising the steps of recombinantly producing CDP-ME kinase by a cell, purifying said CDP-ME kinase from said cell, contacting CDP-ME and a nucleotide phosphate or analogue with said purified CDP-ME kinase and growing a crystal or crystals of said CDP-ME kinase in complex with CDP-ME and the nucleotide phosphate or analogue. The crystal may be grown by any suitable method, e.g. by the hanging drop method as described in the Examples . Reference to a CDP-ME kinase catalytic domain should be taken to include catalytic domains of mutant CDP-ME kinase as described herein below. The term catalytic domain, as used herein refers to the structural domain of the protein and should not be interpreted as requiring the polypeptide to have catalytic activity; for example it may contain a mutation which impairs or abrogates
activity, e.g. at the active site, but which does not affect the gross structure of the domain. In another aspect, the invention provides a method of analysing a CDP-ME kinase ligand/co-factor ligand complex comprising the step of employing i) X-ray crystallographic diffraction data from the CDP-ME kinase ligand/co-factor complex and (ii) a three-dimensional structure of CDP-ME kinase alone or lacking either the ligand or co-factor to generate a difference Fourier electron density map of the complex. If the CDP-ME kinase alone or lacking either the ligand or co-factor is crystallised in a different space group to the crystals described herein, molecular replacement methods may be used instead of difference Fourier methods. Therefore, in the light of the present disclosure, CDP-ME kinase/ligand/co-factor complexes can be crystallised and analysed using X-ray diffraction methods, e.g. according to standard procedures and difference Fourier electron density maps can be calculated based on X-ray diffraction patterns. Electron density maps can be calculated using programs such as those from the Computing Collaborative Project Number 4. For map visualisation and model building programs such as Computing Collaborative Project Number 4 can be used. In another aspect, the invention relates to methods of determining three dimensional structures of closely related kinases of unknown structure by utilising in whole or in part the structural coordinates provided for
CDP-ME kinase in any one pf the data set provided herein (Table 1) . The target kinase will typically be homologous to CDP-ME kinase, such as the GHMP kinase super family (40) . The primary ways in which the three-dimensional coordinate data of the present invention can be used to solve other target kinase structures are as follows. The three-dimensional coordinate data provided herein for CDP-ME kinase may be aligned with an amino acid sequence of a target kinase to match homologous regions of the amino acid sequences, and a structure determined for the target kinase by homology modelling. The three-dimensional coordinate data of the present invention may be used to assist in interpretation of a set of raw X-ray crystallographic data obtained for a target kinase, in order to establish a structure for the target kinase . Thus the invention provides a method of homology modelling comprising the steps of: (a) aligning a representation of an amino acid sequence of a target kinase of unknown structure with the amino acid sequence of CDP-ME kinase to match homologous regions of the amino acid sequences; (b) modelling the structure of the matched homologous regions of the target kinase on the structure as defined by Table 1 of the corresponding regions of CDP-ME kinase; and
(c) determining a conformation (e.g. so that favourable interactions are formed within the target kinase and/or that a low energy conformation is formed) for the target kinase which substantially preserves the structure of said matched homologous regions . The term "homologous regions" describes amino acid residues in two sequences that are identical or have similar (e.g. aliphatic, aromatic, polar, negatively charged, or positively charged) sidechain chemical groups. Identical and similar residues in homologous regions are sometimes described as being respectively "invariant" and "conserved" by those skilled in the art. Preferably one or all of steps (a) to (c) are preformed by computer modelling. Homology modelling is a technique that is well known to those skilled in the art (see e.g. Greer, Science, Vol. 228, (1985), 1055, and Blundell et al . , Bur. J. Biochem, Vol. 172, (1988) f 513). By "homology modelling" , is meant the prediction of related kinase structures based either on x-ray crystallographic data or computer assisted de novo prediction of structure, based upon manipulation of the coordinate data of Table 1. The various in silico modelling techniques described herein may utilise coordinates from the crystal data set provided herein, or from any structure calculated by means of said data set. To avoid unnecessary repetition, reference is made herein to the coordinate data of Table 1.
"Homology modelling" extends to target kinases, in particular GHMP kinases, which are analogues or homologues of the CDP-ME kinase protein whose structure has been determined. It also extends to mutants of CDP- ME kinase protein itself. In general, comparison of amino acid sequences is accomplished by aligning the amino acid sequence of a polypeptide of a known structure with the amino acid sequence of the polypeptide of unknown structure. Amino acids in the sequences are then compared and groups of amino acids that are homologous are grouped together. This method detects conserved regions of the polypeptides and accounts for amino acid insertions or deletions . Homology between amino acid sequences can be determined using commercially available algorithms. The programs BLAST, gapped BLAST, BLASTN, PSI -BLAST and BLAST 2 sequences (provided by the National Center for Biotechnology Information) are widely used in the art for this purpose, and can align homologous regions of two amino acid, sequences. These may be used with default parameters to determine the degree of homology between the amino acid sequence of the protein of known structure and other target proteins which are to be modelled. Analogues are defined as proteins with similar three-dimensional structures and/or functions and little evidence of a common ancestor at a sequence level.
Homologues are defined as proteins with evidence of a common ancestor i.e. likely to be the result of evolutionary divergence and are divided into remote, medium and close sub-divisions based on the degree (usually expressed as a percentage) of sequence identity. A homologue is defined here as a protein with at least 40% sequence identity or which has at least one functional domain, which is characteristic of CDP-ME kinase. . There are two types of homologue : orthologues and paralogues . Orthologues are defined as homologous genes in different organisms, i.e. the genes share a common ancestor coincident with the speciation event that generated them. Paralogues are defined as homologous genes in the same organism derived from a gene/chromosome/genome duplication, i.e. the common ancestor of the genes occurred since the last speciation event . A mutant is a kinase characterised by replacement or deletion of at least one amino acid from a wild type CDP- ME kinase . Such a mutant may be prepared for example by site-specific mutagenesis, or incorporation of natural or unnatural amino acids. The present invention contemplates "mutants", and the application of the methods of the present invention to "mutants", wherein a "mutant" refers to a polypeptide which is obtained by replacing at least one amino acid residue in a native or synthetic CDP-ME kinase with a
different amino acid residue and/or by adding and/or deleting amino acid residues within the native polypeptide or at the N- and/or C-terminus of a polypeptide corresponding to a wildtype kinase and which has substantially the same three-dimensional structure as the kinase from which it is derived. By having substantially the same three-dimensional structure is meant having a set of atomic structure co-ordinates that have a root mean square deviation (r.m.s.d.) of less than or equal to about 2. oA when superimposed with the atomic structure co-ordinates of the wildtype kinase from which the mutant is derived when at least about 50% to 100% of the C, , , atoms of the kinase are included in the superposition. A mutant may have, but need not have, enzymatic or catalytic activity. To produce homologues or mutants, amino acids present in the said protein can be replaced by other amino acids having similar properties, for example hydrophobicity, hydrophobic moment, antigenicity, propensity to form or break -helical or β -pleated-sheet structures, and such like. Substitutional variants of a protein are those in which at least one amino acid in the protein sequence has been removed and a different residue inserted in its place. Amino acid substitutions are typically of single residues but may be clustered depending on functional constraints e.g. at a crystal contact .
Preferably amino acid substitutions will comprise conservative amino acid substitutions. Insertional amino acid variants are those in which one or more amino acids are introduced. This can be amino-terminal and/or carboxy-terminal fusion as well as intrasequence . Examples of amino-terminal and/or carboxy-terminal fusions are affinity tags, an MBP tag, and epitope tags. Amino acid substitutions, deletions and additions which do not significantly interfere with the three- dimensional structure of the kinase will depend, in part, on the region of the molecule where the substitution, addition or deletion occurs. In highly variable regions of the molecule, non-conservative substitutions as well as conservative substitutions may be tolerated without significantly disrupting the three-dimensional structure of the molecule. In highly conserved regions, or regions containing significant secondary structure, conservative amino acid substitutions are preferred. Conservative amino acid substitutions are well-known in the art, and include substitutions made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity and/or the amphipathic nature of the amino acid residues involved. For example, negatively charged amino acids include aspartic acid and glutamic acid; positively charged amino acids include lysine and arginine; amino acids with uncharged polar head groups having similar hydrophilicity values include the following: leucine, isoleucine, valine; glycine, alanine, asparagine, glutamine; serine, threonine;
phenylalanine, tyrosine. Other conservative amino acid substitutions are well known in the art. In some instances, it may be particularly advantageous or convenient to substitute, delete and/or add amino acid residues to a particular binding site or catalytic residue, in order to provide convenient cloning sites to cDNA encoding the polypeptide, to aid in purification of the polypeptide, etc. Such substitutions, deletions and/or additions which do not substantially alter the three dimensional structure of the wild-type kinase will be apparent to those having skills in the art. It should be noted that the mutants contemplated herein need not exhibit enzymatic activity. Indeed, amino acid substitutions, additions or deletions that interfere with the catalytic activity of the kinase but which do not significantly alter the three dimensional structure of the catalytic region are specifically contemplated by the invention. Such crystalline polypeptides, or the atomic structure co-ordinates obtained therefrom, can be used to identify compounds that bind to the protein. Once the amino acid sequences of the polypeptides with known and unknown structures are aligned, the structures of the conserved amino acids in a computer representation of the polypeptide with known structure are transferred to the corresponding amino acids of the polypeptide whose structure is unknown. For example, a tyrosine in the amino acid sequence of known structure
may be replaced by a phenylalanine, the corresponding homologous amino acid in the amino acid sequence of unknown structure . The structured of amino acids located in non- conserved regions may be assigned manually by using standard peptide geometries or by molecular simulation techniques, such as molecular dynamics. The final step in the process is accomplished by refining the entire structure using molecular dynamics and/or energy minimization. In a further aspect, the invention provides a method for determining the structure of a target kinase, which method comprises; providing the co-ordinates of Table 1, and positioning the co-ordinates in the crystal unit cell of said target kinase so as to provide a structure for said target kinase. In a preferred aspect of this invention the coordinates are used to solve the structure of target kinases particularly homologues of CDP-ME kinase such as in the GHMP family of kinases. The structures of the presently described CDP-ME kinase can be used to solve the crystal structure of other target GHMP kinases including other crystal forms of CDP-ME kinase, mutants, where X-ray diffraction data of these target proteins has been generated and requires interpretation in order to provide the structure.
In the case of other GHMP referred to above, the present invention allows the structures of such kinases to be obtained more readily where raw X-ray diffraction data is generated. Thus, where X-ray crystallographic or NMR spectroscopic data is provided for a target kinase of unknown three-dimensional structure, the structure of CDP-ME kinase as defined by Table 1 may be used to interpret that data to provide a likely structure for the other kinase by techniques which are well known in the art, e.g. phasing in the case of X-ray crystallography and assisting peak assignments in NMR spectra. One method that may be employed for these purposes is molecular replacement. In this method, the unknown crystal structure, whether it is another crystal form of CDP-ME kinase, a mutant or co-complex thereof, or the crystal of a target kinase with amino acid sequence homology to any functional domain of CDP-ME kinase, may be determined using any one of the data sets of CDP-ME kinase structure coordinates of this invention as provided herein. This method will provide an accurate structural form for the unknown crystal more quickly and efficiently than attempting to determine such information ab initio. Examples of computer programs known in the art for performing molecular replacement are CNS (Brunger A.T.;
Adams P.D.; Rice L.M. , Current Opinion in Structural
Biology, Volume 8, Issue 5, October 1998, Pages 606-611 (also commercially available from Accelerys San Diego,
CA) or AMORE (Navaza, J. (1994) . AMoRE : an automated package for molecular replacement. Acta Cryst . A50, 157- 163) . The invention may also be used to assign peaks of NMR spectra of such proteins, by manipulation of the data provided herein. In another aspect, the present invention provides systems, particularly a computer system, intended to generate structures and/or perform rational drug design for CDP-ME kinase/ligand/co-factor or CDP-ME kinase with either ligand or co-factor, or homologues or mutants, the system containing either (a) atomic coordinate data according to Table 1 recorded thereon, said data defining the three-dimensional structure of CDP-ME kinase, or at least selected coordinates thereof; (b) structure factor data of CDP-ME kinase recorded thereon, the structure factor data being derivable from the atomic coordinate data of Table 1; (c) a Fourier transform of atomic coordinate data according to Table 1 or at least selected coordinates thereof; (d) atomic coordinate data of a target kinase generated by homology modelling of the target based on the data of Table 1; (e) atomic coordinate data of a target kinase generated by interpreting X-ray crystallographic data or NMR data by reference to the data of Table 1; or (f) structure factor data derivable from the atomic coordinate data of is (d) or (e) .
The invention also provides such systems containing atomic coordinate data of GHMP kinases wherein such data has been generated according to the methods of the invention described herein based on the starting data provided by Table 1. Such data is useful for a number of purposes, including the generation of structures to analyse the mechanisms of action of kinases, and/or to perform rational drug design of compounds which interact with them, such as modulators of kinase activity, e.g. activators or inhibitors. In a further aspect, the present invention provides computer readable media with either (a) atomic coordinate data according from Table 1 recorded thereon, said data defining the three-dimensional structure of CDP-ME kinase, preferably in complex with a ligand and/or co- factor, or at least selected coordinates thereof; (b) structure factor data for CDP-ME kinase recorded thereon, the structure factor data being derivable from the atomic coordinate data of Table 1; (c) a Fourier transform of atomic coord-mate data according to Table 1, or at least selected coord-inates thereof; (d) atomic coordinate data of a target kinase generated by homology modelling of the target based on the data of Table 1; (e) atomic coordinate data of a target kinase generated by interpreting X-ray crystallographic data or NMR data by reference to the data of Table 1; or (f) structure factor data derivable from the atomic coordinate date of (d) or (e) .
By providing such computer readable media, the atomic coordinate data can be routinely accessed to model CDP-ME kinase or selected coordinates thereof. For example, RASMOL (Sayle et al . , TIBS, Vol. 20, (1995), 374) is a publicly available computer software package which allows access and analysis of atomic coordinate data for structure determination and/or rational drug design. On the other hand, structure factor data, which are derivable from atomic coordinate data (see e.g. Blundell et al . , in Protein Crystallography, Academic Press, New York, London and San Francisco, (1976) ) , are particularly useful for calculating e.g. difference Fourier electron density maps. In another aspect, the present invention provides methods for modelling the interactions between CDP-ME kinase and modulators of CDP-ME kinase activity. Thus there is provided a method for modelling the interaction between CDP-ME kinase and an agent compound which modulates CDP-ME kinase activity, comprising the steps of : (a) employing three-dimensional atomic coordinate data according to either of Table 1 to characterise the CDP-ME binding site; (b) providing the structure of said agent compound; and (c) fitting said agent compound to the binding site. The present invention further provides a method for identifying an agent compound (e.g. an inhibitor) which modulates CDP-ME kinase activity, comprising the steps:
(a) employing three-dimensional atomic coordinate data according to Table 1 to characterise at least one CDP-ME kinase binding site; (b) providing the structure of a candidate agent compound; (c) fitting the candidate agent compound to the binding site(s); and (d) selecting the candidate agent compound. Preferably a plurality of binding sites are characterised; preferably sufficient binding sites are characterised to define the CDP-ME binding activity and/or the ATP binding site which forms part of the catalytic site. For ease of reference, and to avoid unnecessary repetition, only the production of modulators of CDP-ME kinase activity is discussed here. However the present invention is considered to apply equally to the identification of modulators of any target enzyme whose structure has been determined by reference to the three-dimensional coordinate data for CDP-ME kinase provided herein. For example, the data provided herein may be used to calculate a structure for a related GHMP family kinase. Accordingly, the present invention extends to the use of such a structure for identification of modulators of that target enzyme . The data presented here shows details of the interaction between CDP-ME kinase and its co-factor, ATP. Since all known small molecule inhibitors of protein kinases are competitive with ATP, and therefore interact with the ATP binding site, an understanding of the CDP-ME kinase residues involved in the interaction with ATP
allows the development of specific and potent inhibitors of this kinase. The determination of the three-dimensional structure of CDP-ME kinase provides a basis for the identification of new and specific ligands for CDP-ME kinase, and other members of the GHMP family of kinases, for instance by computer modelling. As the structures of Table 1 show coordinate data for complexes of the active structures of CDP-ME kinase, they may enable the design of competitive inhibitors of CDP-ME kinase, or other GHMP kinases, by modelling compounds which compete for the ATP binding site, and/or the substrate binding site of the kinase. Thus the CDP-ME binding site may comprise one or more residues implicated in interaction with ATP (or the non-hydrolysable ATP analogue in Table 1) in the active conformation of the enzyme. Residues making particularly close contacts with AMP-PNP in the structure defined by Table 1 are described in more detail hereinafter. Thus the binding site may comprise one or more of these residues, or their equivalents in other isoforms of CDP-ME kinase or other GHMP kinases. Some of these contacts are conserved in other CDP-ME kinases and GHMP kinases . Thus the present invention enables the design of inhibitors of CDP-ME kinase which may have general activity across the family or be more specific for only CDP-ME kinases. That is to say, the candidate agent compound may be a better fit to the CDP-ME binding site
than to a corresponding binding site defined by the corresponding residues of the other kinase. Thus the method may involve the step of comparing the binding of the candidate agent compound to the CDP-ME binding site, and to a corresponding binding site defined by the corresponding residues of the other kinase. Likewise the structures provided enable the design of candidate agent compounds which are selective from other GHMP kinases over CDP-ME kinase, by designing compounds which are a better fit to binding sites on those GHMP kinases than to corresponding binding sites on CDP-ME kinase. Alternatively, the method may involve the step of comparing the binding of the candidate agent compound to the CDP-ME kinase or GHMP kinase binding site, and to a corresponding binding site of a mutant of the same kinase, in which significant residues are changed to those present in the corresponding positions in the other kinase . The candidate agent compound may be modelled on the nonhydrolysable ATP analogue (AMP-PNP) shown in either of
X JL S X ■ An interaction between a candidate agent compound and a residue of the binding site is considered to mimic an interaction between AMP-PNP and that residue if atoms from the candidate agent compound make similar interactions with corresponding residues in the binding site, e.g. ionic bonds, and electrostatic interactions
such as salt bridges, hydrogen bonds, and van der Waals interactions, as well as hydrophobic interactions. Preferably the atoms from the candidate agent compound, when fitted to the binding site, lie at a similar distance from atoms of the relevant residue as atoms of AMP-PNP when fitted to the binding site. Distances between atoms of AMP-PNP and atoms of residues in the CDP-ME kinase ATP binding site are shown in Table 1. More generally, an interaction between the candidate agent compound and the binding site may be considered to mimic an interaction between the substrate and the binding site if the relevant atoms have the relevant separations shown in Table 1 +/- IA, preferably +/- 0.5A, more preferably +/- 0.2A. The CDP-ME kinase binding site may comprise one or more residues implicated in interaction with the substrate, CDP-ME shown in Table 1 in the active configuration of the enzyme. Residues making particularly close contacts with CDP-ME in the structure defined by Table 1 are described in detail hereinafter. The candidate binding agent may¬ be modelled on the CDP-ME peptide identified from Table 1 information. When the candidate agent compound is fitted to the binding site, an interaction between the candidate agent compound and the binding site may mimic an interaction between the set of residues of Table 1.
An interaction between a candidate agent compound and a residue of the binding site is considered to mimic an interaction between the substrate peptide and that residue if atoms from the candidate agent compound make similar interactions with corresponding residues in the binding site, ionic bonds, and electrostatic interactions such as salt bridges, hydrogen bonds, and van der Waals interactions, as well as hydrophobic interactions. Preferably the atoms from the candidate agent compound, when fitted to the binding site, lie at a similar distance from atoms of the relevant residue as atoms of the substrate when fitted to the binding site. Distances between atoms of the substrate and atoms of residues in the substrate binding site are shown in Table 1. More generally, an interaction between the candidate agent compound and the binding site may be considered to mimic an interaction between the substrates and the binding site if the relevant atoms have the relevant separations shown in Table 1 +/- IA, preferably +/- 0.5A, more preferably +/- 0.2A. More specifically, a potential modulator of CDP-M kinase activity can be examined through the use of computer modelling using a docking program such as GRAM, DOCK, or AUTODOCK (see Walters et al . , Drug Discovery Today, Vol. 3, No. 4, (1998), 160-178, and Dunbrack et al., Folding and Design, 2, (1997), 27-42). This procedure can include computer fitting of candidate inhibitors to CDP-ME kinase to ascertain how well the
shape and the chemical structure of the candidate inhibitor will bind to the enzyme. Also computer-assisted, manual examination of the binding cavity structure of CDP-ME kinase may be performed. The use of programs such as GRID (Goodford, J. Med. Chem., 28, (1985), 849-857) - a program that determines probable interaction sites between molecules with various functional groups and the enzyme surface - may also be used to analyse the binding cavity to predict partial structures of inhibiting compounds. Computer programs can be employed to estimate the attraction, repulsion, and steric hindrance of the two binding partners (e.g. CDP-ME kinase) and a candidate inhibitor) . Generally the tighter the fit, the fewer the steric hindrances, and the greater the attractive forces, the more potent the potential modulator since these properties are consistent with a tighter binding constant . Furthermore, the more specificity in the design of a potential drug, the . more likely it is that the drug will not interact with other proteins as well. This will tend to minimise potential side effects due to unwanted interactions with other proteins. In one embodiment a plurality of candidate agent compounds are screened or interrogated for interaction with the binding sites. In one example, step (b) involves providing the structures of the candidate agent compounds, each of which is then fitted in step (c) to computationally
screen a database of compounds (such as the Cambridge Structural Database) for interaction with the binding sites. In another example, a 3-D descriptor for the agent compound is derived, the descriptor including e.g. geometric and functional constraints derived from the architecture and chemical nature of the binding cavity. The descriptor may then be used to interrogate the compound database, the identified agent compound being the compound which matches with the features of the descriptor. In effect, the descriptor is a type of virtual pharmacophore . For example, the descriptor may be based on the AMP- PNP molecule which interacts with the ATP binding site, or CDP-ME. Having designed or selected possible binding partners, these can then be screened for activity. Consequently, the method preferably comprises the further steps of: (e) obtaining or synthesising the candidate agent compound; and (f) contacting the candidate agent compound with CDP-ME kinase to determine the ability of the candidate agent compound to interact with CDP-ME kinase (or similarly with other homologous isoforms or GHMP kinase family members) . In step (f) the candidate agent compound may be contacted with CDP-ME kinase in the presence of a substrate, and typically a buffer, to determine the ability of the candidate agent compound to inhibit CDP-ME kinase. The buffer will typically contain ATP. So, for
example, an assay mixture for CDP-ME kinase may be produced which comprises the candidate inhibitor, substrate and buffer. Instead of, or in addition to, performing e.g. a chemical assay, the method may comprise the further steps of: (e) obtaining or synthesising the candidate agent compound; (f) forming a complex of CDP-ME kinase and the candidate agent compound; and (g) analysing (e.g. by the method of an earlier aspect of the invention) said complex by X-ray crystallography or NMR spectroscopy to determine the ability of the candidate agent compound to interact with CDP-ME kinase. Detailed structural information can then be obtained about the binding of the agent compound to CDP-ME kinase, and in the light of this information adjustments can be made to the structure or functionality of the compound, e.g. to improve binding to the binding cavity. Steps (e) to (g) may be repeated and re-repeated as necessary. For X-ray crystallographic analysis, the complex may be formed by crystal soak-in methods or co-crystallisation. Greer et al . describes an iterative approach to ligand design based on repeated sequences of computer modelling, protein-ligand complex formation and X-ray crystallographic or NMR spectroscopic analysis. Related approaches to structure-based drug design are also discussed in Bohacek et al . , medicinal Research Reviews, Vol. 16, (1996). As a result of the determination of the CDP-ME kinase 3D structure, more
purely computational techniques for rational drug design may also be used to design CDP-ME kinase modulators, e.g. activators or inhibitors (for an overview of these techniques see e.g. Walters et al) . For example, automated ligand-receptor docking programs (discussed e.g. by Jones et al . in Current Opinion in Biotechnology, Vol. 6, (1995). 652-656) which require accurate information on the atomic coordinates of target receptors may be used to design potential CDP-ME kinase. Linked-fragment approaches to drug design also require accurate information on the atomic coordinates of target receptors. The basic idea behind these approaches is to determine (computationally or experimentally) the binding locations of plural ligands to a target molecule, and the construct a molecular scaffold to connect the ligands together in such a way that their relative binding positions are preserved. The connected ligands thus form a potential lead compound that can be further refined using e.g. the iterative technique of Greer et al .. For a virtual linked-fragment approach see Verlinde et al . , J. of Computer-Aided Molecular Design, 6, (1992), 131-147, and for NMR and X-ray approaches see Shuker et al . , Science, 274, (1996), 1531-1534 and Stout et al . , Structure, 6. (1998), 839. The use of these approaches to design CDP-ME kinase inhibitors is made possible by the determination of the CDP-ME kinase structure complexed with its substrate and/or co-factor.
Many of the techniques and approaches to structure- based drug described above rely at some stage on X-ray analysis to identify the binding position of a ligand in a ligand-protein complex. A common way of doing this is to perform X-ray crystallography on the complex, produce a difference Fourier electron density map, and associate a particular pattern of electron density with the ligand. However, in order to produce the map (as explained e.g. by Blundell et al . ) it is necessary to know beforehand the protein 3D structure (or at least the protein structure factors) . Therefore, determination of the CDP- ME kinase complex structure also allows difference Fourier electron density maps of CDP-ME kinase alone or with either the substrate or co-factor to be produced, which can greatly assist the process of rational drug design. The approaches to structure-based drug design described above all require initial identification of possible compounds for interaction with the target bio- molecule (in this case CDP-ME) . Sometimes these compounds are known e.g. from the research literature. Thus the present invention provided methods of identifying mimetics of known modulators of CDP-ME kinase activity. The methods may involve the identification of a binding site for the known modulator. Subsequently, candidate compounds may be fitted to the same binding site in order to identify a compound which will mimic the activity of the known modulator.
For example, the methods described above may be used to model the binding site at with CDP-ME kinase interacts with a known modulator. A mimetic of the activating agent may then be designed by fitting candidate compounds to that binding site. Thus the methods of the present invention for identifying agent compounds which modulate CDP-ME kinase activity may involve fitting a candidate agent compound to a CDP-ME kinase binding site, wherein the binding site has previously been determined to bind a known agent compound as described above . When no suitable known starting compounds are known, or when novel compounds are wanted, a first stage of the drug design program may involve computer-based in silco screening of compound databases (such as the Cambridge Structural Database) with the aim of identifying compounds which interact with the binding site or sites of the target bio-molecule. Screening selection criteria may be based on pharmacokinetic properties such as metabolic stability and toxicity. However, determination of the CDP-ME kinase structure allows the architecture and chemical nature of each CDP-ME kinase binding site to be identified, which in turn allows the geometric and functional constraints of a descriptor for the potential inhibitor to be derived. The descriptor is, therefore, a type of virtual 3-D pharmacophore, which can also be used as selection criteria or filter for database screening.
In another aspect, the invention includes a compound which is identified as a modulator of CDP-ME kinase activity by the method of the earlier aspect. Following identification of a suitable modulator compound, it may be manufactured and/or used in the preparation, i.e. manufacture or formulation, or a composition such as a medicament, pharmaceutical composition or drug. These may be administered to individuals for treatment of an appropriate condition, e.g. inhibitors for use in the treatment of bacterial infection e.g. as an antibiotic. Inhibitors may also find applications as herbicides. Thus, the present invention extends in various aspects not only to a modulator as provided by the invention, but also a pharmaceutical composition, medicament, drug or other composition comprising such a modulator e.g. for treatment (which may include preventative treatment) of disease; a method comprising administration of such a composition to a patient, e.g. for treatment of disease; use of such a modulator in the manufacture of a composition for administration, e.g. for treatment of disease; and a method of making a pharmaceutical composition comprising admixing such a modulator with a pharmaceutically acceptable excipient, vehicle or carrier, and optionally other ingredients. The term "catalytic site" as used herein refers to a protein domain which when folded has particular characteristic structure, and not necessarily to a domain having any particular catalytic activity. Thus the
catalytic domain may contain a mutation which impairs or abrogates activity, e.g. substitution or deletion of one or more amino acid residues at the active siter but which does not affect the gross structure of the folded domain. The minimum catalytic site of a given kinase is the minimum polypeptide sequence from that kinase which will fold stably into the appropriate conformation when expressed independently. Catalytic site of other target GHMP kinases may be identified by alignment of the target sequences with that of CDP-ME kinase. In general, comparison of amino acid sequences is accomplished by aligning the amino acid sequence of a polypeptide of a known structure with the amino acid sequence of the polypeptide of unknown structure. Amino acids in the sequences are then compared and groups of amino acids that are homologous are group together. This method detects conserved regions of the polypeptides and accounts for amino acid insertions or deletions . Homology between amino acid sequences can be determined using commercially available algorithms. The programs BLAST, gapped BLAST, BLASTIN, PSI-BLAST and BLAST 2 sequences (provided by the National Center for Biotechnology Information) are widely used in the art for this purpose, and can align homologous regions of two amino acid sequences. These may be used with default parameters to determine the degree of homology between
the amino acid sequence of the protein of known structure and those of target proteins. The polypeptide may consist solely or essentially of the catalytic site in isolated form, e.g. a recombinant single domain. In a further aspect, the present invention provides nucleic acids encoding the CDP-ME kinase or GHMP kinase polypeptide as described herein. Throughout this specification, where nucleic acids are referred to, they may be wholly or partially synthetic. In particular they may be recombinant in that nucleic acid sequences which are not found together in nature (do not run contiguously) have been ligated or otherwise combined artificially. Alternatively they may have been synthesised directly e.g. using an automated synthesiser. Nucleic acid according to the present invention may be polynucleotides or oligonucleotides, and may include cDNA, RNA, genomic DNA (gDNA) and modified nucleic acids or nucleic acid analogs. Where a nucleic acid (or nucleotide sequence) of the invention is referred to herein, the complement of that nucleic acid (or nucleotide sequence) will also be embraced by the invention. The "complement" in each case is the same length as the reference, but is 100% complementary thereto whereby by each nucleotide is base paired to its counterpart i.e. G to C, and A to T or U.
The nucleic acids of the present invention may differ from any specific sequences recited or referred to herein by a change which is one or more of addition, insertion, deletion and substitution of one or more nucleotides . Preferably the reading frame is maintained. Changes to a nucleotide sequence may result in an amino acid change at the protein level, or not, as determined by the degeneracy of the genetic code. Nucleic acids of the present invention may be provided as part of a vector, and also provided by the present invention is a vector comprising nucleic acid as described herein, particularly vectors from which the polypeptide can be expressed under appropriate conditions, and a host cell containing any such vector or nucleic acid. "Vector" is defined to include, inter alia, any virus, plasmid, cosmid, or phage vector in double or single stranded linear or circular form which may or may not be self transmissible or mobilizable, and which can transform a prokaryotic or eukaryotic host either by integration into the cellular genome or exist extrachromosomally (e.g. autonomous replicating plasmid with an origin of replication) . Generally speaking, those skilled in the art are well able to construct vectors and design protocols for recombinant gene expression. Suitable vectors can be chosen or constructed, containing appropriate regulatory sequences, including promoter sequences, terminator
fragments, polyadenylation sequences, enhancer sequences, marker genes and other sequences as appropriat . For further details see, for example, Molecular Cloning: a Laboratory Manual: 3rd edition, Sambrook et al, 2000, Cold Spring Harbor Laboratory Press or Current Protocols in Molecular Biology, Second Edition, Ausubel et al . eds., John Wiley & Sons, 1992. Specifically included are shuttle vectors by which is mean a DNA vehicle capable, naturally or by design, of replication in two different host organisms, which may be selected from actinomycetes and related species, bacteria and eukaryotic (e.g. higher plant, mammalian, insect, yeast or fungal cells) . A vector including nucleic acid according to the present invention need not include a promoter or other regulatory sequence, particularly if the vector is to be used to introduce the nucleic acid into cells for recombination into the genome. Preferably a nucleic acid sequence of the present invention in the vector is under the control of, and operably linked to, an appropriate promoter or other regulatory elements for transcription in a host cell such as a microbial, e.g. bacterial, or yeast cell, or an insect of mammalian cell. The vector may be a bi- functional expression vector which functions in multiple hosts. In the case of genomic DNA, this may contain its own promoter or other regulatory elements and in the case of cDNA this may be under the control of an appropriate promoter or other regulatory elements for expression in
the host cell. By "promoter" is meant a sequence of nucleotides from which transcription may be initiated of DNA operably linked downstream (i.e. in the 3' direction on the sense strand of double-stranded DNA) . "Operably linked" means joined as part of the same nucleic acid molecule, suitably positioned and oriented for transcription to be initiated from the promoter. DNA operably linked to a promoter is "under transcriptional initiation regulation" of the promoter. In a preferred embodiment, the promoter is an inducible promoter. The term "inducible" as applied to a promoter is well understood by those skilled in the art. In essence, expression under the control of an inducible promoter is "switched on" or increased in response to an applied stimulus. The nature of the stimulus varies between promoters. Some inducible promoters cause little or undetectable levels of expression (or no expression) in the absence of the appropriate stimulus. Other inducible promoters cause detectable constitutive expression in the absence of the stimulus. Whatever the level of expression is in the absence of the stimulus, expression from any inducible promoter is increased in the presence of the correct stimulus. Thus these aspects of the invention provide a gene construct, preferably a replicable vector, comprising a promoter (optionally inducible) operably linked to a nucleotide sequence provided by the present invention.
Preferably the vector is capable of providing expression in a bacterial cell, especially where the expressed product is to be crystallised. The polypeptide may be encoded by a vector construct substantially similar to those disclosed herein. The present invention also encompasses method of making peptides or polypeptides as disclosed, the method including the step of expressing said polypeptide or peptide from nucleic acid encoding it, which in most embodiments will be nucleic acid according to the present invention. This may conveniently be achieved by growing a host cell containing such a vector in culture under appropriate conditions which cause or allow expression of the polypeptide. Polypeptides and peptides may also be expressed in in vi tro systems, such as reticulocyte lysates, as will be appreciated by the skilled person. Although certain specific amino acid sequences are referred to herein, e.g. in the context of peptides capable of activating GHMP kinases, it will be appreciated that similar sequences having functionally insignificant changes are equally appropriate for practising the present invention. Therefore amino acids present in the said sequences can be replaced by other amino acids having similar properties, for example hydrophobicity, hydrophobic moment, antigenicity, propensity to form or break α-helical or -pleated-sheet structures, and so. Substitutional variants of a protein are those in which at least one amino acid in the protein
sequence has been removed and a different residue inserted in its place. Amino acid substitutions are typically of single residues but may be clustered depending on functional constraints e.g. at a crystal contact . Preferably amino acid substitutions will comprise conservative amino acid substitutions. Insertional amino acid variants are those in which one or more amino acids are introduced. This can be amino-terminal and/or carboxy-terminal fusion as well as intrasequence . Examples of amino-terminal and/or carboxy-terminal fusions are affinity tags, maltose binding protein (MBP) tags, and epitope tags. Amino acid substitutions, deletions and additions which do not significantly interfere with three- dimensional structure will depend, in part, on the region of the molecule where the substitution, addition or deletion occurs. In highly variable regions of the molecule, non-conservative substitutions as well as conservative substitutions may be tolerated without significantly disruption the three-dimensional structure of the molecule. In highly conserved regions, or regions containing significant secondary structure, conservative amino acid substitutions are preferred. Conservative amino acid substitutions are well-known in the art, and include substitutions made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity and/or the amphipathic nature of the amino acid residues involved. For example,
negatively charged amino acids include aspartic acid and glutamic acid; positively charged amino acids include lysine and arginine; amino acids with uncharged polar head groups having similar hydrophiliciy values include the following: leucine, isoleucine, valine; glycine, alanine; asparagines, glutamine; serine, threonine; phenylalanine, tyrosine. Other conservative amino acid substitutions are well known in the art. In some instances, it may be particularly advantageous or convenient to substitute, delete and/or add amino acid residues to a particular binding site or catalytic residue, in order to provide convenient cloning sites in cDNA encoding the polypeptide, to aid in purification of the polypeptide, etc. Such substitutions, deletions and/or additions which do not substantially alter the three dimensional structure of the wild-type kinase will be apparent to those having skills in the art. Particular embodiments of the invention will now be described by way of example only, with reference to the accompanying drawings. Figure 1. The reaction catalyzed by CDP-ME kinase. Figure 2. A portion of the 2|FO|-|F0| o electron density map. Fo are observed, F- the calculated structure factors and <xo phases derived using SIGMAA (63) . A stick representation of the substrate observed in subunit B is colored according to atom type where blue, grey, purple and red represent nitrogen, carbon, phosphorus and oxygen positions respectively. The map is contoured at 1.3σ.
Figure 3. The CDP-ME kinase homodimer. (a) Ribbon diagram viewed parallel to the NCS twofold. The residues shown as red or blue ball-and-sticks (Arg21, Ala22, Asp80 and Gly87) contribute to dimer formation through electrostatic interactions. Substrate and cofactor are shown as black ball-and-sticks . (b) Surface representation colored blue for basic, red acidic residues. Ligands are depicted as black spheres. Figure 4. The sequence and structure of E. coli CDP- ME kinase. (a) Stereoview ribbon diagram of a monomer (β-strand numbers are black, α-helix numbers blue) .
Strands and helices in the cofactor-binding domain are colored red and yellow respectively, strands associated with the two β-sheets in the substrate-binding domain are colored light and dark green, the helices orange. Substrate and AMP-PNP are depicted as black ball-and- stick models. N and C identify the amino and carboxy termini of the polypeptide. (b) The amino acid sequence of E. coli CDP-ME kinase with the elements of secondary structure assigned and colored according to (a) . Residues strictly conserved or highly homologous in the sequences of the enzymes from Salmonella typhi , Vibrio cholera, Haemophilus influenzae, Pseudomonas aeruginosa, Neisseria meningitidis , Mycobacterium tuberculosis , Chlamydia trachomatis and Clostridium perfringens are black on a purple background, when conserved in at least six of the sequences they are enclosed in a purple box. The sequences were retrieved from EXPASY (http://www.expasy.ch) and aligned using CLUSTALW (64).
Open triangles identify key residues interacting with the substrate using the side chain; filled triangles are for those using their main chain. His26 uses both. θl and
Θ2 identify 310-helices and three red lines mark motifs I,
II and III. Figure 5. (a) Stereoview of the active site. Bonds in AMP-PNP are black, in the protein yellow, in CDP-ME grey. Selected hydrogen bonding interactions are shown as green dashed lines. Water molecules have been omitted; GlylOl and Glyl03 are semi-transparent for the purpose of clarity. (b) The proposed mechanism for CDP- ME kinase .
Experimental procedures Sample preparation and crystallization. The E. coli ispE gene, which encodes CDP-ME kinase was amplified from genomic DNA by polymerase chain reaction and cloned into the pET15b expression vector (Novagen) . The resulting plasmid was heat-shock transformed into E. coli strain BL21 (DE3) (Stratagene) for protein expression. Cells were grown in M9 medάum supplemented with the usual amino acids except that L-selenomethionine (SeMet; 100 mg/L) replaced L-methionine . The culture was incubated at 37 °C for 3 hours to an OD600 of 0.5 and protein expression was induced overnight at room temperature with 0.5 mM isopropyl- β-D-thiogalactopyranoside. Cells were harvested by centrifugation and disrupted in a French press. Following centrifugation, the supernatant was filtered and applied to a metal-chelating HiTrap column
(Pharmacia) previously equilibrated with nickel chloride (50 mM) followed by 50 mM Tris hydrochloride, pH 7.7, containing 50 mM NaCl (buffer A) . The column was washed with 25 mM bis-Tris propane, pH 7.7, containing 10 mM imidazole. CDP-ME kinase was eluted by 90 mM imidazole and dialyzed overnight against buffer A. The protein solution was applied to a Q-Sepharose anion exchange column (Pharmacia) which was then washed with 50 mM Tris hydrochloride, pH 8.5, containing 50 mM NaCl and developed with 100 mM NaCl. Fractions were analyzed on SDS-PAGE, combined and dialyzed against buffer A overnight. The solution was concentrated to 25 mg/mL. Sample purity was assessed by SDS-PAGE and MALDI-TOF (matrix-assisted laser desorption time-of-flight) mass spectrometry; the latter technique also confirmed full incorporation of SeMet . The enzyme was incubated with 2 mM AMP-PNP (Sigma) and 3 mM CDP-ME (48) on ice for two hours to provide a stock solution for crystallization. Monoclinic platelike crystals grew in hanging drops consisting of 1 μL of stock, 1 μL of reservoir solution (20% polyethylene glycol 8000, 0.2 M magnesium acetate, 0.1 M sodium cacodylate, pH 6.5) and 0.2 μL of 0.25 M sulfo-betaine .
Data collection, structure solution and refinement . Experimental details are presented in Table 2 and
appendix I. Crystals were maintained at 100 K in the presence of 20% glycerol as a cryoprotectant , and characterized in-house. Measurements were then made on beamline ID29 at the European Synchrotron Radiation Facility with an ADSC/-Q210 CCD detector. A single crystal of SeMet derivatised protein was used to measure 180 degrees of data at a wavelength (λ 0.9791A), determined from a Se K-edge X-ray absorption near-edge scan, to maximize the dispersive f" signal. A single- wavelength anomalous dispersion approach provided initial phases . Data were processed and scaled with DENZO/SCALEPACK (49) . Twelve Se positions were identified and phases calculated to 2A resolution with an overall figure-of- merit of 0.33 using the program SOLVE (50). Density modification (51) by solvent flattening and two-fold non- crystallographic symmetry (NCS) averaging raised the figure-of-merit to 0.59 and resulted in an electron density map of excellent quality. The map was interpreted automatically (51) and a model of 242 residues for each subunit was constructed. The remaining amino acids were subsequently included using the graphics program 0 (52) following rounds of refinement (53-55) interspersed with map inspection. NCS restraints were employed in the early stages of refinement then completely released. The careful placement of solvent molecules and active site ligands concluded the analysis. The refinement process was monitored with the use of R- free (56) and an example of electron density is shown in
Figure 2. Figures were prepared using MOLSCRIPT (57), RASTER3D (58), PROMOTIF (59) and ALINE (C.S. Bond, personal communication) .
Results and Discussion The subunit architecture and quaternary structure .
Recombinant E. coli CDP-ME kinase has been expressed, purified and crystallized. The crystals display space group P2. with unit cell dimensions of a = 61.0, b = 76.3 c = 68.6 A, β = 107.8 degrees. The asymmetric unit consists of two subunits, A and B, of approximate total mass 62 kDa. The subunits assemble with C2 symmetry to form an extended homodimer, of approximate dimensions 90 x 50 x 33 A (Fig. 3) , positioned in the unit cell with the NCS axis near perpendicular to the ab plane. The surface accessible area of the dimer is 25,150 A2. The surface areas for subunits A and B are approximately 13,210 and 12,980 A2 respectively so about 1,040 A2, i.e. only 4 % of the total surface area of two monomers, are buried on dimer formation. Despite such a small area of interaction, a dimer is observed in gel filtration experiments and persists even in MALDI-TOF mass spectrometry (data not shown) . The homodimer encloses a solvent filled channel, about 23A in length and lOA wide, with two active sites positioned at either end of this channel (Fig. 3) . A single type of subunit-subunit interface, adjacent to the substrate-binding site, creates the dimer and involves the placement of a type-1 turn between β2 and β3 of one
subunit into a depression formed between the C-terminal section of ocl and β6 of the partner. Salt bridges between Arg21 on one subunit with Asp80 of the partner, hydrogen bonds donated from the amide of Gly87 to the carbonyl of Ala22, a number of solvent mediated hydrogen bonding networks and the hydrophobic interactions between the side chains of Tyr25 of one subunit and Lys76 of the partner contribute to the stability of the dimer. The NCS is well conserved in the asymmetric unit. For example, the root-mean-square deviation (r.m.s.d.) between 278 Coc atoms is 0.6 A. The inventors describe the details in the active site of subunit B (see below) . The CDP-ME kinase subunit comprises ten α-helices
(approximately 40% of residues) , twelve β-strands
(approximately 28% of residues) and two short 310 sections (Fig. 4) . The subunit displays the characteristic two- domain fold of the GHMP kinase superfamily (60) . One domain, the cofactor or ATP-binding domain, comprises residues 1-10, 34-150 and 275-283 which form a four- stranded β-sheet (in order βl-β4-β6-β5, with β4 antiparallel to the others) on one side with a five-helix bundle (αl- 4, otlO) on the other. The second domain is constructed from residues 11-33 and 151-274 with, at its core, two four-stranded twisted antiparallel β-sheets (β2-β3-β7-β8 and βl0-βll-β9-βl2) and five helices at the periphery of the domain. This is the CDP-ME or substrate- binding domain.
Binding of AMP-PNP and CDP-ME; specificity and meσhanism. The ATP binding site is constructed by two sections of the protein structure. One segment comprises the C- terminal section of β6, the N-terminal section of α2 and a glycine-rich phosphate-binding loop linking these elements of secondary structure. The helix dipole of α2 may contribute to phosphate binding. The other segment lies over the purine-binding pocket and comprises the loop, with a turn of 310-helix, linking β5 to αl (Fig. (a) ) . The adenine binds in an aliphatic cleft formed by the side chains of Val57, Val60, Leu66, Ile67, Lys96 and MetlOO, near Ccc of Glyl07. The purine forms hydrogen- bonding interactions that stabilize the less common syn orientation of the base with respect to the glycosidic bond. The side chain carbonyl groups of two asparagines (Asn65, AsnllO) on either side of Ade N6 , accept hydrogen bonds from the amino group (Fig. 5) . The asparagines ND2 groups participate in a network of water-mediated hydrogen bonding interactions to the amide and carbonyl groups of Val57 and Val60 respectively. AsnllO ND2 also interacts with Ser7 OG and Asp39 OD2 , the latter positioned by hydrogen bonds donated from the main chain amides of Arg97 and Leu98, and a salt bridge with Lys96. Ade Nl and N7 accept hydrogen bonds from Lys96 NZ and the amide of Leu66 respectively. The ribose and phosphates of AMP-PNP are solvent accessible. The α-phosphate binds a water molecule, which also interacts with Lys96 NZ, the Pro99 carbonyl
and GlylOl amide. The α-β linking oxygen accepts a hydrogen bond from the amide of Glyl07 while the β- phosphate accepts hydrogen bonds donated from the hydroxyl and main chain amide nitrogen of Serl08. A well-ordered water molecule interacts with this phosphate and participates in hydrogen bonding interactions with Aspl41 OD2, the γ-phosphate of AMPPNP and the β-phosphate of the CDP-ME substrate. A γ-phosphate oxygen of AMP-PNP accepts a hydrogen bond donated from the amide group of Glyl05. Another interacts with the carbonyl of GlylOl and is likely protonated given the close contact of 2.7 A. The proton may participate in a bifurcated hydrogen bond to the α-phosphate oxygen nearby; alternatively the α-phosphate itself may also be protonated. Two water molecules interact with the terminal phosphate, one links to the β-phosphate (see above) whilst the other forms hydrogen bonds with the amide group of Thr240 and the 02M hydroxyl of CDP-ME, which is the phosphorylation site. The CDP-ME binding site is formed by contributions from β3, <x5, and three turns that link <x3 to <x4 , β7 to β8 and βlO to βll. The cytosine is tucked in towards β3, sandwiched between the aromatic side chains of Tyr25 and Phel85 with the ribose directed out of the cleft and placed between Tyr25 and Prol82. A water molecule interacts with the ribose 02' and also Cyt 02. His26 is a key residue providing three hydrogen-bonding interactions with the pyrimidine. Cyt 02 and N3 accept hydrogen bonds donated by His26 ND1 and amide
respectively while Cyt N4 donates to the His26 carbonyl. The His26 side chain is oriented by NE2 accepting a hydrogen bond from the side chain of Argl92 (not shown) . The substrate α-phosphate interacts with the hydroxyl group of Tyr25 and a water molecule. The 0 link between α and β-phosphate accepts a hydrogen bond from the amide of Alal40 and the β-phosphate has solvent mediated associations with Aspl41 OD2 , the β-phosphate of AMP-PNP and Thrlδl OG1. The CDP-ME tail, with α- and β- phosphates in a staggered conformation, is directed over towards the γ-phosphate of AMP-PNP and the 01M and 02M hydroxyls form hydrogen bonds with Aspl41 0D1 and OD2 , respectively. The CDP-ME 02M group also interacts with the carbonyl of Vall56 via a water bridge whilst 03M accepts hydrogen bonds from LyslO NZ and interacts with a water molecule that bridges over to the AMP-PNP γ- phosphate. The CDP-ME 04M hydroxyl accepts a hydrogen bond from Asnl2 ND2 and donates one to Aspl41. Asnl2 is held in place by OD1 accepting hydrogen bonds from LyslO NZ and the Gly239 amide. The catalytic center is located in a deep cavity near the interface of the cofactor and substrate-binding domains. LyslO and Aspl41 are positioned here to participate in hydrogen bonding interactions with CDP-ME 02M (Fig. 5(a)). This combination of residues would polarize the hydroxyl group and facilitate proton abstraction with Aspl41 acting as a general base to generate the 02M nucleophile and LyslO also contributing
to the stabilization of the transition state (Fig. 5(b)). The binding of the cofactor places the γ-phosphate nearby ready to accept nucleophilic attack from CDP-ME 02M. This will likely involve an associative inline mechanism to form a pentacovalent intermediate, and subsequently the production of CDP-ME2P and ADP. Such a mechanism is widely recognized as the most likely for enzyme-catalyzed phospho-group transfer (60, 61) . In contrast to structures of rat MVK (45) and M. jannaschii HSK (40) , we see no evidence for a divalent metal ion binding to the cofactor phosphates despite the presence of magnesium ions in the crystallization buffer. We observed well-defined peaks in electron and difference density maps in the active sites, which were assigned as water molecules on the basis of interatomic distances and types of contacts with functional groups. In rat MVK and M. jannaschii HSK, Mg2+ is bound to the ATP triphosphate and coordinated by a conserved glutamic acid residue (Glul30 and Glul93 respectively) . This residue is not conserved in CDP-ME kinase, which in a structural overlay is occupied by Glyl39 (not shown) . GHMP kinase superfamily members carry three conserved sequence motifs (40) which in E. coli CDP-ME kinase occur at Lysll-Tyrl5 (I) , Pro99-Serl09 (II) and Leu237-Val244 (III) . They are positioned beside each other at the domain-domain interface and help to create the active site. Motif I forms a bulge after βl and leading into β2; it is adjacent to motif III which forms a type II turn between βlO and βll and together these
sections of polypeptide help to create the catalytic center. Motif II forms a loop that closes over then extends into the N-terminal region of α2 , and binds the
ATP phosphates .
Structural homologues. An architectural comparison using DALI (62) identified a close structural relationship between CDP-ME kinase and four members of the GHMP kinase superfamily, HSK (40, 44), MVK (45), PMVK (46) and MDD (42) . The overall structure of the ATP- binding domains and the core of the substrate-binding domains are well conserved. However, there are noteworthy differences in the catalytic centers and purine-binding pockets. The structural variation on the surface of these domains contributes to different modes of oligomerisation in the GHMP family of enzymes (40) whilst the differences in the catalytic centers reflect the different molecular features required for distinct specificities. In particular we note that the pyrimidine- binding site in CDP-ME kinase is constructed with an extension to the first β-turn-β unit, a feature lacking in the other enzymes, which process smaller substrates lacking a nucleotide moiety.
The most relevant structures for a detailed comparison are HSK and MVK, in part because they are the best characterized of the GHMP family with structures of ligand complexes having been determined (40, 44, 45) and
they are also most similar to CDP-ME kinase. A single subunit of CDP-ME kinase aligned with HSK (PDB accession code: IFWK) with a Z-score of 21 and an r.m.s.d. of 3.0 A for 254 Cα atoms. The alignment with MVK (PDB code 1KKH) is comparable with a Z-score of 20 and r.m.s.d. of 3.0 A for 251 Cα atoms. The Z-score is a measure of the statistical significance of the best subunit-subunit alignment and was determined by DALI . Typically, dissimilar proteins will have a Z-score less than 2.0. Both HSK and CDP-ME kinase bind the purine moiety of the cofactor in syn orientation with respect to the ribose. There is strong conservation of secondary structure around the whole ATP-binding site and this extends to conservation of side chains in the purine- binding pocket. In E. coli CDP-ME kinase the aliphatic side chains that contribute to the purine-binding pocket (Leu66, Ile67, Leu53, Ile94) are replaced by Val63, Ala64, Ile48 and Ile85 in M. jannaschii HSK. Strikingly, four of the hydrogen bonding interactions between the base and the enzyme, only possible with the adenine in syn conformation, are also conserved. These involve the side chains of Asn62, Lys87 Asp34 strictly conserved as Asn65, Lys96 and Asp39. Adjacent to, and orientating the lysine side chains are the conserved aspartate residues, Asp34 and Asp39 in CDP-ME kinase and HSK, respectively. The remaining hydrogen bonding interaction involves AsnllO in CDP-ME kinase that in HSK is SerlOl, positioned such that the amine is replaced by the hydroxyl thereby retaining the hydrogen bond donating capacity.
By way of contrast, in the binary complex of rat MVK-ATP the nucleotide adopts the more common anti orientation (43) . Although much of the MVK ATP-binding domain overlays well with the corresponding domain of CDP-ME kinase we note that MVK carries an additional β- strand, producing an extended β-sheet, and a completely different loop leading into helix αl . In addition, the adenine-binding pocket of MVK carries specific amino acid side chains (for example Tyr80 and Ilel20 which correspond to Leu66 and AsnllO in E. coli CDP-ME kinase) , which on steric considerations would preclude a syn conformation for the base. As described, the ternary complex structure suggests a likely mechanism based on the combination of LyslO and Aspl41. The mechanism postulated for HSK is different since there is no obvious catalytic base in that active site (40) and we note that the corresponding positions of LyslO and Aspl41 in HSK are Thrl4 and Asnl41. MVK on the other hand has the same lysine-aspartate combination (Lysl3 and AsplδO in the M. jannaschii enzyme) and is likely to catalyze phosphoryl transfer in similar fashion to CDP-ME kinase.
Functional homologues. The sequences of CDP-ME kinase from eight species, selected to be representative of bacterial pathogens, were aligned with the sequence of the E. coli enzyme (Fig. 4(b)). Pair wise alignments
indicate that identity and homology range from 90 and 95% between E. coli and Salmonella typhi enzymes to 21 and 38% between E. coli and Mycobacterium tuberculosis enzymes. The averages are 45 and 60% over all species. Amino acid conservation extends throughout the sequence and is particularly well maintained in elements of secondary structure and in the active sites. Some 29 residues have been discussed above in the context of direct or solvent mediated interactions involving CDP-ME kinase with ligands and also in organizing the active site. Of these, 16 are absolutely conserved in all nine sequences and a further nine are strictly conserved in at least six of the sequences. In conclusion, our high-resolution crystallographic analysis of a ternary complex of E. coli CDP-ME kinase has delineated the structure, specificity and mechanism of the enzyme responsible for phosphorylation in the non- mevalonate route of isoprenoid biosynthesis and one shown to be essential for cell viability. The high level of sequence conservation indicates a well-conserved structure of CDP-ME kinase in microbial pathogens and our crystallographic model therefore provides a high- resolution template for a structure-based approach to aid the search for inhibitors of the enzyme and subsequently of isoprenoid biosynthesis. Such inhibitors could be lead compounds to support the development of novel broad- spectrum antimicrobial drugs.
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Table 2. Data collection and refinement statistics.
Resolution (A) / Completeness 2.0 / 94.3 (92.3)
No. of measurements / unique reflections 364,197 / 39,761
1/(5(1) /R-merge (%) 12.9 (5.6) / 4.8 (14.7)
Protein residues / Water molecules 566 / 384
AMP-PNP / CDP-ME / Cl- ' 2 / 2 / 1
R-work (%) / No. of reflections 16.6 / 37,773
R-free (%) / No. of reflections 20.2 / 1 ,988
Wilson B (A2) 17.8 Average isotropic thermal parameters (A2) Main chain / Side chain 15.3 / 18.4 Solvents / AMP-PNP / CDP-ME 28.9 / 44.0 / 29.1
R.m.s.d. for bond lengths (A) / bond angles (°) 0.009 / 1.33 Ramachandran analysis (%)
Favored regions / Additionally allowed regions 92.9 / 7.1
Numbers in parenthesis refer to a high-resolution bin of approximate width 0.1A.
Appendix I
COMPND — • CDP-ME kinase
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
REMARK 3 AUTHORS : MURSHUDOVNAGIN.DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.79
REMARK 3 NUMBER OF REFLECTIONS : 37160
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.16478
REMARK 3 R VALUE (WORKING SET) : 0.16262
REMARK 3 FREE R VALUE : 0.20502
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1972
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.003
REMARK 3 BIN RESOLUTION RANGE LOW : 2.055
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2089
REMARK 3 BIN R VALUE (WORKING SET) : 0.175
REMARK 3 BIN FREE R VALUE SET COUNT : 108
REMARK 3 BIN FREE R VALUE : 0.245
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 5012
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.772
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) 0.35
REMARK 3 B22 (A**2) -0.18
REMARK 3 B33 (A**2) -0.55
REMARK 3 B12 (A**2) 0.00
REMARK 3 B13 (A**2) -0.62
REMARK 3 B23 (A**2) 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.181
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.101
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.576
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4743 ; 0.010 ; 0.021
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6494 ; 1.338 ; 1.996
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 580 ; 6.550 ; 5.000
REMARK 3 CHI RAL-CENTER RESTRAINTS (A**3): 743 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3553 ; 0.009 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2152 ; 0.187 ; 0.300
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 641 ; 0.185 ; 0.500
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 43 ; 0.131 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 37 ; 0.341 ; 0.500
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2861 ; 0.864 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4647 ; 1.600 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1882 ; 2.904 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1839 ; 4.476 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 3
CISPEP 1 GLY A 241 ALA A 242 0.00
CISPEP 2 GLY B 241 ALA B 242 0.00
CRYST1 61.000 76.000 69.000 90.00 108.00 90.00 P21
SCALE1 0.016393 0.000000 0.005327 0.00000
SCALE2 0.000000 0.013158 0.000000 0.00000
SCALES 0.000000 0.000000 0.015239 0.00000
Table 1
ATOM 1 N MSEA 1 5.18041.441 18.9671.0029.55 N
ATOM 2 CA MSEA 1 4.76639.997 18.927 1.0029.60 C
ATOM 3 CB MSEA 1 4.20639.61217.5481.0030.42 C
ATOM 4 CG MSEA 1 3.05440.47717.0371.0036.00 C
ATOM 5SE MSEA 1 1.42740.29718.101 1.0042.31 SE
ATOM 6 CE MSEA 1 1.47942.01519.0651.0042.05 C
ATOM 7 C MSEA 1 5.91839.04619.2781.0027.70 C
ATOM 8 O MSEA 1 7.02939.179 18.7641.0027.63 O
ATOM 9 N ARG A 2 5.63038.08320.146 1.0025.10 N
ATOM 10 CA ARG A 2 6.531 36.97220.417 1.0023.49 C
ATOM 11 CBAARGA 2 6.251 36.40921.811 0.5023.55 C
ATOM 12 CBBARGA 2 6.30436.42521.8290.5023.92 C
ATOM 13 CGAARGA 2 7.45635.83522.541 0.5024.73 C
ATOM 14 CGBARGA 2 6.79237.35022.9430.5026.36 C
ATOM 15 CDAARGA 2 7.18035.47724.0070.5026.78 C
ATOM 16 CDBARGA 2 5.68738.15223.6300.5031.18 C
ATOM 17 NEAARGA 2 6.791 36.64924.7900.5029.65 N
ATOM 18 NEBARGA 2 5.46339.44322.9760.5034.93 N
ATOM 19 CZAARGA 2 7.01236.79526.0940.5031.13 C
ATOM 20 CZBARGA 2 5.38040.60823.6120.5036.44 C
ATOM 21 NH1AARGA 2 7.62435.83926.7830.5031.30 N
ATOM 22 NH1BARGA 2 5.49540.661 24.9330.5036.10 N
ATOM 23 NH2AARGA 2 6.61937.90326.7140.5032.27 N
ATOM 24 NH2BARGA 2 5.18341.72422.9240.5037.30 N
ATOM 25 C ARG A 2 6.33435.87519.3721.0020.92 C
ATOM 26 O ARG A 2 5.19235.511 19.0521.0020.41 O
ATOM 27 N THR A 3 7.43235.36718.8191.0017.23 N
ATOM 28 CA THR A 3 7.37734.192 17.952 1.0014.24 C
ATOM 29 CB THR A 3 8.01834.460 16.567 1.0014.92 C
ATOM 30 OG1 THR A 3 9.341 34.990 16.738 1.0010.81 O
ATOM 31 CG2THRA 3 7.27035.566 15.813 1.0016.65 C
ATOM 32 C THR A 3 8.07333.02218.634 1.0013.75 C
ATOM 33 O THR A 3 8.96433.231 19.451 1.0012.78 O
ATOM 34 N GLNA 4 7.65331.80018.303 1.0012.61 N
ATOM 35 CA GLN A 4 8.19530.58218.9091.0012.60 C
ATOM 36 CB GLNA 4 7.12729.830 19.711 1.0012.72 C
ATOM 37 CG GLN 4 6.92930.33221.1081.0018.29 C
67
ATOM 38 CD GL A 4 6.166 29.354 22.004 1.00 23.10 C
ATOM 39 OE1 GLN A 4 5.562 28.392 21.524 1.00 19.53 O
ATOM 40 NE2 GLN A 4 6.185 29.616 23.308 1.00 25.48 N
ATOM 41 C GL A 4 8.731 29.677 17.817 1.00 11.85 C
ATOM 42 O GLN A 4 8.078 29.486 16.789 1.00 12.64 O
ATOM 43 N TRP A 5 9.912 29.114 18.044 1.00 9.91 N
ATOM 44 CA TRP A 5 10.648 28.398 17.007 1.00 10.05 C
ATOM 45 CB TRP A 5 11.814 29.247 16.478 1.00 9.86 C
ATOM 46 CG TRP A 5 11.416 30.599 15.945 1.00 9.75 C
ATOM 47 CD1 TRP A 5 11.122 31.718 16.675 1.00 10.10 C
ATOM 48 NE1 TRP A 5 10.799 32.758 15.839 1.00 10.19 N
ATOM 49 CE2 TRP A 5 10.862 32.321 14.541 1.00 10.55 C
ATOM 50 CD2 TRP A 5 11.263 30.966 14.574 1.00 9.98 C
ATOM 51 CE3 TRP A 5 11.434 30.292 13.3.61 1.00 11.46 C
ATOM 52 CZ3 TRP A 5 11.205 30.982 12.165 1.00 11.35 C
ATOM 53 CH2 TRP A 5 10.817 32.325 12.171 1.00 13.47 C
ATOM 54 CZ2 TRP A 5 10.643 33.013 13.344 1.00 12.40 C
ATOM 55 C TRP A 5 11.192 27.082 17.549 1.00 9.75 C
ATOM 56 O TRP A 5 11.792 27.053 18.624 1.00 10.28 O
ATOM 57 N PRO A 6 10.981 25.997 16.812 1.00 9.47 N
ATOM 58 CA PRO A 6 11.493 24.686 17.221 1.00 9.39 C
ATOM 59 CB PRO A 6 10.917 23.733 16.168 1.00 9.42 C
ATOM 60 CG PRO A 6 9.779 24.487 15.554 1.00 11.77 C
ATOM 61 CD PRO A 6 10.233 25.934 15.552 1.00 9.34 C
ATOM 62 C PRO A 6 13.010 24.661 17.162 1.00 9.57 C
ATOM 63 O PRO A 6 13.607 25.304 16.281 1.00 9.04 O
ATOM 64 N SER A 7 13.612 23.948 18.110 1.00 9.19 N
ATOM 65 CA SER A 7 15.036 23.678 18.100 1.00 8.73 C
ATOM 66 CB SER A 7 15.739 24.541 19.144 1.00 9.05 C
ATOM 67 OG SER A 7 17.135 24.557 18.937 1.00 12.46 O
ATOM 68 C SER A 7 15.215 22.199 18.387 1.00 8.06 C
ATOM 69 O SER A 7 15.448 21.811 19.538 1.00 8.75 O
ATOM 70 N PRO A 8 15.065 21.374 17.348 1.00 6.97 N
ATOM 71 CA PRO A 8 15.033 19.914 17.498 1.00 7.80 C
ATOM 72 CB PRO A 8 14.642 19.428 16.097 1.00 8.23 C
ATOM 73 CG PRO A 8 15.159 20.501 15.173 1.00 6.79 C
ATOM 74 CD PRO A 8 14.892 21.782 15.939 1.00 6.80 C
ATOM 75 C PRO A 8 16.387 19.345 17.841 1.00 8.88 C
ATOM 76 O PRO A 8 17.410 19.984 17.567 1.00 9.32 O
ATOM 77 N ALAA 9 16.388 18.158 18.440 1.00 8.01 N
ATOM 78 CA ALA A 9 17.601 17.373 18.601 1.00 7.20 C
ATOM 79 CB ALA A 9 17.406 16.345 19.694 1.00 7.68 C
ATOM 80 C ALA A 9 17.954 16.674 17.300 1.00 7.38 C
ATOM 81 O ALA A 9 17.120 16.605 16.393 1.00 6.50 O
ATOM 82 N LYS A 10 19.189 16.158 17.203 1.00 6.24 N
ATOM 83 CA LYS A 10 19.525 15.160 16.173 1.00 7.27 C
ATOM 84 CB LYS A 10 20.584 15.679 15.168 1.00 6.72 C
ATOM 85 CG LYS A 10 21.886 16.194 15.787 1.00 6.15 C
ATOM 86 CD LYS A 10 22.918 15.078 16.092 1.00 7.99 C
ATOM 87 CE LYS A 10 24.126 15.657 16.851 1.00 4.99 C
ATOM 88 NZ LYS A 10 25.046 14.597 17.377 1.00 9.62 N
ATOM 89 C LYS A 10 20.022 13.858 16.778 1.00 7.44 C
ATOM 90 O LYS A 10 20.358 13.795 17.972 1.00 7.76 O
ATOM 91 N LEU A 11 20.086 12.832 15.934 1.00 6.80 N
ATOM 92 CA LEU A 11 20.848 11.615 16.215 1.00 7.26 C
ATOM 93 CB LEU A 11 19.932 10.377 16.282 1.00 6.45 C
ATOM 94 CG LEU A 11 18.837 10.369 17.351 1.00 6.73 C
ATOM 95 CD1 LEU A 11 17.985 9.111 17.219 1.00 9.61 C
ATOM 96 CD2 LEU A 11 19.423 10.470 18.757 1.00 5.39 C
ATOM 97 C LEU A 11 21.864 11.396 15.118 1.00 7.99 C
ATOM 98 O LEU A 11 21.597 11.686 13.941 1.00 8.88 O
ATOM 99 N ASN A 12 23.028 10.877 15.480 1.00 8.39 N
ATOM 100 CA ASN A 12 23.865 10.245 14.482 1.00 9.30 C
ATOM 101 CB ASN A 12 25.346 10.341 14.832 1.00 8.37 C
ATOM 102 CG ASN A 12 25.791 11.777 15.113 1.00 10.04 C
ATOM 103 OD1 ASN A 12 25.699 12.247 16.237 1.00 11.64 O
ATOM 104 ND2 ASN A 12 26.281 12.468 14.083 1.00 11.89 N
ATOM 105 C ASN A 12 23.420 8.794 14.352 1.00 9.67 C
ATOM 106 O ASN A 12 23.717 7.970 15.214 1.00 9.72 O
ATOM 107 N LEU A 13 22.682 8.501 13.279 1.00 9.19 N
ATOM 108 CA LEU A 13 22.200 7.149 13.011 1.00 8.70 C
ATOM 109 CB LEU A 13 21.278 7.146 11.786 1.00 8.57 C
ATOM 110 CG LEU A 13 20.016 8.033 11.920 1.00 9.50 C
ATOM 111 CD1 LEU A 13 19.040 7.817 10.754 1.00 9.41 C
ATOM 112 CD2 LEU A 13 19.321 7.802 13.259 1.00 10.55 C
ATOM 113 C LEU A 13 23.376 6.181 12.850 1.00 8.88 C
ATOM 114 O LEU A 13 23.313 5.034 13.286 1.00 9.78 O
ATOM 115 N PHE A 14 24.462 6.671 12.261 1.00 8.90 N
ATOM 116 CA PHE A 14 25.756 5.988 12.319 1.00 8.70 C
ATOM 117 CB PHE A 14 25.939 4.975 11.144 1.00 8.91 C
ATOM 118 CG PHE A 14 25.992 5.598 9.746 1.00 8.49 C
ATOM 119 CD1 PHE A 14 27.049 6.425 9.350 1.00 8.74 C
ATOM 120 CE1 PHE A 14 27.122 6.947 8.032 1.00 5.19 C
ATOM 121 CZ PHE A 14 26.132 6.633 7.121 1.00 9.08 C
ATOM 122 CE2 PHE A 14 25.080 5.801 7.502 1.00 8.52 C
ATOM 123 CD2 PHE A 14 25.018 5.285 8.805 1.00 11.16 C
ATOM 124 C PHE A 14 26.886 7.010 12.385 1.00 9.15 C
ATOM 125 O PHE A 14 26.671 8.188 12.099 1.00 9.50 O
ATOM 126 N LEU A 15 28.080 6.553 12.763 1.00 9.29 N
ATOM 127 CA LEU A 15 29.241 7.418 12.933 1.00 11.07 C
ATOM 128 CB LEU A 15 29.175 8.148 14.290 1.00 10.64 C
ATOM 129 CG LEU A 15 30.225 9.189 14.703 1.00 14.24 C
ATOM 130 CD1 LEU A 15 30.771 9.976 13.534 1.00 18.42 C
ATOM 131 CD2 LEU A 15 29.624 10.135 15.763 1.00 12.16 C
ATOM 132 C LEU A 15 30.522 6.593 12.825 1.00 10.89 C
ATOM 133 O LEU A 15 30.795 5.748 13.666 1.00 11.33 O
ATOM 134 N TYR A 16 31.284 6.844 11.768 1.00 10.67 N
ATOM 135 CA TYR A 16 32.504 6.114 11.502 1.00 10.13 C
ATOM 136 CB . TYR A 16 32.395 5.335 10.172 1.00 8.59 C
ATOM 137 CG TYR A 16 31.182 4.416 10.140 1.00 8.22 C
ATOM 138 CD1 TYR A 16 30.145 4.630 9.246 1.00 7.67 C
ATOM 139 CE1 TYR A 16 29.010 3.817 9.249 1.00 7.29 C
ATOM 140 CZ TYR A 16 28.911 2.775 10.150 1.00 7.68 C
ATOM 141 OH TYR A 16 27.792 1.991 10.144 1.00 11.12 O
ATOM 142 CE2 TYR A 16 29.913 2.538 11.057 1.00 9.49 C
ATOM 143 CD2 TYR A 16 31.051 3.361 11.056 1.00 11.22 C
ATOM 144 C TYR A 16 33.654 7.096 11.470 1.00 10.59 C
ATOM 145 O TYR A 16 33.558 8.149 10.851 1.00 11.68 O
ATOM 146 N ILE A 17 34.726 6.752 12.163 1.00 11.42 N
ATOM 147 CA AILE A 17 35.934 7.565 12.210 0.50 11.83 C
ATOM 148 CA BILE A 17 35.921 7.587 12.183 0.50 11.97 C
ATOM 149 CB AILE A 17 36.498 7.582 13.645 0.50 11.95 C
ATOM 150 CB BILE A 17 36.463 7.738 13.615 0.50 12.16 C
ATOM 151 CG1AILE A 17 35.356 7.621 14.678 0.50 11.05 C
ATOM 152 CG1 BILE A 17 35.375 8.302 14.530 0.50 12.08 C
ATOM 153 CD1AILE A 17 34.727 8.971 14.895 0.50 12.21 C
ATOM 154 CD1 BILE A 17 35.433 7.802 15.946 0.50 13.32 C
ATOM 155 CG2AILE A 17 37.506 8.730 13.830 0.50 12.38 C
ATOM 156 CG2BILE A 17 37.708 8.642 13.635 0.50 12.35 C
ATOM 157 C ILE A 17 36.966 7.001 11.242 1.00 11.96 C
ATOM 158 O ILE A 17 37.443 5.881 11.438 1.00 11.61 O
ATOM 159 N THR A 18 37.299 7.767 10.202 1.00 12.99 N
ATOM 160 CA THR A 18 38.101 7.251 9.086 1.00 14.29 C
ATOM 161 CB THR A 18 37.509 7.728 7.741 1.00 14.60 C
ATOM 162 OG1 THR A 18 37.439 9.159 7.717 1.00 15.39 O
ATOM 163 CG2 THR A 18 36.042 7.286 7.607 1.00 12.45 C
ATOM 164 C THR A 18 39.589 7.612 9.156 1.00 15.67 C
ATOM 165 O THR A 18 40.417 7.047 8.429 1.00 15.73 O
ATOM 166 N GLY A 19 39.924 8.553 10.023 1.00 16.24 N
ATOM 167 CA GLY A 19 41.301 8.984 10.158 1.00 17.63 C
ATOM 168 C GLY A 19 41.419 10.261 10.954 1.00 19.07 C
ATOM 169 O GLY A 19 40.453 10.732 11.553 1.00 17.89 O
ATOM 170 N GLN A 20 42.619 10.820 10.957 1.00 19.74 N
ATOM 171 CA GLN A 20 42.900 12.013 11.718 1.00 22.48 C
ATOM 172 CB GLN A 20 43.690 11.647 12.962 1.00 22.59 C
ATOM 173 CG GLN A 20 43.383 12.482 14.147 1.00 24.13 C
ATOM 174 CD GLN A 20 44.105 12.007 15.379 1.00 25.46 C
ATOM 175 OE1 GLN A 20 44.754 10.957 15.357 1.00 24.94 O
ATOM 176 NE2 GLN A 20 43.991 12.767 16.463 1.00 21.28 N
ATOM 177 C GLN A 20 43.685 12.993 10.861 1.00 22.99 C
ATOM 178 O GLN A 20 44.700 12.633 10.274 1.00 23.83 O
ATOM 179 N ARG A 21 43.183 14.219 10.776 1.00 23.42 N
ATOM 180 CA ARG A 21 43.845 15.313 10.077 1.00 23.88 C
ATOM 181 CB ARG A 21 42.967 16.553 10.124 1.00 24.74 C
ATOM 182 CG ARG A 21 41.779 16.542 9.241 1.00 26.74 C
ATOM 183 CD ARG A 21 41.469 17.905 8.687 1.00 27.27 C
ATOM 184 NE ARG A 21 41.400 18.948 9.710 1.00 25.25 N
ATOM 185 CZ ARG A 21 40.567 19.985 9.647 1.00 26.17 C
ATOM 186 NH1 ARG A 21 39.725 20.092 8.626 1.00 26.20 N
ATOM 187 NH2 ARG A 21 40.560 20.907 10.599 1.00 25.01 N
ATOM 188 C ARG A 21 45.172 15.704 10.713 1.00 22.80 C
ATOM 189 O ARG A 21 45.459 15.338 11.848 1.00 22.16 O
ATOM 190 N ALA A 22 45.940 16.519 9.992 1.00 22.55 N
ATOM 191 CA ALA A 22 47.201 17.073 10.487 1.00 21.67 C
ATOM 192 CB ALA A 22 47.795 17.999 9.447 1.00 21.73 C
ATOM 193 C ALA A 22 47.063 17.814 11.821 1.00 21.38 C
ATOM 194 O ALA A 22 48.012 17.860 12.597 1.00 22.26 O
ATOM 195 N ASP A 23 45.893 18.402 12.075 1.00 20.31 N
ATOM 196 CA ASP A 23 45.659 19.138 13.325 1.00 20.32 C
ATOM 197 CB ASP A 23 44.842 20.416 13.070 1.00 19.40 C
ATOM 198 CG ASP A 23 43.409 20.132 12.621 1.00 20.05 C
ATOM 199 OD1 ASP A 23 43.144 19.021 12.134 1.00 20.56 O
ATOM 200 OD2 ASP A 23 42.489 20.976 12.697 1.00 18.54 O
ATOM 201 C ASP A 23 44.988 18.290 14.421 1.00 20.31 C
ATOM 202 O ASP A 23 44.560 18.810 15.449 1.00 20.41 O
ATOM 203 N GLY A 24 44.906 16.986 14.194 1.00 20.18 N
ATOM 204 CA GLY A 24 44.327 16.087 15.177 1.00 20.62 C
ATOM 205 C GLY A 24 42.812 15.954 15.127 1.00 20.03 C
ATOM 206 O GLY A 24 42.256 15.098 15.812 1.00 20.80 O
ATOM 207 N TYR A 25 42.135 16.787 14.334 1.00 19.41 N
ATOM 208 CA TYR A 25 40.699 16.596 14.100 1.00 19.24 C
ATOM 209 CB TYR A 25 40.102 17.744 13.284 1.00 20.25 C
ATOM 210 CG TYR A 25 39.331 18.771 14.090 1.00 23.19 C
ATOM 211 CD1 TYR A 25 39.996 19.678 14.908 1.00 24.86 C
ATOM 212 CE1 TYR A 25 39.303 20.632 15.640 1.00 29.85 C
ATOM 213 CZ TYR A 25 37.925 20.700 15.558 1.00 30.07 C
ATOM 214 OH TYR A 25 37.259 21.663 16.296 1.00 33.81 O
ATOM 215 CE2 TYR A 25 37.228 19.819 14.743 1.00 28.40 C
ATOM 216 CD2 TYR A 25 37.938 18.862 14.002 1.00 27.34 C
ATOM 217 C TYR A 25 40.480 15.286 13.366 1.00 18.49 C
ATOM 218 O TYR A 25 41.335 14.850 12.598 1.00 17.75 O
ATOM 219 N HIS A 26 39.326 14.666 13.586 1.00 17.90 N
ATOM 220 CA HIS A 26 39.049 13.355 13.009 1.00 17.38 C
ATOM 221 CB HIS A 26 38.430 12.425 14.052 1.00 16.42 C
ATOM 222 CG HIS A 26 39.373 12.042 15.149 1.00 18.28 C
ATOM 223 ND1 HIS A 26 39.736 12.910 16.154 1.00 16.16 N
ATOM 224 CE1 HIS A 26 40.586 12.309 16.967 1.00 19.38 C
ATOM 225 NE2 HIS A 26 40.778 11.078 16.530 1.00 18.32 N
ATOM 226 CD2 HIS 26 40.038 10.888 15.391 1.00 19.07 C
ATOM 227 C HIS A 26 38.132 13.462 11.805 1.00 17.31 C
ATOM 228 O HIS A 26 37.104 14.159 11.855 1.00 16.45 O
ATOM 229 N THR A 27 38.494 12.762 10.729 1.00 15.67 N
ATOM 230 CA THR A 27 37.618 12.676 9.579 1.00 15.05 C
ATOM 231 CB THR A 27 38.396 12.388 8.266 1.00 15.64 C
ATOM 232 OG1 THR A 27 39.204 11.209 8.415 1.00 14.50 O
ATOM 233 CG2 THR A 27 39.406 13.507 7.991 1.00 12.58 C
ATOM 234 C THR A 27 36.569 11.612 9.855 1.00 15.63 C
ATOM 235 0 THR A 27 36.846 10.611 10.531 1.00 16.64 O
ATOM 236 N LEU A 28 35.365 11.853 9.342 1.00 14.75 N
ATOM 237 CA LEU A 28 34.162 11.155 9.761 1.00 13.54 C
ATOM 238 CB LEU A 28 33.266 12.076 10.604 1.00 14.70 C
ATOM 239 CG LEU A 28 33.809 12.815 11.814 1.00 16.98 C
ATOM 240 CD1 LEU A 28 32.695 13.568 12.508 1.00 18.89 C
ATOM 241 CD2 LEU A 28 34.449 11.816 12.753 1.00 22.05 C
ATOM 242 C LEU A 28 33.364 10.755 8.555 1.00 11.52 C
ATOM 243 O LEU A 28 33.457 11.394 7.519 1.00 9.59 O
ATOM 244 N GLN A 29 32.555 9.711 8.705 1.00 9.66 N
ATOM 245 CA GLN A 29 31.400 9.515 7.851 1.00 8.62 C
ATOM 246 CB GLN A 29 31.598 8.343 6.893 1.00 9.15 C
ATOM 247 CG GLN A 29 32.686 8.574 5.854 1.00 8.85 C
ATOM 248 CD GLN A 29 32.665 7.547 4.744 1.00 9.91 C
ATOM 249 OE1 GLN A 29 32.754 6.354 5.001 1.00 9.93 O
ATOM 250 NE2 GLN A 29 32.571 8.008 3.511 1.00 12.34 N
ATOM 251 C GLN A 29 30.222 9.279 8.778 1.00 8.61 C
ATOM 252 O GLN A 29 30.247 8.368 9.600 1.00 8.60 O
ATOM 253 N THR A 30 29.202 10.124 8.677 1.00 8.68 N
ATOM 254 CA THR A 30 28.102 10.053 9.621 1.00 9.60 C
ATOM 255 CB THR A 30 28.446 10.891 10.910 1.00 10.62 C
ATOM 256 OG1 THR A 30 27.437 10.691 11.904 1.00 8.74 O
ATOM 257 CG2 THR A 30 28.429 12.395 10.641 1.00 9.95 C
ATOM 258 C THR A 30 26.771 10.460 8.981 1.00 10.50 C
ATOM 259 O THR A 30 26.740 11.116 7.936 1.00 10.42 O
ATOM 260 N LEU A 31 25.680 10.008 9.583 1.00 10.24 N
ATOM 261 CA LEU A 31 24.355 10.277 9.076 1.00 9.82 C
ATOM 262 CB LEU A 31 23.705 8.970 8.605 1.00 9.62 C
ATOM 263 CG LEU A 31 22.243 8.964 8.175 1.00 11.05 C
ATOM 264 CD1 LEU A 31 22.028 9.858 6.966 1.00 9.40 C
ATOM 265 CD2 LEU A 31 21.753 7.499 7.909 1.00 11.54 C
ATOM 266 C LEU A 31 23.501 10.947 10.153 1.00 9.73 C
ATOM 267 O LEU A 31 23.323 10.402 11.251 1.00 8.79 O
ATOM 268 N PHE A 32 22.973 12.124 9.819 1.00 8.95 N
ATOM 269 CA PHE A 32 22.118 12.896 10.707 1.00 9.46 C
ATOM 270 CB PHE A 32 22.396 14.378 10.535 1.00 9.98 C
ATOM 271 CG PHE A 32 23.685 14.822 11.100 1.00 12.35 C
ATOM 272 CD1 PHE A 32 24.839 14.801 10.325 1.00 11.71 C
ATOM 273 CE1 PHE A 32 26.043 15.224 10.849 1.00 11.35 C
ATOM 274 CZ PHE A 32 26.103 15.683 12.140 1.00 12.26 C
ATOM 275 CE2 PHE A 32 24.957 15.715 12.922 1.00 12.58 C
ATOM 276 CD2 PHE A 32 23.756 15.295 12.399 1.00 12.10 C
ATOM 277 C PHE A 32 20.653 12.683 10.380 1.00 9.61 C
ATOM 278 O PHE A 32 20.270 12.673 9.210 1.00 9.37 O
ATOM 279 N GLN A 33 19.839 12.544 11.413 1.00 8.15 N
ATOM 280 CA GLN A 33 18.402 12.624 11.287 1.00 8.16 C
ATOM 281 CB GLN A 33 17.787 11.225 11.297 1.00 7.74 C
ATOM 282 CG GLN A 33 16.265 11.181 11.074 1.00 6.62 C
ATOM 283 CD GLN A 33 15.762 9.762 10.974 1.00 7.00 C
ATOM 284 OE1 GLN A 33 15.684 9.068 11.973 1.00 7.98 O
ATOM 285 NE2 GLN A 33 15.459 9.313 9.753 1.00 8.97 N
ATOM 286 C GLN A 33 17.888 13.450 12.462 1.00 8.41 C
ATOM 287 O GLN A 33 18.439 13.388 13.565 1.00 8.01 O
ATOM 288 N PHE A 34 16.832 14.217 12.240 1.00 8.12 N
ATOM 289 CA PHE A 34 16.280 15.054 13.299 1.00 8.10 C
ATOM 290 CB PHE A 34 15.574 16.260 12.680 1.00 8.24 C
ATOM 291 CG PHE A 34 16.453 17.042 11.731 1.00 5.05 C
ATOM 292 CD1 PHE A 34 16.267 16.954 10.356 1.00 4.78 C
ATOM 293 CE1 PHE A 34 17.086 17.648 9.484 1.00 6.05 C
ATOM 294 CZ PHE A 34 18.124 18.428 9.979 1.00 7.87 C
ATOM 295 CE2 PHE A 34 18.328 18.524 11.351 1.00 8.08 C
ATOM 296 CD2 PHE A 34 17.490 17.828 12.222 1.00 8.65 C
ATOM 297 C PHE A 34 15.322 14.261 14.170 1.00 9.29 C
ATOM 298 O PHE A 34 14.748 13.280 13.712 1.00 8.72 O
ATOM 299 N LEU A 35 15.152 14.687 15.423 1.00 7.38 N
ATOM 300 CA LEU A 35 14.046 14.199 16.230 1.00 8.42 C
ATOM 301 CB LEU A 35 14.504 13.849 17.669 1.00 6.88 C
ATOM 302 CG LEU A 35 15.555 12.745 17.777 1.00 7.17 C
ATOM 303 CD1 LEU A 35 15.948 12.485 19.236 1.00 8.97 C
ATOM 304 CD2 LEU A 35 15.041 11.477 17.131 1.00 8.95 C
ATOM 305 C LEU A 35 12.954 15.246 16.272 1.00 9.31 C
ATOM 306 O LEU A 35 13.237 16.457 16.340 1.00 7.47 O
ATOM 307 N ASP A 36 11.710 14.782 16.253 1.00 9.53 N
ATOM 308 CA ASP A 36 10.561 15.666 16.430 1.00 11.15 C
ATOM 309 CB ASP A 36 9.312 15.051 15.787 1.00 12.27 C
ATOM 310 CG ASP A 36 8.201 16.065 15.597 1.00 15.28 C
ATOM 311 OD1 ASP A 36 7.079 15.651 15.246 1.00 20.80 O
ATOM 312 OD2 ASP A 36 8.363 17.296 15.786 1.00 17.62 O
ATOM 313 C ASP A 36 10.332 15.974 17.926 1.00 11.87 C
ATOM 314 O ASP A 36 9.269 15.674 18.500 1.00 10.83 O
ATOM 315 N TYR A 37 11.337 16.604 18.528 1.00 11.23 N
ATOM 316 CA TYR A 37 11.446 16.793 19.963 1.00 10.89 C
ATOM 317 CB TYR A 37 11.703 15.454 20.663 1.00 10.35 C
ATOM 318 CG TYRA 37 11.862 15.516 22.183 1.0014.62 C
ATOM 319 CD1TYRA 37 10.816 15.139 23.037 1.0017.99 C
ATOM 320 CE1 TYRA 37 10.972 15.17524.422 1.0019.63 C
ATOM 321 CZ TYRA 37 12.183 15.585 24.957 1.0021.49 C
ATOM 322 OH TYRA 37 12.372 15.629 26.322 1.0024.90 O
ATOM 323 CE2TYRA 37 13.228 15.938 24.127 1.0018.28 C
ATOM 324 CD2 TYR A 37 13.065 15.895 22.759 1.0013.57 C
ATOM 325 C TYRA 37 12.630 17.719 20.187 1.0010.62 C
ATOM 326 O TYRA 37 13.694 17.507 19.602 1.0010.24 O
ATOM 327 N GLYA 38 12.486 18.702 21.065 1.0010.51 N
ATOM 328 CA GLYA 38 13.639 19.480 21.470 1.0010.08 C
ATOM 329 C GLYA 38 13.243 20.700 22.245 1.0011.23 C
ATOM 330 O GLYA 38 12.22020.709 22.946 1.0010.61 O
ATOM 331 N ASP A 39 14.052 21.746 22.121 1.0010.41 N
ATOM 332 CA ASP A 39 13.793 22.978 22.825 1.00 9.76 C
ATOM 333 CB ASP A 39 15.08923.77523.039 1.00 9.66 C
ATOM 334 CG ASP A 39 16.173 22.95423.684 1.0011.07 C
ATOM 335 OD1ASPA 39 15.84922.12224.568 1.00 9.83 O
ATOM 336 OD2ASPA 39 17.37223.07223.370 1.0010.85 O
ATOM 337 C ASP A 39 12.853 23.829 22.024 1.00 9.86 C
ATOM 338 O ASP A 39 12.60223.579 20.840 1.00 9.27 O
ATOM 339 N THRA 40 12.343 24.854 22.677 1.0010.04 N
ATOM 340 CAATHRA 40 11.537 25.873 22.039 0.5010.08 C
ATOM 341 CABTHRA 40 11.61425.87221.951 0.5011.16 C
ATOM 342 CBATHRA 40 10.110 25.800 22.610 0.5010.43 C
ATOM 343 CBBTHRA 40 10.07325.75522.1830.5011.87 C
ATOM 344 OG1ATHRA 40 9.445 24.644 22.076 0.50 5.80 O
ATOM 345 OG1BTHRA 40 9.380 26.53021.196 0.5013.84 O
ATOM 346 CG2ATHR 40 9.251 26.97722.134 0.50 9.44 C
ATOM 347 CG2BTHRA 40 9.651 26.399 23.480 0.5010.55 C
ATOM 348 C THRA 40 12.179 27.236 22.308 1.0011.30 C
ATOM 349 O THRA 40 12.489 27.542 23.467 1.0012.17 O
ATOM 350 N ILEA 41 12.393 28.035 21.266 1.0010.97 N
ATOM 351 CA ILEA 41 13.00529.341 21.423 1.0010.14 C
ATOM 352 CB ILEA 41 14.274 29.443 20.528 1.00 9.84 C
ATOM 353 CG1 ILEA 41 15.380 28.530 21.094 1.00 9.73 C
ATOM 354 CD1 ILEA 41 16.652 28.470 20.251 1.0012.76 C
ATOM 355 CG2ILEA 41 14.749 30.899 20.393 1.00 8.57 C
ATOM 356 C ILEA 41 11.994 30.439 21.108 1.0010.46 C
ATOM 357 O ILEA 41 11.356 30.420 20.061 1.0011.08 O
ATOM 358 N SER A 42 11.836 31.383 22.026 1.00 10.51 N
ATOM 359 CA SER A 42 10.909 32.490 21.804 1.00 11.03 C
ATOM 360 CB SER A 42 9.942 32.653 22.982 1.00 11.18 C
ATOM 361 OG SER A 42 9.153 31.493 23.158 1.00 12.54 O
ATOM 362 C SER A 42 11.679 33.767 21.582 1.00 10.68 C
ATOM 363 O SER A 42 12.683 34.021 22.258 1.00 10.07 O
ATOM 364 N ILE A 43 11.226 34.560 20.617 1.00 10.39 N
ATOM 365 CA ILE A 43 11.925 35.791 20.255 1.00 11.07 C
ATOM 366 CB ILE A 43 12.630 35.649 18.876 1.00 10.62 C
ATOM 367 CG1 ILE A 43 13.779 34.640 18.949 1.00 12.06 C
ATOM 368 CD1 ILE A 43 14.284 34.218 17.596 1.00 10.97 C
ATOM 369 CG2 ILE A 43 13.157 36.998 18.388 1.00 8.93 C
ATOM 370 C ILE A 43 10.960 36.971 20.236 1.00 11.30 C
ATOM 371 O ILE A 43 9.878 36.876 19.665 1.00 11.72 O
ATOM 372 N GLU A 44 11.361 38.072 20.866 1.00 11.94 N
ATOM 373 CA GLU A 44 10.684 39.348 20.700 1.00 13.40 C
ATOM 374 CB GLU A 44 10.118 39.827 22.038 1.00 13.97 C
ATOM 375 CG GLU A 44 9.227 41.059 21.936 1.00 20.51 C
ATOM 376 CD GLU A 44 8.752 41.550 23.300 1.00 28.67 C
ATOM 377 OE1 GLU A 44 8.624 40.721 24.227 1.00 31.16 O
ATOM 378 OE2 GLU A 44 8.510 42.767 23.447 1.00 32.52 O
ATOM 379 C GLU A 44 11.681 40.357 20.152 1.00 13.50 C
ATOM 380 O GLU A 44 12.742 40.551 20.742 1.00 12.80 O
ATOM 381 N LEU A 45 11.345 41.000 19.033 1.00 12.98 N
ATOM 382 CA LEU A 45 12.265 41.950 18.394 1.00 13.07 C
ATOM 383 CB LEU A 45 11.775 42.334 16.988 1.00 12.96 C
ATOM 384 CG LEU A 45 11.806 41.234 15.928 1.00 15.56 C
ATOM 385 CD1 LEU A 45 11.584 41.820 14.540 1.00 18.37 C
ATOM 386 CD2 LEU A 45 13.121 40.448 15.992 1.00 15.97 C
ATOM 387 C LEU A 45 12.462 43.202 19.231 1.00 13.10 C
ATOM 388 O LEU A 45 11.560 43.615 19.958 1.00 11.85 O
ATOM 389 N ARG A 46 13.664 43.771 19.138 1.00 13.50 N
ATOM 390 CA ARG A 46 14.007 45.038 19.762 1.00 13.33 C
ATOM 391 CB ARG A 46 15.246 44.899 20.647 1.00 13.57 C
ATOM 392 CG ARG A 46 15.128 43.968 21.849 1.00 11.64 C
ATOM 393 CD ARG A 46 16.333 44.058 22.780 1.00 11.85 C
ATOM 394 NE ARG A 46 16.401 45.354 23.466 1.00 11.90 N
ATOM 395 CZ ARG A 46 15.861 45.598 24.655 1.00 13.71 C
ATOM 396 NH1 ARG A 46 15.216 44.635 25.309 1.00 11.15 N
ATOM 397 NH2 ARG A 46 15.960 46.807 25.195 1.00 13.44 N
ATOM 398 C ARG A 46 14.317 46.046 18.669 1.00 14.28 C
ATOM 399 O ARG A 46 14.595 45.651 17.531 1.00 13.64 O
ATOM 400 N ASP A 47 14.313 47.339 19.009 1.00 15.20 N
ATOM 401 CA ASP A 47 14.687 48.378 18.034 1.00 16.94 C
ATOM 402 CB ASP A 47 13.493 49.308 17.705 1.00 18.40 C
ATOM 403 CG ASP A 47 12.981 50.086 18.909 1.00 23.28 C
ATOM 404 OD1 ASP A 47 11.877 50.660 18.790 1.00 33.18 O
ATOM 405 OD2 ASP A 47 13.580 50.198 20.002 1.00 27.26 O
ATOM 406 C ASP A 47 15.927 49.179 18.455 1.00 16.38 C
ATOM 407 O ASP A 47 16.243 50.204 17.850 1.00 16.17 O
ATOM 408 N ASP A 48 16.631 48.694 19.471 1.00 15.89 N
ATOM 409 CA ASP A 48 17.800 49.389 20.002 1.00 16.19 C
ATOM 410 CB ASP A 48 17.639 49.643 21.511 1.00 15.99 C
ATOM 411 CG ASP A 48 17.564 48.365 22.324 1.00 18.43 C
ATOM 412 OD1 ASP A 48 17.521 47.253 21.737 1.00 16.56 O
ATOM 413 OD2 ASP A 48 17.541 48.381 23.575 1.00 20.60 O
ATOM 414 C ASP A 48 19.102 48.637 19.718 1.00 16.01 C
ATOM 415 O ASP A 48 20.151 48.957 20.280 1.00 15.48 O
ATOM 416 N GLY A 49 19.015 47.616 18.870 1.00 15.85 N
ATOM 417 CA GLY A 49 20.187 46.876 18.438 1.00 15.27 C
ATOM 418 C GLY A 49 20.811 45.972 19.479 1.00 15.39 C
ATOM 419 O GLY A 49 21.906 45.469 19.269 1.00 15.33 O
ATOM 420 N ASP A 50 20.116 45.765 20.599 1.00 15.61 N
ATOM 421 CA ASP A 50 20.602 44.898 21.670 1.00 15.70 C
ATOM 422 CB ASP A 50 20.005 45.356 22.999 1.00 17.33 C
ATOM 423 CG ASP A 50 20.955 45.182 24.164 1.00 22.37 C
ATOM 424 OD1 ASP A 50 22.053 44.612 23.972 1.00 26.32 O
ATOM 425 OD2 ASP A 50 20.672 45.572 25.317 1.00 25.49 O
ATOM 426 C ASP A 50 20.250 43.420 21.427 1.00 14.53 C
ATOM 427 O ASP A 50 19.219 43.117 20.825 1.00 13.39 O
ATOM 428 N ILE A 51 21.100 42.509 21.904 1.00 12.86 N
ATOM 429 CA ILE A 51 20.746 41.091 21.996 1.00 12.44 C
ATOM 430 CB ILE A 51 21.795 40.197 21.269 1.00 12.31 C
ATOM 431 CG1 ILE A 51 21.881 40.522 19.774 1.00 13.21 C
ATOM 432 CD1 ILE A 51 20.564 40.419 19.017 1.00 15.11 C
ATOM 433 CG2 ILE A 51 21.497 38.710 21.487 1.00 12.35 C
ATOM 434 C ILE A 51 20.655 40.707 23.476 1.00 12.58 C
ATOM 435 O ILE A 51 21.649 40.804 24.191 1.00 11.75 O
ATOM 436 N ARG A 52 19.466 40.303 23.942 1.00 11.82 N
ATOM 437 CA ARG A 52 19.289 39.886 25.344 1.00 11.41 C
ATOM 438 CB ARG A 52 18.395 40.875 26.104 1.00 11.29 C
ATOM 439 CG ARG A 52 18.816 42.350 25.975 1.00 12.12 C
ATOM 440 CD ARG A 52 17.985 43.320 26.807 1.00 12.99 C
ATOM 441 NE ARG A 52 18.578 44.659 26.767 1.00 15.23 N
ATOM 442 CZ ARG A 52 18.226 45.670 27.553 1.00 17.33 C
ATOM 443 NH1 ARG A 52 17.257 45.520 28.446 1.00 15.98 N
ATOM 444 NH2 ARG A 52 18.844 46.839 27.437 1.00 16.07 N
ATOM 445 C ARG A 52 18.704 38.474 25.485 1.00 11.45 C
ATOM 446 O ARG A 52 17.518 38.245 25.224 1.00 12.07 O
ATOM 447 N LEU A 53 19.535 37.533 25.902 1.00 10.56 N
ATOM 448 CA LEU A 53 19.046 36.215 26.265 1.00 10.87 C
ATOM 449 CB LEU A 53 20.172 35.187 26.183 1.00 9.16 C
ATOM 450 CG LEU A 53 19.839 33.804 26.728 1.00 9.29 C
ATOM 451 CD1 LEU A 53 18.759 33.114 25.885 1.00 6.50 C
ATOM 452 CD2 LEU A 53 21.119 32.953 26.808 1.00 10.65 C
ATOM 453 C LEU A 53 18.461 36.275 27.676 1.00 11.01 C
ATOM 454 O LEU A 53 19.190 36.459 28.645 1.00 10.17 O
ATOM 455 N LEU A 54 17.144 36.117 27.787 1.00 11.91 N
ATOM 456 CA LEU A 54 16.447 36.363 29.056 1.00 12.87 C
ATOM 457 CB LEU A 54 14.978 36.735 28.803 1.00 12.32 C
ATOM 458 CG LEU A 54 14.658 37.945 27.932 1.00 12.64 C
ATOM 459 CD1 LEU A 54 13.134 38.220 27.934 1.00 12.81 C
ATOM 460 CD2 LEU A 54 15.444 39.175 28.373 1.00 12.60 C
ATOM 461 C LEU A 54 16.508 35.181 30.013 1.00 14.00 C
ATOM 462 O LEU A 54 16.263 35.329 31.214 1.00 14.69 O
ATOM 463 N THR A 55 16.841 34.014 29.481 1.00 15.33 N
ATOM 464 CA ATHR A 55 16.842 32.811 30.303 0.50 16.02 C
ATOM 465 CA BTHR A 55 16.835 32.757 30.232 0.50 16.35 C
ATOM 466 CB ATHR A 55 15.802 31.779 29.801 0.50 16.25 C
ATOM 467 CB BTHR A 55 15.988 31.705 29.493 0.50 16.37 C
ATOM 468 OG1ATHR A 55 15.747 31.798 28.375 0.50 12.99 O
ATOM 469 OG1 BTHR A 55 14.749 32.286 29.076 0.50 15.29 O
ATOM 470 CG2ATHR A 55 14.383 32.191 30.222 0.50 16.45 C
ATOM 471 CG2BTHR A 55 15.568 30.581 30.444 0.50 17.13 C
ATOM 472 C THR A 55 18.235 32.201 30.372 1.00 16.80 C
ATOM 473 O THR A 55 18.836 31.837 29.366 1.00 17.48 O
ATOM 474 N PRO A 56 18.751 32.095 31.592 1.00 17.76 N
ATOM 475 CA PRO A 56 20.050 31.459 31.788 1.00 18.93 C
ATOM 476 CB PRO A 56 20.372 31.724 33.267 1.00 19.53 C
ATOM 477 CG PRO A 56 19.306 32.680 33.766 1.00 17.58 C
ATOM 478 CD PRO A 56 18.138 32.531 32.863 1.00 17.97 C
ATOM 479 C PRO A 56 19.934 29.963 31.511 1.00 20.98 C
ATOM 480 O PRO A 56 18.981 29.317 31.965 1.00 20.78 O
ATOM 481 N VAL A 57 20.870 29.452 30.716 1.00 22.33 N
ATOM 482 CA VAL A 57 21.013 28.034 30.464 1.00 24.37 C
ATOM 483 CB VAL A 57 21.398 27.755 28.983 1.00 24.62 C
ATOM 484 CG1 VAL A 57 21.903 26.317 28.798 1.00 25.05 C
ATOM 485 CG2 VAL A 57 20.229 28.018 28.071 1.00 23.15 C
ATOM 486 C VAL A 57 22.096 27.544 31.395 1.00 25.56 C
ATOM 487 O VAL A 57 23.173 28.120 31.438 1.00 25.87 O
ATOM 488 N GLU A 58 21.801 26.492 32.152 1.00 27.87 N
ATOM 489 CA GLU A 58 22.647 26.063 33.276 1.00 29.53 C
ATOM 490 CB GLU A 58 22.214 24.665 33.758 1.00 30.95 C
ATOM 491 CG GLU A 58 23.109 24.055 34.830 1.00 36.15 C
ATOM 492 CD GLU A 58 22.589 24.308 36.234 1.00 43.29 C
ATOM 493 OE1 GLU A 58 22.325 23.320 36.957 1.00 45.55 O
ATOM 494 OE2 GLU A 58 22.439 25.496 36.614 1.00 44.93 O
ATOM 495 C GLU A 58 24.154 26.075 32.984 1.00 28.02 C
ATOM 496 O GLU A 58 24.638 25.364 32.103 1.00 27.97 O
ATOM 497 N GLY A 59 24.876 26.906 33.734 1.00 27.46 N
ATOM 498 CA GLY A 59 26.332 26.925 33.709 1.00 26.02 C
ATOM 499 C GLY A 59 26.952 27.599 32.495 1.00 25.45 C
ATOM 500 O GLY A 59 28.166 27.501 32.265 1.00 26.41 O
ATOM 501 N VAL A 60 26.128 28.277 31.703 1.00 22.41 N
ATOM 502 CA VAL A 60 26.620 28.927 30.501 1.00 19.84 C
ATOM 503 CB VAL A 60 25.938 28.366 29.244 1.00 19.70 C
ATOM 504 CG1 VAL A 60 26.456 29.064 28.005 1.00 19.37 C
ATOM 505 CG2 VAL A 60 26.166 26.855 29.157 1.00 20.15 C
ATOM 506 C VAL A 60 26.405 30.432 30.584 1.00 18.53 C
ATOM 507 O VAL A 60 25.269 30.896 30.712 1.00 17.95 O
ATOM 508 N GLU A 61 27.506 31.181 30.513 1.00 17.40 N
ATOM 509 CA GLU A 61 27.466 32.636 30.571 1.00 16.88 C
ATOM 510 CB GLU A 61 28.876 33.206 30.769 1.00 17.45 C
ATOM 511 CG GLU A 61 29.578 32.697 32.024 1.00 21.19 C
ATOM 512 CD GLU A 61 30.989 33.254 32.184 1.00 25.96 C
ATOM 513 OE1 GLU A 61 31.357 34.203 31.452 1.00 26.35 O
ATOM 514 OE2 GLU A 61 31.728 32.745 33.054 1.00 30.51 O
ATOM 515 C GLU A 61 26.843 33.208 29.311 1.00 15.37 C
ATOM 516 O GLU A 61 26.954 32.619 28.238 1.00 14.93 O
ATOM 517 N HIS A 62 26.208 34.369 29.454 1.00 13.87 N
ATOM 518 CA HIS A 62 25.456 35.018 28.381 1.00 13.06 C
ATOM 519 CB HIS A 62 25.061 36.427 28.823 1.00 11.83 C
ATOM 520 CG HIS A 62 24.072 37.108 27.925 1.00 10.95 C
ATOM 521 ND1 HIS A 62 24.453 37.866 26.839 1.00 9.63 N
ATOM 522 CE1 HIS A 62 23.381 38.385 26.264 1.00 7.88 C
ATOM 523 NE2 HIS A 62 22.318 38.002 26.945 1.00 7.68 N
ATOM 524 CD2 HIS A 62 22.724 37.222 28.005 1.00 8.69 C
ATOM 525 C HIS A 62 26.232 35.048 27.051 1.00 13.47 C
ATOM 526 O HIS A 62 25.739 34.558 26.035 1.00 11.69 O
ATOM 527 N GLU A 63 27.458 35.576 27.072 1.00 13.30 N
ATOM 528 CA GLU A 63 28.272 35.682 25.844 1.00 13.70 C
ATOM 529 CB GLU A 63 29.419 36.693 26.031 1.00 13.64 C
ATOM 530 CG GLU A 63 28.937 38.136 26.179 1.00 13.60 C
ATOM 531 CD GLU A 63 27.890 38.508 25.147 1.00 15.59 C
ATOM 532 OE1 GLU A 63 28.205 38.456 23.934 1.00 14.88 O
ATOM 533 OE2 GLU A 63 26.750 38.854 25.540 1.00 17.02 O
ATOM 534 C GLU A 63 28.824 34.338 25.336 1.00 13.97 C
ATOM 535 O GLU A 63 29.265 34.234 24.186 1.00 14.62 O
ATOM 536 N ASP A 64 28.788 33.315 26.180 1.00 13.64 N
ATOM 537 CA ASP A 64 29.238 31.988 25.770 1.00 13.66 C
ATOM 538 CB ASP A 64 29.812 31.228 26.951 1.00 14.75 C
ATOM 539 CG ASP A 64 31.160 31.759 27.387 1.00 18.32 C
ATOM 540 OD1 ASP A 64 31.857 32.401 26.566 1.00 19.97 O
ATOM 541 OD2 ASP A 64 31.596 31.578 28.539 1.00 22.75 O
ATOM 542 C ASP A 64 28.105 31.170 25.170 1.00 12.77 C
ATOM 543 0 ASP A 64 28.344 30.173 24.493 1.00 11.84 O
ATOM 544 N ASN A 65 26.872 31.583 25.443 1.00 12.34 N
ATOM 545 CA ASN A 65 25.715 30.853 24.965 1.00 11.49 C
ATOM 546 CB ASN A 65 24.434 31.349 25.650 1.00 11.67 C
ATOM 547 CG ASN A 65 23.286 30.401 25.460 1.00 11.65 C
ATOM 548 OD1 ASN A 65 22.917 30.088 24.333 1.00 9.81 O
ATOM 549 ND2 SN 65 22.724 29.914 26.558 1.00 10.74 N
ATOM 550 C ASN A 65 25.605 30.928 23.446 1.00 11.13 C
ATOM 551 O ASN A 65 25.689 32.007 22.860 1.00 11.48 O
ATOM 552 N LEU A 66 25.438 29.770 22.815 1.00 9.96 N
ATOM 553 CA LEU A 66 25.407 29.686 21.356 1.00 10.24 C
ATOM 554 CB LEU A 66 25.358 28.223 20.911 1.00 10.56 C
ATOM 555 CG LEU A 66 26.733 27.537 20.944 1.00 12.77 C
ATOM 556 CD1 LEU A 66 26.583 26.029 21.048 1.00 15.45 C
ATOM 557 CD2 LEU A 66 27.550 27.911 19.716 1.00 16.24 C
ATOM 558 C LEU A 66 24.247 30.488 20.743 1.00 8.57 C
ATOM 559 O LEU A 66 24.320 30.908 19.611 1.00 8.49 O
ATOM 560 N ILE A 67 23.189 30.694 21.513 1.00 8.62 N
ATOM 561 CA ILE A 67 22.097 31.577 21.102 1.00 8.66 C
ATOM 562 CB ILE A 67 20.993 31.588 22.177 1.00 8.68 C
ATOM 563 CG1 ILE A 67 20.247 30.246 22.184 1.00 8.46 C
ATOM 564 CD1 ILE A 67 19.398 30.001 23.453 1.00 11.72 C
ATOM 565 CG2 1LE A 67 20.034 32.779 21.963 1.00 9.80 C
ATOM 566 C ILE A 67 22.605 33.000 20.833 1.00 8.91 C
ATOM 567 O ILE A 67 22.334 33.580 19.785 1.00 8.44 O
ATOM 568 N VAL A 68 23.365 33.537 21.783 1.00 7.67 N
ATOM 569 CA VAL A 68 23.911 34.882 21.683 1.00 8.19 C
ATOM 570 CB VAL A 68 24.397 35.388 23.087 1.00 8.48 C
ATOM 571 CG1 VAL A 68 25.109 36.741 22.998 1.00 8.56 C
ATOM 572 CG2 VAL A 68 23.217 35.448 24.069 1.00 7.65 C
ATOM 573 C VAL A 68 25.031 34.952 20.627 1.00 7.80 C
ATOM 574 O VAL A 68 25.076 35.885 19.829 1.00 7.62 O
ATOM 575 N ARG A 69 25.906 33.953 20.591 1.00 8.32 N
ATOM 576 CA ARG A 69 26.982 33.949 19.572 1.00 9.77 C
ATOM 577 CB ARG A 69 27.980 32.803 19.802 1.00 8.71 C
ATOM 578 CG ARG A 69 28.726 32.896 21.135 1.00 13.16 C
ATOM 579 CD ARG A 69 29.663 31.726 21.410 1.00 16.98 C
ATOM 580 NE ARG A 69 30.610 31.541 20.317 1.00 21.25 N
ATOM 581 CZ ARG A 69 31.176 30.380 19.995 1.00 27.55 C
ATOM 582 NH1 ARG A 69 30.899 29.281 20.688 1.00 25.08 N
ATOM 583 NH2 ARG A 69 32.029 30.320 18.975 1.00 29.15 N
ATOM 584 C ARG A 69 26.422 33.903 18.144 1.00 9.62 C
ATOM 585 O ARG A 69 26.894 34.623 17.268 1.00 9.66 O
ATOM 586 N ALA A 70 25.391 33.087 17.926 1.00 9.50 N
ATOM 587 CA ALA A 70 24.714 33.048 16.611 1.00 9.84 C
ATOM 588 CB ALA 70 23.651 31.950 16.582 1.00 9.63 C
ATOM 589 C ALA A 70 24.093 34.389 16.221 1.00 9.10 C
ATOM 590 O ALA A 70 24.265 34.856 15.095 1.00 9.27 O
ATOM 591 N ALA A 71 23.360 34.994 17.149 1.00 9.58 N
ATOM 592 CA ALA A 71 22.718 36.281 16.907 1.00 9.67 C
ATOM 593 CB ALA A 71 21.887 36.698 18.129 1.00 8.67 C
ATOM 594 C ALA A 71 23.748 37.370 16.547 1.00 10.29 C
ATOM 595 O ALA A 71 23.550 38.128 15.592 1.00 10.60 O
ATOM 596 N ARG A 72 24.849 37.431 17.298 1.00 10.80 N
ATOM 597 CA ARG A 72 25.898 38.426 17.026 1.00 10.54 C
ATOM 598 CB ARG A 72 26.935 38.468 18.156 1.00 11.12 C
ATOM 599 CG ARG A 72 26.359 38.897 19.519 1.00 11.77 C
ATOM 600 CD ARG A 72 27.400 39.475 20.497 1.00 16.70 C
ATOM 601 NE ARG A 72 26.834 39.736 21.827 1.00 15.73 N
ATOM 602 CZ ARG A 72 26.001 40.735 22.109 1.00 16.15 C
ATOM 603 NH1 ARG A 72 25.628 41.594 21.159 1.00 12.25 N
ATOM 604 NH2 ARG A 72 25.542 40.881 23.349 1.00 15.93 N
ATOM 605 C ARG A 72 26.594 38.175 15.686 1.00 9.63 C
ATOM 606 O ARG A 72 26.921 39.118 14.960 1.00 9.47 O
ATOM 607 N LEU A 73 26.779 36.903 15.347 1.00 9.88 N
ATOM 608 CA LEU A 73 27.462 36.531 14.112 1.00 10.30 C
ATOM 609 CB LEU A 73 27.800 35.026 14.105 1.00 10.60 C
ATOM 610 CG LEU A 73 28.421 34.413 12.832 1.00 12.79 C
ATOM 611 CD1 LEU A 73 29.748 35.076 12.449 1.00 14.09 C
ATOM 612 CD2 LEU A 73 28.599 32.893 12.984 1.00 12.88 C
ATOM 613 C LEU A 73 26.623 36.918 12.900 1.00 10.54 C
ATOM 614 O LEU A 73 27.147 37.470 11.921 1.00 11.04 O
ATOM 615 N LEU A 74 25.317 36.655 12.978 1.00 9.94 N
ATOM 616 CA LEU A 74 24.397 37.052 11.917 1.00 10.25 C
ATOM 617 CB LEU A 74 22.981 36.543 12.190 1.00 8.30 C
ATOM 618 CG LEU A 74 21.896 37.031 11.233 1.00 10.55 C
ATOM 619 CD1 LEU A 74 22.213 36.704 9.758 1.00 8.54 C
ATOM 620 CD2 LEU A 74 20.551 36.431 11.644 1.00 12.52 C
ATOM 621 C LEU A 74 24.376 38.562 11.769 1.00 11.17 C
ATOM 622 O LEU A 74 24.446 39.082 10.657 1.00 11.39 O
ATOM 623 N MSE A 75 24.266 39.264 12.891 1.00 11.62 N
ATOM 624 CA MSE A 75 24.241 40.723 12.871 1.00 14.01 C
ATOM 625 CB MSE A 75 24.236 41.270 14.293 1.00 14.57 C
ATOM 626 CG MSE 75 22.887 41.400 14.868 1.00 21.97 C
ATOM 627 SE MSE A 75 22.984 42.037 16.702 1.00 44.24 SE
ATOM 628 CE MSE A 75 24.047 43.512 16.475 1.00 25.56 C
ATOM 629 C MSE A 75 25.450 41.289 12.137 1.00 13.15 C
ATOM 630 O MSE A 75 25.315 42.139 11.255 1.00 12.93 O
ATOM 631 N LYS A 76 26.629 40.814 12.517 1.00 13.75 N
ATOM 632 CA LYS A 76 27.885 41.278 11.917 1.00 15.63 C
ATOM 633 CB LYS A 76 29.078 40.674 12.676 1.00 16.45 C
ATOM 634 CG LYS A 76 30.467 41.131 12.218 1.00 21.92 C
ATOM 635 CD LYS A 76 31.496 40.941 13.341 1.00 30.83 C
ATOM 636 CE LYS A 76 32.922 41.275 12.881 1.00 36.89 C
ATOM 637 NZ LYS A 76 33.241 42.747 12.968 1.00 39.84 N
ATOM 638 C LYS A 76 27.946 40.954 10.409 1.00 15.69 C
ATOM 639 0 LYS A 76 28.264 41.821 9.590 1.00 15.89 O
ATOM 640 N THR A 77 27.596 39.725 10.040 1.00 14.98 N
ATOM 641 CA THR A 77 27.688 39.307 8.641 1.00 15.65 C
ATOM 642 CB THR A 77 27.483 37.791 8.499 1.00 15.55 C
ATOM 643 OG1 THR A 77 28.395 37.111 9.368 1.00 17.30 O
ATOM 644 CG2 THR A 77 27.903 37.331 7.108 1.00 18.14 C
ATOM 645 C THR A 77 26.703 40.069 7.762 1.00 15.60 C
ATOM 646 O THR A 77 27.094 40.584 6.712 1.00 15.05 O
ATOM 647 N ALA A 78 25.437 40.152 8.196 1.00 14.18 N
ATOM 648 CA ALA A 78 24.432 40.921 7.458 1.00 15.22 C
ATOM 649 CB ALA A 78 23.053 40.783 8.096 1.00 14.46 C
ATOM 650 C ALA A 78 24.818 42.403 7.325 1.00 15.80 C
ATOM 651 O ALA A 78 24.677 42.981 6.248 1.00 16.52 O
ATOM 652 N ALA A 79 25.309 43.008 8.411 1.00 16.20 N
ATOM 653 CA ALA A 79 25.747 44.407 8.365 1.00 17.50 C
ATOM 654 CB ALA A 79 26.156 44.898 9.748 1.00 17.39 C
ATOM 655 C ALA A 79 26.885 44.622 7.356 1.00 18.17 C
ATOM 656 O ALA A 79 26.951 45.666 6.725 1.00 17.94 O
ATOM 657 N ASP A 80 27.762 43.623 7.209 1.00 19.69 N
ATOM 658 CA ASP A 80 28.870 43.665 6.236 1.00 21.01 C
ATOM 659 CB ASP A 80 29.725 42.395 6.321 1.00 21.08 C
ATOM 660 CG ASP A 80 30.676 42.408 7.498 1.00 25.02 C
ATOM 661 OD1 ASP A 80 30.832 43.474 8.136 1.00 27.70 O
ATOM 662 OD2 ASP A 80 31.310 41.395 7.865 1.00 30.11 O
ATOM 663 C ASP A 80 28.412 43.870 4.787 1.00 21.31 C
ATOM 664 0 ASP A 80 29.147 44.430 3.976 1.00 22.21 O
ATOM 665 N SER A 81 27.209 43.411 4.455 1.00 21.02 N
ATOM 666 CA SER 81 26.700 43.601 3.095 1.00 21.15 C
ATOM 667 CB SER A 81 26.297 42.262 2.465 1.00 21.58 C
ATOM 668 OG SER A 81 25.270 41.633 3.214 1.00 23.64 O
ATOM 669 C SER A 81 25.534 44.588 3.063 1.00 20.48 C
ATOM 670 O SER A 81 24.851 44.720 2.043 1.00 20.73 O
ATOM 671 N GLY A 82 25.320 45.287 4.177 1.00 18.86 N
ATOM 672 CA GLY A 82 24.236 46.246 4.276 1.00 18.45 C
ATOM 673 C GLY A 82 22.864 45.596 4.280 1.00 18.47 C
ATOM 674 0 GLY A 82 21.883 46.190 3.818 1.00 18.13 O
ATOM 675 N ARG A 83 22.776 44.379 4.811 1.00 17.72 N
ATOM 676 CA ARG A 83 21.487 43.673 4.806 1.00 17.88 C
ATOM 677 CB ARG A 83 21.652 42.278 4.193 1.00 17.97 C
ATOM 678 CG ARG A 83 21.725 42.331 2.656 1.00 19.83 C
ATOM 679 CD ARG A 83 21.825 40.987 1.981 1.00 23.80 C
ATOM 680 NE ARG A 83 23.083 40.315 2.290 1.00 28.01 N
ATOM 681 CZ ARG A 83 23.405 39.090 1.868 1.00 30.99 C
ATOM 682 NH1 ARG A 83 22.550 38.394 1.120 1.00 29.10 N
ATOM 683 NH2 ARG A 83 24.577 38.554 2.206 1.00 27.98 N
ATOM 684 C ARG A 83 20.800 43.596 6.177 1.00 17.56 C
ATOM 685 O ARG A 83 19.777 42.909 6.327 1.00 18.11 O
ATOM 686 N LEU A 84 21.339 44.319 7.158 1.00 16.17 N
ATOM 687 CA LEU A 84 20.722 44.409 8.479 1.00 16.01 C
ATOM 688 CB LEU A 84 21.762 44.134 9.581 1.00 15.85 C
ATOM 689 CG LEU A 84 21.230 44.002 11.014 1.00 14.91 C
ATOM 690 CD1 LEU A 84 20.504 42.685 11.170 1.00 13.95 C
ATOM 691 CD2 LEU A 84 22.344 44.107 12.024 1.00 15.78 C
ATOM 692 C LEU A 84 20.092 45.786 8.690 1.00 17.23 C
ATOM 693 O LEU A 84 20.790 46.791 8.658 1.00 16.98 O
ATOM 694 N PRO A 85 18.771 45.838 8.879 1.00 18.40 N
ATOM 695 CA PRO A 85 18.086 47.105 9.165 1.00 18.29 C
ATOM 696 CB PRO A 85 16.624 46.679 9.333 1.00 19.42 C
ATOM 697 CG PRO A 85 16.523 45.422 8.527 1.00 19.72 C
ATOM 698 CD PRO A 85 17.830 44.708 8.796 1.00 18.42 C
ATOM 699 C PRO A 85 18.594 47.755 10.451 1.00 18.54 C
ATOM 700 O PRO A 85 18.916 47.065 11.430 1.00 16.84 O
ATOM 701 N THR A 86 18.695 49.079 10.426 1.00 18.18 N
ATOM 702 CA THR A 86 19.132 49.845 11.577 1.00 18.81 C
ATOM 703 CB THR A 86 18.976 51.346 11.287 1.00 19.27 C
ATOM 704 OG1 THR A 86 19.610 51.650 10.035 1.00 23.16 O
ATOM 705 CG2 THR A 86 19.766 52.170 12.290 1.00 21.98 C
ATOM 706 C THR A 86 18.316 49.468 12.800 1.00 17.86 C
ATOM 707 O THR A 86 17.092 49.369 12.725 1.00 16.89 O
ATOM 708 N GLY A 87 18.996 49.251 13.920 1.00 17.30 N
ATOM 709 CA GLY A 87 18.305 49.034 15.181 1.00 17.48 C
ATOM 710 C GLY A 87 17.868 47.601 15.436 1.00 16.52 C
ATOM 711 O GLY A 87 17.356 47.301 16.520 1.00 16.40 O
ATOM 712 N SER A 88 18.085 46.712 14.461 1.00 14.86 N
ATOM 713 CA SER A 88 17.731 45.300 14.629 1.00 13.35 C
ATOM 714 CB SER A 88 18.217 44.471 13.434 1.00 13.69 C
ATOM 715 OG SER A 88 17.521 44.817 12.245 1.00 9.85 O
ATOM 716 C SER A 88 18.300 44.732 15.928 1.00 12.59 C
ATOM 717 O SER A 88 19.501 44.836 16.188 1.00 13.16 O
ATOM 718 N GLY A 89 17.429 44.150 16.745 1.00 11.50 N
ATOM 719 CA GLY A 89 17.837 43.493 17.978 1.00 9.90 C
ATOM 720 C GLY A 89 16.792 42.479 18.408 1.00 8.81 C
ATOM 721 O GLY A 89 15.806 42.268 17.696 1.00 8.99 O
ATOM 722 N ALA A 90 16.987 41.863 19.567 1.00 8.71 N
ATOM 723 CA ALA A 90 16.089 40.790 20.014 1.00 10.20 C
ATOM 724 CB ALA A 90 16.286 39.518 19.150 1.00 9.44 C
ATOM 725 C ALA A 90 16.243 40.435 21.488 1.00 11.08 C
ATOM 726 O ALA A 90 17.360 40.348 22.001 1.00 10.54 O
ATOM 727 N ASN A 91 15.104 40.233 22.153 1.00 10.51 N
ATOM 728 CA ASN A 91 15.033 39.458 23.376 1.00 11.01 C
ATOM 729 CB ASN A 91 13.888 39.929 24.267 1.00 10.60 C
ATOM 730 CG ASN A 91 14.215 41.194 25.023 1.00 13.45 C
ATOM 731 OD1 ASN A 91 15.312 41.747 24.903 1.00 12.92 O
ATOM 732 ND2 ASN A 91 13.252 41.668 25.816 1.00 15.13 N
ATOM 733 C ASN A 91 14.785 38.004 23.010 1.00 10.32 C
ATOM 734 O ASN A 91 13.926 37.715 22.189 1.00 9.69 O
ATOM 735 N ILE A 92 15.544 37.098 23.608 1.00 10.24 N
ATOM 736 CA ILE A 92 15.413 35.688 23.291 1.00 9.75 C
ATOM 737 CB ILE A 92 16.653 35.186 22.517 1.00 9.71 C
ATOM 738 CG1 ILE A 92 16.927 36.076 21.299 1.00 9.81 C
ATOM 739 CD1 ILE A 92 18.290 35.803 20.627 1.00 10.43 C
ATOM 740 CG2 ILE A 92 16.475 33.738 22.072 1.00 8.32 C
ATOM 741 C ILE A 92 15.241 34.922 24.578 1.00 9.71 C
ATOM 742 O ILE A 92 15.901 35.211 25.565 1.00 9.84 O
ATOM 743 N SER A 93 14.337 33.949 24.575 1.00 10.21 N
ATOM 744 CA SER A 93 14.219 33.052 25.708 1.00 10.31 C
ATOM 745 CB SER A 93 12.995 33.407 26.563 1.00 10.70 C
ATOM 746 OG SER A 93 11.791 33.130 25 877 1.00 15.88 O
ATOM 747 C SER A 93 14.143 31.628 25.200 1.00 10.38 C
ATOM 748 O SER A 93 13.803 31.394 24.049 1.00 9.61 O
ATOM 749 N ILE A 94 14.467 30.675 26.059 1.00 9.92 N
ATOM 750 CA ILE A 94 14.428 29.284 25.652 1.00 10.40 C
ATOM 751 CB ILE A 94 15.865 28.769 25.322 1.00 9.12 C
ATOM 752 CG1 ILE A 94 15.837 27.285 24.933 1.00 10.69 C
ATOM 753 CD1 ILE A 94 17.117 26.811 24.208 1.00 8.94 C
ATOM 754 CG2 ILE A 94 16.830 29.030 26.486 1.00 9.04 C
ATOM 755 C ILE A 94 13.755 28.422 26.715 1.00 11.67 C
ATOM 756 O ILE A 94 13.972 28.611 27.912 1.00 10.76 O
ATOM 757 N ASP A 95 12.900 27.513 26.253 1.00 12.69 N
ATOM 758 CA ASP A 95 12.420 26.411 27.056 1.00 13.85 C
ATOM 759 CB ASP A 95 10.960 26.084 26.710 1.00 13.93 C
ATOM 760 CG ASP A 95 10.324 25.064 27.672 1.00 21.41 C
ATOM 761 OD1 ASP A 95 10.935 24.730 28.713 1.00 23.13 O
ATOM 762 OD2 ASP A 95 9.197 24.554 27.467 1.00 28.27 O
ATOM 763 C ASP A 95 13.340 25.237 26.768 1.00 13.71 C
ATOM 764 O ASP A 95 13.241 24.602 25.726 1.00 12.48 O
ATOM 765 N LYS A 96 14.260 24.983 27.692 1.00 14.76 N
ATOM 766 CA LYS A 96 15.326 24.016 27.478 1.00 16.28 C
ATOM 767 CB LYS A 96 16.609 24.491 28.172 1.00 16.27 C
ATOM 768 CG LYS A 96 17.822 23.604 27.920 1.00 20.26 C
ATOM 769 CD LYS A 96 18.757 24.242 26.895 1.00 21.96 C
ATOM 770 CE LYS A 96 19.379 23.201 26.032 1.00 20.79 C
ATOM 771 NZ LYS A 96 19.733 23.733 24.694 1.00 15.43 N
ATOM 772 C LYS A 96 14.921 22.640 27.989 1.00 16.84 C
ATOM 773 O LYS A 96 14.885 22.414 29.204 1.00 17.18 O
ATOM 774 N ARG A 97 14.603 21.736 27.059 1.00 17.74 N
ATOM 775 CA ARG A 97 14.255 20.342 27.380 1.00 19.16 C
ATOM 776 CB ARG A 97 13.039 19.872 26.566 1.00 20.09 C
ATOM 777 CG ARG A 97 11.866 20.851 26.541 1.00 25.08 C
ATOM 778 CD AARG A 97 10.499 20.181 26.523 0.50 28.56 C
ATOM 779 CD BARG A 97 10.523 20.225 26.863 0.50 29.31 C
ATOM 780 NE AARG A 97 10.070 19.782 27.865 0.50 31.32 N
ATOM 781 NE BARG A 97 10.219 19.074 26.012 0.50 31.61 N
ATOM 782 CZ AARG A 97 8.821 19.465 28.197 0.50 31.94 C
ATOM 783 CZ BARG A 97 9.260 19.055 25.091 0.50 33.02 C
ATOM 784 NH1AARG A 97 7.854 19.493 27.286 0.50 30.41 N
ATOM 785 NH1 BARG A 97 8.510 20.130 24.885 0.50 33.32 N
ATOM 786 NH2AARG A 97 8.537 19.118 29.448 0.50 33.07 N
ATOM 787 NH2BARG A 97 9.052 17.961 24.368 0.50 31.32 N
ATOM 788 C ARG A 97 15.417 19.377 27.125 1.00 19.28 C
ATOM 789 O ARG A 97 15.487 18.312 27.737 1.00 19.52 O
ATOM 790 N LEU A 98 16.303 19.739 26.199 1.00 18.06 N
ATOM 791 CA LEU A 98 17.426 18.880 25.819 1.00 17.95 C
ATOM 792 CB LEU A 98 17.968 19.262 24.424 1.00 16.12 C
ATOM 793 CG LEU A 98 17.044 19.035 23.217 1.00 13.64 C
ATOM 794 CD1 LEU A 98 17.695 19.491 21.885 1.00 9.05 C
ATOM 795 CD2 LEU A 98 16.606 17.579 23.136 1.00 9.19 C
ATOM 796 C LEU A 98 18.537 18.949 26.857 1.00 19.76 C
ATOM 797 O LEU A 98 18.775 19.998 27.446 1.00 19.55 O
ATOM 798 N PRO A 99 19.211 17.825 27.089 1.00 21.64 N
ATOM 799 CA PRO A 99 20.370 17.805 27.980 1.00 22.86 C
ATOM 800 CB PRO A 99 20.763 16.322 28.011 1.00 22.46 C
ATOM 801 CG PRO A 99 20.234 15.775 26.740 1.00 23.50 C
ATOM 802 CD PRO A 99 18.923 16.493 26.532 1.00 21.77 C
ATOM 803 C PRO A 99 21.503 18.641 27.405 1.00 24.02 C
ATOM 804 O PRO A 99 21.443 19.084 26.250 *1.00 24.17 O
ATOM 805 N MSE A 100 22.516 18.874 28.218 1.00 24.58 N
ATOM 806 CA MSE A 100 23.702 19.566 27.766 1.00 27.20 C
ATOM 807 CB MSE A 100 24.446 20.168 28.956 1.00 28.23 C
ATOM 808 CG MSE A 100 23.570 21.048 29.856 1.00 35.98 C
ATOM 809 SE MSE A 100 22.932 22.677 28.929 1.00 57.93 SE
ATOM 810 CE MSE A 100 24.564 23.604 28.857 1.00 48.25 C
ATOM 811 C MSE A 100 24.584 18.579 27.015 1.00 26.44 C
ATOM 812 0 MSE A 100 24.981 17.544 27.563 1.00 26.70 O
ATOM 813 N GLY A 101 24.867 18.888 25.754 1.00 25.05 N
ATOM 814 CA GLY A 101 25.625 17.987 24.908 1.00 23.63 C
ATOM 815 C GLY A 101 24.934 16.644 24.711 1.00 22.59 C
ATOM 816 O GLY A 101 23.859 16.551 24.076 1.00 22.94 O
ATOM 817 N GLY A 102 25.558 15.595 25.246 1.00 19.82 N
ATOM 818 CA GLY A 102 24.963 14.276 25.242 1.00 17.25 C
ATOM 819 C GLY A 102 24.925 13.610 23.873 1.00 15.54 C
ATOM 820 O GLY A 102 24.541 12.461 23.767 1.00 14.21 O
ATOM 821 N GLY A 103 25.340 14.316 22.826 1.00 13.42 N
ATOM 822 CA GLY A 103 25.270 13.754 21.486 1.00 12.74 C
ATOM 823 C GLY A 103 23.967 14.037 20.756 1.00 11.16 C
ATOM 824 0 GLY A 103 23.715 13.475 19.678 1.00 12.23 O
ATOM 825 N LEU A 104 23.152 14.927 21.325 1.00 10.03 N
ATOM 826 CA LEU A 104 21.879 15.332 20.720 1.00 9.14 C
ATOM 827 CB LEU A 104 20.791 15.457 21.793 1.00 8.32 C
ATOM 828 CG LEU A 104 20.416 14.109 22.438 1.00 9.71 C
ATOM 829 CD1 LEU A 104 19.284 14.276 23.434 1.00 8.08 C
ATOM 830 CD2 LEU A 104 20.045 13.095 21.367 1.00 6.86 C
ATOM 831 C LEU A 104 21.976 16.638 19.950 1.00 9.18 C
ATOM 832 O LEU A 104 21.024 17.022 19.256 1.00 9.41 O
ATOM 833 N GLY A 105 23.096 17.346 20.108 1.00 7.68 N
ATOM 834 CA GLY A 105 23.357 18.553 19.331 1.00 9.16 C
ATOM 835 C GLY A 105 22.535 19.763 19.734 1.00 8.82 C
ATOM 836 O GLY 105 22.312 20.650 18.917 1.00 8.19 O
ATOM 837 N GLY A 106 22.097 19.804 20.994 1.00 9.59 N
ATOM 838 CA GLY A 106 21.154 20.823 21.453 1.00 9.44 C
ATOM 839 C GLY A 106 21.663 22.251 21.293 1.00 10.19 C
ATOM 840 O GLY A 106 20.923 23.121 20.861 1.00 10.15 O
ATOM 841 N GLY A 107 22.931 22.486 21.637 1.00 9.86 N
ATOM 842 CA GLY A 107 23.516 23.814 21.502 1.00 9.30 C
ATOM 843 C GLY A 107 23.634 24.270 20.053 1.00 9.04 C
ATOM 844 O GLY A 107 23.321 25.424 19.719 1.00 8.72 O
ATOM 845 N SER A 108 24.102 23.363 19.197 1.00 7.48 N
ATOM 846 CA SER A 108 24.170 23.606 17.760 1.00 8.08 C
ATOM 847 CB SER A 108 24.810 22.417 17.054 1.00 8.12 C
ATOM 848 OG SER A 108 26.174 22.318 17.419 1.00 10.80 O
ATOM 849 C SER A 108 22.801 23.869 17.152 1.00 7.20 C
ATOM 850 O SER A 108 22.675 24.689 16.245 1.00 7.34 O
ATOM 851 N SER A 109 21.789 23.154 17.636 1.00 6.11 N
ATOM 852 CA SER A 109 20.421 23.357 17.178 1.00 6.67 C
ATOM 853 CB SER A 109 19.495 22.266 17.725 1.00 5.68 C
ATOM 854 OG SER A 109 18.206 22.319 17.090 1.00 6.49 O
ATOM 855 C SER A 109 19.913 24.730 17.602 1.00 6.15 C
ATOM 856 O SER A 109 19.280 25.422 16.811 1.00 7.20 O
ATOM 857 N ASN A 110 20.179 25.109 18.858 1.00 6.34 N
ATOM 858 CA ASN A 110 19.840 26.458 19.339 1.00 6.06 C
ATOM 859 CB ASN A 110 20.276 26.717 20.799 1.00 5.81 C
ATOM 860 CG ASN A 110 19.607 25.793 21.825 1.00 8.78 C
ATOM 861 OD1 ASN A 110 20.071 25.711 22.969 1.00 8.43 O
ATOM 862 ND2 ASN A 110 18.534 25.106 21.437 1.00 6.43 N
ATOM 863 C ASN A 110 20.459 27.509 18.434 1.00 5.95 C
ATOM 864 O ASN A 110 19.776 28.426 18.013 1.00 6.66 O
ATOM 865 N ALA A 111 21.752 27.364 18.116 1.00 5.49 N
ATOM 866 CA AL 111 22.424 28.316 17.219 1.00 5.57 C
ATOM 867 CB ALA A 111 23.925 27.993 17.091 1.00 6.24 C
ATOM 868 C ALA A 111 21.766 28.390 15.833 1.00 6.62 C
ATOM 869 O ALAA 111 21.519 29.477 15.322 1.00 7.12 . O
ATOM 870 N ALA A 112 21.455 27.234 15.248 1.00 6.72 N
ATOM 871 CA ALA A 112 20.857 27.194 13.914 1.00 5.78 C
ATOM 872 CB ALA A 112 20.787 25.766 13.408 1.00 6.37 C
ATOM 873 C ALA A 112 19.472 27.820 13.917 1.00 6.59 C
ATOM 874 O ALA A 112 19.130 28.600 13.023 1.00 6.61 O
ATOM 875 N THR A 113 18.675 27.486 14.929 1.00 6.26 N
ATOM 876 CA THR A 113 17.327 28.025 15.025 1.00 5.66 C
ATOM 877 CB THR A 113 16.609 27.426 16.240 1.00 5.92 C
ATOM 878 OG1 THR A 113 16.226 26.078 15.942 1.00 5.87 O
ATOM 879 CG2 THR A 113 15.272 28.146 16.499 1.00 5.41 C
ATOM 880 C THR A 113 17.359 29.552 15.117 1.00 5.45 C
ATOM 881 O THR A 113 16.568 30.236 14.477 1.00 4.89 O
ATOM 882 N VAL A 114 18.288 30.067 15.915 1.00 5.65 N
ATOM 883 CA VAL A 114 18.489 31.517 16.056 1.00 6.05 C
ATOM 884 CB VAL A 114 19.516 31.827 17.185 1.00 6.29 C
ATOM 885 CG1 VAL A 114 19.907 33.306 17.218 1.00 5.58 C
ATOM 886 CG2 VAL A 114 18.939 31.413 18.520 1.00 7.01 C
ATOM 887 C VAL A 114 18.890 32.175 14.728 1.00 7.02 C
ATOM 888 O VAL A 114 18.308 33.206 14.343 1.00 5.86 O
ATOM 889 N LEU A 115 19.861 31.573 14.023 1.00 7.12 N
ATOM 890 CA LEU A 115 20.273 32.078 12.703 1.00 7.07 C
ATOM 891 CB LEU A 115 21.347 31.188 12.071 1.00 7.03 C
ATOM 892 CG LEU A 115 22.721 31.205 12.727 1.00 6.38 C
ATOM 893 CD1 LEU A 115 23.634 30.167 12.062 1.00 8.90 C
ATOM 894 CD2 LEU A 115 23.345 32.606 12.673 1.00 7.72 C
ATOM 895 C LEU A 115 19.097 32.161 11.756 1.00 7.47 C
ATOM 896 O LEU A 115 18.860 33.209 11.144 1.00 6.87 O
ATOM 897 N VAL A 116 18.343 31.067 11.648 1.00 7.01 N
ATOM 898 CA VAL A 116 17.220 31.016 10.704 1.00 8.76 C
ATOM 899 CB VAL A 116 16.705 29.565 10.528 1.00 8.57 C
ATOM 900 CG1 VAL A 116 15.392 29.538 9.751 1.00 11.34 C
ATOM 901 CG2 VAL A 116 17.759 28.722 9.826 1.00 9.47 C
ATOM 902 C VAL A 116 16.092 31.984 11.127 1.00 8.50 C
ATOM 903 O VAL A 116 15.563 32.744 10.303 1.00 8.44 O
ATOM 904 N ALA A 117 15.768 31.987 12.417 1.00 8.81 N
ATOM 905 CA ALA A 117 14.674 32.815 12.927 1.00 8.96 C
ATOM 906 CB ALA A 117 14.387 32.482 14.366 1.00 9.05 C
ATOM 907 C ALA A 117 14.970 34.310 12.783 1.00 9.25 C
ATOM 908 O ALA A 117 14.152 35.049 12.248 1.00 9.39 O
ATOM 909 N LEU 118 16.142 34.746 13.246 1.00 8.72 N
ATOM 910 CA LEU A 118 16.499 36.165 13.140 1.00 8.72 C
ATOM 911 CB LEU A 118 17.720 36.494 14.007 1.00 7.92 C
ATOM 912 CG LEU A 118 17.486 36.366 15.523 1.00 8.50 C
ATOM 913 CD1 LEU A 118 18.752 36.706 16.276 1.00 8.29 C
ATOM 914 CD2 LEU A 118 16.335 37.239 16.013 1.00 9.04 C
ATOM 915 C LEU A 118 16.706 36.612 11.686 1.00 8.90 C
ATOM 916 O LEU A 118 16.284 37.713 11.313 1.00 10.56 O
ATOM 917 N ASN A 119 17.314 35.769 10.853 1.00 8.60 N
ATOM 918 CA ASN A 119 17.379 36.086 9.419 1.00 9.53 C
ATOM 919 CB ASN A 119 18.058 34.958 8.622 1.00 9.66 C
ATOM 920 CG ASN A 119 18.144 35.254 7.118 1.0011.41 C
ATOM 921 OD1ASNA119 18.732 36.253 6.701 1.0012.81 O
ATOM 922 ND2 ASN A 119 17.577 34.371 6.308 1.0010.55 N
ATOM 923 C ASN A 119 15.979 36.379 8.879 1.0010.14 C
ATOM 924 O ASN A 119 15.758 37.381 8.172 1.00 9.53 O
ATOM 925 N HIS A 120 15.023 35.528 9.253 1.0010.22 N
ATOM 926 CA HIS A 120 13.637 35.729 8.860 1.0011.46 C
ATOM 927 CB HIS A 120 12.777 34.513 9.225 1.0012.37 C
ATOM 928 CG HIS A 120 11.336 34.667 8.840 1.0016.99 C
ATOM 929 ND1 HIS A 120 10.86834.366 7.578 1.0020.61 N
ATOM 930 CE1 HIS A 120 9.570 34.607 7.524 1.0022.29 C
ATOM 931 NE2HISA120 9.180 35.061 8.701 1.0023.65 N
ATOM 932 CD2 HIS A 120 10.26635.107 9.543 1.0020.85 C
ATOM 933 C HIS A 120 13.026 36.989 9.481 1.0010.95 C
ATOM 934 O HIS A 120 12.445 37.812 8.779 1.0011.66 O
ATOM 935 N LEU A 121 13.156 37.133 10.795 1.0010.88 N
ATOM 936 CA LEUA121 12.48438.221 11.510 1.0011.15 C
ATOM 937 CB LEUA121 12.469 37.938 13.019 1.00 9.76 C
ATOM 938 CG LEU A 121 11.63536.725 13.450 1.0010.49 C
ATOM 939 CD1 LEUA121 11.976 36.312 14.880 1.00 8.55 C
ATOM 940 CD2LEUA121 10.134 37.027 13.303 1.0010.48 C
ATOM 941 C LEUA121 13.107 39.590 11.232 1.0011.90 C
ATOM 942 O LEUA121 12.400 40.592 11.163 1.0012.34 O
ATOM 943 N TRP A 122 14.42439.636 11.068 1.0012.69 N
ATOM 944 CA TRP A 122 15.08340.901 10.734 1.0013.83 C
ATOM 945 CB TRPA122 16.55240.874 11.156 1.0012.32 C
ATOM 946 CG TRP 122 16.77940.973 12.647 1.0012.29 C
ATOM 947 CD1 TRP A 122 15.93841.518 13.588 1.0011.02 C
ATOM 948 NE1TRPA122 16.51541.443 14.834 1 .00 9.81 N
ATOM 949 CE2TRPA122 17.741 40.844 14.719 1 00 7.66 C
ATOM 950 CD2TRPA122 17.93940.540 13.353 1 .00 8.45 C
ATOM 951 CE3TRPA122 19.138 39.922 12.969 1 00 9.28 C
ATOM 952 CZ3TRPA122 20.07339.623 13.940 1 0012.46 C
ATOM 953 CH2TRPA122 19.848 39.948 15.284 1 ,0011.47 C
ATOM 954 CZ2TRPA122 18.68240.548 15.691 1 00 8.12 C
ATOM 955 C TRP A 122 14.97941.229 9.240 1.0014.82 C
ATOM 956 0 TRP A 122 15.32742.333 8.819 1.0016.05 O
ATOM 957 N GLN A 123 14.50640.261 8.452 1.0015.71 N
ATOM 958 CA GLN A 123 14.344 40.399 6.990 1.00 16.53 C
ATOM 959 CB GLN A 123 13.292 41.470 6.633 1.00 17.89 C
ATOM 960 CG GLN A 123 11.963 41.304 7.380 1.00 22.58 C
ATOM 961 CD GLN A 123 10.826 42.085 6.743 1.00 30.58 C
ATOM 962 OE1 GLN A 123 10.849 43.320 6.719 1.00 30.95 O
ATOM 963 NE2 GLN A 123 9.828 41.368 6.223 1.00 33.95 N
ATOM 964 C GLN A 123 15.674 40.672 6.289 1.00 16.48 C
ATOM 965 0 GLN A 123 15.763 41.543 5.414 1.00 15.93 O
ATOM 966 N CYS A 124 16.709 39.931 6.688 1.00 15.32 N
ATOM 967 CA CYS A 124 18.047 40.103 6.119 1.00 14.46 C
ATOM 968 CB CYS A 124 19.111 39.446 7.006 1.00 14.17 C
ATOM 969 SG CYS A 124 19.227 40.163 8.659 1.00 14.34 S
ATOM 970 C CYS A 124 18.131 39.534 4.716 1.00 14.59 C
ATOM 971 O CYS A 124 18.921 40.003 3.888 1.00 14.56 O
ATOM 972 N GLY A 125 17.328 38.509 4.459 1.00 13.89 N
ATOM 973 CA GLY A 125 17.280 37.901 3.147 1.00 14.31 C
ATOM 974 C GLY A 125 18.499 37.063 2.805 1.00 14.31 C
ATOM 975 0 GLY A 125 18.794 36.861 1.630 1.00 14.02 O
ATOM 976 N LEU A 126 19.204 36.550 3.814 1.00 13.65 N
ATOM 977 CA LEU A 126 20.322 35.652 3.516 1.00 13.45 C
ATOM 978 CB LEU A 126 21.306 35.518 4.684 1.00 12.86 C
ATOM 979 CG LEU A 126 21.914 36.731 5.410 1.00 17.49 C
ATOM 980 CD1 LEU A 126 23.279 36.369 5.977 1.00 18.24 C
ATOM 981 CD2 LEU A 126 22.035 37.932 4.533 1.00 18.11 C
ATOM 982 C LEU A 126 19.781 34.281 3.129 1.00 13.83 C
ATOM 983 O LEU A 126 18.711 33.880 3.583 1.00 14.32 O
ATOM 984 N SER A 127 20.517 33.569 2.283 1.00 12.73 N
ATOM 985 CA SER A 127 20.117 32.237 1.878 1.00 13.00 C
ATOM 986 CB SER A 127 20.805 31.858 0.580 1.00 12.63 C
ATOM 987 OG SER A 127 22.200 31.741 0.799 1.00 11.89 O
ATOM 988 C SER A 127 20.499 31.240 2.965 1.00 13.11 C
ATOM 989 O SER A 127 21.354 31.536 3.815 1.00 12.81 O
ATOM 990 N MSE A 128 19.875 30.058 2.941 1.00 12.40 N
ATOM 991 CA MSE A 128 20.278 28.983 3.836 1.00 12.56 C
ATOM 992 CB MSE A 128 19.429 27.709 3.628 1.00 12.04 C
ATOM 993 CG MSE A 128 17.969 27.831 4.036 1.00 14.90 C
ATOM 994 SE MSE A 128 17.708 28.477 5.864 1.00 27.03 SE
ATOM 995 CE MSE A 128 17.153 30.350 5.383 1.00 21.83 C
ATOM 996 C MSE A 128 21.756 28.660 3.646 1.00 11.56 C
ATOM 997 O MSE A 128 22.437 28.317 4.601 1.00 10.55 O
ATOM 998 N ASP A 129 22.242 28.760 2.407 1.00 12.14 N
ATOM 999 CA ASP A 129 23.680 28.602 2.125 1.00 12.40 C
ATOM 1000 CB ASP A 129 23.973 28.822 0.639 1.00 13.29 C
ATOM 1001 CG ASP A 129 23.461 27.699 -0.241 1.00 15.25 C
ATOM 1002 OD1 ASP A 129 23.179 26.584 0.268 1.00 12.88 O
ATOM 1003 OD2 ASP A 129 23.329 27.852 -1.469 1.00 16.39 O
ATOM 1004 C ASP A 129 24.547 29.568 2.924 1.00 12.14 C
ATOM 1005 O ASP A 129 25.556 29.183 3.492 1.00 12.20 O
ATOM 1006 N GLU A 130 24.173 30.837 2.931 1.00 12.20 N
ATOM 1007 CA GLU A 130 24.949 31.839 3.666 1.00 12.88 C
ATOM 1008 CB GLU A 130 24.453 33.236 3.333 1.00 13.51 C
ATOM 1009 CG GLU A 130 24.653 33.619 1.872 1.00 16.69 C
ATOM 1010 CD GLU A 130 24.155 35.014 1.568 1.00 19.62 C
ATOM 1011 OE1 GLU A 130 24.990 35.944 1.550 1.00 22.79 O
ATOM 1012 OE2 GLU A 130 22.935 35.185 1.355 1.00 20.37 O
ATOM 1013 C GLU A 130 24.883 31.589 5.181 1.00 11.25 C
ATOM 1014 O GLU A 130 25.887 31.711 5.880 1.00 11.40 O
ATOM 1015 N LEU A 131 23.706 31.206 5.666 1.00 9.72 N
ATOM 1016 CA LEU A 131 23.519 30.906 7.091 1.00 9.43 C
ATOM 1017 CB LEU A 131 22.031 30.718 7.435 1.00 8.09 C
ATOM 1018 CG LEU A 131 21.088 31.924 7.264 1.00 10.54 C
ATOM 1019 CD1 LEU A 131 19.717 31.625 7.897 1.00 10.12 C
ATOM 1020 CD2 LEU A 131 21.672 33.203 7.848 1.00 6.36 C
ATOM 1021 C LEU A 131 24.312 29.678 7.514 1.00 9.64 C
ATOM 1022 O LEU A 131 24.884 29.651 8.600 1.00 9.27 O
ATOM 1023 N ALA A 132 24.339 28.653 6.659 1.00 10.16 N
ATOM 1024 CA ALA A 132 25.090 27.440 6.964 1.00 9.97 C
ATOM 1025 CB ALA A 132 24.714 26.287 5.995 1.00 9.11 C
ATOM 1026 C ALA A 132 26.583 27.712 6.924 1.00 10.70 C
ATOM 1027 O ALA A 132 27.334 27.145 7.706 1.00 11.03 O
ATOM 1028 N GLU A 133 27.012 28.600 6.024 1.00 11.23 N
ATOM 1029 CA GLU A 133 28.443 28.927 5.917 1.00 12.92 C
ATOM 1030 CB GLU A 133 28.705 29.804 4.687 1.00 13.54 C
ATOM 1031 CG GLU A 133 30.176 30.079 4.436 1.00 20.14 C
ATOM 1032 CD GLU A 133 30.400 31.108 3.344 1.00 27.92 C
ATOM 1033 OE1 GLU A 133 29.614 31.130 2.373 1.00 29.26 O
ATOM 1034 OE2 GLU A 133 31.364 31.898 3.456 1.00 33.70 O
ATOM 1035 C GLU A 133 28.970 29.605 7.195 1.00 12.38 C
ATOM 1036 O GLU 133 29.985 29.192 7.755 1.00 11.70 O
ATOM 1037 N MSE A 134 28.267 30.629 7.670 1.00 10.86 N
ATOM 1038 CA MSE A 134 28.645 31.251 8.941 1.00 12.09 C
ATOM 1039 CB MSE A 134 27.906 32.582 9.151 1.00 12.11 C
ATOM 1040 CG MSE A 134 26.513 32.447 9.719 1.00 16.35 C
ATOM 1041 SE MSE A 134 25.571 34.159 9.705 1.00 28.82 SE
ATOM 1042 CE MSE A 134 25.582 34.431 7.766 1.00 17.44 C
ATOM 1043 C MSE A 134 28.422 30.302 10.124 1.00 11.40 C
ATOM 1044 O MSE A 134 29.223 30.275 11.064 1.00 11.11 O
ATOM 1045 N GLY A 135 27.376 29.471 10.039 1.00 11.34 N
ATOM 1046 CA GLY A 135 27.039 28.562 11.116 1.00 10.30 C
ATOM 1047 C GLY A 135 28.133 27.553 11.399 1.00 10.88 C
ATOM 1048 O GLY A 135 28.350 27.175 12.549 1.00 10.70 O
ATOM 1049 N LEU A 136 28.842 27.136 10.349 1.00 11.09 N
ATOM 1050 CA LEU A 136 29.959 26.192 10.483 1.00 11.42 C
ATOM 1051 CB LEU A 136 30.623 25.964 9.121 1.00 11.11 C
ATOM 1052 CG LEU A 136 31.768 24.948 9.004 1.00 13.46 C
ATOM 1053 CD1 LEU A 136 31.363 23.556 9.521 1.00 12.68 C
ATOM 1054 CD2 LEU A 136 32.259 24.888 7.553 1.00 13.97 C
ATOM 1055 C LEU A 136 31.017 26.644 11.500 1.00 12.34 C
ATOM 1056 O LEU A 136 31.620 25.812 12.174 1.00 12.05 O
ATOM 1057 N THR A 137 31.236 27.954 11.612 1.00 12.68 N
ATOM 1058 CA THR A 137 32.245 28.470 12.548 1.00 14.40 C
ATOM 1059 CB THR A 137 32.547 29.978 12.313 1.00 14.10 C
ATOM 1060 OG1 THR A 137 31.384 30.764 12.627 1.00 16.19 O
ATOM 1061 CG2 THR A 137 32.808 30.264 10.839 1.00 15.06 C
ATOM 1062 C THR A 137 31.832 28.256 13.991 1.00 14.54 C
ATOM 1063 O THR A 137 32.662 28.354 14.888 1.00 15.73 O
ATOM 1064 N LEU A 138 30.549 27.962 14.212 1.00 14.34 N
ATOM 1065 CA LEU A 138 30.043 27.639 15.541 1.00 14.43 C
ATOM 1066 CB LEU A 138 28.648 28.246 15.745 1.00 14.50 C
ATOM 1067 CG LEU A 138 28.536 29.763 15.578 1.00 14.49 C
ATOM 1068 CD1 LEU A 138 27.098 30.198 15.732 1.00 16.56 C
ATOM 1069 CD2 LEU A 138 29.425 30.485 16.578 1.00 15.96 C
ATOM 1070 C LEU A 138 29.982 26.135 15.815 1.00 15.16 C
ATOM 1071 O LEU A 138 29.593 25.723 16.903 1.00 15.27 O
ATOM 1072 N GLY A 139 30.336 25.313 14.827 1.00 14.96 N
ATOM 1073 CA GLY A 139 30.342 23.869 15.029 1.00 13.89 C
ATOM 1074 C GLY A 139 29.823 23.116 13.819 1.00 13.71 C
ATOM 1075 O GLY A 139 28.918 23.590 13.142 1.00 12.95 O
ATOM 1076 N ALA A 140 30.388 21.934 13.555 1.00 12.68 N
ATOM 1077 CA ALA A 140 30.040 21.164 12.361 1.00 12.23 C
ATOM 1078 CB ALA A 140 30.962 19.937 12.223 1.00 13.73 C
ATOM 1079 C . ALA A 140 28.569 20.737 12.304 1.00 11.40 C
ATOM 1080 O ALA A 140 28.036 20.532 11.215 1.00 11.84 O
ATOM 1081 N ASP A 141 27.920 20.579 13.462 1.00 11.61 N
ATOM 1082 CA ASP A 141 26.486 20.217 13.493 1.00 11.09 C
ATOM 1083 CB ASP A 141 26.014 19.820 14.891 1.00 11.07 C
ATOM 1084 CG ASP A 141 26.568 18.478 15.369 1.00 16.20 C
ATOM 1085 OD1 ASP A 141 27.100 17.692 14.563 1.00 17.05 O
ATOM 1086 OD2 ASP A 141 26.497 18.133 16.569 1.00 19.64 O
ATOM 1087 C ASP A 141 25.587 21.358 13.014 1.00 9.57 C
ATOM 1088 O ASP A 141 24.493 21.123 12.516 1.00 9.07 O
ATOM 1089 N VAL A 142 26.034 22.597 13.194 1.00 8.25 N
ATOM 1090 CA VAL A 142 25.150 23.746 12.927 1.00 8.14 C
ATOM 1091 CB VAL A 142 25.809 25.090 13.337 1.00 7.74 C
ATOM 1092 CG1 VAL A 142 24.935 26.272 12.939 1.00 6.21 C
ATOM 1093 CG2 VAL A 142 26.078 25.095 14.832 1.00 7.43 C
ATOM 1094 C VAL A 142 24.604 23.794 11.472 1.00 7.72 C
ATOM 1095 O VAL A 142 23.388 23.955 11.292 1.00 8.61 O
ATOM 1096 N PRO A 143 25.460 23.639 10.447 1.00 7.58 N
ATOM 1097 CA PRO A 143 24.968 23.641 9.057 1.00 7.26 C
ATOM 1098 CB PRO A 143 26.231 23.340 8.234 1.00 8.55 C
ATOM 1099 CG PRO A 143 27.368 23.890 9.078 1.00 6.18 C
ATOM 1100 CD PRO A 143 26.931 23.495 10.495 1.00 6.84 C
ATOM 1101 C PRO A 143 23.877 22.587 8.771 1.00 7.98 C
ATOM 1102 O PRO A 143 23.007 22.856 7.951 1.00 7.23 O
ATOM 1103 N VAL A 144 23.930 21.428 9.431 1.00 7.26 N
ATOM 1104 CA VAL A 144 22.914 20.390 9.249 1.00 6.38 C
ATOM 1105 CB VAL A 144 23.278 19.102 10.014 1.00 7.44 C
ATOM 1106 CG1 VAL A 144 22.219 18.032 9.820 1.00 7.33 C
ATOM 1107 CG2 VAL A 144 24.647 18.584 9.564 1.00 7.12 C
ATOM 1108 C VAL A 144 21.558 20.909 9.710 1.00 6.51 C
ATOM 1109 O VAL A 144 20.553 20.799 8.996 1.00 6.94 O
ATOM 1110 N PHE 145 21.547 21.499 10.899 1.00 6.51 N
ATOM 1111 CA PHE A 145 20.341 22.101 11.453 1.00 7.82 C
ATOM 1112 CB PHE A 145 20.595 22.540 12.891 1.00 6.93 C
ATOM 1113 CG PHE A 145 20.590 21.415 13.879 1.00 7.11 C
ATOM 1114 CD1 PHE A 145 21.746 21.076 14.571 1.00 5.23 C
ATOM 1115 CE1 PHE A 145 21.745 20.036 15.500 1.00 6.12 C
ATOM 1116 CZ PHE A 145 20.584 19.332 15.735 1.00 5.84 C
ATOM 1117 CE2 PHE A 145 19.421 19.650 15.037 1.00 4.96 C
ATOM 1118 CD2 PHE A 145 19.423 20.691 14.119 1.00 6.97 C
ATOM 1119 C PHE A 145 19.866 23.295 10.622 1.00 7.58 C
ATOM 1120 O PHE A 145 18.663 23.472 10.421 1.00 8.22 O
ATOM 1121 N VAL A 146 20.808 24.125 10.164 1.00 7.64 N
ATOM 1122 CA VAL A 146 20.460 25.265 9.308 1.00 8.15 C
ATOM 1123 CB VAL A 146 21.680 26.140 8.946 1.00 8.97 C
ATOM 1124 CG1 VAL A 146 21.326 27.143 7.814 1.00 9.10 C
ATOM 1125 CG2 VAL A 146 22.214 26.887 10.173 1.00 6.87 C
ATOM 1126 C VAL A 146 19.791 24.800 8.013 1.00 9.25 C
ATOM 1127 O VAL A 146 18.777 25.364 7.610 1.00 8.97 O
ATOM 1128 N ARG A 147 20.352 23.767 7.375 1.00 8.49 N
ATOM 1129 CA ARG A 147 19.882 23.365 6.044 1.00 10.07 C
ATOM 1130 CB ARG A 147 20.978 22.608 5.275 1.00 10.61 C
ATOM 1131 CG ARG A 147 22.102 23.540 4.772 1.00 11.05 C
ATOM 1132 CD ARG A 147 23.353 22.824 4.288 1.00 11.20 C
ATOM 1133 NE ARG A 147 23.058 21.895 3.202 1.00 10.51 N
ATOM 1134 CZ ARG A 147 23.974 21.391 2.372 1.00 12.76 C
ATOM 1135 NH1 ARG A 147 25.253 21.738 2.489 1.00 13.32 N
ATOM 1136 NH2 ARG A 147 23.607 20.549 1.412 1.00 11.89 N ATOM 1137 C ARG A 147 18.574 22.573 6.111 1.00 9.21 C
ATOM 1138 O ARG A 147 17.790 22.593 5.177 1.00 9.60 O
ATOM 1139 N GLY A 148 18.350 21.891 7.225 1.00 8.61 N
ATOM 1140 CA GLY A 148 17.038 21.350 7.544 1.00 7.98 C
ATOM 1141 C GLY A 148 16.694 19.978 7.001 1.00 8.05 C
ATOM 1142 O GLY A 148 15.559 19.518 7.181 1.00 8.56 O
ATOM 1143 N HIS A 149 17.661 19.301 6.377 1.00 7.01 N
ATOM 1144 CA HIS A 149 17.399 17.991 5.777 1.00 7.69 C
ATOM 1145 CB HIS A 149 17.535 18.072 4.242 1.00 8.06 C
ATOM 1146 CG HIS A 149 16.450 18.872 3.593 1.00 10.72 C
ATOM 1147 ND1 HIS A 149 15.271 18.308 3.157 1.00 11.14 N
ATOM 1148 CE1 HIS A 149 14.493 19.252 2.656 1.00 12.51 C
ATOM 1149 NE2 HIS 149 15.117 20.411 2.775 1.00 12.37 N
ATOM 1150 CD2 HIS A 149 16.343 20.201 3.357 1.00 9.71 C
ATOM 1151 C HIS A 149 18.332 16.933 6.308 1.00 7.53 C
ATOM 1152 O HIS A 149 19.509 17.204 6.534 1.00 8.03 O
ATOM 1153 N ALA A 150 17.820 15.716 6.492 1.00 8.06 N
ATOM 1154 CA ALA A 150 18.678 14.585 6.868 1.00 7.91 C
ATOM 1155 CB ALA A 150 17.892 13.279 6.876 1.00 8.26 C
ATOM 1156 C ALA A 150 19.838 14.514 5.895 1.00 7.97 C
ATOM 1157 O ALA A 150 19.658 14.708 4.688 1.00 7.68 O
ATOM 1158 N ALAA 151 21.036 14.280 6.418 1.00 8.00 N
ATOM 1159 CA ALAA 151 22.244 14.497 5.637 1.00 8.08 C
ATOM 1160 CB ALAA 151 22.726 15.956 5.767 1.00 7.65 C
ATOM 1161 C ALA A 151 23.340 13.545 6.035 1.00 8.66 C
ATOM 1162 O ALAA 151 23.493 13.192 7.206 1.007.94 O
ATOM 1163 N PHE A 152 24.067 13.093 5.022 1.00 8.94 N
ATOM 1164 CA PHE A 152 25.284 12.340 5.185 1.00 9.64 C
ATOM 1165 CB PHE A 152 25.445 11.415 3.974 1.00 9.66 C
ATOM 1166 CG PHEA152 26.777 10.746 3.892 1.0013.04 C
ATOM 1167 CD1 PHE A 152 27.077 9.673 4.709 1.0015.46 C
ATOM 1168 CE1 PHEA 152 28.312 9.058 4.645 1.0016.57 C
ATOM 1169 CZ PHEA 152 29.257 9.495 3.737 1.0020.05 C
ATOM 1170 CE2 PHE A 152 28.971 10.559 2.913 1.0020.46 C
ATOM 1171 CD2PHEA152 27.731 11.185 2.991 1.0016.44 C
ATOM 1172 C PHE A 152 26.440 13.336 5.275 1.00 9.79 C
ATOM 1173 0 PHEA152 26.515 14.261 4.481 1.0010.75 O
ATOM 1174 N ALAA153 27.322 13.180 6.253 1.0010.44 N
ATOM 1175 CA ALAA 153 28.407 14.153 6.436 1.00 9.77 C
ATOM 1176 CB ALAA 153 28.281 14.869 7.761 1.00 9.43 C
ATOM 1177 C ALAA 153 29.740 13.456 6.355 1.0010.08 C
ATOM 1178 O ALAA 153 29.915 12.383 6.936 1.00 9.24 O
ATOM 1179 N GLU A 154 30.673 14.078 5.632 1.0010.12 N
ATOM 1180 CA GLU A 154 32.031 13.579 5.486 1.0012.11 C
ATOM 1181 CBAGLUA154 32.243 13.108 4.048 0.5012.07 C
ATOM 1182 CBBGLU A 154 32.283 12.891 4.109 0.5011.78 C
ATOM 1183 CGAGLU A154 32.235 11.613 3.863 0.5014.30 C
ATOM 1184 CGBGLU A 154 31.532 13.468 2.924 0.5013.60 C
ATOM 1185 CDAGLU A154 32.643 11.189 2.463 0.5016.15 C
ATOM 1186 CDBGLU 154 31.401 12.505 1.7450.5015.38 C
ATOM 1187 OE1AGLU A 154 32.868 12.066 1.5950.5016.00 O
ATOM 1188 OE1BGLUA154 30.751 12.879 0.746 0.5016.32 O
ATOM 1189 OE2AGLUA154 32.731 9.974 2.228 0.5016.13 O
ATOM 1190 OE2BGLUA154 31.933 11.375 1.809 0.5016.12 O
ATOM 1191 C GLUA154 33.049 14.692 5.792 1.0012.28 C
ATOM 11920 GLU A 154 32.698 15.723 6.381 1.0011.46 O
ATOM 1193 N GLYA 155 34.306 14.482 5.407 1.0012.60 N
ATOM 1194 CA GLY A 155 35.379 15.371 5.829 1.0013.65 C
ATOM 1195 C GLYA155 35.493 15.302 7.333 1.0014.13 C
ATOM 1196 0 GLYA155 35.448 14.215 7.907 1.0014.32 O
ATOM 1197 N VAL A 156 35.575 16.454 7.987 1.0014.34 N
ATOM 1198 CA VAL A 156 35.481 16.472 9.442 1.00 15.33 C
ATOM 1199 CB VAL A 156 36.527 17.434 10.102 1.00 14.92 C
ATOM 1200 CG1 VAL A 156 37.942 16.925 9.862 1.00 16.30 C
ATOM 1201 CG2 VAL A 156 36.365 18.872 9.599 1.00 16.26 C
ATOM 1202 C VAL A 156 34.047 16.802 9.897 1.00 15.99 C
ATOM 1203 O VAL A 156 33.821 17.189 11.049 1.00 16.75 O
ATOM 1204 N GLY A 157 33.081 16.604 8.999 1.00 15.53 N
ATOM 1205 CA GLY A 157 31.691 16.914 9.290 1.00 14.82 C
ATOM 1206 C GLY A 157 31.153 18.036 8.418 1.00 14.93 C
ATOM 1207 O GLY A 157 29.958 18.301 8.413 1.00 14.85 O
ATOM 1208 N GLU A 158 32.030 18.678 7.653 1.00 14.48 N
ATOM 1209 CA GLU A 158 31.653 19.886 6.912 1.00 14.36 C
ATOM 1210 CB GLU A 158 32.844 20.878 6.878 1.00 14.68 C
ATOM 1211 CG GLU A 158 33.822 20.720 5.704 1.00 16.22 C
ATOM 1212 CD GLU A 158 34.820 19.578 5.883 1.00 18.30 C
ATOM 1213 OE1 GLU A 158 34.643 18.726 6.784 1.00 20.06 O
ATOM 1214 OE2 GLU A 158 35.785 19.516 5.104 1.00 17.41 O
ATOM 1215 C GLU A 158 31.098 19.603 5.500 1.00 14.03 C
ATOM 1216 0 GLU A 158 30.464 20.466 4.896 1.00 14.36 O
ATOM 1217 N ILE A 159 31.327 18.392 4.988 1.00 13.48 N
ATOM 1218 CA ILE A 159 30.887 18.029 3.646 1.00 11.58 C
ATOM 1219 CB ILE A 159 31.954 17.149 2.933 1.00 12.01 C
ATOM 1220 CG1 ILE A 159 33.318 17.853 2.883 1.00 13.99 C
ATOM 1221 CD1 ILE A 159 34.476 16.900 2.491 1.00 15.92 C
ATOM 1222 CG2 ILE A 159 31.519 16.788 1.518 1.00 10.15 C
ATOM 1223 C ILE A 159 29.544 17.290 3.714 1.00 11.01 C
ATOM 1224 0 ILE A 159 29.491 16.140 4.151 1.00 9.04 O
ATOM 1225 N LEU A 160 28.469 17.959 3.288 1.00 9.67 N
ATOM 1226 CA LEU A 160 27.108 17.433 3.453 1.00 10.11 C
ATOM 1227 CB LEU A 160 26.185 18.496 4.086 1.00 9.57 C
ATOM 1228 CG LEU A 160 26.581 19.009 5.485 1.00 10.18 C
ATOM 1229 CD1 LEU A 160 25.555 19.988 6.044 1.00 7.75 C
ATOM 1230 CD2 LEU A 160 26.764 17.854 6.424 1.00 8.78 C
ATOM 1231 C LEU A 160 26.504 16.969 2.141 1.00 10.21 C
ATOM 1232 0 LEU A 160 26.667 17.625 1.111 1.00 10.64 O
ATOM 1233 N THR A 161 25.791 15.846 2.200 1.00 9.91 N
ATOM 1234 CA THR A 161 24.966 15.360 1.105 1.00 9.54 C
ATOM 1235 CB THR A 161 25.603 14.103 0.467 1.00 9.61 C
ATOM 1236 OG1 THR A 161 26.867 14.432 -0.116 1.00 9.77 O
ATOM 1237 CG2 THR A 161 24.772 13.591 -0.718 1.00 7.41 C
ATOM 1238 C THR A 161 23.608 14.970 1.666 1.00 9.22 C
ATOM 1239 O THR A 161 23.520 14.052 2.485 1.00 9.17 O
ATOM 1240 N PRO A 162 22.544 15.649 1.239 1.00 8.85 N
ATOM 1241 CA PRO A 162 21.203 15.298 1.716 1.00 8.21 C
ATOM 1242 CB PRO A 162 20.297 16.344 1.058 1.00 8.68 C
ATOM 1243 CG PRO A 162 21.106 16.917 -0.080 1.00 9.27 C
ATOM 1244 CD PRO A 162 22.538 16.792 0.304 1.00 8.26 C
ATOM 1245 C PRO A 162 20.834 13.886 1.275 1.00 9.20 C
ATOM 1246 O PRO A 162 21.151 13.490 0.145 1.00 8.38 O
ATOM 1247 N VAL A 163 20.227 13.120 2.181 1.00 9.72 N
ATOM 1248 CA VAL A 163 19.806 11.745 1.899 1.00 10.92 C
ATOM 1249 CB VAL A 163 20.846 10.711 2.352 1.00 10.41 C
ATOM 1250 CG1 VAL A 163 22.034 10.653 1.383 1.00 11.93 C
ATOM 1251 CG2 VAL A 163 21.317 11.037 3.751 1.00 13.46 C
ATOM 1252 C VAL A 163 18.502 11.468 2.627 1.00 11.31 C
ATOM 1253 O VAL A 163 18.063 12.264 3.459 1.00 11.45 O
ATOM 1254 N ASP A 164 17.900 10.322 2.350 1.00 11.24 N
ATOM 1255 CA ASP A 164 16.580 10:042 2.876 1.00 12.72 C
ATOM 1256 CB ASP A 164 15.556 10.119 1.738 1.00 13.88 C
ATOM 1257 CG ASP A 164 14.129 10.197 2.236 1.00 16.86 C
ATOM 1258 OD1 ASP A 164 13.835 11.024 3.129 1.00 17.65 O
ATOM 1259 OD2 ASP A 164 13.230 9.478 1.771 1.00 20.44 O
ATOM 1260 C ASP A 164 16.520 8.673 3.554 1.00 12.81 C
ATOM 1261 O ASP A 164 16.017 7.718 2.964 1.00 12.61 O
ATOM 1262 N PRO A 165 17.030 8.581 4.787 1.00 12.12 N
ATOM 1263 CA PRO A 165 17.029 7.317 5.535 1.00 12.19 C
ATOM 1264 CB PRO A 165 18.047 7.586 6.654 1.00 11.89 C
ATOM 1265 CG PRO A 165 17.939 9.052 6.903 1.00 11.24 C
ATOM 1266 CD PRO A 165 17.667 9.669 5.554 1.00 11.32 C
ATOM 1267 C PRO A 165 15.663 7.006 6.141 1.00 12.68 C
ATOM 1268 O PRO A 165 14.853 7.925 6.294 1.00 12.17 O
ATOM 1269 N PRO A 166 15.407 5.743 6.496 1.00 13.93 N
ATOM 1270 CA PRO A 166 14.141 5.377 7.158 1.00 14.59 C
ATOM 1271 CB PRO A 166 14.353 3.901 7.540 1.00 15.27 C
ATOM 1272 CG PRO A 166 15.360 3.404 6.567 1.00 15.39 C
ATOM 1273 CD PRO A 166 16.283 4.576 6.289 1.00 13.87 C
ATOM 1274 C PRO A 166 13.878 6.215 8.410 1.00 14.70 C
ATOM 1275 0 PRO A 166 14.802 6.480 9.182 1.00 14.16 O
ATOM 1276 N GLU A 167 12.629 6.629 8.593 1.00 15.39 N
ATOM 1277 CA GLU A 167 12.211 7.335 9.799 1.00 16.93 C
ATOM 1278 CB GLU A 167 11.182 8.411 9.449 1.00 17.24 C ATOM 1279 CG GLU A 167 11.746 9.540 8.599 1.00 17.70 C ATOM 1280 CD GLU A 167 10.695 10.549 8.184 1.00 19.56 C ATOM 1281 OE1 GLU A 167 9.494 10.279 8.372 1.00 24.75 O ATOM 1282 OE2 GLU A 167 11.070 11.618 7.671 1.00 15.98 O ATOM 1283 C GLU A 167 11.641 6.360 10.838 1.00 17.55 c ATOM 1284 O GLU A 167 10.647 5.692 10.590 1.00 18.39 O ATOM 1285 N LYS A 168 12.292 6.269 11.991 1.00 16.53 N ATOM 1286 CA LYS A 168 11.888 5.325 13.030 1.00 15.49 C ATOM 1287 CB LYS A 168 13.052 4.399 13.374 1.00 16.51 C ATOM 1288 CG LYS A 168 13.628 3.654 12.186 1.00 19.69 C ATOM 1289 CD LYS A 168 13.426 2.153 12.324 1.00 28.96 C ATOM 1290 CE LYS A 168 13.762 1.422 11.024 1.00 33.05 c ATOM 1291 NZ LYS A 168 15.080 0.733 11.094 1.00 35.19 N ATOM 1292 C LYS A 168 11.436 6.081 14.277 1.00 14.61 C ATOM 1293 O LYS A 168 11.567 7.309 14.350 1.00 12.38 O ATOM 1294 N TRP A 169 10.886 5.353 15.249 1.00 12.11 N ATOM 1295 CA TRP A 169 10.655 5.927 16.561 1.00 12.57 C ATOM 1296 CB TRP A 169 9.320 5.444 17.142 1.00 12.32 C ATOM 1297 CG TRP A 169 8.132 6.161 16.528 1.00 13.65 C ATOM 1298 CD1 TRP A 169 7.496 5.843 15.358 1.00 14.37 C ATOM 1299 NE1 TRP A 169 6.474 6.731 15.115 1.00 13.75 N ATOM 1300 CE2 TRP A 169 6.427 7.644 16.132 1.00 16.73 C ATOM 1301 CD2 TRP A 169 7.466 7.318 17.039 1.00 15.61 C ATOM 1302 CE3 TRP A 169 7.639 8.125 18.174 1.00 17.30 C ATOM 1303 CZ3 TRP A 169 6.780 9.209 18.367 1.00 16.54 C ATOM 1304 CH2 TRP A 169 5.756 9.497 17.449 1.00 17.22 C ATOM 1305 CZ2 TRP A 169 5.570 8.735 16.325 1.00 16.44 C ATOM 1306 C TRP A 169 11.834 5.574 17.460 1.00 12.48 C ATOM 1307 O TRP A 169 12.433 4.504 17.311 1.00 14.36 O ATOM 1308 N TYR A 170 12.187 6.477 18.372 1.00 11.63 N ATOM 1309 CA TYR A 170 13.350 6.269 19.238 1.00 11.43 C ATOM 1310 CB TYR A 170 14.528 7.189 18.832 1.00 11.27 C ATOM 1311 CG TYR A 170 14.952 7.039 17.383 1.00 11.00 C ATOM 1312 CD1 TYR A 170 14.485 7.912 16.411 1.00 11.18 C ATOM 1313 CE1 TYR A 170 14.864 7.774 15.074 1.00 12.05 C ATOM 1314 CZ TYR A 170 15.715 6.757 14.705 1.00 11.32 C ATOM 1315 OH TYR A 170 16.073 6.621 13.382 1.00 14.06 O ATOM 1316 CE2 TYR 170 16.194 5.869 15.655 1.00 12.42 C ATOM 1317 CD2 TYR A 170 15.813 6.015 16.988 1.00 11.93 C
ATOM 1318 C TYR A 170 13.022 6.468 20.722 1.00 11.42 C
ATOM 1319 O TYR A 170 12.242 7.352 21.090 1.00 11.29 o
ATOM 1320 N LEU A 171 13.603 5.622 21.562 1.00 10.25 N
ATOM 1321 CA LEU A 171 13.682 5.905 22.979 1.00 10.80 C
ATOM 1322 CB LEU A 171 13.423 4.649 23.816 1.00 10.20 C
ATOM 1323 CG LEU A 171 13.154 4.841 25.325 1.00 11.54 C
ATOM 1324 CD1 LEU A 171 12.764 3.505 25.955 1.00 11.55 C
ATOM 1325 CD2 LEU A 171 14.334 5.431 26.084 1.00 12.98 C
ATOM 1326 C LEU A 171 15.079 6.423 23.225 1.00 10.25 C
ATOM 1327 O LEU A 171 16.044 5.725 22.948 1.00 12.80 O
ATOM 1328 N VAL A 172 15.197 7.643 23.726 1.00 10.81 N
ATOM 1329 CA VAL A 172 16.505 8.248 23.939 1.00 10.74 C
ATOM 1330 CB VAL A 172 16.606 9.641 23.268 1.00 10.82 C
ATOM 1331 CG1 VAL A 172 17.937 10.290 23.575 1.00 10.52 C
ATOM 1332 CG2 VAL A 172 16.374 9.536 21.742 1.00 10.39 C
ATOM 1333 C VAL A 172 16.764 8.377 25.428 1.00 11.69 C
ATOM 1334 O VAL A 172 15.993 9.010 26.138 1.00 11.55 O
ATOM 1335 N ALA A 173 17.849 7.771 25.893 1.00 12.43 N
ATOM 1336 CA ALA A 173 18.171 7.723 27.320 1.00 14.65 C
ATOM 1337 CB ALA A 173 18.258 6.289 27.780 1.00 14.73 C
ATOM 1338 C ALA A 173 19.479 8.453 27.628 1.00 16.19 C
ATOM 1339 O ALA A 173 20.301 8.660 26.738 1.00 15.42 O
ATOM 1340 N HIS A 174 19.664 8.809 28.901 1.00 17.94 N
ATOM 1341 CA HIS A 174 20.847 9.516 29.390 1.00 19.69 C
ATOM 1342 CB AHIS A 174 20.641 11.008 29.122 0.50 19.11 C
ATOM 1343 CB BHIS A 174 20.868 11.008 28.952 0.50 20.22 C
ATOM 1344 CG AHIS A 174 21.833 11.873 29.408 0.50 18.78 C
ATOM 1345 CG BHIS A 174 20.354 11.981 29.967 0.50 22.16 C
ATOM 1346 ND1AHIS 174 22.701 11.642 30453 0.50 17.23 N
ATOM 1347 ND1BHIS A 174 19.105 12.557 29 875 0.50 24 37 N
ATOM 1348 CE1AHIS A 174 23.636 12.575 30.461 0.50 14 94 C
ATOM 1349 CE1 BHIS A 174 18.935 13.400 30.878 0.50 25 55 C
ATOM 1350 NE2AHIS A 174 23.397 13.414 29.470 0.50 15 66 N
ATOM 1351 NE2BHIS A 174 20.038 13.411 31.604 0.50 25 83 N
ATOM 1352 CD2AHIS A 174 22.272 13.002 28.800 0.50 16 20 C
ATOM 1353 CD2BHIS A 174 20.949 12.548 31.044 0.50 24 72 C
ATOM 1354 C HIS A 174 20.995 9.263 30.909 1.00 21.31 C
ATOM 1355 O HIS A 174 20.078 9.548 31.663 1.00 22.11 O
ATOM 1356 N PRO A 175 22.118 8.673 31.345 1.00 22.35 N
ATOM 1357 CA PRO A 175 22.307 8.316 32.768 1.00 24.03 C
ATOM 1358 CB PRO A 175 23.476 7.319 32.725 1.00 24.05 C
ATOM 1359 CG PRO A 175 24.257 7.704 31.494 1.00 22.87 C
ATOM 1360 CD PRO A 175 23.277 8.291 30.518 1.00 22.13 C
ATOM 1361 C PRO A 175 22.670 9.485 33.709 1.00 24.95 C
ATOM 1362 O PRO A 175 22.640 9.312 34.934 1.00 25.52 O
ATOM 1363 N GLY A 176 23.030 10.635 33.153 1.00 25.68 N
ATOM 1364 CA GLY A 176 23.335 11.805 33.962 1.00 26.55 C
ATOM 1365 C GLY A 176 24.752 12.344 33.829 1.00 27.32 C
ATOM 1366 O GLY A 176 25.008 13.508 34.175 1.00 29.03 O
ATOM 1367 N VAL A 177 25.675 11.517 33.343 1.00 26.53 N
ATOM 1368 CA VAL A 177 27.072 11.941 33.171 1.00 26.18 C
ATOM 1369 CB VAL A 177 28.052 10.717 33.094 1.00 26.41 C
ATOM 1370 CG1 VAL A 177 27.780 9.856 31.867 1.00 25.18 C
ATOM 1371 CG2 VAL A 177 29.513 11.168 33.126 1.00 26.98 C
ATOM 1372 C VAL A 177 27.249 12.855 31.948 1.00 26.55 C
ATOM 1373 O VAL A 177 26.692 12.593 30.882 1.00 24.94 O
ATOM 1374 N SER A 178 27.998 13.945 32.117 1.00 26.99 N
ATOM 1375 CA SER A 178 28.348 14.796 30.988 1.00 28.23 C
ATOM 1376 CB SER A 178 28.418 16.270 31.398 1.00 29.51 C
ATOM 1377 OG SER A 178 28.869 17.078 30.317 1.00 33.35 O
ATOM 1378 C SER A 178 29.675 14.339 30.402 1.00 27.97 C
ATOM 1379 O SER A 178 30.710 14.408 31.065 1.00 28.86 O
ATOM 1380 N ILE A 179 29.630 13.827 29.174 1.00 26.24 N
ATOM 1381 CA ILE A 179 30.836 13.435 28.463 1.00 25.01 C
ATOM 1382 CB ILE A 179 30.623 12.139 27.664 1.00 24.35 C
ATOM 1383 CG1 ILE A 179 30.220 10.991 28.586 1.00 22.95 C
ATOM 1384 CD1 ILE A 179 29.947 9.688 27.856 1.00 19.88 C
ATOM 1385 CG2 ILE A 179 31.891 11.787 26.884 1.00 23.05 C
ATOM 1386 C ILE A 179 31.242 14.548 27.517 1.00 25.32 C
ATOM 1387 O ILE A 179 30.522 14.858 26.568 1.00 25.73 O
ATOM 1388 N PRO A 180 32.382 15.168 27.782 1.00 25.30 N
ATOM 1389 CA PRO A 180 32.894 16.212 26.893 1.00 25.14 C
ATOM 1390 CB PRO A 180 34.076 16.795 27.677 1.00 25.36 C
ATOM 1391 CG PRO A 180 33.919 16.263 29.085 1.00 25.64 C
ATOM 1392 CD PRO A 180 33.259 14.934 28.942 1.00 24.99 C
ATOM 1393 C PRO A 180 33.361 15.581 25.585 1.00 25.16 C
ATOM 1394 0 PRO A 180 34.089 14.591 25.619 1.00 24.02 O
ATOM 1395 N THR A 181 32.922 16.135 24.456 1.00 25.70 N
ATOM 1396 CA THR A 181 33.329 15.640 23.135 1.00 25.69 C
ATOM 1397 CB THR A 181 32.882 16.631 22.018 1.00 26.02 C
ATOM 1398 OG1 THR A 181 31.452 16.648 21.941 1.00 27.14 G
ATOM 1399 CG2 THR A 181 33.304 16.133 20.637 1.00 26.13 C
ATOM 1400 C THR A 181 34.849 15.272 23.018 1.00 25.60 C
ATOM 1401 O THR A 181 35.163 14.154 22.602 1.00 25.77 O
ATOM 1402 N PRO A 182 35.775 16.180 23.383 1.00 25.35 N
ATOM 1403 CA PRO A 182 37.224 15.893 23.262 1.00 24.99 C
ATOM 1404 CB PRO A 182 37.894 17.196 23.756 1.00 25.41 C
ATOM 1405 CG PRO A 182 36.844 17.938 24.485 1.00 24.71 C
ATOM 1406 CD PRO A 182 35.542 17.559 23.860 1.00 25.74 C
ATOM 1407 C PRO A 182 37.743 14.685 24.072 1.00 24.28 C
ATOM 1408 O PRO A 182 38.734 14.085 23.668 1.00 23.12 O
ATOM 1409 N VAL A 183 37.076 14.334 25.171 1.00 24.32 N
ATOM 1410 CA VAL A 183 37.452 13.171 25.995 1.00 23.19 C
ATOM 1411 CB VAL A 183 36.583 13.117 27.285 1.00 24.10 C
ATOM 1412 CG1 VAL A 183 36.770 11.805 28.050 1.00 23.54 C
ATOM 1413 CG2 VAL A 183 36.895 14.314 28.181 1.00 24.39 C
ATOM 1414 C VAL A 183 37.368 11.842 25.215 1.00 23.68 C
ATOM 1415 O VAL A 183 38.230 10.965 25.352 1.00 23.69 O
ATOM 1416 N ILE A 184 36.339 11.709 24.378 1.00 22.82 N
ATOM 1417 CA ILE A 184 36.207 10.544 23.506 1.00 21.52 C
ATOM 1418 CB ILE A 184 34.760 10.442 22.956 1.00 20.90 C
ATOM 1419 CG1 ILE A 184 33.770 10.283 24.104 1.00 20.09 C
ATOM 1420 CD1 ILE A 184 33.924 8.968 24.882 1.00 19.13 C
ATOM 1421 CG2 ILE A 184 34.621 9.283 21.960 1.00 18.70 C
ATOM 1422 C ILE A 184 37.228 10.585 22.361 1.00 21.68 C
ATOM 1423 O ILE A 184 37.962 9.618 22.140 1.00 21.17 O
ATOM 1424 N PHE A 185 37.294 11.717 21.664 1.00 22.18 N
ATOM 1425 CA PHE A 185 38.153 11.836 20.479 1.00 23.62 C
ATOM 1426 CB PHE A 185 37.867 13.144 19.735 1.00 22.86 C
ATOM 1427 CG PHE A 185 36.753 13.028 18.748 1.00 21.78 C
ATOM 1428 CD1 PHE A 185 35.646 13.862 18.826 1.00 20.30 C
ATOM 1429 CE1 PHE A 185 34.601 13.742 17.920 1.00 22.38 C
ATOM 1430 CZ PHE A 185 34.653 12.770 16.928 1.00 22.82 C
ATOM 1431 CE2 PHE A 185 35.752 11.922 16.846 1.00 22.61 C
ATOM 1432 CD2 PHE A 185 36.790 12.050 17.760 1.00 23.02 C
ATOM 1433 C PHE A 185 39.651 11.693 20.776 1.00 24.77 C
ATOM 1434 O PHE A 185 40.427 11.282 19.908 1.00 25.61 O
ATOM 1435 N LYS A 186 40.045 12.010 22.003 1.00 25.71 N
ATOM 1436 CA LYS A 186 41.447 11.950 22.391 1.00 27.05 C
ATOM 1437 CB LYS A 186 41.791 13.126 23.313 1.00 27.77 C
ATOM 1438 CG LYS A 186 42.428 14.303 22.586 1.00 31.27 C
ATOM 1439 CD LYS A 186 41.440 15.450 22.388 1.00 35.90 C
ATOM 1440 CE LYS A 186 41.813 16.657 23.243 1.00 39.07 C
ATOM 1441 NZ LYS A 186 42.430 17.756 22.438 1.00 40.95 N
ATOM 1442 C LYS A 186 41.833 10.622 23.052 1.00 26.75 C
ATOM 1443 O LYS A 186 42.980 10.437 23.439 1.00 26.85 O
ATOM 1444 N ASP A 187 40.878 9.701 23.168 1.00 26.23 N
ATOM 1445 CA ASP A 187 41.161 8.370 23.705 1.00 26.24 C
ATOM 1446 CB ASP A 187 39.864 7.596 23.950 1.00 25.83 C
ATOM 1447 CG ASP A 187 40.014 6.514 25.004 1.00 24.79 C
ATOM 1448 OD1 ASP A 187 40.613 5.450 24.716 1.00 21.94 O
ATOM 1449 OD2 ASP A 187 39.524 6.626 26.143 1.00 25.34 O
ATOM 1450 C ASP A 187 42.058 7.564 22.774 1.00 26.31 C
ATOM 1451 O ASP A 187 41.778 7.451 21.585 1.00 26.64 O
ATOM 1452 N PRO A 188 43.134 7.004 23.326 1.00 26.23 N
ATOM 1453 CA PRO A 188 44.064 6.145 22.572 1.00 25.87 C
ATOM 1454 CB PRO A 188 45.033 5.648 23.660 1.00 26.05 C
ATOM 1455 CG PRO A 188 44.966 6.673 24.720 1.00 26.38 C
ATOM 1456 CD PRO A 188 43.559 7.189 24.724 1.00 26.56 C
ATOM 1457 C PRO A 188 43.417 4.937 21.889 1.00 25.05 C
ATOM 1458 O PRO A 188 43.896 4.524 20.833 1.00 24.41 O
ATOM 1459 N GLU A 189 42.367 4.373 22.486 1.00 25.10 N
ATOM 1460 CA GLU A 189 41.771 3.131 21.978 1.00 25.48 C
ATOM 1461 CB GLU A 189 41.246 2.272 23.135 1.00 26.38 C
ATOM 1462 CG GLU A 189 42.330 1.508 23.881 1.00 30.27 C
ATOM 1463 CD GLU A 189 41.850 0.955 25.211 1.00 35.26 C
ATOM 1464 OE1 GLU A 189 40.769 0.322 25.246 1.00 36.19 O
ATOM 1465 OE2 GLU A 189 42.557 1.150 26.225 1.00 37.97 O
ATOM 1466 C GLU A 189 40.654 3.358 20.948 1.00 24.49 C
ATOM 1467 O GLU A 189 40.147 2.398 20.353 1.00 24.40 O
ATOM 1468 N LEU A 190 40.276 4.618 20.751 1.00 22.98 N
ATOM 1469 CA LEU A 190 39.287 4.980 19.735 1.00 22.41 C
ATOM 1470 CB LEU A 190 39.076 6.492 19.714 1.00 22.21 C
ATOM 1471 CG LEU A 190 38.024 7.023 18.740 1.00 20.89 C
ATOM 1472 CD1 LEU A 190 36.640 6.906 19.359 1.00 22.37 C
ATOM 1473 CD2 LEU A 190 38.323 8.457 18.363 1.00 19.74 C
ATOM 1474 C LEU A 190 39.691 4.501 18.338 1.00 21.80 C
ATOM 1475 O LEU A 190 40.802 4.765 17.889 1.00 22.01 O
ATOM 1476 N PRO A 191 38.785 3.796 17.662 1.00 22.13 N
ATOM 1477 CA PRO A 191 39.011 3.379 16.277 1.00 22.07 C
ATOM 1478 CB PRO A 191 37.723 2.626 15.915 1.00 22.75 C
ATOM 1479 CG PRO A 191 37.091 2.265 17.235 1.00 22.96 C
ATOM 1480 CD PRO A 191 37.467 3.370 18.168 1.00 22.23 C
ATOM 1481 C PRO A 191 39.174 4.608 15.383 1.00 22.27 C
ATOM 1482 O PRO A 191 38.367 5.534 15.479 1.00 22.91 O
ATOM 1483 N ARG A 192 40.215 4.624 14.555 1.00 20.72 N
ATOM 1484 CA ARG A 192 40.502 5.761 13.681 1.00 20.39 C
ATOM 1485 CB ARG A 192 41.688 6.570 14.209 1.00 19.79 C
ATOM 1486 CG ARG A 192 41.511 7.140 15.594 1.00 20.77 C
ATOM 1487 CD ARG A 192 42.662 8.013 16.057 1.00 18.90 C
ATOM 1488 NE ARG A 192 42.286 8.787 17.238 1.00 19.72 N
ATOM 1489 CZ ARG A 192 42.401 8.357 18.486 1.00 19.47 C
ATOM 1490 NH1 ARG A 192 42.918 7.154 18.739 1.00 19.20 N
ATOM 1491 NH2 ARG A 192 42.018 9.141 19.488 1.00 18.24 N
ATOM 1492 C ARG A 192 40.828 5.304 12.271 1.00 19.83 C
ATOM 1493 0 ARG A 192 41.373 6.071 11.482 1.00 18.94 O
ATOM 1494 N ASN A 193 40.496 4.059 11.947 1.00 19.86 N
ATOM 1495 CA AASN A 193 40.909 3.505 10.656 0.50 19.85 C
ATOM 1496 CA BASN A 193 40 .922 3, 447 10.695 0.50 19.35 C
ATOM 1497 CB AASN A 193 42.129 2. 5: 84 10.833 0.50 20.75 C
ATOM 1498 CB BASN A 193 42.023 2. 4. 05 10.968 0.50 19.69 C
ATOM 1499 CG AASN A 193 43 i.405 3. 3: 63 11.120 0.50 22.85 C
ATOM 1500 CG BASN A 193 41.517 1. 203 11.762 0.50 19.78 C
ATOM 1501 OD1AASN A 193 43.783 3.563 12.279 0.50 26.56 O
ATOM 1502 OD1 BASN A 193 40.537 1.295 12.510 0.50 20.03 O
ATOM 1503 ND2AASN A 193 44.063 3.829 10.064 0.50 25.56 N
ATOM 1504 ND2BASN A 193 42.186 0.065 11.596 0.50 20.53 N
ATOM 1505 C AS A 193 39.777 2.809 9.916 1.00 19.10 C
ATOM 1506 O ASN A 193 40.007 1.938 9.070 1.00 18.84 O
ATOM 1507 N THR A 194 38.545 3.217 10.219 1.00 17.73 N
ATOM 1508 CA THR A 194 37.391 2.674 9.527 1.00 16.29 C
ATOM 1509 CB THR A 194 36.082 3.139 10.193 1.00 16.07 C
ATOM 1510 OG1 THR A 194 36.060 2.711 11.563 1.00 14.34 O
ATOM 1511 CG2 THR A 194 34.889 2.430 9.577 1.00 14.16 C
ATOM 1512 C THR A 194 37.449 3.124 8.072 1.00 16.48 C
ATOM 1513 O THR A 194 37.594 4.309 7.797 1.00 14.74 O
ATOM 1514 N PRO A 195 37.406 2.177 7.142 1.00 17.09 N
ATOM 1515 CA PRO A 195 37.519 2.513 5.717 1.00 17.60 C
ATOM 1516 CB PRO A 195 37.395 1.149 5.032 1.00 17.51 C
ATOM 1517 CG PRO A 195 37.892 0.189 6.081 1.00 19.50 C
ATOM 1518 CD PRO A 195 37.300 0.721 7.362 1.00 17.47 C
ATOM 1519 C PRO A 195 36.420 3.481 5.249 1.00 16.70 C
ATOM 1520 O PRO A 195 35.254 3.352 5.655 1.00 16.15 O
ATOM 1521 N LYS A 196 36.812 4.460 4.434 1.00 16.84 N
ATOM 1522 CA LYS A 196 35.860 5.371 3.803 1.00 17.02 C
ATOM 1523 CB LYS A 196 36.580 6.549 3.141 0.50 16.68 C
ATOM 1524 CG LYS A 196 36.892 7.697 4.077 0.50 17.66 C
ATOM 1525 CD LYS A 196 37.916 8.660 3.483 0.50 20.19 C
ATOM 1526 CE LYS A 196 39.236 8.613 4.244 0.50 20.46 C
ATOM 1527 NZ LYS A 196 40.068 9.830 4.000 0.50 20.90 N
ATOM 1528 C LYS A 196 35.063 4.595 2.766 1.00 17.20 C
ATOM 1529 0 LYS A 196 35.643 3.913 1.919 1.00 16.94 O
ATOM 1530 N ARG A 197 33.737 4.668 2.854 1.00 16.36 N
ATOM 1531 CA ARG A 197 32.876 3.916 1.944 1.00 16.85 C
ATOM 1532 CB ARG A 197 32.115 2.818 2.705 1.00 17.02 C
ATOM 1533 CG ARG A 197 33.025 1.696 3.227 1.00 18.71 C
ATOM 1534 CD ARG A 197 32.421 0.857 4.353 1.00 20.26 C
ATOM 1535 NE ARG A 197 32.370 1.604 5.608 1.00 20.58 N
ATOM 1536 CZ ARG A 197 31.745 1.194 6.700 1.00 19.61 C
ATOM 1537 NH1 ARG A 197 31.100 0.031 6.705 1.00 20.36 N
ATOM 1538 NH2 ARG A 197 31.741 1.959 7.787 1.00 18.01 N
ATOM 1539 C ARG A 197 31.905 4.845 1.219 1.00 16.20 C
ATOM 1540 O ARG A 197 31.731 5.992 1.609 1.00 15.43 O
ATOM 1541 N SER A 198 31.287 4.346 0.158 1.00 16.29 N
ATOM 1542 CA SER A 198 30.252 5.101 -0.536 1.00 16.59 C
ATOM 1543 CB SER A 198 29.956 4.478 -1.899 1.00 16.04 C
ATOM 1544 OG SER A 198 29.302 3.232 -1.752 1.00 16.44 O
ATOM 1545 C SER A 198 28.977 5.168 0.297 1.00 16.54 C
ATOM 1546 0 SER A 198 28.732 4.306 1.146 1.00 15.74 O
ATOM 1547 N ILE A 199 28.176 6.204 0.046 1.00 17.77 N
ATOM 1548 CA ILE A 199 26.841 6.350 0.640 1.00 18.57 C
ATOM 1549 CB ILE A 199 26.137 7.603 0.062 1.00 18.78 C
ATOM 1550 CG1 ILE A 199 26.936 8.854 0.423 1.00 21.15 C
ATOM 1551 CD1 ILE A 199 26.553 10.106 -0.357 1.00 25.88 C
ATOM 1552 CG2 ILE A 199 24.715 7.705 0.574 1.00 19.64 C
ATOM 1553 C ILE A 199 25.964 5.109 0.445 1.00 18.01 C
ATOM 1554 0 ILE A 199 25.348 4.640 1.398 1.00 18.45 O
ATOM 1555 N GLU A 200 25.916 4.584 -0.782 1.00 18.30 N
ATOM 1556 CA GLU A 200 25.120 3.390 -1.083 1.00 19.02 C
ATOM 1557 CB AGLU A 200 25.292 2.985 -2.552 0.50 19.28 C
ATOM 1558 CBBGLUA200 25.265 2.959 -2.551 0.5019.33 C
ATOM 1559 CGAGLUA200 24.580 1.698 -2.949 0.5021.68 C
ATOM 1560 CGBGLUA200 24.384 1.767 -2.9280.5021.91 C
ATOM 1561 CDAGLUA200 24.577 1.471 -4.4540.5024.97 C
ATOM 1562 CDBGLUA200 24.853 1.042 -4.183 0.5025.33 C
ATOM 1563 OE1AGLUA200 25.653 1.158 -5.017 0.5025.68 O
ATOM 1564 OE1BGLUA200 24.272 1.285 -5.269 0.5026.06 O
ATOM 1565 OE2AGLUA200 23.500 1.604 -5.076 0.5022.45 O
ATOM 1566 OE2BGLUA200 25.793 0.221 -4.086 0.5023.44 O
ATOM 1567 C GLUA200 25.501 2.239 -0.155 1.0018.07 C
ATOM 1568 O GLUA200 24.635 1.632 0.456 1.0017.22 O
ATOM 1569 N THRA201 26.803 1.978 -0.038 1.0017.51 N
ATOM 1570 CA THRA201 27.317 0.936 0.843 1.0017.17 C
ATOM 1571 CB THR A 201 28.845 0.829 0.703 1.0017.74 C
ATOM 1572 OG1 THR A 201 29.180 0.413 -0.628 1.0018.00 O
ATOM 1573 CG2 THR A 201 29.395 -0.293 1.579 1.0016.18 C
ATOM 1574 C THRA201 26.944 1.185 2.303 1.0016.81 C
ATOM 1575 O THR A 201 26.486 0.275 2.995 1.0016.84 O
ATOM 1576 N LEU A 202 27.134 2.420 2.763 1.0015.56 N
ATOM 1577 CA LEU A202 26.880 2.763 4.164 1.0015.05 C
ATOM 1578 CB LEU A 202 27.395 4.182 4.479 1.0013.51 C
ATOM 1579 CG LEU A 202 28.927 4.307 4.434 1.0013.89 C
ATOM 1580 CD1 LEU A 202 29.376 5.768 4.474 1.0015.87 C
ATOM 1581 CD2LEUA202 29.563 3.532 5.572 1.0011.73 C
ATOM 1582 C LEU A 202 25.400 2.619 4.541 1.0015.53 C
ATOM 1583 O LEUA202 25.079 2.185 5.648 1.0015.03 O
ATOM 1584 N LEU A 203 24.511 2.941 3.602 1.0016.28 N
ATOM 1585 CA LEU A 203 23.069 2.867 3.849 1.0017.90 C
ATOM 1586 CB LEU A 203 22.289 3.678 2.795 1.0017.42 C
ATOM 1587 CG LEU A 203 22.370 5.205 2.911 1.0017.32 C
ATOM 1588 CD1 LEU A 203 21.625 5.879 1.767 1.0015.98 C
ATOM 1589 CD2 LEU A 203 21.823 5.682 4.247 1.0019.13 C
ATOM 1590 C LEU A 203 22.526 1.427 3.924 1.0019.28 C
ATOM 1591 O LEUA203 21.487 1.192 4.547 1.0019.43 O
ATOM 1592 N LYSA204 23.213 0.474 3.292 1.0020.59 N
ATOM 1593 CA LYS A 204 22.770 -0.926 3.347 1.0022.64 C
ATOM 1594 CB LYS A 204 22.884 -1.622 1.976 1.0023.10 C
ATOM 1595 CG LYS A 204 24.046 -1.193 1.123 1.0026.77 C
ATOM 1596 CD LYS A 204 23.844 -1.586 -0.343 1.0030.23 C
ATOM 1597 CE LYS A 204 23.918 -3.101 -0.535 1.0033.39 C
ATOM 1598 NZ LYSA204 24.911 -3.490 -1.579 1.0035.67 N
ATOM 1599 C LYS A 204 23.490 -1.742 4.435 1.0023.12 C
ATOM 1600 O LYS A 204 22.996 -2.790 4.851 1.0024.41 O
ATOM 1601 N CYS A 205 24.640 -1.249 4.893 1.0022.23 N
ATOM 1602 CA CYS A 205 25.380 -1.859 5.999 1.0022.31 C
ATOM 1603 CBACYSA205 26.828 -1.357 6.028 0.5022.25 C
ATOM 1604 CBBCYSA205 26.812 -1.303 6.013 0.5022.16 C
ATOM 1605 SGACYSA205 27.910 -2.192 4.843 0.5026.72 S
ATOM 1606 SGBCYSA205 27.925 -1.963 7.271 0.5025.82 S
ATOM 1607 C CYSA205 24.696 -1.606 7.350 1.0020.71 C
ATOM 1608 O CYSA205 23.970 -0.631 7.512 1.0019.62 O
ATOM 1609 N GLU A 206 24.928 -2.500 8.309 1.0019.25 N
ATOM 1610 CA GLU A206 24.479 -2.312 9.681 1.0019.29 C
ATOM 1611 CB GLU A 206 24.969 -3.474 10.552 1.0020.26 C
ATOM 1612 CG GLU A 206 24.408 -3.504 11.969 1.0026.86 C
ATOM 1613 CD GLU A 206 25.105 -4.533 12.866 1.0033.53 C
ATOM 1614 OE1GLUA206 25.071 -4.363 14.106 1.0034.59 O
ATOM 1615 OE2 GLU A 206 25.682 -5.512 12.335 1.0035.64 O
ATOM 1616 C GLUA206 24.999 -0.971 10.216 1.0017.43 C
ATOM 1617 O GLUA206 26.157 -0.624 9.990 1.0017.60 O
ATOM 1618 N PHEA207 24.137 -0.209 10.884 1.0015.78 N
ATOM 1619 CA PHE A 207 24.540 1.081 11.438 1.0014.33 C
ATOM 1620 CB PHEA207 23.336 2.006 11.657 1.0013.97 C
ATOM 1621 CG PHEA207 22.727 2.550 10.393 1.0013.20 C
ATOM 1622 CD1 PHE A 207 23.203 2.181 9.142 1.0011.61 C
ATOM 1623 CE1 PHE A 207 22.615 2.682 7.974 1.0013.22 C
ATOM 1624 CZ PHE A 207 21.543 3.563 8.058 1.0011.69 C
ATOM 1625 CE2 PHE A 207 21.060 3.947 9.306 1.0014.24 C
ATOM 1626 CD2PHEA207 21.650 3.436 10.465 1.0013.30 C
ATOM 1627 C PHEA207 25.230 0.861 12.768 1.0014.11 C
ATOM 1628 O PHEA207 24.702 0.152 13.628 1.0013.19 O
ATOM 1629 N SERA208 26.404 1.468 12.944 1.0012.68 N
ATOM 1630 CA SER A 208 27.035 1.513 14.262 1.0012.08 C
ATOM 1631 CB SERA208 28.007 0.345 14.454 1.0012.23 C
ATOM 1632 OG SERA208 29.034 0.375 13.481 1.0012.80 O
ATOM 1633 C SERA208 27.742 2.844 14.487 1.0012.32 C
ATOM 1634 O SER A 208 27.856 3.661 13.567 1.0011.89 O
ATOM 1635 N ASNA209 28.199 3.058 15.716 1.0010.98 N
ATOM 1636 CA ASN A 209 28.894 4.272 16.098 1.0011.80 C
ATOM 1637 CB ASN A 209 28.056 5.045 17.121 1.0010.20 C
ATOM 1638 CG ASN A 209 28.693 6.370 17.551 1.00 13.13 C
ATOM 1639 OD1 ASN A 209 29.914 6.554 17.483 1.00 11.62 O
ATOM 1640 ND2 ASN A 209 27.855 7.296 18.028 1.00 9.39 N
ATOM 1641 C ASN A 209 30.247 3.887 16.680 1.00 12.45 C
ATOM 1642 O ASN A 209 30.308 3.219 17.714 1.00 11.39 O
ATOM 1643 N ASP A 210 31.323 4.313 16.018 1.00 12.84 N
ATOM 1644 CA ASP A 210 32.685 3.930 16.405 1.00 13.77 C
ATOM 1645 CB ASP A 210 33.713 4.438 15.384 1.00 13.57 C
ATOM 1646 CG ASP A 210 33.819 3.563 14.150 1.00 12.85 C
ATOM 1647 OD1 ASP A 210 33.287 2.436 14.139 1.00 12.41 O
ATOM 1648 OD2 ASP A 210 34.438 3.931 13.126 1.00 13.12 O
ATOM 1649 C ASP A 210 33.074 4.449 17.798 1.00 14.64 C
ATOM 1650 O ASP A 210 33.985 3.911 18.421 1.00 13.99 O
ATOM 1651 N CYS A 211 32.395 5.496 18.278 1.00 14.63 N
ATOM 1652 CA CYS A 211 32.690 6.050 19.610 1.00 14.77 C
ATOM 1653 CB CYS A 211 32.120 7.456 19.751 1.00 14.59 C
ATOM 1654 SG CYS A 211 32.818 8.650 18.606 1.00 16.10 S
ATOM 1655 C CYS A 211 32.153 5.196 20.756 1.00 14.53 C
ATOM 1656 O CYS A 211 32.556 5.372 21.916 1.00 13.24 O
ATOM 1657 N GLU A 212 31.221 4.306 20.436 1.00 14.28 N
ATOM 1658 CA GLU A 212 30.474 3.567 21.451 1.00 15.04 C
ATOM 1659 CB GLU A 212 29.431 2.681 20.799 1.00 14.17 C
ATOM 1660 CG GLU A 212 28.554 1.933 21.792 1.00 15.36 C
ATOM 1661 CD GLU A 212 27.326 1.377 21.129 1.00 14.63 C
ATOM 1662 OE1 GLU A 212 26.706 2.127 20.346 1.00 12.74 O
ATOM 1663 OE2 GLU A 212 27.004 0.192 21.355 1.00 16.27 O
ATOM 1664 C GLU A 212 31.362 2.709 22.349 1.00 15.66 C
ATOM 1665 O GLU A 212 31.155 2.666 23.556 1.00 15.34 O
ATOM 1666 N VAL A 213 32.335 2.023 21.752 1.00 16.38 N
ATOM 1667 CA VAL A 213 33.240 1.144 22.505 1.00 17.95 C
ATOM 1668 CB VAL A 213 34.239 0.391 21.547 1.00 19.13 C
ATOM 1669 CG1 VAL A 213 35.166 1.385 20.796 1.00 18.88 C
ATOM 1670 CG2 VAL A 213 35.023 -0.697 22.288 1.00 18.74 C
ATOM 1671 C VAL A 213 33.968 1.922 23.604 1.00 18.74 C
ATOM 1672 O VAL A 213 34.082 1.453 24.741 1.00 19.53 O
ATOM 1673 N ILE A 214 34.382 3.145 23.283 1.00 18.91 N
ATOM 1674 CA ILE A 214 35.083 3.998 24.231 1.00 19.22 C
ATOM 1675 CB ILE A 214 35.772 5.183 23.498 1.00 19.09 C
ATOM 1676 CG1 ILE A 214 36.778 4.670 22.466 1.00 20.72 C
ATOM 1677 CD1 ILE A 214 37.666 3.532 22.953 1.00 22.18 C
ATOM 1678 CG2 ILEA 214 36.455 6.13224.489 1.0020.78 C
ATOM 1679 C ILEA214 34.136 4.505 25.312 1.0018.67 C
ATOM 1680 0 ILEA214 34.475 4.489 26.500 1.0018.81 O
ATOM 1681 N ALAA215 32.948 4.938 24.901 1.0017.77 N
ATOM 1682 CA ALA A 215 31.974 5.491 25.840 1.0017.92 C
ATOM 1683 CB ALA A 215 30.757 6.008 25.102 1.0016.80 C
ATOM 1684 C ALAA215 31.568 4.448 26.878 1.0018.10 C
ATOM 16850 ALAA 215 31.477 4.75828.070 1.0018.20 O
ATOM 1686 N ARGA216 31.341 3.219 26.413 1.0018.77 N
ATOM 1687 CA ARG A 216 31.011 2.083 27.282 1.0020.73 C
ATOM 1688 CB ARG A 216 30.723 0.824 26.455 1.0020.87 C
ATOM 1689 CG ARG A216 29.406 0.813 25.710 1.0022.04 C
ATOM 1690 CD ARGA216 29.034 -0.56625.169 1.0024.60 C
ATOM 1691 NE ARG A 216 28.269 -1.345 26.147 1.0023.63 N
ATOM 1692 CZ ARG A 216 27.364 -2.274 25.839 1.0022.68 C
ATOM 1693 NH1ARGA216 27.100 -2.559 24.573 1.0021.95 N
ATOM 1694 NH2ARGA216 26.713 -2.914 26.811 1.0022.36 N
ATOM 1695 C ARG A 216 32.136 1.77228.260 1.0021.33 C
ATOM 1696 O ARG A 216 31.894 1.571 29.458 1.0022.02 O
ATOM 1697 N LYS A 217 33.365 1.730 27.746 1.0021.84 N
ATOM 1698 CA LYS A 217 34.518 1.36928.563 1.0023.16 C
ATOM 1699 CB LYSA217 35.777 1.201 27.702 1.0023.86 C
ATOM 1700 CG LYS A 217 36.664 0.06728.179 1.0027.52 C
ATOM 1701 CD LYS A 217 38.079 0.156 27.617 1.0032.05 C
ATOM 1702 CE LYSA217 39.021 -0.788 28.384 1.0033.54 C
ATOM 1703 NZ LYSA217 40.282 -1.09227.633 1.0033.68 N
ATOM 1704 C LYS A 217 34.783 2.384 29.663 1.0022.33 C
ATOM 1705 O LYSA217 35.043 2.012 30.800 1.0023.44 O
ATOM 1706 N ARG 218 34.708 3.662 29.328 1.0021.60 N
ATOM 1707 CA ARG A 218 35.117 4.704 30.266 1.0021.81 C
ATOM 1708 CB ARG A 218 35.725 5.89529.513 1.0022.28 C
ATOM 1709 CG ARG 218 36.849 5.527 28.558 1.0025.19 C
ATOM 1710 CD ARG A 218 38.124 5.023 29.234 1.0029.59 C
ATOM 1711 NE ARGA218 39.202 4.880 28.262 1.0034.74 N
ATOM 1712 CZ ARGA218 40.010 3.829 28.169 1.0037.01 C
ATOM 1713 NH1 ARG A 218 39.882 2.803 29.001 1.0038.20 N
ATOM 1714 NH2ARGA218 40.957 3.807 27.241 1.0037.85 N
ATOM 1715 C ARGA218 33.986 5.186 31.176 1.0021.65 C
ATOM 1716 O ARGA218 34.244 5.780 32.221 1.0022.13 O
ATOM 1717 N PHE A 219 32.736 4.943 30.787 1.0020.59 N
ATOM 1718 CA PHE A 219 31.602 5.409 31.594 1.0020.45 C
ATOM 1719 CB PHE A 219 30.882 6.568 30.899 1.0020.51 C
ATOM 1720 CG PHEA219 31.759 7.760 30.663 1.0022.17 C
ATOM 1721 CD1 PHE A 219 32.472 7.890 29.478 1.0021.07 C
ATOM 1722 CE1 PHE A 219 33.294 8.97529.262 1.0022.95 C
ATOM 1723 CZ PHEA219 33.420 9.94730.240 1.0025.01 C
ATOM 1724 CE2 PHE A 219 32.718 9.825 31.432 1.0024.78 C
ATOM 1725 CD2 PHE A 219 31.900 8.735 31.640 1.0022.57 C
ATOM 1726 C PHEA219 30.630 4.287 31.905 1.0020.43 C
ATOM 1727 0 PHE A 219 29.809 3.913 31.069 1.0019.53 O
ATOM 1728 N ARG A 220 30.726 3.766 33.129 1.0020.69 N
ATOM 1729 CA ARG A 220 30.008 2.559 33.539 1.0020.69 C
ATOM 1730 CBAARGA220 30.321 2.211 34.995 0.5021.18 C
ATOM 1731 CBBARGA220 30.329 2.244 35.004 0.5020.75 C
ATOM 1732 CGAARGA220 31.006 0.860 35.181 0.5023.59 C
ATOM 1733 CGBARGA220 29.620 1.026 35.574 0.5021.16 C
ATOM 1734 CDAARGA220 31.601 0.645 36.573 0.5027.98 C
ATOM 1735 CDBARGA220 30.249 -0.296 35.181 0.5023.60 C
ATOM 1736 NEAARGA220 32.137 1.886 37.131 0.5031.20 N
ATOM 1737 NEBARGA220 29.509 -1.436 35.7120.5024.21 N
ATOM 1738 CZAARGA220 32.523 2.039 38.3920.5032.18 C
ATOM 1739 CZBARGA220 28.493 -2.028 35.0920.5024.83 C
ATOM 1740 NH1AARGA220 32.444 1.02539.2420.5032.45 N
ATOM 1741 NH1BARGA220 28.079 -1.588 33.9070.5023.33 N
ATOM 1742 NH2AARGA220 32.994 3.211 38.804 0.5031.98 N
ATOM 1743 NH2BARGA220 27.888 -3.064 35.6600.5023.05 N
ATOM 1744 C ARGA220 28.494 2.685 33.347 1.0019.98 C
ATOM 1745 O ARGA220 27.825 1.728 32.974 1.0020.41 O
ATOM 1746 N GLUA221 27.967 3.867 33.596 1.0019.10 N
ATOM 1747 CA GLU A 221 26.529 4.066 33.523 1.0020.47 C
ATOM 1748 CB GLUA221 26.112 5.270 34.385 1.0020.52 C
ATOM 1749 CG GLU A 221 26.466 5.066 35.865 1.0023.66 C
ATOM 1750 CD GLU A221 25.697 5.975 36.817 1.0026.40 C
ATOM 1751 OE1 GLU A 221 24.896 6.816 36.356 1.0030.84 O
ATOM 1752 OE2GLUA221 25.900 5.850 38.037 1.0026.16 O
ATOM 1753 C GLU A 221 26.029 4.176 32.067 1.0018.67 C
ATOM 1754 O GLUA221 24.896 3.823 31.788 1.0018.71 O
ATOM 1755 N VALA222 26.885 4.619 31.148 1.0017.89 N
ATOM 1756 CA VAL A 222 26.564 4.518 29.716 1.0017.33 C
ATOM 1757 CB VAL A 222 27.601 5.23428.813 1.0016.45 C
ATOM 1758 CG1 VAL A 222 27.349 4.920 27.348 1.0016.15 C
ATOM 1759 CG2 VAL A 222 27.562 6.724 29.032 1.0018.23 C
ATOM 1760 C VALA222 26.484 3.047 29.324 1.0016.91 C
ATOM 1761 O VALA222 25.538 2.613 28.664 1.0016.62 O
ATOM 1762 N ASP A 223 27.482 2.277 29.749 1.0017.14 N
ATOM 1763 CA ASP A 223 27.481 0.83029.527 1.0017.44 C
ATOM 1764 CB ASP A 223 28.718 0.199 30.164 1.0018.07 C
ATOM 1765 CG ASPA223 28.862 -1.277 29.840 1.0020.10 C
ATOM 1766 OD1 ASP A 223 28.684 -1.671 28.667 1.0023.48 O
ATOM 1767 OD2 ASP A 223 29.158 -2.117 30.704 1.0023.82 O
ATOM 1768 C ASP A 223 26.197 0.176 30.068 1.0017.00 C
ATOM 1769 O ASPA223 25.614 -0.679 29.418 1.0017.23 O
ATOM 1770 N ALAA224 25.760 0.606 31.250 1.0017.27 N
ATOM 1771 CA ALA A 224 24.546 0.063 31.880 1.0016.90 C
ATOM 1772 CB ALA A 224 24.466 0.50833.336 1.0016.05 C
ATOM 1773 C ALAA224 23.268 0.45431.131 1.0016.23 C
ATOM 17740 ALAA224 22.372 -0.368 30.966 1.0016.54 O
ATOM 1775 N VAL A 225 23.190 1.71030.682 1.0015.83 N
ATOM 1776 CA VALA225 22.056 2.16829.865 1.0014.67 C
ATOM 1777 CB VAL A 225 22.165 3.67929.521 1.0015.23 C
ATOM 1778 CG1VALA225 21.192 4.068 28.398 1.0013.57 C
ATOM 1779 CG2 VAL A 225 21.921 4.540 30.760 1.0014.67 C
ATOM 1780 C VALA225 21.943 1.34228.586 1.0015.30 C
ATOM 1781 O VALA225 20.853 0.86928.223 1.0015.31 O
ATOM 1782 N LEUA226 23.080 1.151 27.920 1.0015.01 N
ATOM 1783 CA LEU A226 23.159 0.30526.731 1.0015.71 C
ATOM 1784 CB LEUA226 24.583 0.30326.184 1.0015.33 C
ATOM 1785 CG LEU A226 24.925 0.708 24.740 1.0019.97 C
ATOM 1786 CD1 LEU A 226 23.707 0.961 23.845 1.0018.33 C
ATOM 1787 CD2 LEU A 226 25.851 1.919 24.766 1.0018.27 C
ATOM 1788 C LEUA226 22.736 -1.130 27.035 1.0015.63 C
ATOM 1789 0 LEU A 226 22.017 -1.73926.256 1.0015.27 O
ATOM 1790 N SERA227 23.194 -1.665 28.165 1.0015.87 N
ATOM 1791 CA SERA227 22.808 -3.018 28.580 1.0016.70 C
ATOM 1792 CB SER A 227 23.467 -3.393 29.909 1.0017.00 C
ATOM 1793 OG SERA227 24.839 -3.651 29.719 1.0019.89 O
ATOM 1794 C SERA227 21.303 -3.16228.712 1.0016.08 C
ATOM 1795 O SERA227 20.727 -4.131 28.221 1.0016.46 O
ATOM 1796 N TRPA228 20.671 -2.193 29.370 1.0016.20 N
ATOM 1797 CA TRPA228 19.226 -2.252 29.619 1.0016.15 C
ATOM 1798 CB TRP A 228 18.789 -1.174 30.631 1.0015.62 C
ATOM 1799 CG TRPA228 18.950 -1.612 32.094 1.0018.85 C
ATOM 1800 CD1TRPA228 19.961 -1.254 32.964 1.0019.26 C
ATOM 1801 NE1TRPA228 19.769 -1.854 34.191 1.0019.23 N
ATOM 1802 CE2 TRP A 228 18.640 -2.633 34.144 1.0018.47 C
ATOM 1803 CD2 TRP A 228 18.093 -2.508 32.835 1.0019.27 C
ATOM 1804 CE3 TRP A 228 16.912 -3.212 32.532 1.0019.66 C
ATOM 1805 CZ3 TRP A 228 16.322 -4.017 33.532 1.0018.74 C
ATOM 1806 CH2 TRP A 228 16.899 -4.113 34.819 1.0016.46 C
ATOM 1807 CZ2 TRP A 228 18.048 -3.430 35.142 1.0019.23 C
ATOM 1808 C TRPA228 18.432 -2.141 28.308 1.0016.47 C
ATOM 1809 O TRP A 228 17.532 -2.945 28.050 1.0015.65 O
ATOM 1810 N LEUA229 18.795 -1.170 27.469 1.0015.56 N
ATOM 1811 CA LEU A229 18.068 -0.923 26.221 1.0015.18 C
ATOM 1812 CB LEU A229 18.513 0.40525.591 1.0014.25 C
ATOM 1813 CG LEU A 229 17.941 1.647 26.291 1.0014.55 C
ATOM 1814 CD1 LEU A 229 18.497 2.954 25.702 1.0012.79 C
ATOM 1815 CD2 LEU A 229 16.404 1.641 26.250 1.0013.36 C
ATOM 1816 C LEUA229 18.216 -2.081 25.231 1.0015.15 C
ATOM 1817 O LEU A 229 17.256 -2.450 24.576 1.0013.87 O
ATOM 1818 N LEU A 230 19.408 -2.67625.162 1.0016.20 N
ATOM 1819 CA LEU A230 19.655 -3.80524.256 1.0018.02 C
ATOM 1820 CB LEUA230 21.155 -4.13824.189 1.0017.78 C
ATOM 1821 CG LEU A 230 22.005 -3.137 23.391 1.0017.79 C
ATOM 1822 CD1 LEU A 230 23.483 -3.31723.715 1.0018.38 C
ATOM 1823 CD2 LEU A 230 21.739 -3.25821.879 1.0017.08 C
ATOM 1824 C LEU A 230 18.849 -5.05824.616 1.0019.51 C
ATOM 1825 O LEU A 230 18.764 -5.991 23.813 1.0020.72 O
ATOM 1826 N GLU A 231 18.263 -5.07225.813 1.0021.12 N
ATOM 1827 CA GLUA231 17.268 -6.087 26.188 1.0023.85 C
ATOM 1828 CB GLU A 231 16.880 -5.963 27.668 1.0023.88 C
ATOM 1829 CG GLUA231 17.990 -6.273 28.666 1.0028.22 C
ATOM 1830 CD GLU A 231 18.349 -7.744 28.694 1.0033.44 C
ATOM 1831 OE1 GLUA231 19.336 -8.129 28.034 1.0034.56 O
ATOM 1832 OE2 GLU A 231 17.634 -8.518 29.368 1.0039.47 O
ATOM 1833 C GLU A 231 16.000 -5.974 25.344 1.0023.76 C
ATOM 1834 O GLUA231 15.284 -6.958 25.152 1.0024.75 O
ATOM 1835 N TYR A 232 15.715 -4.765 24.858 1.0023.17 N
ATOM 1836 CA TYRA232 14.427 -4.485 24.218 1.0022.01 C
ATOM 1837 CB TYR A 232 13.731 -3.302 24.914 1.0023.13 C
ATOM 1838 CG TYR A 232 13.591 -3.448 26.425 1.00 26.69 C
ATOM 1839 CD1 TYR A 232 14.434 -2.760 27.289 1.00 30.11 C
ATOM 1840 CE1 TYR A 232 14.313 -2.880 28.677 1.00 33.61 C
ATOM 1841 CZ TYR A 232 13.333 -3.699 29.214 1.00 36.43 C
ATOM 1842 OH TYR A 232 13.225 -3.823 30.590 1.00 39.68 O
ATOM 1843 CE2 TYR A 232 12.469 -4.391 28.378 1.00 34.55 C
ATOM 1844 CD2 TYR A 232 12.598 -4.259 26.985 1.00 33.70 C
ATOM 1845 C TYR A 232 14.515 -4.233 22.703 1.00 21.17 C
ATOM 1846 O TYR A 232 13.574 -4.545 21.967 1.00 20.35 O
ATOM 1847 N ALA A 233 15.632 -3.670 22.235 1.00 19.39 N
ATOM 1848 CA ALA A 233 15.697 -3.166 20.861 1.00 17.99 C
ATOM 1849 CB ALA A 233 14.771 -1.926 20.711 1.00 17.70 C
ATOM 1850 C ALA A 233 17.122 -2.820 20.434 1.00 17.14 C
ATOM 1851 O ALA A 233 17.990 -2.622 21.289 1.00 17.25 O
ATOM 1852 N PRO A 234 17.374 -2.749 19.121 1.00 17.05 N
ATOM 1853 CA PRO A 234 18.675 -2.288 18.626 1.00 15.93 C
ATOM 1854 CB PRO A 234 18.461 -2.167 17.118 1.00 16.60 C
ATOM 1855 CG PRO A 234 17.295 -3.083 16.823 1.00 18.34 C
ATOM 1856 CD PRO A 234 16.429 -3.032 18.023 1.00 16.70 C
ATOM 1857 C PRO A 234 18.936 -0.918 19.222 1.00 14.27 C
ATOM 1858 O PRO A 234 18.039 -0.076 19.186 1.00 12.98 O
ATOM 1859 N SER A 235 20.110 -0.731 19.815 1.00 12.71 N
ATOM 1860 CA SER A 235 20.416 0.468 20.569 1.00 11.98 C
ATOM 1861 CB SER A 235 20.150 0.247 22.062 1.00 12.25 C
ATOM 1862 OG SER A 235 18.785 -0.096 22.300 1.00 12.43 O
ATOM 1863 C SER A 235 21.869 0.865 20.346 1.00 11.16 C
ATOM 1864 0 SER A 235 22.747 0.005 20.251 1.00 10.16 O
ATOM 1865 N ARG A 236 22.120 2.163 20.240 1.00 10.05 N
ATOM 1866 CA ARG A 236 23.489 2.657 20.042 1.00 11.06 C
ATOM 1867 CB ARG A 236 23.880 2.774 18.554 1.00 10.96 C
ATOM 1868 CG ARG A 236 23.324 1.791 17.596 1.00 14.29 C
ATOM 1869 CD ARG A 236 23.838 2.008 16.152 1.00 11.64 C
ATOM 1870 NE ARG A 236 22.997 2.910 15.357 1.00 10.44 N
ATOM 1871 CZ ARG A 236 21.792 2.581 14.904 1.00 12.67 C
ATOM 1872 NH1 ARG A 236 21.284 1.386 15.186 1.00 13.03 N
ATOM 1873 NH2 ARG A 236 21.094 3.435 14.173 1.00 10.74 N
ATOM 1874 C ARG A 236 23.673 4.026 20.642 1.00 9.79 C
ATOM 1875 0 ARG A 236 22.709 4.740 20.877 1.00 10.92 O
ATOM 1876 N LEU A 237 24.932 4.388 20.852 1.00 8.40 N
ATOM 1877 CA LEU A 237 25.314 5.734 21.209 1.00 8.42 C
ATOM 1878 CB LEUA237 26.805 5.770 21.514 1.00 8.44 C
ATOM 1879 CG LEUA237 27.328 6.921 22.360 1.0010.14 C
ATOM 1880 CD1 LEUA237 27.162 6.59523.829 1.00 8.08 C
ATOM 1881 CD2LEUA237 28.786 7.18922.030 1.009.27 C
ATOM 1882 C LEUA237 25.030 6.689 20.061 1.00 8.13 C
ATOM 1883 O LEU A 237 25.182 6.317 18.894 1.007.76 O
ATOM 1884 N THR A 238 24.636 7.918 20.391 1.00 6.88 N
ATOM 1885 CA THR A 238 24.633 9.000 19.421 1.00 6.96 C
ATOM 1886 CB THR A 238 23.253 9.691 19.369 1.00 6.81 C
ATOM 1887 OG1 THR A 238 23.316 10.825 18.488 1.00 7.94 O
ATOM 1888 CG2THRA238 22.888 10.293 20.735 1.005.04 C
ATOM 1889 C THR A 238 25.751 9.996 19.756 1.007.43 C
ATOM 1890 O THRA238 26.117 10.161 20.930 1.008.32 O
ATOM 1891 N GLYA239 26.295 10.645 18.729 1.007.19 N
ATOM 1892 CA GLY A 239 27.414 11.556 18.894 1.00 8.76 C
ATOM 1893 C GLY A 239 28.560 10.893 19.644 1.00 9.66 C
ATOM 1894 O GLY A 239 28.877 9.719 19.405 1.00 9.27 O
ATOM 1895 N THR A 240 29.163 11.633 20.570 1.00 9.95 N
ATOM 1896 CA THRA240 30.153 11.049 21.481 1.0011.41 C
ATOM 1897 CB THR A 240 31.362 11.996 21.686 1.0011.58 C
ATOM 1898 OG1THRA240 30.904 13.317 21.989 1.0013.09 O
ATOM 1899 CG2THRA240 32.135 12.177 20.373 1.0010.86 C
ATOM 1900 C THRA240 29.533 10.66722.833 1.0012.08 C
ATOM 1901 O THR A 240 30.255 10.477 23.811 1.0013.49 O
ATOM 1902 N GLY A 241 28.204 10.543 22.883 1.0011.62 N
ATOM 1903 CA GLYA241 27.507 10.214 24.125 1.0010.88 C
ATOM 1904 C GLYA241 27.329 11.433 25.018 1.0011.55 C
ATOM 1905 O GLY A 241 27.760 12.517 24.643 1.0012.45 O
ATOM 1906 N ALAA242 26.721 11.287 26.197 1.0011.33 N
ATOM 1907 CA ALA A 242 26.340 10.005 26.803 1.0012.02 C
ATOM 1908 CB ALA A 242 26.246 10.169 28.329 1.0012.76 C
ATOM 1909 C ALAA242 25.037 9.38526.295 1.0011.45 C
ATOM 1910 O ALAA242 24.721 8.24226.654 1.0011.11 O
ATOM 1911 N CYSA243 24.264 10.127 25.501 1.0010.77 N
ATOM 1912 CA CYS A 243 22.940 9.633 25.097 1.0010.78 C
ATOM 1913 CB CYS A 243 22.115 10.715 24.388 1.0011.02 C
ATOM 1914 SG CYSA243 21.590 12.075 25.476 1.0015.33 S
ATOM 1915 C CYSA243 23.018 8.375 24.230 1.0010.16 C
ATOM 1916 O CYS A 243 23.898 8.225 23.370 1.00 9.99 O
ATOM 1917 N VALA244 22.073 7.488 24.482 1.0010.16 N
ATOM 1918 CA VAL A 244 21.918 6.24523.770 1.0010.48 C
ATOM 1919 CB VALA244 22.195 5.04524.722 1.0010.82 C
ATOM 1920 CG1 VAL A 244 21.762 3.736 24.103 1.0011.97 C
ATOM 1921 CG2VALA244 23.695 4.995 25.111 1.0010.40 C
ATOM 1922 C VAL A 244 20.488 6.21923.266 1.00 9.76 C
ATOM 1923 0 VAL A 244 19.599 6.719 23.945 1.0011.42 O
ATOM 1924 N PHE A 245 20.264 5.70722.062 1.00 9.99 N
ATOM 1925 CA PHEA245 18.906 5.549 21.557 1.00 9.97 C
ATOM 1926 CB PHE A 245 18.644 6.461 20.342 1.00 9.92 C
ATOM 1927 CG PHEA245 19.541 6.189 19.150 1.00 9.86 C
ATOM 1928 CD1 PHE A 245 19.132 5.337 18.133 1.00 9.54 C
ATOM 1929 CE1 PHE A 245 19.944 5.092 17.020 1.00 9.37 C
ATOM 1930 CZ PHEA245 21.166 5.721 16.908 1.00 9.85 C
ATOM 1931 CE2PHEA245 21.585 6.590 17.909 1.0010.22 C
ATOM 1932 CD2PHEA245 20.763 6.828 19.023 1.0010.76 C
ATOM 1933 C PHE A 245 18.597 4.090 21.214 1.00 9.77 C
ATOM 1934 0 PHE A 245 19.481 3.337 20.806 1.0010.99 O
ATOM 1935 N ALAA246 17.346 3.703 21.413 1.0011.01 N
ATOM 1936 CA ALA A 246 16.842 2.416 20.953 1.0011.95 C
ATOM 1937 CB ALAA246 16.153 1.691 22.070 1.0010.70 C
ATOM 1938 C ALA A 246 15.874 2.680 19.828 1.0012.89 C
ATOM 1939 0 ALAA246 15.100 3.639 19.905 1.0012.92 O
ATOM 1940 N GLUA247 15.914 1.831 18.796 1.0014.92 N
ATOM 1941 CA GLU A247 15.095 1.993 17.584 1.0017.26 C
ATOM 1942 CB GLU A 247 15.894 1.620 16.325 1.0018.31 C
ATOM 1943 CG GLU A 247 17.155 2.429 16.096 1.0023.10 C
ATOM 1944 CD GLUA247 17.913 2.014 14.841 1.0027.88 C
ATOM 1945 OE1 GLU A 247 18.058 0.798 14.579 1.0028.57 O
ATOM 1946 OE2GLUA247 18.378 2.915 14.119 1.0032.83 O
ATOM 1947 C GLUA247 13.828 1.145 17.619 1.0018.04 C
ATOM 1948 O GLUA247 13.866 -0.019 18.000 1.0018.06 O
ATOM 1949 N PHEA248 12.713 1.741 17.191 1.0017.85 N
ATOM 1950 CA PHE A 248 11.416 1.078 17.167 1.0017.89 C
ATOM 1951 CB PHEA248 10.566 1.513 18.360 1.0016.88 C
ATOM 1952 CG PHE A 248 11.162 1.163 19.688 1.0015.00 C
ATOM 1953 CD1 PHE A 248 11.902 2.097 20.398 1.0012.29 C
ATOM 1954 CE1 PHE A 248 12.461 1.772 21.636 1.0015.53 C
ATOM 1955 CZ PHE A 248 12.275 0.48622.173 1.0013.47 C
ATOM 1956 CE2PHEA248 11.545 -0.454 21.470 1.0013.84 C
ATOM 1957 CD2PHEA248 10.992 -0.11420.226 1.0014.98 C
ATOM 1958 C PHEA248 10.674 1.413 15.880 1.0019.35 C
ATOM 1959 O PHEA248 10.860 2.491 15.307 1.0018.25 O
ATOM 1960 N ASP A 249 9.820 0.493 15.441 1.0020.87 N
ATOM 1961 CA ASP A 249 8.978 0.714 14.271 1.0022.26 C
ATOM 1962 CB ASP A 249 8.447 -0.619 13.734 1.0023.28 C
ATOM 1963 CG ASP A 249 9.455 -1.352 12.883 1.0025.57 C
ATOM 1964 OD1 ASP A 249 10.484 -0.748 12.503 1.0027.22 O
ATOM 1965 OD2 ASP A 249 9.302 -2.547 12.539 1.0033.57 O
ATOM 1966 C ASP A 249 7.809 1.643 14.582 1.0022.36 C
ATOM 1967 O ASPA249 7.382 2.409 13.724 1.0023.61 O
ATOM 1968 N THR A 250 7.289 1.571 15.806 1.0021.65 N
ATOM 1969 CA THRA250 6.106 2.344 16.184 1.0021.51 C
ATOM 1970 CB THR A 250 4.860 1.427 16.363 1.0021.75 C
ATOM 1971 OG1THRA250 5.086 0.516 17.451 1.0022.13 O
ATOM 1972 CG2THRA250 4.648 0.509 15.147 1.0021.42 C
ATOM 1973 C THR A 250 6.315 3.123 17.466 1.0020.97 C
ATOM 1974 O THR A 250 7.183 2.798 18.272 1.0020.85 O
ATOM 1975 N GLUA251 5.480 4.135 17.658 1.0020.83 N
ATOM 1976 CA GLU A 251 5.446 4.916 18.887 1.0021.33 C
ATOM 1977 CB GLU A 251 4.479 6.083 18.723 1.0021.44 C
ATOM 1978 CG GLUA251 4.351 6.977 19.940 1.0021.84 C
ATOM 1979 CD GLU A 251 3.440 8.160 19.692 1.0024.43 C
ATOM 1980 OE1 GLU A 251 2.807 8.207 18.617 1.0028.85 O
ATOM 1981 OE2GLUA251 3.357 9.03620.569 1.0025.86 O
ATOM 1982 C GLU A 251 5.026 4.08020.100 1.0021.34 C
ATOM 1983 O GLU A 251 5.556 4.263 21.205 1.0021.10 O
ATOM 1984 N SER A 252 4.062 3.185 19.897 1.0021.47 N
ATOM 1985 CA SER A 252 3.478 2.420 21.007 1.0021.05 C
ATOM 1986 CBASERA252 2.243 1.63720.5420.5021.15 C
ATOM 1987 CBBSERA252 2.249 1.62720.5370.5021.07 C
ATOM 1988 OGASERA252 1.055 2.236 21.0380.5021.83 O
ATOM 1989 OGBSERA252 2.566 0.775 19.4500.5021.09 O
ATOM 1990 C SERA252 4.497 1.483 21.664 1.0020.23 C
ATOM 1991 O SER A 252 4.575 1.41822.882 1.0019.85 O
ATOM 1992 N GLU A 253 5.286 0.779 20.862 1.0019.84 N
ATOM 1993 CA GLUA253 6.337 -0.06221.427 1.0020.01 C
ATOM 1994 CB GLU A 253 6.993 -0.926 20.355 1.0020.34 C
ATOM 1995 CG GLU A 253 7.696 -2.144 20.946 1.0023.27 C
ATOM 1996 CD GLU A253 8.589 -2.861 19.957 1.0027.04 C
ATOM 1997 OE1 GLUA253 8.402 -2.682 18.724 1.0030.27 O
ATOM 1998 OE2 GLU A 253 9.473 -3.617 20.418 1.00 25.72 O
ATOM 1999 C GLU A 253 7.397 0.760 22.183 1.00 19.47 c
ATOM 2000 O GLU A 253 7.801 0.398 23.291 1.00 19.21 O
ATOM 2001 N ALA A 254 7.819 1.876 21.594 1.00 18.01 N
ATOM 2002 CA ALA A 254 8.807 2.749 22.230 1.00 16.85 C
ATOM 2003 CB ALA A 254 9.129 3.939 21.320 1.00 14.68 C
ATOM 2004 C ALA A 254 8.334 3.225 23.603 1.00 16.50 C
ATOM 2005 O ALA A 254 9.090 3.181 24.584 1.00 15.50 O
ATOM 2006 N ARG A 255 7.076 3.661 23.678 1.00 16.70 N
ATOM 2007 CA ARG A 255 6.527 4.196 24.924 1.00 18.42 C
ATOM 2008 CB ARG A 255 5.228 4.964 24.660 1.00 19.55 C
ATOM 2009 CG ARG A 255 5.468 6.289 23.967 1.00 20.16 C
ATOM 2010 CD ARG A 255 4.326 7.300 24.058 1.00 24.89 C
ATOM 2011 NE ARG A 255 4.603 8.439 23.189 1.00 26.90 N
ATOM 2012 CZ ARG A 255 5.389 9.457 23.518 1.00 28.00 C
ATOM 2013 NH1 ARG A 255 5.948 9.505 24.719 1.00 28.74 N
ATOM 2014 NH2 ARG A 255 5.601 10.442 22.652 1.00 28.42 N
ATOM 2015 C ARG A 255 6.291 3.109 25.964 1.00 19.47 C
ATOM 2016 O ARG A 255 6.338 3.372 27.164 1.00 19.54 O
ATOM 2017 N GLN A 256 6.049 1.886 25.502 1.00 20.64 N
ATOM 2018 CA AGLN A 256 5.858 0.767 26.418 0.50 21.19 C
ATOM 2019 CA BGLN A 256 5.870 0.742 26.398 0.50 21.17 C
ATOM 2020 CB AGLN A 256 5.106 -0.382 25.721 0.50 21.61 C
ATOM 2021 CB BGLN A 256 5.236 -0.432 25.652 0.50 21.54 C
ATOM 2022 CG AGLN A 256 5.890 -1.667 25.498 0.50 23.81 C
ATOM 2023 CG BGLN A 256 4.313 -1.297 26.508 0.50 23.82 C
ATOM 2024 CD AGLN A 256 5.171 -2.636 24.566 0.50 27.16 C
ATOM 2025 CD BGLN A 256 4.294 -2.750 26.062 0.50 26.35 C
ATOM 2026 OE1AGLN 256 4.085 -2.334 24.056 0.50 27.95 O
ATOM 2027 OE1BGLN A 256 3.237 -3.289 25.733 0.50 27.75 O
ATOM 2028 NE2AGLN A 256 5.774 -3.799 24.343 0.50 28.63 N
ATOM 2029 NE2BGL A 256 5.463 -3.385 26.048 0.50 26.86 N
ATOM 2030 C GLN A 256 7.204 0.328 27.018 1.00 20.91 C
ATOM 2031 O GLN A 256 7.268 -0.066 28.184 1.00 21.25 O
ATOM 2032 N VAL A 257 8.280 0.441 26.235 1.00 20.11 N
ATOM 2033 CA VAL A 257 9.614 0.128 26.734 1.00 18.87 C
ATOM 2034 CB VAL A 257 10.643 -0.068 25.574 1.00 18.45 C
ATOM 2035 CG1 VAL A 257 12.075 -0.027 26.089 1.00 17.54 C
ATOM 2036 CG2 VAL A 257 10.387 -1.379 24.870 1.00 16.12 C
ATOM 2037 C VAL A 257 10.053 1.215 27.726 1.00 19.34 C
ATOM 2038 O VAL A 257 10.706 0.925 28.738 1.00 19.11 O
ATOM 2039 N LEU A 258 9.635 2.450 27.460 1.00 18.46 N
ATOM 2040 CA LEU A 258 9.894 3.569 28.368 1.00 20.10 C
ATOM 2041 CB LEU A 258 9.437 4.891 27.733 1.00 18.63 C
ATOM 2042 CG LEU A 258 9.765 6.157 28.533 1.00 20.53 C
ATOM 2043 CD1 LEU A 258 11.276 6.280 28.755 1.00 18.26 C
ATOM 2044 CD2 LEU A 258 9.202 7.402 27.851 1.00 21.08 C
ATOM 2045 C LEU A 258 9.258 3.409 29.761 1.00 20.34 C
ATOM 2046 O LEU A 258 9.863 3.778 30.764 1.00 20.01 O
ATOM 2047 N GLU A 259 8.036 2.880 29.806 1.00 22.80 N
ATOM 2048 CA GLU A 259 7.354 2.576 31.073 1.00 25.10 C
ATOM 2049 CB GLU A 259 5.925 2.088 30.822 1.00 25.98 C
ATOM 2050 CG GLU A 259 4.955 3.131 30.291 1.00 30.83 C
ATOM 2051 CD GLU A 259 3.597 2.528 29.961 1.00 39.30 C
ATOM 2052 OE1 GLU A 259 3.340 2.231 28.766 1.00 42.04 O
ATOM 2053 OE2 GLU A 259 2.790 2.334 30.901 1.00 40.70 O
ATOM 2054 C GLU A 259 8.089 1.505 31.867 1.00 25.43 C
ATOM 2055 O GLU A 259 8.094 1.536 33.098 1.00 26.77 O
ATOM 2056 N GLN A 260 8.701 0.561 31.153 1.00 25.64 N
ATOM 2057 CA GLN A 260 9.363 -0.594 31.757 1.00 26.63 C
ATOM 2058 CB GLN A 260 9.465 -1.724 30.741 1.00 27.53 C
ATOM 2059 CG GLN A 260 8.206 -2.521 30.538 1.00 31.29 C
ATOM 2060 CD GLN A 260 8.368 -3.567 29.454 1.00 37.11 C
ATOM 2061 OE1 GLN A 260 9.328 -4.341 29.469 1.00 40.26 O
ATOM 2062 NE2 GLN A 260 7.438 -3.591 28.506 1.00 39.00 N
ATOM 2063 C GLN A 260 10.767 -0.274 32.249 1.00 26.62 C
ATOM 2064 O GLN A 260 11.239 -0.844 33.239 1.00 25.81 O
ATOM 2065 N ALA A 261 11.437 0.628 31.540 1.00 26.28 N
ATOM 2066 CA ALA A 261 12.857 0.887 31.759 1.00 25.09 C
ATOM 2067 CB ALA A 261 13.437 1.703 30.587 1.00 25.42 C
ATOM 2068 C ALA A 261 13.106 1.590 33.088 1.00 23.76 C
ATOM 2069 O ALAA 261 12.223 2.275 33.605 1.00 22.79 O
ATOM 2070 N PRO A 262 14.306 1.412 33.645 1.00 22.80 N
ATOM 2071 CA PRO A 262 14.688 2.086 34.886 1.00 22.46 C
ATOM 2072 CB PRO A 262 16.187 1.803 34.985 1.00 21.98 C
ATOM 2073 CG PRO A 262 16.380 0.543 34.249 1.00 21.91 C
ATOM 2074 CD PRO A 262 15.391 0.558 33.125 1.00 22.82 C
ATOM 2075 C PRO A 262 14.456 3.592 34.785 1.00 22.89 C
ATOM 2076 O PRO A 262 14.701 4.181 33.728 1.00 23.26 O
ATOM 2077 N GLU A 263 13.998 4.204 35.863 1.00 22.70 N
ATOM 2078 CA GLUA263 13.716 5.636 35.862 1.0023.61 C
ATOM 2079 CB GLU A 263 12.993 6.032 37.151 1.0025.25 C
ATOM 2080 CG GLU A 263 11.545 5.551 37.209 1.0031.45 C
ATOM 2081 CD GLU A 263 11.047 5.354 38.634 1.0039J2 C
ATOM 2082 OE1 GLU A 263 11.247 6.270 39.471 1.0042.28 O
ATOM 2083 OE2GLUA263 10.453 4.284 38.918 1.0042.07 O
ATOM 2084 C GLU A 263 14.984 6.481 35.678 1.0021.97 C
ATOM 2085 O GLU A 263 14.931 7.575 35.103 1.0021.53 O
ATOM 2086 N TRPA264 16.121 5.966 36.147 1.0019.48 N
ATOM 2087 CA TRP A 264 17.404 6.66635.984 1.0018.71 C
ATOM 2088 CB TRP A 264 18.482 6.08336.923 1.0018.27 C
ATOM 2089 CG TRPA264 18.715 4.581 36.812 1.0016.89 C
ATOM 2090 CD1TRPA264 18.089 3.601 37.530 1.0015.89 C
ATOM 2091 NE1TRPA264 18.581 2.365 37.183 1.0012.38 N
ATOM 2092 CE2 TRP A 264 19.548 2.523 36.224 1.0016.69 C
ATOM 2093 CD2 TRP A 264 19.671 3.910 35.976 1.0016.35 C
ATOM 2094 CE3TRPA264 20.622 4.338 35.036 1.0019.17 C
ATOM 2095 CZ3TRPA264 21.407 3.377 34.381 1.0020.09 C
ATOM 2096 CH2TRPA264 21.250 2.010 34.649 1.0018.64 C
ATOM 2097 CZ2 TRP A 264 20.331 1.564 35.566 1.0018.99 C
ATOM 2098 C TRPA264 17.920 6.701 34.532 1.0018.48 C
ATOM 2099 O TRPA264 18.957 7.313 34.263 1.0020.07 O
ATOM 2100 N LEUA265 17.211 6.04933.603 1.0017.40 N
ATOM 2101 CA LEUA265 17.523 6.198 32.178 1.0017.32 C
ATOM 2102 CB LEU A265 16.800 5.163 31.304 1.0017.52 C
ATOM 2103 CG LEU A 265 17.259 3.695 31.229 1.0019.49 C
ATOM 2104 CD1 LEU A 265 17.191 3.17429.799 1.0021.52 C
ATOM 2105 CD2 LEU A 265 18.638 3.497 31.790 1.0019.20 C
ATOM 2106 C LEU 265 17.153 7.58931.683 1.0016.84 C
ATOM 2107 O LEUA265 17.614 7.999 30.628 1.0016.62 O
ATOM 2108 N AS A266 16.307 8.297 32.441 1.0016.01 N
ATOM 2109 CA ASN A266 15.850 9.63232.072 1.0017.11 C
ATOM 2110 CB ASN A 266 16.956 10.67532.274 1.0017.89 C
ATOM 2111 CG ASNA266 17.404 10.778 33.706 1.0022.13 C
ATOM 2112 OD1 ASN A 266 16.632 11.167 34.581 1.0027.44 O
ATOM 2113 ND2AS A266 18.668 10.44233.958 1.0024.21 N
ATOM 2114 C ASNA266 15.393 9.678 30.631 1.0016.11 C
ATOM 2115 O AS A266 15.811 10.55529.877 1.0017.28 O
ATOM 2116 N GLYA267 14.556 8.723 30.241 1.0015.27 N
ATOM 2117 CA GLY A 267 14.241 8.523 28.832 1.0014.29 C
ATOM 2118 C GLYA267 13.153 9.434 28.291 1.0013.92 C
ATOM 2119 0 GLYA267 12.301 9.913 29.042 1.0012.25 O
ATOM 2120 N PHEA268 13.202 9.69226.984 1.0012.44 N
ATOM 2121 CA PHE A 268 12.071 10.276 26.281 1.0012.24 C
ATOM 2122 CB PHE A 268 12.244 11.807 26.079 1.0012.14 C
ATOM 2123 CG PHE A 268 13.355 12.197 25.109 1.0012.74 C
ATOM 2124 CD1 PHEA268 13.135 12.201 23.733 1.0013.82 C
ATOM 2125 CE1 PHE A 268 14.151 12.57422.832 1.0010.04 C
ATOM 2126 CZ PHE A 268 15.384 12.978 23.308 1.00 8.20 C
ATOM 2127 CE2PHEA268 15.618 13.000 24.693 1.0012.44 C
ATOM 2128 CD2PHEA268 14.597 12.612 25.583 1.0013.53 C
ATOM 2129 C PHEA268 11.885 9.536 24.964 1.0012.25 C
ATOM 2130 O PHEA268 12.816 8.88824.473 1.0012.16 O
ATOM 2131 N VALA269 10.673 9.60524.423 1.0011.79 N
ATOM 2132 CA VAL A269 10.353 8.99823.134 1.0011.76 C
ATOM 2133 CB VAL A 269 9.101 8.07723.226 1.0012.07 C
ATOM 2134 CG1 VAL A 269 8.621 7.64821.834 1.00 8.84 C
ATOM 2135 CG2 VAL A 269 9.407 6.86424.053 1.0012.94 C
ATOM 2136 C VALA269 10.124 10.094 22.097 1.0012.32 C
ATOM 2137 O VALA269 9.458 11.095 22.385 1.0012.42 O
ATOM 2138 N ALAA270 10.710 9.919 20.910 1.0012.05 N
ATOM 2139 CA ALA A 270 10.530 10.862 19.811 1.0012.20 C
ATOM 2140 CB ALAA270 11.530 12.004 19.927 1.0011.87 C
ATOM 2141 C ALAA270 10.666 10.186 18.450 1.0011.86 C
ATOM 2142 O ALAA270 11.386 9.188 18.294 1.0011.43 O
ATOM 2143 N LYSA271 9.977 10.743 17.459 1.0011.86 N
ATOM 2144 CA LYSA271 10.062 10.242 16.105 1.0011.79 C
ATOM 2145 CB LYSA271 8.756 10.511 15.367 1.0012.88 C
ATOM 2146 CG LYSA271 8.617 9.745 14.062 1.0015.60 C
ATOM 2147 CD LYSA271 7.427 10.270 13.278 1.0022.79 C
ATOM 2148 CE LYS A 271 7.644 10.140 11.783 1.0025.31 C
ATOM 2149 NZ LYS A 271 7.479 8.730 11.352 1.0028.39 N
ATOM 2150 C LYS A 271 11.206 10.915 15.357 1.0011.93 C
ATOM 2151 O LYSA271 11.371 12.142 15.443 1.0011.36 O
ATOM 2152 N GLYA272 11.974 10.113 14.620 1.0010.27 N
ATOM 2153 CA GLYA272 12.970 10.616 13.682 1.0010.83 C
ATOM 2154 C GLYA272 12.316 11.157 12.411 1.0010.79 C
ATOM 21550 GLYA272 11.368 10.562 11.878 1.0011.56 O
ATOM 2156 N VALA273 12.783 12.310 11.955 1.00 8.91 N
ATOM 2157 CA VAL A 273 12.198 12.980 10.796 1.00 8.79 C
ATOM 2158 CB VALA273 11.205 14.137 11.170 1.00 8.61 C
ATOM 2159 CG1VALA273 9.887 13.594 11.736 1.0010.68 C
ATOM 2160 CG2VALA273 11.842 15.152 12.145 1.007.79 C
ATOM 2161 C VAL A 273 13.317 13.531 9.943 1.00 8.71 C
ATOM 2162 O VAL A 273 14.329 14.008 10.466 1.007.90 O
ATOM 2163 N ASNA274 13.142 13.446 8.631 1.007.86 N
ATOM 2164 CA ASNA274 14.175 13.857 7.690 1.007.96 C
ATOM 2165 CB AS A274 14.150 12.953 6.444 1.00 7.98 C
ATOM 2166 CG ASN A 274 14.606 11.551 6.756 1.00 8.94 C
ATOM 2167 OD1ASNA274 15.203 11.313 7.807 1.00 9.41 O
ATOM 2168 ND2ASNA274 14.319 10.610 5.863 1.00 6.15 N
ATOM 2169 C ASNA274 14.083 15.318 7.284 1.00 7.96 C
ATOM 2170 O ASN A 274 15.024 15.854 6.715 1.00 7.69 O
ATOM 2171 N LEU A 275 12.930 15.941 7.539 1.00 7.67 N
ATOM 2172 CA LEUA275 12.803 17.385 7.438 1.00 8.95 C
ATOM 2173 CB LEU A 275 11.532 17.788 6.668 1.00 8.51 C
ATOM 2174 CG LEU A 275 11.295 19.302 6.540 1.0011.22 C
ATOM 2175 CD1 LEUA275 12.247 19.910 5.531 1.00 9.61 C
ATOM 2176 CD2 LEU A 275 9.854 19.616 6.152 1.0014.10 C
ATOM 2177 C LEUA275 12.768 17.942 8.853 1.00 8.90 C
ATOM 2178 O LEU A 275 11.981 17.483 9.679 1.00 7.53 O
ATOM 2179 N SER A 276 13.642 18.896 9.152 1.00 8.50 N
ATOM 2180 CA SER A 276 13.704 19.447 10.514 1.009.75 C
ATOM 2181 CB SER A 276 14.831 20.478 10.630 1.00 8.28 C
ATOM 2182 OG SERA276 14.67821.252 11.808 1.0010.16 O
ATOM 2183 C SERA276 12.373 20.081 10.921 1.00 9.43 C
ATOM 2184 O SERA276 11.746 20.743 10.109 1.0010.07 O
ATOM 2185 N PRO A 277 11.922 19.842 12.156 1.00 9.61 N
ATOM 2186 CA PROA277 10.773 20.580 12.720 1.0010.01 C
ATOM 2187 CB PRO A 277 10.832 20.221 14.207 1.00 8.83 C
ATOM 2188 CG PRO A 277 11.388 18.827 14.217 1.00 8.69 C
ATOM 2189 CD PRO A 277 12.396 18.783 13.071 1.00 8.94 C
ATOM 2190 C PRO A 277 10.86822.104 12.541 1.00 9.96 C
ATOM 2191 O PRO A 277 9.826 22.757 12.403 1.00 9.01 O
ATOM 2192 N LEU A 278 12.087 22.660 12.540 1.0010.43 N
ATOM 2193 CA LEUA278 12.25624.104 12.315 1.0010.73 C
ATOM 2194 CB LEU A 278 13.73024.528 12.453 1.00 9.61 C
ATOM 2195 CG LEUA278 14.13425.962 12.079 1.00 9.91 C
ATOM 2196 CD1 LEUA278 13.44826.998 12.964 1.00 7.91 C
ATOM 2197 CD2LEUA278 15.65926.132 12.136 1.00 6.74 C
ATOM 2198 C LEUA278 11.70224.490 10.942 1.0012.35 C
ATOM 2199 O LEUA278 10.82625.360 10.829 1.0013.49 O
ATOM 2200 N HISA279 12.17323.802 9.910 1.0011.84 N
ATOM 2201 CA HIS A 279 11.750 24.098 8.541 1.0013.27 C
ATOM 2202 CB HIS A 279 12.712 23.440 7.546 1.0012.55 C
ATOM 2203 CG HIS A 279 14.116 23.938 7.690 1.0014.42 C
ATOM 2204 ND1 HIS A 279 14.715 24.753 6.756 1.0013.63 N
ATOM 2205 CE1 HIS A 279 15.929 25.070 7.170 1.0012.30 C
ATOM 2206 NE2 HIS A 279 16.12524.517 8.352 1.0012.76 N
ATOM 2207 CD2 HIS A 279 14.997 23.827 8.715 1.0011.29 C
ATOM 2208 C HISA279 10.29823.707 8.291 1.0013.99 C
ATOM 2209 O HIS A 279 9.590 24.401 7.571 1.0014.25 O
ATOM 2210 N ARGA280 9.86222.614 8.921 1.0015.54 N
ATOM 2211 CA ARGA280 8.47622.160 8.829 1.0017.09 C
ATOM 2212 CBAARGA280 8.286 20.843 9.597 0.5017.22 C
ATOM 2213 CBBARGA280 8.283 20.852 9.605 0.5016.73 C
ATOM 2214 CGAARGA280 6.856 20.286 9.572 0.5019.92 C
ATOM 2215 CGBARGA280 6.856 20.295 9.565 0.5017.78 C
ATOM 2216 CDAARGA280 6.728 18.883 8.978 0.5023.04 C
ATOM 2217 CDBARGA280 6.649 19.024 10.381 0.5016.96 C
ATOM 2218 NEAARGA280 5.935 18.885 7.751 0.5026.62 N
ATOM 2219 NEBARGA280 6.578 19.293 11.817 0.5018.35 N
ATOM 2220 CZAARGA280 6.094 18.027 6.744 0.5027.40 C
ATOM 2221 CZBARGA280 7.237 18.605 12.7520.5016.38 C
ATOM 2222 NH1AARGA280 7.025 17.079 6.805 0.5026.22 N
ATOM 2223 NH1BARGA280 8.028 17.593 12.415 0.5013.50 N
ATOM 2224 NH2AARGA280 5.321 18.118 5.670 0.5027.99 N
ATOM 2225 NH2BARGA280 7.101 18.929 14.030 0.5013.39 N
ATOM 2226 C ARGA280 7.512 23.233 9.341 1.0017.90 C
ATOM 2227 O ARG A 280 6.535 23.558 8.668 1.0018.51 O
ATOM 2228 N ALA A 281 7.823 23.815 10.500 1.0018.99 N
ATOM 2229 CA ALA A 281 7.027 24.913 11.073 1.0020.59 C
ATOM 2230 CB ALA A 281 7.537 25.271 12.466 1.0020.60 C
ATOM 2231 C ALAA281 6.98526.172 10.205 1.0022.44 C
ATOM 2232 O ALAA281 6.12527.031 10.403 1.0023.35 O
ATOM 2233 N MSE A 282 7.908 26.280 9.254 1.0023.24 N
ATOM 2234 CA MSE A 282 7.979 27.443 8.372 1.0025.52 C
ATOM 2235 CB MSEA282 9.433 27.857 8.167 1.0024.85 C
ATOM 2236 CG MSEA282 10.104 28.361 9.418 1.0026.30 C
ATOM 2237 SE MSE A 282 12.022 28.559 9.137 1.0038.08 SE
ATOM 2238 CE MSE A 282 11.971 30.307 8.185 1.00 26.29 C
ATOM 2239 C MSE A 282 7.328 27.195 7.007 1.00 26.73 c
ATOM 2240 O MSE A 282 7.415 28.035 6.111 1.00 26.62 o
ATOM 2241 N LEU A 283 6.707 26.032 6.846 1.00 28.39 N
ATOM 2242 CA LEU A 283 5.995 25.721 5.618 1.00 29.51 C
ATOM 2243 CB LEU A 283 5.746 24.216 5.488 1.00 29.19 C
ATOM 2244 CG LEU A 283 6.939 23.283 5.251 1.00 28.78 C
ATOM 2245 CD1 LEU A 283 6.454 21.860 5.117 1.00 24.65 C
ATOM 2246 CD2 LEU A 283 7.754 23.689 4.020 1.00 31.18 C
ATOM 2247 C LEU A 283 4.673 26.487 5.577 1.00 30.57 C
ATOM 2248 O LEU A 283 4.242 26.918 4.514 1.00 31.66 O
ATOM 2249 OXT LEU A 283 4.014 26.713 6.600 1.00 31.36 O
ATOM 2250 N MSE B 1 64.585 25.143 17.934 1.00 24.19 N
ATOM 2251 CA MSE B 1 65.118 26.485 18.350 1.00 24.01 C
ATOM 2252 CB MSE B 1 66.019 27.079 17.256 1.00 24.38 C
ATOM 2253 CG MSE B 1 67.242 26.213 16.901 1.00 28.04 C
ATOM 2254 SE MSE B 1 68.497 26.000 18.408 1.00 37.42 SE
ATOM 2255 CE MSE B 1 67.951 24.175 19.067 1.00 35.76 C
ATOM 2256 C MSE B 1 63.972 27.445 18.691 1.00 22.57 C
ATOM 2257 O MSE B 1 62.910 27.397 18.071 1.00 22.65 O
ATOM 2258 N ARG B 2 64.185 28.289 19.696 1.00 20.99 N
ATOM 2259 CA AARG B 2 63.260 29.370 20.005 0.50 20.26 C
ATOM 2260 CA BARG B 2 63.249 29.362 19.994 0.50 20.26 C
ATOM 2261 CB AARG B 2 63.452 29.834 21.448 0.50 20.73 C
ATOM 2262 CB BARG B 2 63.383 29.814 21.450 0.50 20.77 C
ATOM 2263 CG AARG B 2 62.183 29.873 22.293 0.50 23.00 C
ATOM 2264 CG BARG B 2 62.689 28.905 22.459 0.50 22.88 C
ATOM 2265 CD AARG B 2 62.393 30.430 23.706 0.50 26.15 C
ATOM 2266 CD BARG B 2 63.637 28.041 23.281 0.50 27.88 c
ATOM 2267 NE AARG B 2 63.237 31.624 23.694 0.50 29.24 N
ATOM 2268 NE BARG B 2 63.228 27.947 24,682 0.50 30.10 N
ATOM 2269 CZ AARG B 2 64.362 31.761 24.390 0.50 31.76 C
ATOM 2270 CZ BARG B 2 63.282 26.834 25.407 0.50 31.82 C
ATOM 2271 NH1AARG B 2 64.790 30.776 25.174 0.50 32.91 N
ATOM 2272 NH1 BARG B 2 63.723 25.705 24.867 0.50 32.05 N
ATOM 2273 NH2AARG B 2 65.064 32.887 24.302 0.50 31.44 N
ATOM 2274 NH2BARG B 2 62.887 26.846 26.676 0.50 32.35 N
ATOM 2275 C ARG B 2 63.496 30.533 19.047 1.00 19.05 C
ATOM 2276 O ARG B 2 64.629 30.965 18.868 1.00 18.37 O
ATOM 2277 N THR B 3 62.433 31.029 18.416 1.00 16.97 N
ATOM 2278 CA THR B 3 62.547 32.224 17.584 1.00 14.40 C
ATOM 2279 CB THR B 3 61.991 31.993 16.176 1.00 14.71 C
ATOM 2280 OG1 THR B 3 60.674 31.423 16.267 1.00 13.02 O
ATOM 2281 CG2 THR B 3 62.817 30.946 15.418 1.00 15.51 C
ATOM 2282 C THR B 3 61.807 33.384 18.243 1.00 14.40 C
ATOM 2283 O THR B 3 60.819 33.176 18.948 1.00 13.94 O
ATOM 2284 N GLN B 4 62.274 34.600 17.997 1.00 12.40 N
ATOM 2285 CA GLN B 4 61.686 35.779 18.607 1.00 12.71 C
ATOM 2286 CB GLN B 4 62.710 36.525 19.457 1.00 12.73 C
ATOM 2287 CG GLN B 4 63.081 35.845 20.744 1.00 15.70 C
ATOM 2288 CD GLN B 4 63.557 36.835 21.801 1.00 19.76 C
ATOM 2289 OE1 GLN B 4 63.983 37.945 21.477 1.00 20.13 O
ATOM 2290 NE2 GLN B 4 63.470 36.438 23.062 1.00 20.65 N
ATOM 2291 C GLN B 4 61.167 36.696 17.520 1.00 12.53 C
ATOM 2292 O GLN B 4 61.838 36.900 16.497 1.00 12.00 O
ATOM 2293 N TRP B 5 59.979 37.254 17.757 1.00 11.04 N
ATOM 2294 CA TRP B 5 59.240 38.021 16.756 1.00 10.27 C
ATOM 2295 CB TRP B 5 58.066 37.196 16.217 1.00 10.79 C
ATOM 2296 CG TRP B 5 58.473 35.860 15.670 1.00 10.09 C
ATOM 2297 CD1 TRP B 5 58.768 34.734 16.383 1.00 7.94 C
ATOM 2298 NE1 TRP B 5 59.121 33.713 15.531 1.00 10.62 N
ATOM 2299 CE2 TRP B 5 59.041 34.165 14.239 1.00 12.43 C
ATOM 2300 CD2 TRP B 5 58.641 35.520 14.292 1.00 10.87 C
ATOM 2301 CE3 TRP B 5 58.479 36.221 13.085 1.00 12.73 C
ATOM 2302 CZ3 TRP B 5 58.724 35.565 11.891 1.00 12.85 C
ATOM 2303 CH2 TRP B 5 59.123 34.211 11.876 1.00 12.53 C
ATOM 2304 CZ2 TRP B 5 59.284 33.500 13.036 1.00 11.61 C
ATOM 2305 C TRP B 5 58.713 39.330 17.350 1.00 10.89 C
ATOM 2306 O TRP B 5 58.162 39.330 18.457 1.00 11.12 O
ATOM 2307 N PRO B 6 58.901 40.439 16.633 1.00 10.15 N
ATOM 2308 CA PRO B 6 58.382 41.737 17.069 1.00 9.25 C
ATOM 2309 CB PRO B 6 58.959 42.719 16.029 1.00 9.77 C
ATOM 2310 CG PRO B 6 60.116 41.961 15.374 1.00 12.46 C
ATOM 2311 CD PRO B 6 59.665 40.536 15.372 1.00 10.41 C
ATOM 2312 C PRO B 6 56.865 41.768 17.019 1.00 8.09 C
ATOM 2313 O PRO B 6 56.250 41.149 16.138 1.00 6.49 O
ATOM 2314 N SER B 7 56.278 42.494 17.959 1.00 7.73 N
ATOM 2315 CA SER B 7 54.858 42.772 17.981 1.00 7.30 C
ATOM 2316 CB SER B 7 54.176 41.941 19.061 1.00 8.06 C
ATOM 2317 OG SER B 7 52.770 41.923 18.892 1.00 8.89 O
ATOM 2318 C SER B 7 54.718 44.248 18.284 1.00 7.35 C
ATOM 2319 O SER B 7 54.592 44.633 19.450 1.00 6.94 O
ATOM 2320 N PRO B 8 54.828 45.082 17.250 1.00 6.98 N
ATOM 2321 CA PRO B 8 54.907 46.538 17.438 1.00 8J0 C
ATOM 2322 CB PRO B 8 55.311 47.049 16.049 1.00 7.57 C
ATOM 2323 CG PRO B 8 54.750 46.006 15.091 1.00 8.96 C
ATOM 2324 CD PRO B 8 54.948 44.696 15.826 1.00 7.07 C
ATOM 2325 C PRO B 8 53.584 47.163 17.847 1.00 8.09 C
ATOM 2326 O PRO B 8 52.528 46.590 17.616 1.00 7.93 O
ATOM 2327 N ALA B 9 53.653 48.341 18.451 1.00 8.76 N
ATOM 2328 CA ALA B 9 52.468 49.145 18.686 1.00 9.31 C
ATOM 2329 CB ALA B 9 52.748 50.205 19.747 1.00 9.07 C
ATOM 2330 C ALA B 9 52.042 49.806 17.385 1.00 9.46 C
ATOM 2331 O ALA B 9 52.807 49.833 16.426 1.00 9.50 O
ATOM 2332 N LYS B 10 50.818 50.337 17.360 1.00 9.18 N
ATOM 2333 CA LYS B 10 50.413 51.294 16.336 1.00 8.90 C
ATOM 2334 CB LYS B 10 49.294 50.740 15.428 1.00 8.73 C
ATOM 2335 CG LYS B 10 47.996 50.287 16.151 1.00 8.30 C
ATOM 2336 CD LYS B 10 47.027 51.430 16.531 1.00 8.72 C
ATOM 2337 CE LYS B 10 45.717 50.865 17.106 1.00 6.86 C
ATOM 2338 NZ LYS B 10 44.855 51.938 17.735 1.00 8.49 N
ATOM 2339 C LYS B 10 49.959 52.593 16.978 1.00 8.97 C
ATOM 2340 O LYS B 10 49.640 52.627 18.174 1.00 8.54 O
ATOM 2341 N LEU B 11 49.962 53.659 16.177 1.00 8.16 N
ATOM 2342 CA LEU B 11 49.216 54.882 16.474 1.00 9.14 C
ATOM 2343 CB LEU B 11 50.130 56.113 16.515 1.00 8.09 C
ATOM 2344 CG LEU B 11 51.276 56.158 17.527 1.00 9.14 C
ATOM 2345 CD1 LEU B 11 52.077 57.450 17.351 1.00 8.55 C
ATOM 2346 CD2 LEU B 11 50.768 56.044 18.944 1.00 6.62 C
ATOM 2347 C LEU B 11 48.177 55.092 15.390 1.00 8.84 C
ATOM 2348 O LEU B 11 48.435 54.801 14.226 1.00 9.19 O
ATOM 2349 N ASN B 12 46.986 55.541 15.774 1.00 9.13 N
ATOM 2350 CA ASN B 12 46.110 56.218 14.819 1.00 9.39 C
ATOM 2351 CB ASN B 12 44.635 56.160 15.240 1.00 8.93 C
ATOM 2352 CG ASN B 12 44.188 54.762 15.622 1.00 8.05 C
ATOM 2353 OD1 ASN B 12 44.367 54.335 16.762 1.00 8.91 O
ATOM 2354 ND2 ASN B 12 43.608 54.042 14.671 1.00 7.89 N
ATOM 2355 C ASN B 12 46.553 57.663 14.685 1.00 9.84 C
ATOM 2356 O ASN B 12 46.282 58.483 15.564 1.00 11.13 O
ATOM 2357 N LEU B 13 47.241 57.977 13.590 1.00 9.11 N
ATOM 2358 CA LEU B 13 47.762 59.328 13.388 1.00 9.32 C
ATOM 2359 CB LEU B 13 48.715 59.367 12.194 1.00 8.79 C
ATOM 2360 CG LEU B 13 50.021 58.578 12.387 1.00 8.38 C
ATOM 2361 CD1 LEU B 13 50.933 58.778 11.187 1.00 12.00 C
ATOM 2362 CD2 LEU B 13 50.748 58.977 13.675 1.00 8.86 C
ATOM 2363 C LEU B 13 46.602 60.310 13.222 1.00 8.77 C
ATOM 2364 O LEU B 13 46.665 61.452 13.674 1.00 9J7 O
ATOM 2365 N PHE B 14 45.539 59.843 12.583 1.00 8.56 N
ATOM 2366 CA PHE B 14 44.237 60.490 12.698 1.00 7.94 C
ATOM 2367 CB PHE B 14 43.977 61.491 11.542 1.00 7.70 C
ATOM 2368 CG PHE B 14 43.972 60.882 10.132 1.00 7.72 C
ATOM 2369 CD1 PHE B 14 42.971 60.006 9.723 1.00 7.07 C
ATOM 2370 CE1 PHE B 14 42.937 59.507 8.401 1.00 9.76 C
ATOM 2371 CZ PHE B 14 43.904 59.922 7.473 1.00 7.74 C
ATOM 2372 CE2 PHE B 14 44.886 60.822 7.869 1.00 7.46 C
ATOM 2373 CD2 PHE B 14 44.907 61.310 9.180 1.00 7.79 C
ATOM 2374 C PHE B 14 43.140 59.431 12.819 1.00 7.93 C
ATOM 2375 O PHE B 14 43.371 58.269 12.508 1.00 8.73 O
ATOM 2376 N LEU B 15 41.963 59.835 13.280 1.00 7.97 N
ATOM 2377 CA LEU B 15 40.844 58.903 13.466 1.00 9.11 C
ATOM 2378 CB LEU B 15 40.972 58.140 14.800 1.00 9.05 C
ATOM 2379 CG LEU B 15 39.942 57.055 15.186 1.00 11.11 C
ATOM 2380 CD1 LEU B 15 39.564 56.192 14.028 1.00 14.81 C
ATOM 2381 CD2 LEU B 15 40.514 56.184 16.298 1.00 11.52 C
ATOM 2382 C LEU B 15 39.526 59.645 13.412 1.00 8.44 C
ATOM 2383 O LEU B 15 39.218 60.435 14.299 1.00 7.59 O
ATOM 2384 N TYR B 16 38.753 59.377 12.361 1.00 8.74 N
ATOM 2385 CA TYR B 16 37.449 59.991 12.176 1.00 8.06 C
ATOM 2386 CB TYR B 16 37.423 60.802 10.869 1.00 7.59 C
ATOM 2387 CG TYR B 16 38.561 61.785 10.819 1.00 8.28 C
ATOM 2388 CD1 TYR B 16 39.599 61.634 9.901 1.00 7.36 C
ATOM 2389 CE1 TYR B 16 40.678 62.524 9.884 1.00 7.47 C
ATOM 2390 CZ TYR B 16 40.729 63.557 10.817 1.00 8.91 C
ATOM 2391 OH TYR B 16 41.794 64.434 10.814 1.00 11.64 O
ATOM 2392 CE2 TYR B 16 39.705 63.717 11.746 1.00 10.55 C
ATOM 2393 CD2 TYR B 16 38.641 62.829 11.751 1.00 7.71 C
ATOM 2394 C TYR B 16 36.367 58.928 12.180 1.00 9J0 C
ATOM 2395 O TYR B 16 36.521 57.871 11.579 1.00 7.86 O
ATOM 2396 N ILE B 17 35.282 59.210 12.885 1.00 10.05 N
ATOM 2397 CA ILE B 17 34.170 58.286 12.969 1.00 10.66 C
ATOM 2398 CB ILE B 17 33.679 58.187 14.430 1.00 11.17 C
ATOM 2399 CG1 ILE B 17 34.827 57.755 15.344 1.00 11.48 C
ATOM 2400 CD1 ILE B 17 34.652 58.156 16.772 1.00 13.88 C
ATOM 2401 CG2 ILE B 17 32.503 57.209 14.558 1.00 11.60 C
ATOM 2402 C ILE B 17 33.075 58.769 12.018 1.00 10.80 C
ATOM 2403 O ILE B 17 32.493 59.826 12.223 1.00 9.87 O
ATOM 2404 N THR B 18 32.821 57.996 10.967 1.00 11.24 N
ATOM 2405 CA THR B 18 31.953 58.445 9.873 1.00 12.63 C
ATOM 2406 CB THR B 18 32.521 58.024 8.515 1.00 11.96 C
ATOM 2407 OG1 THR B 18 32.790 56.615 8.523 1.00 15.15 O
ATOM 2408 CG2 THR B 18 33.898 58.673 8.287 1.00 12.41 C
ATOM 2409 C THR B 18 30.515 57.950 9.988 1.00 13.74 C
ATOM 2410 O THR B 18 29.639 58.431 9.279 1.00 13.98 O
ATOM 2411 N GLY B 19 30.272 56.983 10.864 1.00 15.29 N
ATOM 2412 CA GLY B 19 28.924 56.477 11.044 1.00 16.68 C
ATOM 2413 C GLY B 19 28.908 55.237 11.894 1.00 17.91 C
ATOM 2414 O GLY B 19 29.955 54.764 12.326 1.00 18.06 O
ATOM 2415 N GLN B 20 27.718 54.701 12.135 1.00 19.09 N
ATOM 2416 CA GLN B 20 27.594 53.472 12.903 1.00 20.75 C
ATOM 2417 CB GLN B 20 26.893 53.738 14.240 1.00 21.83 C
ATOM 2418 CG GLN B 20 27.231 52.710 15.302 1.00 23.28 C
ATOM 2419 CD GLN B 20 26.491 52.927 16.608 1.00 27.00 C
ATOM 2420 OE1 GLN B 20 25.616 53.788 16.702 1.00 26.56 O
ATOM 2421 NE2 GLN B 20 26.838 52.134 17.621 1.00 27.11 N
ATOM 2422 C GLN B 20 26.850 52.407 12.103 1.00 22.07 C
ATOM 2423 O GLN B 20 25.832 52.697 11.468 1.00 22.05 O
ATOM 2424 N ARG B 21 27.386 51.188 12.109 1.00 22.57 N
ATOM 2425 CA ARG B 21 26.736 50.055 11.464 1.00 23.74 C
ATOM 2426 CB ARG B 21 27.739 48.959 11.140 1.00 23.51 C
ATOM 2427 CG ARG B 21 28.879 49.344 10.232 1.00 22.19 C
ATOM 2428 CD ARG B 21 30.112 48.487 10.454 1.00 24.47 C
ATOM 2429 NE ARG B 21 29.763 47.085 10.709 1.00 23.11 N
ATOM 2430 CZ ARG B 21 29.990 46.095 9.860 1.00 24.17 C
ATOM 2431 NH1 ARG B 21 30.573 46.336 8.692 1.00 23.41 N
ATOM 2432 NH2 ARG B 21 29.640 44.858 10.177 1.00 25.09 N
ATOM 2433 C ARG B 21 25.657 49.467 12.373 1.00 24.42 C
ATOM 2434 O ARG B 21 25.691 49.652 13.594 1.00 24.77 O
ATOM 2435 N ALA B 22 24.732 48.713 11.782 1.00 25.03 N
ATOM 2436 CA ALA B 22 23.598 48.158 12.529 1.00 24.93 C
ATOM 2437 CB ALA B 22 22.541 47.631 11.568 1.00 25.79 C
ATOM 2438 C ALA B 22 24.012 47.077 13.535 1.00 25.06 C
ATOM 2439 O ALA B 22 23.247 46.739 14.434 1.00 26.77 O
ATOM 2440 N ASP B 23 25.227 46.551 13.400 1.00 24.74 N
ATOM 2441 CA ASP B 23 25.737 45.583 14.363 1.00 24.26 C
ATOM 2442 CB ASP B 23 26.684 44.584 13.681 1.00 24.35 C
ATOM 2443 CG ASP B 23 27.994 45.210 13.263 1.00 23.26 C
ATOM 2444 OD1 ASP B 23 28.975 44.460 13.063 1.00 22.91 O
ATOM 2445 OD2 ASP B 23 28.136 46.440 13.108 1.00 20.92 O
ATOM 2446 C ASP B 23 26.422 46.241 15.583 1.00 25.23 C
ATOM 2447 O ASP B 23 26.990 45.552 16.439 1.00 25.08 O
ATOM 2448 N GLY B 24 26.368 47.568 15.649 1.00 25.67 N
ATOM 2449 CA GLY B 24 26.961 48.305 16.758 1.00 26.13 C
ATOM 2450 C GLY B 24 28.357 48.862 16.505 1.00 26.39 C
ATOM 2451 O GLY B 24 28.827 49.734 17.242 1.00 26.65 O
ATOM 2452 N TYR B 25 29.032 48.365 15.475 1.00 25.78 N
ATOM 2453 CA TYR B 25 30.369 48.852 15.163 1.00 25.09 C
ATOM 2454 CB TYR B 25 31.164 47.809 14.367 1.00 26.07 C
ATOM 2455 CG TYR B 25 31.813 46.729 15.224 1.00 30.54 C
ATOM 2456 CD1 TYR B 25 31.040 45.885 16.024 1.00 34.84 C
ATOM 2457 CE1 TYR B 25 31.623 44.894 16.809 1.00 38.05 C
ATOM 2458 CZ TYR B 25 32.995 44.727 16.791 1.00 39.82 C
ATOM 2459 OH TYR B 25 33.568 43.739 17.572 1.00 43.32 O
ATOM 2460 CE2 TYR B 25 33.794 45.553 16.004 1.00 38.62 C
ATOM 2461 CD2 TYR B 25 33.199 46.549 15.227 1.00 35.23 C
ATOM 2462 C TYR B 25 30.310 50.197 14.419 1.00 23.12 C
ATOM 2463 O TYR B 25 29.328 50.506 13.739 1.00 23.43 O
ATOM 2464 N HIS B 26 31.364 50.991 14.568 1.00 20.77 N
ATOM 2465 CA HIS B 26 31.463 52.288 13.903 1.00 17.80 C
ATOM 2466 CB HIS B 26 31.976 53.342 14.890 1.00 18.01 C
ATOM 2467 CG HIS B 26 31.042 53.583 16.034 1.00 17.74 C
ATOM 2468 ND1 HIS B 26 30.887 52.683 17.068 1.00 18.67 N
ATOM 2469 CE1 HIS B 26 29.989 53.147 17.919 1.00 19.74 C
ATOM 2470 NE2 HIS B 26 29.543 54.304 17.466 1.00 16.84 N
ATOM 2471 CD2 HIS B 26 30.184 54.599 16.286 1.00 17.07 C
ATOM 2472 C HIS B 26 32.371 52.214 12.689 1.00 15.94 C
ATOM 2473 O HIS B 26 33.382 51.531 12.713 1.00 15.59 O
ATOM 2474 N THR B 27 31.993 52.897 11.611 1.00 14.45 N
ATOM 2475 CA THR B 27 32.872 52.994 10.455 1.00 12.99 C
ATOM 2476 CB THR B 27 32.080 53.177 9.141 1.00 12.28 C
ATOM 2477 OG1 THR B 27 31.198 54.287 9.270 1.00 11.68 O
ATOM 2478 CG2 THR B 27 31.132 51.991 8.906 1.00 12.89 C
ATOM 2479 C THR B 27 33.857 54.144 10.665 1.00 11.57 C
ATOM 2480 O THR B 27 33.530 55.147 11.293 1.00 11.04 O
ATOM 2481 N LEU B 28 35.053 53.982 10.119 1.00 10.38 N
ATOM 2482 CA LEU B 28 36.163 54.873 10.392 1.00 10.16 C
ATOM 2483 CB LEU B 28 37.234 54.145 11.230 1.00 9.72 C
ATOM 2484 CG LEU B 28 36.814 53.367 12.485 1.00 11.22 C
ATOM 2485 CD1 LEU B 28 38.011 52.676 13.101 1.00 14.49 C
ATOM 2486 CD2 LEU B 28 36.120 54.275 13.531 1.00 11.99 C
ATOM 2487 C LEU B 28 36.828 55.374 9.118 1.00 9.65 C
ATOM 2488 O LEU B 28 36.746 54.748 8.069 1.00 7.86 O
ATOM 2489 N GLN B 29 37.530 56.492 9.234 1.00 8.46 N
ATOM 2490 CA GLN B 29 38.654 56.768 8.349 1.00 8.71 C
ATOM 2491 CB GLN B 29 38.389 57.956 7.434 1.00 8.91 C
ATOM 2492 CG GLN B 29 37.197 57.780 6.497 1.00 9.99 C
ATOM 2493 CD GLN B 29 37.160 58.848 5.428 1.00 9.13 C
ATOM 2494 OE1 GLN B 29 36.986 60.028 5.729 1.00 9.12 O
ATOM 2495 NE2 GLN B 29 37.338 58.445 4.187 1.00 8.22 N
ATOM 2496 C GLN B 29 39.833 57.041 9.258 1.00 8.90 C
ATOM 2497 O GLN B 29 39.800 57.962 10.073 1.00 7.36 O
ATOM 2498 N THR B 30 40.855 56.205 9.161 1.00 8.05 N
ATOM 2499 CA THR B 30 41.964 56.316 10.079 1.00 8.05 C
ATOM 2500 CB THR B 30 41.746 55.367 11.319 1.00 8.41 C
ATOM 2501 OG1 THR B 30 42.766 55.606 12.304 1.00 6.64 O
ATOM 2502 CG2 THR B 30 41.891 53.896 10.939 1.00 7.31 C
ATOM 2503 C THR B 30 43.293 56.071 9.372 1.00 9.28 C
ATOM 2504 O THR B 30 43.343 55.454 8.305 1.00 9.75 O
ATOM 2505 N LEU B 31 44.353 56.634 9.935 1.00 9.19 N
ATOM 2506 CA LEU B 31 45.688 56.442 9.405 1.00 9.29 C
ATOM 2507 CB LEU B 31 46.317 57.792 9.045 1.00 8.19 C
ATOM 2508 CG LEU B 31 47.762 57.783 8.539 1.00 11.28 C
ATOM 2509 CD1 LEU B 31 47.931 56.832 7.340 1.00 11.03 C
ATOM 2510 CD2 LEU B 31 48.255 59.205 8.194 1.00 9.02 C
ATOM 2511 C LEU B 31 46.534 55.719 10.435 1.00 9.18 C
ATOM 2512 O LEU B 31 46.829 56.276 11.499 1.00 8.75 O
ATOM 2513 N PHE B 32 46.920 54.483 10.116 1.00 8.61 N
ATOM 2514 CA PHE B 32 47.817 53.691 10.956 1.00 9.19 C
ATOM 2515 CB PHE B 32 47.555 52.203 10.776 1.00 9.31 C
ATOM 2516 CG PHE B 32 46.217 51.734 11.277 1.00 9.27 C
ATOM 2517 CD1 PHE B 32 45.235 51.335 10.377 1.00 9.43 C
ATOM 2518 CE1 PHE B 32 44.008 50.849 10.823 1.00 10.23 C
ATOM 2519 CZ PHE B 32 43.761 50.754 12.186 1.00 10.56 C
ATOM 2520 CE2 PHE B 32 44.745 51.119 13.094 1.00 10.74 C
ATOM 2521 CD2 PHE B 32 45.967 51.610 12.642 1.00 7.69 C
ATOM 2522 C PHE B 32 49.293 53.909 10.620 1.00 10.10 C
ATOM 2523 O PHE B 32 49.687 53.886 9.451 1.00 8.99 O
ATOM 2524 N GLN B 33 50.115 54.048 11.654 1.00 8.87 N
ATOM 2525 CA GLN B 33 51.554 53.924 11.494 1.00 8.91 C
ATOM 2526 CB GLN B 33 52.218 55.306 11.468 1.00 8.48 C
ATOM 2527 CG GLN B 33 53.715 55.263 11.209 1.00 9.05 C
ATOM 2528 CD GLN B 33 54.333 56.635 11.189 1.00 12.14 C
ATOM 2529 OE1 GLN B 33 54.285 57.353 12.187 1.00 12.46 O
ATOM 2530 NE2 GLN B 33 54.905 57.019 10.045 1.00 12.68 N
ATOM 2531 C GLN B 33 52.078 53.104 12.649 1.00 8.30 C
ATOM 2532 O GLN B 33 51.589 53.234 13.772 1.00 8.88 O
ATOM 2533 N PHE B 34 53.054 52.246 12.385 1.00 6.93 N
ATOM 2534 CA PHE B 34 53.637 51.447 13.444 1.00 8.18 C
ATOM 2535 CB PHE B 34 54.318 50.225 12.849 1.00 8.35 C
ATOM 2536 CG PHE B 34 53.425 49.443 11.945 1.00 8.62 C
ATOM 2537 CD1 PHE B 34 53.631 49.450 10.580 1.00 8.53 C
ATOM 2538 CE1 PHE B 34 52.799 48.731 9.724 1.00 7.09 C
ATOM 2539 CZ PHE B 34 51.717 48.024 10.240 1.00 8.01 C
ATOM 2540 CE2 PHE B 34 51.484 48.024 11.612 1.00 6.99 C
ATOM 2541 CD2 PHE B 34 52.339 48.738 12.462 1.00 8.44 C
ATOM 2542 C PHE B 34 54.627 52.248 14.263 1.00 8.56 C
ATOM 2543 O PHE B 34 55.163 53.248 13.792 1.00 9.47 O
ATOM 2544 N LEU B 35 54.852 51.810 15.497 1.00 9.15 N
ATOM 2545 CA LEU B 35 55.983 52.287 16.285 1.00 9.66 C
ATOM 2546 CB LEU B 35 55.561 52.570 17.724 1.00 9.32 C
ATOM 2547 CG LEU B 35 54.524 53.680 17.900 1.00 10.18 C
ATOM 2548 CD1 LEU B 35 54.186 53.876 19.374 1.00 10.66 C
ATOM 2549 CD2 LEU B 35 55.029 54.986 17.277 1.00 8.09 C
ATOM 2550 C LEU B 35 57.048 51.221 16.279 1.00 11.12 C
ATOM 2551 O LEU B 35 56.730 50.027 16.350 1.00 10.78 O
ATOM 2552 N ASP B 36 58.313 51.637 16.226 1.00 11.05 N
ATOM 2553 CA ASP B 36 59.429 50.697 16.337 1.00 11.10 C
ATOM 2554 CB ASP B 36 60.678 51.274 15.666 1.00 12.19 C
ATOM 2555 CG ASP B 36 61.778 50.246 15.480 1.00 15.84 C
ATOM 2556 OD1 ASP B 36 62.939 50.672 15.341 1.00 19.74 O
ATOM 2557 OD2 ASP B 36 61.592 49.003 15.472 1.00 16.04 O
ATOM 2558 C ASP B 36 59.682 50.374 17.807 1.00 11.58 C
ATOM 2559 O ASP B 36 60.723 50.733 18.386 1.00 10.11 O
ATOM 2560 N TYR B 37 58.721 49.673 18.399 1.00 9.96 N
ATOM 2561 CA TYR B 37 58.635 49.485 19.833 1.00 10.87 C
ATOM 2562 CB TYR B 37 58.407 50.825 20.537 1.00 10.75 C
ATOM 2563 CG TYR B 37 58.228 50.753 22.047 1.00 11.83 C
ATOM 2564 CD1 TYR B 37 59.298 50.993 22.904 1.00 18.20 C
ATOM 2565 CE1 TYR B 37 59.145 50.935 24.286 1.00 18.10 C
ATOM 2566 CZ TYR B 37 57.901 50.654 24.822 1.00 17.99 C
ATOM 2567 OH TYR B 37 57.750 50.604 26.183 1.00 21.43 O
ATOM 2568 CE2 TYR B 37 56.818 50.422 23.997 1.00 14.77 C
ATOM 2569 CD2 TYR B 37 56.984 50.479 22.616 1.00 14.12 C
ATOM 2570 C TYR B 37 57.448 48.591 20.070 1.00 10.61 C
ATOM 2571 O TYR B 37 56.389 48.813 19.481 1.00 11.77 O
ATOM 2572 N GLY B 38 57.585 47.611 20.946 1.00 9.94 N
ATOM 2573 CA GLY B 38 56.434 46.816 21.305 1.00 10.31 C
ATOM 2574 C GLY B 38 56.766 45.585 22.098 1.00 10.70 C
ATOM 2575 O GLY B 38 57.794 45.520 22.793 1.00 11.15 O
ATOM 2576 N ASP B 39 55.883 44.603 22.005 1.00 9.65 N
ATOM 2577 CA ASP B 39 56.079 43.350 22.690 1.00 9.90 C
ATOM 2578 CB ASP B 39 54.747 42.623 22.859 1.00 9.17 C
ATOM 2579 CG ASP B 39 53.707 43.446 23.612 1.00 12.25 C
ATOM 2580 OD1 ASP B 39 54.068 44.302 24.449 1.00 10.55 O
ATOM 2581 OD2 ASP B 39 52.486 43.266 23.451 1.00 14.21 O
ATOM 2582 C ASP B 39 57.014 42.477 21.888 1.00 8.93 C
ATOM 2583 O ASP B 39 57.221 42.706 20.693 1.00 8.85 O
ATOM 2584 N THR B 40 57.592 41.475 22.547 1.00 10.08 N
ATOM 2585 CA ATHR B 40 58.343 40.443 21.851 0.50 9.65 C
ATOM 2586 CA BTHR B 40 58.326 40.426 21.829 0.50 10.43 C
ATOM 2587 CB ATHR B 40 59.817 40.481 22.288 0.50 10.21 C
ATOM 2588 CB BTHR B 40 59.845 40.401 22.172 0.50 11.12 C
ATOM 2589 OG1ATHR B 40 60.379 41.738 21.900 0.50 10.08 O
ATOM 2590 OG1 BTHR B 40 60.043 39.853 23.479 0.50 12.96 O
ATOM 2591 CG2ATHR B 40 60.643 39.475 21.504 0.50 7.75 C
ATOM 2592 CG2BTHR B 40 60.380 41.788 22.296 0.50 11.46 C
ATOM 2593 C THR B 40 57.710 39.083 22.121 1.00 9.86 C
ATOM 2594 O THR B 40 57.456 38.735 23.270 1.00 9.71 O
ATOM 2595 N ILE B 41 57.452 38.333 21.058 1.00 9.25 N
ATOM 2596 CA ILE B 41 56.836 37.028 21.191 1.00 9.20 C
ATOM 2597 CB ILE B 41 55.565 36.963 20.334 1.00 9.32 C
ATOM 2598 CG1 ILE B 41 54.499 37.907 20.928 1.00 8.01 C
ATOM 2599 CD1 ILE B 41 53.314 38.087 20.067 1.00 8.65 C
ATOM 2600 CG2 ILE B 41 55.046 35.506 20.208 1.00 8.39 C
ATOM 2601 C IL'E B 41 57.837 35.945 20.805 1.00 9.70 C
ATOM 2602 O ILE B 41 58.451 36.008 19.738 1.00 10.23 O
ATOM 2603 N SER B 42 58.006 34.970 21.691 1.00 9.21 N
ATOM 2604 CA SER B 42 58.919 33.862 21.459 1.00 10.05 C
ATOM 2605 CB SER B 42 59.834 33.645 22.670 1.00 9.91 C
ATOM 2606 OG SER B 42 60.602 34.804 22.928 1.00 13.17 O
ATOM 2607 C SER B 42 58.133 32.604 21.174 1.00 9.57 C
ATOM 2608 O SER B 42 57.076 32.379 21.765 1.00 9.34 O
ATOM 2609 N ILE B 43 58.629 31.802 20.240 1.00 11.06 N
ATOM 2610 CA ILE B 43 57.944 30.580 19.820 1.00 11.18 C
ATOM 2611 CB ILE B 43 57.264 30.785 18.445 1.00 11.32 C
ATOM 2612 CG1 ILE B 43 56.198 31.889 18.522 1.00 11.84 C
ATOM 2613 CD1 ILE B 43 55.747 32.429 17.170 1.00 10.48 C
ATOM 2614 CG2 ILE B 43 56.661 29.461 17.928 1.00 10.61 C
ATOM 2615 C ILE B 43 58.924 29.416 19.738 1.00 12.29 C
ATOM 2616 O ILE B 43 60.008 29.553 19.169 1.00 12.61 O
ATOM 2617 N GLU B 44 58.543 28.283 20.319 1.00 12.49 N
ATOM 2618 CA GLU B 44 59.224 27.022 20.078 1.00 13.84 C
ATOM 2619 CB GLU B 44 59.836 26.483 21.372 1.00 13.99 C
ATOM 2620 CG GLU B 44 60.485 25.110 21.229 1.00 17.66 C
ATOM 2621 CD GLU B 44 61.194 24.652 22.493 1.00 24.26 C
ATOM 2622 OE1 GLU B 44 61.582 23.465 22.555 1.00 26.60 O
ATOM 2623 OE2 GLU B 44 61.371 25.474 23.423 1.00 27.16 O
ATOM 2624 C GLU B 44 58.206 26.039 19.524 1.00 13.81 C
ATOM 2625 O GLU B 44 57.136 25.866 20.106 1.00 14.36 O
ATOM 2626 N LEU B 45 58.527 25.402 18.403 1.00 14.32 N
ATOM 2627 CA LEU B 45 57.597 24.464 17.762 1.00 15.54 C
ATOM 2628 CB LEU B 45 58.064 24.113 16.340 1.00 15.55 C
ATOM 2629 CG LEU B 45 57.975 25.270 15.326 1.00 17.60 C
ATOM 2630 CD1 LEU B 45 58.360 24.808 13.928 1.00 19.10 C
ATOM 2631 CD2 LEU B 45 56.579 25.900 15.311 1.00 17.97 C
ATOM 2632 C LEU B 45 57.389 23.198 18.595 1.00 15.60 C
ATOM 2633 O LEU B 45 58.275 22.779 19.323 1.00 14.92 O
ATOM 2634 N ARG B 46 56.177 22.648 18.528 1.00 15.76 N
ATOM 2635 CA ARG B 46 55.868 21.355 19.109 1.00 15.88 C
ATOM 2636 CB ARG B 46 54.680 21.440 20.068 1.00 15.84 C
ATOM 2637 CG ARG B 46 54.820 22.408 21.247 1.00 13.24 C
ATOM 2638 CD ARG B 46 53.613 22.355 22.211 1.00 13.37 C
ATOM 2639 NE ARG B 46 53.532 21.062 22.890 1.00 10.83 N
ATOM 2640 CZ ARG B 46 54.116 20.793 24.052 1.00 14.93 C
ATOM 2641 NH1 ARG B 46 54.798 21.742 24.691 1.00 12.19 N
ATOM 2642 NH2 ARG B 46 54.014 19.577 24.584 1.00 15.36 N
ATOM 2643 C ARG B 46 55.525 20.418 17.968 1.00 17.44 C
ATOM 2644 0 ARG B 46 55.208 20.881 16.871 1.00 16.76 O
ATOM 2645 N ASP B 47 55.589 19.107 18.208 1.00 18.89 N
ATOM 2646 CA ASP B 47 55.092 18.146 17.214 1.00 19.91 C
ATOM 2647 CB ASP B 47 56.222 17.256 16.663 1.00 21.61 C
ATOM 2648 CG ASP B 47 56.938 16.458 17.741 1.00 24.99 C
ATOM 2649 OD1 ASP B 47 58.072 16.007 17.470 1.00 31.64 O
ATOM 2650 OD2 ASP B 47 56.464 16.215 18.870 1.00 26.86 O
ATOM 2651 C ASP B 47 53.926 17.296 17.731 1.00 20.23 C
ATOM 2652 O ASP B 47 53.630 16.245 17.158 1.00 20.36 O
ATOM 2653 N ASP B 48 53.252 17.760 18.786 1.00 18.92 N
ATOM 2654 CA ASP B 48 52.131 17.011 19.374 1.00 18.04 C
ATOM 2655 CB ASP B 48 52.399 16.710 20.864 1.00 18.29 C
ATOM 2656 CG ASP B 48 52.428 17.974 21.739 1.00 19.83 C
ATOM 2657 OD1 ASP B 48 52.383 19.121 21.201 1.00 13.79 O
ATOM 2658 OD2 ASP B 48 52.497 17.905 22.990 1.00 17.96 O
ATOM 2659 C ASP B 48 50.786 17.715 19.203 1.00 16.93 C
ATOM 2660 O ASP B 48 49.781 17.338 19.813 1.00 16.09 O
ATOM 2661 N GLY B 49 50.777 18.765 18.395 1.00 16.78 N
ATOM 2662 CA GLY B 49 49.546 19.465 18.092 1.00 15.81 C
ATOM 2663 C GLY B 49 49.087 20.456 19.135 1.00 15.76 C
ATOM 2664 O GLY B 49 48.074 21.120 18.942 1.00 16.83 O
ATOM 2665 N ASP B 50 49.818 20.573 20.243 1.00 15.22 N
ATOM 2666 CA ASP B 50 49.360 21.430 21.331 1.00 15.07 C
ATOM 2667 CB ASP B 50 49.978 20.990 22.659 1.00 16.61 C
ATOM 2668 CG ASP B 50 48.996 21.085 23.809 1.00 22.52 C
ATOM 2669 OD1 ASP B 50 49.278 20.505 24.888 1.00 22.77 O
ATOM 2670 OD2 ASP B 50 47.915 21.727 23.719 1.00 27.24 O
ATOM 2671 C ASP B 50 49.674 22.896 21.076 1.00 13.00 C
ATOM 2672 O ASP B 50 50.628 23.204 20.395 1.00 12.68 O
ATOM 2673 N ILE B 51 48.852 23.784 21.628 1.00 11.85 N
ATOM 2674 CA ILE B 51 49.175 25.204 21.721 1.00 11.19 C
ATOM 2675 CB ILE B 51 48.114 26.073 20.995 1.00 11.56 C
ATOM 2676 CG1 ILE B 51 48.115 25.799 19.487 1.00 11.15 C
ATOM 2677 CD1 ILE B 51 49.470 25.974 18.824 1.00 17.04 C
ATOM 2678 CG2 ILE B 51 48.351 27.557 21.276 1.00 11.22 C
ATOM 2679 C ILE B 51 49.259 25.597 23.179 1.00 10.67 C
ATOM 2680 O ILE B 51 48.261 25.513 23.914 1.00 9.55 O
ATOM 2681 N ARG B 52 50.450 26.023 23.613 1.00 10.33 N
ATOM 2682 CA ARG B 52 50.659 26.391 25.011 1.00 10.52 C
ATOM 2683 CB ARG B 52 51.604 25.406 25.691 1.00 10.77 C
ATOM 2684 CG ARG B 52 51.194 23.947 25.565 1.00 11.88 C
ATOM 2685 CD ARG B 52 52.015 23.008 26.427 1.00 13.43 C
ATOM 2686 NE ARG B 52 51.533 21.631 26.326 1.00 10.93 N
ATOM 2687 CZ ARG B 52 51.823 20.673 27.194 1.00 16.68 C
ATOM 2688 NH1 ARG B 52 52.607 20.928 28.233 1.00 17.07 N
ATOM 2689 NH2 ARG B 52 51.325 19.456 27.028 1.00 17.46 N
ATOM 2690 C ARG B 52 51.235 27.784 25.148 1.00 10.75 C
ATOM 2691 O ARG B 52 52.386 28.020 24.773 1.00 9.83 O
ATOM 2692 N LEU B 53 50.432 28.702 25.686 1.00 10.04 N
ATOM 2693 CA LEU B 53 50.909 30.020 26.049 1.00 9.82 C
ATOM 2694 CB LEU B 53 49.780 31.059 25.970 1.00 9.22 C
ATOM 2695 CG LEU B 53 50.109 32.434 26.555 1.00 10.14 C
ATOM 2696 CD1 LEU B 53 51.212 33.127 25.755 1.00 9.38 C
ATOM 2697 CD2 LEU B 53 48.848 33.302 26.647 1.00 11.07 C
ATOM 2698 C LEU B 53 51.470 29.926 27.455 1.00 9.84 C
ATOM 2699 O LEU B 53 50.730 29.670 28.409 1.00 9.18 O
ATOM 2700 N LEU B 54 52.783 30.106 27.570 1.00 9.24 N
ATOM 2701 CA LEU B 54 53.526 29.817 28.799 1.00 10.36 C
ATOM 2702 CB LEU B 54 54.985 29.461 28.456 1.00 9.94 C
ATOM 2703 CG LEU B 54 55.243 28.241 27.563 1.00 12.82 C
ATOM 2704 CD1 LEU B 54 56.732 27.891 27.528 1.00 13.15 C
ATOM 2705 CD2 LEU B 54 54.423 27.042 28.010 1.00 12.21 C
ATOM 2706 C LEU B 54 53.531 30.969 29.799 1.00 11.62 C
ATOM 2707 O LEU B 54 53.848 30.774 30.970 1.00 10.94 O
ATOM 2708 N THR B 55 53.235 32.178 29.327 1.00 12.94 N
ATOM 2709 CA THR B 55 53.241 33.340 30.205 1.00 14.24 C
ATOM 2710 CB ATHR B 55 54.317 34.350 29.731 0.50 14,45 C
ATOM 2711 CB BTHR B 55 54.324 34.380 29.819 0.50 14.87 C
ATOM 2712 OG1ATHR B 55 54.217 34.531 28.318 0.50 10.32 O
ATOM 2713 OG1 BTHR B 55 53.784 35.708 29.946 0.50 17.28 O
ATOM 2714 CG2ATHR B 55 55.729 33.779 29.901 0.50 14.97 C
ATOM 2715 CG2BTHR B 55 54.626 34.300 28.390 0.50 11.28 C
ATOM 2716 C THR B 55 51.868 33.995 30.235 1.00 14,87 C
ATOM 2717 O THR B 55 51.354 34.428 29.203 1.00 16.00 O
ATOM 2718 N PRO B 56 51.267 34.040 31.418 1.00 15.12 N
ATOM 2719 CA PRO B 56 49.982 34.709 31.597 1.00 16.30 C
ATOM 2720 CB PRO B 56 49.648 34.458 33.079 1.00 16.15 C
ATOM 2721 CG PRO B 56 50.921 34.108 33.714 1.00 15.91 C
ATOM 2722 CD PRO B 56 51.756 33.424 32.664 1.00 14.46 C
ATOM 2723 C PRO B 56 50.096 36.201 31.327 1.00 17.99 C
ATOM 2724 0 PRO B 56 51.075 36.839 31.714 1.00 17.84 O
ATOM 2725 N VAL B 57 49.101 36.735 30.633 1.00 19.62 N
ATOM 2726 CA VAL B 57 48.951 38.168 30.482 1.00 21.35 C
ATOM 2727 CB VAL B 57 48.558 38.547 29.042 1.00 21.09 C
ATOM 2728 CG1 VAL B 57 48.163 40.021 28.956 1.00 20.02 C
ATOM 2729 CG2 VAL B 57 49.699 38.252 28.094 1.00 21.30 C
ATOM 2730 C VAL B 57 47.883 38.604 31.464 1.00 22.90 C
ATOM 2731 O VAL B 57 46.793 38.028 31.491 1.00 23.03 O
ATOM 2732 N GLU B 58 48.218 39.599 32.284 1.00 25.14 N
ATOM 2733 CA GLU B 58 47.384 40.054 33.407 1.00 26.37 C
ATOM 2734 CB GLU B 58 47.831 41.459 33.851 1.00 28.00 C
ATOM 2735 CG GLU B 58 46.900 42.159 34.831 1.00 32.60 C
ATOM 2736 CD GLU B 58 47.530 42.347 36.201 1.00 40.14 C
ATOM 2737 OE1 GLU B 58 48.528 43.095 36.302 1.00 41.41 O
ATOM 2738 OE2 GLU B 58 47.027 41.742 37.176 1.00 42.99 O
ATOM 2739 C GLU B 58 45.885 40.048 33.108 1.00 25.35 C
ATOM 2740 O GLU B 58 45.417 40.753 32.212 1.00 25.53 O
ATOM 2741 N GLY B 59 45.150 39.218 33.851 1.00 23.83 N
ATOM 2742 CA GLY B 59 43.697 39.194 33.788 1.00 23.02 C
ATOM 2743 C GLY B 59 43.101 38.535 32.549 1.00 22.41 C
ATOM 2744 O GLY B 59 41.882 38.551 32.361 1.00 23.24 O
ATOM 2745 N VAL B 60 43.944 37.964 31.695 1.00 19.59 N
ATOM 2746 CA VAL B 60 43.438 37.282 30.508 1.00 17.96 C
ATOM 2747 CB VAL B 60 44.120 37.767 29.209 1.00 17.87 C
ATOM 2748 CG1 VAL B 60 43.377 37.225 27.993 1.00 15.55 C
ATOM 2749 CG2 VAL B 60 44.193 39.297 29.164 1.00 16.82 C
ATOM 2750 C VAL B 60 43.626 35.781 30.633 1.00 18.04 C
ATOM 2751 O VAL B 60 44.755 35.297 30.733 1.00 16.39 O
ATOM 2752 N GLU B 61 42.512 35.051 30.622 1.00 17.30 N
ATOM 2753 CA GLU B 61 42.548 33.597 30.672 1.00 17.08 C
ATOM 2754 CB GLU B 61 41.136 33.032 30.870 1.00 17.61 C
ATOM 2755 CG GLU B 61 40.515 33.369 32.224 1.00 20.17 C
ATOM 2756 CD GLU B 61 39.051 32.980 32.312 1.00 23.27 C
ATOM 2757 OE1 GLU B 61 38.609 32.095 31.549 1.00 24.35 O
ATOM 2758 OE2 GLU B 61 38.336 33.565 33.144 1.00 29.30 O
ATOM 2759 C GLU B 61 43.174 33.052 29.391 1.00 15.84 C
ATOM 2760 O GLU B 61 43.047 33.658 28.338 1.00 15.73 O
ATOM 2761 N HIS B 62 43.850 31.910 29.500 1.00 15.16 N
ATOM 2762 CA HIS B 62 44.567 31.282 28.383 1.00 14.43 C
ATOM 2763 CB HIS B 62 44.947 29.850 28.775 1.00 13.57 C
ATOM 2764 CG HIS B 62 45.888 29.168 27.823 1.00 12.34 C
ATOM 2765 ND1 HIS B 62 45.446 28.409 26.760 1.00 9.47 N
ATOM 2766 CE1 HIS B 62 46.486 27.887 26.129 1.00 9.78 C
ATOM 2767 NE2 HIS B 62 47.587 28.268 26.754 1.00 8.91 N
ATOM 2768 CD2 HIS B 62 47.240 29.056 27.828 1.00 11.49 C
ATOM 2769 C HIS B 62 43.773 31.301 27.065 1.00 14.63 C
ATOM 2770 O HIS B 62 44.266 31.772 26.047 1.00 13.33 O
ATOM 2771 N GLU B 63 42.532 30.829 27.108 1.00 14.86 N
ATOM 2772 CA GLU B 63 41.741 30.672 25.893 1.00 15.69 C
ATOM 2773 CB GLU B 63 40.640 29.621 26.099 1.00 16.41 C
ATOM 2774 CG GLU B 63 41.167 28.195 26.245 1.00 15.75 C
ATOM 2775 CD GLU B 63 42.124 27.781 25.134 1.00 19.11 C
ATOM 2776 OE1 GLU B 63 41.725 27.821 23.939 1.00 19.91 O
ATOM 2777 OE2 GLU B 63 43.281 27.398 25.449 1.00 15.21 O
ATOM 2778 C GLU B 63 41.150 31.993 25.387 1.00 16.16 C
ATOM 2779 O GLU B 63 40.753 32.085 24.219 1.00 16.06 O
ATOM 2780 N ASP B 64 41.125 33.011 26.254 1.00 15.34 N
ATOM 2781 CA ASP B 64 40.716 34.354 25.858 1.00 15.48 C
ATOM 2782 CB ASP B 64 40.169 35.143 27.063 1.00 16.69 C
ATOM 2783 CG ASP B 64 38.852 34.586 27.580 1.00 17.08 C
ATOM 2784 OD1 ASP B 64 38.098 33.998 26.779 1.00 17.87 O
ATOM 2785 OD2 ASP B 64 38.500 34.686 28.774 1.00 20.65 O
ATOM 2786 C ASP B 64 41.862 35.144 25.237 1.00 14.61 C
ATOM 2787 O ASP B 64 41.639 36.162 24.587 1.00 13.94 O
ATOM 2788 N ASN B 65 43.093 34.694 25.463 1.00 13.03 N
ATOM 2789 CA ASN B 65 44.247 35.432 24.965 1.00 12.22 C
ATOM 2790 CB ASN B 65 45.549 34.907 25.584 1.00 11.56 C
ATOM 2791 CG ASN B 65 46.681 35.886 25.433 1.00 11.50 C
ATOM 2792 OD1 ASN B 65 47.062 36.239 24.312 1.00 11.19 O
ATOM 2793 ND2 ASN B 65 47.213 36.356 26.551 1.00 7.56 N
ATOM 2794 C ASN B 65 44.314 35.400 23.438 1.00 10.97 C
ATOM 2795 O ASN B 65 44.200 34.330 22.830 1.00 10.83 O
ATOM 2796 N LEU B 66 44.491 36.571 22.824 1.00 10.18 N
ATOM 2797 CA LEU B 66 44.470 36.675 21.355 1.00 10.12 C
ATOM 2798 CB LEU B 66 44.486 38.144 20.914 1.00 11.18 C
ATOM 2799 CG LEU B 66 43.167 38.901 21.144 1.00 12.65 C
ATOM 2800 CD1 LEU B 66 43.312 40.368 20.782 1.00 16.05 C
ATOM 2801 CD2 LEU B 66 42.040 38.273 20.354 1.00 17.21 C
ATOM 2802 C LEU B 66 45.614 35.892 20.693 1.00 9.64 C
ATOM 2803 O LEU B 66 45.517 35.509 19.534 1.00 9.96 O
ATOM 2804 N ILE B 67 46.690 35.671 21.438 1.00 8.59 N
ATOM 2805 CA ILE B 67 47.789 34.802 21.007 1.00 8.40 C
ATOM 2806 CB ILE B 67 48.914 34.821 22.072 1.00 7.54 C
ATOM 2807 CG1 ILE B 67 49.664 36.160 22.046 1.00 9.93 C
ATOM 2808 CD1 ILE B 67 50.561 36.406 23.296 1.00 11.92 C
ATOM 2809 CG2 ILE B 67 49.876 33.645 21.891 1.00 8.71 C
ATOM 2810 C ILE B 67 47.310 33.360 20.767 1.00 8.53 C
ATOM 2811 O ILE B 67 47.613 32.743 19.742 1.00 7.67 O
ATOM 2812 N VAL B 68 46.559 32.830 21.724 1.00 9.08 N
ATOM 2813 CA VAL B 68 46.075 31.457 21.619 1.00 9.24 C
ATOM 2814 CB VAL B 68 45.582 30.934 22.990 1.00 10.04 C
ATOM 2815 CG1 VAL B 68 44.864 29.584 22.847 1.00 8.90 C
ATOM 2816 CG2 VAL B 68 46.757 30.836 23.956 1.00 8.39 C
ATOM 2817 C VAL B 68 44.977 31.378 20.575 1.00 9.24 C
ATOM 2818 O VAL B 68 44.955 30.457 19.756 1.00 10.10 O
ATOM 2819 N ARG B 69 44.090 32.370 20.568 1.00 8.54 N
ATOM 2820 CA ARG B 69 43.008 32.386 19.580 1.00 10.21 C
ATOM 2821 CB ARG B 69 42.028 33.541 19.828 1.00 8.32 C
ATOM 2822 CG ARG B 69 41.250 33.418 21.142 1.00 13.74 C
ATOM 2823 CD ARG B 69 40.224 34.524 21.370 1.00 15.78 C
ATOM 2824 NE ARG B 69 39.302 34.621 20.242 1.00 24.27 N
ATOM 2825 CZ ARG B 69 38.615 35.713 19.928 1.00 27.15 C
ATOM 2826 NH1 ARG B 69 38.722 36.810 20.674 1.00 23.51 N
ATOM 2827 NH2 ARG B 69 37.810 35.704 18.871 1.00 26.09 N
ATOM 2828 C ARG B 69 43.570 32.430 18.159 1.00 10.01 C
ATOM 2829 O ARG B 69 43.073 31.734 17.288 1.00 10.34 O
ATOM 2830 N ALA B 70 44.628 33.221 17.938 1.00 9.78 N
ATOM 2831 CA ALA B 70 45.282 33.266 16.617 1.00 9.66 C
ATOM 2832 CB ALA B 70 46.336 34.386 16.561 1.00 9.28 C
ATOM 2833 C ALA B 70 45.911 31.935 16.214 1.00 9.29 C
ATOM 2834 O ALA B 70 45.735 31.476 15.084 1.00 8.87 O
ATOM 2835 N ALA B 71 46.659 31.321 17.128 1.00 9.02 N
ATOM 2836 CA ALA B 71 47.336 30.064 16.821 1.00 9.44 C
ATOM 2837 CB ALA B 71 48.221 29.634 17.983 1.00 9.52 C
ATOM 2838 C ALA B 71 46.332 28.962 16.472 1.00 10.10 C
ATOM 2839 O ALA B 71 46.539 28.194 15.523 1.00 9.56 O
ATOM 2840 N ARG B 72 45.243 28.899 17.235 1.00 9.45 N
ATOM 2841 CA ARG B 72 44.218 27.885 17.025 1.00 10.05 C
ATOM 2842 CB ARG B 72 43.228 27.894 18.187 1.00 9.90 C
ATOM 2843 CG ARG B 72 43.773 27.287 19.482 1.00 9.16 C
ATOM 2844 CD ARG B 72 42.687 26.717 20.412 1.00 13.41 C
ATOM 2845 NE ARG B 72 43.159 26.589 21.795 1.00 14.76 N
ATOM 2846 CZ ARG B 72 44.042 25.686 22.211 1.00 16.24 C
ATOM 2847 NH1 ARG B 72 44.545 24.795 21.365 1.00 13.73 N
ATOM 2848 NH2 ARG B 72 44.402 25.658 23.485 1.00 17.47 N
ATOM 2849 C ARG B 72 43.472 28.118 15.708 1.00 10.93 C
ATOM 2850 O ARG B 72 43.155 27.170 14.981 1.00 10.02 O
ATOM 2851 N LEU B 73 43.211 29.385 15.407 1.00 11.56 N
ATOM 2852 CA LEU B 73 42.508 29.747 14.181 1.00 13.12 C
ATOM 2853 CB LEU B 73 42.120 31.230 14.193 1.00 13.97 C
ATOM 2854 CG LEU B 73 41.390 31.791 12.969 1.00 16.31 C
ATOM 2855 CD1 LEU B 73 40.071 31.053 12.697 1.00 16.71 C
ATOM 2856 CD2 LEU B 73 41.156 33.283 13.165 1.00 16.58 C
ATOM 2857 C LEU B 73 43.351 29.411 12.961 1.00 13.37 C
ATOM 2858 O LEU B 73 42.839 28.833 11.999 1.00 13.77 O
ATOM 2859 N LEU B 74 44.645 29.742 13.006 1.00 11.81 N
ATOM 2860 CA LEU B 74 45.548 29.397 11.907 1.00 11.80 C
ATOM 2861 CB LEU B 74 46.955 29.974 12.119 1.00 10.65 C
ATOM 2862 CG LEU B 74 47.986 29.525 11.074 1.00 11.82 C
ATOM 2863 CD1 LEU B 74 47.546 29.893 9.628 1.00 9.80 C
ATOM 2864 CD2 LEU B 74 49.366 30.091 11.366 1.00 8.35 C
ATOM 2865 C LEU B 74 45.635 27.883 11.733 1.00 11.72 C
ATOM 2866 O LEU B 74 45.529 27.370 10.615 1.00 11.24 O
ATOM 2867 N MSE B 75 45.834 27.174 12.844 1.00 11.65 N
ATOM 2868 CA MSE B 75 45.933 25.722 12.816 1.00 12.50 C
ATOM 2869 CB MSE B 75 46.058 25.159 14.241 1.00 11.47 C
ATOM 2870 CG MSE B 75 46.020 23.626 14.310 1.00 16.51 C
ATOM 2871 SE MSE B 75 46.245 22.929 16.142 1.00 30.32 SE
ATOM 2872 CE MSE B 75 48.024 23.612 16.478 1.00 17.19 C
ATOM 2873 C MSE B 75 44.724 25.099 12.108 1.00 12.72 C
ATOM 2874 O MSE B 75 44.887 24.264 11.223 1.00 13.09 O
ATOM 2875 N LYS B 76 43.524 25.519 12.497 1.00 13.93 N
ATOM 2876 CA LYS B 76 42.285 24.947 11.947 1.00 16.48 C
ATOM 2877 CB LYS B 76 41.062 25.409 12.761 1.00 17.26 C
ATOM 2878 CG LYS B 76 39.722 24.826 12.287 1.00 21.15 C
ATOM 2879 CD LYS B 76 39.319 23.594 13.091 1.00 29.21 C
ATOM 2880 CE LYS B 76 37.800 23.318 12.981 1.00 31.02 C
ATOM 2881 NZ LYS B 76 37.435 22.735 11.651 1.00 32.03 N
ATOM 2882 C LYS B 76 42.119 25.296 10.467 1.00 16.87 C
ATOM 2883 O LYS B 76 41.878 24.418 9.634 1.00 16.53 O
ATOM 2884 N THR B 77 42.266 26.579 10.147 1.00 17.14 N
ATOM 2885 CA THR B 77 42.186 27.047 8.763 1.00 17.63 C
ATOM 2886 CB THR B 77 42.402 28.560 8.711 1.00 17.05 C
ATOM 2887 OG1 THR B 77 41.461 29.189 9.577 1.00 17.55 O
ATOM 2888 CG2 THR B 77 42.041 29.109 7.322 1.00 18.82 C
ATOM 2889 C THR B 77 43.184 26.347 7.838 1.00 17.80 C
ATOM 2890 O THR B 77 42.822 25.921 6.738 1.00 18.03 O
ATOM 2891 N ALA B 78 44.436 26.247 8.276 1.00 17.91 N
ATOM 2892 CA ALA B 78 45.474 25.605 7.471 1.00 18.72 C
ATOM 2893 CB ALA B 78 46.844 25.784 8.103 1.00 18.81 C
ATOM 2894 C ALA B 78 45.180 24.123 7.261 1.00 19.77 C
ATOM 2895 O ALA B 78 45.375 23.603 6.157 1.00 20.02 O
ATOM 2896 N ALA B 79 44.716 23.445 8.312 1.00 20.03 N
ATOM 2897 CA ALA B 79 44.366 22.026 8.192 1.00 21.82 C
ATOM 2898 CB ALA B 79 44.150 21.413 9.544 1.00 20.94 C
ATOM 2899 C ALA B 79 43.131 21.825 7.305 1.00 22.79 C
ATOM 2900 O ALA B 79 43.070 20.863 6.543 1.00 23.87 O
ATOM 2901 N ASP B 80 42.169 22.745 7.399 1.00 23.86 N
ATOM 2902 CA ASP B 80 40.955 22.720 6.567 1.00 25.84 C
ATOM 2903 CB ASP B 80 40.088 23.960 6.819 1.00 26.09 C
ATOM 2904 CG ASP B 80 39.220 23.837 8.051 1.00 28.46 C
ATOM 2905 OD1 ASP B 80 39.187 22.744 8.659 1.00 29.42 O
ATOM 2906 OD2 SP B 80 38.532 24.793 8.487 1.00 30.38 O
ATOM 2907 C ASP B 80 41.282 22.679 5.088 1.00 26.57 C
ATOM 2908 O ASP B 80 40.534 22.107 4.293 1.00 26.91 O
ATOM 2909 N SER B 81 42.394 23.309 4.718 1.00 26.81 N
ATOM 2910 CA SER B 81 42.756 23.460 3.318 1.00 27.20 C
ATOM 2911 CB SER B 81 42.945 24.944 2.980 1.00 26.81 C
ATOM 2912 OG SER B 81 43.990 25.513 3.752 1.00 26.92 O
ATOM 2913 C SER B 81 44.016 22.675 2.960 1.00 27.06 C
ATOM 2914 O SER B 81 44.646 22.949 1.947 1.00 28.17 O
ATOM 2915 N GLY B 82 44.384 21.710 3.800 1.00 26.68 N
ATOM 2916 CA GLY B 82 45.501 20.817 3.510 1.00 25.73 C
ATOM 2917 C GLY B 82 46.886 21.438 3.566 1.00 25.72 C
ATOM 2918 O GLY B 82 47.827 20.925 2.946 1.00 25.21 O
ATOM 2919 N ARG B 83 47.034 22.527 4.320 1.00 24.43 N
ATOM 2920 CA ARG B 83 48.306 23.258 4.334 1.00 23.62 C
ATOM 2921 CB ARG B 83 48.083 24.699 3.855 1.00 24.21 C
ATOM 2922 CG ARG B 83 47.608 24.807 2.382 1.00 25.32 C
ATOM 2923 CD ARG B 83 47.386 26.231 1.894 1.00 29.38 C
ATOM 2924 NE ARG B 83 46.100 26.779 2.329 1.00 32.79 N
ATOM 2925 CZ ARG B 83 45.661 28.001 2.033 1.00 33.39 C
ATOM 2926 NH1 ARG B 83 46.401 28.822 1.299 1.00 36.03 N
ATOM 2927 NH2 ARG B 83 44.486 28.410 2.482 1.00 33.01 N
ATOM 2928 C ARG B 83 49.021 23.241 5.698 1.00 22.62 C
ATOM 2929 O ARG B 83 49.854 24.096 5.975 1.00 23.40 O
ATOM 2930 N LEU B 84 48.705 22.262 6.540 1.00 21.09 N
ATOM 2931 CA LEU B 84 49.355 22.136 7.841 1.00 19.55 C
ATOM 2932 CB LEU B 84 48.329 22.235 8.977 1.00 19.44 C
ATOM 2933 CG LEU B 84 48.912 22.393 10.389 1.00 18.40 C
ATOM 2934 CD1 LEU B 84 49.323 23.842 10.622 1.00 17.16 C
ATOM 2935 CD2 LEU B 84 47.934 21.943 11.451 1.00 15.05 C
ATOM 2936 C LEU B 84 50.103 20.816 7.950 1.00 19.84 C
ATOM 2937 O LEU B 84 49.506 19.764 7.793 1.00 20.14 O
ATOM 2938 N PRO B 85 51.407 20.871 8.205 1.00 19.34 N
ATOM 2939 CA PRO B 85 52.185 19.665 8.506 1.00 19.79 C
ATOM 2940 CB PRO B 85 53.596 20.208 8.774 1.00 20.10 C
ATOM 2941 CG PRO B 85 53.637 21.517 8.055 1.00 19.29 C
ATOM 2942 CD PRO B 85 52.246 22.081 8.195 1.00 19.03 C
ATOM 2943 C PRO B 85 51.658 18.938 9.740 1.00 19.96 C
ATOM 2944 O PRO B 85 51.278 19.569 10.729 1.00 19.33 O
ATOM 2945 N TH B 86 51.619 17.614 9.656 1.00 19.87 N
ATOM 2946 CA THR B 86 51.097 16.774 10.723 1.00 20.57 C
ATOM 2947 CB THR B 86 51.295 15.290 10.357 1.00 21.18 C
ATOM 2948 OG1 THR B 86 50.609 15.008 9.129 1.00 24.53 O
ATOM 2949 CG2 THR B 86 50.604 14.395 11.376 1.00 22.19 C
ATOM 2950 C THR B 86 51.774 17.062 12.054 1.00 19.78 C
ATOM 2951 O THR B 86 52.999 17.029 12.150 1.00 20.53 O
ATOM 2952 N GLY B 87 50.970 17.333 13.077 1.00 18.79 N
ATOM 2953 CA GLY B 87 51.484 17.488 14.428 1.00 17.99 C
ATOM 2954 C GLY B 87 51.941 18.893 14.788 1.00 17.61 C
ATOM 2955 O GLY B 87 52.408 19.118 15.901 1.00 17.91 O
ATOM 2956 N SER B 88 51.803 19.839 13.857 1.00 16.68 N
ATOM 2957 CA SER B 88 52.202 21.227 14.104 1.00 16.06 C
ATOM 2958 CB SER B 88 51.776 22.130 12.944 1.00 15.89 C
ATOM 2959 OG SER B 88 52.438 21.776 11.756 1.00 14.66 O
ATOM 2960 C SER B 88 51.600 21.758 15.397 1.00 15.19 C
ATOM 2961 O SER B 88 50.393 21.678 15.605 1.00 14.07 O
ATOM 2962 N GLY B 89 52.454 22.273 16.272 1.00 14.32 N
ATOM 2963 CA GLY B 89 52.001 22.929 17.480 1.00 14.24 C
ATOM 2964 C GLY B 89 53.008 23.980 17.891 1.00 14.12 C
ATOM 2965 O GLY B 89 53.937 24.271 17.136 1.00 13.91 O
ATOM 2966 N ALA B 90 52.839 24.544 19.085 1.00 13.57 N
ATOM 2967 CA ALA B 90 53.721 25.625 19.526 1.00 12.78 C
ATOM 2968 CB ALA B 90 53.490 26.905 18.679 1.00 12.27 C
ATOM 2969 C ALA B 90 53.598 25.964 20.994 1.00 12.41 C
ATOM 2970 O ALA B 90 52.493 26.039 21.540 1.00 12.05 O
ATOM 2971 N ASN B 91 54.759 26.174 21.613 1.00 11.04 N
ATOM 2972 CA ASN B 91 54.885 26.862 22.878 1.00 11.29 C
ATOM 2973 CB ASN B 91 56.084 26.341 23.673 1.00 11.51 C
ATOM 2974 CG ASN B 91 55.756 25.107 24.497 1.00 12.52 C
ATOM 2975 OD1 ASN B 91 54.691 24.523 24.358 1.00 11.91 O
ATOM 2976 ND2 ASN B 91 56.684 24.709 25.363 1.00 11.92 N
ATOM 2977 C ASN B 91 55.118 28.321 22.557 1.00 11.41 C
ATOM 2978 O ASN B 91 55.954 28.636 21.697 1.00 10.69 O
ATOM 2979 N ILE B 92 54.358 29.207 23.195 1.00 10.51 N
ATOM 2980 CA ILE B 92 54.462 30.630 22.911 1.00 10.69 C
ATOM 2981 CB ILE B 92 53.213 31.153 22.153 1.00 10.68 C
ATOM 2982 CG1 ILE B 92 52.877 30.249 20.953 1.00 10.39 C
ATOM 2983 CD1 ILE B 92 51.535 30.573 20.286 1.00 11.48 C
ATOM 2984 CG2 ILE B 92 53.424 32.602 21.702 1.00 8.95 C
ATOM 2985 C ILE B 92 54.640 31.382 24.217 1.00 10.64 C
ATOM 2986 O ILE B 92 53.990 31.077 25.205 1.00 11.74 O
ATOM 2987 N SER B 93 55.529 32.358 24.226 1.00 9.88 N
ATOM 2988 CA SER B 93 55.670 33.203 25.394 1.00 10.34 C
ATOM 2989 CB SER B 93 56.896 32.784 26.225 1.00 9.40 C
ATOM 2990 OG SER B 93 58.089 33.100 25.549 1.00 14.25 O
ATOM 2991 C SER B 93 55.755 34.650 24.951 1.00 10.84 C
ATOM 2992 O SER B 93 56.078 34.938 23.795 1.00 10.36 O
ATOM 2993 N ILE B 94 55.445 35.573 25.854 1.00 10.18 N
ATOM 2994 CA ILE B 94 55.482 36.980 25.487 1.00 11.03 C
ATOM 2995 CB ILE B 94 54.046 37.497 25.142 1.00 10.58 C
ATOM 2996 CG1 ILE B 94 54.063 39.008 24.866 1.00 12.67 C
ATOM 2997 CD1 ILE B 94 52.801 39.526 24.205 1.00 9.05 C
ATOM 2998 CG2 ILE B 94 53.033 37.112 26.246 1.00 10.98 C
ATOM 2999 C ILE B 94 56.146 37.848 26.554 1.00 11.54 C
ATOM 3000 O ILE B 94 55.934 37.664 27.745 1.00 10.55 O
ATOM 3001 N ASP B 95 56.991 38.762 26.103 1.00 12.60 N
ATOM 3002 CA ASP B 95 57.453 39.828 26.950 1.00 14.53 C
ATOM 3003 CB ASP B 95 58.908 40.149 26.634 1.00 16.21 C
ATOM 3004 CG ASP B 95 59.530 41.116 27.629 1.00 22.79 C
ATOM 3005 OD1 ASP B 95 58.875 41.475 28.638 1.00 24.66 O
ATOM 3006 OD2 ASP B 95 60.685 41.576 27.471 1.00 29.65 O
ATOM 3007 C ASP B 95 56.550 41.005 26.661 1.00 14.40 C
ATOM 3008 O ASP B 95 56.684 41.653 25.626 1.00 12.66 O
ATOM 3009 N LYS B 96 55.597 41.237 27.559 1.00 14.29 N
ATOM 3010 CA LYS B 96 54.565 42.243 27.365 1.00 16.35 C
ATOM 3011 CB LYS B 96 53.255 41.804 28.037 1.00 16.33 C
ATOM 3012 CG LYS B 96 52.063 42.728 27.760 1.00 19.98 C
ATOM 3013 CD LYS B 96 51.011 42.036 26.905 1.00 22.98 C
ATOM 3014 CE LYS B 96 50.228 43.032 26.122 1.00 24.20 C
ATOM 3015 NZ LYS B 96 50.389 42.823 24.670 1.00 21.76 N
ATOM 3016 C LYS B 96 55.028 43.597 27.896 1.00 16.74 C
ATOM 3017 O LYS B 96 55.181 43.783 29.109 1.00 16.59 O
ATOM 3018 N ARG B 97 55.272 44.529 26.977 1.00 17.41 N
ATOM 3019 CA ARG B 97 55.680 45.890 27.329 1.00 18.56 C
ATOM 3020 CB ARG B 97 56.923 46.301 26.535 1.00 19.36 C
ATOM 3021 CG ARG B 97 58.139 45.455 26.864 1.00 25.62 C
ATOM 3022 CD ARG B 97 59.459 46.067 26.453 1.00 36.07 C
ATOM 3023 NE ARG B 97 59.728 45.838 25.037 1.00 43.60 N
ATOM 3024 CZ ARG B 97 60.213 44.705 24.528 1.00 46.09 C
ATOM 3025 NH1 ARG B 97 60.506 43.674 25.316 1.00 47.93 N
ATOM 3026 NH2 RG B 97 60.411 44.608 23.220 1.00 44.86 N
ATOM 3027 C ARG B 97 54.556 46.888 27.096 1.00 17.82 C
ATOM 3028 O ARG B 97 54.485 47.906 27.773 1.00 16.42 O
ATOM 3029 N LEU B 98 53.669 46.574 26.148 1.00 17.19 N
ATOM 3030 CA LEU B 98 52.566 47.467 25.778 1.00 17.33 C
ATOM 3031 CB LEU B 98 52.055 47.150 24.356 1.00 16.36 C
ATOM 3032 CG LEU B 98 53.040 47.267 23.177 1.00 14.39 C
ATOM 3033 CD1 LEU B 98 52.389 46.883 21.825 1.00 8.12 C
ATOM 3034 CD2 LEU B 98 53.661 48.664 23.099 1.00 12.77 C
ATOM 3035 C LEU B 98 51.412 47.416 26.788 1.00 19.04 C
ATOM 3036 O LEU B 98 51.029 46.351 27.247 1.00 18.42 O
ATOM 3037 N PRO B 99 50.849 48.576 27.120 1.00 21.24 N
ATOM 3038 CA PRO B 99 49.751 48.647 28.091 1.00 22.91 C
ATOM 3039 CB PRO B 99 49.564 50.152 28.305 1.00 22.59 C
ATOM 3040 CG PRO B 99 50.073 50.777 27.059 1.00 23.70 C
ATOM 3041 CD PRO B 99 51.221 49.902 26.601 1.00 21.09 C
ATOM 3042 C PRO B 99 48.470 48.038 27.549 1.00 24.99 C
ATOM 3043 O PRO B 99 48.236 48.065 26.341 1.00 25.94 O
ATOM 3044 N MSE B 100 47.663 47.477 28.439 1.00 26.54 N
ATOM 3045 CA MSE B 100 46.343 46.982 28.088 1.00 28.67 C
ATOM 3046 CB MSE B 100 45.856 45.978 29.127 1.00 30.08 C
ATOM 3047 CG MSE B 100 46.879 44.917 29.493 1.00 39.23 C
ATOM 3048 SE MSE B 100 46.310 43.136 28.928 1.00 57.93 SE
ATOM 3049 CE MSE B 100 44.535 43.077 29.842 1.00 55.34 C
ATOM 3050 C MSE B 100 45.365 48.147 27.987 1.00 27.46 C
ATOM 3051 O MSE B 100 45.383 49.057 28.816 1.00 27.39 O
ATOM 3052 N GLY B 101 44.489 48.103 26.989 1.00 26.98 N
ATOM 3053 CA GLY B 101 43.725 49.280 26.624 1.00 26.31 C
ATOM 3054 C GLY B 101 44.712 50.155 25.876 1.00 24.92 C
ATOM 3055 O GLY B 101 45.416 49.691 24.979 1.00 27.92 O
ATOM 3056 N GLY B 102 44.807 51.407 26.265 1.00 23.11 N
ATOM 3057 CA GLY B 102 45.867 52.245 25.752 1.00 19.85 C
ATOM 3058 C GLY B 102 45.618 52.829 24.380 1.00 16.88 C
ATOM 3059 O GLY B 102 45.937 53.982 24.153 1.00 17.40 O
ATOM 3060 N GLY B 103 45.042 52.051 23.465 1.00 14.56 N
ATOM 3061 CA GLY B 103 44.839 52.522 22.105 1.00 11.18 C
ATOM 3062 C GLY B 103 46.059 52.270 21.221 1.00 10.65 C
ATOM 3063 O GLY B 103 46.168 52.824 20.118 1.00 10.04 O
ATOM 3064 N LEU B 104 46.965 51.415 21.709 1.00 9.94 N
ATOM 3065 CA LEU B 104 48.201 51.068 21.000 1.00 10.25 C
ATOM 3066 CB LEU B 104 49.361 50.960 21.993 1.00 9.99 C
ATOM 3067 CG LEU B 104 49.807 52.291 22.607 1.00 9.81 C
ATOM 3068 CD1 LEU B 104 50.956 52.075 23.600 1.00 8.50 C
ATOM 3069 CD2 LEU B 104 50.195 53.327 21.527 1.00 6.67 C
ATOM 3070 C LEU B 104 48.088 49.778 20.193 1.00 9.99 C
ATOM 3071 O LEU B 104 49.026 49.392 19.481 1.00 9.83 O
ATOM 3072 N GLY B 105 46.953 49.098 20.314 1.00 9.18 N
ATOM 3073 CA GLY B 105 46.685 47.938 19.480 1.00 9.24 C
ATOM 3074 C GLY B 105 47.459 46.698 19.897 1.00 9.14 C
ATOM 3075 O GLY B 105 47.629 45.791 19.103 1.00 8.26 O
ATOM 3076 N GLY B 106 47.908 46.667 21.155 1.00 9.61 N
ATOM 3077 CA GLY B 106 48.797 45.626 21.663 1.00 10.32 C
ATOM 3078 C GLY B 106 48.299 44.200 21.478 1.00 10.39 C
ATOM 3079 O GLY B 106 49.003 43.367 20.917 1.00 9.26 O
ATOM 3080 N GLY B 107 47.070 43.931 21.916 1.00 10.06 N
ATOM 3081 CA GLY B 107 46.463 42.614 21.735 1.00 10.25 C
ATOM 3082 C GLY B 107 46.317 42.190 20.282 1.00 10.39 C
ATOM 3083 O GLY B 107 46.562 41.032 19.943 1.00 11.63 O
ATOM 3084 N SER B 108 45.912 43.123 19.420 1.00 10.07 N
ATOM 3085 CA SER B 108 45.768 42.841 17.991 1.00 9.47 C
ATOM 3086 CB SER B 108 45.073 43.995 17.281 1.00 10.64 C
ATOM 3087 OG SER B 108 43.692 44.065 17.624 1.00 13.30 O
ATOM 3088 C SER B 108 47.127 42.599 17.342 1.00 9.37 C
ATOM 3089 O SER B 108 47.263 41.750 16.452 1.00 8.15 O
ATOM 3090 N SER B 109 48.132 43.349 17.790 1.00 7.70 N
ATOM 3091 CA SER B 109 49.479 43.170 17.267 1.00 8.77 C
ATOM 3092 CB SER B 109 50.409 44.261 17.788 1.00 7.05 C
ATOM 3093 OG SER B 109 51.683 44.194 17.155 1.00 9.74 O
ATOM 3094 C SER B 109 50.006 41.784 17.649 1.00 7.45 C
ATOM 3095 O SER B 109 50.624 41.106 16.831 1.00 9.02 O
ATOM 3096 N ASN B 110 49.777 41.380 18.902 1.00 9.11 N
ATOM 3097 CA ASN B 110 50.097 40.014 19.343 1.00 8.22 C
ATOM 3098 CB ASN B 110 49.646 39.756 20.794 1.00 8.80 C
ATOM 3099 CG ASN B 110 50.362 40.639 21.825 1.00 5.96 C
ATOM 3100 OD1 ASN B 110 49.956 40.683 22.976 1.00 8.37 O
ATOM 3101 ND2 ASN B 110 51.408 41.354 21.409 1.00 6.92 N
ATOM 3102 C ASN B 110 49.472 38.971 18.410 1.00 7.89 C
ATOM 3103 O ASN B 110 50.142 38.049 17.956 1.00 8.49 O
ATOM 3104 N ALA B 111 48.199 39.144 18.086 1.00 8.00 N
ATOM 3105 CA ALA B 111 47.511 38.179 17.218 1.00 7.72 C
ATOM 3106 CB ALA B 111 46.005 38.494 17.133 1.00 8.09 C
ATOM 3107 C ALA B 111 48.134 38.123 15.824 1.00 7.74 C
ATOM 3108 O ALA B 111 48.359 37.048 15.288 1.00 6.82 O
ATOM 3109 N ALA B 112 48.420 39.289 15.253 1.00 7.31 N
ATOM 3110 CA ALA B 112 48.980 39.385 13.902 1.00 7.25 C
ATOM 3111 CB ALA B 112 49.048 40.829 13.475 1.00 6.59 C
ATOM 3112 C ALA B 112 50.362 38.768 13.820 1.00 7.58 C
ATOM 3113 O ALA B 112 50.702 38.090 12.846 1.00 8.83 O
ATOM 3114 N THR B 113 51.161 39.017 14.846 1.00 6.87 N
ATOM 3115 CA THR B 113 52.505 38.468 14.914 1.00 6.43 C
ATOM 3116 CB THR B 113 53.247 39.062 16.111 1.00 6.74 C
ATOM 3117 OG1 THR B 113 53.661 40.394 15.779 1.00 6.87 O
ATOM 3118 CG2 THR B 113 54.559 38.318 16.348 1.00 5.25 C
ATOM 3119 C THR B 113 52.470 36.952 15.003 1.00 6.32 C
ATOM 3120 O THR B 113 53.248 36.268 14.340 1.00 7.09 O
ATOM 3121 N VAL B 114 51.552 36.430 15.804 1.00 6.73 N
ATOM 3122 CA VAL B 114 51.379 34.977 15.919 1.00 6.39 C
ATOM 3123 CB VAL B 114 50.394 34.623 17.067 1.00 6.47 C
ATOM 3124 CG1 VAL B 114 50.031 33.140 17.069 1.00 5.28 C
ATOM 3125 CG2 VAL B 114 51.002 35.019 18.410 1.00 7.43 C
ATOM 3126 C VAL B 114 50.935 34.382 14.573 1.00 7.55 C
ATOM 3127 O VAL B 114 51.512 33.382 14.103 1.00 7.87 O
ATOM 3128 N LEU B 115 49.939 35.008 13.940 1.00 7.48 N
ATOM 3129 CA LEU B 115 49.488 34.561 12.608 1.00 8.81 C
ATOM 3130 CB LEU B 115 48.375 35.460 12.075 1.00 8.72 C
ATOM 3131 CG LEU B 115 47.027 35.351 12.789 1.00 10.82 C
ATOM 3132 CD1 LEU B 115 46.048 36.368 12.204 1.00 14.09 C
ATOM 3133 CD2 LEU B 115 46.464 33.918 12.721 1.00 11.99 C
ATOM 3134 C LEU B 115 50.625 34.513 11.594 1.00 9.10 C
ATOM 3135 O LEU B 115 50.836 33.500 10.930 1.00 8.58 O
ATOM 3136 N VAL B 116 51.374 35.606 11.492 1.00 9.30 N
ATOM 3137 CA VAL B 116 52.441 35.701 10.493 1.00 10.22 C
ATOM 3138 CB VAL B 116 52.929 37.175 10.329 1.00 9.41 C
ATOM 3139 CG1 VAL B 116 54.210 37.254 9.520 1.00 11.25 C
ATOM 3140 CG2 VAL B 116 51.833 38.025 9.677 1.00 10.67 C
ATOM 3141 C VAL B 116 53.613 34.745 10.814 1.00 10.13 C
ATOM 3142 O VAL B 116 54.157 34.082 9.918 1.00 10.49 O
ATOM 3143 N ALA B 117 53.996 34.678 12.085 1.00 10.41 N
ATOM 3144 CA ALA B 117 55.128 33.844 12.503 1.00 9.69 C
ATOM 3145 CB ALA B 117 55.480 34.120 13.947 1.00 8.73 C
ATOM -3146 C ALA B 117 54.827 32.360 12.312 1.00 10.16 C
ATOM 3147 O ALA B 117 55.627 31.616 11.735 1.00 10.93 O
ATOM 3148 N LEU B 118 53.671 31.928 12.800 1.00 10.45 N
ATOM 3149 CA LEU B 118 53.325 30.509 12.712 1.00 10.75 C
ATOM 3150 CB LEU B 118 52.152 30.157 13.636 1.00 9.76 C
ATOM 3151 CG LEU B 118 52.476 30.160 15.143 1.00 11.01 C
ATOM 3152 CD1 LEU B 118 51.241 29.803 15.964 1.00 11.03 C
ATOM 3153 CD2 LEU B 118 53.616 29.216 15.468 1.00 12.11 C
ATOM 3154 C LEU B 118 53.037 30.114 11.259 1.00 10.26 C
ATOM 3155 O LEU B 118 53.332 29.003 10.869 1.00 9.77 O
ATOM 3156 N ASN B 119 52.493 31.033 10.460 1.00 10.48 N
ATOM 3157 CA ASN B 119 52.358 30.767 9.013 1.00 12.84 C
ATOM 3158 CB ASN B 119 51.718 31.957 8.271 1.00 11.72 C
ATOM 3159 CG ASN B 119 51.488 31.678 6.786 1.00 15.58 C
ATOM 3160 OD1 ASN B 119 50.816 30.709 6.424 1.00 15.51 o
ATOM 3161 ND2 ASN B 119 52.051 32.532 5.919 1.00 11.09 N
ATOM 3162 C ASN B 119 53.714 30.409 8.404 1.00 13.15 C
ATOM 3163 O ASN B 119 53.829 29.449 7.635 1.00 12.67 O
ATOM 3164 N HIS B 120 54.743 31.164 8.791 1.00 14.48 N
ATOM 3165 CA HIS B 120 56.106 30.911 8.343 1.00 15.98 C
ATOM 3166 CB HIS B 120 57.004 32.106 8.686 1.00 17.15 C
ATOM 3167 CG HIS B 120 58.443 31.896 8.335 1.00 21.07 C
ATOM 3168 ND1 HIS B 120 58.917 32.009 7.045 1.00 23.60 N
ATOM 3169 CE1 HIS B 120 60.217 31.773 7.035 1.00 25.21 C
ATOM 3170 NE2 HIS B 120 60.603 31.511 8.270 1.00 25.23 N
ATOM 3171 CD2 HIS B 120 59.512 31.579 9.103 1.00 23.11 C
ATOM 3172 C HIS B 120 56.697 29.635 8.951 1.00 16.41 C
ATOM 3173 O HIS B 120 57.256 28.791 8.229 1.00 17.21 O
ATOM 3174 N LEU B 121 56.591 29.504 10.274 1.00 14.47 N
ATOM 3175 CA LEU B 121 57.240 28.399 10.985 1.00 14.28 C
ATOM 3176 CB LEU B 121 57.265 28.658 12.507 1.00 13.27 C
ATOM 3177 CG LEU B 121 58.130 29.839 12.984 1.00 12.95 C
ATOM 3178 CD1 LEU B 121 57.782 30.200 14.429 1.00 8.92 C
ATOM 3179 CD2 LEU B 121 59.626 29.553 12.827 1.00 10.08 C
ATOM 3180 C LEU B 121 56.582 27.051 10.675 1.00 14.41 C
ATOM 3181 O LEU B 121 57.268 26.030 10.546 1.00 13.05 O
ATOM 3182 N TRP B 122 55.255 27.052 10.546 1.00 14.60 N
ATOM 3183 CA TRP B 122 54.533 25.826 10.181 1.00 15.38 C
ATOM 3184 CB TRP B 122 53.106 25.847 10.700 1.00 13.99 C
ATOM 3185 CG TRP B 122 52.929 25.693 12.180 1.00 11.52 C
ATOM 3186 CD1 TRP B 122 53.806 25.138 13.078 1.00 9.90 C
ATOM 3187 NE1 TRP B 122 53.256 25.155 14.339 1.00 11.33 N
ATOM 3188 CE2 TRP B 122 52.005 25.717 14.272 1.00 8.40 C
ATOM 3189 CD2 TRP B 122 51.772 26.063 12.924 1.00 9.34 C
ATOM 3190 CE3 TRP B 122 50.543 26.658 12.586 1.00 8.74 C
ATOM 3191 CZ3 TRP B 122 49.604 26.886 13.590 1.00 10.90 C
ATOM 3192 CH2 TRP B 122 49.867 26.523 14.916 1.00 8.90 C
ATOM 3193 CZ2 TRP B 122 51.065 25.946 15.278 1.00 9.56 C
ATOM 3194 C TRP B 122 54.468 25.633 8.667 1.00 16.85 C
ATOM 3195 O TRP B 122 53.860 24.680 8.202 1.00 16.65 O
ATOM 3196 N GLN B 123 55.045 26.563 7.907 1.00 17.86 N
ATOM 3197 CA GLN B 123 55.160 26.437 6.440 1.00 19.48 C
ATOM 3198 CB GLN B 123 56.062 25.244 6.067 1.00 21.24 C
ATOM 3199 CG GLN B 123 57.437 25.266 6.724 1.00 27.38 C
ATOM 3200 CD GLN B 123 58.317 24.119 6.275 1.00 35.73 C
ATOM 3201 OE1 GLN B 123 58.215 23.007 6.801 1.0040.04 O
ATOM 3202 NE2 GLN B 123 59.192 24.384 5.306 1.00 39.09 N
ATOM 3203 C GLN B 123 53.809 26.323 5.710 1.00 19.29 C
ATOM 3204 O GLN B 123 53.689 25.581 4.736 1.00 19.19 O
ATOM 3205 N CYS B 124 52.806 27.068 6.170 1.00 18.36 N
ATOM 3206 CA- CYS B 124 51.444 26.910 5.668 1.00 18.91 C
ATOM 3207 CB CYS B 124 50.426 27.482 6.661 1.00 18.12 C
ATOM 3208 SG CYS B 124 50.490 26.754 8.316 1.00 17.13 S
ATOM 3209 C CYS B 124 51.256 27.562 4.301 1.00 20.47 C
ATOM 3210 O CYS B 124 50.380 27.155 3.525 1.00 19.94 O
ATOM 3211 N GLY B 125 52.070 28.584 4.023 1.00 21.33 N
ATOM 3212 CA GLY B 125 52.046 29.268 2.738 1.00 21.71 C
ATOM 3213 C GLY B 125 50.785 30.071 2.457 1.00 22.15 C
ATOM 3214 0 GLY B 125 50.452 30.309 1.293 1.00 21.65 O
ATOM 3215 N LEU B 126 50.083 30.492 3.510 1.00 21.91 N
ATOM 3216 CA LEU B 126 48.890 31.317 3.345 1.00 22.12 C
ATOM 3217 CB LEU B 126 48.075 31.412 4.638 1.00 22.39 C
ATOM 3218 CG LEU B 126 47.472 30.204 5.384 1.00 24.82 C
ATOM 3219 CD1 LEU B 126 46.019 30.492 5.724 1.00 25.35 C
ATOM 3220 CD2 LEU B 126 47.580 28.916 4.622 1.00 21.21 C
ATOM 3221 C LEU B 126 49.311 32.709 2.909 1.00 22.24 C
ATOM 3222 0 LEU B 126 50.404 33.163 3.249 1.00 22.44 O
ATOM 3223 N SER B 127 48.455 33.385 2.148 1.00 22.05 N
ATOM 3224 CA SER B 127 48.757 34.735 1.709 1.00 22.45 C
ATOM 3225 CB SER B 127 47.966 35.089 0.448 1.00 21.91 C
ATOM 3226 OG SER B 127 46.603 35.299 0.760 1.00 22.08 O
ATOM 3227 C SER B 127 48.433 35.719 2.819 1.00 23.21 C
ATOM 3228 0 SER B 127 47.751 35.377 3.796 1.00 22.53 O
ATOM 3229 N MSE B 128 48.894 36.952 2.655 1.00 24,40 N
ATOM 3230 CA MSE B 128 48.608 37.992 3.626 1.00 25.64 C
ATOM 3231 CB AMSE B 128 49.480 39.229 3.408 1.00 27.15 C
ATOM 3232 CB BMSE B 128 49.454 39.225 3.297 1.00 27.61 C
ATOM 3233 CG AMSE B 128 50.319 39.678 4.662 0.50 26.27 C
ATOM 3234 CG BMSE B 128 50.955 39.053 3.620 0.50 27.61 C
ATOM 3235 SE AMSE B 128 51.555 38.352 5.486 0.50 31.57 SE
ATOM 3236 SE BMSE B 128 51.845 40.748 3.940 0.50 37.10 SE
ATOM 3238 C MSE B 128 47.133 38.350 3.593 1.00 24.59 C
ATOM 3239 O MSE B 128 46.561 38.710 4.614 1.00 24.25 O
ATOM 3240 N ASP B 129 46.519 38.226 2.416 1.00 23.38 N
ATOM 3241 CA ASP B 129 45.069 38.348 2.263 1.00 22.41 C
ATOM 3242 CB ASP B 129 44.663 38.091 0.807 1.00 23.58 C
ATOM 3243 CG ASP B 129 44.583 39.360 -0.034 1.00 25.40 C
ATOM 3244 OD1 ASP B 129 44.647 40.488 0.516 1.00 23.91 O
ATOM 3245 OD2 ASP B 129 44.447 39.309 -1.277 1.00 29.59 O
ATOM 3246 C ASP B 129 44.310 37.362 3.164 1.00 20.81 C
ATOM 3247 O ASP B 129 43.329 37.721 3.819 1.00 20.65 O
ATOM 3248 N GLU B 130 44.758 36.113 3.169 1.00 19.82 N
ATOM 3249 CA GLU B 130 44.097 35.060 3.941 1.00 18.98 C
ATOM 3250 CB GLU B 130 44.617 33.692 3.514 1.00 19.53 C
ATOM 3251 CG GLU B 130 44.198 33.299 2.109 1.00 23.09 C
ATOM 3252 CD GLU B 130 44.700 31.929 1.716 1.00 24.93 C
ATOM 3253 OE1 GLU B 130 43.895 30.972 1.787 1.00 30.07 O
ATOM 3254 OE2 GLU B 130 45.892 31.806 1.341 1.00 24.56 O
ATOM 3255 C GLU B 130 44.312 35.253 5.435 1.00 17.45 C
ATOM 3256 0 GLU B 130 43.382 35.092 6.242 1.00 16.74 O
ATOM 3257 N LEU B 131 45.534 35.622 5.798 1.00 15.57 N
ATOM 3258 CA LEU B 131 45.862 35.873 7.194 1.00 14.58 C
ATOM 3259 CB LEU B 131 47.377 36.072 7.366 1.00 13.43 C
ATOM 3260 CG LEU B 131 48.297 34.861 7.164 1.00 14.09 C
ATOM 3261 CD1 LEU B 131 49.711 35.212 7.578 1.00 14.73 C
ATOM 3262 CD2 LEU B 131 47.807 33.629 7.945 1.00 12.44 C
ATOM 3263 C LEU B 131 45.081 37.071 7.709 1.00 14.74 C
ATOM 3264 0 LEU B 131 44.535 37.031 8.813 1.00 13.94 O
ATOM 3265 N ALA B 132 44.990 38.128 6.893 1.00 15.00 N
ATOM 3266 CA ALA B 132 44.226 39.322 7.285 1.00 15.15 C
ATOM 3267 CB ALA B 132 44.489 40.492 6.320 1.00 14.91 C
ATOM 3268 C ALA B 132 42.728 39.040 7.404 1.00 14.89 C
ATOM 3269 0 AL B 132 42.055 39.588 8.276 1.00 13.52 O
ATOM 3270 N GLU B 133 42.219 38.167 6.543 1.00 16.79 N
ATOM 3271 CA GLU B 133 40.810 37.768 6.603 1.00 18.01 C
ATOM 3272 CB GLU B 133 40.454 36.823 5.448 1.00 19.20 C
ATOM 3273 CG GLU B 133 38.987 36.401 5.447 1.00 24.85 C
ATOM 3274 CD GLU B 133 38.614 35.514 4.270 1.00 28.93 C
ATOM 3275 OE1 GLU B 133 39.476 35.262 3.403 1.00 31.92 O
ATOM 3276 OE2 GLU B 133 37.448 35.073 4.213 1.00 33.89 O
ATOM 3277 C GLU B 133 40.482 37.107 7.938 1.00 17.05 C
ATOM 3278 0 GLU B 133 39.530 37.494 8.612 1.00 16.69 O
ATOM 3279 N MSE B 134 41.284 36.128 8.339 1.00 18.01 N
ATOM 3280 CA MSE B 134 41.011 35.439 9.602 1.00 18.72 C
ATOM 3281 CB MSE B 134 41.737 34.080 9.665 1.00 19.62 C
ATOM 3282 CG MSE B 134 43.220 34.121 10.020 1.00 23.96 C
ATOM 3283 SE MSE B 134 44.043 32.315 9.922 1.00 36.59 SE
ATOM 3284 CE MSE B 134 43.908 32.076 8.005 1.00 21.57 C
ATOM 3285 C MSE B 134 41.347 36.333 10.791 1.00 18.01 C
ATOM 3286 O MSE B 134 40.643 36.321 11.812 1.00 18.34 O
ATOM 3287 N GLY B 135 42.367 37.174 10.625 1.00 17.15 N
ATOM 3288 CA GLY B 135 42.738 38.123 11.657 1.00 15.85 C
ATOM 3289 C GLY B 135 41.626 39.074 12.044 1.00 14.68 C
ATOM 3290 O GLY B 135 41.478 39.430 13.213 1.00 14.98 O
ATOM 3291 N LEU B 136 40.841 39.486 11.054 1.00 14.81 N
ATOM 3292 CA LEU B 136 39.696 40.365 11.281 1.00 15.92 C
ATOM 3293 CB LEU B 136 39.023 40.720 9.937 1.00 15.48 C
ATOM 3294 CG LEU B 136 37.737 41.550 9.908 1.00 17.51 C
ATOM 3295 CD1 LEU B 136 37.937 42.923 10.514 1.00 19.80 C
ATOM 3296 CD2 LEU B 136 37.206 41.672 8.466 1.00 18.96 C
ATOM 3297 C LEU B 136 38.684 39.764 12.269 1.00 15.45 C
ATOM 3298 O LEU B 136 38.053 40.499 13.031 1.00 15.91 O
ATOM 3299 N THR B 137 38.552 38.435 12.295 1.00 16.27 N
ATOM 3300 CA THR B 137 37.613 37.806 13.251 1.00 16.24 C
ATOM 3301 CB THR B 137 37.366 36.297 12.947 1.00 16.40 C
ATOM 3302 OG1 THR B 137 38.547 35.530 13.228 1.00 17.32 O
ATOM 3303 CG2 THR B 137 37.112 36.068 11.456 1.00 16.76 C
ATOM 3304 C THR B 137 38.055 37.990 14.700 1.00 16.71 C
ATOM 3305 O THR B 137 37.226 37.945 15.621 1.00 17.22 O
ATOM 3306 N LEU B 138 39.345 38.264 14.893 1.00 15.28 N
ATOM 3307 CA LEU B 138 39.901 38.467 16.232 1.00 15.75 C
ATOM 3308 CB LEU B 138 41.304 37.852 16.330 1.00 14.97 C
ATOM 3309 CG LEU B 138 41.431 36.388 15.886 1.00 17.54 C
ATOM 3310 CD1 LEU B 138 42.876 35.985 15.796 1.00 20.40 C
ATOM 3311 CD2 LEU B 138 40.672 35.464 16.842 1.00 18.73 C
ATOM 3312 C LEU B 138 39.960 39.930 16.632 1.00 16.33 C
ATOM 3313 O LEU B 138 40.047 40.243 17.812 1.00 17.21 O
ATOM 3314 N GLY B 139 39.911 40.827 15.652 1.00 16.02 N
ATOM 3315 CA GLY B 139 39.961 42.245 15.940 1.00 16.16 C
ATOM 3316 C GLY B 139 40.053 43.107 14.699 1.00 15.97 C
ATOM 3317 O GLY B 139 40.668 42.720 13.703 1.00 16.08 O
ATOM 3318 N ALA B 140 39.427 44.279 14.770 1.00 15.85 N
ATOM 3319 CA ALA B 140 39.443 45.262 13.690 1.00 16.18 C
ATOM 3320 CB ALA B 140 38.557 46.456 14.050 1.00 15.57 C
ATOM 3321 C ALA B 140 40.860 45.741 13.356 1.00 15.90 C
ATOM 3322 O ALA B 140 41.154 46.047 12.197 1.00 16.49 O
ATOM 3323 N ASP B 141 41.726 45.805 14.372 1.00 15.58 N
ATOM 3324 CA ASP B 141 43.101 46.280 14.191 1.00 14.94 C
ATOM 3325 CB ASP B 141 43.644 46.879 15.487 1.00 16.20 C
ATOM 3326 CG ASP B 141 43.127 48.273 15.758 1.00 19.41 C
ATOM 3327 OD1 ASP B 141 42.492 48.880 14.865 1.00 20.12 O
ATOM 3328 OD2 ASP B 141 43.288 48.827 16.862 1.00 20.82 O
ATOM 3329 C ASP B 141 44.071 45.188 13.733 1.00 13.81 C
ATOM 3330 O ASP B 141 45.219 45.479 13.401 1.00 12.85 O
ATOM 3331 N VAL B 142 43.638 43.935 13.733 1.00 12.90 N
ATOM 3332 CA VAL B 142 44.576 42.853 13.391 1.00 11.82 C
ATOM 3333 CB VAL B 142 44.014 41.432 13.727 1.00 12.02 C
ATOM 3334 CG1 VAL B 142 44.958 40.344 13.225 1.00 9.87 C
ATOM 3335 CG2 VAL B 142 43.765 41.286 15.219 1.00 10.21 C
ATOM 3336 C VAL B 142 45.086 42.921 11.931 1.00 11.66 C
ATOM 3337 O VAL B 142 46.280 42.751 11.714 1.00 12.27 O
ATOM 3338 N PRO B 143 44.209 43.147 10.936 1.00 11.00 N
ATOM 3339 CA PRO B 143 44.655 43.219 9.526 1.00 9.99 C
ATOM 3340 CB PRO B 143 43.364 43.606 8.768 1.00 10.05 C
ATOM 3341 CG PRO B 143 42.267 43.002 9.612 1.00 10.56 C
ATOM 3342 CD PRO B 143 42.740 43.267 11.039 1.00 10.96 C
ATOM 3343 C PRO B 143 45.796 44.222 9.218 1.00 8.79 C
ATOM 3344 O PRO B 143 46.681 43.897 8.432 1.00 8.12 O
ATOM 3345 N VAL B 144 45.789 45.415 9.800 1.00 8.74 N
ATOM 3346 CA VAL B 144 46.875 46.362 9.468 1.00 7.94 C
ATOM 3347 CB VAL B 144 46.655 47.784 10.060 1.00 8.79 C
ATOM 3348 CG1 VAL B 144 46.703 47.790 11.596 1.00 7.30 C
ATOM 3349 CG2 VAL B 144 47.682 48.752 9.481 1.00 6.26 C
ATOM 3350 C VAL B 144 48.245 45.784 9.866 1.00 8.65 C
ATOM 3351 O VAL B 144 49.214 45.855 9.089 1.00 7.27 O
ATOM 3352 N PHE B 145 48.292 45.150 11.043 1.00 8.01 N
ATOM 3353 CA PHE B 145 49.515 44.523 11.526 1.00 8.65 C
ATOM 3354 CB PHE B 145 49.338 44.034 12.973 1.00 7.91 C
ATOM 3355 CG PHE B 145 49.315 45.128 13.980 1.00 7.75 C
ATOM 3356 CD1 PHE B 145 48.125 45.485 14.605 1.00 6.53 C
ATOM 3357 CE1 PHE B 145 48.098 46.493 15.551 1.00 8.12 C
ATOM 3358 CZ PHE B 145 49.260 47.168 15.871 1.00 8.91 C
ATOM 3359 CE2 PHE B 145 50.450 46.835 15.247 1.00 8.94 C
ATOM 3360 CD2 PHE B 145 50.475 45.815 14.307 1.00 7.53 C
ATOM 3361 C PHE B 145 49.936 43.361 10.639 1.00 9.32 C
ATOM 3362 O PHE B 145 51.138 43.167 10.389 1.00 9.64 O
ATOM 3363 N VAL B 146 48.955 42.583 10.175 1.00 9.56 N
ATOM 3364 CA VAL B 146 49.220 41.457 9.270 1.00 10.19 C
ATOM 3365 CB VAL B 146 47.939 40.648 8.978 1.00 10.69 C
ATOM 3366 CG1 VAL B 146 48.168 39.675 7.814 1.00 11.68 C
ATOM 3367 CG2 VAL B 146 47.466 39.896 10.240 1.00 8.25 C
ATOM 3368 C VAL B 146 49.858 41.912 7.945 1.00 11.79 C
ATOM 3369 0 VAL B 146 50.843 41.328 7.487 1.00 11.27 O
ATOM 3370 N ARG B 147 49.302 42.957 7.337 1.00 11.39 N
ATOM 3371 CA ARG B 147 49.767 43.382 6.022 1.00 11.72 C
ATOM 3372 CB ARG B 147 48.692 44.205 5.304 1.00 11.65 C
ATOM 3373 CG ARG B 147 47.385 43.451 5.066 1.00 13.14 C
ATOM 3374 CD ARG B 147 46.384 44.233 4.209 1.00 14.99 C
ATOM 3375 NE ARG B 147 45.098 43.554 4.060 1.00 17.74 N
ATOM 3376 CZ ARG B 147 44.846 42.602 3.160 1.00 15.38 C
ATOM 3377 NH1 ARG B 147 45.798 42.191 2.346 1.00 14.64 N
ATOM 3378 NH2 ARG B 147 43.633 42.064 3.079 1.00 15.95 N
ATOM 3379 C ARG B 147 51.072 44.166 6.141 1.00 11.85 C
ATOM 3380 O ARG B 147 51.833 44.244 5.184 1.00 11.62 O
ATOM 3381 N GLY B 148 51.322 44.732 7.327 1.00 10.34 N
ATOM 3382 CA GLY B 148 52.632 45.256 7.682 1.00 11.03 C
ATOM 3383 C GLY B 148 53.095 46.585 7.090 1.00 11.04 C
ATOM 3384 0 GLY B 148 54.298 46.878 7.100 1.00 12.03 O
ATOM 3385 N HIS B 149 52.168 47.397 6.582 1.00 10.56 N
ATOM 3386 CA HIS B 149 52.531 48.725 6.076 1.00 10.16 C
ATOM 3387 CB AHIS B 149 52.445 48.786 4.540 0.50 9.47 C
ATOM 3388 CB BHIS B 149 52.457 48 .752 4.535 0.50 11.45 C
ATOM 3389 CG AHIS B 149 53.298 49 858 3.930 0.50 5.91 C
ATOM 3390 CG BHIS B 149 53.411 47 804 3.865 0.50 14.80 C
ATOM 3391 ND1AHIS B 149 52.935 51 .189 3.923 0.50 3.16 N
ATOM 3392 ND1BHIS B 149 54.583 48 .223 3.269 0.50 18.46 N
ATOM 3393 CE1AHIS B 149 53.877 51 .899 3.329 0.50 3.85 C
ATOM 3394 CE1 BHIS B 149 55.214 47, .178 2.759 0.50 18.39 C
ATOM 3395 NE2AHIS B 149 54.841 51 .077 2.951 0.50 5.71 N
ATOM 3396 NE2BHIS B 149 54.500 46 .096 3.009 0.50 16.42 N
ATOM 3397 CD2AHIS B 149 54.506 49 .796 3.320 0.50 6.52 C
ATOM 3398 CD2BHIS B 149 53.364 46 .460 3.692 0.50 18.14 C
ATOM 3399 C HIS B 149 51.656 49.823 6.674 1.00 9.86 C
ATOM 3400 0 HIS B 149 50.461 49.623 6.898 1.00 8.67 O
ATOM 3401 N ALA B 150 52.241 50.995 6.921 1.00 9.01 N
ATOM 3402 CA ALA B 150 51.424 52.158 7.246 1.00 9.11 C
ATOM 3403 CB ALA B 150 52.256 53.429 7.311 1.00 9.38 C
ATOM 3404 C ALA B 150 50.342 52.288 6.198 1.00 9.87 C
ATOM 3405 O ALA B 150 50.588 52.066 4.999 1.00 8.37 O
ATOM 3406 N ALA B 151 49.127 52.606 6.645 1.00 9.59 N
ATOM 3407 CA ALA B 151 47.975 52.496 5.761 1.00 9.65 C
ATOM 3408 CB ALA B 151 47.494 51.054 5.694 1.00 8.09 C
ATOM 3409 C ALA B 151 46.833 53.378 6.201 1.00 9.92 C
ATOM 3410 O ALA B 151 46.605 53.569 7.395 1.00 9.04 O
ATOM 3411 N PHE B 152 46.114 53.882 5.207 1.00 9.24 N
ATOM 3412 CA PHE B 152 44.810 54.473 5.381 1.00 9.15 C
ATOM 3413 CB PHE B 152 44.511 55.371 4.181 1.00 9.96 C
ATOM 3414 CG PHE B 152 43.168 56.032 4.238 1.00 10.00 C
ATOM 3415 CD1 PHE B 152 43.013 57.247 4.891 1.00 9.40 C
ATOM 3416 CE1 PHE B 152 41.774 57.876 4.953 1.00 12.52 C
ATOM 3417 CZ PHE B 152 40.677 57.286 4.349 1.00 15.10 C
ATOM 3418 CE2 PHE B 152 40.824 56.074 3.671 1.00 12.56 C
ATOM 3419 CD2 PHE B 152 42.065 55.450 3.628 1.00 11.26 C
ATOM 3420 C PHE B 152 43.791 53.355 5.457 1.00 9.55 C
ATOM 3421 O PHE B 152 43.883 52.378 4.702 1.00 10.22 O
ATOM 3422 N ALA B 153 42.808 53.491 6.346 1.00 8.72 N
ATOM 3423 CA ALA B 153 41.807 52.445 6.522 1.00 9.06 C
ATOM 3424 CB ALA B 153 42.111 51.617 7.772 1.00 8.57 C
ATOM 3425 C ALA B 153 40.382 52.974 6.585 1.00 9.77 C
ATOM 3426 O ALA B 153 40.105 53.978 7.260 1.00 9.25 O
ATOM 3427 N GLU B 154 39.484 52.287 5.873 1.00 9.70 N
ATOM 3428 CA GLU B 154 38.044 52.496 6.020 1.00 10.92 C
ATOM 3429 CB GLU B 154 37.398 52.913 4.681 1.00 11.16 C
ATOM 3430 CG GLU B 154 38.045 54.141 4.067 1.00 13.52 C
ATOM 3431 CD GLU B 154 37.131 54.926 3.135 1.00 17.14 C
ATOM 3432 OE1 GLU B 154 36.106 54.374 2.667 1.00 18.25 O
ATOM 3433 OE2 GLU B 154 37.463 56.096 2.850 1.00 14.85 O
ATOM 3434 C GLU B 154 37.395 51.224 6.591 1.00 11.02 C
ATOM 3435 0 GLU B 154 38.089 50.358 7.137 1.00 11.62 O
ATOM 3436 N GLY B 155 36.078 51.109 6.458 1.00 11.03 N
ATOM 3437 CA GLY B 155 35.334 50.060 7.138 1.00 12.81 C
ATOM 3438 C GLY B 155 35.400 50.243 8.647 1.00 13.57 C
ATOM 3439 0 GLY B 155 35.221 51.349 9.152 1.00 14.62 O
ATOM 3440 N VAL B 156 35.679 49.166 9.368 1.00 13.19 N
ATOM 3441 CA VAL B 156 35.950 49.271 10.797 1.00 13.70 C
ATOM 3442 CB VAL B 156 35.292 48.115 11.579 1.00 13.69 C
ATOM 3443 CG1 VAL B 156 33.788 48.151 11.379 1.00 13.43 C
ATOM 3444 CG2 VAL B 156 35.864 46.752 11.152 1.00 12.83 C
ATOM 3445 C VAL B 156 37.464 49.341 11.069 1.00 13.70 C
ATOM 3446 O VAL B 156 37.905 49.235 12.221 1.00 13.98 O
ATOM 3447 N GLY B 157 38.242 49.521 9.998 1.00 12.27 N
ATOM 3448 CA GLY B 157 39.689 49.664 10.086 1.00 11.73 C
ATOM 3449 C GLY B 157 40.454 48.651 9.248 1.00 12.33 C
ATOM 3450 O GLY B 157 41.679 48.645 9.248 1.00 11.54 O
ATOM 3451 N GLU B 158 39.726 47.814 8.512 1.00 11.70 N
ATOM 3452 CA GLU B 158 40.322 46.685 7.790 1.00 12.38 C
ATOM 3453 CB GLU B 158 39.498 45.419 8.059 1.00 12.34 C
ATOM 3454 CG GLU B 158 38.320 45.214 7.101 1.00 13.89 C
ATOM 3455 CD GLU B 158 37.090 46.041 7.458 1.00 15.53 C
ATOM 3456 OE1 GLU B 158 35.987 45.641 7.034 1.00 16.90 O
ATOM 3457 OE2 GLU B 158 37.210 47.098 8.142 1.00 12.03 O
ATOM 3458 C GLU B 158 40.457 46.909 6.271 1.00 12.14 C
ATOM 3459 O GLU B 158 41.151 46.150 5.587 1.00 12.11 O
ATOM 3460 N ILE B 159 39.802 47.943 5.745 1.00 10.91 N
ATOM 3461 CA ILE B 159 39.861 48.216 4.306 1.00 10.56 C
ATOM 3462 CB ILE B 159 38.537 48.834 3.812 1.00 11.48 C
ATOM 3463 CG1 ILE B 159 37.352 47.931 4.172 1.00 12.47 C
ATOM 3464 CD1 ILE B 159 36.009 48.512 3.779 1.00 19.10 C
ATOM 3465 CG2 ILE B 159 38.579 49.089 2.296 1.00 10.21 C
ATOM 3466 C ILE B 159 41.046 49.137 4.026 1.00 9.79 C
ATOM 3467 O ILE B 159 40 948 50.333 4.175 1.00 9.57 O
ATOM 3468 N LEU B 160 42.175 48.559 3.632 1.00 9.78 N
ATOM 3469 CA LEU B 160 43.461 49.242 3.791 1.00 9.94 C
ATOM 3470 CB LEU B 160 44.422 48.353 4.598 1.00 10.53 C
ATOM 3471 CG LEU B 160 44.063 48.118 6.075 1.00 11.61 C
ATOM 3472 CD1 LEU B 160 44.549 46.747 6.534 1.00 12.38 C
ATOM 3473 CD2 LEU B 160 44.654 49.215 6.939 1.00 8.31 C
ATOM 3474 C LEU B 160 44.144 49.660 2.488 1.00 10.24 C
ATOM 3475 0 LEU B 160 44.227 48.871 1.540 1.00 11.25 O
ATOM 3476 N THR B 161 44.671 50.884 2.480 1.00 9.64 N
ATOM 3477 CA THR B 161 45.491 51.396 1.384 1.00 10.73 C
ATOM 3478 CB THR B 161 44.789 52.578 0.708 1.00 11.29 C
ATOM 3479 OG1 THR B 161 43.568 52.133 0.116 1.00 11.58 O
ATOM 3480 CG2 THR B 161 45.612 53.080 -0.479 1.00 14.07 C
ATOM 3481 C THR B 161 46.836 51.861 1.908 1.00 12.00 C
ATOM 3482 O THR B 161 46.898 52.793 2.716 1.00 11.95 O
ATOM 3483 N PRO B 162 47.918 51.234 1.452 1.00 12.78 N
ATOM 3484 CA PRO B 162 49.257 51.623 1.898 1.00 13.58 C
ATOM 3485 CB PRO B 162 50.189 50.665 .137 1.00 14.54 C
ATOM 3486 CG PRO B 162 49.308 49.527 0.710 1.00 14.17 C
ATOM 3487 CD PRO B 162 47.951 50.130 0.477 1.00 13.45 C
ATOM 3488 C PRO B 162 49.546 53.062 1.517 1.00 14.36 C
ATOM 3489 O PRO B 162 49.302 53.457 0.382 1.00 14.64 O
ATOM 3490 N VAL B 163 50.001 53.846 2.485 1.00 13.91 N
ATOM 3491 CA VAL B 163 50.463 55.206 2.243 1.00 14.85 C
ATOM 3492 CB VAL B 163 49.428 56.275 2.685 1.00 14.22 C
ATOM 3493 CG1 VAL B 163 48.166 56.251 1.786 1.00 16.06 C
ATOM 3494 CG2 VAL B 163 49.053 56.078 4.112 1.00 13.45 C
ATOM 3495 C VAL B 163 51.773 55.394 3.001 1.00 14.81 C
ATOM 3496 O VAL B 163 52.198 54.507 3.744 1.00 13.88 O
ATOM 3497 N ASP B 164 52.414 56.546 2.828 1.00 16.02 N
ATOM 3498 CA ASP B 164 53.739 56.746 3.392 1.00 17.09 C
ATOM 3499 CB ASP B 164 54.788 56.701 2.278 1.00 19.00 C
ATOM 3500 CG ASP B 164 54.918 55.331 1.658 1.00 21.16 C
ATOM 3501 OD1 ASP B 164 54.329 55.103 0.583 1.00 25.33 O
ATOM 3502 OD2 ASP B 164 55.588 54.423 2.177 1.00 23.68 O
ATOM 3503 C ASP B 164 53.853 58.072 4.145 1.00 18.30 C
ATOM 3504 O ASP B 164 54.499 58.999 3.653 1.00 17.53 O
ATOM 3505 N PRO B 165 53.241 58.167 5.331 1.00 17.58 N
ATOM 3506 CA PRO B 165 53.292 59.408 6.109 1.00 18.20 C
ATOM 3507 CB PRO B 165 52.286 59.155 7.249 1.00 17.75 C
ATOM 3508 CG PRO B 165 52.232 57.685 7.397 1.00 16.72 C
ATOM 3509 CD PRO B 165 52.478 57.112 6.027 1.00 17.25 C
ATOM 3510 C PRO B 165 54.689 59.616 6.660 1.00 18.84 C
ATOM 3511 O PRO B 165 55.451 58.647 6.749 1.00 19.24 O
ATOM 3512 N PRO B 166 55.036 60.856 7.004 1.00 19.30 N
ATOM 3513 CA PRO B 166 56.338 61.144 7.612 1.00 19.29 C
ATOM 3514 CB PRO B 166 56.194 62.601 8.054 1.00 19.91 C
ATOM 3515 CG PRO B 166 55.192 63.181 7.094 1.00 19.95 C
ATOM 3516 CD PRO B 166 54.221 62.073 6.831 1.00 18.60 C
ATOM 3517 C PRO B 166 56.608 60.246 8.818 1.00 19.15 C
ATOM 3518 O PRO B 166 55.695 59.987 9.599 1.00 19.45 O
ATOM 3519 N GLU B 167 57.848 59.777 8.946 1.00 19.24 N
ATOM 3520 CA GLU B 167 58.255 58.916 10.050 1.00 19.22 C
ATOM 3521 CB GLU B 167 59.239 57.842 9.556 1.00 19.12 C
ATOM 3522 CG GLU B 167 58.596 56.822 8.609 1.00 18.81 C
ATOM 3523 CD GLU B 167 59.565 55.778 8.081 1.00 21.10 C
ATOM 3524 OE1 GLU B 167 60.752 56.107 7.853 1.00 24.56 O
ATOM 3525 OE2 GLU B 167 59.137 54.616 7.883 1.00 16.94 O
ATOM 3526 C GLU B 167 58.855 59.729 11.201 1.00 20.04 C
ATOM 3527 O GLU B 167 60.069 59.882 11.306 1.00 20.71 O
ATOM 3528 N LYS B 168 57.987 60.227 12.072 1.00 19.52 N
ATOM 3529 CA LYS B 168 58.397 61.092 13.171 1.00 18.91 C
ATOM 3530 CB LYS B 168 57.266 62.063 13.527 1.00 20.23 C
ATOM 3531 CG LYS B 168 56.707 62.847 12.346 1.00 24.10 C
ATOM 3532 CD LYS B 168 56.228 64.222 12.773 1.00 31.16 C
ATOM 3533 CE LYS B 168 54.879 64.562 12.153 1.00 35.04 C
ATOM 3534 NZ LYS B 168 54.994 65.537 11.021 1.00 38.30 N
ATOM 3535 C LYS B 168 58.789 60.280 14.406 1.00 17.60 C
ATOM 3536 O LYS B 168 58.634 59.054 14.438 1.00 16.45 O
ATOM 3537 N TRP B 169 59.299 60.977 15.419 1.00 15.18 N
ATOM 3538 CA TRP B 169 59.517 60.386 16.724 1.00 14.05 C
ATOM 3539 CB TRP B 169 60.847 60.855 17.291 1.00 14.04 C
ATOM 3540 CG TRP B 169 61.998 60.194 16.610 1.00 15.91 C
ATOM 3541 CD1 TRP B 169 62.566 60.554 15.417 1.00 17.99 C
ATOM 3542 NE1 TRP B 169 63.583 59.687 15.097 1.00 19.07 N
ATOM 3543 CE2 TRP B 169 63.689 58.744 16.086 1.00 18.33 C
ATOM 3544 CD2 TRP B 169 62.691 59.025 17.045 1.00 14.89 C
ATOM 3545 CE3 TRP B 169 62.586 58.189 18.165 1.00 17.46 C
ATOM 3546 CZ3 TRP B 169 63.466 57.109 18.285 1.00 17.31 C
ATOM 3547 CH2 TRP B 169 64.443 56.862 17.315 1.00 15.26 C
ATOM 3548 CZ2 TRP B 169 64.574 57.665 16.213 1.00 19.28 C
ATOM 3549 C TRP B 169 58.363 60.749 17.652 1.00 13.68 C
ATOM 3550 O TRP B 169 57.803 61.839 17.550 1.00 14.14 O
ATOM 3551 N TYR B 170 57.992 59.830 18.542 1.00 13.21 N
ATOM 3552 CA TYR B 170 56.834 60.053 19.416 1.00 11.58 C
ATOM 3553 CB TYR B 170 55.646 59.166 19.003 1.00 11.05 C
ATOM 3554 CG TYR B 170 55.200 59.374 17.579 1.00 11.30 C
ATOM 3555 CD1 TYR B 170 55.636 58.523 16.569 1.00 12.31 C
ATOM 3556 CE1 TYR B 170 55.247 58.713 15.249 1.00 11.85 C
ATOM 3557 CZ TYR B 170 54.412 59.751 14.928 1.00 12.98 C
ATOM 3558 OH TYR B 170 54.034 59.908 13.611 1.00 16.07 O
ATOM 3559 CE2 TYR B 170 53.945 60.612 15.914 1.00 14.04 C
ATOM 3560 CD2 TYR B 170 54.345 60.424 17.234 1.00 11.73 C
ATOM 3561 C TYR B 170 57.151 59.825 20.889 1.00 11.16 C
ATOM 3562 O TYR B 170 57.873 58.895 21.246 1.00 10.38 O
ATOM 3563 N LEU B 171 56.622 60.699 21.737 1.00 10.99 N
ATOM 3564 CA LEU B 171 56.529 60.421 23.157 1.00 11.63 C
ATOM 3565 CB LEU B 171 56.839 61.682 23.984 1.00 11.96 C
ATOM 3566 CG LEU B 171 57.121 61.507 25.487 1.00 12.85 C
ATOM 3567 CD1 LEU B 171 57.647 62.802 26.072 1.00 14.37 C
ATOM 3568 CD2 LEU B 171 55.889 61.067 26.271 1.00 13.39 C
ATOM 3569 C LEU B 171 55.117 59.914 23.442 1.00 10.79 C
ATOM 3570 O LEU B 171 54.155 60.638 23.246 1.00 12.44 O
ATOM 3571 N VAL B 172 54.996 58.676 23.899 1.00 11.19 N
ATOM 3572 CA VAL B 172 53.686 58.073 24.161 1.00 10.62 C
ATOM 3573 CB VAL B 172 53.543 56.700 23.467 1.00 10.66 C
ATOM 3574 CG1 VAL B 172 52.172 56.045 23.773 1.00 9.37 C
ATOM 3575 CG2 VAL B 172 53.772 56.827 21.936 1.00 8.45 C
ATOM 3576 C VAL B 172 53.470 57.937 25.663 1.00 11.46 C
ATOM 3577 O VAL B 172 54.308 57.368 26.364 1.00 11.33 O
ATOM 3578 N ALA B 173 52.350 58.465 26.148 1.00 11.54 N
ATOM 3579 CA ALA B 173 52.077 58.538 27.581 1.00 12.86 C
ATOM 3580 CB ALA B 173 52.136 59.998 28.040 1.00 14.06 C
ATOM 3581 C ALA B 173 50.728 57.919 27.973 1.00 14.48 C
ATOM 3582 O ALA B 173 49.820 57.829 27.144 1,00 14.33 O
ATOM 3583 N HIS B 174 50.616 57.518 29.246 1.00 15.29 N
ATOM 3584 CA AHIS B 174 49.343 57.087 29.804 0.50 16.42 C
ATOM 3585 CA BHIS B 174 49.428 56.867 29 .829 0.50 16.57 C
ATOM 3586 CB AHIS B 174 48.971 55.653 29, 365 0.5016.32 C
ATOM 3587 CB BHIS B 174 49.573 55.348 29, 651 0.5016.02 C
ATOM 3588 CG AHIS B 174 49.801 54.582 29 993 0.5015.65 c
ATOM 3589 CG BHIS B 174 48.327 54.552 29 923 0.5017.09 c
ATOM 3590 ND1AHIS B 174 49.449 53.966 31.174 0.50 16.79 N
ATOM 3591 ND1BHIS B 174 48.071 53.347 29.298 0.50 17.46 N
ATOM 3592 CE1 AHIS B 174 50.358 53.058 31.483 0.50 16.90 C
ATOM 3593 CE1 BHIS B 174 46.925 52.858 29.736 0.50 14.67 C
ATOM 3594 NE2 AHIS B 174 51.277 53.051 30.534 0.50 17.09 N
ATOM 3595 NE2BHIS B 174 46.428 53.698 30.626 0.50 17.90 N
ATOM 3596 CD2AHIS B 174 50.948 53.991 29.587 0.50 15.08 C
ATOM 3597 CD2BHIS B 174 47.288 54.762 30.765 0.50 16.45 C
ATOM 3598 C HIS B 174 49.355 57.241 31.324 1.00 16.98 C
ATOM 3599 0 HIS B 174 50.357 57.040 32.001 1.00 18.12 O
ATOM 3600 N PRO B 175 48.224 57.728 31.866 1.00 17.46 N
ATOM 3601 CA PRO B 175 48.152 58.011 33.313 1.00 18.46 C
ATOM 3602 CB PRO B 175 47.021 59.050 33.411 1.00 18.31 C
ATOM 3603 CG PRO B 175 46.093 58.705 32.275 1.00 17.65 C
ATOM 3604 CD PRO B 175 46.956 58.076 31.188 1.00 17.04 C
ATOM 3605 C PRO B 175 47.815 56.783 34.179 1.00 19.35 C
ATOM 3606 O PRO B 175 47.753 56.896 35.405 1.00 19.01 O
ATOM 3607 N GLY B 176 47.601 55.632 33.557 1.00 20.57 N
ATOM 3608 CA GLY B 176 47.351 54.413 34.309 1.00 23.71 C
ATOM 3609 C GLY B 176 45.943 53.848 34.212 1.00 25.86 C
ATOM 3610 O GLY B 176 45.733 52.669 34.507 1.00 28.25 O
ATOM 3611 N VAL B 177 44.973 54.666 33.811 1.00 26.78 N
ATOM 3612 CA VAL B 177 43.590 54.188 33.706 1.00 27.45 C
ATOM 3613 CB VAL B 177 42.553 55.356 33.795 1.00 28.36 C
ATOM 3614 CG1 VAL B 177 42.536 56.205 32.516 1.00 28.32 C
ATOM 3615 CG2 VAL B 177 41.159 54.822 34.124 1.00 28.43 C
ATOM 3616 C VAL B 177 43.395 53.337 32.440 1.00 28.20 C
ATOM 3617 O VAL B 177 43.928 53.654 31.373 1.00 27.79 O
ATOM 3618 N SER B 178 42.686 52.220 32.580 1.00 28.77 N
ATOM 3619 CA SER B 178 42.460 51.336 31.446 1.00 28.59 C
ATOM 3620 CB ASER B 178 42.632 49.862 31.836 0.50 28.89 C
ATOM 3621 CB BSER B 178 42.654 49.877 31.855 0.50 28.93 C
ATOM 3622 OG ASER B 178 42.242 48.993 30.772 0.50 28.12 O
ATOM 3623 OG BSER B 178 44.014 49.624 32.171 0.50 28.64 O
ATOM 3624 C SER B 178 41.072 51.579 30.917 1.00 28.29 C
ATOM 3625 0 SER B 178 40.087 51.249 31.572 1.00 28.67 O
ATOM 3626 N ILE B 179 40.999 52.204 29.745 1.00 27.51 N
ATOM 3627 CA ILE B 179 39.726 52.508 29.113 1.00 26.87 C
ATOM 3628 CB ILE B 179 39.799 53.834 28.325 1.00 26.44 C
ATOM 3629 CG1 ILE B 179 40.218 54.992 29.235 1.00 26.00 C
ATOM 3630 CD1 ILE B 179 40.407 56.315 28.497 1.00 23.86 C
ATOM 3631 CG2 ILE B 179 38.460 54.130 27.655 1.00 26.89 C
ATOM 3632 C ILE B 179 39.342 51.377 28.171 1.00 26.80 C
ATOM 3633 O ILE B 179 40.039 51.129 27.187 1.00 25.76 O
ATOM 3634 N PRO B 180 38.244 50.681 28.467 1.00 26.88 N
ATOM 3635 CA PRO B 180 37.726 49.671 27.540 1.00 26.32 C
ATOM 3636 CB PRO B 180 36.549 49.052 28.301 1.00 26.51 C
ATOM 3637 CG PRO B 180 36.741 49.470 29.730 1.00 27.76 C
ATOM 3638 CD PRO B 180 37.401 50.818 29.667 1.00 27.50 C
ATOM 3639 C PRO B 180 37.241 50.358 26.268 1.00 25.46 C
ATOM 3640 O PRO B 180 36.520 51.355 26.350 1.00 23.93 O
ATOM 3641 N THR B 181 37.657 49.840 25.113 1.00 25.72 N
ATOM 3642 CA THR B 181 37.186 50.338 23.812 1.00 25.87 C
ATOM 3643 CB THR B 181 37.562 49.349 22.672 1.00 26.18 C
ATOM 3644 OG1 THR B 181 38.964 49.056 22.733 1.00 28.94 O
ATOM 3645 CG2 THR B 181 37.420 50.006 21.322 1.00 26.69 C
ATOM 3646 C THR B 181 35.675 50.699 23.775 1.00 26.06 C
ATOM 3647 O THR B 181 35.338 51.822 23.405 1.00 25.44 O
ATOM 3648 N PRO B 182 34.773 49.774 24.160 1.00 26.31 N
ATOM 3649 CA PRO B 182 33.325 50.051 24.106 1.00 25.61 C
ATOM 3650 CB PRO B 182 32.692 48.752 24.647 1.00 26.25 C
ATOM 3651 CG PRO B 182 33.786 48.031 25.334 1.00 25.00 C
ATOM 3652 CD PRO B 182 35.035 48.392 24.616 1.00 26.59 C
ATOM 3653 C PRO B 182 32.850 51.245 24.942 1.00 25.15 C
ATOM 3654 O PRO B 182 31.852 51.863 24.577 1.00 25.00 O
ATOM 3655 N VAL B 183 33.542 51.571 26.029 1.00 24.81 N
ATOM 3656 CA VAL B 183 33.124 52.696 26.871 1.00 24.32 C
ATOM 3657 CB VAL B 183 33.992 52.801 28.151 1.00 25.00 C
ATOM 3658 CG1 VAL B 183 33.664 54.054 28.936 1.00 26.76 C
ATOM 3659 CG2 VAL B 183 33.779 51.570 29.025 1.00 27.20 C
ATOM 3660 C VAL B 183 33.130 54.013 26.093 1.00 22.72 C
ATOM 3661 O VAL B 183 32.218 54.837 26.234 1.00 22.02 O
ATOM 3662 N ILE B 184 34.145 54.206 25.255 1.00 21.44 N
ATOM 3663 CA ILE B 184 34.207 55.412 24.426 1.00 20.32 C
ATOM 3664 CB ILE B 184 35.647 55.657 23.907 1.00 19.56 C
ATOM 3665 CG1 ILE B 184 36.606 55.946 25.078 1.00 18.24 C
ATOM 3666 CD1 ILE B 184 36.250 57.177 25.921 1.00 14.80 C
ATOM 3667 CG2 ILE B 184 35.676 56.796 22.899 1.00 17.52 C
ATOM 3668 C ILE B 184 33.212 55.326 23.264 1.00 20.62 C
ATOM 3669 O ILE B 184 32.445 56.260 23.021 1.00 20.02 O
ATOM 3670 N PHE B 185 33.213 54.196 22.566 1.00 21.85 N
ATOM 3671 CA PHE B 185 32.365 54.029 21.375 1.00 23.07 C
ATOM 3672 CB PHE B 185 32.727 52.743 20.624 1.00 22.89 C
ATOM 3673 CG PHE B 185 33.759 52.947 19.556 1.00 22.19 C
ATOM 3674 CD1 PHE B 185 34.959 52.255 19.589 1.00 24.19 C
ATOM 3675 CE1 PHE B 185 35.917 52.452 18.601 1.00 24.90 C
ATOM 3676 CZ PHE B 185 35.676 53.355 17.577 1.00 23.92 C
ATOM 3677 CE2 PHE B 185 34.485 54.053 17.538 1.00 21.33 C
ATOM 3678 CD2 PHE B 185 33.538 53.854 18.526 1.00 21.48 C
ATOM 3679 C PHE B 185 30.865 54.069 21.683 1.00 24.18 C
ATOM 3680 O PHE B 185 30.068 54.441 20.823 1.00 24.91 O
ATOM 3681 N LYS B 186 30.486 53.703 22.906 1.00 25.54 N
ATOM 3682 CA LYS B 186 29.071 53.691 23.287 1.00 26.85 C
ATOM 3683 CB LYS B 186 28.760 52.488 24.192 1.00 28.12 C
ATOM 3684 CG LYS B 186 28.794 51.146 23.468 1.00 31.08 C
ATOM 3685 CD LYS B 186 28.328 50.020 24.372 1.00 38.17 C
ATOM 3686 CE LYS B 186 27.922 48.796 23.551 1.00 40.70 C
ATOM 3687 NZ LYS B 186 28.850 47.648 23.771 1.00 42.30 N
ATOM 3688 C LYS B 186 28.614 54.990 23.960 1.00 27.13 C
ATOM 3689 0 LYS B 186 27.471 55.082 24.401 1.00 27.24 O
ATOM 3690 N ASP B 187 29.497 55.990 24.020 1.00 26.85 N
ATOM 3691 CA ASP B 187 29.159 57.297 24.602 1.00 26.51 C
ATOM 3692 CB ASP B 187 30.424 58.114 24.854 1.00 26.58 C
ATOM 3693 CG ASP B 187 30.226 59.191 25.893 1.00 26.12 C
ATOM 3694 OD1 ASP B 187 29.606 60.234 25.582 1.00 27.27 O
ATOM 3695 OD2 ASP B 187 30.675 59.086 27.049 1.00 26.50 O
ATOM 3696 C ASP B 187 28.214 58.100 23.710 1.00 27.33 C
ATOM 3697 O ASP B 187 28.466 58.250 22.518 1.00 26.96 O
ATOM 3698 N PRO B 188 27.130 58.615 24.296 1.00 28.02 N
ATOM 3699 CA PRO B 188 26.132 59.423 23.567 1.00 28.14 C
ATOM 3700 CB PRO B 188 25.156 59.850 24.672 1.00 28.26 C
ATOM 3701 CG PRO B 188 25.287 58.809 25.719 1.00 29.22 C
ATOM 3702 CD PRO B 188 26.742 58.399 25.704 1.00 28.58 C
ATOM 3703 C PRO B 188 26.691 60.671 22.895 1.00 28.05 C
ATOM 3704 O PRO B 188 26.122 61.130 21.895 1.00 28.51 O
ATOM 3705 N GLU B 189 27.770 61.225 23.443 1.00 27.24 N
ATOM 3706 CA GLU B 189 28.311 62.488 22.948 1.00 26.20 C
ATOM 3707 CB GLU B 189 28.822 63.343 24.113 1.00 26.62 C
ATOM 3708 CG GLU B 189 27.720 64.003 24.934 1.00 31.73 C
ATOM 3709 CD GLU B 189 28.226 64.535 26.265 1.00 36.10 C ATOM - 3710 OE1 GLU B 189 29.089 65.440 26.253 1.00 38.61 O
ATOM 3711 OE2 GLU B 189 27.769 64.043 27.322 1.00 37.76 O
ATOM 3712 C GLU B 189 29.422 62.287 21.907 1.00 24.13 C
ATOM 3713 O GLU B 189 29.954 63.255 21.377 1.00 23.56 O
ATOM 3714 N LEU B 190 29.768 61.033 21.623 1.00 22.82 N
ATOM 3715 CA LEU B 190 30.781 60.719 20.607 1.00 21.08 C
ATOM 3716 CB LEU B 190 31.044 59.214 20.581 1.00 20.40 C
ATOM 3717 CG LEU B 190 32.158 58.696 19.668 1.00 20.27 C
ATOM 3718 CD1 LEU B 190 33.532 58.850 20.331 1.00 15.11 C
ATOM 3719 CD2 LEU B 190 31.899 57.242 19.267 1.00 19.14 C
ATOM 3720 C LEU B 190 30.353 61.184 19.215 1.00 20.88 C
ATOM 3721 O LEU B 190 29.230 60.914 18.798 1.00 21.26 O
ATOM 3722 N PRO B 191 31.232 61.890 18.502 1.00 20.99 N
ATOM 3723 CA PRO B 191 30.987 62.216 17.092 1.00 20.59 C
ATOM 3724 CB PRO B 191 32.260 62.963 16.678 1.00 20.26 C
ATOM 3725 CG PRO B 191 32.813 63.499 17.964 1.00 21.86 C
ATOM 3726 CD PRO B 191 32.526 62.422 18.975 1.00 20.53 C
ATOM 3727 C PRO B 191 30.831 60.933 16.280 1.00 19.97 C
ATOM 3728 O PRO B 191 31.635 60.014 16.420 1.00 19.38 O
ATOM 3729 N ARG B 192 29.780 60.859 15.475 1.00 19.81 N
ATOM 3730 CA ARG B 192 29.483 59.655 14.716 1.00 20.14 C
ATOM 3731 CB ARG B 192 28.317 58.893 15.348 1.00 21.58 C
ATOM 3732 CG ARG B 192 28.685 58.074 16.543 1.00 21.84 C
ATOM 3733 CD ARG B 192 27.530 57.306 17.139 1.00 21.07 C
ATOM 3734 NE ARG B 192 27.972 56.576 18.322 1.00 23.24 N
ATOM 3735 CZ ARG B 192 27.895 57.037 19.562 1.00 21.00 C
ATOM 3736 NH1 ARG B 192 27.362 58.225 19.800 1.00 19.82 N
ATOM 3737 NH2 ARG B 192 28.349 56.301 20.566 1.00 24.26 N
ATOM 3738 C ARG B 192 29.113 60.015 13.305 1.00 19.43 C
ATOM 3739 O ARG B 192 28.597 59.186 12.564 1.00 20.14 O
ATOM 3740 N ASN B 193 29.367 61.262 12.935 1.00 18.30 N
ATOM 3741 CA ASN B 193 28.850 61.803 11.685 1.00 19.13 C
ATOM 3742 CB AASN B 193 27.524 62.544 11.924 0.50 19.26 C
ATOM 3743 CB BASN B 193 27.588 62.644 11.967 0.50 19.21 C
ATOM 3744 CG AASN B 193 26.378 61.585 12.246 0.50 21.33 C
ATOM 3745 CG BASN B 193 27.868 63.887 12.847 0.50 21.27 C
ATOM 3746 OD1AASN B 193 25.945 60.805 11.391 0.50 23.63 O
ATOM 3747 OD1 BASN B 193 27.047 64.810 12.909 0.50 23.99 O
ATOM 3748 ND2AASN B 193 25.910 61.614 13.491 0.50 21.14 N
ATOM 3749 ND2BASN B 193 29.022 63.909 13.521 0.50 20.69 N
ATOM 3750 C ASN B 193 29.868 62.653 10.908 1.00 17.76 C
ATOM 3751 O ASN B 193 29.495 63.528 10.140 1.00 18.16 O
ATOM 3752 N THR B 194 31.152 62.409 11.140 1.00 16.17 N
ATOM 3753 CA THR B 194 32.200 63.106 10.401 1.00 14.91 C
ATOM 3754 CB THR B 194 33.571 62.749 10.978 1.00 13.62 C
ATOM 3755 OG1 THR B 194 33.622 63.145 12.349 1.00 12.51 O
ATOM 3756 CG2 THR B 194 34.682 63.582 10.319 1.00 13.57 C
ATOM 3757 C TH B 194 32.121 62.721 8.921 1.00 15.21 C
ATOM 3758 O THR B 194 32.096 61.534 8.595 1.00 15.01 O
ATOM 3759 N PRO B 195 32.058 63.714 8.030 1.00 15.80 N
ATOM 3760 CA PRO B 195 31.962 63.445 6.586 1.00 15.37 C
ATOM 3761 CB PRO B 195 31.981 64.850 5.955 1.00 16.08 C
ATOM 3762 CG PRO B 195 31.579 65.777 7.051 1.00 17.32 C
ATOM 3763 CD PRO B 195 32.066 65.156 8.330 1.00 16.35 C
ATOM 3764 C PRO B 195 33.146 62.630 6.074 1.00 13.62 C
ATOM 3765 0 PRO B 195 34.288 62.888 6.481 1.00 12.40 O
ATOM 3766 N LYS B 196 32.872 61.656 5.204 1.00 12.28 N
ATOM 3767 CA LYS B 196 33.925 60.882 4.553 1.00 12.55 C
ATOM 3768 CB LYS B 196 33.344 59.700 3.780 1.00 12.33 C
ATOM 3769 CG LYS B 196 32.845 58.581 4.665 1.00 15.68 C
ATOM 3770 CD LYS B 196 32.594 57.321 3.868 1.00 16.17 C
ATOM 3771 CE LYS B 196 33.895 56.614 3.566 1.00 18.55 C
ATOM 3772 NZ LYS B 196 33.662 55.278 2.986 1.00 21.10 N
ATOM 3773 C LYS B 196 34.712 61.763 3.605 1.00 12.31 C
ATOM 3774 0 LYS B 196 34.129 62.513 2.815 1.00 13.13 O
ATOM 3775 N ARG B 197 36.033 61.695 3.696 1.00 11.80 N
ATOM 3776 CA ARG B 197 36.892 62.507 2.838 1.00 11.33 C
ATOM 3777 CB ARG B 197 37.588 63.583 3.665 1.00 11.39 C
ATOM 3778 CG ARG B 197 36.610 64.624 4.210 1.00 13.53 C
ATOM 3779 CD ARG B 197 37.163 65.490 5.316 1.00 16.28 C
ATOM 3780 NE ARG B 197 37.239 64.760 6.575 1.00 18.70 N
ATOM 3781 CZ ARG B 197 37.824 65.229 7.667 1.00 18.04 C
ATOM 3782 NH1 ARG B 197 38.381 66.436 7.657 1.00 15.58 N
ATOM 3783 NH2 ARG B 197 37.866 64.487 8.767 1.00 14.80 N
ATOM 3784 C ARG B 197 37.906 61.644 2.084 1.00 11.68 C
ATOM 3785 0 ARG B 197 38.088 60.475 2.410 1.00 10.99 O
ATOM 3786 N SER B 198 38.538 62.220 1.056 1.00 11.49 N
ATOM 3787 CA SER B 198 39.491 61.483 0.235 1.00 11.74 C
ATOM 3788 CB SER B 198 39.701 62.185 -1.113 1.00 10.88 C
ATOM 3789 OG SER B 198 40.623 63.258 -0.982 1.00 10.85 O
ATOM 3790 C SER B 198 40.822 61.331 0.963 1.00 12.02 C
ATOM 3791 O SER B 198 41.171 62.162 1.811 1.00 12.86 O
ATOM 3792 N ILE B 199 41.550 60.260 0.643 1.00 10.92 N
ATOM 3793 CA ILE B 199 42.907 60.067 1.156 1.00 11.84 C
ATOM 3794 CB ILE B 199 43.594 58.869 0.462 1.00 11.05 C
ATOM 3795 CG1 ILE B 199 42.924 57.559 0.866 1.00 12.60 C
ATOM 3796 CD1 ILE B 199 43.587 56.304 0.285 1.00 14.36 C
ATOM 3797 CG2 ILE B 199 45.093 58.837 0.796 1.00 13.26 C
ATOM 3798 C ILE B 199 43.766 61.330 1.002 1.00 11.50 C
ATOM 3799 0 ILE B 199 44.380 61.784 1.966 1.00 10.97 O
ATOM 3800 N GLU B 200 43.808 61.897 -0.206 1.00 11.35 N
ATOM 3801 CA GLU B 200 44.720 63.011 -0.479 1.00 12.00 C
ATOM 3802 CB GLU B 200 44.763 63.352 -1.980 1.00 11.91 C
ATOM 3803 CG GLU B 200 45.373 62.259 -2.850 1.00 10.75 C
ATOM 3804 CD GLU B 200 46.830 61.960 -2.503 1.00 13.33 C
ATOM 3805 OE1 GLU B 200 47.191 60.770 -2.351 1.00 16.40 O
ATOM 3806 OE2 GLU B 200 47.605 62.916 -2.367 1.00 15.89 O
ATOM 3807 C GLU B 200 44.360 64.245 0.345 1.00 12.59 C
ATOM 3808 O GLU B 200 45.236 64.939 0.827 1.00 13.33 O
ATOM 3809 N THR B 201 43.068 64.495 0.523 1.00 12.77 N
ATOM 3810 CA THR B 201 42.623 65.615 1.343 1.00 13.29 C
ATOM 3811 CB THR B 201 41.132 65.887 1.115 1.00 12.50 C
ATOM 3812 OG1 THR B 201 40.957 66.431 -0.195 1.00 14.61 O
ATOM 3813 CG2 THR B 201 40.630 67.017 2.016 1.00 13.47 C
ATOM 3814 C THR B 201 42.919 65.354 2.823 1.00 13.92 C
ATOM 3815 O THR B 201 43.370 66.244 3.537 1.00 14.19 O
ATOM 3816 N LEU B 202 42.702 64.122 3.268 1.00 13.38 N
ATOM 3817 CA LEU B 202 42.921 63.791 4.675 1.00 13.61 C
ATOM 3818 CB LEU B 202 42.334 62.417 5.000 1.00 14.05 C
ATOM 3819 CG LEU B 202 40.811 62.467 5.194 1.00 15.11 C
ATOM 3820 CD1 LEU B 202 40.246 61.087 5.505 1.00 14.25 C
ATOM 3821 CD2 LEU B 202 40.432 63.461 6.288 1.00 16.22 C
ATOM 3822 C LEU B 202 44.398 63.861 5.056 1.00 14.59 C
ATOM 3823 O LEU B 202 44.730 64.302 6.163 1.00 13.96 O
ATOM 3824 N LEU B 203 45.275 63.455 4.129 1.00 13.91 N
ATOM 3825 CA LEU B 203 46.721 63.512 4.347 1.00 15.26 C
ATOM 3826 CB LEU B 203 47.473 62.742 3.250 1.00 14.90 C
ATOM 3827 CG LEU B 203 47.339 61.206 3.224 1.00 15.29 C
ATOM 3828 CD1 LEU B 203 48.006 60.623 1.969 1.00 17.33 C
ATOM 3829 CD2 LEU B 203 47.914 60.572 4.475 1.00 16.87 C
ATOM 3830 C LEU B 203 47.252 64.952 4.432 1.00 16.34 C
ATOM 3831 O LEU B 203 48.305 65.190 5.015 1.00 17.03 O
ATOM 3832 N LYS B 204 46.502 65.896 3.871 1.00 17.66 N
ATOM 3833 CA LYS B 204 46.900 67.304 3.853 1.00 20.06 C
ATOM 3834 CB ALYS B 204 46.566 67.940 2.502 0.50 19.64 C
ATOM 3835 CB BLYS B 204 46.562 67.936 2.495 0.50 19.65 C
ATOM 3836 CG ALYS B 204 47.260 67.286 1.321 0.50 22.02 C
ATOM 3837 CG BLYS B 204 47.607 67.687 1.405 0.50 21.98 C
ATOM 3838 CD ALYS B 204 48.762 67.532 1.332 0.50 21.88 C
ATOM 3839 CD BLYS B 204 47.152 68.247 0.050 0.50 22.29 C
ATOM 3840 CE ALYS B 204 49.357 67.343 -0.051 0.50 22.52 C
ATOM 3841 CE BLYS B 204 47.082 67.160 -1.024 0.50 20.78 C
ATOM 3842 NZ ALYS B 204 48.598 68.079 -1.101 0.50 21.98 N
ATOM 3843 NZ BLYS B 204 45.752 67.078 -1.730 0.50 14.84 N
ATOM 3844 C LYS B 204 46.244 68.107 4.978 1.00 20.07 C
ATOM 3845 0 LYS B 204 46.731 69.167 5.342 1.00 22.33 O
ATOM 3846 N CYS B 205 45.134 67.587 5.497 1.00 19.95 N
ATOM 3847 CA CYS B 205 44.346 68.191 6.573 1.00 20.56 C
ATOM 3848 CB ACYS B 205 43.021 67.447 6.732 0.50 20.23 C
ATOM 3849 CB BCYS B 205 43.000 67.462 6.676 0.50 19.80 C
ATOM 3850 SG ACYS B 205 41.700 67.997 5.655 0.50 26.98 S
ATOM 3851 SG BCYS B 205 41.777 68.221 7.757 0.50 23.32 S
ATOM 3852 C CYS B 205 45.078 68.149 7.913 1.00 19.25 C
ATOM 3853 O CYS B 205 45.980 67.329 8.108 1.00 19.90 O
ATOM 3854 N GLU B 206 44.692 69.018 8.843 1.00 17.65 N
ATOM 3855 CA GLU B 206 45.124 68.859 10.222 1.00 17.48 C
ATOM 3856 CB GLU B 206 44.624 70.005 11.112 1.00 18.54 C
ATOM 3857 CG GLU B 206 45.264 70.007 12.503 1.00 23.68 C
ATOM 3858 CD GLU B 206 44.554 70.917 13.506 1.00 31.16 C
ATOM 3859 OE1 GLU B 206 43.977 71.948 13.082 1.00 30.93 O
ATOM 3860 OE2 GLU B 206 44.582 70.601 14.730 1.00 31.33 O
ATOM 3861 C GLU B 206 44.618 67.501 10.753 1.00 15.47 C
ATOM 3862 O GLU B 206 43.448 67.154 10.571 1.00 15.00 O
ATOM 3863 N PHE B 207 45.514 66.746 11.383 1.00 13.35 N
ATOM 3864 CA PHE B 207 45.193 65.439 11.930 1.00 13.08 C
ATOM 3865 CB PHE B 207 46.474 64.610 12.118 1.00 11.75 C
ATOM 3866 CG PHE B 207 47.091 64.097 10.829 1.00 11.94 C
ATOM 3867 CD1 PHE B 207 46.633 64.523 9.581 1.00 11.76 C
ATOM 3868 CE1 PHE B 207 47.210 64.043 8.398 1.00 13.89 C
ATOM 3869 CZ PHE B 207 48.253 63.122 8.452 1.00 12.62 C
ATOM 3870 CE2 PHE B 207 48.716 62.671 9.696 1.00 14.33 C
ATOM 3871 CD2 PHE B 207 48.132 63.165 10.876 1.00 13.85 C
ATOM 3872 C PHE B 207 44.493 65.599 13.276 1.00 13.04 C
ATOM 3873 O PHE B 207 44.966 66.349 14.130 1.00 13.98 O
ATOM 3874 N SER B 208 43.381 64.886 13.477 1.00 12.03 N
ATOM 3875 CA SER B 208 42.745 64.812 14.805 1.00 11.54 C
ATOM 3876 CB SER B 208 41.722 65.941 14.998 1.00 11.91 C
ATOM 3877 OG SER B 208 40.611 65.786 14.133 1.00 13.50 O
ATOM 3878 C SER B 208 42.100 63.448 15.056 1.00 10.26 C
ATOM 3879 O SER B 208 42.017 62.626 14.145 1.00 9.80 O
ATOM 3880 N ASN B 209 41.656 63.222 16.293 1.00 9.69 N
ATOM 3881 CA ASN B 209 41.038 61.967 16.724 1.00 9.45 C
ATOM 3882 CB ASN B 209 41.937 61.245 17.753 1.00 8.90 C
ATOM 3883 CG ASN B 209 41.402 59.861 18.164 1.00 7.99 C
ATOM 3884 OD1 ASN B 209 40.203 59.597 18.131 1.00 9.21 O
ATOM 3885 ND2 ASN B 209 42.313 58.979 18.570 1.00 7.78 N
ATOM 3886 C ASN B 209 39.674 62.273 17.326 1.00 9.50 C
ATOM 3887 O ASN B 209 39.591 62.914 18.373 1.00 8.46 O
ATOM 3888 N ASP B 210 38.613 61.800 16.678 1.00 9.98 N
ATOM 3889 CA ASP B 210 37.234 62.102 17.094 1.00 11.39 C
ATOM 3890 CB ASP B 210 36.219 61.494 16.109 1.00 10.48 C
ATOM 3891 CG ASP B 210 36.011 62.346 14.864 1.00 10.94 C
ATOM 3892 OD1 ASP B 210 36.479 63.510 14.833 1.00 10.58 O
ATOM 3893 OD2 ASP B 210 35.386 61.924 13.862 1.00 9.58 O
ATOM 3894 C ASP B 210 36.907 61.603 18.510 1.00 12.20 C
ATOM 3895 O ASP B 210 35.966 62.093 19.141 1.00 13.20 O
ATOM 3896 N CYS B 211 37.672 60.622 18.993 1.00 11.70 N
ATOM 3897 CA CYS B 211 37.447 60.047 20.319 1.00 12.63 C
ATOM 3898 CB CYS B 211 38.089 58.662 20.418 1.00 12.40 C
ATOM 3899 SG CYS B 211 37.355 57.433 19.314 1.00 15.05 S
ATOM 3900 C CYS B 211 37.985 60.935 21.435 1.00 12.96 C
ATOM 3901 O CYS B 211 37.627 60.751 22.606 1.00 12.82 O
ATOM 3902 N GLU B 212 38.838 61.896 21.067 1.00 12.46 N
ATOM 3903 CA GLU B 212 39.619 62.655 22.039 1.00 13.36 C
ATOM 3904 CB GLU B 212 40.656 63 .532 21.335 1.00 13.19 C ATOM 3905 CG GLU B 212 41.550 64 .311 22.290 1.00 14.16 C
ATOM 3906 CD GLU B 212 42.778 64.846 21.596 1.00 13.80 C
ATOM 3907 OE1 GLU B 212 43.443 64,058 20.894 1.00 8.18 O
ATOM 3908 OE2 GLU B 212 43.065 66.053 21.742 1.00 13.61 O
ATOM 3909 C GLU B 212 38.745 63.513 22.964 1.00 14,48 C
ATOM 3910 O GLU B 212 38.959 63.530 24.173 1.00 13.54 O
ATOM 3911 N VAL B 213 37.766 64.215 22.398 1.00 15.51 N
ATOM 3912 CA VAL B 213 - 36.853 65.021 23.216 1.00 17.69 C
ATOM 3913 CB VAL B 213 35.784 65.769 22.361 1.00 18.52 C
ATOM 3914 CG1 VAL B 213 34.847 64.780 21.634 1.00 19.87 C
ATOM 3915 CG2 VAL B 213 34.996 66.751 23.219 1.00 18.94 C
ATOM 3916 C VAL B 213 36.184 64.180 24.323 1.00 18.05 C
ATOM 3917 O VAL B 213 36.112 64,615 25.473 1.00 18.92 O
ATOM 3918 N ILE B 214 35.760 62.965 23.985 1.00 16.83 N
ATOM 3919 CA ILE B 214 35.073 62.086 24.936 1.00 17.51 C
ATOM 3920 CB ILE B 214 34.425 60.886 24.199 1.00 17.57 C
ATOM 3921 CG1 ILE B 214 33.356 61.369 23.223 1.00 18.79 C
ATOM 3922 CD1 ILE B 214 32.292 62.249 23.857 1.00 18.95 C
ATOM 3923 CG2 ILE B 214 33.820 59.900 25.188 1.00 19.29 C
ATOM 3924 C ILE B 214 36.016 61.591 26.019 1.00 17.15 C
ATOM 3925 O ILE B 214 35.717 61.687 27.211 1.00 17.27 O
ATOM 3926 N ALA B 215 37.167 61.077 25.602 1.00 16.84 N
ATOM 3927 CA ALA B 215 38.157 60.556 26.530 1.00 16.40 C
ATOM 3928 CB ALA B 215 39.371 60.037 25.767 1.00 16.30 C
ATOM 3929 C ALA B 215 38.569 61.627 27.536 1.00 16.50 C
ATOM 3930 O ALA B 215 38.681 61.351 28.722 1.00 16.29 O
ATOM 3931 N ARG B 216 38.779 62.846 27.049 1.00 17.13 N
ATOM 3932 CA ARG B 216 39.140 63.976 27.900 1.00 20.00 C
ATOM 3933 CB ARG B 216 39.385 65.232 27.053 1.00 20.03 C
ATOM 3934 CG ARG B 216 40.782 65.364 26.469 1.00 22.00 C
ATOM 3935 CD ARG B 216 41.087 66.766 25.934 1.00 25.33 C
ATOM 3936 NE ARG B 216 41.959 67.533 26.835 1.00 25.26 N
ATOM 3937 CZ ARG B 216 42.781 68.516 26.445 1.00 26.91 C
ATOM 3938 NH1 ARG B 216 42.854 68.871 25.164 1.00 25.16 N
ATOM 3939 NH2 ARG B 216 43.530 69.149 27.344 1.00 26.63 N
ATOM 3940 C ARG B 216 38.060 64.274 28.944 1.00 20.46 C
ATOM 3941 O ARG B 216 38.364 64.475 30.122 1.00 21.01 O
ATOM 3942 N LYS B 217 36.808 64.302 28.496 1.00 21.41 N
ATOM 3943 CA LYS B 217 35.667 64.646 29.350 1.00 22.39 C
ATOM 3944 CB LYS B 217 34.406 64.838 28.494 1.00 22.37 C
ATOM 3945 CG LYS B 217 33.456 65.904 29.013 1.00 26.57 C
ATOM 3946 CD LYS B 217 32.007 65.614 28.626 1.00 29.69 C
ATOM 3947 CE LYS B 217 31.051 66.591 29.315 1.00 32.13 C
ATOM 3948 NZ LYS B 217 29.635 66.445 28.840 1.00 34.93 N
ATOM 3949 C LYS B 217 35.393 63.604 30.436 1.00 21.88 C
ATOM 3950 O LYS B 217 35.020 63.949 31.564 1.00 22.46 O
ATOM 3951 N ARG B 218 35.556 62.334 30.092 1.00 20.93 N
ATOM 3952 CA ARG B 218 35.197 61.257 31.001 1.00 20.74 C
ATOM 3953 CB ARG B 218 34.690 60.038 30.219 1.00 21.38 C
ATOM 3954 CG ARG B 218 33.558 60.333 29.251 1.00 22.14 C
ATOM 3955 CD ARG B 218 32.234 60.701 29.916 1.00 28.88 C
ATOM 3956 NE ARG B 218 31.169 60.860 28.926 1.00 31.55 N
ATOM 3957 CZ ARG B 218 30.305 61.871 28.896 1.00 35.41 C
ATOM 3958 NH1 ARG B 218 30.356 62.828 29.816 1.00 34.79 N
ATOM 3959 NH2 ARG B 218 29.375 61.918 27.948 1.00 37.31 N
ATOM 3960 C ARG B 218 36.359 60.850 31.909 1.00 20.72 C
ATOM 3961 O ARG B 218 36.149 60.246 32.966 1.00 20.14 O
ATOM 3962 N PHE B 219 37.581 61.182 31.498 1.00 19.30 N
ATOM 3963 CA PHE B 219 38.771 60.756 32.237 1.00 18.88 C
ATOM 3964 CB PHE B 219 39.499 59.626 31.500 1.00 18.37 C
ATOM 3965 CG PHE B 219 38.668 58.388 31.330 1.00 21.55 C
ATOM 3966 CD1 PHE B 219 37.857 58.225 30.208 1.00 20.04 C
ATOM 3967 CE1 PHE B 219 37.083 57.090 30.054 1.00 21.59 C
ATOM 3968 CZ PHE B 219 37.106 56.098 31.024 1.00 25.10 C
ATOM 3969 CE2 PHE B 219 37.904 56.250 32.151 1.00 25.94 C
ATOM 3970 CD2 PHE B 219 38.680 57.390 32.298 1.00 22.19 C
ATOM 3971 C PHE B 219 39.705 61.932 32.477 1.00 18.31 C
ATOM 3972 O PHE B 219 40.501 62.304 31.606 1.00 17.87 O
ATOM 3973 N ARG B 220 39.591 62.500 33.673 1.00 16.66 N
ATOM 3974 CA ARG B 220 40.315 63.696 34.080 1.00 16.57 C
ATOM 3975 CB AARG B 220 40.015 63.989 35.558 0.50 16.41 C
ATOM 3976 CB BARG B 220 40.016 64.020 35.549 0.50 16.67 C
ATOM 3977 CG AARG B 220 40.703 65.220 36.118 0.50 17.99 C
ATOM 3978 CG BARG B 220 39.295 65.336 35.751 0.50 19.44 C
ATOM 3979 CD AARG B 220 40.138 66.520 35.586 0.50 20.30 C
ATOM 3980 CD BARG B 220 38.923 65.635 37.204 0.50 22.74 C
ATOM 3981 NE AARG B 220 40.794 67.688 36.163 0.50 22.83 N
ATOM 3982 NE BARG B 220 38.833 67.073 37.461 0.50 24.81 N
ATOM 3983 CZ AARG B 220 41.856 68.283 35.637 0.50 23.09 C
ATOM 3984 CZ BARG B 220 37.800 67.839 37.113 0.50 27.71 C
ATOM 3985 NH1AARG B 220 42.403 67.813 34.516 0.50 20.31 N
ATOM 3986 NH1 BARG B 220 36.751 67.316 36.488 0.50 28.11 N
ATOM 3987 NH2AARG B 220 42.376 69.347 36.234 0.50 22.43 N
ATOM 3988 NH2BARG B 220 37.815 69.137 37.392 0.50 29.40 N
ATOM 3989 C ARG B 220 41.828 63.580 33.874 1.00 15.46 C
ATOM 3990 O ARG B 220 42.474 64.527 33.460 1.00 15.25 O
ATOM 3991 N GLU B 221 42.389 62.424 34.196 1.00 14,97 N
ATOM 3992 CA GLU B 221 43.830 62.256 34.120 1.00 15.97 C
ATOM 3993 CB GLU B 221 44.275 61.056 34.973 1.00 16.90 C
ATOM 3994 CG GLU B 221 43.877 61.202 36.445 1.00 20.26 C
ATOM 3995 CD GLU B 221 44.644 60.283 37.387 1.00 23.66 C
ATOM 3996 OE1 GLU B 221 45.392 59.403 36.917 1.00 25.76 O
ATOM 3997 OE2 GLU B 221 44.491 60.445 38.613 1.00 24.83 O
ATOM 3998 C GLU B 221 44.306 62.137 32.657 1.00 16.03 C
ATOM 3999 O GLU B 221 45.412 62.574 32.334 1.00 16.99 O
ATOM 4000 N VAL B 222 43.465 61.586 31.772 1.00 15.26 N
ATOM 4001 CA VAL B 222 43.759 61.659 30.328 1.00 14.32 C
ATOM 4002 CB VAL B 222 42.767 60.863 29.459 1.00 13.58 C
ATOM 4003 CG1 VAL B 222 43.098 61.055 27.980 1.00 12.98 C
ATOM 4004 CG2 VAL B 222 42.798 59.389 29.808 1.00 14.61 C
ATOM 4005 C VAL B 222 43.780 63.124 29.857 1.00 13.81 C
ATOM 4006 O VAL B 222 44.698 63.551 29.137 1.00 13.84 O
ATOM 4007 N ASP B 223 42.779 63.890 30.279 1.00 12.95 N
ATOM 4008 CA ASP B 223 42.757 65.323 30.017 1.00 13.97 C
ATOM 4009 CB ASP B 223 41.541 65.972 30.684 1.00 14.41 C
ATOM 4010 CG ASP B 223 41.410 67.445 30.352 1.00 17.09 C
ATOM 4011 OD1 ASP B 223 41.503 67.801 29.164 1.00 22.31 O
ATOM 4012 OD2 ASP B 223 41.217 68.319 31.209 1.00 20.46 O
ATOM 4013 C ASP B 223 44.052 65.992 30.502 1.00 14.07 C
ATOM 4014 O ASP B 223 44.629 66.818 29.798 1.00 14.95 O
ATOM 4015 N ALA B 224 44.498 65.612 31.702 1.00 13.11 N
ATOM 4016 CA ALA B 224 45.731 66.142 32.293 1.00 13.04 C
ATOM 4017 CB ALA B 224 45.853 65.695 33.751 1.00 11.73 C
ATOM 4018 C ALA B 224 46.994 65.758 31.499 1.00 12.62 C
ATOM 4019 O ALA B 224 47.890 66.594 31.299 1.00 11.72 O
ATOM 4020 N VAL B 225 47.060 64.508 31.037 1.00 12.32 N
ATOM 4021 CA VAL B 225 48.205 64.061 30.235 1.00 12.42 C
ATOM 4022 CB VAL B 225 48.133 62.545 29.876 1.00 12.50 C
ATOM 4023 CG1 VAL B 225 49.215 62.165 28.836 1.00 10.86 C
ATOM 4024 CG2 VAL B 225 48.283 61.695 31.106 1.00 11.33 C
ATOM 4025 C VAL B 225 48.317 64.903 28.961 1.00 12.77 C
ATOM 4026 O VAL B 225 49.402 65.377 28.603 1.00 12.66 O
ATOM 4027 N LEU B 226 47.183 65.108 28.301 1.00 13.17 N
ATOM 4028 CA LEU B 226 47.127 65.931 27.101 1.00 14.51 C
ATOM 4029 CB LEU B 226 45.711 65.928 26.539 1.00 14.75 C
ATOM 4030 CG LEU B 226 45.389 66.115 25.058 1.00 19.88 C
ATOM 4031 CD1 LEU B 226 46.544 65.799 24.121 1.00 20.32 C
ATOM 4032 CD2 LEU B 226 44.207 65.208 24.745 1.00 24.09 C
ATOM 4033 C LEU B 226 47.563 67.369 27.387 1.00 14.47 C
ATOM 4034 O LEU B 226 48.353 67.937 26.646 1.00 14.15 O
ATOM 4035 N SER B 227 47.049 67.948 28.468 1.00 14.40 N
ATOM 4036 CA SER B 227 47.440 69.306 28.852 1.00 14.77 C
ATOM 4037 CB SER B 227 46.722 69.741 30.133 1.00 15.24 C
ATOM 4038 OG SER B 227 45.320 69.694 29.940 1.00 16.44 O
ATOM 4039 C SER B 227 48.950 69.425 29.017 1.00 13.99 C
ATOM 4040 O SER B 227 49.551 70.364 28.518 1.00 13.44 O
ATOM 4041 N TRP B 228 49.558 68.436 29.666 1.00 14.49 N
ATOM 4042 CA TRP B 228 51.007 68.436 29.892 1.00 14.50 C
ATOM 4043 CB TRP B 228 51.394 67.351 30.910 1.00 15.06 C
ATOM 4044 CG TRP B 228 51.309 67.834 32.355 1.00 16.87 C
ATOM 4045 CD1 TRP B 228 50.321 67.552 33.273 1.00 17.14 C
ATOM 4046 NE1 TRP B 228 50.586 68.186 34.467 1.00 18.88 N
ATOM 4047 CE2 TRP B 228 51.744 68.905 34.347 1.00 16.75 C
ATOM 4048 CD2 TRP B 228 52.231 68.705 33.026 1.00 19.06 C
ATOM 4049 CE3 TRP B 228 53.419 69.349 32.645 1.00 17.58 C
ATOM 4050 CZ3 TRP B 228 54.076 70.151 33.579 1.00 19.99 C
ATOM 4051 CH2 TRP B 228 53.571 70.312 34.885 1.00 16.93 C
ATOM 4052 CZ2 TRP B 228 52.410 69.700 35.283 1.00 19.37 C
ATOM 4053 C TRP B 228 51.799 68.282 28.577 1.00 15.22 C
ATOM 4054 O TRP B 228 52.732 69.042 28.315 1.00 14.59 O
ATOM 4055 N LEU B 229 51.406 67.331 27.733 1.00 14.10 N
ATOM 4056 CA LEU B 229 52.120 67.122 26.465 1.00 13.38 C
ATOM 4057 CB LEU B 229 51.704 65.797 25.814 1.00 13.35 C
ATOM 4058 CG LEU B 229 52.251 64.548 26.508 1.00 11.06 C
ATOM 4059 CD1 LEU B 229 51.702 63.273 25.851 1.00 12.27 C
ATOM 4060 CD2 LEU B 229 53.768 64.548 26.490 1.00 12.91 C
ATOM 4061 C LEU B 229 51.963 68.295 25.477 1.00 13.28 C
ATOM 4062 O LEU B 229 52.896 68.616 24.751 1.00 13.02 O
ATOM 4063 N LEU B 230 50.802 68.948 25.490 1.00 14.52 N
ATOM 4064 CA LEU B 230 50.554 70.108 24.627 1.00 14.86 C
ATOM 4065 CB LEU B 230 49.064 70.486 24.637 1.00 15.94 C
ATOM 4066 CG LEU B 230 48.150 69.534 23.849 1.00 14.85 C
ATOM 4067 CD1 LEU B 230 46.680 69.764 24.218 1.00 17.64 C
ATOM 4068 CD2 LEU B 230 48.374 69.658 22.330 1.00 14.21 C
ATOM 4069 C LEU B 230 51.429 71.328 24.967 1.00 16.16 C
ATOM 4070 O LEU B 230 51.580 72.226 24.145 1.00 16.90 O
ATOM 4071 N GLU B 231 52.038 71.341 26.150 1.00 17.19 N
ATOM 4072 CA GLU B 231 53.037 72.367 26.471 1.00 19.14 C
ATOM 4073 CB GLU B 231 53.467 72.292 27.941 1.00 19.80 C
ATOM 4074 CG GLU B 231 52.354 72.523 28.957 1.00 24.58 C
ATOM 4075 CD GLU B 231 51.904 73.969 29.021 1.00 30.40 C
ATOM 4076 OE1 GLU B 231 50.813 74.267 28.500 1.00 33.04 O
ATOM 4077 OE2 GLU B 231 52.640 74.807 29.590 1.00 35.86 O
ATOM 4078 C GLU B 231 54.275 72.252 25.569 1.00 19.07 C
ATOM 4079 O GLU B 231 54.976 73.242 25.341 1.00 17.87 O
ATOM 4080 N TYR B 232 54.521 71.049 25.044 1.00 18.37 N
ATOM 4081 CA TYR B 232 55.785 70.747 24.360 1.00 18.69 C
ATOM 4082 CB TYR B 232 56.476 69.551 25.038 1.00 19.05 C
ATOM 4083 CG TYR B 232 56.653 69.724 26.543 1.00 23.06 C
ATOM 4084 CD1 TYR B 232 55.830 69.051 27.442 1.00 26.01 C
ATOM 4085 CE1 TYR B 232 55.974 69.207 28.824 1.00 28.72 C
ATOM 4086 CZ TYR B 232 56.951 70.047 29.323 1.00 32.23 C
ATOM 4087 OH TYR B 232 57.081 70.199 30.700 1.00 35.98 O
ATOM 4088 CE2 TYR B 232 57.790 70.731 28.452 1.00 30.36 C
ATOM 4089 CD2 TYR B 232 57.637 70.567 27.063 1.00 27.73 C
ATOM 4090 C TYR B 232 55.652 70.507 22.843 1.00 18.77 C
ATOM 4091 O TYR B 232 56.560 70.845 22.079 1.00 19.43 O
ATOM 4092 N ALA B 233 54.536 69.925 22.410 1.00 17.82 N
ATOM 4093 CA ALA B 233 54.400 69.464 21.020 1.00 17.40 C
ATOM 4094 CB ALA B 233 55.256 68.208 20.804 1.00 17.06 C
ATOM 4095 C ALA B 233 52.950 69.171 20.655 1.00 16.64 C
ATOM 4096 O ALA B 233 52.123 68.983 21.549 1.00 17.68 O
ATOM 4097 N PRO B 234 52.638 69.107 19.353 1.00 15.91 N
ATOM 4098 CA PRO B 234 51.331 68.614 18.907 1.00 14.70 C
ATOM 4099 CB PRO B 234 51.499 68.482 17.389 1.00 15.04 C
ATOM 4100 CG PRO B 234 52.592 69.409 17.036 1.00 16.79 C
ATOM 4101 CD PRO B 234 53.504 69.476 18.217 1.00 16.18 C
ATOM 4102 C PRO B 234 51.086 67.249 19.507 1.00 13.60 C
ATOM 4103 O PRO B 234 51.976 66.399 19.432 1.00 12.64 O
ATOM 4104 N SER B 235 49.919 67.052 20.112 1.00 12.42 N
ATOM 4105 CA SER B 235 49.650 65.859 20.887 1.00 12.02 C
ATOM 4106 CB SER B 235 49.936 66.089 22.381 1.00 11.93 C
ATOM 4107 OG SER B 235 51.285 66.427 22.616 1.00 12.28 O
ATOM 4108 C SER B 235 48.201 65.486 20.717 1.00 11.59 C
ATOM 4109 O SER B 235 47.330 66.365 20.668 1.00 12.08 O
ATOM 4110 N ARG B 236 47.942 64.184 20.642 1.00 10.23 N
ATOM 4111 CA ARG B 236 46.605 63.669 20.387 1.00 9.48 C
ATOM 4112 CB ARG B 236 46.348 63.505 18.888 1.00 9.03 C
ATOM 4113 CG ARG B 236 46.452 64.760 18.049 1.00 10.42 C
ATOM 4114 CD ARG B 236 46.037 64.550 16.607 1.00 10.41 C
ATOM 4115 NE ARG B 236 46.904 63.639 15.866 1.00 8.01 N
ATOM 4116 CZ ARG B 236 48.080 63.979 15.347 1.00 11.42 C
ATOM 4117 NH1 ARG B 236 48.546 65.211 15.500 1.00 10.92 N
ATOM 4118 NH2 ARG B 236 48.786 63.093 14.658 1.00 10.48 N
ATOM 4119 C ARG B 236 46.438 62.311 21.036 1.00 9.33 C
ATOM 4120 O ARG B 236 47.416 61.587 21.244 1.00 10.01 O
ATOM 4121 N LEU B 237 45.190 61.960 21.329 1.00 8.06 N
ATOM 4122 CA LEU B 237 44.832 60.603 21.707 1.00 8.03 C
ATOM 4123 CB LEU B 237 43.342 60.538 22.043 1.00 7.49 C
ATOM 4124 CG LEU B 237 42.891 59.402 22.962 1.00 8.75 C
ATOM 4125 CD1 LEU B 237 43.218 59.745 24.403 1.00 8.79 C
ATOM 4126 CD2 LEU B 237 41.405 59.125 22.796 1.00 7.96 C
ATOM 4127 C LEU B 237 45.127 59.610 20.584 1.00 8.13 C
ATOM 4128 O LEU B 237 44.978 59.928 19.401 1.00 7.93 O
ATOM 4129 N THR B 238 45.515 58.395 20.938 1.00 7.82 N
ATOM 4130 CA THR B 238 45.529 57.342 19.929 1.00 8.87 C
ATOM 4131 CB THR B 238 46.912 56.655 19.806 1.00 8.81 C
ATOM 4132 OG1 THR B 238 46.791 55.490 18.966 1.00 8J2 O
ATOM 4133 CG2 THR B 238 47.389 56.093 21.149 1.00 7.62 C
ATOM 4134 C THR B 238 44.430 56.350 20.259 1.00 9.74 C
ATOM 4135 O THR B 238 44.118 56.138 21.439 1.00 9.83 O
ATOM 4136 N GLY B 239 43.841 55.754 19.217 1.00 9.88 N
ATOM 4137 CA GLY B 239 42.689 54.875 19.366 1.00 10.07 C
ATOM 4138 C GLY B 239 41.596 55.525 20.207 1.00 10.96 C
ATOM 4139 O GLY B 239 41.279 56.719 20.033 1.00 9.44 O
ATOM 4140 N THR B 240 41.055 54.753 21.148 1.00 10.34 N
ATOM 4141 CA THR B 240 40.090 55.273 22.129 1.00 10.49 C
ATOM 4142 CB ATHR B 240 38.977 54.244 22.410 0.50 10.07 C
ATOM 4143 CB BTHR B 240 38.954 54.246 22.351 0.50 11.30 C
ATOM 4144 OG1ATHR B 240 39.570 52.982 22.756 0.50 7.97 O
ATOM 4145 OG1 BTHR B 240 38.509 54.306 23.704 0.50 15.32 O
ATOM 4146 CG2ATHR B 240 38.169 53.950 21.149 0.50 5.92 C
ATOM 4147 CG2BTHR B 240 39.488 52.847 22.266 0.50 11.63 C
ATOM 4148 C THR B 240 40.754 55.670 23.471 1.00 11.22 C
ATOM 4149 0 THR B 240 40.069 55.863 24.481 1.00 10.37 O
ATOM 4150 N GLY B 241 42.081 55.789 23.479 1.00 11.04 N
ATOM 4151 CA GLY B 241 42.812 56.045 24.715 1.00 11.17 C
ATOM 4152 C GLY B 241 43.067 54.773 25.504 1.00 11.75 C
ATOM 4153 O GLY B 241 42.704 53.694 25.052 1.00 12.27 O
ATOM 4154 N ALA B 242 43.696 54.873 26.678 1.00 12.42 N
ATOM 4155 CA ALA B 242 44.037 56.141 27.324 1.00 13.45 C
ATOM 4156 CB ALA B 242 44.155 55.936 28.859 1.00 13.68 C
ATOM 4157 C ALA B 242 45.309 56.816 26.801 1.00 13.28 C
ATOM 4158 0 ALA B 242 45.612 57.936 27.210 1.00 13.17 O
ATOM 4159 N CYS B 243 46.060 56.149 25.924 1.00 11.60 N
ATOM 4160 CA CYS B 243 47.359 56.707 25.512 1.00 12.01 C
ATOM 4161 CB CYS B 243 48.220 55.676 24.768 1.00 11.27 C
ATOM 4162 SG CYS B 243 48.804 54.308 25.796 1.00 15.76 S
ATOM 4163 C CYS B 243 47.238 57.980 24.675 1.00 11.14 C
ATOM 4164 O CYS B 243 46.330 58.137 23.852 1.00 11.77 O
ATOM 4165 N VAL B 244 48.174 58.881 24.925 1.00 10.93 N
ATOM 4166 CA VAL B 244 48.323 60.121 24.210 1.00 10.83 C
ATOM 4167 CB VAL B 244 48.093 61.314 25.150 1.00 10.55 C
ATOM 4168 CG1 VAL B 244 48.274 62.624 24.419 1.00 10.56 C
ATOM 4169 CG2 VAL B 244 46.689 61.240 25.778 1.00 12.55 C
ATOM 4170 C VAL B 244 49.743 60.165 23.661 1.00 10.27 C
ATOM 4171 O VAL B 244 50.672 59.737 24.336 1.00 11.21 O
ATOM 4172 N PHE B 245 49.909 60.633 22.430 1.00 9.90 N
ATOM 4173 CA PHE B 245 51.243 60.787 21.861 1.00 10.00 C
ATOM 4174 CB PHE B 245 51.467 59.872 20.639 1.00 9.71 C
ATOM 4175 CG PHE B 245 50.550 60.152 19.468 1.00 10.49 C
ATOM 4176 CD1 PHE B 245 50.938 61.023 18.452 1.00 9.21 C
ATOM 4177 CE1 PHE B 245 50.101 61.275 17.373 1.00 13.76 C
ATOM 4178 CZ PHE B 245 48.861 60.633 17.287 1.00 12.63 C
ATOM 4179 CE2 PHE B 245 48.473 59.754 18.279 1.00 10.81 C
ATOM 4180 CD2 PHE B 245 49.317 59.517 19.366 1.00 9.52 C
ATOM 4181 C PHE B 245 51.530 62.237 21.495 1.00 10.93 C
ATOM 4182 0 PHE B 245 50.626 62.982 21.120 1.00 10.25 O
ATOM 4183 N ALA B 246 52.804 62.599 21.604 1.00 10.49 N
ATOM 4184 CA ALA B 246 53.321 63.888 21.180 1.00 12.46 C
ATOM 4185 CB ALA B 246 53.951 64.607 22.372 1.00 11.16 C
ATOM 4186 C ALA B 246 54.353 63.688 20.050 1.00 12.68 C
ATOM 4187 O ALA B 246 55.212 62.812 20.157 1.00 12.24 O
ATOM 4188 N GLU B 247 54.264 64.490 18.981 1.00 13.15 N
ATOM 4189 CA GLU B 247 55.109 64.308 17.787 1.00 16.03 C
ATOM 4190 CB GLU B 247 54.324 64.542 16.486 1.00 16.87 C
ATOM 4191 CG GLU B 247 52.872 64.091 16.502 1.00 23.15 C
ATOM 4192 CD GLU B 247 52.162 64.380 15.183 1.00 28.26 C
ATOM 4193 OE1 GLU B 247 52.130 65.562 14.758 1.00 28.37 O
ATOM 4194 OE2 GLU B 247 51.624 63.424 14.574 1.00 32.77 O
ATOM 4195 C GLU B 247 56.325 65.230 17.768 1.00 16.16 C
ATOM 4196 O GLU B 247 56.210 66.418 18.057 1.00 15.75 O
ATOM 4197 N PHE B 248 57.475 64.664 17.398 1.00 16.20 N
ATOM 4198 CA PHE B 248 58.745 65.371 17.363 1.00 17.83 C
ATOM 4199 CB PHE B 248 59.603 64.994 18.572 1.00 17.04 C
ATOM 4200 CG PHE B 248 58.973 65.331 19.891 1.00 18.03 C
ATOM 4201 CD1 PHE B 248 58.209 64.384 20.581 1.00 17.62 C
ATOM 4202 CE1 PHE B 248 57.615 64.701 21.798 1.00 17.80 C
ATOM 4203 CZ PHE B 248 57.781 65.969 22.338 1.00 15.96 C
ATOM 4204 CE2 PHE B 248 58.522 66.921 21.655 1.00 17.43 C
ATOM 4205 CD2 PHE B 248 59.113 66.601 20.434 1.00 16.75 C
ATOM 4206 C PHE B 248 59.492 65.032 16.079 1.00 19.13 C
ATOM 4207 O PHE B 248 59.338 63.938 15.535 1.00 18.86 O
ATOM 4208 N ASP B 249 60.318 65.962 15.609 1.00 20.78 N
ATOM 4209 CA ASP B 249 61.093 65.748 14.386 1.00 22.33 C
ATOM 4210 CB ASP B 249 61.563 67.083 13.809 1.00 23.53 C
ATOM 4211 CG ASP B 249 60.445 67.857 13.162 1.00 26.90 C
ATOM 4212 OD1 ASP B 249 59.473 67.224 12.686 1.00 30.70 O
ATOM 4213 OD2 ASP B 249 60.451 69.103 13.078 1.00 31.94 O
ATOM 4214 C ASP B 249 62.292 64.846 14.615 1.00 22.03 C
ATOM 4215 O ASP B 249 62.737 64.152 13.699 1.00 22.33 O
ATOM 4216 N THR B 250 62.831 64.876 15.832 1.00 21.89 N
ATOM 4217 CA THR B 250 64.025 64.104 16.171 1.00 22.47 C
ATOM 4218 CB THR B 250 65.282 65.032 16.293 1.00 22.58 C
ATOM 4219 OG1 THR B 250 65.138 65.917 17.414 1.00 24.07 O
ATOM 4220 CG2 THR B 250 65.397 65.978 15.096 1.00 23.19 C
ATOM 4221 C THR B 250 63.857 63.301 17.456 1.00 22.11 C
ATOM 4222 O THR B 250 63.003 63.609 18.300 1.00 22.21 O
ATOM 4223 N GLU B 251 64.695 62.283 17.599 1.00 21.68 N
ATOM 4224 CA GLU B 251 64.751 61.460 18.798 1.00 21.22 C
ATOM 4225 CB GLU B 251 65.689 60.281 18.568 1.00 20.53 C
ATOM 4226 CG GLU B 251 65.829 59.341 19.752 1.00 22.05 C
ATOM 4227 CD GLU B 251 66.782 58.198 19.475 1.00 24.33 C
ATOM 4228 OE1 GLU B 251 67.521 58.268 18.470 1.00 28.46 O
ATOM 4229 OE2 GLU B 251 66.798 57.238 20.264 1.00 26.63 O
ATOM 4230 C GLU B 251 65.228 62.270 20.002 1.00 21.83 C
ATOM 4231 O GLU B 251 64.758 62.064 21.124 1.00 21.04 O
ATOM 4232 N SER B 252 66.160 63.191 19.760 1.00 21.70 N
ATOM 4233 CA SER B 252 66.747 63.991 20.834 1.00 21.62 C
ATOM 4234 CB ASER B 252 67.895 64.865 20.300 0.50 21.43 C
ATOM 4235 CB BSER B 252 67.878 64.867 20.294 0.50 21.55 C
ATOM 4236 OG ASER B 252 67.414 65.898 19.459 0.50 21.58 O
ATOM 4237 OG BSER B 252 69.087 64.137 20.261 0.50 22.68 O
ATOM 4238 C SER B 252 65.705 64.851 21.542 1.00 20.95 C
ATOM 4239 O SER B 252 65.622 64.830 22.764 1.00 20.62 O
ATOM 4240 N GLU B 253 64.904 65.583 20.776 1.00 21.27 N
ATOM 4241 CA GLU B 253 63.855 66.416 21.363 1.00 21.62 C
ATOM 4242 CB GLU B 253 63.157 67.257 20.295 1.00 22.27 C
ATOM 4243 CG GLU B 253 62.483 68.494 20.875 1.00 27.53 C
ATOM 4244 CD GLU B 253 61.637 69.238 19.868 1.00 30.98 C
ATOM 4245 OE1 GLU B 253 61.812 69.006 18.650 1.00 34.87 O
ATOM 4246 OE2 GLU B 253 60.792 70.055 20.300 1.00 31.78 O
ATOM 4247 C GLU B 253 62.819 65.588 22.136 1.00 20.53 C
ATOM 4248 O GLU B 253 62.400 65.974 23.233 1.00 19.84 O
ATOM 4249 N ALA B 254 62.417 64.455 21.564 1.00 19.74 N
ATOM 4250 CA ALA B 254 61.462 63.552 22.216 1.00 18.97 C
ATOM 4251 CB ALA B 254 61.122 62.384 21.297 1.00 18.66 C
ATOM 4252 C ALA B 254 61.983 63.046 23.571 1.00 18.62 C
ATOM 4253 O ALA B 254 61.243 63.018 24.569 1.00 16.90 O
ATOM 4254 N ARG B 255 63.262 62.677 23.616 1.00 18.24 N
ATOM 4255 CA ARG B 255 63.847 62.170 24.853 1.00 19.59 C
ATOM 4256 CB ARG B 255 65.189 61.474 24.596 1.00 20.40 C
ATOM 4257 CG ARG B 255 65.081 60.283 23.659 1.00 22.82 C
ATOM 4258 CD ARG B 255 65.938 59.077 24.027 1.00 26.91 C
ATOM 4259 NE ARG B 255 65.729 58.004 23.058 1.00 27.35 N
ATOM 4260 CZ ARG B 255 64.912 56.977 23.240 1.00 27.97 C
ATOM 4261 NH1 ARG B 255 64.240 56.844 24.373 1.00 27.83 N
ATOM 4262 NH2 ARG B 255 64.777 56.069 22.282 1.00 32.28 N
ATOM 4263 C ARG B 255 64.022 63.284 25.867 1.00 19.38 C
ATOM 4264 O ARG B 255 63.860 63.057 27.058 1.00 19.29 O
ATOM 4265 N GLN B 256 64.350 64.486 25.388 1.00 19.46 N
ATOM 4266 CA GLN B 256 64.463 65.656 26.262 1.00 20.71 C
ATOM 4267 CB AGLN B 256 64.912 66.896 25.471 0.50 20.63 C
ATOM 4268 CB BGLN B 256 64.884 66.895 25.461 0.50 20.64 c
ATOM 4269 CG AGLN B 256 64.442 68.220 26.065 0.50 22.19 c
ATOM 4270 CG BGLN B 256 66.389 67.018 25.221 0.50 22.21 c
ATOM 4271 CD AGLN B 256 65.539 69.260 26.174 0.50 24.70 c
ATOM 4272 CD BGLN B 256 66.747 68.133 24.238 0.50 24.91 c
ATOM 4273 OE1AGLN B 256 65.283 70.454 25.999 0.50 27.83 o
ATOM 4274 OE1 BGLN B 256 67.548 67.928 23.320 0.50 27.47 o
ATOM 4275 NE2AGLN B 256 66.758 68.819 26.475 0.50 24.35 N
ATOM 4276 NE2BGLN B 256 66.158 69.307 24.428 0.50 24.44 N
ATOM 4277 C GLN B 256 63.134 65.913 26.989 1.00 20.07 C
ATOM 4278 O GLN B 256 63.111 66.065 28.211 1.00 20.38 O
ATOM 4279 N VAL B 257 62.027 65.926 26.238 1.00 19.23 N
ATOM 4280 CA VAL B 257 60.703 66.139 26.838 1.00 18.21 C
ATOM 4281 CB VAL B 257 59.597 66.319 25.764 1.00 19.32 C
ATOM 4282 CG1 VAL B 257 58.198 66.375 26.404 1.00 15.78 C
ATOM 4283 CG2 VAL B 257 59.850 67.580 24.964 1.00 18.17 C
ATOM 4284 C VAL B 257 60.352 65.013 27.813 1.00 19.17 C
ATOM 4285 O VAL B 257 59.845 65.269 28.910 1.00 19.18 O
ATOM 4286 N LEU B 258 60.674 63.774 27.442 1.00 17.97 N
ATOM 4287 CA LEU B 258 60.432 62.640 28.328 1.00 18.45 C
ATOM 4288 CB LEU B 258 60.925 61.335 27.692 1.00 17.55 C
ATOM 4289 CG LEU B 258 60.607 60.075 28.509 1.00 18.70 C
ATOM 4290 CD1 LEU B 258 59.103 59.949 28.715 1.00 17.43 C
ATOM 4291 CD2 LEU B 258 61.173 58.831 27.848 1.00 19.81 C
ATOM 4292 C LEU B 258 61.070 62.837 29.718 1.00 19.54 C
ATOM 4293 O LEU B 258 60.466 62.494 30.740 1.00 17.34 O
ATOM 4294 N GLU B 259 62.275 63.408 29.739 1.00 21.46 N
ATOM 4295 CA GLU B 259 63.003 63.659 30.987 1.00 24.34 C
ATOM 4296 CB GLU B 259 64.442 64.121 30.693 1.00 25.12 C
ATOM 4297 CG GLU B 259 65.395 63.019 30.249 1.00 32.34 C
ATOM 4298 CD GLU B 259 66.716 63.552 29.691 1.00 39.71 C
ATOM 4299 OE1 GLU B 259 67.261 62.930 28.742 1.00 42.65 O
ATOM 4300 OE2 GLU B 259 67.215 64.588 30.200 1.00 41.36 O
ATOM 4301 C GLU B 259 62.292 64.690 31.872 1.00 23.90 C
ATOM 4302 O GLU B 259 62.311 64.578 33.098 1.00 25.30 O
ATOM 4303 N GLN B 260 61.646 65.667 31.240 1.00 23.25 N
ATOM 4304 CA GLN B 260 61.007 66.785 31.942 1.00 24.76 C
ATOM 4305 CB GLN B 260 61.021 68.031 31.049 1.00 24.66 C
ATOM 4306 CG GLN B 260 62.401 68.385 30.526 1.00 28.24 C
ATOM 4307 CD GLN B 260 62.390 69.550 29.552 1.00 35.46 C
ATOM 4308 OE1 GL B 260 61.433 69.734 28.795 1.00 38.93 O
ATOM 4309 NE2 GLN B 260 63.463 70.337 29.562 1.00 37.72 N
ATOM 4310 C GLN B 260 59.566 66.500 32.389 1.00 24.79 C
ATOM 4311 O GLN B 260 59.053 67.138 33.312 1.00 24.56 O
ATOM 4312 N ALA B 261 58.924 65.544 31.724 1.00 24.64 N
ATOM 4313 CA ALA B 261 57.506 65.264 31.930 1.00 23.32 C
ATOM 4314 CB ALA B 261 56.974 64.399 30.778 1.00 24.31 C
ATOM 4315 C ALA B 261 57.265 64.580 33.273 1.00 22.26 C
ATOM 4316 O ALA B 261 58.161 63.930 33.802 1.00 21.10 O
ATOM 4317 N PRO B 262 56.056 64.729 33.827 1.00 21.29 N
ATOM 4318 CA PRO B 262 55.694 64.042 35.070 1.00 20.86 C
ATOM 4319 CB PRO B 262 54.194 64.332 35.207 1.00 20.88 C
ATOM 4320 CG PRO B 262 53.972 65.604 34.447 1.00 20.39 C
ATOM 4321 CD PRO B 262 54.964 65.588 33.329 1.00 21.05 C
ATOM 4322 C PRO B 262 55.927 62.539 34.978 1.00 20.96 C
ATOM 4323 0 PRO B 262 55.630 61.932 33.945 1.00 20.51 O
ATOM 4324 N GLU B 263 56.445 61.950 36.050 1.00 19.69 N
ATOM 4325 CA GLU B 263 56.647 60.506 36.118 1.00 20.41 C
ATOM 4326 CB AGLU B 263 57.337 60.121 37.435 0.50 20.95 C
ATOM 4327 CB BGLU B 263 57.281 60.128 37.460 0.50 21.12 C
ATOM 4328 CG AGLU B 263 58.708 60.770 37.619 0.50 22.60 C
ATOM 4329 CG BGLU B 263 57.723 58.676 37.563 0.50 23.68 C
ATOM 4330 CD AGLU B 263 59.793 59.776 37.999 0.50 26.59 C
ATOM 4331 CD BGLU B 263 57.534 58.101 38.951 0.50 28.43 C
ATOM 4332 OE1 AGLU B 263 59.532 58.907 38.860 0.50 27.18 O
ATOM 4333 OE1 BGLU B 263 57.744 58.840 39.943 0.50 29.43 O
ATOM 4334 OE2AGLU B 263 60.915 59.868 37.443 0.50 27.60 O
ATOM 4335 OE2BGLU B 263 57.173 56.907 39.052 0.50 30.03 O
ATOM 4336 C GLU B 263 55.336 59.710 35.921 1.00 19.22 C
ATOM 4337 O GLU B 263 55.347 58.623 35.341 1.00 18.36 O
ATOM 4338 N TRP B 264 54.209 60.267 36.369 1.00 16.86 N
ATOM 4339 CA TRP B 264 52.927 59.570 36.238 1.00 15.48 C
ATOM 4340 CB TRP B 264 51.880 60.136 37.225 1.00 15.36 C
ATOM 4341 CG TRP B 264 51.653 61.617 37.112 1.00 13.38 C
ATOM 4342 CD1 TRP B 264 52.302 62.599 37.804 1.00 11.33 C
ATOM 4343 NE1 TRP B 264 51.822 63.834 37.439 1.00 11.26 N
ATOM 4344 CE2 TRP B 264 50.840 63.671 36.498 1.00 12.16 C
ATOM 4345 CD2 TRP B 264 50.703 62.282 36.272 1.00 13.19 C
ATOM 4346 CE3 TRP B 264 49.733 61.846 35.355 1.00 11.16 C
ATOM 4347 CZ3 TRP B 264 48.945 62.796 34.709 1.00 14.07 C
ATOM 4348 CH2 TRP B 264 49.118 64.165 34.946 1.00 15.82 C
ATOM 4349 CZ2 TRP B 264 50.056 64.624 35.841 1.00 14.00 C
ATOM 4350 C TRP B 264 52.377 59.568 34.800 1.00 14.53 C
ATOM 4351 O TRP B 264 51.313 59.013 34.551 1.00 14.73 O
ATOM 4352 N LEU B 265 53.090 60.195 33.866 1.00 14.30 N
ATOM 4353 CA LEU B 265 52.767 60.044 32.435 1.00 14.58 C
ATOM 4354 CB LEU B 265 53.410 61.140 31.570 1.00 14.47 C
ATOM 4355 CG LEU B 265 52.906 62.601 31.514 1.00 18.48 C
ATOM 4356 CD1 LEU B 265 52.779 63.074 30.060 1.00 17.24 C
ATOM 4357 CD2 LEU B 265 51.599 62.846 32.281 1.00 16.68 C
ATOM 4358 C LEU B 265 53.197 58.671 31.897 1.00 13.89 C
ATOM 4359 O LEU B 265 52.816 58.306 30.792 1.00 12.33 O
ATOM 4360 N ASN B 266 54.009 57.934 32.665 1.00 13.94 N
ATOM 4361 CA ASN B 266 54.492 56.609 32.246 1.00 15.72 C
ATOM 4362 CB ASN B 266 53.413 55.540 32.436 1.00 15.57 C
ATOM 4363 CG ASN B 266 52.929 55.435 33.870 1.00 19.77 C
ATOM 4364 OD1 ASN B 266 53.671 55.019 34.759 1.00 24.94 O
ATOM 4365 ND2 ASN B 266 51.675 55.797 34.098 1.00 18.67 N
ATOM 4366 C ASN B 266 54.959 56.602 30.787 1.00 15.25 C
ATOM 4367 O ASN B 266 54.565 55.732 29.995 1.00 16.69 O
ATOM 4368 N GLY B 267 55.761 57.594 30.420 1.00 15.31 N
ATOM 4369 CA GLY B 267 56.063 57.839 29.017 1.00 14.52 C
ATOM 4370 C GLY B 267 57.179 56.973 28.457 1.00 14.66 C
ATOM 4371 O GLY B 267 58.099 56.604 29.184 1.00 14.75 O
ATOM 4372 N PHE B 268 57.089 56.652 27.163 1.00 13.04 N
ATOM 4373 CA PHE B 268 58.205 56.077 26.414 1.00 12.96 C
ATOM 4374 CB PHE B 268 58.038 54.548 26.204 1.00 12.34 C
ATOM 4375 CG PHE B 268 56.936 54.165 25.220 1.00 12.30 C
ATOM 4376 CD1 PHE B 268 57.162 54.182 23.840 1.00 12.58 C
ATOM 4377 CE1 PHE B 268 56.149 53.822 22.934 1.00 13.05 C
ATOM 4378 CZ PHE B 268 54.897 53.406 23.414 1.00 10.37 C
ATOM 4379 CE2 PHE B 268 54.666 53.375 24.785 1.00 10.04 C
ATOM 4380 CD2 PHE B 268 55.686 53.753 25.683 1.00 13.46 C
ATOM 4381 C PHE B 268 58.348 56.810 25.080 1.00 12.81 C
ATOM 4382 0 PHE B 268 57.402 57.455 24.613 1.00 12.36 O
ATOM 4383 N VAL B 269 59.532 56.713 24.481 1.00 12.54 N
ATOM 4384 CA VAL B 269 59.809 57.349 23.203 1.00 11.85 C
ATOM 4385 CB VAL B 269 61.022 58.312 23.301 1.00 12.57 C
ATOM 4386 CG1 VAL B 269 61.529 58.698 21.918 1.00 10.48 C
ATOM 4387 CG2 VAL B 269 60.649 59.559 24.108 1.00 12.50 C
ATOM 4388 C VAL B 269 60.047 56.277 22.139 1.00 12.35 C
ATOM 4389 O VAL B 269 60.721 55.279 22.403 1.00 13.79 O
ATOM 4390 N ALA B 270 59.471 56.465 20.955 1.00 11.28 N
ATOM 4391 CA ALA B 270 59.632 55.498 19.872 1.00 11.44 C
ATOM 4392 CB ALA B 270 58.638 54.349 20.029 1.00 10.86 C
ATOM 4393 C ALA B 270 59.468 56.156 18.509 1.00 11.55 C
ATOM 4394 O ALA B 270 58.724 57.130 18.362 1.00 12.80 O
ATOM 4395 N LYS B 271 60.158 55.610 17.510 1.00 12.31 N
ATOM 4396 CA LYS B 271 60.034 56.083 16.138 1.00 12.10 C
ATOM 4397 CB LYS B 271 61.305 55.768 15.345 1.00 13.10 C
ATOM 4398 CG LYS B 271 61.483 56.659 14.111 1.00 15.98 C
ATOM 4399 CD LYS B 271 62.706 56.250 13.329 1.00 22.87 C
ATOM 4400 CE LYS B 271 62.398 56.198 11.852 1.00 28.73 C
ATOM 4401 NZ LYS B 271 63.140 57.262 11.130 1.00 31.69 N
ATOM 4402 C LYS B 271 58.831 55.477 15.414 1.00 12.59 C
ATOM 4403 O LYS B 271 58.599 54.251 15.472 1.00 11.84 O
ATOM 4404 N GLY B 272 58.087 56.329 14.711 1.00 11.70 N
ATOM 4405 CA GLY B 272 57.049 55.867 13.800 1.00 12.75 C
ATOM 4406 C GLY B 272 57.668 55.297 12.535 1.00 13.64 C
ATOM 4407 O GLY B 272 58.536 55.921 11.942 1.00 15.55 O
ATOM 4408 N VAL B 273 57.252 54.101 12.129 1.00 12.37 N
ATOM 4409 CA VAL B 273 57.824 53.480 10.931 1.00 11.64 C
ATOM 4410 CB VAL B 273 58.804 52.320 11.261 1.00 10.74 C
ATOM 4411 CG1 VAL B 273 60.120 52.851 11.843 1.00 14.05 C
ATOM 4412 CG2 VAL B 273 58.167 51.305 12.215 1.00 9.80 C
ATOM 4413 C VAL B 273 56.720 52.964 10.029 1.00 11.84 C
ATOM 4414 O VAL B 273 55.703 52.453 10.506 1.00 11.64 O
ATOM 4415 N ASN B 274 56.933 53.083 8.724 1.00 11.57 N
ATOM 4416 CA ASN B 274 55.908 52.731 7.755 1.00 11.53 C
ATOM 4417 CB ASN B 274 56.001 53.639 6.530 1.00 11.62 C
ATOM 4418 CG ASN B 274 55.628 55.060 6.844 1.00 13.58 C
ATOM 4419 OD1 ASN B 274 54.932 55.322 7.824 1.00 12.07 O
ATOM 4420 ND2 ASN B 274 56.089 55.998 6.014 1.00 10.62 N
ATOM 4421 C ASN B 274 55.950 51.261 7.335 1.00 11.34 C
ATOM 4422 0 ASN B 274 54.978 50.744 6.796 1.00 10.28 O
ATOM 4423 N LEU B 275 57.084 50.609 7.562 1.00 10.78 N
ATOM 4424 CA LEU B 275 57.164 49.160 7.443 1.00 10.37 C
ATOM 4425 CB LEU B 275 58.442 48.730 6.701 1.00 11.88 C
ATOM 4426 CG LEU B 275 58.625 47.219 6.495 1.00 12.41 C
ATOM 4427 CD1 LEU B 275 57.561 46.647 5.573 1.00 15.16 C
ATOM 4428 CD2 LEU B 275 60.026 46.906 5.956 1.00 16.09 C
ATOM 4429 C LEU B 275 57.150 48.575 8.835 1.00 10.07 C
ATOM 4430 O LEU B 275 57.930 49.001 9.688 1.00 9.67 O
ATOM 4431 N SER B 276 56.253 47.622 9.088 1.00 9.34 N
ATOM 4432 CA SER B 276 56.196 46.985 10.411 1.00 9.05 C
ATOM 4433 CB SER B 276 55.055 45.966 10.481 1.00 7.75 C
ATOM 4434 OG SER B 276 55.133 45.204 11.682 1.00 6.12 O
ATOM 4435 C SER B 276 57.513 46.301 10.760 1.00 9.69 C
ATOM 4436 O SER B 276 58.092 45.582 9.917 1.00 10.40 O
ATOM 4437 N PRO B 277 58.004 46.542 11.982 1.00 10.04 N
ATOM 4438 CA PRO B 277 59.145 45.793 12.535 1.00 10.92 C
ATOM 4439 CB PRO B 277 59.095 46.142 14.025 1.00 11.46 C
ATOM 4440 CG PRO B 277 58.569 47.563 14.026 1.00 11.29 C
ATOM 4441 CD PRO B 277 57.548 47.604 12.902 1.00 9.74 C
ATOM 4442 C PRO B 277 59.019 44.284 12.359 1.00 11.56 C
ATOM 4443 O PRO B 277 60.039 43.615 12.176 1.00 10.49 O
ATOM 4444 N LEU B 278 57.793 43.761 12.401 1.00 11.68 N
ATOM 4445 CA LEU B 278 57.558 42.341 12.137 1.00 13.26 C
ATOM 4446 CB LEU B 278 56.066 41.995 12.299 1.00 12.45 C
ATOM 4447 CG LEU B 278 55.582 40.599 11.895 1.00 12.52 C
ATOM 4448 CD1 LEU B 278 56.301 39.498 12.704 1.00 12.08 C
ATOM 4449 CD2 LEU B 278 54.058 40.483 12.038 1.00 7.86 C
ATOM 4450 C LEU B 278 58.053 41.958 10.738 1.00 13.59 C
ATOM 4451 O LEU B 278 58.868 41.046 10.585 1.00 14.54 O
ATOM 4452 N HIS B 279 57.575 42.674 9.731 1.00 13.60 N
ATOM 4453 CA HIS B 279 57.944 42.391 8.344 1.00 15.06 C
ATOM 4454 CB HIS B 279 56.994 43.109 7.391 1.00 14.00 C
ATOM 4455 CG HIS B 279 55.578 42.641 7.510 1.00 14.68 C
ATOM 4456 ND1 HIS B 279 54.890 42.080 6.459 1.00 13.21 N
ATOM 4457 CE1 HIS B 279 53.681 41.735 6.861 1.00 13.88 C
ATOM 4458 NE2 HIS B 279 53.560 42.049 8.138 1.00 13.39 N
ATOM 4459 CD2 HIS B 279 54.736 42.613 8.571 1.00 10.59 C
ATOM 4460 C HIS B 279 59.401 42.743 8.032 1.00 15.98 C
ATOM 4461 O HIS B 279 60.065 42.048 7.258 1.00 16.30 O
ATOM 4462 N ARG B 280 59.889 43.822 8.628 1.00 18.07 N
ATOM 4463 CA ARG B 280 61.290 44.203 8.458 1.00 19.95 C
ATOM 4464 CB AARG B 280 61.578 45.505 9.211 0.50 19.61 C
ATOM 4465 CB BARG B 280 61.611 45.511 9.183 0.50 20.10 C
ATOM 4466 CG AARG B 280 63.043 45.950 9.221 0.50 19.56 C
ATOM 4467 CG BARG B 280 62.942 46.131 8.755 0.50 21.79 C
ATOM 4468 CD AARG B 280 63.302 47.202 10.064 0.50 20.50 C
ATOM 4469 CD BARG B 280 63.353 47.361 9.546 0.50 26.01 C
ATOM 4470 NE AARG B 280 63.298 46.910 11.498 0.50 19.45 N
ATOM 4471 NE BARG B 280 64.495 48.040 8.937 0.50 28.88 N
ATOM 4472 CZ AARG B 280 62.832 47.730 12.439 0.50 19.25 C
ATOM 4473 CZ BARG B 280 65.754 47.913 9.347 0.50 31.47 C
ATOM 4474 NH1AARG B 280 62.319 48.910 12.117 0.50 17.20 N
ATOM 4475 NH1 BARG B 280 66.050 47.128 10.378 0.50 31.80 N
ATOM 4476 NH2AARG B 280 62.878 47.364 13.711 0.50 18.49 N
ATOM 4477 NH2BARG B 280 66.723 48.574 8.726 0.50 30.72 N
ATOM 4478 C ARG B 280 62.216 43.082 8.938 1.00 21.04 C
ATOM 4479 O ARG B 280 63.181 42.737 8.252 1.00 21.32 O
ATOM 4480 N ALA B 281 61.894 42.494 10.088 1.00 22.88 N
ATOM 4481 CA ALA B 281 62.690 41.397 10.660 1.00 25.73 C
ATOM 4482 CB ALA B 281 62.170 41.020 12.057 1.00 25.31 C
ATOM 4483 C ALA B 281 62.733 40.160 9.762 1.00 26.98 C
ATOM 4484 O ALA B 281 63.599 39.297 9.930 1.00 28.48 O
ATOM 4485 N MSE B 282 61.807 40.078 8.812 1.00 28.53 N
ATOM 4486 CA MSE B 282 61.704 38.915 7.925 1.00 30.26 C
ATOM 4487 CB MSE B 282 60.238 38.513 7.759 1.00 29.98 C
ATOM 4488 CG MSE B 282 59.617 38.001 9.042 1.00 31.29 C
ATOM 4489 SE MSE B 282 57.683 37.756 8.918 1.00 40.04 SE
ATOM 4490 CE MSE B 282 57.678 35.968 8.060 1.00 31.76 C
ATOM 4491 C MSE B 282 62.354 39.134 6.549 1.00 31.75 C
ATOM 4492 0 MSE B 282 62.264 38.273 5.669 1.00 32.11 O
ATOM 4493 N LEU B 283 63.010 40.281 6.370 1.00 33.17 N
ATOM 4494 CA LEU B 283 63.712 40.581 5.116 1.00 34.52 C
ATOM 4495 CB LEU B 283 63.943 42.089 4.964 1.00 34.71 C
ATOM 4496 CG LEU B 283 62.734 42.986 4.681 1.00 35.14 C
ATOM 4497 CD1 LEU B 283 63.138 44.453 4.771 1.00 35.02 C
ATOM 4498 CD2 LEU B 283 62.112 42.677 3.322 1.00 36.34 C
ATOM 4499 C LEU B 283 65.049 39.842 5.028 1.00 35.06 C
ATOM 4500 O LEU B 283 65.549 39.532 3.944 1.00 36.64 O
ATOM 4501 OXT LEU B 283 65.687 39.529 6.031 1.00 34.75 O
ATOM 4502 02B CDM C 1 39.514 46.546 20.054 1.00 46.00 O
ATOM 4503 PB CDM C 1 39.570 46.786 18.566 1.00 42.98 P
ATOM 4504 01 B CDM C 1 40.826 46.460 17.794 1.00 44.25 O
ATOM 4505 03B CDM C 1 39.141 48.335 18.354 1.00 42.22 O
ATOM 4506 C1M CDM C 1 39.685 49.141 17.411 1.00 35.68 C
ATOM 4507 C2 CDM C 1 39.969 50.207 16.766 1.00 31.29 C
ATOM 4508 C3M CDM C 1 40.770 51.344 17.363 1.00 26.37 C
ATOM 4509 C4M CD C 1 41.325 52.173 16.203 1.00 22.74 C
ATOM 4510 04M CDM C 1 42.466 51.538 15.638 1.00 16.99 O
ATOM 4511 C5M CDM C 1 39.853 52.200 18.230 1.00 26.75 C
ATOM 4512 03M CDM C 1 41.847 50.873 18.178 1.00 27.21 O
ATOM 4513 02M CDM C 1 39.141 50.496 15.762 1.00 32.63 O
ATOM 4514 03A CDM C 1 38.354 46.020 17.835 1.00 44.65 O
ATOM 4515 PA CDM C 1 37.459 44.853 18.503 1.00 45.16 P
ATOM 4516 01A CDM C 1 38.197 44.211 19.663 1.00 43.26 O
ATOM 4517 02A CDM C 1 37.036 43.977 17.344 1.00 43.46 O
ATOM 4518 05* CDM C 1 36.159 45.677 19.060 1.00 40.12 O
B2004/003024 179
ATOM 4519 C5* CDM C 1 35.822 45.750 20.450 1.00 34.04 c
ATOM 4520 C4* CDM C 1 34.602 46.641 20.716 1.00 32.01 c
ATOM 4521 04* CDM C 1 34.920 48.012 20.437 1.00 30.62 0
ATOM 4522 C1* CDM C 1 33.846 48.700 19.764 1.00 28.93 c
ATOM 4523 C2* CDM C 1 32.741 47.665 19.603 1.00 30.27 c
ATOM 4524 C3* CDM C 1 33.383 46.320 19.860 1.00 31.23 c
ATOM 4525 O3* CDM C 1 32.476 45.420 20.494 1.00 33.08 o
ATOM 4526 O2* CDM C 1 31.717 47.927 20.550 1.00 28.47 0
ATOM 4527 N1 CDM C 1 34.265 49.177 18.434 1.00 23.33 N
ATOM 4528 C6 CDM C 1 35.599 48.699 18.023 1.00 25.26 c
ATOM 4529 C5 CDM C 1 36.127 49.160 16.663 1.00 25.05 c
ATOM 4530 C4 CDM C 1 35.096 49.731 15.664 1.00 23.49 c
ATOM 4531 N4 CDM C 1 35.664 50.337 14.453 1.00 23.29 N
ATOM 4532 N3 CDM C 1 33.930 50.373 16.240 1.00 19.18 N
ATOM 4533 C2 CDM C 1 33.336 49.736 17.414 1.00 22.66 C
ATOM 4534 02 CDM C 1 32.132 50.347 17.903 1.00 19.78 O
ATOM 4535 02B CDM C 2 30.522 19.797 17.890 1.00 35.78 O
ATOM 4536 PB CDM C 2 31.609 19.704 16.829 1.00 39.44 P
ATOM 4537 01 B CDM C 2 31.577 20.579 15.592 1.00 38.54 O
ATOM 4538 OSB CDM C 2 31.812 18.148 16.433 1.00 36.69 O
ATOM 4539 C1M CDM C 2 30.754 17.375 16.054 1.00 33.82 C
ATOM 4540 C2M CDM C 2 30.229 16.317 15.496 1.00 29.31 C
ATOM 4541 C3M CDM C 2 29.816 15.078 16.264 1.00 25.00 C
ATOM 4542 C4M CDM C 2 28.757 14.329 15.448 1.00 21.71 C
ATOM 4543 04M CDM C 2 27.497 14.987 15.473 1.00 16.29 O
ATOM 4544 C5M CDM C 2 31.046 14.187 16.439 1.00 23.51 c
ATOM 4545 03M CDM C 2 29.276 15.406 17.552 1.00 25.88 O
ATOM 4546 02M CDM C 2 30.561 16.209 14.212 1.00 29.49 O
ATOM 4547 03A CDM C 2 33.065 19.938 17.454 1.00 36.27 O
ATOM 4548 PA CDM C 2 33.313 20.349 18.971 1.00 36.97 P
ATOM 4549 01A CDM C 2 32.376 19.570 19.865 1.00 36.06 O
ATOM 4550 02A CDM C 2 33.366 21.857 18.995 1.00 34.41 O
ATOM 4551 05' CDM C 2 34.792 19.754 19.158 1.00 34.30 O
ATOM 4552 C5* CDM C 2 35.398 19.629 20.431 1.00 30.86 c
ATOM 4553 C4* CDM C 2 36.694 18.873 20.224 1.00 26.60 c
ATOM 4554 04* CDM C 2 36.414 17.523 19.810 1.00 26.84 O
ATOM 4555 C1* CDM C 2 37.471 17.034 18.962 1.00 23.20 c
ATOM 4556 C2* CDM C 2 38.399 18.214 18.745 1.00 24.84 c
ATOM 4557 C3* CDM C 2 37.570 19.421 19.106 1.00 26.32 c
ATOM 4558 03* CDM C 2 38.371 20.529 19.488 1.00 29.67 O
180
ATOM 4559 O2* CDM C 2 39.487 18.074 19.633 1.00 25.35 0
ATOM 4560 N1 CDM C 2 36.968 16.600 17.648 1.00 20.40 N
ATOM 4561 C6 CDM C 2 35.675 17.172 17.257 1.00 16.63 C
ATOM 4562 C5 CDM C 2 35.115 16.725 15.915 1.00 16.29 C
ATOM 4563 C4 CDM C 2 36.095 16.087 14.916 1.00 16.22 c
ATOM 4564 N4 CDM C 2 35.496 15.509 13.715 1.00 18.25 N
ATOM 4565 N3 CDM C 2 37.219 15.377 15.482 1.00 17.01 N
ATOM 4566 C2 CDM C 2 37.850 15.989 16.631 1.00 16.73 C
ATOM 4567 O2 CDM C 2 39.004 15.308 17.122 1.00 21.57 O
ATOM 4568 O1A ANP D 1 46.160 45.739 25.031 1.00 61.99 O
ATOM 4569 PA ANP D 1 44.791 45.855 24.240 1.00 62.29 P
ATOM 4570 O2A ANP D 1 44.092 47.254 24.492 1.00 63.05 O
ATOM 4571 O3AANP D 1 45.047 45.639 22.669 1.00 60.56 O
ATOM 4572 PB ANP D 1 43.838 45.711 21.610 1.00 60.13 P
ATOM 4573 O1 B ANP D 1 42.802 44.536 21.916 1.00 60.12 O
ATOM 4574 O2B ANP D 1 44.404 45.502 20.140 1.00 56.68 O
ATOM 4575 N3B ANP D 1 43.013 47.265 21.721 0.50 55.43 N
ATOM 4576 PG ANP D 1 43.853 48.805 21.853 0.50 51.56 P
ATOM 4577 O3G ANP D 1 43.107 49.711 22.924 0.50 51.10 O
ATOM 4578 O2G ANP D 1 43.860 49.555 20.451 0.50 50.50 O
ATOM 4579 O1G ANP D 1 45.348 48.574 22.333 0.50 52.86 O
ATOM 4580 O5* ANP D 1 43.787 44.663 24.668 1.00 61.39 O
ATOM 4581 C5* ANP D 1 42.490 44.939 25.205 1.00 57.24 C
ATOM 4582 C4* ANP D 1 41.706 43.641 25.385 1.00 53.97 C
ATOM 4583 O4* ANP D 1 42.280 42.554 24.634 1.00 50.38 O
ATOM 4584 C1* ANP D 1 42.292 41.356 25.430 1.00 47.48 C
ATOM 4585 C2* ANP D 1 42.245 41.805 26.883 1.00 50.67 c
ATOM 4586 02* ANP D 1 41.425 40.948 27.660 1.00 52.22 0
ATOM 4587 C3* ANP D 1 41.681 43.214 26.841 1.00 53.16 c
ATOM 4588 03" ANP D 1 40.346 43.239 27.321 1.00 54.40 o
ATOM 4589 N9 ANP D 1 43.495 40.534 25.107 1.00 41.15 N
ATOM 4590 C8 ANP D 1 43.505 39.226 24.726 1.00 37.99 C
ATOM 4591 N7 ANP D 1 44.777 38.753 24.474 1.00 32.37 N
ATOM 4592 C5 ANP D 1 45.609 39.775 24.691 1.00 34.56 C
ATOM 4593 C6 ANP D 1 47.068 40.060 24.639 1.00 34.34 c
ATOM 4594 N6 ANP D 1 47.947 39.091 24.275 1.00 27.89 N
ATOM 4595 C4 ANP D 1 44.772 40.889 25.081 1.00 37.41 C
ATOM 4596 N3 ANP D 1 45.345 42.167 25.397 1.00 36.93 N
ATOM 4597 C2 ANP D 1 46.684 42.311 25.318 1.00 36.20 C
ATOM 4598 N1 ANP D 1 47.510 41.307 24.955 1.00 34.25 N
2004/003024 181
ATOM 4599 O1 A ANP D 2 28.412 18.731 23.102 1.00 57.26 O
ATOM 4600 PA ANP D 2 28.780 20.161 22.525 1.00 57.54 P
ATOM 4601 O2A ANP D 2 30.098 20.075 21.632 1.00 58.23 o
ATOM 4602 O3A ANP D 2 27.600 20.872 21.678 1.00 58.65 o
ATOM 4603 PB ANP D 2 26.017 20.605 21.843 1.00 57.41 P
ATOM 4604 O1B ANP D 2 25.352 21.069 20.475 1.00 55.30 o
ATOM 4605 O2B ANP D 2 25.422 21.459 23.046 1.00 57.59 o
ATOM 4606 N3B ANP D 2 25.651 18.915 22.170 1.00 56.88 N
ATOM 4607 PG ANP D 2 26.403 17.559 21.354 1.00 53.82 P
ATOM 4608 O3G ANP D 2 27.119 16.583 22.390 1.00 57.53 O
ATOM 4609 O2G ANP D 2 27.470 18.103 20.310 1.00 57.25 O
ATOM 4610 O1G ANP D 2 25.320 16.715 20.579 1.00 55.14 O
ATOM 4611 O5* ANP D 2 29.000 21.160 23.763 1.00 54.71 o
ATOM 4612 C5* ANP D 2 28.084 21.190 24.854 1.0048.49 c
ATOM 4613 C4* ANP D 2 28.297 22.538 25.508 1.0043.87 c
ATOM 4614 O4* ANP D 2 27.759 23.596 24.700 1.00 40.43 o
ATOM 4615 C1* ANP D 2 27.610 24.734 25.557 1.00 36.68 c
ATOM 4616 C2* ANP D 2 27.430 24.174 26.967 1.00 39.49 c
ATOM 4617 O2* ANP D 2 28.388 24.727 27.848 1.00 39.45 o
ATOM 4618 C3* ANP D 2 27.610 22.674 26.846 1.0041.82 c
ATOM 4619 O3* ANP D 2 28.402 22.141 27.895 1.0043.65 o
ATOM 4620 N9 ANP D 2 26.463 25.602 25.154 1.00 29.90 N
ATOM 4621 C8 ANP D 2 26.547 26.907 24.775 1.00 25.60 c
ATOM 4622 N7 ANP D 2 25.321 27.450 24.460 1.00 21.46 N
ATOM 4623 C5 ANP D 2 24.419 26.474 24.641 1.00 24.70 C
ATOM 4624 C6 ANP D 2 22.948 26.274 24.521 1.00 23.71 C
ATOM 4625 N6 ANP D 2 22.148 27.298 24.117 1.00 21.37 N
ATOM 4626 C4 ANP D 2 25.168 25.317 25.082 1.00 27.16 C
ATOM 4627 N3 ANP D 2 24.504 24.066 25.360 1.00 26.89 N
ATOM 4628 C2 ANP D 2 23.163 24.005 25.224 1.00 27.30 C
ATOM 4629 N1 ANP D 2 22.414 25.060 24.825 1.00 25.94 N
ATOM 4630 OW HOH W 1 18.590 22.642 2.835 1.00 10.28 O
ATOM 4631 OW HOH W 2 24.636 5.577 16.025 1.00 11.02 O
ATOM 4632 OW HOH W 3 16.919 22.450 12.347 1.00 3.98 O
ATOM 4633 OW HOH W 4 15.769 32.412 7.570 1.00 10.20 O
ATOM 4634 OW HOH W 5 28.652 14.344 1.860 1.00 16.67 O
ATOM 4635 OW HOH W 6 14.876 37.250 5.454 1.00 11.29 O
ATOM 4636 OW HOH W 7 33.019 4.442 6.883 1.00 14.38 O
ATOM 4637 OW HOH W 8 43.322 67.867 -1.038 1.00 13.48 O
ATOM 4638 OW HOH W 9 27.317 1.280 17.661 1.00 13.06 O
ATOM 4639 OW HOH W 10 31.307 0.881 14.935 1.00 14.64 O
ATOM 4640 OW HOH W 11 32.371 1.266 18.874 1.00 17.22 O
ATOM 4641 OW HOH W 12 23.050 46.660 7.366 1.00 15.04 O
ATOM 4642 OW HOH W 13 36.028 57.181 0.826 1.00 12.02 O
ATOM 4643 OW HOH W 14 25.945 -1.076 17.594 1.00 16.55 O
ATOM 4644 OW HOH W 15 42.521 22.516 15.074 1.00 16.15 O
ATOM 4645 OW HOH W 16 20.756 19.486 6.361 1.00 12.83 O
ATOM 4646 OW HOH W 17 17.077 11.206 27.550 1.00 16.08 O
ATOM 4647 OW HOH W 18 27.415 41.414 16.238 1.00 16.86 O
ATOM 4648 OW HOH W 19 29.473 35.449 17.539 1.00 13.51 O
ATOM 4649 OW HOH W 20 17.611 23.862 14.605 1.00 9.34 O
ATOM 4650 OW HOH W 21 28.941 22.145 6.119 1.00 14.73 O
ATOM 4651 OW HOH W 22 28.654 36.136 22.219 1.00 16.62 O
ATOM 4652 OW HOH W 23 9.483 37.673 17.160 1.00 17.24 O
ATOM 4653 OW HOH W 24 29.938 36.675 19.909 1.00 14.08 O
ATOM 4654 OW HOH W 25 42.367 45.265 0.642 1.00 38.62 O
ATOM 4655 OW HOH W 26 28.438 17.441 10.410 1.00 14.50 O
ATOM 4656 OW HOH W 27 13.416 -2.422 33.539 1.00 13.06 O
ATOM 4657 OW HOH W 28 8.280 13.030 18.454 1.00 13.20 O
ATOM 4658 OW HOH W 29 25.141 9.106 37.833 1.00 21.88 O
ATOM 4659 OW HOH W 30 11.079 -1.198 36.016 1.00 16.71 O
ATOM 4660 OW HOH W 31 9.354 17.134 10.118 1.00 22.07 O
ATOM 4661 OW HOH W 32 10.681 40.129 25.794 1.00 16.96 O
ATOM 4662 OW HOH W 33 8.469 10.999 26.076 1.00 14.76 O
ATOM 4663 OW HOH W 34 21.920 18.117 23.543 1.00 19.32 O
ATOM 4664 OW HOH W 35 30.213 29.910 30.045 1.00 20.91 O
ATOM 4665 OW HOH W 36 23.646 42.113 25.188 1.00 15.32 O
ATOM 4666 OW HOH W 37 7.535 21.746 13.573 1.00 15.12 O
ATOM 4667 OW HOH W 38 65.322 33.135 20.259 1.00 17.88 O
ATOM 4668 OW HOH W 39 29.286 -1.571 21.997 1.00 29.22 O
ATOM 4669 OW HOH W 40 26.542 1.688 7.871 1.00 15.21 O
ATOM 4670 OW HOH W 41 6.881 -1.319 17.026 1.00 27.55 O
ATOM 4671 OW HOH W 42 25.153 -1.055 20.126 1.00 11.35 O
ATOM 4672 OW HOH W 43 21.173 -0.890 11.216 1.00 23.50 O
ATOM 4673 OW HOH W 44 17.046 4.728 9.716 1.00 17.29 O
ATOM 4674 OW HOH W 45 28.649 21.208 16.324 1.00 21.32 O
ATOM 4675 OW HOH W 46 28.503 20.610 8.512 1.00 18.22 O
ATOM 4676 OW HOH W 47 26.564 -4.881 7.906 1.00 23.59 O
ATOM 4677 OW HOH W 48 66.225 31.844 16.606 1.00 11.61 O
ATOM 4678 OW HOH W 49 32.073 32.609 14.616 1.00 17.78 O
ATOM 4679 OW HOH W 50 26.579 21.112 -0.040 1.00 22.26 O
ATOM 4680 OW HOH W 51 32.090 1.505 -0.779 1.00 16.91 o
ATOM 4681 OW HOH W 52 35.549 10.489 6.080 1.00 23.16 o
ATOM 4682 OW HOH W 53 13.665 7.608 -0.021 1.00 36.27 o
ATOM 4683 OW HOH W 54 19.409 2.722 5.307 1.00 20.79 o
ATOM 4684 OW HOH W 55 14.607 26.671 30.155 1.00 27.52 o
ATOM 4685 OW HOH W 56 17.931 4.540 12.267 1.00 18.35 o
ATOM 4686 OW HOH W 57 10.221 29.488 24.497 1.00 21.94 o
ATOM 4687 OW HOH W 58 40.040 5.047 6.977 1.00 16.63 o
ATOM 4688 OW HOH W 59 22.029 -2.946 18.534 1.00 16.36 o
ATOM 4689 OW HOH W 60 8.617 40.871 17.772 1.00 20.41 o
ATOM 4690 OW HOH W 61 30.405 37.485 15.448 1.00 30.07 o
ATOM 4691 OW HOH W 62 7.505 21.726 16.373 1.00 29.47 o
ATOM 4692 OW HOH W 63 32.460 28.861 7.173 1.00 17.58 o
ATOM 4693 OW HOH W 64 32.995 17.075 13.487 1.00 23.49 o
ATOM 4694 OW HOH W 65 21.513 21.216 24.795 1.00 27.77 o
ATOM 4695 OW HOH W 66 10.739 21.794 19.660 1.00 26.24 o
ATOM 4696 OW HOH W 67 21.661 18.162 31.113 1.00 33.25 o
ATOM 4697 OW HOH W 68 27.860 15:950 26.529 1.00 26.58 o
ATOM 4698 OW HOH W 69 24.155 29.964 -2.789 1.00 23.08 o
ATOM 4699 OW HOH W 70 27.069 23.374 4.324 1.00 22.34 o
ATOM 4700 OW HOH W 71 6.680 24.590 23.447 1.00 31.93 o
ATOM 4701 OW HOH W 72 11.769 20.258 17.894 1.00 27.89 o
ATOM 4702 OW HOH W 73 2.034 3.228 17.463 1.00 29.89 o
ATOM 4703 OW HOH W 74 12.755 -2.427 17.653 1.00 23.57 o
ATOM 4704 OW HOH W 75 41.424 11.014 6.859 1.00 26.47 o
ATOM 4705 OW HOH W 76 10.620 30.803 26.653 1.00 32.13 o
ATOM 4706 OW HOH W 77 12.278 7.745 4.639 1.00 32.93 o
ATOM 4707 OW HOH W 78 13.231 32.839 5.910 1.00 26.21 o
ATOM 4708 OW HOH W 79 13.254 47.836 22.004 1.00 25.58 o
ATOM 4709 OW HOH W 80 3.405 4.867 15.700 1.00 30.55 o
ATOM 4710 OW HOH W 81 48.111 17.359 15.800 1.00 35.87 o
ATOM 4711 OW HOH W 82 34,490 61.676 0.237 1.00 21.21 o
ATOM 4712 OW HOH W 83 26.646 42.429 18.570 1.00 28.34 o
ATOM 4713 OW HOH W 84 8.993 19.448 17.294 1.00 21.99 o
ATOM 4714 OW HOH W 85 10.241 22.498 23.954 1.00 27.25 o
ATOM 4715 OW HOH W 86 32.064 -0.177 32.069 1.00 26.49 o
ATOM 4716 OW HOH W 87 37.762 17.556 4.721 1.00 29.57 o
ATOM 4717 OW HOH W 88 9.501 18.746 22.000 1.00 23.78 o
ATOM 4718 OW HOH W 89 23.468 32.107 -1.577 1.00 19.17 o
ATOM 4719 OW HOH W 90 22.024 19.041 4.300 1.00 23.13 O
ATOM 4720 OW HOH W 91 22.987 30.914 29.246 1.00 20.40 O
ATOM 4721 OW HOH W 92 39.762 18.166 5.953 1.00 32.41 O
ATOM 4722 OW HOH W 93 13.507 6.702 32.080 1.00 25.09 O
ATOM 4723 OW HOH W 94 29.480 14.149 24.346 1.00 22.44 O
ATOM 4724 OW HOH W 95 26.820 26.971 2.437 1.00 21.00 O
ATOM 4725 OW HOH W 96 28.789 20.481 1.947 1.00 21.00 O
ATOM 4726 OW HOH W 97 21.231 -0.618 7.419 1.00 26.13 O
ATOM 4727 OW HOH W 98 37.877 8.760 26.896 1.00 28.59 O
ATOM 4728 OW HOH W 99 19.170 1.006 11.583 1.00 28.99 O
ATOM 4729 OW HOH W 100 10.820 6.169 6.426 1.00 28.80 O
ATOM 4730 OW HOH W 101 28.134 24.201 18.453 1.00 24.00 O
ATOM 4731 OW HOH W 102 36.031 12.211 4.021 1.00 24.38 O
ATOM 4732 OW HOH W 103 13.024 9.554 34.398 1.00 36.33 O
ATOM 4733 OW HOH W 104 39.647 4.632 3.541 1.00 25.45 O
ATOM 4734 OW HOH W 105 33.957 32.153 29.708 1.00 34.29 O
ATOM 4735 OW HOH W 106 2.465 7.111 16.054 1.00 29.72 O
ATOM 4736 OW HOH W 107 10.420 -2.383 16.322 1.00 24.43 O
ATOM 4737 OW HOH W 108 42.954 20.529 16.956 1.00 29.57 O
ATOM 4738 OW HOH W 109 42.417 2.878 14.564 1.00 30.50 O
ATOM 4739 OW HOH W 110 32.960 4.669 34.777 1.00 28.75 O
ATOM 4740 OW HOH W 111 21.604 50.268 14.364 1.00 39.44 O
ATOM 4741 OW HOH W 112 17.999 4.065 3.213 1.00 38.59 O
ATOM 4742 OW HOH W 113 28.460 28.261 0.112 1.00 37.19 O
ATOM 4743 OW HOH W 114 29.115 14.587 35.085 1.00 33.31 O
ATOM 4744 OW HOH W 115 23.738 46 604 17.576 1.00 28.55 O
ATOM 4745 OW HOH W 116 31.917 45 523 4.263 1.00 31.67 O
ATOM 4746 OW HOH W 117 15.415 51 789 15.863 1.00 33.04 O
ATOM 4747 OW HOH W 118 21.571 -6.413 27.445 1.00 24.59 O
ATOM 4748 OW HOH W 119 21.492 2.710 -4.732 1.00 28.94 O
ATOM 4749 OW HOH W 120 23.134 48.062 21.742 1.00 36.61 O
ATOM 4750 OW HOH W 121 7.997 5.947 10.372 1.00 36.30 O
ATOM 4751 OW HOH W 122 47.613 14.013 9.045 1.0041.28 O
ATOM 4752 OW HOH W 123 31.128 -2.403 4.913 1.00 33.32 O
ATOM 4753 OW HOH W 124 16.869 -6.478 20.207 1.00 34.70 O
ATOM 4754 OW HOH W 125 30.518 39.781 16.825 1.00 36.76 O
ATOM 4755 OW HOH W 126 7.412 12.514 24.154 1.00 38.59 O
ATOM 4756 OW HOH W 127 41.599 39.962 3.187 1.00 26.98 O
ATOM 4757 OW HOH W 128 29.180 6.788 34.371 1.00 22.69 O
ATOM 4758 OW HOH W 129 26.855 13.482 28.104 1.00 23.13 O
ATOM 4759 OW HOH W 130 25.175 15.432 28.964 1.00 24.28 G
ATOM 4760 OW HOH W 131 41.054 15.514 18.659 1.00 26.46 O
ATOM 4761 OW HOH W 132 10.104 14.434 7.392 1.00 18.61 O
ATOM 4762 OW HOH W 133 19.342 25.239 32.029 1.00 27.88 O
ATOM 4763 OW HOH W 134 42.213 34.820 -0.519 1.00 35.30 O
ATOM 4764 OW HOH W 135 30.199 0.288 17.867 1.00 27.42 O
ATOM 4765 OW HOH W 136 33.925 24.231 12.906 1.00 34.45 O
ATOM 4766 OW HOH W 137 26.763 21.766 30.632 1.00 40.18 O
ATOM 4767 OW HOH W 138 31.142 -0.238 9.786 1.00 39.21 O
ATOM 4768 OW HOH W 139 36.944 38.115 8.075 1.00 33.07 O
ATOM 4769 OW HOH W 140 33.402 0.253 12.196 1.00 28.43 O
ATOM 4770 OW HOH W 141 27.559 -2.897 -0.613 1.0045.03 O
ATOM 4771 OW HOH W 142 28.577 24.919 5.486 1.00 28.47 O
ATOM 4772 OW HOH W 143 23.770 30.523 33.377 1.00 29.32 O
ATOM 4773 OW HOH W 144 27.427 -0.867 -2.381 1.00 35.31 O
ATOM 4774 OW HOH W 145 10.398 25.578 5.202 1.00 27.49 O
ATOM 4775 OW HOH W 146 44.605 8.655 9.827 1.00 28.70 O
ATOM 4776 OW HOH W 147 34.401 67.421 3.648 1.00 28.56 O
ATOM 4777 OW HOH W 148 32.615 31.780 23.910 1.00 28.78 O
ATOM 4778 OW HOH W 149 29.407 18.931 27.255 1.00 37.19 O
ATOM 4779 OW HOH W 150 25.419 -5.423 16.855 1.00 39.25 O
ATOM 4780 OW HOH W 151 26.209 -1.514 -6.080 1.00 57.09 0
ATOM 4781 OW HOH W 152 48.136 64.532 -4.764 1.00 39.82 o
ATOM 4782 OW HOH W 153 30.411 -3.802 28.011 1.00 33.89 0
ATOM 4783 OW HOH W 154 27.802 33.547 5.222 1.00 28.29 o
ATOM 4784 OW HOH W 155 28.484 14.611 20.210 1.00 24.97 o
ATOM 4785 OW HOH W 156 12.529 -4.346 19.514 1.00 25.24 0
ATOM 4786 OW HOH W 157 32.356 24.008 18.628 1.00 37.48 0
ATOM 4787 OW HOH W 158 24.507 -1 ,886 15.290 1.00 28.80 o
ATOM 4788 OW HOH W 159 11.389 12.379 3.340 1.00 28.89 0
ATOM 4789 OW HOH W 160 33.686 -1.145 25.498 1.00 29.07 0
ATOM 4790 OW HOH W 161 10.209 10.009 3.016 1.00 46.86 o
ATOM 4791 OW HOH W 162 45.409 60.994 16.442 1.00 6.80 0
ATOM 4792 OW HOH W 163 42.325 61.034 -1.939 1.00 39.37 o
ATOM 4793 OW HOH W 164 52.337 42.650 14.611 1.00 7.12 0
ATOM 4794 OW HOH W 165 53.039 44.005 12.267 1.00 5.74 0
ATOM 4795 OW HOH W 166 43.212 46.774 10.599 1.00 10.26 o
ATOM 4796 OW HOH W 167 37.695 64.839 19.575 1.00 16.65 0
ATOM 4797 OW HOH W 168 42.600 65.070 18.402 1.00 13.36 o
ATOM 4798 OW HOH W 169 53.183 55.165 27.730 1.00 17.99 0
186
ATOM 4799 OW HOH W 170 49.220 47.251 6.602 1.00 9.12 O
ATOM 4800 OW HOH W 171 43.221 64.692 8.513 1.00 14.66 o
ATOM 4801 OW HOH W 172 61.914 53.334 18.303 1.00 12.84 0
ATOM 4802 OW HOH W 173 43.563 70.035 0.559 1.00 28.89 0
ATOM 4803 OW HOH W 174 59.369 67.614 36.056 1.00 14.96 0
ATOM 4804 OW HOH W 175 42.556 24.815 16.291 1.00 11.31 o
ATOM 4805 OW HOH W 176 40.506 30.815 17.627 1.00 14.58 o
ATOM 4806 OW HOH W 177 34.375 55.399 6.679 1.00 12.87 0
ATOM 4807 OW HOH W 178 40.028 25.980 16.989 1.00 23.80 0
ATOM 4808 OW HOH W 179 47.483 19.722 6.265 1.00 20.54 0
ATOM 4809 OW HOH W 180 36.703 62.065 7.544 1.00 12.87 0
ATOM 4810 OW HOH W 181 56.885 68.693 33.545 1.00 15.69 o
ATOM 4811 OW HOH W 182 41.465 52.220 1.945 1.00 10.04 0
ATOM 4812 OW HOH W 183 53.978 34.378 7.150 1.00 13.74 0
ATOM 4813 OW HOH W 184 46.967 35.477 29.244 1.00 19.05 0
ATOM 4814 OW HOH W 185 45.225 57.175 38.481 1.00 18.10 0
ATOM 4815 OW HOH W 186 61.536 55.388 26.135 1.00 14.42 0
ATOM 4816 OW HOH W 187 17.421 14.939 2.893 1.00 15.93 0
ATOM 4817 OW HOH W 188 44.877 67.366 20.657 1.00 9.13 0
ATOM 4818 OW HOH W 189 42.580 47.199 0.182 1.00 19.34 0
ATOM 4819 OW HOH W 190 21.123 46.866 15.000 1.00 27.01 0
ATOM 4820 OW HOH W 191 67.989 63.146 17.325 1.00 26.34 0
ATOM 4821 OW HOH W 192 61.216 25.498 17.196 1.00 22.32 o
ATOM 4822 OW HOH W 193 60.392 28.704 16.455 1.00 11.87 o
ATOM 4823 OW HOH W 194 48.374 67.591 11.653 1.00 23.23 0
ATOM 4824 OW HOH W 195 67.533 59.177 15.983 1.00 26.26 o
ATOM 4825 OW HOH W 196 38.462 65.223 15.596 1.00 13.67 0
ATOM 4826 OW HOH W 197 14.358 15.809 3.648 1.00 19.88 0
ATOM 4827 OW HOH W 198 47.884 64.275 -0.101 1.00 34.67 0
ATOM 4828 OW HOH W 199 48.494 45.464 25.072 1.00 24.07 0
ATOM 4829 OW HOH W 200 27.024 5.846 -3.352 1.00 18.97 0
ATOM 4830 OW HOH W 201 48.659 47.495 3.825 1.00 15.66 0
ATOM 4831 OW HOH W 202 41.964 51.697 20.951 1.00 22.44 0
ATOM 4832 OW HOH W 203 50.540 46.292 2.118 1.00 23.56 o
ATOM 4833 OW HOH W 204 48.341 20.092 14.989 1.00 32.45 0
ATOM 4834 OW HOH W 205 29.884 60.379 7.634 1.00 21.61 0
ATOM 4835 OW HOH W 206 46.218 24.145 25.044 1.00 16.05 0
ATOM 4836 OW HOH W 207 60.820 47.037 16.990 1.00 22.55 0
ATOM 4837 OW HOH W 208 42.204 43.762 5.522 1.00 15.83 0
ATOM 4838 OW HOH W 209 47.407 67.804 16.771 1.00 17.87 0
ATOM 4839 OW HOH W 210 66.616 61.742 15.345 1.00 27.54 o
ATOM 4840 OW HOH W 211 60.056 68.574 16.756 1.00 21.27 o
ATOM 4841 OW HOH W 212 43.890 67.349 18.184 1.00 16.80 o
ATOM 4842 OW HOH W 213 35.980 43.647 5.246 1.00 17.21 0
ATOM 4843 OW HOH W 214 58.253 46.101 17.582 1.00 19.75 0
ATOM 4844 OW HOH W 215 41.253 30.094 22.393 1.00 17.99 o
ATOM 4845 OW HOH W 216 57.163 23.346 10.309 1.00 18.43 o
ATOM 4846 OW HOH W 217 46.649 47.092 2.112 1.00 22.38 o
ATOM 4847 OW HOH W 218 47.941 69.314 18.771 1.00 16.83 0
ATOM 4848 OW HOH W 219 59.307 44.644 19.529 1.00 23.85 0
ATOM 4849 OW HOH W 220 50.308 45.322 29.547 1.00 28.04 o
ATOM 4850 OW HOH W 221 59.673 36.850 24.113 1.00 16.63 o
ATOM 4851 OW HOH W 222 48.177 47.479 31.151 1.00 27.92 o
ATOM 4852 OW HOH W 223 32.093 55.816 0.796 1.00 25.90 0
ATOM 4853 OW HOH W 224 39.898 29.701 20.096 1.00 12.79 o
ATOM 4854 OW HOH W 225 48.497 66.948 7.423 1.00 23.32 0
ATOM 4855 OW HOH W 226 40.935 52.131 25.086 1.00 18.86 0
ATOM 4856 OW HOH W 227 39.874 36.446 30.229 1.00 26.22 0
ATOM 4857 OW HOH W 228 31.865 64.976 13.346 1.00 28.41 0
ATOM 4858 OW HOH W 229 40.692 41.716 6.761 1.00 21.67 o
ATOM 4859 OW HOH W 230 55.132 39.578 30.143 1.00 26.59 o
ATOM 4860 OW HOH W 231 56.873 59.519 32.217 1.00 19.92 o
ATOM 4861 OW HOH W 232 56.399 18.574 21.222 1.00 29.13 0
ATOM 4862 OW HOH W 233 59.231 26.202 25.227 1.00 20.33 0
ATOM 4863 OW HOH W 234 27.625 27.313 -2.208 1.00 32.91 o
ATOM 4864 OW HOH W 235 53.371 52.416 28.111 1.00 27.38 0
ATOM 4865 OW HOH W 236 41.303 67.259 11.892 1.00 30.18 o
ATOM 4866 OW HOH W 237 57.306 68.789 17.768 1.00 21.33 o
ATOM 4867 OW HOH W 238 41.594 (J . I iJ 5.860 1.00 24.28 o
ATOM 4868 OW HOH W 239 60.436 47.486 22.381 1.00 34.44 o
ATOM 4869 OW HOH W 240 52.888 16.661 7.042 1.00 27.57 0
ATOM 4870 OW HOH W 241 48.750 72.698 27.874 1.00 21.55 o
ATOM 4871 OW HOH W 242 60.510 49.082 10.075 1.00 29.22 o
ATOM 4872 OW HOH W 243 51.164 37.111 0.767 1.00 23.87 0
ATOM 4873 OW HOH W 244 43.856 71.460 8.034 1.00 33.69 0
ATOM 4874 OW HOH W 245 35.938 33.923 29.431 1.00 33.79 0
ATOM 4875 OW HOH W 246 33.885 47.071 6.974 1.00 26.24 o
ATOM 4876 OW HOH W 247 55.225 18.253 13.470 1.00 29.21 o
ATOM 4877 OW HOH W 248 55.292 22.123 11.844 1.00 21.48 0
ATOM 4878 OW HOH W 249 54.373 67.406 13.992 1.0045.18 o
ATOM 4879 OW HOH W 250 50.501 63.381 5.648 1.00 26.15 O ATOM 4880 OW HOH W 251 55.976 31.638 32.604 1.00 30.80 O ATOM 4881 OW HOH W 252 47.574 19.523 26.437 1.00 29.49 O ATOM 4882 OW HOH W 253 32.061 48.636 7.730 1.00 30.16 O ATOM 4883 OW HOH W 254 43.731 23.971 18.631 1.00 17.38 O ATOM 4884 OW HOH W 255 59.808 51.937 7.316 1.00 16.91 O ATOM 4885 OW HOH W 256 25.069 25.187 1.589 1.00 18.78 O ATOM 4886 OW HOH W 257 51.796 61.977 3.474 1.00 27.32 O ATOM 4887 OW HOH W 258 37.984 65.894 32.538 1.00 29.72 O ATOM 4888 OW HOH W 259 37.402 61.316 35.587 1.00 29.23 O ATOM 4889 OW HOH W 260 64.722 34.532 16.397 1.00 19.25 O ATOM 4890 OW HOH W 261 45.240 68.218 16.018 1.00 29.39 O ATOM 4891 OW HOH W 262 50.692 41.136 31.675 1.00 25.48 O ATOM 4892 OW HOH W 263 54.582 29.668 4.969 1.00 23.07 O ATOM 4893 OW HOH W 264 41.243 67.733 22.581 1.00 21.52 O ATOM 4894 OW HOH W 265 49.085 55.311 -1.628 1.00 20.24 O ATOM 4895 OW HOH W 266 28.782 54.410 7.785 1.00 31.44 O ATOM 4896 OW HOH W 267 28.099 14.173 -2.608 1.00 31.53 O ATOM 4897 OW HOH W 268 30.112 61.407 4.393 1.00 24.15 O ATOM 4898 OW HOH W 269 41.898 27.989 3.744 1.00 30.18 O ATOM 4899 OW HOH W 270 32.574 56.970 27.813 1.00 31.07 0 ATOM 4900 OW HOH W 271 57.851 70.530 19.659 1.00 25.64 0 ATOM 4901 OW HOH W 272 62.713 53.530 20.887 1.00 28.61 o ATOM 4902 OW HOH W 273 59.831 59.795 6.734 1.00 31.50 0 ATOM 4903 OW HOH W 274 59.016 40.797 4.828 1.00 25.33 0 ATOM 4904 OW HOH W 275 43.000 42.758 -0.740 1.00 28.35 0 ATOM 4905 OW HOH W 276 45.631 22.101 19.393 1.00 27.99 0 ATOM 4906 OW HOH W 277 40.867 69.987 4.517 1.00 31.49 0 ATOM 4907 OW HOH W 278 25.212 54.217 20.349 1.00 28.31 0 ATOM 4908 OW HOH W 279 Oy.u Η' 35.387 26.340 1.00 36.60 0 ATOM 4909 OW HOH W 280 62.917 57.649 8.598 1.00 25.94 0 ATOM 4910 OW HOH W 281 OO . t?ϊ2 42.982 4.221 1.00 37.02 0 ATOM 4911 OW HOH W 282 62.384 44.613 13.141 1.00 25.65 0 ATOM 4912 OW HOH W 283 38.662 27.231 7.114 1.00 31.00 0 ATOM 4913 OW HOH W 284 48.126 38.464 -0.137 1.00 44.77 0 ATOM 4914 OW HOH W 285 41.967 30.885 3.859 1.00 33.30 0 ATOM 4915 OW HOH W 286 38.448 32.578 17.674 1.00 32.08 o ATOM 4916 OW HOH W 287 25.500 56.158 10.558 1.00 28.36 0 ATOM 4917 OW HOH W 288 36.536 67.289 26.319 1.00 30.15 0 ATOM 4918 OW HOH W 289 20.476 3.632 -1.148 1.00 35.95 0
ATOM 4919 OW HOH W 290 40.946 59.674 34.823 1.00 22.31 O
ATOM 4920 OW HOH W 291 42.449 45.763 2.860 1.00 17.88 O
ATOM 4921 OW HOH W 292 38.604 66.716 10.521 1.00 27.06 O
ATOM 4922 OW HOH W 293 35.284 22.497 9.227 1.00 28.44 O
ATOM 4923 OW HOH W 294 29.285 8.079 -1.790 1.00 38.44 O
ATOM 4924 OW HOH W 295 39.720 28.549 15.951 1.00 21.15 O
ATOM 4925 OW HOH W 296 30.192 49.908 19.996 1.00 29.07 O
ATOM 4926 OW HOH W 297 34.850 21.898 11.913 1.00 35.06 O
ATOM 4927 OW HOH W 298 40.192 69.835 27.952 1.00 34.69 O
ATOM 4928 OW HOH W 299 38.411 46.104 22.541 1.00 57.51 O
ATOM 4929 OW HOH W 300 49.988 51.672 34.390 1.00 41.55 O
ATOM 4930 OW HOH W 301 61.466 38.017 25.943 1.00 47.21 O
ATOM 4931 OW HOH W 302 59.658 64.582 36.083 1.00 28.37 O
ATOM 4932 OW HOH W 303 61.772 27.101 14.794 1.00 35.17 O
ATOM 4933 OW HOH W 304 47.252 18.376 21.154 1.00 30.67 O
ATOM 4934 OW HOH W 305 44.564 71.579 26.415 1.00 37.29 O
ATOM 4935 OW HOH W 306 50.453 26.202 0.776 1.0046.50 O
ATOM 4936 OW HOH W 307 37.493 33.660 14.956 1.00 26.15 O
ATOM 4937 OW HOH W 308 48.090 17.501 4.175 1.00 37.51 O
ATOM 4938 OW HOH W 309 64.622 60.500 28.150 1.00 27.48 O
ATOM 4939 OW HOH W 310 33.645 52.768 5.245 1.00 28.05 O
ATOM 4940 OW HOH W 311 62.550 53.547 24.091 1.00 46.49 O
ATOM 4941 OW HOH W 312 44.928 18.585 7.027 1.00 31.66 O
ATOM 4942 OW HOH W 313 53.434 61.679 10.395 1.0040.18 O
ATOM 4943 OW HOH W 314 37.600 68.254 28.945 1.00 28.87 O
ATOM 4944 OW HOH W 315 50.188 16.885 6.089 1.0041.73 O
ATOM 4945 OW HOH W 316 35.901 42.281 14.037 1.0040.91 O
ATOM 4946 OW HOH W 317 21.918 1.731 -0.095 1.00 27.87 O
ATOM 4947 OW HOH 318 44.910 34.887 -1.217 1.00 31.90 O
ATOM 4948 OW HOH W 319 36.373 42.713 21.540 1.00 38.30 O
ATOM 4949 OW HOH W 320 34.430 38.821 14.807 1.00 38.98 O
ATOM 4950 OW HOH W 321 51.712 58.599 0.784 1.00 34.44 O
ATOM 4951 OW HOH W 322 59.662 56.478 35.899 1.00 38.64 O
ATOM 4952 OW HOH W 323 45.692 70.216 20.092 1.00 31.01 O
ATOM 4953 OW HOH W 324 25.795 44.864 19.021 1.00 27.60 O
ATOM 4954 OW HOH W 325 36.288 35.365 8.156 1.00 37.94 O
ATOM 4955 OW HOH W 326 62.897 35.160 13.272 1.00 35.53 O
ATOM 4956 OW HOH W 327 34.782 67.487 9.248 1.00 32.66 O
ATOM 4957 OW HOH W 328 4.172 35.369 25.682 1.00 70.30 O
ATOM 4958 OW HOH W 329 45.947 35.549 33.365 1.00 34.38 O
ATOM 4959 OW HOH W 330 48.489 41.466 -0.354 1.00 27.48 O
ATOM 4960 OW HOH W 331 33.933 44.034 9.550 1.00 38.22 O
ATOM 4961 OW HOH W 332 57.325 56.963 34.474 1.00 35.86 O
ATOM 4962 OW HOH W 333 61.756 37.687 13.129 1.00 45.85 O
ATOM 4963 OW HOH W 334 41.714 57.832 36.070 1.0043.49 O
ATOM 4964 OW HOH W 335 40.346 49.787 13.671 1.00 24.00 O
ATOM 4965 OW HOH W 336 29.114 17.267 12.795 1.00 30.82 O
ATOM 4966 OW HOH W 337 26.204 8.611 34.649 1.00 50.58 O
ATOM 4967 OW HOH W 338 63.641 42.140 22.415 1.00 45.74 O
ATOM 4968 OW HOH W 339 47.043 59.588 28.549 1.00 44.67 O
ATOM 4969 OW HOH W 340 33.914 34.005 13.141 1.00 24.71 O
ATOM 4970 OW HOH W 341 38.083 33.391 9.672 1.00 34.86 O
ATOM 4971 OW HOH W 342 18.248 42.598 2.760 1.00 30.88 O
ATOM 4972 OW HOH W 343 28.550 -0.862 11.291 1.00 26.82 O
ATOM 4973 OW HOH W 344 45.058 7.929 12.279 1.00 40.76 O
ATOM 4974 OW HOH W 345 24.004 49.528 18.485 1.00 41.32 O
ATOM 4975 OW HOH W 346 30.444 35.559 8.466 1.00 28.55 O
ATOM 4976 OW HOH W 347 10.814 5.488 42.093 1.00 39.82 O
ATOM 4977 OW HOH W 348 56.346 38.773 6.006 1.00 43.00 O
ATOM 4978 OW HOH W 349 57.911 55.763 31.794 1.00 35.77 O
ATOM 4979 OW HOH W 350 13.167 4.713 31.472 1.0040.42 0
ATOM 4980 OW HOH W 351 17.453 50.196 7.753 1.00 33.57 0
ATOM 4981 OW HOH W 352 12.251 10.409 31.992 1.00 33.92 0
ATOM 4982 OW HOH W 353 36.008 20.705 2.774 1.00 25.29 0
ATOM 4983 OW HOH W 354 15.504 15.810 27.002 1.00 32.55 0
ATOM 4984 OW HOH W 355 40.304 44.909 2.296 1.0044.83 0
ATOM 4985 OW HOH W 356 19.315 -6.038 20.500 1.00 36.81 0
ATOM 4986 OW HOH W 357 25.556 -5.301 25.910 1.00 37.87 0
ATOM 4987 OW HOH W 358 1.769 0.317 1.00 50.61 0
ATOM 4988 OW HOH W 359 35.870 32.174 13.175 1.00 35.88 o
ATOM 4989 OW HOH W 360 7.998 39.486 14.904 1.00 29.01 0
ATOM 4990 OW HOH W 361 11.258 uu. I
29.034 1.00 31.82 0
ATOM 4991 OW HOH W 362 11.126 37.794 6.185 1.00 31.82 0
ATOM 4992 OW HOH W 363 43.019 47.301 18.979 1.00 29.46 0
ATOM 4993 OW HOH W 364 30.128 17.988 19.987 1.00 34.35 o
ATOM 4994 OW HOH W 365 26.942 16.334 18.412 1.00 17.84 0
ATOM 4995 OW HOH W 366 32.619 20.051 22.407 1.00 36.74 o
ATOM 4996 OW HOH W 367 43.422 52.603 28.277 1.00 26.85 o
ATOM 4997 OW HOH W 368 10.356 35.546 25.854 1.00 24.50 0
ATOM 4998 OW HOH W 369 24.996 48.435 8.526 1.00 24.06 0
ATOM 4999 OW HOH W 370 63.758 59.971 30.779 1.00 32.31 O
ATOM 5000 OW HOH W 371 5.873 43.887 18.041 1.00 34.46 O
ATOM 5001 OW HOH W 372 21.479 35.760 -0.698 1.00 30.97 O
ATOM 5002 OW HOH W 373 27.204 35.741 3.472 1.00 37.90 O
ATOM 5003 OW HOH W 374 30.098 28.784 23.056 1.00 26.12 O
ATOM 5004 OW HOH W 375 31.042 35.444 29.071 1.00 31.24 O
ATOM 5005 OW HOH W 376 58.006 59.496 4.380 1.00 36.05 O
ATOM 5006 OW HOH W 377 35.433 25.073 8.913 1.00 29.78 O
ATOM 5007 OW HOH W 378 9.451 40.342 11.234 1.00 37.59 O
ATOM 5008 OW HOH W 379 64.159 24.469 20.081 1.00 24.97 O
ATOM 5009 OW HOH W 380 43.323 69.025 3.278 1.00 31.46 O
ATOM 5010 OW HOH W 381 45.906 22.389 22.179 1.00 26.51 O
ATOM 5011 OW HOH W 382 55.758 37.813 3.774 1.00 43.73 O
ATOM 5012 OW HOH W 383 27.095 -2.664 2.553 1.00 34.76 O
ATOM 5013 CL CL M 1 20.334 20.373 2.006 1.00 13.99 CL