Kinase crystal structures and materials and methods for kinase activation

FIELD OF THE INVENTION

[0001] The present invention relates to the enzyme protein kinase B (PKB/Akt), and in particular its crystal structure and the use of this structure in drug discovery.

BACKGROUND TO THE INVENTION

[0002] Protein kinase B (PKB/Akt) is a component of an intracellular signalling pathway of fundamental importance that functions to exert the effects of growth and survival factors, and which mediates the response to insulin and inflammatory signals (Datta et al., 1999; Brazil and Hemmings, 2001). The enzyme is rapidly activated by phosphorylation following stimulation of phosphoinositide 3-kinase, and generation of the lipid second messenger phosphatidylinositol 3,4,5 trisphosphate [PtdIns(3,4,5)P3]. Activation of PKB occurs by a multi-step mechanism. PKB is first recruited to the membrane by association with PtdIns(3,4,5)P3 mediated by its N-terminal pleckstrin homology domain in a process that also induces a conformational change of the protein. In this state, PKB is a substrate for phosphorylation at two regulatory sites by membrane-localised kinases (Meier et al. 1997). PDK1 phosphorylates PKB on a Thr residue (Thr-308 of PKBα, Thr-309 of PKBβ, Thr-305 of PKBγ) within the activation segment, stimulating its activity by 30-fold (Alessi et al., 1996; 1997). A distinct kinase activity, termed PDK2, phosphorylates PKB at a Ser residue of a C-terminal hydrophobic motif (Ser 473 of PKBα, Ser-474 of PKBβ, Ser-472 of PKBγ). Phosphorylation of Ser-474 promotes a 7-10-fold stimulation (Alessi et al., 1996), which is synergistic with pThr-309 so that phosphorylation of both sites results in an ˜300-fold elevation of protein kinase activity. Whereas PDK1 is well characterised, the identity of PDK2 (also designated Ser-473 Kinase) remains controversial.

[0003] Activated PKB phosphorylates numerous cytosolic and nuclear proteins to regulate cell metabolism, growth and survival. In the insulin signalling pathway, PKB phosphorylates GSK-3, PFK2 and mTOR, inducing glycogenesis and protein synthesis, and regulates glucose uptake by promoting the translocation of Glut4 to the plasma membrane. Cell survival and transformation are controlled by phosphorylation of BAD, caspase-9, forkhead transcription factors and IKB kinase, promoting proliferation and suppressing cell apoptosis (Datta et al., 1999). A mechanism by which PKB stimulates cell cycle progression is by phosphorylation of the CDK inhibitors p21WAFl and p27KiPl, causing their retention in the cytoplasm (Zhou et al., 2001), whereas in contrast, PKB mediates nuclear localisation of mdm2 and subsequent regulation of the mdm2/p53 pathway (Mayo and Donner, 2001). In humans, the three isoforms of PKB are highly conserved, with a mean sequence identity of 73%, and share the same regulatory phosphorylation sites. However, a splice variant of PKBγ lacks the C-terminal regulatory phosphorylation site, and interestingly, the specific activity of this splice variant, isolated from stimulated cells, is ˜10-fold lower than the full length γ isoform, a value which is consistent with the role of the C-terminal phosphorylation site to stimulate PKB activity (Brodbeck et al., 2001). CTMP is a negative regulator of PKBα, which by binding to the C-terminal region of the protein, suppresses phosphorylation of Thr-308 and Ser-473 (Maira et al., 2001).

[0004] PKB plays an important role in the generation of human malignancy. The enzyme is the cellular homologue of v-Akt, an oncogene of the transforming murine leukaemia virus AKT8 isolated from a mouse lymphoma (Staal et al., 1977). Viral-Akt is a fusion of the viral Gag protein with the PKBα sequence (Bellacosa et al., 1991). Myristoylation of the Gag sequence targets v-Akt to the cell membrane, resulting in its constitutive phosphorylation. The genes for the α and β isoforms of PKB are over-expressed and amplified in ovarian, prostate, pancreatic, gastric, and breast tumours (Testa and Bellacosa, 2001). Compelling evidence linking PKB to oncogenesis stems from the elucidation of the mechanism of the PTEN tumour suppressor gene. PTEN is one of the most commonly mutated genes in human cancer and somatic deletions or mutations of PTEN have been identified in glioblastomas, melanoma and prostate cancers, and are associated with increased susceptibility to breast and thyroid tumours (Cantley and Neel, 1999). PTEN negatively regulates the PI-3 kinase/PKB pathway by dephosphorylating PtdIns(3,4,5)P3 on the D-3 position, and therefore loss of PTEN activity leads to a constitutive cell survival stimulus (Maehama and Dixon., 1998; Myers et al., 1998).

[0005] Protein kinase B is a member of the AGC-family of serine/threonine specific protein kinases that also includes PKA, PKC, PDK1 and the p70 and p90 S6-kinases (Coffer and Woodgett, 1991; Jones et al., 1991a). As well as being structurally related, AGC-protein kinases share numerous functional similarities such as activation in response to second messengers and dependence on phosphorylation for activity. Members of the family are phosphorylated on a conserved Thr-residue within their activation segment. In vitro PDK1 is capable of phosphorylating AGC-kinases on this position (Vanhaesebroeck and Alessi, 2000), although recent studies using PDK1 deficient ES cells suggest that PDK1 activity is only necessary for PKB and a subset of other AGC-kinases (Williams et al., 2000). The site of C-terminal regulatory phosphorylation of PKB (Ser-474) is within a hydrophobic activation sequence motif (F-x-x-F-[S/T]-Y), conserved within a large proportion of AGC-kinases (Keranen et al., 1995; Pearson et al., 1995). In PKB, substitution of Ser-474 with Asp mimics Ser-474 phosphorylation (Alessi et al., 1996), and significantly, some atypical PKC isoforms and PRK2 (PKC related kinase-2) have Asp or Glu residues at this position. PKA requires phosphorylation of the activation segment Thr residue (Thr-197) for activity (Yonemoto et al., 1997), although this is a constitutive site of phosphorylation, and unlike other AGC-kinases, is resistant to dephosphorylation by protein phosphatases (Shoji et al., 1979). The hydrophobic motif of PKA is also unusual and comprises the sequence -Phe-Thr-Glu-Phe-350, with Phe-350 corresponding to the C-terminus of the PKA catalytic subunit, and therefore the enzyme lacks a site of regulatory phosphorylation. In the structure of PKA, the motif lies within a surface groove formed in the N-terminal lobe, with the side-chains of the two Phe-residues buried deep into the groove (Knighton et al., 1991a,b; Bossemeyer et al., 1993). Other AGC-kinases are likely to have an equivalent groove, and for PDK1, the groove is thought to allow recognition of specific target kinase substrates via their phosphorylated regulatory segment sequences, although this interaction has been suggested not to be essential for phosphorylation of PKB by PDK1 (Biondi et al., 2000; 2001).

[0006] In order to understand the mechanism of activation of PKB by phosphorylation, and as a framework for the rational development of modulators of PKB activity, knowledge of a PKB protein structure would be extremely valuable. Such knowledge would significantly assist the rational design of novel therapeutics for, e.g. the treatment of diabetes, cancer, neurodegeneration and erectile dysfunction, based on PKB modulators.

DEFINITIONS

[0007] In the following by “binding site” we mean a site (such as an atom, a functional group of an amino acid residue or a plurality of such atoms and/or groups) in a PKB binding cavity which may bind to an agent compound such as a candidate modulator (e.g. inhibitor). Depending on the particular molecule in the cavity, sites may exhibit attractive or repulsive binding interactions, brought about by charge, steric considerations and the like.

[0008] By “AGC kinase” is meant any protein kinase comprising a sequence which has a sequence identity of equal to or greater than 35% at the amino acid level with residues 37-350 of the catalytic subunit of PKA (Shoji et al., 1983). Determination of percentage sequence identity may be performed with the AMPS package as described by Barton (1994). AGC kinases are also described in detail by Hanks and Hunter, FASEB J. (1995) 9: 576, and Hardie, G. and Hanks, S. (eds) The Protein Kinase Facts Book—Protein Serine Kinases (1995) Academic Press Ltd., London).

[0009] By “fitting”, is meant determining by manual, automatic, or semi-automatic means, interactions between one or more atoms of an agent molecule and one or more atoms or binding sites of the PKB, and calculating the extent to which such interactions are stable. Various computer-based methods for fitting are described further herein.

[0010] By “root mean square deviation” we mean the square root of the arithmetic mean of the squares of the deviations from the mean.

[0011] By a “computer system” we mean the hardware means, software means and data storage means used to analyse atomic coordinate data. The minimum hardware means of the computer-based systems of the present invention comprises a central processing unit (CPU), input means, output means and data storage means. Desirably a monitor is provided to visualise structure data. The data storage means may be RAM or means for accessing computer readable media of the invention. Examples of such systems are microcomputer workstations available from Silicon Graphics Incorporated and Sun Microsystems running Unix based, Windows NT or IBM OS/2 operating systems.

[0012] By “computer readable media” we mean any media which can be read and accessed directly by a computer e.g. so that the media is suitable for use in the above-mentioned computer system. Such media include, but are not limited to: magnetic storage media such as floppy discs, hard disc storage medium and magnetic tape; optical storage media such as optical discs or CD-ROM; electrical storage media such as RAM and ROM; and hybrids of these categories such as magnetic/optical storage media.

DISCLOSURE OF THE INVENTION

[0013] The present invention is at least partly based on overcoming several technical hurdles: the present inventors have (i) produced PKBβ crystals of suitable quality for performing X-ray diffraction analyses, (ii) collected X-ray diffraction data from the crystals, (iii) determined the three-dimensional structure of PKBβ, and (iv) identified binding sites on the enzyme which are likely to be involved in the enzymatic reaction.

[0014] In order to understand the nature of the mechanism of regulation of PKB by PIP3, the N-terminal PH domain and phosphorylation of the regulatory Thr and Ser phosphorylation sites, the present inventors have determined the crystal structures of PKBβ and have generated Sf9/baculovirus expression systems for full length PKBα, PKBβ, PKBγ and PDK1 and also a number of modified forms of the three PKB isoforms.

[0015] Limited trypsinolysis of full length PKBβ purified from Sf9 cells led to the identification of a protease resistant domain with an N-terminus at Lys-146, which we refer to as ΔPH-PKB. Lys-146 is located within the structurally diverse region linking the pleckstrin homology (PH) and kinase domains of PKB, close to the N-terminus of the corresponding β1-strand of PKA. During the course of the purification, partial cleavage of a C-terminal 3 kDa fragment was observed, suggesting conformational flexibility at the C-terminus of the protein. Human PKBα, PKBβ and PKBγ sequences are structurally diverse within a 12 residue region C-terminal to the conserved PP(D/E) motif (residues 452-454 of PKBβ), preceding the C-terminal hydrophobic motif, and corresponding to the C-terminus of the PKBγ splice variant. Using this information, the present inventors constructed a number of new PKB baculovirus Fastbac entry vectors for the generation of PKB insect cell/baculovirus expression systems, and expressed the α and β-isoforms of PKB as the kinase domain, with an N-terminus at Lys-146 (i.e. lacking the PH domain), with and without the C-terminal 21 residues that includes the hydrophobic regulatory segment. These two kinase domains are termed ΔPH-PKB and ΔPH-PKB-ΔC, respectively.

[0016] Thus, using this limited proteolysis, the inventors have defined a stable, compact, crystallisable domain of PKB. The systems used express high levels of protein, that the inventors have purified to homogeneity. Moreover, the inventors have expressed PDK1 using the insect cell/baculovirus system and MAPKAPK2 in the E. coli expression system to enable phosphorylation of PKBβ on Thr309 and Ser474, respectively.

[0017] To prepare defined phosphorylated states of PKB, phosphorylation and dephosphorylation reactions were performed using PDK1 (for pThr-309) and the non-specific λ-protein phosphatase, respectively. Distinct phosphorylated states of the protein were resolved using hydrophobic interaction chromatography.

[0018] The phosphorylation state of the protein was analysed by Western blots using phospho-specific antibodies, and the stoichiometry and sites of phosphorylation were quantitatively assessed by mass spectroscopic analysis of trypsin-generated peptides of the protein.

[0019] The inventors have succeeded in the expression, purification, crystallisation and structure determination of three forms of PKBβ, that differ in their state of phosphorylation.

[0020] The three crystal forms of human PKBβ are; (i) pΔPH-PKB-ΔC (residues 146 to 460, phosphorylated in vitro on Thr-309), (ii) ΔPH-PKB-ΔC(residues 146 to 460, not phosphorylated on Thr-309), and (iii) ΔPH-PKBβ (residues 146 to 481, dephosphorylated in vitro)

[0021] Two batches of crystals were prepared for crystal form (i), i.e. pΔPH-PKB-ΔC. Sets of coordinate data, having different resolutions, are provided for each of these crystals. thus, data are provided for four crystals in total.

[0022] All four crystals of PKB belong to the same space group and have similar cell dimensions. Summary data for the higher resolution pΔPH-PKB-ΔC crystal, as well as the ΔPH-PKB-ΔC and ΔPH-PKB crystals are shown in Table 1.

[0023] The two crystal preparations of pΔPH-PKB-ΔC diffract to 2.8 and 2.3 Å resolution, when exposed to synchrotron radiation, whereas ΔPH-PKB-ΔC and ΔPH-PKB diffract to 2.7 Å and 2.5 Å respectively.

[0024] The structure of PKB was solved by means of molecular replacement using the ternary complex of mouse PKA (Knighton et al., 1991) as a search object. During initial stages of the refinement, the relative orientations of the N- and C-terminal lobes of the kinase domain were refined, prior to atomic positional refinement (Table 1).

[0025] The resultant structures are believed to provide important insights into the structure activity relationships in the full length PKBβ and its highly homologous isoforms (see Brodbeck et al. 1999). For brevity, as used herein, unless the context demands otherwise, the term PKB is used to encompass full or part-length molecules of any of the three isoforms, which may not or may be phosphorylated e.g. ‘PKBβ’ encompasses the full length PKBβ molecule or a truncated form such as ΔPH-PKBβ (residues 146-481) or ΔPH-PKBβ-ΔC (residues 146-460).

[0026] In general aspects, the present invention is concerned with identifying or obtaining agent compounds for modulating PKB 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.

[0027] Crystal structure information presented herein is useful in designing potential modulators and modelling them or their potential interaction with PKB binding cavities, for example, the PKB substrate binding cavity, ATP binding site, or other region of interest (e.g. the hydrophobic motif, or regulatory phosphorylation sites), preferably the ATP binding site. Potential modulators may be brought into contact with PKB to test for ability to interact with the PKB binding cavity. 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.

[0028] In a first aspect, the present invention provides a crystal of PKBβ having a tetragonal space group P41212, and unit cell dimensions of a=149.33 Å, b=149.33 Å, c=39.77 Å, or more generally a=149.33±0.5 Å, b=149.33±0.5 Å, c=39.77±0.5 Å, more preferably a=149.33±0.2 Å, b=149.33±0.2 Å, c=39.77±0.2 Å.

[0029] The present invention further provides a crystal of PKBβ having a tetragonal space group P41212, and unit cell dimensions of a=148.40 Å, b=148.40 Å, c=38.55 Å, or more generally a=148.40±0.5 Å, b=148.40±0.5 Å, c=38.55±0.5 Å, more preferably a=148.40±0.2 Å, b=148.40±0.2 Å, c=38.55±0.2 Å.

[0030] The present invention further provides a crystal of PKBβ having a tetragonal space group P41212, and unit cell dimensions of a=149.70 Å, b=149.70 Å, c=39.19 Å, or more generally a=149.70±0.5 Å, b=149.70±0.5 Å, c=39.19±0.5 Å, more preferably a=149.70±0.2 Å, b=149.70±0.2 Å, c=39.19±0.2 Å.

[0031] The present invention further provides a crystal of PKBβ having a tetragonal space group P41212, and unit cell dimensions of a=149.52 Å, b=149.52 Å, c=39.06 Å, or more generally a=149.52±0.5 Å, b=149.52±0.5 Å, c=39.06±0.5 Å, more preferably a=149.52±0.2 Å, b=149.52±0.2 Å, c=39.06±0.2 Å.

[0032] Alternatively, or additionally, the crystal may have the three dimensional atomic coordinates of Tables 2 to 5. An advantageous feature of the structural data according to Tables 2 to 5 are that they have a high resolution of from about 2.3 Å to 2.8 Å.

[0033] Indeed a further aspect of the invention includes within its scope a crystal of protein kinase Bβ (PKBβ) defined by structural data having a resolution of from about 2.3 Å to 2.8 Å, in particular 2.8 Å, 2.7 Å, 2.5 Å or 2.3 Å.

[0034] The coordinates of Tables 2 to 5 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 Å (preferably less than 1.0 Å and more preferably less than 0.5 Å) 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 Tables 2 to 5 in terms of both its structural characteristics and usefulness for structure-based analysis, including design of PKBβ modulators.

[0035] 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 Å (preferably less than 1.0 Å and more preferably less than 0.5 Å) when superimposed on the coordinates provided in Tables 2 to 5 for the residue backbone atoms. Reference herein to the coordinate data of Tables 2 to 5 thus includes the coordinate data in which one or more individual values of the Tables are varied in this way.

[0036] Modifications in the native PKBβ crystal structure due to e.g. mutations, additions, substitutions, and/or deletions of amino acid residues could lead to variations in the PKBβ atomic coordinates and where such modified forms of PKBβ are being investigated, atomic coordinate data of PKBβ modified so that a ligand that bound to one or more binding sites of PKBβ would be expected to bind to the corresponding binding sites of the modified PKBβ 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 Tables 2 to 5 thus includes the coordinates modified in this way. Preferably, the modified coordinate data define at least one PKBβ binding site.

[0037] In a further aspect, the invention provides a method for crystallizing a PKB derivative which comprises producing PKB by recombinant production in a host cell, recovering a PKB derivative from the host cell and growing one or more crystals from the recovered PKB derivative, wherein the PKB derivative is a stable protease-resistant form of PKB. The host cell may be of any suitable cell type, for example a eukaryotic cell host, such as a yeast cell, a mammalian cell, or an insect cell. In a preferred embodiment, the host cell is an insect cell, such as an Sf9 cell.

[0038] Typically the derivative lacks all or substantially all of the PH domain. Thus the derivative may be a truncated derivative e.g. truncated to positions 146-460 for PKBβ, or corresponding residues in other isoforms. The derivative may optionally include amino acid residues C-terminal of position 460 in PKBβ or its equivalent, e.g. the C-terminal 21 amino acids of PKBβ.

[0039] The method may further comprise the steps of phosphorylating one or more phosphorylatable residues in vitro with a suitable kinase. For example, PDK1 can be used to phosphorylate Thr-309 in vitro. It has been suggested that MAPKAP 2 kinase can be used to phosphorylate Ser-474 of PKBβ/Ser-473 of PKBα (Alessi et al. 1996).

[0040] Alternatively, the method may comprise the step of dephosphorylation in vitro, to ensure that any adventitious phosphorylation occurring during expression is removed. Numerous suitable enzymes will be known to the skilled person, e.g. the λ protein phosphatase.

[0041] The derivative may be encoded by a vector construct substantially similar to one disclosed herein. The method may include the further step of X-ray diffraction analysis of the obtained crystal.

[0042] Thus, the PKBβ produced by crystallising PKBβ (see the detailed description below) is provided as a crystallised protein suitable for X-ray diffraction analysis.

[0043] The crystal may be grown by any suitable method, e.g. the under oil batch method as described in the Examples.

[0044] The present invention further provides a recombinant polypeptide comprising the catalytic domain of PKB, the N-terminus of said polypeptide corresponding to Lys-146 of human PKBβ. The polypeptide will typically comprise the full kinase domain which may correspond, for example to amino acid residues 144 to 439 of human PKBα, 146 to 440 of human PKBβ, or 143 to 436 of human PKBγ.

[0045] In a preferred embodiment the polypeptide comprises amino acids 146 to 460 of human PKBβ, which corresponds to residues 145-459 of PKBα, and 143-456 of PKBγ. It may optionally further comprise the C-terminal region corresponding to amino acids 461 to 481 of human PKBβ or a portion thereof.

[0046] Reference to a PKB catalytic domain should be taken to include catalytic domains of mutant PKBs as described below (under ‘Homology Modelling’). 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.

[0047] The present invention further provides a crystallisable composition comprising a recombinant polypeptide as described above.

[0048] In a further aspect, the present invention provides nucleic acids encoding the polypeptides as described herein. Thus in these nucleic acids, the sequences encoding the catalytic domain are not contiguous with sequences encoding the PH domain of PKB, preferably not contiguous with sequences coding for any amino acids N-terminal of Lys-146.

[0049] The present invention also encompasses a method of making a polypeptide 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.

[0050] In another aspect, the invention provides a method of analysing a PKBβ-ligand complex comprising the step of employing (i) X-ray crystallographic diffraction data from the PKBβ-ligand complex and (ii) a three-dimensional structure of PKBβ to generate a difference Fourier electron density map of the complex, the three-dimensional structure being defined by atomic coordinate data according to Tables 2 to 5. If the PKBβ-ligand complex is crystallised in a different space group to the crystals described herein, molecular replacement methods may be used instead of difference Fourier methods.

[0051] Therefore, in the light of the present disclosure, PKBβ-ligand complexes can be crystallised and analysed using X-ray diffraction methods, e.g. according to the approach described by Greer et al., J. of Medicinal Chemistry, Vol. 37, (1994), 1035-1054, and difference Fourier electron density maps can be calculated based on X-ray diffraction patterns of soaked or co-crystallised PKBβ and the solved structure of un-complexed PKBβ. These maps can then be used to determine whether and where a particular ligand binds to PKBβ and/or changes the conformation of PKBβ.

[0052] Electron density maps can be calculated using programs such as those from the CCP4 computing package (Collaborative Computational Project 4. The CCP4 Suite: Programs for Protein Crystallography, Acta Crystallographica, D50, (1994), 760-763.). For map visualisation and model building programs such as O (Jones et al., Acta Crystallography, A47, (1991), 110-119) can be used.

[0053] In another aspect, the invention relates to methods of determining three dimensional structures of target kinases of unknown structure by utilising in whole or in part the structural coordinates provided for PKBβ in any one of the data sets provided herein (Tables 2 to 5).

[0054] The target kinase will typically be homologous to PKB, such as an AGC family kinase(e.g. SGK) (Hanks and Hunter (1995) FASEB J. 9: 576; Hardie, G. and Hanks, S. (eds) The Protein Kinase Facts Book—Protein Serine Kinases (1995) Academic Press Ltd., London). In particular, it may be an isoform of PKB, such as PKBα or PKBγ. The data provided here relate to the inactive conformation of PKBβ, and so will be useful for determining the structure of the corresponding conformation of other kinases. However, the present invention also extends to the elucidation of the structure of alternative conformations such as active conformations of such target kinases, including PKB, and including the active conformation of PKBβ, or PKB-ligand complexes.

[0055] There are three primary ways in which the three-dimensional coordinate data of the present invention can be used to solve other target kinase structures.

[0056] Firstly, the three-dimensional coordinate data provided herein for PKB 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.

[0057] Secondly, the three-dimensional coordinate data of the present invention may be used to align the amino acid sequence of PKB with a known three-dimensional structure of a template kinase, in order to establish a target PKB structure; for example a structure for an alternative PKB conformation, such as an active PKB conformation

[0058] Thirdly, 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.

[0059] Typically, in each of these alternatives, the target structure will be established by the calculation of a set of three-dimensional coordinate data for some or all of the atoms in the target structure.

[0060] Homology Modelling

[0061] Thus the invention provides a method of homology modelling comprising the steps of:

[0062] (a) aligning a representation of an amino acid sequence of a target kinase of unknown structure with the amino acid sequence of PKBβ to match homologous regions of the amino acid sequences;

[0063] (b) modelling the structure of the matched homologous regions of the target kinase on the structure as defined by Tables 2 to 5 of the corresponding regions of PKBβ; and

[0064] (c) determining a conformation (e.g. so that favourable interactions are formed within the target kinase and/or so that a low energy conformation is formed) for the target kinase which substantially preserves the structure of said matched homologous regions.

[0065] The target kinase will typically be a PKB homologue, such as a member of the AGC kinase family. In particular, such a method may be used to determine the structure of the α isoform, γ isoform, or other isoforms of PKB or of related kinases such as the AGC kinase family.

[0066] 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) side-chain chemical groups. Identical and similar residues in homologous regions are sometimes described as being,respectively “invariant” and “conserved” by those skilled in the art.

[0067] Preferably one or all of steps (a) to (c) are performed by computer modelling.

[0068] 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., Eur. J. Biochem, Vol. 172, (1988), 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 Tables 2 to 5.

[0069] The various in silico modelling techniques described in this section and in the other sections of this application may utilize coordinates from any of the four crystal data sets provided herein, or from any structure calculated by means of those data sets. To avoid unnecessary repetition, reference is made herein to the coordinate data of Tables 2 to 5.

[0070] “Homology modelling” extends to target kinases, in particular AGC kinases, which are analogues or homologues of the PKB protein whose structure has been determined in the accompanying examples. It also extends to mutants of PKB protein itself.

[0071] 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.

[0072] 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 modeled.

[0073] Analogues are defined as proteins with similar three-dimensional structures and/or functions and little evidence of a common ancestor at a sequence level.

[0074] 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.

[0075] A homologue is defined here as a protein with at least 15% sequence identity or which has at least one functional domain, which is characteristic of PKB. This includes polymorphic forms of PKB.

[0076] 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.

[0077] A mutant is a kinase characterized by replacement or deletion of at least one amino acid from a wild type AGC kinase, e.g. PKB. Such a mutant may be prepared for example by site-specific mutagenesis, or incorporation of natural or unnatural amino acids.

[0078] 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 ACG 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 wild-type 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 2.0 Å when superimposed with the atomic structure co-ordinates of the wild-type kinase from which the mutant is derived when at least about 50% to 100% of the Cαatoms of the kinase are included in the superposition. A mutant may have, but need not have, enzymatic or catalytic activity.

[0079] 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 α-helical or β-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, an MBP tag, and epitope tags.

[0080] 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.

[0081] 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.

[0082] 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.

[0083] 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.

[0084] 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.

[0085] The structures 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.

[0086] Determination of Alternative Conformations of PKB

[0087] The present invention further provides a method for determining three-dimensional atomic coordinate data for a target conformation of a PKB isoform, comprising the steps of:

[0088] (a) employing three-dimensional atomic coordinate data of Tables 2 to 5;

[0089] (b) employing three-dimensional atomic coordinate data of a template kinase structure, and:

[0090] (c) determining three-dimensional atomic coordinate data for said target conformation.

[0091] The template kinase will typically be a homologue of PKB, such as an AGC family kinase. For example, the structure of the ternary complex of mouse PKA in its active conformation is known (Knighton et al., 1991a, b), so these coordinates would be suitable for this purpose.

[0092] It may be possible to estimate a structure for the target conformation of PKB by the homology modelling procedures outlined above, with reference only to the amino acid sequence of PKB. However, the three-dimensional coordinate data provided in Tables 2 to 5 shows features which cannot be determined from the sequence alone, such as the conformations and orientations of the amino acid side chains in the inactive conformation of PKB. Thus use of the PKB structural data provided here will provide a far more accurate structure for the target conformation than could be obtained simply by use of sequence data.

[0093] This aspect of the invention is applicable to the determination of structures for PKB isoforms other than the β isoform, e.g the α and γ isoforms, and mutants thereof as described above, using e.g. the mouse PKA structure as a template.

[0094] Structure Solution

[0095] In a further aspect, the invention provides a method for determining the structure of a target kinase, which method comprises;

[0096] providing the co-ordinates of Tables 2 to 5, and positioning the co-ordinates in the crystal unit cell of said target kinase so as to provide a structure for said target kinase.

[0097] In a preferred aspect of this invention the co-ordinates are used to solve the structure of target kinases particularly homologues of PKB, such as AGC family kinases, including, without limitation, NDR, p70 S6K, p90, PKC, etc..

[0098] The structures of the human PKB provided can be used to solve the crystal structure of other target AGC kinases including other crystal forms of PKB, mutants, and co-complexes of PKB, where X-ray diffraction data of these target proteins has been generated and requires interpretation in order to provide the structure.

[0099] In the case of PKB, this protein may crystallize in more than one crystal form. The structure coordinates of PKB, or portions thereof, as provided by this invention are particularly useful to solve the structure of those other crystal forms of PKB, such as that of the active conformation. They may also be used to solve the structure of PKB mutants or co-complexes, or of the crystalline form of any other protein with significant amino acid sequence homology to any functional domain of PKB, such as an AGC kinase family member.

[0100] In the case of other target proteins, particularly the AGC kinases referred to above, the present invention allows the structures of such targets to be obtained more readily where raw X-ray diffraction data is generated.

[0101] Thus, where X-ray crystallographic or NMR spectroscopic data is provided for a target kinase of unknown three-dimensional structure, the structure of PKB as defined by Tables 2 to 5 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.

[0102] 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 PKB, a mutant or co-complex thereof, or the crystal of a target kinase with amino acid sequence homology to any functional domain of PKB, may be determined using any one of the data sets of PKB 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.

[0103] Examples of computer programs known in the art for performing molecular replacement are CNX (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, Calif.) or AMORE (Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Cryst. ASO, 157-163).

[0104] The invention may also be used to assign peaks of NMR spectra of such proteins, by manipulation of the data provided herein.

[0105] Computer Systems

[0106] In another aspect, the present invention provides systems, particularly a computer system, intended to generate structures and/or perform rational drug design for PKBβ, PKBβ-ligand complexes or PKBβ homologues or mutants, the system containing either (a) atomic coordinate data according to Tables 2 to 5 recorded thereon, said data defining the three-dimensional structure of PKB, or at least selected coordinates thereof; (b) structure factor data for PKB recorded thereon, the structure factor data being derivable from the atomic coordinate data of Tables 2 to 5; (c) a Fourier transform of atomic coordinate data according to Tables 2 to 5, 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 Tables 2 to 5; (e) atomic coordinate data of a target kinase generated by interpreting X-ray crystallographic data or NMR data by reference to the data of Tables 2 to 5; or (f) structure factor data derivable from the atomic coordinate data of (d) or (e).

[0107] The invention also provides such systems containing atomic coordinate data of target kinases wherein such data has been generated according to the methods of the invention described herein based on the starting data provided by Tables 2 to 5.

[0108] Such data is useful for a number of purposes, including the generation of structures to analyze 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.

[0109] In a further aspect, the present invention provides computer readable media with either (a) atomic coordinate data according to Tables 2 to 5 recorded thereon, said data defining the three-dimensional structure of PKB, or at least selected coordinates thereof; (b) structure factor data for PKB recorded thereon, the structure factor data being derivable from the atomic coordinate data of Tables 2 to 5; (c) a Fourier transform of atomic coordinate data according to Tables 2 to 5, 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 Tables 2 to 5; (e) atomic coordinate data of a target kinase generated by interpreting X-ray crystallographic data or NMR data by reference to the data of Tables 2 to 5; or (f) structure factor data derivable from the atomic coordinate data of (d) or (e).

[0110] By providing such computer readable media, the atomic coordinate data can be routinely accessed to model PKB 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.

[0111] 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.

[0112] Uses of the Structures of the Invention

[0113] In another aspect, the present invention provides methods for modelling the interactions between PKB and modulators of PKB activity. Thus there is provided a method for modelling the interaction between PKB and an agent compound which modulates PKB activity, comprising the steps of:

[0114] (a) employing three-dimensional atomic coordinate data according to any one of Tables 2 to 5 to characterise at least one PKBβ binding site;

[0115] (b) providing the structure of said agent compound; and

[0116] (c) fitting said agent compound to the binding site.

[0117] The agent compound may be any compound known to have an effect on PKB activity, such as the peptide activating agents, e.g. PIFtide, described below.

[0118] The present invention further provides a method for identifying an agent compound (e.g. an inhibitor) which modulates PKB (e.g. PKBβ) activity, comprising the steps of:

[0119] (a) employing three-dimensional atomic coordinate data according to Tables 2 to 5 to characterise at least one PKBβ binding site;

[0120] (b) providing the structure of a candidate agent compound;

[0121] (c) fitting the candidate agent compound to the binding sites; and

[0122] (d) selecting the candidate agent compound.

[0123] Preferably a plurality of binding sites are characterised; preferably sufficient binding sites are characterised to define a PKBβ binding cavity and/or the ATP binding site which forms part of the catalytic site.

[0124] For ease of reference, and to avoid unnecessary repetition, only the production of modulators of PKB 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 PKBβ provided herein. For example, the data provided herein may be used to calculate a structure for a related AGC family kinase, such as (without limitation) SGK, p70 S6K, p90 RSK, PKC, and NDR. Accordingly, the present invention extends to the use of such a structure for identification of modulators of that target enzyme.

[0125] As discussed above, the data provided herein may enable the calculation of a structure for an active conformation of a PKB enzyme, such as PKBβ. This may prove particularly useful, because the structures described herein show that in the inactive conformation of PKBβ, the adenine moiety of ATP is prevented from binding to the ATP binding site by Phe-294. 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 PKB residues involved in the interaction with ATP allows the development of specific and potent inhibitors of this kinase. This information may thus be used to develop potent and specific small molecule inhibitors of PKB in a number of ways. PKBβ may be co-crystallised, and/or existing PKBβ crystals may be soaked, for example with known inhibitors of PKB, such as staurosporine, or those discovered in high-throughput screening programmes known to the skilled person. Alternatively, or additionally, rational drug design programmes may make full use of the crystallographic coordinates. These techniques are discussed in more detail below.

[0126] However, it may equally be possible to use the data provided herein to identify a modulator which binds to the inactive conformation of PKB and so stabilises it, inhibiting the transition to the active conformation. By analogy, STI571 is an inhibitor which binds to the ATP binding site of Abl tyrosine kinase but stabilises the inactive conformation of the enzyme.

[0127] It may be desirable to compare the structures of the inactive and active conformations of the enzyme, in order to identify binding sites present on only one of said conformations. The three-dimensional coordinate data for such a site could then be used to identify a ligand capable of binding selectively to, and stabilising, that conformation.

[0128] A plurality (for example two, three or four) of spaced PKBβ binding sites may be characterised and a plurality of respective compounds designed or selected. The agent compound may then be formed by linking the respective compounds into a larger compound which maintains the relative positions and orientations of the respective compounds at the binding sites. The larger compound may be formed as a real molecule or by computer modelling.

[0129] In any event, the determination of the three-dimensional structure of PKBβ provides a basis for the identification of new and specific ligands for PKB e.g. PKBβ, and other members of the AGC family of kinases, e.g. NDR, p70 S6K, p90, PKC, etc., for instance by computer modelling.

[0130] More specifically, a potential modulator of PKB 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 PKB to ascertain how well the shape and the chemical structure of the candidate inhibitor will bind to the enzyme.

[0131] Also computer-assisted, manual examination of the binding cavity structure of PKBβ 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.

[0132] Computer programs can be employed to estimate the attraction, repulsion, and steric hindrance of the two binding partners (e.g. the PKBβ 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.

[0133] 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.

[0134] Having designed or selected possible binding partners, these can then be screened for activity. Consequently, the method preferably comprises the further steps of:

[0135] (e) obtaining or synthesising the candidate agent compound; and

[0136] (f) contacting the candidate agent compound with PKBβ to determine the ability of the candidate agent compound to interact with PKBβ (or similarly with other homologous isoforms or AGC kinase family members).

[0137] In step (f) the candidate agent compound may be contacted with PKBβ in the presence of a substrate, and typically a buffer, to determine the ability of the candidate agent compound to inhibit PKBβ. The buffer will typically contain ATP. The substrate may be e.g. a peptide corresponding to the sequence GRPRTTSFAE, or salts thereof. So, for example, an assay mixture for PKB may be produced which comprises the candidate inhibitor, substrate and buffer.

[0138] Instead of, or in addition to, performing e.g. a chemical assay, the method may comprise the further steps of:

[0139] (e) obtaining or synthesising the candidate agent compound;

[0140] (f) forming a complex of PKB and the candidate agent compound; and

[0141] (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 PKB.

[0142] Detailed structural information can then be obtained about the binding of the agent compound to PKB, 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, preferably co-crystallisation.

[0143] 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. Thus novel thymidylate synthase inhibitor series were designed de novo by Greer et al., and PKB inhibitors may also be designed in the this way. More specifically, using e.g. GRID on the solved 3D structure of PKBβ, a ligand (e.g. a potential inhibitor) for PKB may be designed that complements the functionalities of the PKB binding site(s). The ligand can then be synthesised, formed into a complex with PKB or other AGC family kinase, and the complex then analysed by X-ray crystallography to identify the actual position of the bound ligand. The structure and/or functional groups of the ligand can then be adjusted, if necessary, in view of the results of the X-ray analysis, and the synthesis and analysis sequence repeated until an optimised ligand is obtained. Related approaches to structure-based drug design are also discussed in Bohacek et al., Medicinal Research Reviews, Vol.16, (1996), 3-50.

[0144] As a result of the determination of the PKBβ 3D structure, more purely computational techniques for rational drug design may also be used to design PKB 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 PKB modulators.

[0145] 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 then 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), 839-848. The use of these approaches to design PKB inhibitors is made possible by the determination of the PKBβ structure.

[0146] Many of the techniques and approaches to structure-based drug design 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 PKBβ structure also allows difference Fourier electron density maps of PKBβ-ligand complexes to be produced, which can greatly assist the process of rational drug design.

[0147] 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 PKB). Sometimes these compounds are known e.g. from the research literature.

[0148] Thus the present invention provides methods of identifying mimetics of known modulators of PKB 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.

[0149] For example, the methods described above may be used to model the binding site at which PKB interacts with a known modulator, e.g. an activating agent such as PIFtide, as described elsewhere in this specification. A mimetic of the activating agent may then be designed by fitting candidate compounds to that binding site.

[0150] Thus the methods of the present invention for identifying agent compounds which modulate PKB activity may involve fitting a candidate agent compound to a PKB binding site, wherein the binding site has previously been determined to bind a known agent compound as described above.

[0151] 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 silico 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 PKBβ structure allows the architecture and chemical nature of each PKBβ 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.

[0152] In another aspect, the invention includes a compound which is identified as a modulator of PKB activity by the method of the earlier aspect.

[0153] Following identification of a suitable modulator compound, it may be manufactured and/or used in the preparation, i.e. manufacture or formulation, of 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 cancers, or activators in the use of diabetes, erectile dysfunction or neurodegeneration.

[0154] 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 such as cancer; a method comprising administration of such a composition to a patient, e.g. for treatment of disease such as cancer; use of such a modulator in the manufacture of a composition for administration, e.g. for treatment of disease such as cancer; 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.

[0155] Activation of AGC Kinases

[0156] The insights into the mechanism of kinase activation, which the crystal structure of PKB provides, enables the provision of novel methods for activating AGC kinases, and materials for use it hose methods.

[0157] The present invention further provides a method of inducing a catalytic domain of an AGC kinase to adopt an active conformation, wherein the AGC kinase in its native form is regulated by phosphorylation of a regulatory phosphorylation site residue in a C-terminal regulatory segment distinct from said catalytic domain, said method comprising the steps of:

[0158] (a) providing a polypeptide comprising said catalytic domain, and

[0159] (b) forming a non-covalent complex between said polypeptide and an activating agent, wherein contact between said activating agent and said catalytic domain induces said catalytic domain to adopt an active conformation.

[0160] The activating agent does not catalyse covalent modification of the polypeptide; in particular, the activating agent is not a kinase and does not phosphorylate the polypeptide. Rather the activating agent interacts with the catalytic domain to induce ordering of the regions of the kinase corresponding to the αB and αC helices and activation segment of PKB. Full activity may also require phosphorylation of a residue in the activation segment corresponding to Thr-309 of human PKBβ. This disorder to order transition forms a hydrophobic surface groove in the N-terminal lobe of the catalytic domain which binds the activating agent. The interaction is believed to be stabilised further by electrostatic interactions between residues of the catalytic domain and one or more negative charges of the activating agent.

[0161] The catalytic domain may be that of any AGC kinase which, in its native form, is regulated by phosphorylation of a regulatory phosphorylation site residue in a C-terminal regulatory segment distinct from the catalytic domain. Such phosphorylation typically activates the kinase. Such kinases include, but are not limited to, PKB, PKC, NDR, SGK, and the p70 and p90 S6-kinases and include variants of these kinases which do not possess the regulatory phosphorylation site, such as the splice variant of PKBγ (Brodbeck et al., 2001). However, they do not include kinases which are not regulated by phosphorylation of this sort, such as PKA, PRK2, and PDK1.

[0162] By “AGC kinase” is meant any protein kinase which has a sequence identity of equal to or greater than 35% at the amino acid level with residues 37-350 of the catalytic subunit of PKA (Shoji et al., 1983). Determination of percentage sequence identity may be performed with the AMPS package as described by Barton (1994). AGC kinases are also described in detail by Hanks and Hunter FASEB J. (1995) 9: 576 and Hardie, G. and Hanks, S. (eds) The Protein Kinase Facts Book—Protein-Serine Kinases (1995) Academic Press Ltd., London).

[0163] Thus the kinases which can be activated by the methods of the present invention possess a regulatory segment distinct from the catalytic domain, which in PKB constitutes the portion of the protein C-terminal of the catalytic domain. Thus the term ‘C-terminal regulatory segment’ signifies only that this portion of the polypeptide is located C-terminal of the catalytic domain, and does not imply that any portion of the regulatory segment need form the C-terminus of the polypeptide. In a preferred embodiment, the C-terminal regulatory segment corresponds to amino acid residues 440 to 480 of PKBα, 441 to 481 of PKBβ, 438 to 479 of PKBγ, or corresponding residues in other kinases.

[0164] The regulatory segment contains a hydrophobic motif at least four amino acids and typically six amino acid residues in length, which typically contains the sequence FXXF, e.g. FXXFXY/F, although the kinase NDR has the sequence FXXY at this position. Here, and throughout this specification, X represents any amino acid. The regulatory segment further comprises a regulatory phosphorylation site, which typically lies within the hydrophobic motif, e.g. Ser-473 of PKBα, Ser-474 of PKBβ, Ser 472 of PKBγ. For example, PKBα, β and γ all have the sequence FPQFSY within their regulatory segment.

[0165] The term ‘catalytic domain’ as used herein refers to a protein domain which when folded has a 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 site, but which does not affect the gross structure of the folded domain.

[0166] The minimum catalytic domain of a given kinase is the minimum polypeptide sequence from that kinase which will fold stably into the appropriate conformation when expressed independently, and may correspond, for example to amino acid residues 144 to 439 of human PKBα, 146 to 440 of human PKBβ, or 143 to 436 of human PKBγ (see FIG. 7—all references made herein to numbering of residues of PKBα or β refer to the human PKB sequences as shown in FIG. 7).

[0167] Catalytic domains of other target AGC kinases may be identified by alignment of the target sequences with that of PKBβ.

[0168] 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.

[0169] 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 those of target proteins.

[0170] The polypeptide may consist solely or essentially of the catalytic domain in isolated form, e.g. a recombinant single domain. Alternatively the polypeptide may contain further domains of the AGC kinase, fusion partners, epitope tags, etc. For example, the catalytic domain may be contiguous with all or part of one or more further domains found in the native wild-type form of the enzyme, such as a pleckstrin homology (PH) domain or the C-terminal regulatory segment of PKB.

[0171] In preferred embodiments, the catalytic domain is from an isoform of PKB, e.g. from the α, β or γ isoforms of PKB.

[0172] The catalytic domain may be provided in phosphorylated form, e.g. in the activation segment of the catalytic domain. For example, in a preferred embodiment the catalytic domain is from PKB and is provided phosphorylated at Thr-308 (PKBα), Thr-309 (PKBβ) or Thr-305 (PKBγ). In alternative embodiments where the catalytic domain is derived from another AGC kinase, it may be phosphorylated at the corresponding position.

[0173] The methods of the present invention may further comprise the steps of phosphorylating one or more phosphorylatable residues of the catalytic domain in vitro with a suitable kinase. For example, PDK1 can be used to phosphorylate Thr-309 in vitro, while it has been suggested that MAPKAP 2 kinase can be used to phosphorylate Ser-474 (Alessi et al., 1996).

[0174] Additionally or alternatively, the methods of the present invention may comprise the step of dephosphorylation in vitro, to ensure that any adventitious phosphorylation occurring during expression is removed. The skilled person will be aware of numerous suitable enzymes for this purpose, e.g. the λ protein phosphatase.

[0175] The activating agent may be a peptide. The peptide comprises an activation motif which is primarily responsible for mediating interaction with the catalytic domain. The activation motif may comprise a sequence derived from the native C-terminal regulatory segment of the same AGC kinase as the catalytic domain, or from the native C-terminal regulatory segment of a different AGC kinase, or may be a modified or mutated variant of either. Alternatively, the activation motif may be a synthetic sequence which does not occur naturally in an AGC kinase but which can activate the relevant catalytic domain in vitro, e.g. as described below.

[0176] The activation motif may comprise a hydrophobic motif. The hydrophobic motif is typically at least four amino acids in length, e.g. four, five or six amino acids in length, of which at least two amino acids, preferably at least three amino acids, are hydrophobic amino acids, preferably aromatic amino acids (e.g. phenylalanine, tyrosine). Preferably the hydrophobic motif comprises the sequence BXXB, where B represents an aromatic amino acid, e.g. tyrosine of phenylalanine and X is any amino acid. Thus in any sequence for an activating agent set out herein, it will be understood that phenylalanine can be replaced by tyrosine.

[0177] In a preferred embodiment, the hydrophobic motif comprises the sequence FXXF, YXXF, YXXY, FXXFX(Y/F), YXXFX(Y/F), or YXXYX(Y/F). In preferred embodiments, the hydrophobic motif comprises the sequence FXXFX(Y/F).

[0178] The activation motif preferably comprises an amino acid residue which carries a negative electrostatic charge at physiological pH. This amino acid may be located within, adjacent to or near (e.g. within one, two, three, four or five amino acids of) the hydrophobic motif, e.g. within the FXXF motif, or C-terminal of the FXXF motif, e.g. within one, two, three, four or five amino acids of the FXXF motif. The activation motif may comprise two such amino acids. In certain embodiments, one such amino acid may be located within the FXXF motif, and one may lie C terminal thereof, preferably one amino acid C-terminal thereof.

[0179] Preferably the activation motif comprises the sequence FXXFX′, FXXFX′(F/Y), FXX′FX′, or FXX′FX′(F/Y); YXXFX′, YXXFX′(F/Y), YXX′FX′, or YXX′FX′(F/Y); FXXYX′, FXXYX′(F/Y), FXX′YX′, or FXX′YX′(F/Y); YXXYX′, YXXYX′(F/Y), YXX′YX′, or YXX′YX′(F/Y); where X′ represents an amino acid residue which carries a negative charge at physiological pH. This may be a naturally ionisable acidic amino acid, such as aspartic acid or glutamic acid. Alternatively, X′ may be charged as a result of chemical derivatisation or enzymatic modification, e.g. it may be a phosphorylated amino acid residue, such as phosphoserine or phosphothreonine. Thus, particularly when X′ is phosphoserine or phosphothreonine, X′ may carry more than one negative charge at physiological pH.

[0180] In preferred embodiments, the activation motif comprises the sequence FXXFX′, FXXFX′(F/Y), FXX′FX′, or FXX′FX′(F/Y).

[0181] In preferred embodiments the activation motif is derived from the regulatory segment of PKB or PRK2. Preferably the activation motif comprises the sequence FPQFpSY (where pS is phosphoserine), FPQFDY or FRDFDY. For example, the activating agent may comprise the whole or part of one of the sequences GLLELDQRTHFPQFpSYSASIRE, GLLELDQRTHFPQFDYSASIRE and REPRILSEEEQEMFRDFDYIADWC (PIFtide—Biondi et al., 2000).

[0182] Activation of an AGC kinase according to the present invention may be performed in vivo or in vitro.

[0183] When performed in vitro, the methods of the present invention may be used, inter alia, to generate an active conformation of an AGC kinase catalytic domain for the purposes of structural analysis. Thus the present invention further provides a method of determining a structure for an active conformation of a catalytic domain of an AGC kinase, wherein the AGC kinase in its native form is regulated by phosphorylation of a regulatory phosphorylation site residue in a C-terminal regulatory segment, said method comprising the steps of inducing the catalytic domain of the AGC kinase to adopt an active conformation by any of the methods described herein.

[0184] The method may further comprise the step of obtaining a data set for said active conformation from which a structure can be calculated, and may additionally involve the step of calculating a structure therefor.

[0185] In preferred embodiments, especially where the active conformation is to be crystallised, a stable protease-resistant form of the catalytic domain is used, preferably in recombinant form. The catalytic domain may be a PKB catalytic domain, which may lack all or substantially all of the PH domain, e.g. corresponding to residues 1 to 139, 1 to 140, 1 to 141, 1 to 142, 1 to 143, 1 to 144, or 1 to 145 of human PKBβ, or their corresponding residues in other isoforms. In a preferred embodiment, the catalytic domain lacks residues corresponding to residues 1 to 145 of human PKBβ.

[0186] Additionally or alternatively the catalytic domain may be truncated at the C-terminus, e.g. lacking amino acid residues C-terminal of position 440 in PKBβ or its equivalent. In one embodiment, the catalytic domain lacks amino acid residues C-terminal of position 460 in PKBβ or its equivalent e.g. the C-terminal 21 amino acids of PKBβ. Thus it may be a truncated derivative of PKB, e.g. truncated to positions 146-460 for PKBβ, or corresponding residues in other isoforms.

[0187] The structure may be determined by any suitable method, e.g. X-ray crystallography or NMR. Thus the method may further comprise the step of crystallising the catalytic domain of the kinase in its active conformation.

[0188] The method may include the further step of X-ray diffraction analysis of the obtained crystal.

[0189] Alternatively, the methods of the present invention may be applied in assays for assessing the ability of a candidate agent to modulating the activity of an AGC kinase.

[0190] Thus the present invention further provides a method of assessing the ability of a candidate compound to modulate the catalytic activity of an AGC kinase, which in its native form is regulated by phosphorylation of a regulatory phosphorylation site residue in a C-terminal regulatory segment, comprising the steps of

[0191] (a) providing a polypeptide comprising a catalytic domain of said kinase,

[0192] (b) forming a non-covalent complex between said polypeptide and an activating agent, wherein contact between said activating agent and said catalytic domain induces said catalytic domain to adopt an active conformation, and

[0193] (c) contacting said non-covalent complex with said candidate agent.

[0194] The method may further comprise the step of measuring the effect of the candidate agent on the AGC kinase activity.

[0195] Preferably, the AGC kinase is phosphorylated at a position corresponding to Thr-309 of human PKBβ.

[0196] The methods may be used to identify modulators, such as inhibitors or activators of AGC kinases. Suitable methods for measuring the effect of candidate compounds on AGC kinase activity will be well known to the skilled person. For example, the activity of PKB can be assayed by monitoring phosphorylation of an appropriate substrate, e.g. the peptide Crosstide, as described in the Examples.

[0197] In a further aspect, the present invention provides a non-covalent complex between a catalytic domain of an AGC kinase, which in its native form is regulated by phosphorylation of a regulatory phosphorylation site residue in a C-terminal regulatory segment, and an activating agent, wherein said catalytic domain is in an active conformation, i.e. the regions of the catalytic domain corresponding to the αB and αC helices and activation segment of PKB are in an ordered conformation.

[0198] It will be clear from the above disclosure that a catalytic domain of an AGC kinase may also be induced to adopt an active conformation if covalently linked to an activating agent such as those described above.

[0199] Thus, the present invention also provides a method of inducing a catalytic domain of an AGC kinase to adopt an active conformation, wherein the AGC kinase in its native form is regulated by phosphorylation of a regulatory phosphorylation site residue in a C-terminal regulatory segment distinct from said catalytic domain, said method comprising the steps of:

[0200] (a) providing a polypeptide comprising said catalytic domain, and

[0201] (b) covalently joining said polypeptide to an activating agent, wherein contact between said activating agent and said catalytic domain induces said catalytic domain to adopt an active conformation.

[0202] Typically the polypeptide lacks some or all of a C-terminal regulatory domain prior to step (b). In preferred embodiments the polypeptide lacks the relevant regulatory phosphorylation site prior to step (b).

[0203] Preferably the activating agent is a peptide comprising an activation motif as described above, e.g. the peptide GLLELDQRTHFPQFDYSASIRE or REPRILSEEEQEMFRDFDYIADWC (PIFtide).

[0204] Ligation of a peptide to a polypeptide may be achieved by native chemical ligation, by protein splicing, or may be catalysed by a heterologous enzyme. Methods for carrying out such ligations are reviewed in Cotton, G. J. and Muir, T. W. (1999) Chemistry and Biology 6(9): R247-R256.

[0205] In preferred embodiments a phosphopeptide derived from the C-terminal regulatory segment of an AGC kinase is ligated to the catalytic domain. Preferably, the phosphopeptide is derived from the same AGC kinase as the catalytic domain. Thus this technique enables the active phosphorylated form of the enzyme to be mimicked without needing to phosphorylate the whole enzyme. This may be particularly useful where the kinase responsible for phosphorylation in vivo has not been conclusively identified.

[0206] In a preferred embodiment a polypeptide comprising a PKB catalytic domain is ligated to a peptide comprising the whole or part of the sequence GLLELDQRTHFPQFpSYSASIRE.

[0207] In a yet further aspect, the present invention provides a method of determining a structure for an active conformation of a catalytic domain of an AGC kinase, wherein the AGC kinase in its native form is regulated by phosphorylation of a regulatory phosphorylation site residue in a C-terminal regulatory segment distinct from said catalytic domain, said method comprising the steps of:

[0208] (a) providing a mutant AGC kinase protein comprising a catalytic domain and a C-terminal regulatory segment distinct from said catalytic domain, the protein further comprising a mutation which enhances the interaction between said regulatory segment and said catalytic domain relative to the wild type enzyme, such that an active conformation is induced in said catalytic domain, and

[0209] (b) obtaining a data set for said mutant protein from which a structure can be calculated.

[0210] The mutation enhances interaction between the regulatory segment (as described above) and the catalytic domain, such as to enable ordering of the regions of the kinase corresponding to the activation segment and αB and αC helices of PKB, without phosphorylation of a regulatory phosphorylation site in the C-terminal regulatory segment. The mutation may comprise one or more amino acid insertions, deletions or substitutions in the C-terminal regulatory segment, preferably in or around the hydrophobic motif, or in the catalytic domain, or in both C-terminal and catalytic domains. Alternatively, the mutation may involve the insertion or substitution of a number of contiguous residues of the C-terminal regulatory segment, e.g. with the corresponding residues from a second AGC kinase. Such a mutant AGC kinase may be considered to be a chimeric kinase.

[0211] Preferably, the C-terminal regulatory segment is mutated so that its interaction with the wild-type catalytic domain is enhanced. Preferably the mutation is made in or around the hydrohobic motif of the C-terminal regulatory segment, i.e. the region corresponding to the sequence FPQFSY of PKBβ (amino acid residues 470-475). The mutation may comprise substitution, deletion or insertion of one or more amino acids, e.g. 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, or 20 amino acids. In preferred embodiments the regulatory phosphorylation site is mutated.

[0212] In preferred embodiments, the mutation comprises the introduction into the C-terminal regulatory segment of a residue which carries an electrostatic charge at physiological pH, preferably a negative electrostatic charge, e.g. aspartic acid or glutamic acid.

[0213] In a preferred embodiment the amino acid residue which would be phosphorylated to activate the wild-type enzyme (e.g. the residue corresponding to Ser-474 of PKBβ) is mutated to a residue which carries a negative electrostatic charge at physiological pH, e.g. aspartic acid or glutamic acid. For example, where the AGC kinase is PKBβ, the mutation may involve alteration of the sequence FPQFSY to FPQFDY.

[0214] In other embodiments, the mutation may involve the substitution of a number of contiguous residues of the C-terminal regulatory segment, e.g. with the corresponding residues from a second AGC kinase. Thus the sequence FPQFSY of PKBβ may be replaced by the sequence FRDFDY from PRK2. The chimera may contain further sequences from the second kinase, e.g. one or more of the flanking residues in the sequence GLLELDQRTHFPQFDYSASIRE from PKBβ may be replaced by one or more corresponding residues of the sequence REPRILSEEEQEMFRDFDYIADWC from PRK2 (PIFtide).

[0215] Additionally or alternatively, the catalytic domain may be mutated to enhance its interaction with the wild-type C-terminal regulatory segment, or with a mutated C-terminal regulatory segment. Thus the catalytic domain may be mutated in or around the binding groove which interacts with the C terminal regulatory segment. For example, polar or charged residues (e.g. serine, threonine, aspartic acid, glutamic acid, lysine, etc.) may be mutated to more hydrophobic residues (e.g. phenylalanine, tyrosine, etc.), or hydrophobic residues replaced by more hydrophobic or larger hydrophobic residues, in order to enhance the interaction between the catalytic domain and the hydrophobic motif of the regulatory segment.

[0216] Possible target residues include V194 and V198 of PKBβ. These may, for example, be replaced by the corresponding residues of the hydrophobic groove from PKA. This is capable of binding the regulatory segment of PKA without phosphorylation, which implies that the hydrophobic interactions involved are stronger than are seen in PKB. Thus possible substitutions include V194I and V198L.

[0217] Additionally or alternatively, substitutions may be made which enhance the binding of the catalytic domain to a negative charge of the regulatory segment, e.g. incorporating further positive charges. A possible target residue is S201; therefore a possible substitution is S201K.

[0218] Alternatively, both catalytic domain and C-terminal regulatory segment may be mutated in order to enhance the affinity between them. Mutants may be prepared for example, by site-specific mutagenesis, or incorporation of natural or unnatural amino acids.

[0219] In preferred embodiments, especially where the mutant AGC kinase is to be crystallised, a stable protease-resistant form of the catalytic domain truncated at the N-terminus is used. The kinase may lack some or all of the wild-type residues upstream of the catalytic domain, e.g. corresponding to all or substantially all of the PH domain of PKB, e.g. corresponding to residues 1 to 139, 1 to 140, 1 to 141, 1 to 142, 1 to 143, 1 to 144, 1 to 145, 1 to 146, 1 to 147, 1 to 148, 1 to 149 or 1 to 150 of human PKBβ, or their corresponding residues in other isoforms. In a preferred embodiment the kinase lacks residues corresponding to residues 1 to 145 of PKBβ.

[0220] In a further aspect, the present invention provides a mutant AGC kinase protein, wherein the AGC kinase in its native form is regulated by phosphorylation of a regulatory phosphorylation site residue in a C-terminal regulatory segment, said mutant AGC kinase protein comprising a catalytic domain and a C-terminal regulatory segment distinct from said catalytic domain, and having an N-terminus corresponding to residue 139, 140, 141, 142, 143, 144, 145, 146, 147, 148, 149 or 150 of PKBβ, or their corresponding residues in other isoforms, the mutant AGC kinase protein comprising a mutation which enhances the interaction between said regulatory segment and said catalytic domain relative to the wild type enzyme, such that an active conformation is induced in said catalytic domain.

[0221] The mutation enhances interaction between the regulatory segment and the catalytic domain, such as to enable ordering of the regions of the kinase corresponding to the activation segment and αB and αC helices of PKB, without phosphorylation of the regulatory segment, and may have any of the characteristics described above.

[0222] In a preferred embodiment the kinase has an N-terminus corresponding to residue 146 of PKBβ.

[0223] In a further aspect, the present invention provides nucleic acids encoding the mutant AGC kinase polypeptides as described herein.

[0224] 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.

[0225] 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.

[0226] 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.

[0227] 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 of the sequences shown, e.g. 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 40, 50 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.

[0228] 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.

[0229] ‘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).

[0230] 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 appropriate. For further details see, for example, Molecular Cloning: a Laboratory Manual: 2nd edition, Sambrook et al, 1989, Cold Spring Harbor Laboratory Press or Current Protocols in Molecular Biology, Second Edition, Ausubel et al. eds., John Wiley & Sons, 1992.

[0231] Specifically included are shuttle vectors by which is meant 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).

[0232] 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.

[0233] 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 or 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

[0234] 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).

[0235] “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.

[0236] In a preferred embodiment, the promoter is an inducible proimoter 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.

[0237] 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.

[0238] Preferably the vector is capable of providing expression in an insect cell, such as an Sf9 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.

[0239] 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 vitro systems, such as reticulocyte lysates, as will be appreciated by the skilled person.

[0240] Systems for cloning and expression of a polypeptide in a variety of different host cells are well known. Suitable host cells include bacteria, eukaryotic cells such as mammalian and yeast, and baculovirus-based insect expression systems. Mammalian cell lines available in the art for expression of a heterologous polypeptide include Chinese hamster ovary cells, HeLa cells, baby hamster kidney cells, COS cells and many others.

[0241] Although certain specific amino acid sequences are referred to herein, e.g. in the context of peptides capable of activating AGC 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 β-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.

[0242] 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 disrupting the three-dimensional structure of the molecule. In highly conserved regions, or regions containing significant secondary structure, conservative amino acid substitutions are preferred.

[0243] 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.

[0244] 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.

[0245] Particular embodiments of the invention will now be described, by way of example only, with reference to the accompanying drawings.

BRIEF DESCRIPTION OF THE DRAWINGS

[0246]
FIG. 1 shows a comparison of PKB and PKA structures, with ribbon representations of PKA (A) and PKB (B). PKA and PKB were superimposed onto their C-terminal lobes. Phe 294 of the DFG motif of PKB occupies a site equivalent to the adenine pocket of the nucleotide binding site of PKA. (C) Stereo view of a superimposition of PKA and PKB to show different relative orientations of their N- and C-terminal lobes. Conformational differences in C-lobe are localised to the activation segment and αF/αG loop. Figure drawn using BOBSCRIPT (Esnouf, 1997) and RASTER3D (Merit and Murphy, 1994)

[0247]
FIG. 2 shows the structure of the N-terminal Lobe:

[0248] (A) Flexibility of αB- and αC-helices. 2Fo-Fc electron density map contoured at 1σ of a portion of the N-terminal lobe of pΔPH-PKB-ΔC (β3, β4, β5-strands, βB- and βC-helices). Electron density for the β-sheet is well resolved, whereas the αB- and αC-helices are disordered. The main-chain of the N-terminal lobe and hydrophobic motif of PKA is shown superimposed onto PKB.

[0249] (B and C) Role of hydrophobic motif to order the αB- and αC-helices and link to activation segment. (B) Interactions of hydrophobic motif of PKA with the β3, β, β5-strands and αB- and αC-helices of the N-terminal lobe. Phe 347 and Phe 350 are buried by hydrophobic residues. Glu 349 and C-terminal carboxylate form hydrogen bonds with basic residues of the αC-helix. (C) Disorder of the αB- and αC-helices of PKB is correlated with absence of bound hydrophobic motif. In (B) bracketed residues corresponds to PKB numbering.

[0250]
FIG. 3. Role of αC-helix to regulate conformation of PKA and PKB and structure of activation segment and DFG motif. (A) αC-helix stabilises an active state of PKA by interaction with pThr 197 of the activation segment via His 87, and Phe 185 of the DFG motif via Ile 93 and Leu 94. (B) In PKB, disorder of the αC-helix prevents His 196 from interacting with pThr 309. Loss of interactions with Phe 294 of the DFG motif binds within the nucleotide-binding site of ATP.

[0251]
FIG. 4 shows a multiple sequence alignment of the catalytic domains and C-terminal regulatory segments of various AGC-family protein kinases. Invariant residues are shown with dark shading and conserved residues with light shading. The position of critical functional residues are indicated with a dark arrow and numbered according to PKA residues. PKB Thr 309 and Ser 474 phosphorylation sites are indicated. The conserved AGC-kinase hydrophobic motif is shown and mutated residues of PKB that influence PIFtide activation (FIG. 7B) are indicated by light arrows. Figure drawn using ALSCRIPT (Barton, 1993).

[0252]
FIG. 5 illustrates the activation of PKB by hydrophobic motif peptides and complex formation between PKB and PIFtide.

[0253] (A) Dose response curve for the activation of ΔPH-PKB-ΔC by various synthetic 23 residue peptides derived from the PKB regulatory segment. &Circlesolid;: PKB HM-P has a phosphoserine residue at position 474; ▴: PKB HM-D has aspartate at position 474; ∘: has an unphosphorylated serine residue at position 474 and so corresponds to the wild type sequence.

[0254] (B) Dose response curve for the activation of (p) ΔPH-PKB-ΔC by PIFtide a synthetic 24 residue peptide encompassing the PRK2 HM motif. &Circlesolid;: PIFtide and pΔPH-PKB-ΔC, ▴: PIFtide and ΔPH-PKB-ΔC, ∘: mutant PIFtide (D>A) and pΔPH-PKB-ΔC. PIFtide can bind to ΔPH-PKB-ΔC but cannot activate it in the absence of Thr-309 phosphorylation.

[0255] (C) Isothermal titration calorimetry measurements of the binding of PIFtide to pΔPH-PKB-ΔC (left) and ΔPH-PKB-ΔC (right). Upper panel, raw data of the titration of PIFtide into pΔPH-PKB-ΔC. Lower panel, integrated heats of injections, corrected for the heat of dilution, with the solid line corresponding to the best fit of the data using the MicroCal software.

[0256]
FIG. 6 shows that conserved residues of the hydrophobic motif, and residues of the N-lobe of PKB, are required for PIFtide and PKB HM-peptide mediated stimulation of PKB kinase activity. Mutations of conserved hydrophobic motif residues of PIFtide and PKB HM-peptide reduce or eliminate their potential to activate ΔPH-PKB-ΔC phosphorylated on Thr 309. Mutations of hydrophobic and electrostatic residues of the ΔPH-PKB-ΔC N-lobe hydrophobic groove reduces the stimulation of PKB activity by 130 μM PIFtide. The position of mutated residues on PKA and PKB (R202D, V194A-V198A and L225A) are shown in FIG. 4.

[0257]
FIG. 7 is a comparison of the amino acid sequences of human PKBα, PKBβ and PKBγ. The PH and catalytic domains are shown boxed, and are connected by the linker domain. The GXXGXG ATP binding site, the catalytic lysine residue, and the regulatory phosphorylation sites are shown in bold type.

DETAILED DESCRIPTION OF THE INVENTION

[0258] Limited trypsinolysis of full length PKBβ purified from Sf9 cells led the present inventors to the identification of a protease resistant domain with an N-terminus at Lys-146, referred to as ΔPH-PKB. Lys-146 is located within the structurally diverse region linking the pleckstrin homology (PH) and kinase domains of PKB, close to the N-terminus of the corresponding β1-strand of PKA. During the course of the purification, partial cleavage of a C-terminal 3 kDa fragment was observed, suggesting conformational flexibility at the C-terminus of the protein. Human PKBα, PKBβ and PKBγ sequences are structurally diverse within a 12 residue region C-terminal to the conserved PP(D/E) motif (residues 452-454 of PKBβ), preceding the C-terminal hydrophobic motif, and corresponding to the C-terminus of the PKBβ splice variant.

[0259] Using this information, the present inventors constructed a number of new PKB baculovirus Fastbac entry vectors for the generation of PKB insect cell/baculovirus expression systems, and expressed the β and γ-isoforms of PKB as the kinase domain, with an N-terminus at Lys-146 (i.e. lacking the PH domain), with and without the C-terminal 21 residues that includes the hydrophobic regulatory segment. These two kinase domains are termed ΔPH-PKB and ΔPKB-ΔC, respectively.

[0260] These expression systems express high levels of protein, which have been purified to homogeneity. Moreover, PDK1 has been expressed using the insect cell/baculovirus system and MAPKAPK2 in the E. coli expression system to enable phosphorylation of PKBβ on Thr309 and Ser474, respectively.

[0261] To prepare defined phosphorylated states of PKB, phosphorylation and dephosphorylation reactions were performed using PDK1 (for pThr-309) and the non-specific λ-protein phosphatase, respectively. Distinct phosphorylated states of the protein were resolved using hydrophobic interaction chromatography.

[0262] The phosphorylation state of the protein was analysed by Western blots using phospho-specific antibodies, and the stoichiometry and sites of phosphorylation were quantitatively assessed by mass spectroscopic analysis of trypsin-generated peptides of the protein.

[0263] Crystals were successfully obtained for the PKBβ derivatives, and structures determined for ΔPH-PKBβ-ΔC, pΔPH-PKBβ-ΔC and ΔPH-PKBβ by X-ray crystallographic techniques. High resolution structures were obtained, apparently showing the catalytic domain of PKBβ in the inactive conformation.

[0264] The phosphorylation state of the protein was analysed by Western blots using phospho-specific antibodies, and the stoichiometry and sites of phosphorylation were quantitatively assessed by mass spectroscopic analysis of trypsin-generated peptides of the protein. The three crystal forms of human PKBβ are; (i) pΔPH-PKB-ΔC, phosphorylated in vitro on Thr-309, (ii) ΔPH-PKB-ΔC, not phosphorylated on Thr-309, and (iii) ΔPH-PKB-β, dephosphorylated in vitro.

[0265] Two different batches of crystals, having different resolution, were produced for crystal form (i), i.e. pΔPH-PKB-ΔC.

RESULTS

[0266] Each of the crystals belonged to the tetragonal space group P41212, and accommodated one molecule of PKB per asymmetric unit with cell parameters as follows:

[0267] pΔPH-PKB-ΔC (first batch): a=149.33 Å, b=149.33 Å, c=39.77 Å;

[0268] pΔPH-PKB-ΔC (second batch): a=148.40 Å, b=148.40 Å, c=38.55 Å;

[0269] ΔPH-PKB-ΔC: a=149.70 Å, b=149.70 Å, c=39.19 Å;

[0270] ΔPH-PKB: a=149.52 Å, b=149.52 Å, c=39.06.

[0271] Resolution was determined to be 2.8 Å for the first batch and 2.3 Å for the second batch of pΔPH-PKB-ΔC crystals, 2.7 Å for ΔPH-PKB-ΔC and 2.5 Å for ΔPH-PKB.

[0272] The current refined R-factor:

[0273] (Σ|F0−Fc|/Σ|F0|, where F0=observed amplitude, and Fc=calculated amplitude) is as follows:

[0274] pΔPH-PKBβ-ΔC (second batch): 0.237 to 2.3 Å resolution.

[0275] ΔPH-PKBβ-ΔC: 0.238 to 2.7 Å resolution.

[0276] ΔPH-PKBβ: 0.254 to 2.5 Å resolution.

[0277] More detailed information about the data collection and refinement statistics are provided for all crystals except the first batch of pΔPH-PKB-ΔC is provided in Table 1 below.

1TABLE 1Crystallographic Data Collection and Refinement StatisticsProteinpΔPH-PKBβ-ΔCΔPH-PKBβ-ΔCΔPH-PKBβAmino acid residues146-460146-460146-481PhosphorylationThr-309——Space group (Z)P41212 (1)P41212 (1)P41212 (1)Cell parameters a148.40149.70149.52(Å)c (Å)38.5539.1939.06X-ray sourceID14eh4 ESRFID14eh4 ESRFID14eh4 ESRFResolution (Å)2.32.72.5Observations (N)113 67750 87592 809Unique (N)18 90512 14716 090Completeness (%)96.194.299.7aRsym0.050 (0.243)0.065 (0.236)0.057(0.255)I/σI21.018.014.8RefinementResolution range35-2.335-2.7535-2.6(Å)Reflections used (N)17 57610 32014 317Rfree set (N) (%)1398 (7.1)1199 (9.9)1598 (10.0)bRcryst/Rfree0.237/0.3090.238/0.300.254/0.314Protein atoms (N)2 1982 1982198Solvent atoms (N)15427125r.m.s.d. bond angles1.541.571.53(°)r.m.s.d. bond0.01050.01120.0104lengths (Å)

[0278] Values in parentheses are for the highest shell aRsym=ΣhΣj|<I(h)>-I (h)j|/ΣhΣj<I(h)>, where <I(h)> is the mean intensity of symmetry-equivalent reflections.

[0279]

b
Rcryst/free=Σ||Fobs|−|Fcalc||/Σ|Fobs|, where Fobs and Fcalc are the observed and calculated structure factors, respectively.

[0280] Root-mean-square deviations relate to the Engh and Huber parameters.

[0281] Coordinate data for the four crystals is provided at the end of this specification as follows:

[0282] Table 2: pΔPH-PKBβ-ΔC (first batch)

[0283] Table 3: pΔPH-PKBβ-ΔC (second batch)

[0284] Table 4: ΔPH-PKBβ-ΔC

[0285] Table 5: ΔPH-PKBβ

[0286] Overall Description of the Structure and Comparison with PKA

[0287] The structure of pΔPH-PKB-ΔC is essentially identical to those of ΔPH-PKB-ΔC and ΔPH-PKB (rms deviations of 0.3 Å and 0.4 Å, respectively), and this similarity to inactive forms of PKB, together with features of the structure, indicates that the crystallisation conditions favoured the inactive conformation of pΔPH-PKB-ΔC. Because of the higher resolution of the pΔPH-PKB-ΔC crystal structure, most of the discussion is focussed on this form.

[0288] The structure of pΔPH-PKBβ-ΔC (residues 146-460) resembles the catalytic domain of other protein kinases (reviewed by Johnson et al., 1996). In particular, it resembles that of the catalytic subunit of PKA (FIG. 1). The PKB molecule is organised into an N-terminal and C-terminal lobe, with the N-terminal lobe (residues 146-233) formed from a 5-membered β-sheet and flanking α-helix, αA (equivalent to αC of PKA). The C-terminal lobe (residues 234-450) is predominantly α-helical and is joined to the N-terminal lobe via a single polypeptide chain connection.

[0289] The catalytic site of PKB is situated at the interface of the N and C-terminal lobes and is formed from residues of the catalytic loop (residues 274-282), and the activation segment (residues 304-312) of the C-terminal lobe, together with the ATP binding site and the αA helix of the N-terminal lobe. The ATP binding site consists of a hydrophobic pocket formed by residues (Val158, Val166) that interact with the adenine ring of the nucleotide, and a more hydrophilic region that interacts with the ribose ring and phosphate groups. By analogy with other protein kinases (Hubbard, 1997), the activation segment provides the binding site for the peptide substrate, orientating the substrate amino acid towards the phosphates of the ATP.

[0290] The catalytic mechanism of all protein kinases is similar and involves a phosphoryl transfer reaction from the γ-phosphate group of the ATP onto the hydroxyl group of the substrate amino acid residue. The reaction commences with the nucleophilic attack by the hydroxyl group of the substrate amino acid residues onto the γ-phosphate of ATP. A catalytic base in PKBβ, Asp265, facilitates this attack by increasing the nucleophilicity of the substrate hydroxyl group. The phosphate moieties of ATP are coordinated by the glycine rich loop and Lys181 of the N-terminal lobe and by a Mg2+ ion that interacts with Asp293 of the protein kinase C-terminal lobe.

[0291] PKA and PKB share essentially the same secondary structure topology, except that in PKB there is no counterpart to the αA-helix of PKA, and some of the structural elements of PKB are disordered. The architecture of PKA consists of an N-terminal lobe based on a 5-stranded β-sheet, with two α-helices (the αB- and αC-helices), and a larger, mainly α-helical C-terminal lobe, containing the activation segment. The catalytic site for ATP is located at the interface of the two lobes, whereas the substrate peptide-binding site is within the C-lobe, centred on the activation segment.

[0292] The inactive state of PKB differs in structure from the catalytically active form of PKA in a number of respects that are important for the regulation of PKB by multi-site phosphorylation. These differences involve the overall juxtaposition of the N- and C-lobes of the kinase, and structural disorder of the αB- and αC-helices of the N-lobe, activation segment of the C-lobe, and C-terminal regulatory segment. When superimposed, equivalent Cα-atoms of PKB and the ternary complex of PKA differ by an rms deviation of 2.3 Å (FIG. 1C). This deviation is larger than the expected value of 1.2 Å for a pair of proteins with 43% sequence identity (Cothia and Lesk, 1986), and results from differences in the relative orientations of the N- and C-terminal lobes of PKA and PKB. When superimposed individually, differences in conformation between the equivalent N- and C-lobes of PKA and PKB are seen to be localised to the β1-strand and αC-helix in the N-lobe, and DFG motif and αF/αG loop in the C-lobe.

[0293] PKA adopts open and closed conformational states resulting from relative rotations of the N- and C-lobes that are associated with various substrate-PKA complexes, with the ternary-PKA complex adopting a closed state, and the apo and binary complexes being more open. However, the relative position of the N- and C-lobes of PKB, do not resemble any of the various PKA-ligand complexes. Compared with the PKA-ternary complex, the N-lobe of PKB is rotated by 20° relative to its C-lobe, causing catalytic site residues from the two lobes to be misaligned.

[0294] Comparison of a number of activated protein kinase structures indicates that their N- and C-terminal lobes adopt similar relative configurations. For example, the Cα-Cα distance of two residues (Val-57 and Leu-173) that span the nucleotide-binding site in the PKA ternary complex is 12.9 Å, the same as that between equivalent residues of the phosphorylated insulin receptor kinase (Hubbard, 1997). In contrast, for PKB this distance is 15.2 Å.

[0295] Structural Disorder in PKB

[0296] In addition to variations in their overall bilobal configuration, the structures of PKB and PKA differ in other respects that are significant for the reduced catalytic activity of unphosphorylated and mono-phosphorylated forms of PKB. In the inactive PKB structures, three inter-related regions of the polypeptide chain are disordered; (i) the αB- and αC-helices of the N-terminal lobe, (ii) the activation segment between the invariant DFG and APE motifs, and (iii) the C-terminal regulatory segment in ΔPH-PKB. Concerted disorder to order transitions of these regions, linked to a conformational change of the activation segment DFG motif, and reorganisation of the N- and C-lobes, are required to generate a catalytically active protein kinase on phosphorylation of Thr-309 and Ser-474.

[0297] Although the structures of the three disordered regions are interdependent, each region is described in turn, before discussing the biological implications that these regions are disordered. This analysis is greatly assisted by the ability to compare the structural differences between an inactive PKB molecule with that of the related active PKA catalytic subunit, the latter serving as a model for an active phosphorylated form of PKB.

[0298] Flexibility of the αB- and αC-helices

[0299] Within the N-terminal lobe of PKB, the β-sheet is well ordered, however, residues Ala-189 to Thr-207, equivalent to the αB-helix and the majority of the αC-helix of PKA, are highly mobile, as judged by disorder in the weighted 2Fo-Fc electron density, and composite simulated annealing omit maps, and analysis of the atomic temperature-factors (FIG. 2A). Specifically, for all crystal forms, there is no visible electron density to account for residues Ala-189 to Thr-197, whose counterparts in PKA form the C-terminus and N-terminus of the αB- and αC-helices, respectively.

[0300] Electron density corresponding to the main-chain of the remaining residues of the αC-helix is fragmented, and the side-chains of these residues are disordered. The short αB-helix, which connects the αC-helix with the central β3-strand of the β-sheet, is unique to the AGC-protein kinases, and causes the N-terminus of the αC-helix to be displaced from the β4/β5-strands of the β-sheet (FIG. 1, 2). As a consequence, the αC-helix packs less tightly against the hydrophobic side-chains of the β-sheet, compared with other protein kinases, and, significantly a deep surface groove is created at the interface between the αB/αC-helices and β-sheet. In PKA this groove permits interactions between the N-terminal lobe and C-terminal hydrophobic motif.

[0301] The importance of the conserved αC-helix for both catalytic and regulatory functions has been demonstrated for many protein kinases. An invariant glutamate residue located near the N-terminus of the helix, (Glu-91 of PKA, Glu-200 of PKB), is responsible for its catalytic function by forming a hydrogen bond with an invariant lysine side-chain; Lys-72 of PKA (FIG. 3). Lys-72 in turn coordinates the β-phosphate of ATP in active protein kinases.

[0302] In addition, because the αC-helix is responsible for the major interfacial contacts between the N- and C-lobes, particularly via its interactions with the DFG motif of the activation segment, it plays a role both in aligning catalytic and substrate-peptide binding residues of the C-terminal lobe, and in governing the overall juxtaposition of the N- and C-lobes.

[0303] Motion of the αC-helix represents a general mechanism for the modulation of kinase catalytic activity, and the integration of diverse regulatory signals. For example, the position of the αC-helix of CDK2 is shifted to an active conformation on the association of the monomeric CDK2 subunit with cyclin A (Jeffrey et al., 1995), and similar changes in the αC-helix are observed on activation of the insulin receptor kinase and ERK2 on phosphorylation of their activation segments (Hubbard 1997; Canagarajah et al., 1997), and in the Src- and Eph-family tyrosine kinases (Sicheri et al., 1997, Xu et al., 1997; Wybenga-Groot et al., 2001). Significantly, in many protein kinases that are regulated by phosphorylation of the activation segment, the αC-helix provides a basic residue to contact the phosphate group of the phospho-amino acid, hence coordinating the relative positions of the αC-helix with the activation segment, and the N- and C-terminal lobes. In PKA, the basic residue is His-87 at the N-terminus of the αC-helix, which contacts pThr-197 of the activation segment (FIG. 2, 3). In the inactive state of PKB, His-196 and Glu-200 of the αC-helix (equivalent to His-87 and Glu-91 of PKA) are disordered, and contacts between Glu-200 and Lys-181 (Lys-72 of PKA), and those between His-196 and pThr-309, are not formed (FIG. 3).

[0304] Disorder of the αC-helix contributes to an inactive state of PKB for two reasons. First, the side-chain of Lys-181 is not properly positioned, and second, there are associated changes in the structure of the activation segment, and relative disposition of the N- and C-terminal lobes. As described below, disorder of the αB- and αC-helices of PKB is coupled to the disorder of its non-phosphorylated C-terminal regulatory segment.

[0305] Role of the C-terminal Regulatory Segment

[0306] A distinctive structural feature of PKA, not usually observed in other protein kinases, is the interaction of the extreme C-terminus of the protein with its N-terminal lobe. In PKA, the polypeptide chain emerges from the C-terminal lobe and extends along the entire length of the bi-lobal structure. At the tip of the N-lobe, the chain forms a reverse turn, allowing the extreme C-terminal eight residues of PKA to lie within an amphipathic/hydrophobic groove on the surface of the N-lobe (FIG. 1A, 2B). Importantly, these interactions are mediated by residues of the C-terminal hydrophobic motif, which contact the surface groove formed by residues of the αB- and αC-helices, and the β5-strand of the N-lobe. The dominant interactions at the interface involve those between the side chains of the two phenylalanine residues of the hydrophobic motif, Phe-347 and Phe-350, which protrude into a pocket formed by hydrophobic residues of the N-lobe (FIG. 2). Specifically, the phenyl-ring of Phe-347 is extensively buried by the side-chains of five amino acids: Lys-76, Val-79 and Val-80 of the αB-helix, Ile-85 of the αC-helix, and Leu-116 of the β5-strand, whereas the side-chain of Phe-350 contacts Leu-89 and Lys-92 of the αC-helix, and Leu-116 and Met-118 of the β5-strand (FIG. 2B). At one end of the channel, two adjacent basic residues of the αC-helix form salt-bridge interactions with two carboxylate groups of the hydrophobic motif.

[0307] In all three crystal structures of PKB, residues corresponding to the regions of the αB- and αC-helices of PKA that interact with the hydrophobic motif, are disordered, and this probably results from loss of interactions with the hydrophobic motif of PKB (FIG. 2A, C). In the crystal structures of ΔPH-PKB-ΔC, the 21 residues C-terminal to Ser-460 were removed from the expression construct, and therefore potential interactions between the hydrophobic motif and the N-lobe are not possible. Moreover, in these structures, electron density for residues C-terminal to Asp-441 is not visible, suggesting that they are conformational disordered. However, in the ΔPH-PKB structure, which contains a non-phosphorylated hydrophobic motif, and therefore retains the potential to interact with the N-lobe, we are also unable to detect visible electron density for residues C-terminal to Asp-441, indicating that the C-terminal 40 residues, including the hydrophobic motif, are mobile.

[0308] Conformation of the Activation Segment and Nucleotide Binding Site

[0309] The activation segment is central to the regulation and catalytic activity of protein kinases (Johnson et al., 1996). In the structure of active protein kinases, the activation segment contributes to the correct conformation of the catalytic site and ATP-binding residues, and participates in peptide-substrate recognition and specificity. By functioning as a link between the N- and C-lobes, conformational changes of the activation segment, resulting from regulatory phosphorylation, and/or modulator subunits, are coupled to global changes in kinase structure. In all three crystal forms of PKB, a contiguous region of the activation segment (residues 297 to 312) located between the invariant DFG and APE motifs, and including (p)Thr-309, is disordered. There is no electron density visible for these residues in either the 2Fo-Fc, or the simulated annealling omit maps. It was determined that pΔPH-PKB-ΔC was phosphorylated on Thr-309 by quantitative mass spectroscopic analysis of a tryptic digest of the protein. Moreover, it was confirmed that the protein forming the pΔPH-PKB-ΔC crystal was phosphorylated by Western blot analysis of a dissolved crystal using pThr-309-specific antibodies.

[0310] In the inactive PKB structures, residues of the DFG sequence are ordered, but adopt a different conformation from their counterparts in PKA, functioning to inhibit PKB by disrupting the nucleotide-binding site (FIG. 3). The DFG motif of activated protein kinases is important because its Asp residue (Asp-184 of PKA) coordinates the Mg2+ ion responsible for contacting the β- and γ-phosphates of ATP. In PKB, the side-chain of Asp-293 (equivalent to Asp-184 of PKA) is directed away from the ATP binding site (FIG. 3B). This structural change is accompanied by a shift in the positions of Phe-294 and Gly-295 of the DFG motif, and main-chain of Leu-296, towards the glycine-rich β1-β2 nucleotide-binding loop of the N-lobe. Motion of the DFG-motif residues is accommodated by a change in the relative orientation of the N- and C-lobes of PKB, compared with PKA, to avoid their clash with the β1-strand of the N-lobe. Relative to the conformation of the equivalent Phe-185 residue of PKA, the phenyl ring of Phe-294 is displaced by as much as 10 Å, and is situated within the hydrophobic adenine-binding pocket for ATP. This structural feature of PKB is similar to the inactive state of IRK where the Phe residue of the DFG motif blocks the nucleotide-binding. site by mimicking the ATP adenine ring (Hubbard et al., 1994). Thus, in PKB, the ATP binding site is disrupted both because the Lys-181 and Asp-293, residues responsible for coordinating the phosphate groups, are displaced, and because ATP is sterically hindered from binding by Phe-294. In PKA, and in the structures of other activated protein kinases, Phe-185 of the DFG motif packs deep into the interface between the two lobes, and forms intimate contacts with hydrophobic residues of the αC-helix of the N-lobe. These interactions serve to stabilise the relative positions of the αC-helix and activation segment. The altered conformation of Phe-294 of PKB is correlated with the relative dispositions of its N- and C-lobes, and the disorder of the αC-helix.

[0311] Crystal structures of protein kinase-peptide substrate complexes indicate that a common function of the activation segment is to coordinate the peptide-substrate with the correct geometry to allow phosphorylation of the incoming hydroxyl-group of a Ser/Thr or Tyr residue (Knighton et al., 1991b, Bossemeyer, 1993, Hubbard, 1997; Lowe et al., 1997). In PKA, the P+1 region of the activation segment, immediately C-terminus to pThr-197, contributes to peptide binding. The conservation of the P+1 region amongst AGC-kinases, suggests that in the phosphorylated active state of a PKB-substrate complex, similar peptide-protein interactions will exist. Disorder of the activation segment of PKB in both the unphosphorylated and mono-phosphorylated (pThr-309) states will preclude interactions with protein substrates.

[0312] PKB Peptide Substrate Specificity

[0313] The substrate specificity of PKB is known from an analysis of physiological PKB phosphorylation sites, and from an oriented peptide library screen (Obata et al., 2000). PKB only phosphorylates peptides with an arginine at the P-3 position and also strongly prefers substrates with an Arg residue at P-5 and with large hydrophobic residues at P+1. The structural basis for this substrate specificity can be rationalised by comparing the ternary PKA complex with our structure of PKB including the activation segment modelled on that of PKA. Optimal peptide substrates of PKA are related, although not identical, to those of PKB and other AGC-kinases. In the ternary PKA structure, PKI has the sequence T-G-R-R-N-A-I-H, with Ala at P-0. Arg at P-3 forms a salt bridge to Glu-127 (Knighton et al., 1991b; Bossemeyer et al., 1993), and because this residue is also conserved in PKB and phosphorylase kinase (where it contacts an Arg at P-3, Lowe et al., 1997), it is likely that the equivalent interaction will be formed in PKB-peptide complexes. Interestingly, the side-chain of Tyr-330 of PKA that is directed towards the Arg P-3 residue is a glutamate in PKB, possibly enhancing the affinity for a peptide with an Arg at P-3. Unlike PKB, PKA does not have a preference for an Arg at P-5, and in the PKA structure, Arg-133 is in close proximity to the Thr side-chain at P-5 of PKI. In PKB, however, Arg-133 is replaced with a serine, and this less bulky residue would accommodate a potential interaction between the peptide Arg residue at P-5 and Glu-342 of PKB. Finally, PKB prefers bulky hydrophobic residues at P+1, in contrast to PKA which is only able to accommodate smaller aliphatic residues. This P+1 hydrophobic site is larger in PKB because the side-chain of Phe-359 lacks the hydroxyl group of the equivalent Tyr-247 residue of PKA.

[0314] Mechanism of PKB Activation by Phosphorylation

[0315] The crystal structures of PKB, combined with an analysis of the structural differences between PKB and an activated conformation of PKA, provides a framework for understanding the mechanism of activation of PKB by phosphorylation of Thr-309 and Ser-474. Central to the conversion to the activated state on phosphorylation, are concerted disorder to order transitions of the αB- and αC-helices, activation segment, and C-terminal regulatory segment, all of which are linked to conformational changes of the DFG motif and re orientation of the N- and C-lobes to relieve steric hindrance to ATP binding, and to align catalytic site residues. Because the known structures of activated protein kinases all share the same overall features, including juxtaposition of catalytic site, and ATP and peptide binding residues, we can assume that phosphorylation of PKB converts the enzyme into a conformation similar to that of PKA phosphorylated on Thr-197. However, what distinguishes PKB from PKA, is the requirement for phosphorylation of both the C-terminal regulatory segment and the activation segment, to activate the kinase maximally. The role of Thr-309 phosphorylation will be similar to activation segment phosphorylation of PKA, CDK2 and ERK2, namely to coordinate contacts between the activation segment and other structural elements of the protein kinase, specifically, (i) the αC-helix of the N-lobe, (ii) a conserved arginine residue immediately preceding the catalytic Asp residue (Arg-165 and Asp-166, respectively of PKA), and (iii) a basic residue of the activation segment situated close to the Asp of the DFG motif (Lys-189 of PKA). Conservation of the three basic residues of PKA that contact the phosphate group of pThr-197 in all PKB-isoforms, suggests that the equivalent charge neutralisation observed in PKA will occur in the active state of PKB. In all three crystal forms of PKB, which represent low and partially active forms of the enzyme, and includes pΔPH-PKB-ΔC phosphorylated on Thr-309, the activation segment is disordered, and the enzyme adopts an inactive conformation. Thus phosphorylation of Thr-309 alone is not sufficient to order the activation segment and promote an active state of the enzyme; additional phosphorylation of Ser-474 is required. The hydrophobic motif of PKA is not regulated by phosphorylation, and in the PKA crystal structure lies within a surface hydrophobic groove formed by residues whose counterparts in the αB- and αC-helices of the inactive states of PKB are disordered. The finding that the C-terminal regulatory segment, comprising the unphosphorylated hydrophobic motif of ΔPH-PKB was disordered, suggests that activation by Ser-474 phosphorylation is caused by the concomitant ordering of the regulatory segment and αB- and αC-helices mediated by the interaction of the motif with the induced N-terminal lobe surface groove. Ordering of the αC-helix will induce global changes in the PKB conformation by facilitating interactions between the residues of the αC-helix and critical regions of the molecule. These interactions include those between Lys-181 and Glu-200, and two αC-helix-activation segment interactions; His-196 and pThr-309, and hydrophobic contacts with Phe-294 of the DFG motif. Reconfiguration of the activation segment allows the correct alignment of catalytic site and substrate binding residues. Consistent with this model of activation by ordering of the regulatory segment induced by Ser-474 phosphorylation, previous studies of PKA suggested that an ordered hydrophobic motif is important for enzyme activity and stability.

[0316] Replacing the conserved Phe residues of the motif with alanines, reduces catalytic activity to only 0.5% of the wild-type enzyme, and leads to decreased thermal stability (Etchebehere et al., 1997).

[0317] Allosteric Activation of pThr 309-PKB by Hydrophobic Motif Peptides

[0318] To test the model that Ser 474 phosphorylation promotes an interaction between the hydrophobic motif and the induced hydrophobic groove of the N-terminal lobe, thereby causing an allosteric activation of the kinase, the ability of peptides modelled on the hydrophobic motif of PKB to activate the enzyme via an intermolecular association with the N-terminal lobe was assessed.

[0319] First, it was shown that towards Crosstide, a peptide-substrate derived from the PKB phosphorylation site of GSK-3, the unphosphorylated form of ΔPH-PKB-ΔC has no significant catalytic activity, whereas its Thr 309 phosphorylated counterpart was active. Addition of a peptide modelled on the phosphorylated hydrophobic motif of PKBβ (HM-P, residues 460-481), activated pΔPH-PKB-ΔC, with the stimulation reaching a maximum of 4-fold at 0.6 mM, the highest concentration of HM-P peptide achievable in our assay (FIG. 5A). Significantly, this 4-fold stimulation of PKB by HM-P peptide is lower than the 7-10 fold stimulation of PKB by Ser 474 phosphorylation (Alessi et al., 1996). Analysis of the concentration-dependent activation of PKB by HM-P (FIG. 5A) revealed that the binding sites for HM-P on ΔPH-PKB-ΔC were not fully titrated even at a peptide concentration of 0.6 mM, suggesting that higher concentrations of HM-P are necessary to fully stimulate PKB activity. The modest activation of PKB by HM-P peptide suggests a relatively low affinity of peptide for the PKB N-terminal lobe. An equivalent HM-peptide with an Asp substitution of Ser 474 was also capable of activating pΔPH-PKB-ΔC, consistent with studies showing that Asp mimics Ser 474 phosphorylation (Alessi et al., 1996). However, the maximum activation by this peptide was only 3-fold because of the lower affinity towards ΔPH-PKB-ΔC than the HM-P peptide (FIG. 5A). Finally, as expected, the unphosphorylated HM-peptide did not stimulate PKB activity. It was also found that the phosphorylated HM-peptide did not further activate ΔPH-PKB phosphorylated on both Thr 309 and Ser 474. Furthermore, HM-P peptide was unable to activate ΔPH-PKB-ΔC with unphosphorylated Thr 309, in agreement with earlier findings that growth factor stimulation fails to activate T308A mutants of PKBα (Bellacosa et al., 1998) indicating an essential role of Thr 308/309 phosphorylation for PKB activity.

[0320] Phosphorylation of a Ser or Thr residue within the hydrophobic motif is a conserved feature of the activation of varied AGC-kinases, including PKC (Keranen et al., 1995) and the p70 and p90 S6-kinases (Pearson et al., 1995; Frodin et al., 2000). However, in some PKC isoforms, and in the PKC related kinase, PRK2, the site of Ser/Thr phosphorylation is replaced with either an Asp or Glu residue, suggesting that in these kinases, the hydrophobic motif will be constitutively activated, similarly to PKA, because of a permanent negative charge at this site. The C-terminal region of PRK2 that encompasses the carboxy-terminal hydrophobic motif was previously shown by Alessi and colleagues to interact tightly with the AGC-family kinase PDK1 (Balendran et al., 1999). PIFtide, a peptide representing the C-terminal 24 residues of PRK2, including its hydrophobic motif, was observed to stimulate PDK1 activity by four-fold (Biondi et al., 2000). Remarkably, PIFtide was found here to activate pΔPH-PKB-ΔC by 15-fold, substantially more strongly than the activation achieved by the phosphorylated HM-peptide. Analysis of the concentration dependence of pΔPH-PKB-ΔC activation by PIFtide, revealed that the peptide binds the kinase with high affinity, resulting in a maximum and saturable activation at 20 μM and a corresponding EC50 value of 3 μM (FIG. 5B). Significantly, the specific activity of pΔPH-PKB-ΔC maximally activated by PIFtide was 350 nmol/min/mg, essentially identical to the specific activity of ΔPH-PKB phosphorylated on both Thr 309 and Ser 474. These specific activity data indicate that the stimulation of pΔPH-PKB-ΔC by an intermolecular association with PIFtide is equivalent to Ser 474 phosphorylation and the resultant intramolecular association between the N-lobe of PKB and phosphorylated HM and furthermore suggests that an analysis of PKB-PIFtide interactions will provide insights concerning the mechanism of activation by Ser 474 phosphorylation. PIFtide promotes a 5-fold activation of ΔPH-PKB phosphorylated on Thr 309 to a specific activity similar to that of pΔPH-PKB-ΔC. The lower level of stimulation relative to the 15-fold observed for pΔPH-PKB-ΔC can be explained by the partial phosphorylation of Ser-474 on pΔPH-PKB purified from Sf9 cells.

[0321] Using isothermal titration calorimetry, the affinity between PIFtide and both pΔPH-PKB-ΔC and ΔPH-PKB-ΔC was determined (FIG. 5C). Firstly, we found that the equilibrium dissociation constant defining the interaction between PIFtide and pΔPH-PKB-ΔC was 6 μM, essentially identical to the EC50 value for the activation of pΔPH-PKB-ΔC by PIFtide (FIG. 5B). This result suggests that the association of PIFtide to PKB correlates with the activation of the kinase. Secondly, it was found that the interaction of PIFtide with ΔPH-PKB-ΔC is driven by a large negative enthalpy change (ΔH of −16.0 kcal.mol−1) that compensates the energetically unfavourable decrease in entropy (TΔS of −9.2 kcal.mol−1). The observed large decrease in entropy is not generally typical of protein-peptide interactions, for example SH2-domain-phosphotyrosine peptide complexes (Ladbury et al., 1996), and is consistent with an ordering of both the protein, presumably the αB- and αC-helices of the N-lobe, and peptide on complex formation. Although PIFtide does not stimulate the activity of ΔPH-PKB-ΔC (FIG. 5B), ITC data revealing a dissociation constant of 5.5 μM indicated that PIFtide interacts with this form of the enzyme as strongly as it does to phosphorylated ΔPH-PKB-ΔC, further emphasising the crucial role of Thr 309 phosphorylation for PKB activity (FIG. 5C).

[0322] The finding that PIFtide interacts with PKB with high affinity provided a model system for testing the notion that the essential role of Ser 474 phosphorylation is to promote the association of the hydrophobic motif with the N-lobe of PKB. The residue of PIFtide equivalent to Ser 474 of PKB is an Asp, which presumably mimics a phosphorylated Ser 474 residue. To assess the importance of this residue for the ability of PIFtide to activate PKB, the concentration dependent activation of pΔPH-PKB-ΔC by PIFtide with an Ala residue substituting for the Asp was determined. Although higher concentrations of this mutant PIFtide(D->A) are required to activate pΔPH-PKB-ΔC than wild type PIFtide, suggesting a lower affinity, the maximal activation of the kinase achieved by saturating concentrations of the mutant peptide is identical to that of the wild type peptide (FIG. 5B). The estimated EC50 value for PIFtide(D->A) is 30 μM, indicating a 10-fold lower affinity than PIFtide. ITC experiments also revealed an approximately 25-fold lower affinity between PIFtide(D->A) and pΔPH-PKB-ΔC relative to PIFtide. Thus, these experiments demonstrate an important concept that the PIFtide-induced conformational change of pΔPH-PKB-ΔC that results when PIFtide interacts with the kinase, and which leads to a maximal stimulation of the kinase activity, does not require a negatively charged residue at the equivalent of Ser 474 of the hydrophobic motif. The major role of a negative charge at this site is to increase the association of PIFtide with the PKB N-lobe, and that other residues, particularly the conserved Phe residues of the FxxF motif (see below), are more critical for promoting the conformational change of the protein.

[0323] Because of the low affinity between pΔPH-PKB-ΔC and the PKB HM peptides, it was not possible to determine a KD value defining their interaction with PKB using ITC. However, by assuming that the association between pΔPH-PKB-ΔC and the PKB HM-peptides is an equilibrium process and that at saturating concentrations of peptide, the activation of pΔPH-PKB-ΔC will be similar to that induced by PIFtide, the data in FIG. 5A were used to estimate the EC50 constants for the phosphorylated and S474D HM-peptides to be 2.3 mM and 3.6 mM, respectively, an affinity ˜1000-fold lower than for PIFtide.

[0324] Mutagenesis of the Hydrophobic Motif and N-lobe Hydrophobic Groove

[0325] By assessing the ability of modified PIFtide and HM peptides to activate pΔPH-PKB-ΔC, the role of conserved residues of the hydrophobic motif (HM) to induce the active conformation of PKB was delineated. These experiments used an 11-residue peptide encompassing the six-residue hydrophobic motif of PIFtide (PIFtide1, .FIG. 6A) that essentially recapitulates the activation of pΔPH-PKB-ΔC observed for the 24-residue PIFtide. The slightly lower activation suggests that residues of PIFtide N-terminal to the HM contribute to high affinity PKB interactions. The PKB activities were determined at PIFtide concentrations ranging from 210-250 μM, where wild-type PIFtide fully activates PKB (FIGS. 5B, 6A). While all conserved residues of the HM motif contribute to PKB activation, significantly, the two phenylalanine residues of the motif are essential for HM-induced activation. Ala substitutions of these residues in both PIFtide and the phosphorylated PKB HM-peptide, completely eliminated the potential of these peptide to stimulate PKB, even at PKB HM-peptide concentrations of 1.2 mM (FIG. 6A). A similar essential role for the equivalent Phe residues has been proposed for PKA where Ala substitutions lower the thermal stability, and virtually abolishes the catalytic activity of the enzyme (Etchebehere et al., 1997). Mutation of either the conserved Tyr residue or of both Asp residues of the PIFtide motif showed that these residues also contribute to the stimulatory affect of PIFtide on PKB activity (FIG. 6A). PIFtide activates PKB by interacting with, and simultaneously stabilising the activated conformation of PKB. Therefore, the lower stimulatory effect of mutant PIFtide and PKB peptides most likely results from a reduced affinity for the activated conformation of PKB, however, because mutant PIFtide peptides have either low or no activity even at >200 μM, we were unable to determine EC50 values for their activation of PKB.

[0326] The crucial role of the conserved Phe residues of the hydrophobic motif to promote PIFtide and PKB HM-peptide mediated stimulation of PKB, and for the activity of PKA, suggests that they stabilise the active state of both PKB and PKA by a related structural mechanism. To test the notion that a hydrophobic groove is induced in PKB to engage the hydrophobic motif, and activate the kinase, a series of His tagged pΔPH-PKB-ΔC hydrophobic groove mutants were prepared and their responsiveness to PIFtide assessed. PKB mutants were transiently expressed in HEK cells, phosphorylated in vitro with PDK1, and purified using Ni-NTA agarose. SDS-PAGE and western blot analysis of the purified fractions revealed that wild type and mutant proteins were expressed to similar levels, and that the enzyme was quantitatively isolated in a phosphorylated state. Moreover, the basal kinase activities of wild type and mutant proteins were similar, indicating that the mutations did not disrupt the overall structure of the protein. Wild type PKB prepared using this procedure was stimulated ˜5-fold by 130 μM PIFtide (FIG. 6B). The slightly lower activation probably results from incomplete Thr 309 phosphorylation, and consequently the PKB HM-peptide did not elicit measurable activation. The substitution of hydrophobic groove residues significantly reduced, but did not completely abolish the potential of PIFtide to stimulate PKB (FIG. 6B). Mutation of two αC-helix residues, Val 194 and Val 198 (Ile 85 and Leu 89 of PKA), reduced PIFtide activation to only 25% of wild type, whereas a Leu 225 mutant of the β-5 strand (Leu 116 of PKA) caused almost a complete loss of responsiveness to PIFtide (FIGS. 2, 4, 6B).

[0327] Electrostatic interactions are important in defining high affinity PIFtide and PKB HM peptide associations with PKB (FIG. 5B), and form the basis for the increased affinity of the HM for the N-lobe and subsequent activation of PKB by Ser 474 phosphorylation. Examination of the PKA and PKB crystal structures suggests that Arg 202 of the αC-helix is likely to be important in mediating contacts to pSer 474 and the corresponding Asp residue of PIFtide. The equivalent residue of PKA, Arg 93, which is also conserved in PKC and PRK2, forms a water-mediated salt bridge to the carboxylate group of Glu 349 (FIG. 2). A charge reversal at this site (R202D) almost eliminates the ability of 130 μM PIFtide to activate PKB (FIG. 6B), consistent with the notion that Arg 202 forms electrostatic contacts with PIFtide. However, analogous to the finding that at high concentrations, the PIFtide(D->A) mutant could activate PKB maximally (FIG. 5B), the R202D PKB mutant was more responsive to higher concentrations of the peptide.

[0328] Conservation of the Hydrophobic Motif Groove in AGC-Protein Kinases

[0329] The role of a phosphorylated hydrophobic motif to activate PKB that is described here, is probably applicable to other AGC-protein kinases that are regulated via dual phosphorylation of an activation segment residue and a hydrophobic motif residue, for example PKC, the p70 and p90 S6 kinases and SGK (Parekh et al., 2000; Pearson et al., 1995; Frodin et al., 2000; Kobayashi and Cohen, 1999). A disorder-order transition of PKC induced by phosphorylation is implied by the resistance of the fully phosphorylated, but not partially phosphorylated forms of PKC, to protein phosphatases, and their enhanced resistance to temperature-induced denaturation (Bornancin and Parker, 1997). Substitutions of the Phe residues of the hydrophobic motif of PKA lowers its thermal stability, and virtually abolishes its catalytic activity (Etchebehere et al., 1997). The conservation of the hydrophobic motif of AGC-kinases is correlated with the invariance of the residues equivalent to Lys-76 and Leu-116 of PKA that would be predicted to form the base of the hydrophobic groove in a number of diverse AGC-kinases, including PKA, PKB, PKC, p70-S6K, p90-S6K, SGK, NDR and PDK1. Alessi and colleagues have shown that the hydrophobic motif of PIFtide determines the ability of this peptide to bind to the N-lobe, hence activating PDK1 (Balendran et al., 1999), and the presence of PIFtide greatly increases the thermal stability of PDK1 (Biondi et al., 2000). By analogy to PKB, we suggest that the activation of PDK1 by PIFtide involves a disorder-order transition of the αB- and αC-helices, and consequent global conformational changes.

[0330] Structure-Based Drug Design

[0331] Determination of the 3D structure of PKBβ provides important information about the binding sites of PKBβ, particularly when comparisons were made with similar enzymes. This information may then be used for rational design of PKBβ inhibitors, e.g. by computational techniques which identify possible binding ligands for the binding sites, by enabling linked-fragment approaches to drug design, and by enabling the identification and location of bound ligands using X-ray crystallographic analysis.

[0332] 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 PKB residues involved in the interaction with ATP enables the development of specific and potent inhibitors of this kinase. This information may thus be used to develop potent and specific small molecule inhibitors of PKB in a number of ways. PKBβ may be co-crystallised, and/or existing PKBβ crystals may be soaked, with known inhibitors of PKB, including staurosporin, and those discovered in high-throughput screening programmes known to the skilled person. Alternatively, or additionally, rational drug design programmes may make full use of the crystallographic coordinates.

[0333] Discussion and Implications for Other AGC Kinases

[0334] This study presents a model for the regulation of PKB by hydrophobic motif phosphorylation. The data indicates that the role of HM phosphorylation is to induce an ordered N-terminal lobe as a result of an increased affinity between the hydrophobic motif and the hydrophobic groove. Ordering of the αC-helix transmits a structural change to the activation segment and re-orients the N- and C-lobes. In the inactive PKB crystal structures residues of the αB- and αC-helices are disordered. Consistent with a disorder-to-order transition, the interaction of PIFtide with PKB is accompanied by a large negative entropy change. Mutation of key hydrophobic residues of the N-lobe groove and hydrophobic motif either reduce or eliminate the ability of PIFtide to activate PKB. Using PIFtide as a model system shows that the role of a negative charge within the HM (e.g. PKB Ser 474 phosphorylation) is to increase the affinity of the HM for the N-lobe.

[0335] In the context of the PKB kinase domain, phosphorylation of Ser 474 will increase the ability of the HM to interact with the N-lobe via an intramolecular association. However, because PIFtide(D->A) had only 10-fold lower affinity for PKB relative to PIFtide (FIG. 5B), it is likely that the unphosphorylated HM of PKB will still retain a weak affinity for the N-lobe. It can therefore be rationalised why PKB mono-phosphorylated on Thr 309 has between 7-10-fold lower activity than doubly phosphorylated PKB.

[0336] Disorder to order transitions of the αC-helix as a result of phosphorylation represents a previously unrecognised mechanism for the stimulation of protein kinase activity. However, there is evidence that other AGC-kinases undergo similar transitions, modulated by the hydrophobic motif. For example, phosphorylation of the HM of PKC increases its resistance to temperature-induced denaturation (Bornancin and Parker, 1997) and the Phe residues of the PKA HM motif are critical for its stability and catalytic activity (Etchebehere et al., 1997). The conservation of the hydrophobic motif of AGC-kinases is correlated with the invariance of the residues equivalent to Lys 76 and Leu 116 of PKA predicted to form the base of the hydrophobic groove in a number of diverse AGC-kinases, (FIG. 4). Uniquely amongst AGC-kinases, PDK1 lacks a C-terminal hydrophobic motif, although its N-terminal lobe hydrophobic groove is proposed to interact with PIFtide (Biondi et al., 2000). Similarly to the findings with PKB, high affinity interactions between PIFtide and PDK1 required the conserved aromatic and Asp residues of the hydrophobic motif of the peptide (Balendran et al., 1999), and were disrupted by substitutions of PDK1 HM groove residues (Biondi et al., 2000).

[0337] The affinity of the HM-P peptide for PKB that is not phosphorylated on Ser 474 is ˜1000-fold lower than that of PIFtide, and is reminiscent of the low affinity of the tyrosine phosphorylated C-terminus of Src for its own SH2 domain, compared with optimal phosphotyrosine binding sequences (Bradshaw et al., 1998). The covalent attachment of the phosphorylated hydrophobic motif to the PKB kinase domain will greatly increase its effective concentrations presumably in excess of the EC50 value estimated for the activation of PKB by the HM-P peptide. However, a modest mutual affinity may be important for two reasons. First, in order for phosphorylation of the HM to be capable of modulating its affinity for the N-lobe, the affinity of the unphosphorylated HM for the N-lobe must be sufficiently low that it is not constitutively associated with the N-lobe. For example, a substitution of PIFtide(D->A) for the PKB HM motif would render PKB fully active and therefore unresponsive to HM phosphorylation. Second, it allows modulator proteins to gain access either to the hydrophobic groove or the phosphorylated motif, or for protein phosphatases to dephosphorylate pSer 474. Whether the activation of PKB by PIFtide reflects a biologically significant regulatory mechanism for stimulation of PKB by a modulator protein that interacts with the N-lobe is unknown. However, the affinity of PIFtide for PKB may provide insight concerning the nature of the PDK2 enzyme responsible for phosphorylating Ser 474. A possible candidate for this enzyme is a kinase that interacts with the hydrophobic binding groove of PKB, perhaps via a sequence similar to the hydrophobic motif of PKB or PIFtide.

MATERIALS AND METHODS

[0338] The Genebank accession numbers for the PKB isoforms are as follows:

[0339] α gi 190827 (m63167); β gi 178325 ( m95936); γgi 4757578 (af124141)

[0340] Expression of ΔPH-PKBβ-ΔC (Residues 146-460) and ΔPH-PKBβ (Residues 146-481)

[0341] Generation of recombinant baculovirus using the GIBCO/Life Sciences Bacmid system was performed using standard procedures.

[0342] For ΔPH-PKBβ-ΔC, 3 PCR reactions were set up as follows:

236.5μlH2O5μl10x pfu buffer5μldNTPs0.2 mM1μl5′ Primer 3611760 pmols1μl3′ Primer 3650860 pmols1μlPfastBacHTa ΔPH PKBβ2851a(170 ng)50μltotal + 2.5 u pfu

[0343] Pfu polymerase and buffer were purchased from Promega (M7741). All PCR reactions were performed in a Perkin Elmer Geneamp PCR system 9700.

3PCR conditions60 s at 95° C.,then 15 cycles:60 s at 95° C.120 s at annealing temperature 62° C.180 s at 72° C.

[0344] Primers were:

436117:GCC ATG GAT CCG AAA GTG ACC ATG AAT GAC TTC(5′ BamHI)36508:GGG GGT ACC TCA GAG GCT GTC ATA GCG GTC AGG(3′ KpnI)

[0345] For ΔPH-PKBβ, 3 PCR reactions were set up as follows:

537 μlH2O 5 μl10x pfu buffer 5 μldNTPs2.5 mM 1 μl5′ Primer 3611770 pmols 1 μl3′ Primer 2858554 pmols 1 μlPFaStBaCHTa.ΔPH PKBβ 2702b(200 ng)50 μltotal + 2.5 u pfu

[0346] Pfu polymerase and buffer were purchased from Promega (M7741). All PCR reactions were performed in a Perkin Elmer Geneamp PCR system 9700

6PCR conditions60 s at 95° C.,then 15 cycles:60 s at 95° C.120 s at annealing temperature 66° C.180 s at 72° C.

[0347] Primers were:

736117:GCC ATG GAT CCG AAA GTG ACC ATG AAT GAC TTC(5′ BamHI)28585:GGG GGT ACC TCA CTC GCG CAT GCT GGC CGA GTA GG(3′ KpnI)

[0348] All PCR fragments were pooled and purified using the Qiagen PCR purification kit (28106) and digested with the appropriate restriction enzymes and subcloned into the pFastBacHTa (10584-027) vector from Gibco BRL life technologies.

[0349] Ligation mixes were used to transform E. coli XL1 blue (Stratagene) and colonies containing recombinant DNA were grown up for miniprep DNA analysis. Miniprep was prepared using Qiagen miniprep kit 27106. All expression constructs were fully sequenced on an Applied Biosystems 3700 automated sequencer.

[0350] Insect cells (density ˜2.0×106 cells/ml, total volume of 2.7 L; 5.4×109 Sf9 cells), grown in a culture of GIBCO/Life Sciences supplemented Sf900II medium were infected at a moiety of infection of 2 and grown for 72 hours prior to harvesting.

[0351] Purification of ΔPH-PKBβ-ΔC (Residues 146-460) and ΔPH-PKBβ (Residues 146-481)

[0352] All procedures were performed at 4° C.

[0353] 1. Cell lysis: Insect cells were lysed in a Q-sepharose buffer A (25 mM Tris.HCl, [pH 7.5], 25 mM NaCl, 25 mM NaF, 25 mM β-glycerophosphate, 0.1% (v/v) β-mercaptoethanol, 2 mM benzamidine, 0.2 mM PMSF, 10% (v/v) glycerol, 1 μg/ml of DNAase.

[0354] 2. Q-sepharose, anion exchange chromatography: The lysate was cleared by centrifugation and loaded onto a 50 mL Q-sepharose column equilibrated in buffer A. The column was washed in 200 mL of buffer A and PKB was eluted using 100 mL of buffer A+1 M NaCl.

[0355] 3. Ni-NTA affinity chromatography: The pH of the eluate was raised to 8.0 using a 1 M of Tris.HCl (pH 9.2) and this sample was loaded onto a Ni-NTA agarose column containing 10 mL of Ni-NTA agarose resin that had been pre-equilibrated in buffer B: 20 mM imidazole, 20 mM Tris.HCl (pH 8.0), 25 mM NaF, 25 mM β-glycerophosphate, 500 mM NaCl, 0.1% (v/v) β-mercaptoethanol, 2 mM benzamidine, 0.2 mM PMSF. The column was washed and the protein was eluted using buffer B+300 mM imidazole. EDTA and DTT to final concentrations of 0.5 mM and 2 mM, respectively, were added immediately to the eluted protein. Phosphorylation reactions (see below) were performed after this step.

[0356] 4. Phenyl TSK hydrophobic interaction chromatography: The protein was brought to the appropriate concentration of ammonium sulphate and loaded onto a phenyl TSK column equilibrated in buffer C: 50 mM Tris.HCl (pH 7.5), 100 mM NaCl, 2 mM DTT, 2 mM benzamidine, 0.2 mM PMSF, with the same concentration of ammonium sulphate as the protein solution. The column was washed and PKB was eluted using a linear gradient developed to a buffer D consisting of 50 mM Tris.HCl (pH 7.5), 100 mM NaCl, 15% (v/v) glycerol, 2 mM DTT, 2 mM benzamidine, 0.2 mM PMSF.

[0357] Concentrations of ammonium sulphate used were as follows:

8pΔPH-PKBβ-ΔC1.23 M ammonium sulphateΔPH-PKBβ-ΔC0.63-0.68 M ammonium sulphateΔPH-PKBβ0.82-0.86 M ammonium sulphate

[0358] Following this HIC step, those proteins which were to be dephosphorylated were treated with λ protein phosphatase, as described below.

[0359] 5. Tev protease cleavage. The 6×His affinity tag was removed by cleavage using Tev (tobacco etch virus) protease. Tev protease was added to PKB from step 4 and this solution was dialysed over 14 hr into buffer E: 50 mM Tris.HCl (pH 8.0), 100 mM NaCl, 5 mM DTT.

[0360] 6. To remove Tev protease (as well as PDK1 and λ protein phosphatase, where appropriate) from PKB after cleavage of the His-tag from PKB, the solution of Tev protease and PKB were dialysed into buffer B: 20 mM imidazole, 20 mM Tris.HCl (pH 8.0), 25 mM NaF, 25 mM β-glycerophosphate, 500 mM NaCl, 0.1% (v/v) β-mercaptoethanol, 2 mM benzamidine, 0.2 mM PMSF and loaded onto a Ni-NTA agarose column. Cleaved PKB was recovered in the flow through.

[0361] 7. Q-sepharose, anion exchange chromatography. The PKB collected in step 6 was dialysed into Q-sepharose buffer F: 25 mM Tris.HCl (pH 7.5), 25 mM NaCl, 5% (v/v) glycerol, 0.5 mM EDTA, 2 mM DTT, 0.2 mM PMSF. The column was washed in the above buffer and the protein was eluted by developing a shallow gradient to buffer F+0.5 M NaCl.

[0362] 8. Size exclusion chromatography. The protein from step 7 was concentrated to <2 mL and loaded onto an S75 gel filtration column equilibrated in buffer G: 10 mM Tris.HCl (pH 7.5), 100 mM NaCl, 2 mM DTT.

[0363] Expression of PDK1

[0364] Recombinant PDK1, for phosphorylation of ΔPH-PKβ-ΔC, was expressed from recombinant baculovirus generated by standard procedures.

[0365] 3 PCR reactions were set up as follows using pCMV5.myc PDK1 fl-1 (Pullen et al., 1998) as a template:

923 μlH2O 5 μl10x Taq buffer10 μlQ-solution (5x) 5 μldNTPs0.25 mM 4 μl5′ Primer 3066560 pmols 1 μl3′ Primer 2277760 pmols 2 μlpCMV5.myc PDK1 fl-1(200 ng)50 μltotal + 2.5 u pfu

[0366] Taq polymerase, Q-solution and buffer were purchased from Qiagen 201203. All PCR reactions were performed in a Perkin Elmer Geneamp PCR system 9700

10PCR conditions60 s at 94° C.,Then 5 cycles:30 s at 94° C.4 min at 72° C.then 5 cycles:30s at 94° C.4 min at 70° C.then 20 cycles:30s at 94° C.4 min at 68° C.

[0367] Primers

1130665CCT GCT AGC ACG GCC AGG ACC ACC AGC CAG CTG TAT GACNheI22777CCC GAA TTC TCA CTG CAC AGC GGC GTC CGG GTG GCEcoRI

[0368] All PCR fragments were pooled and purified using the Qiagen PCR purification kit (28106) and digested with the appropriate restriction enzymes and subcloned into the vectors indicated below. The PCR fragment was subcloned into pRSETA as a NheI/KpnI fragment, subsequently released as a NdeI/KpnI fragment and subcloned into pFastBac1 (10360-014 from Gibco BRL life technologies) between the BamHI and KpnI sites using a BamHI-NdeI linker.

[0369] All PCR fragments were pooled and purified using the Qiagen PCR purification kit (28106) and digested with the appropriate restriction enzymes and subcloned into pFastBac1 (10360-014) from Gibco BRL life technologies to yield pFastbac1. His PDK1-c(full length aa 1-556).

[0370] Ligation mixes were used to transform E. coli XL1 blue (Stratagene) and colonies containing recombinant DNA were grown up for miniprep analysis.

[0371] Miniprep was prepared using Qiagen miniprep kit 27106. All expression constructs were fully sequenced on Applied Biosystems 3700.

[0372] Insect cells (density ˜2.0×106 cells/ml, total volume of 2.7 L; 5.4×109 Sf9 cells), grown in a culture of GIBCO/Life Sciences supplemented Sf900II medium were infected at a moiety of infection of 2 and grown for 72 hours prior to harvesting.

[0373] Purification of PDK1

[0374] PDK1 was purified by following steps 1, 2, 3 5 and 6 described above, as for recombinant PKB.

[0375] Phosphorylation of ΔPH-PKBβ-ΔC (Residues 146-460) and ΔPH-PKBβ (Residues 146-481) on Thr309 Using PDK1

[0376] PKB from step 3 above was dialysed into a buffer containing 50 mM Tris.HCl (pH 7.5), 100 mM NaCl, 5 mM DTT. MgCl2 and ATP were added to a final concentration of 5 mM. PDK1 was added and the mixture was incubated at 4° C. for 14 hrs and at 20° C. for 2 hrs. PDK1 was removed from phosphorylated PKB by Ni-NTA agarose. The PKB-PDK1 solution was dialysed into buffer B (step 3) and loaded onto Ni-NTA agarose and eluted as described in step 3. The phosphorylated PKB was further purified using steps 4-8 above.

[0377] Dephosphorylation of ΔPH-PKBβ (Residues 146-481) Using λ Protein Phosphatase

[0378] ΔPH-PKBβ (residues 146-481) was dialysed into the following buffer: 50 mM Tris.HCl (pH 7.5), 150 mM NaCl, 2 mM MnCl2, 5 mM DTT, λ protein phosphatase was added at a ratio of 1 mg of λ protein phosphatase to 8 mg of ΔPH-PKBβ. ΔPH-PKBβ was incubated in these conditions at 20° C. for 2 h. Simultaneously, TEV protease was added to cleave the N-terminal His tag. After 2 h ΔPH-PKBβ was dialysed into buffer B (step 3) and loaded onto a Ni-NTA column to remove λ phosphatase and TEV. PKB was collected in the flow through. The protein was further purified using Q-sepharose and gel filtration chromatography (steps 7 and 8).

[0379] Crystallisation of pΔPH-PKBβ-ΔC (Residues 146-460)—First Batch.

[0380] The protein was concentrated to 10 mg/ml and AMPPNP/MgCl2 was added to a final concentration of 5 mM. Crystals were grown using the under-oil batch method. A small volume of protein (3 μl) was mixed with an equal volume of crystallisation buffer: 30% (w/v) polyethylene glycol 4000, 0.2 M lithium sulphate, 0.1 M Tris.HCl (pH 7.5), 5 mM DTT, within individual wells of a 72 well polystyrene tray (Nunc) and immersed under 5 ml of silicone oil. The trays were incubated at 20° C. and crystals appeared within a few days and grew to a maximum size of 0.1 mm×0.1 mm×0.5 mm in a week. The crystals exhibited a rod-like rectangular morphology.

[0381] Crystallisation of pΔPH-PKB-ΔC (Second Batch), ΔPH-PKB-ΔC, and ΔPH-PKB.

[0382] The protein was concentrated to 10 mg/ml and AMP-PNP/MgCl2 was added to a final concentration of 5 mM. Crystals were grown using the under-oil batch method. A small volume of protein (1 μl) was mixed with an equal volume of crystallisation buffer: 30% (w/v) polyethylene glycol 4000, 0.2 M lithium sulphate, 0.1 M Tris.HCl (pH 8.5), 5 mM DTT, within individual wells of a 72 well polystyrene tray and immersed under silicone oil and incubated at 20° C.

[0383] Data Collection and Structure Determination

[0384] Preparation of crystals for X-ray data collection: Crystals were harvested from the crystallisation trays and incubated in a cryoprotection buffer consisting of 18% (w/v) polyethylene glycol 4000, 120 mM lithium sulphate, 60 mM Tris.HCl (pH 7.5), 15% (v/v) polyethylene glycol 400, 5 mM AMPPNP/MgCl2 for 20 secs, prior to mounting the crystals in a ryan loop, and freezing in a nitrogen gas stream at 100 K. X-ray diffraction data were collected at the SRS, Daresbury, UK and at the European Synchrotron Radiation Facility, Grenoble, France.

[0385] Data were collected and these were analysed and processed using the HKL (Otwinowski and Minor, 1997) and CCP4 (CCP4, 1994) program suites. The structure was solved by means of molecular replacement using the coordinates of the ternary complex of the catalytic subunit of murine PKA as a search model (Knighton et al., 1991) with the program CNS (Brünger et al., 1998). The atomic structure was refined using rigid body and least squares refinement with CNS. Model building and analysis was done using O (Jones et al., 1991).

[0386] Protein Kinase B Assay

[0387] PKB was assayed essentially as described by Andjelkovic et al. (1999) with 30 μM Crosstide (GRPRTSSAEG) as substrate except the protein kinase A inhibitor peptide was not added to the reactions. For peptide stimulation experiments the various peptides were dissolved in water and added to the kinase assay mix prior to adding the PKB protein. Peptides were synthesized by Franz Fischer at the FMI or purchased from Neosystem, Strasburg, France.

[0388] Peptides used were:

12PKB HM-PGLLELDQRTHFPQFpSYSASIRBPKB HM-DGLLELDQRTHFPQFDYSASIREPKB HM-SGLLELDQRTHFPQFSYSASIREPKB HM-PFGLLELDQRTHABQApSYSASIREPIFtideREPRILSEEEQEMFRDFDYIADWPIFtide (D->A)REPRILSEEEQEMFRDFAYIADWPIFtide1 MFRDFDYIADWPIFtide2 MFRDFAYIADWPTFtide3 MFRAFAYIADWPIFtide4 MARDADYIADWPIFtide5 MFRDFDATADW

[0389] pS is used to indicate phosphoserine.

[0390] All experiments were performed in either duplicate or triplicate.

[0391] While the invention has been described in conjunction with the exemplary embodiments described above, many equivalent modifications and variations will be apparent to those skilled in the art when given this disclosure. Accordingly, the exemplary embodiments of the invention set forth are considered to be illustrative and not limiting. Various changes to the described embodiments may be made without departing from the spirit and scope of the invention. The references in the above text and listed below are incorporated by reference.

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13TABLE 2Coordinate data for pΔPH-PKBβ-ΔC (first batch)REMARK coordinates from restrained individual B-factor refinementREMARK refinement resolution: 500.0-2.8 AREMARK starting r = 0.3586 free_r = 0.4460REMARK final r = 0.3498 free_r = 0.4274REMARK B rmsd for bonded mainchain atoms = 1.346 target = 1.5REMARK B rmsd for bonded sidechain atoms = 1.595 target = 2.0REMARK B rmsd for angle mainchain atoms = 2.356 target = 2.0REMARK B rmsd for angle sidechain atoms = 2.450 target = 2.5REMARK rweight = 0.1000 (with wa = 7.46871)REMARK target = mlf steps = 30REMARK sg = P4 (1) 2 (1) 2 a = 149.33 b = 149.33 c = 39.371 alpha = 90 beta = 90gamma = 90REMARK parameter file 1: CNS_TOPPAR: protein_rep.paramREMARK molecular structure file: generate_easy.mtfREMARK input coordinates: anneal_1.pdbREMARK reflection file = pkb12-free.fobREMARK ncs = noneREMARK B-correction resolution: 6.0-2.8REMARK initial B-factor correction applied to fobs:REMARK B11 = −3.842 B22 = −3.842 B33 = 7.684REMARK B12 = 0.000 B13 = 0.000 B23 = 0.000REMARK B-factor correction applied to coordinate array B: −3.876REMARK bulk solvent: density level = 0.312838 e/A{circumflex over ( )}3, B-factor = 24.4035 A{circumflex over ( )}2REMARK reflections with |Fobs|/sigma_F < 0.0 rejectedREMARK reflections with |Fobs| > 10000 * rms (Fobs) rejectedREMARK theoretical total number of refl. in resol. range: 11510 (100.0%)REMARK number of unobserved reflections (no entry or |F| = 0): 116 (1.0%)REMARK number of reflections rejected: 0 (0.0%)REMARK total number of reflections used: 11394 (99.0%)REMARK number of reflections in working set: 10537 (91.5%)REMARK number of reflections in test set: 857 (7.4%)CRYST1 149.330 149.330 39.371 90.00 90.00 90.00 P 41 21 2REMARK FILENAME = “bindividual.pdb”REMARK DATE: 08-Aug-01 09:23:49REMARK VERSION: 1.0ATOM1CBMETA149−33.12275.969−56.4531.0041.57AATOM2CGMETA149−31.77376.431−55.9561.0039.81AATOM3SDMETA149−30.71377.256−57.1411.0032.34AATOM4CEMETA149−29.26076.531−56.6861.0039.03AATOM5CMETA149−35.44776.466−57.0481.0048.00AATOM6OMETA149−35.76376.754−58.1961.0049.15AATOM7NMETA149−34.47377.511−55.0301.0044.08AATOM8CAMETA149−34.20777.047−56.4231.0045.80AATOM9NASNA150−36.14175.634−56.2791.0050.82AATOM10CAASNA150−37.34674.969−56.7421.0052.03AATOM11CBASNA150−37.76273.906−55.7291.0052.70AATOM12CGASNA150−38.45972.725−56.3741.0054.27AATOM13OD1ASNA150−38.81171.759−55.7031.0056.34AATOM14ND2ASNA150−38.66072.796−57.6861.0053.74AATOM15CASNA150−38.49975.938−57.0071.0052.68AATOM16OASNA150−39.63975.522−57.1811.0055.34AATOM17NASPA151−38.20677.231−57.0291.0051.91AATOM18CAASPA151−39.22978.220−57.3281.0051.33AATOM19CBASPA151−39.18379.384−56.3281.0052.09AATOM20CGASPA151−39.60478.973−54.9301.0051.99AATOM21OD1ASPA151−40.42578.044−54.8311.0053.76AATOM22OD2ASPA151−39.13379.583−53.9401.0050.00AATOM23CASPA151−38.95678.744−58.7381.0050.85AATOM24OASPA151−39.76579.468−59.3161.0050.83AATOM25NPHEA152−37.81578.350−59.2931.0050.55AATOM26CAPHEA152−37.41578.805−60.6191.0051.05AATOM27CBPHEA152−36.12879.643−60.5331.0050.53AATOM28CGPHEA152−36.09580.596−59.3801.0049.74AATOM29CD1PHEA152−36.88581.730−59.3741.0048.38AATOM30CD2PHEA152−35.28880.332−58.2771.0051.27AATOM31CE1PHEA152−36.87682.589−58.2841.0049.17AATOM32CE2PHEA152−35.26881.182−57.1811.0049.87AATOM33CZPHEA152−36.06282.309−57.1821.0049.50AATOM34CPHEA152−37.17077.696−61.6381.0050.08AATOM35OPHEA152−36.80576.573−61.2871.0050.15AATOM36NASPA153−37.35878.059−62.9061.0049.19AATOM37CAASPA153−37.13877.185−64.0501.0047.34AATOM38CBASPA153−38.37577.153−64.9461.0046.91AATOM39CGASPA153−39.23275.934−64.6961.0047.34AATOM40OD1ASPA153−38.69574.822−64.8831.0047.91AATOM41OD2ASPA153−40.41976.075−64.3081.0046.26AATOM42CASPA153−35.95677.758−64.8171.0047.18AATOM43OASPA153−35.80478.972−64.9141.0048.16AATOM44NTYRA154−35.11876.884−65.3531.0045.64AATOM45CATYRA154−33.93777.306−66.0881.0043.40AATOM46CBTYRA154−32.80876.329−65.7991.0043.14AATOM47CGTYRA154−31.64076.382−66.7520.0040.46AATOM48CD1TYRA154−30.74677.454−66.7551.0041.17AATOM49CE1TYRA154−29.61077.429−67.5591.0039.92AATOM50CD2TYRA154−31.37375.309−67.5861.0040.00AATOM51CE2TYRA154−30.24775.283−68.3801.0039.95AATOM52CZTYRA154−29.37076.333−68.3550.0039.99AATOM53OHTYRA154−28.21176.231−69.0611.0039.63AATOM54CTYRA154−34.17977.395−67.5801.0043.66AATOM55OTYRA154−34.63876.439−68.1911.0044.55AATOM56NLEUA155−33.85578.545−68.1621.0044.30AATOM57CALEUA155−34.04478.773−69.5921.0044.60AATOM58CBLEUA155−34.84080.063−69.8231.0043.16AATOM59CGLEUA155−36.15580.228−69.0541.0040.74AATOM60CD1LEUA155−36.98681.300−69.7251.0040.57AATOM61CD2LEUA155−36.92078.926−69.0291.0038.72AATOM62CLEUA155−32.72078.833−70.3511.0045.07AATOM63OLEUA155−32.52478.097−71.3151.0044.89AATOM64NLYSA156−31.81379.711−69.9421.0046.46AATOM65CALYSA156−30.51579.774−70.6171.0047.97AATOM66CBLYSA156−30.61480.583−71.9181.0048.50AATOM67CGLYSA156−31.04982.031−71.7661.0050.02AATOM68CDLYSA156−30.69482.860−73.0091.0050.68AATOM69CELYSA156−31.28682.290−74.3011.0050.37AATOM70NZLYSA156−30.60881.038−74.7711.0049.95AATOM71CLYSA156−29.38680.338−69.7681.0047.79AATOM72OLYSA156−29.60580.795−68.6451.0046.87AATOM73NLEUA157−28.16880.279−70.2981.0047.58AATOM74CALEUA157−27.03580.847−69.5811.0047.46AATOM75CBLEUA157−25.71480.138−69.8971.0047.94AATOM76CGLEUA157−24.58680.672−68.9891.0047.41AATOM77CD1LEUA157−24.78780.142−67.5831.0046.53AATOM78CD2LEUA157−23.21080.264−69.5071.0047.40AATOM79CLEUA157−26.92982.278−70.0501.0047.03AATOM80OLEUA157−27.08982.556−71.2341.0046.03AATOM81NLEUA158−26.67883.186−69.1181.0047.66AATOM82CALEUA158−26.54384.588−69.4531.0048.86AATOM83CBLEUA158−27.61185.417−68.7281.0048.65AATOM84CGLEUA158−28.81685.910−69.5411.0048.13AATOM85CD1LEUA158−29.82886.568−68.6271.0047.43AATOM86CD2LEUA158−28.35186.900−70.5871.0047.99AATOM87CLEUA158−25.14985.075−69.0881.0050.00AATOM88OLEUA158−24.67286.056−69.6371.0051.27AATOM89NGLYA159−24.48584.382−68.1741.0051.99AATOM90CAGLYA159−23.14884.804−67.7881.0054.26AATOM91CGLYA159−22.40683.946−66.7721.0055.56AATOM92OGLYA159−22.95483.537−65.7521.0054.77AATOM93NLYSA160−21.14283.673−67.0601.0056.79AATOM94CALYSA160−20.31882.881−66.1611.0058.77AATOM95CBLYSA160−20.10581.468−66.7221.0059.06AATOM96CGLYSA160−21.38880.619−66.7691.0060.55AATOM97CDLYSA160−21.13779.170−67.2821.0060.33AATOM98CELYSA160−22.30878.198−66.9441.0058.20AATOM99NZLYSA160−22.19376.854−67.6151.0056.57AATOM100CLYSA160−18.98083.576−65.9421.0059.57AATOM101OLYSA160−18.60284.484−66.6791.0058.96AATOM102NGLYA161−18.27183.155−64.9071.0060.56AATOM103CAGLYA161−16.98783.759−64.6121.0061.18AATOM104CGLYA161−16.31283.045−63.4631.0060.79AATOM105OGLYA161−16.65481.903−63.1441.0060.23AATOM106NTHRA162−15.34683.716−62.8461.0060.89AATOM107CATHRA162−14.63883.129−61.7241.0061.12AATOM108CBTHRA162−13.31283.839−61.4751.0061.60AATOM109OG1THRA162−12.56783.870−62.6981.0062.30AATOM110CG2THRA162−12.50283.097−60.4031.0061.02AATOM111CTHRA162−15.49883.253−60.4831.0060.80AATOM112OTHRA162−15.84982.247−59.8551.0060.74AATOM113NPHEA163−15.84184.492−60.1391.0060.04AATOM114CAPHEA163−16.66884.749−58.9661.0059.38AATOM115CBPHEA163−16.37686.138−58.3881.0059.76AATOM116CGPHEA163−15.08286.225−57.6311.0059.50AATOM117CD1PHEA163−14.94987.111−56.5721.0059.24AATOM118CD2PHEA163−13.99285.444−57.9891.0059.94AATOM119CE1PHEA163−13.76187.223−55.8831.0059.00AATOM120CE2PHEA163−12.79385.550−57.3041.0060.58AATOM121CZPHEA163−12.67986.444−56.2461.0059.90AATOM122CPHEA163−18.16484.623−59.2281.0058.25AATOM123OPHEA163−18.91385.592−59.0861.0057.44AATOM124NGLYA164−18.59483.424−59.6111.0056.59AATOM125CAGLYA164−20.00483.207−59.8571.0053.58AATOM126CGLYA164−20.40782.857−61.2711.0050.76AATOM127OGLYA164−19.65182.255−62.0251.0050.72AATOM128NLYSA165−21.63083.244−61.6101.0048.90AATOM129CALYSA165−22.21382.996−62.9181.0047.11AATOM130CBLYSA165−22.28981.501−63.1761.0046.63AATOM131CGLYSA165−23.39280.810−62.3891.0046.17AATOM132CDLYSA165−23.31779.301−62.5041.0044.60AATOM133CELYSA165−23.17678.907−63.9391.0043.03AATOM134NZLYSA165−24.09679.748−64.7411.0041.76AATOM135CLYSA165−23.62683.559−62.8421.0046.26AATOM136OLYSA165−24.18183.676−61.7501.0047.67AATOM137NVALA166−24.20683.907−63.9841.0043.14AATOM138CAVALA166−25.56184.449−64.0181.0040.38AATOM139CBVALA166−25.56985.950−64.4891.0040.92AATOM140CG1VALA166−26.99586.420−64.7691.0039.28AATOM141CG2VALA166−24.93486.843−63.4141.0039.18AATOM142CVALA166−26.41683.604−64.9481.0037.94AATOM143OVALA166−25.97283.204−66.0131.0036.79AATOM144NILEA167−27.64483.329−64.5261.0036.83AATOM145CAILEA167−28.57082.523−65.3121.0035.64AATOM146CBILEA167−28.96181.213−64.5751.0035.37AATOM147CG2ILEA167−29.42380.176−65.5601.0034.94AATOM148CG1ILEA167−27.78080.613−63.8351.0034.93AATOM149CD1ILEA167−28.16779.382−63.0551.0033.89AATOM150CILEA167−29.88983.247−65.5961.0035.24AATOM151OILEA167−30.28084.178−64.9011.0033.88AATOM152NLEUA168−30.57082.795−66.6371.0035.11AATOM153CALEUA168−31.87783.314−66.9871.0035.36AATOM154CBLEUA168−31.99683.528−68.4941.0034.75AATOM155CGLEUA168−33.36683.975−69.0041.0034.38AATOM156CD1LEUA168−33.81285.260−68.3471.0032.36AATOM157CD2LEUA168−33.27184.153−70.5001.0035.39AATOM158CLEUA168−32.83682.209−66.5241.0035.95AATOM159OLEUA168−32.77781.079−67.0061.0035.39AATOM160NVALA169−33.70182.541−65.5731.0036.20AATOM161CAVALA169−34.64481.586−65.0141.0035.94AATOM162CBVALA169−34.19281.153−63.5901.0035.90AATOM163CG1VALA169−32.73880.690−63.6251.0034.70AATOM164CG2VALA169−34.34182.321−62.5941.0033.08AATOM165CVALA169−36.03682.205−64.9291.0036.81AATOM166OVALA169−36.24083.336−65.3481.0036.80AATOM167NARGA170−36.98981.452−64.3911.0038.62AATOM168CAARGA170−38.35681.932−64.2221.0041.59AATOM169CBARGA170−39.31381.175−65.1231.0041.05AATOM170CGARGA170−39.16381.373−66.6071.0041.93AATOM171CDARGA170−40.37880.720−67.2521.0041.73AATOM172NEARGA170−40.21480.387−68.6621.0041.15AATOM173CZARGA170−40.90079.413−69.2501.0040.13AATOM174NH1ARGA170−41.75978.714−68.5201.0038.96AATOM175NH2ARGA170−40.75379.153−70.5461.0038.13AATOM176CARGA170−38.80081.686−62.7831.0044.40AATOM177OARGA170−38.00281.285−61.9421.0046.61AATOM178NGLUA171−40.07781.928−62.5061.0045.48AATOM179CAGLUA171−40.64081.682−61.1821.0046.88AATOM180CBGLUA171−41.08382.992−60.5351.0045.05AATOM181CGGLUA171−41.85282.821−59.2341.0044.74AATOM182CDGLUA171−41.59183.945−58.2531.0043.50AATOM183OE1GLUA171−41.50285.109−58.6971.0042.40AATOM184OE2GLUA171−41.48083.663−57.0401.0041.55AATOM185CGLUA171−41.82980.754−61.4161.0048.84AATOM186OGLUA171−42.91381.204−61.7661.0050.30AATOM187NLYSA172−41.60679.457−61.2331.0050.01AATOM188CALYSA172−42.61678.423−61.4701.0052.21AATOM189CBLYSA172−42.21777.130−60.7471.0052.80AATOM190CGLYSA172−41.12876.319−61.4471.0052.82AATOM191CDLYSA172−40.66475.147−60.5921.0052.49AATOM192CELYSA172−39.54274.371−61.2721.0053.23AATOM193NZLYSA172−39.02773.244−60.4321.0054.40AATOM194CLYSA172−44.08778.707−61.1771.0053.85AATOM195OLYSA172−44.94777.914−61.5661.0054.79AATOM196NALAA173−44.39279.816−60.5101.0054.56AATOM197CAALAA173−45.78280.127−60.1831.0054.27AATOM198CBALAA173−45.99780.000−58.6781.0053.96AATOM199CALAA173−46.23181.504−60.6551.0054.12AATOM200OALAA173−47.41081.836−60.5761.0053.43AATOM201NTHRA174−45.29282.295−61.1611.0053.53AATOM202CATHRA174−45.60483.640−61.6171.0051.68AATOM203CBTHRA174−44.95884.692−60.6951.0050.61AATOM204OG1THRA174−43.53384.639−60.8330.0051.12AATOM205CG2THRA174−45.33184.428−59.2430.0051.12AATOM206CTHRA174−45.16283.925−63.0481.0051.48AATOM207OTHRA174−45.57884.918−63.6301.0052.45AATOM208NGLYA175−44.31883.070−63.6181.0050.81AATOM209CAGLYA175−43.86383.300−64.9811.0050.84AATOM210CGLYA175−43.14184.624−65.2001.0051.27AATOM211OGLYA175−42.82784.990−66.3271.0051.55AATOM212NARGA176−42.88385.350−64.1211.0051.58AATOM213CAARGA176−42.18186.624−64.1891.0052.10AATOM214CBARGA176−42.43387.390−62.8821.0052.63AATOM215CGARGA176−41.72488.736−62.7321.0052.82AATOM216CDARGA176−42.15789.432−61.4281.0052.17AATOM217NEARGA176−43.18290.451−61.6591.0051.02AATOM218CZARGA176−43.92391.009−60.7031.0050.91AATOM219NH1ARGA176−43.77090.648−59.4361.0050.44AATOM220NH2ARGA176−44.81391.940−61.0161.0048.56AATOM221CARGA176−40.68886.310−64.3841.0052.83AATOM222OARGA176−40.21085.275−63.9131.0053.10AATOM223NTYRA177−39.95587.188−65.0771.0052.76AATOM224CATYRA177−38.52786.956−65.3391.0050.54AATOM225CBTYRA177−38.16787.324−66.7721.0048.93AATOM226CGTYRA177−38.69986.366−67.7891.0048.99AATOM227CD1TYRA177−39.67186.768−68.6891.0049.82AATOM228CE1TYRA177−40.19885.893−69.6221.0049.26AATOM229CD2TYRA177−38.25085.050−67.8451.0049.34AATOM230CE2TYRA177−38.76884.161−68.7791.0047.95AATOM231CZTYRA177−39.74684.599−69.6611.0047.44AATOM232OHTYRA177−40.29483.757−70.5831.0046.98AATOM233CTYRA177−37.51587.632−64.4331.0049.87AATOM234OTYRA177−37.74588.714−63.8991.0049.64AATOM235NTYRA178−36.37686.963−64.2881.0049.12AATOM236CATYRA178−35.27187.436−63.4731.0047.33AATOM237CBTYRA178−35.45187.049−62.0031.0049.56AATOM238CGTYRA178−36.82787.256−61.4321.0051.23AATOM239CD1TYRA178−37.86086.370−61.7231.0053.31AATOM240CE1TYRA178−39.12086.545−61.1901.0053.33AATOM241CD2TYRA178−37.09688.323−60.5941.0050.67AATOM242CE2TYRA178−38.34788.504−60.0591.0051.62AATOM243CZTYRA178−39.35787.612−60.3531.0052.88AATOM244OHTYRA178−40.59987.757−59.7721.0055.62AATOM245CTYRA178−33.98086.796−63.9601.0045.27AATOM246OTYRA178−33.98985.747−64.6021.0042.18AATOM247NALAA179−32.87287.446−63.6301.0043.82AATOM248CAALAA179−31.54786.975−63.9841.0043.28AATOM249CBALAA179−30.75288.104−64.6261.0043.85AATOM250CALAA179−30.91486.558−62.6671.0042.16AATOM251OALAA179−30.59287.410−61.8501.0043.31AATOM252NMETA180−30.75185.253−62.4581.0040.86AATOM253CAMETA180−30.18584.733−61.2111.0040.26AATOM254CBMETA180−30.83283.391−60.8631.0039.84AATOM255CGMETA180−29.92282.436−60.1091.0038.62AATOM256SDMETA180−30.77581.338−58.9711.0038.70AATOM257CEMETA180−31.92080.493−60.0371.0035.83AATOM258CMETA180−28.66884.591−61.1451.0039.94AATOM259OMETA180−28.05583.835−61.8991.0039.52AATOM260NLYSA181−28.07185.315−60.2091.0038.57AATOM261CALYSA181−26.63185.285−60.0341.0038.78AATOM262CBLYSA181−26.11786.667−59.6121.0041.30AATOM263CGLYSA181−24.59786.768−59.5011.0041.79AATOM264CDLYSA181−24.17387.958−58.6521.0042.77AATOM265CELYSA181−24.68389.247−59.2281.0044.50AATOM266NZLYSA181−24.04789.504−60.5431.0046.45AATOM267CLYSA181−26.25984.264−58.9771.0037.44AATOM268OLYSA181−26.64684.390−57.8251.0036.11AATOM269NILEA182−25.50683.252−59.3831.0036.93AATOM270CAILEA182−25.07182.214−58.4621.0037.57AATOM271CBILEA182−25.49180.787−58.9391.0036.60AATOM272CG2ILEA182−25.53779.838−57.7561.0033.85AATOM273CG1ILEA182−26.87480.826−59.5951.0036.23AATOM274CD1ILEA182−27.43579.471−59.9451.0034.13AATOM275CILEA182−23.55182.263−58.3531.0038.41AATOM276OILEA182−22.84181.945−59.2971.0038.20AATOM277NLEUA183−23.05982.696−57.2041.0039.83AATOM278CALEUA183−21.62982.762−56.9761.0042.27AATOM279CBLEUA183−21.25484.014−56.1861.0040.30AATOM280CGLEUA183−22.20385.202−56.1161.0037.57AATOM281CD1LEUA183−21.70586.182−55.0771.0035.14AATOM282CD2LEUA183−22.29585.847−57.4651.0036.20AATOM283CLEUA183−21.36681.555−56.1021.0045.16AATOM284OLEUA183−22.28881.054−55.4681.0045.96AATOM285NARGA184−20.12081.098−56.0501.0048.36AATOM286CAARGA184−19.78179.949−55.2181.0051.03AATOM287CBARGA184−18.69279.116−55.8991.0051.26AATOM288CGARGA184−19.11278.584−57.2491.0052.11AATOM289CDARGA184−17.92778.342−58.1701.0053.15AATOM290NEARGA184−18.38278.278−59.5621.0054.88AATOM291CZARGA184−18.95377.210−60.1271.0054.67AATOM292NH1ARGA184−19.13376.093−59.4231.0053.05AATOM293NH2ARGA184−19.36477.269−61.3931.0053.05AATOM294CARGA184−19.32680.370−53.8151.0051.71AATOM295OARGA184−18.13680.490−53.5441.0051.78AATOM296NLYSA185−20.29180.612−52.9341.0053.52AATOM297CALYSA185−20.01080.998−51.5531.0055.78AATOM298CBLYSA185−21.17580.593−50.6511.0054.52AATOM299CGLYSA185−20.86680.567−49.1661.0051.97AATOM300CDLYSA185−21.79779.603−48.4241.0050.42AATOM301CELYSA185−23.26879.917−48.6701.0048.41AATOM302NZLYSA185−24.19179.115−47.8111.0045.97AATOM303CLYSA185−18.77680.238−51.1311.0057.59AATOM304OLYSA185−17.78580.820−50.6851.0057.98AATOM305NGLUA186−18.86978.922−51.3021.0059.79AATOM306CAGLUA186−17.81377.971−50.9721.0060.74AATOM307CBGLUA186−18.06576.650−51.7051.0058.76AATOM308CGGLUA186−17.10275.543−51.3451.0058.03AATOM309CDGLUA186−17.31275.026−49.9390.0057.11AATOM310OE1GLUA186−16.53774.150−49.5010.0057.26AATOM311OE2GLUA186−18.25775.494−49.2731.0055.43AATOM312CGLUA186−16.43178.495−51.3441.0062.32AATOM313OGLUA186−15.77879.193−50.5601.0061.63AATOM314NVALA187−15.99278.163−52.5511.0063.85AATOM315CAVALA187−14.67878.587−52.9921.0064.76AATOM316CBVALA187−14.34078.038−54.4161.0065.26AATOM317CG1VALA187−14.06176.522−54.3251.0063.82AATOM318CG2VALA187−15.48278.315−55.3951.0064.58AATOM319CVALA187−14.47180.091−52.9321.0065.28AATOM320OVALA187−13.34780.546−53.0701.0065.80AATOM321NILEA188−15.53480.861−52.7031.0065.89AATOM322CAILEA188−15.39182.318−52.5981.0066.91AATOM323CBILEA188−16.69883.064−52.9721.0067.17AATOM324CG2ILEA188−16.91384.267−52.0491.0066.41AATOM325CG1ILEA188−16.62883.512−54.4411.0067.59AATOM326CD1ILEA188−15.41584.421−54.7921.0065.98AATOM327CILEA188−14.93282.764−51.2021.0067.30AATOM328OILEA188−14.44383.889−51.0331.0067.01AATOM329NILEA189−15.10481.886−50.2101.0066.94AATOM330CAILEA189−14.66082.166−48.8461.0065.50AATOM331CBILEA189−15.01481.031−47.8681.0063.89AATOM332CG2ILEA189−14.31381.254−46.5471.0062.84AATOM333CG1ILEA189−16.52080.936−47.6661.0063.52AATOM334CD1ILEA189−16.92479.812−46.7051.0062.06AATOM335CILEA189−13.14782.178−48.9421.0066.75AATOM336OILEA189−12.46582.909−48.2221.0066.52AATOM337NALAA190−12.64581.345−49.8551.0068.03AATOM338CAALAA190−11.21481.183−50.0891.0069.25AATOM339CBALAA190−10.86979.696−50.1081.0069.48AATOM340CALAA190−10.72081.847−51.3751.0069.13AATOM341OALAA190−9.86281.297−52.0751.0068.80AATOM342NLYSA191−11.25783.023−51.6841.0068.08AATOM343CALYSA191−10.85183.747−52.8811.0068.08AATOM344CBLYSA191−11.95083.681−53.9451.0067.83AATOM345CGLYSA191−11.93982.365−54.7171.0066.64AATOM346CDLYSA191−13.27882.051−55.3591.0064.94AATOM347CELYSA191−13.26480.658−55.9811.0063.39AATOM348NZLYSA191−14.45980.412−56.8551.0062.03AATOM349CLYSA191−10.56285.172−52.4801.0067.99AATOM350OLYSA191−10.60886.105−53.2871.0068.39AATOM351NASPA192−10.27185.316−51.1961.0068.39AATOM352CAASPA192−9.93986.593−50.5961.0068.75AATOM353CBASPA192−8.51686.968−50.9831.0069.38AATOM354CGASPA192−7.52785.928−50.5331.0069.87AATOM355OD1ASPA192−7.74485.385−49.4201.0069.31AATOM356OD2ASPA192−6.55285.657−51.2741.0070.22AATOM357CASPA192−10.86987.763−50.8441.0067.98AATOM358OASPA192−10.50988.900−50.5531.0069.16AATOM359NGLUA193−12.05987.504−51.3721.0066.63AATOM360CAGLUA193−13.00788.585−51.5931.0065.37AATOM361CBGLUA193−13.36088.726−53.0741.0062.79AATOM362CGGLUA193−12.39889.623−53.8321.0059.71AATOM363CDGLUA193−13.10690.528−54.8231.0058.50AATOM364OE1GLUA193−12.81190.413−56.0361.0057.60AATOM365OE2GLUA193−13.95191.354−54.3831.0054.02AATOM366CGLUA193−14.26788.396−50.7631.0065.86AATOM367OGLUA193−15.38488.491−51.2641.0065.15AATOM368NVALA194−14.07188.129−49.4771.0066.94AATOM369CAVALA194−15.19187.950−48.5701.0067.58AATOM370CBVALA194−14.71087.716−47.1051.0067.57AATOM371CG1VALA194−15.32186.417−46.5511.0065.78AATOM372CG2VALA194−13.18487.664−47.0531.0066.34AATOM373CVALA194−16.09189.190−48.6181.0068.02AATOM374OVALA194−16.79689.404−49.6021.0067.33AATOM375NALAA195−16.04190.010−47.5701.0068.20AATOM376CAALAA195−16.87291.216−47.4671.0069.06AATOM377CBALAA195−16.35992.100−46.3111.0069.49AATOM378CALAA195−17.05792.071−48.7341.0068.86AATOM379OALAA195−18.16492.554−49.0021.0068.15AATOM380NHISA196−15.98792.276−49.5001.0068.70AATOM381CAHISA196−16.07193.083−50.7191.0069.07AATOM382CBHISA196−14.69393.198−51.3711.0071.05AATOM383CGHISA196−13.72594.056−50.6151.0072.47AATOM384CD2HISA196−12.65193.731−49.8561.0072.84AATOM385ND1HISA196−13.79895.432−50.6071.0072.65AATOM386CE1HISA196−12.81095.918−49.8771.0072.90AATOM387NE2HISA196−12.09994.907−49.4101.0073.11AATOM388CHISA196−17.03992.460−51.7211.0068.13AATOM389OHISA196−17.38093.071−52.7341.0066.34AATOM390NTHRA197−17.45691.230−51.4261.0067.28AATOM391CATHRA197−18.37490.467−52.2651.0066.08AATOM392CBTHRA197−17.71389.150−52.7381.0066.62AATOM393OG1THRA197−16.45389.451−53.3461.0067.62AATOM394CG2THRA197−18.57488.437−53.7611.0067.49AATOM395CTHRA197−19.62290.161−51.4451.0065.19AATOM396OTHRA197−20.54189.482−51.8991.0063.58AATOM397NVALA198−19.62790.659−50.2141.0065.19AATOM398CAVALA198−20.76390.499−49.3191.0064.81AATOM399CBVALA198−20.33690.441−47.8351.0063.54AATOM400CG1VALA198−21.55790.500−46.9521.0062.91AATOM401CG2VALA198−19.57589.163−47.5481.0062.42AATOM402CVALA198−21.57191.768−49.5401.0066.34AATOM403OVALA198−22.70891.721−50.0171.0066.25AATOM404NTHRA199−20.95292.902−49.2131.0066.72AATOM405CATHRA199−21.57294.216−49.3671.0066.80AATOM406CBTHRA199−20.50395.310−49.4711.0066.00AATOM407OG1THRA199−19.37894.957−48.6541.0063.44AATOM408CG2THRA199−21.06796.632−48.9861.0065.21AATOM409CTHRA199−22.44594.240−50.6201.0067.92AATOM410OTHRA199−23.62594.612−50.5671.0067.59AATOM411NGLUA200−21.85693.833−51.7431.0068.85AATOM412CAGLUA200−22.57193.756−53.0171.0069.27AATOM413CBGLUA200−21.88092.753−53.9601.0069.46AATOM414CGGLUA200−22.75792.311−55.1331.0069.97AATOM415CDGLUA200−22.83090.792−55.3071.0070.34AATOM416OE1GLUA200−23.19890.079−54.3451.0069.12AATOM417OE2GLUA200−22.53290.314−56.4231.0071.08AATOM418CGLUA200−23.99893.282−52.7511.0068.62AATOM419OGLUA200−24.94993.756−53.3651.0067.85AATOM420NSERA201−24.12592.337−51.8261.0068.47AATOM421CASERA201−25.41691.773−51.4671.0069.83AATOM422CBSERA201−25.23790.415−50.7991.0069.46AATOM423OGSERA201−26.42790.062−50.1051.0069.45AATOM424CSERA201−26.23592.635−50.5271.0070.17AATOM425OSERA201−27.45592.759−50.6881.0071.51AATOM426NARGA202−25.56293.199−49.5271.0069.38AATOM427CAARGA202−26.22394.021−48.5281.0068.27AATOM428CBARGA202−25.19894.516−47.5041.0069.10AATOM429CGARGA202−24.50493.396−46.7321.0069.21AATOM430CDARGA202−25.41292.780−45.6791.0069.20AATOM431NEARGA202−24.94191.464−45.2541.0070.05AATOM432CZARGA202−23.82991.235−44.5621.0070.53AATOM433NH1ARGA202−23.04992.242−44.1951.0071.39AATOM434NH2ARGA202−23.48789.990−44.2471.0070.02AATOM435CARGA202−26.94795.203−49.1591.0067.39AATOM436OARGA202−28.04295.583−48.7311.0066.26AATOM437NVALA203−26.36395.770−50.2021.0066.06AATOM438CAVALA203−27.00396.922−50.8061.0065.47AATOM439CBVALA203−26.01898.085−50.8351.0063.69AATOM440CG1VALA203−26.77599.408−51.0031.0062.35AATOM441CG2VALA203−25.23298.071−49.5361.0061.10AATOM442CVALA203−27.66996.702−52.1741.0065.54AATOM443OVALA203−28.62897.400−52.5081.0066.36AATOM444NLEUA204−27.18495.745−52.9581.0064.28AATOM445CALEUA204−27.82695.461−54.2311.0063.96AATOM446CBLEUA204−27.28194.146−54.8151.0066.28AATOM447CGLEUA204−28.03193.292−55.8591.0067.36AATOM448CD1LEUA204−28.35894.077−57.1331.0066.35AATOM449CD2LEUA204−27.15992.087−56.1881.0067.07AATOM450CLEUA204−29.32895.341−53.9491.0063.04AATOM451OLEUA204−30.15795.596−54.8251.0062.93AATOM452NGLNA205−29.67094.973−52.7131.0062.12AATOM453CAGLNA205−31.07594.823−52.3121.0060.78AATOM454CBGLNA205−31.21793.700−51.2681.0061.18AATOM455CGGLNA205−31.14194.128−49.8051.0061.58AATOM456CDGLNA205−32.49794.033−49.1001.0061.72AATOM457OE1GLNA205−32.62594.380−47.9171.0060.53AATOM458NE2GLNA205−33.51493.561−49.8261.0059.94AATOM459CGLNA205−31.71096.121−51.7861.0059.08AATOM460OGLNA205−32.91696.298−51.8841.0058.87AATOM461NASNA206−30.89297.013−51.2311.0057.04AATOM462CAASNA206−31.35698.303−50.7141.0055.33AATOM463CBASNA206−30.45298.773−49.5741.0055.76AATOM464CGASNA206−30.88698.252−48.2211.0054.49AATOM465OD1ASNA206−31.57998.941−47.4601.0052.73AATOM466ND2ASNA206−30.47997.031−47.9111.0054.14AATOM467CASNA206−31.27299.318−51.8521.0053.75AATOM468OASNA206−32.126100.202−52.0111.0053.90AATOM469NTHRA207−30.19699.192−52.6161.0051.29AATOM470CATHRA207−29.940100.037−53.7631.0048.01AATOM471CBTHRA207−28.63099.591−54.4641.0045.91AATOM472OG1THRA207−27.533100.326−53.9101.0044.17AATOM473CG2THRA207−28.69199.791−55.9641.0044.96AATOM474CTHRA207−31.12799.883−54.6871.0047.31AATOM475OTHRA207−31.21398.919−55.4441.0048.96AATOM476NARGA208−32.065100.816−54.5971.0045.32AATOM477CAARGA208−33.247100.764−55.4431.0044.91AATOM478CBARGA208−34.480100.402−54.6071.0044.62AATOM479CGARGA208−34.49698.948−54.0971.0046.51AATOM480CDARGA208−35.46898.036−54.8671.0047.18AATOM481NEARGA208−35.66496.753−54.1781.0048.87AATOM482GZARGA208−36.48695.773−54.5791.0049.41AATOM483NH1ARGA208−37.22695.900−55.6821.0047.51AATOM484NH2ARGA208−36.54394.636−53.8881.0047.45AATOM485CARGA208−33.469102.075−56.2041.0043.71AATOM486OARGA208−33.923103.079−55.6531.0045.29AATOM487NHISA209−33.140102.050−57.4881.0041.05AATOM488CAHISA209−33.291103.213−58.3331.0037.67AATOM489CBHISA209−31.922103.786−58.6241.0036.08AATOM490CGHISA209−31.957105.160−59.1991.0036.05AATOM491CD2HISA209−31.571106.348−58.6821.0036.46AATOM492ND1HISA209−32.424105.423−60.4641.0035.06AATOM493CE1HISA209−32.321106.716−60.7061.0038.25AATOM494NE2HISA209−31.805107.299−59.6411.0037.40AATOM495CHISA209−33.968102.781−59.6191.0036.00AATOM496OHISA209−33.756101.663−60.0731.0036.98AATOM497NPROA210−34.807103.653−60.2131.0034.34AATOM498CDPROA210−35.258104.936−59.6471.0034.21AATOM499CAPROA210−35.535103.384−61.4561.0032.85AATOM500CBPROA210−36.115104.744−61.8021.0031.55AATOM501CGPROA210−36.480105.244−60.4801.0031.88AATOM502CPROA210−34.743102.785−62.6061.0031.89AATOM503OPROA210−35.293102.044−63.4111.0031.56AATOM504NPHEA211−33.457103.100−62.6791.0030.98AATOM505CAPHEA211−32.616102.590−63.7501.0030.28AATOM506CBPHEA211−31.855103.747−64.3901.0029.32AATOM507CGPHEA211−32.743104.900−64.7841.0027.81AATOM508CD1PHEA211−33.840104.697−65.6161.0026.67AATOM509CD2PHEA211−32.511106.179−64.2881.0026.15AATOM510CE1PHEA211−34.675105.743−65.9301.0025.33AATOM511CE2PHEA211−33.351107.227−64.6061.0023.91AATOM512CZPHEA211−34.426107.014−65.4191.0023.11AATOM513CPHEA211−31.652101.506−63.2911.0030.43AATOM514OPHEA211−31.164100.735−64.0991.0030.84AATOM515NLEUA212−31.377101.452−61.9921.0030.56AATOM516CALEUA212−30.484100.437−61.4501.0031.26AATOM517CBLEUA212−29.911100.876−60.0981.0031.17AATOM518CGLEUA212−28.721101.844−60.2351.0031.98AATOM519CD1LEUA212−28.476102.553−58.9301.0030.89AATOM520CD2LEUA212−27.471101.084−60.7031.0029.63AATOM521CLEUA212−31.31399.191−61.3051.0030.74AATOM522OLEUA212−32.47299.280−60.9311.0031.25AATOM523NTHRA213−30.73598.035−61.6151.0030.78AATOM524CATHRA213−31.47196.785−61.5441.0031.45AATOM525CBTHRA213−30.67095.657−62.1671.0031.33AATOM526OG1THRA213−30.13196.097−63.4161.0030.27AATOM527CG2THRA213−31.56894.452−62.4161.0031.83AATOM528CTHRA213−31.83696.414−60.1181.0032.46AATOM529OTHRA213−30.97896.374−59.2361.0033.33AATOM530NALAA214−33.11496.136−59.8941.0033.86AATOM531CAALAA214−33.58995.805−58.5581.0035.77AATOM532CBALAA214−35.06196.188−58.4001.0035.44AATOM533CALAA214−33.40994.353−58.2431.0037.09AATOM534OALAA214−33.47093.509−59.1191.0038.14AATOM535NLEUA215−33.18394.077−56.9721.0039.49AATOM536CALEUA215−33.01092.722−56.4861.0042.45AATOM537CBLEUA215−31.89792.697−55.4461.0042.72AATOM538CGLEUA215−31.88891.514−54.4921.0043.40AATOM539CD1LEUA215−32.05190.237−55.2741.0045.35AATOM540CD2LEUA215−30.59091.511−53.7091.0043.94AATOM541CLEUA215−34.32192.304−55.8501.0044.19AATOM542OLEUA215−34.81292.989−54.9521.0044.78AATOM543NLYSA216−34.90091.201−56.3151.0046.18AATOM544CALYSA216−36.16690.735−55.7511.0048.67AATOM545CBLYSA216−36.85989.819−56.7461.0048.50AATOM546CGLYSA216−37.20590.520−58.0311.0051.05AATOM547CDLYSA216−38.41391.434−57.8691.0051.75AATOM548CELYSA216−38.77992.107−59.1911.0050.82AATOM549NZLYSA216−40.05692.858−59.0691.0049.52AATOM550CLYSA216−35.95090.021−54.4081.0049.81AATOM551OLYSA216−36.67590.257−53.4311.0049.27AATOM552NTYRA217−34.94189.157−54.3691.0050.73AATOM553CATYRA217−34.58888.430−53.1631.0052.36AATOM554CBTYRA217−35.76687.590−52.6521.0054.56AATOM555CGTYRA217−36.52886.787−53.6831.0055.56AATOM556CD1TYRA217−37.83186.359−53.4161.0057.36AATOM557CE1TYRA217−38.55985.610−54.3401.0057.83AATOM558CD2TYRA217−35.96486.445−54.9071.0055.19AATOM559CE2TYRA217−36.68485.694−55.8441.0056.62AATOM560CZTYRA217−37.98285.279−55.5511.0057.77AATOM561OHTYRA217−38.70884.525−56.4521.0057.86AATOM562CTYRA217−33.36987.554−53.3531.0052.04AATOM563OTYRA217−33.12787.033−54.4321.0052.56AATOM564NALAA218−32.59287.414−52.2901.0051.08AATOM565CAALAA218−31.39386.600−52.3311.0050.68AATOM566CBALAA218−30.19987.469−52.0871.0051.45AATOM567CALAA218−31.46585.512−51.2691.0050.45AATOM568OALAA218−31.64585.807−50.0961.0050.53AATOM569NPHEA219−31.33784.255−51.6711.0050.36AATOM570CAPHEA219−31.37383.184−50.6951.0051.82AATOM571CBPHEA219−32.35482.086−51.1191.0053.27AATOM572CGPHEA219−32.18181.606−52.5271.0054.08AATOM573CD1PHEA219−32.60982.379−53.5951.0055.73AATOM574CD2PHEA219−31.63880.353−52.7811.0054.53AATOM575CE1PHEA219−32.50781.907−54.9031.0057.06AATOM576CE2PHEA219−31.52979.872−54.0721.0055.44AATOM577CZPHEA219−31.96680.648−55.1411.0056.54AATOM578CPHEA219−29.99482.586−50.3891.0052.37AATOM579OPHEA219−28.99183.302−50.3751.0052.39AATOM580NGLNA220−29.94281.284−50.1291.0053.26AATOM581CAGLNA220−28.67380.639−49.8011.0054.94AATOM582CBGLNA220−28.45380.665−48.2821.0056.53AATOM583CGGLNA220−28.70482.003−47.5851.0059.25AATOM584CDGLNA220−27.47082.902−47.5241.0060.67AATOM585OE1GLNA220−26.37882.461−47.1011.0060.21AATOM586NE2GLNA220−27.63784.179−47.9311.0057.63AATOM587CGLNA220−28.55979.183−50.2711.0054.81AATOM588OGLNA220−29.50978.590−50.7631.0054.81AATOM589NTHRA221−27.36478.632−50.0901.0054.74AATOM590CATHRA221−27.00077.252−50.4171.0054.03AATOM591CBTHRA221−26.77177.043−51.9721.0054.42AATOM592OG1THRA221−27.94476.463−52.5501.0053.92AATOM593CG2THRA221−25.57776.110−52.2791.0052.97AATOM594CTHRA221−25.68677.081−49.6611.0053.41AATOM595OTHRA221−24.74577.813−49.9431.0054.69AATOM596NHISA222−25.63276.169−48.6841.0051.78AATOM597CAHISA222−24.40475.911−47.8981.0050.07AATOM598CBHISA222−24.41474.515−47.2521.0053.13AATOM599CGHISA222−24.78874.504−45.8041.0055.35AATOM600CD2HISA222−25.23373.501−45.0091.0056.31AATOM601ND1HISA222−24.65475.608−44.9901.0055.97AATOM602CE1HISA222−24.99975.286−43.7551.0056.19AATOM603NE2HISA222−25.35374.013−43.7401.0057.22AATOM604CHISA222−23.17175.973−48.7801.0046.06AATOM605OHISA222−22.04975.997−48.2961.0044.34AATOM606NASPA223−23.40176.003−50.0811.0042.83AATOM607CAASPA223−22.33376.036−51.0461.0040.84AATOM608CBASPA223−22.41874.743−51.8541.0042.11AATOM609CGASPA223−21.23174.530−52.7361.0041.53AATOM610OD1ASPA223−21.37374.719−53.9711.0041.16AATOM611OD2ASPA223−20.16574.178−52.1791.0040.46AATOM612CASPA223−22.32877.262−51.9791.0039.06AATOM613OASPA223−21.33677.511−52.6521.0038.32AATOM614NARGA224−23.41478.033−52.0241.0037.35AATOM615CAARGA224−23.46679.193−52.9161.0035.45AATOM616CBARGA224−23.83178.755−54.3331.0034.31AATOM617CGARGA224−22.89777.708−54.8551.0032.43AATOM618CDARGA224−23.15477.302−56.2611.0030.11AATOM619NEARGA224−22.23776.212−56.5681.0029.45AATOM620CZARGA224−21.94575.788−57.7871.0029.32AATOM621NH1ARGA224−22.48976.350−58.8631.0028.21AATOM622NH2ARGA224−21.09074.798−57.9251.0029.74AATOM623CARGA224−24.41580.283−52.4961.0034.18AATOM624OARGA224−25.24480.082−51.6301.0034.36AATOM625NLEUA225−24.27481.447−53.1211.0034.49AATOM626CALEUA225−25.12782.603−52.8341.0034.86AATOM627CBLEUA225−24.27983.820−52.4151.0034.45AATOM628CGLEUA225−23.42883.696−51.1431.0034.20AATOM629CD1LEUA225−22.56184.903−50.9961.0032.85AATOM630CD2LEUA225−24.31583.543−49.9221.0033.81AATOM631CLEUA225−25.92482.928−54.0951.0034.83AATOM632OLEUA225−25.35083.164−55.1551.0034.55AATOM633NCYSA226−27.24582.935−53.9741.0034.97AATOM634CACYSA226−28.09783.198−55.1161.0035.79AATOM635CBCYSA226−29.10282.064−55.2851.0036.99AATOM636SGCYSA226−28.37480.414−55.2131.0040.23AATOM637CCYSA226−28.84684.514−55.0301.0035.90AATOM638OCYSA226−29.58784.768−54.0831.0036.05AATOM639NPHEA227−28.65385.335−56.0551.0035.75AATOM640CAPHEA227−29.29486.635−56.1651.0033.68AATOM641CBPHEA227−28.24087.746−56.2921.0032.87AATOM642CGPHEA227−27.25987.775−55.1611.0030.58AATOM643CD1PHEA227−25.94387.419−55.3591.0030.80AATOM644CD2PHEA227−27.67288.101−53.8801.0028.54AATOM645CE1PHEA227−25.06487.387−54.2991.0030.44AATOM646CE2PHEA227−26.80188.069−52.8241.0026.58AATOM647CZPHEA227−25.49887.710−53.0311.0029.42AATOM648CPHEA227−30.17986.640−57.3931.0033.39AATOM649OPHEA227−29.69386.616−58.5221.0033.00AATOM650NVALA228−31.48386.649−57.1701.0032.74AATOM651CAVALA228−32.42786.688−58.2731.0032.72AATOM652CBVALA228−33.71185.891−57.9331.0030.83AATOM653CG1VALA228−34.58385.757−59.1521.0028.11AATOM654CG2VALA228−33.33684.513−57.4031.0028.93AATOM655CVALA228−32.73588.168−58.4781.0034.22AATOM656OVALA228−33.30088.816−57.6021.0034.89AATOM657NMETA229−32.33388.700−59.6301.0035.98AATOM658CAMETA229−32.53390.115−59.9561.0037.87AATOM659CBMETA229−31.19690.736−60.3801.0038.28AATOM660CGMETA229−30.04690.401−59.4561.0041.11AATOM661SDMETA229−28.40390.651−60.1911.0047.29AATOM662CEMETA229−28.05889.073−60.9031.0043.74AATOM663CMETA229−33.56190.338−61.0721.0037.89AATOM664OMETA229−33.74189.495−61.9421.0037.51AATOM665NGLUA230−34.23591.482−61.0471.0039.52AATOM666CAGLUA230−35.20391.792−62.0871.0041.39AATOM667CBGLUA230−35.85993.151−61.8471.0042.98AATOM668CGGLUA230−34.85694.304−61.8361.0048.22AATOM669CDGLUA230−35.38995.606−62.4491.0052.74AATOM670OE1GLUA230−35.74195.615−63.6591.0052.91AATOM671OE2GLUA230−35.44196.624−61.7171.0053.57AATOM672CGLUA230−34.38891.852−63.3661.0042.15AATOM673OGLUA230−33.41392.604−63.4561.0041.51AATOM674NTYRA231−34.77691.048−64.3491.0043.05AATOM675CATYRA231−34.08191.021−65.6321.0043.46AATOM676CBTYRA231−33.91289.554−66.0661.0044.83AATOM677CGTYRA231−34.06089.274−67.5381.0047.32AATOM678CD1TYRA231−33.03689.556−68.4421.0047.92AATOM679CE1TYRA231−33.20189.330−69.8101.0048.98AATOM680CD2TYRA231−35.24788.754−68.0331.0049.05AATOM681CE2TYRA231−35.42588.525−69.3891.0051.23AATOM682CZTYRA231−34.40988.816−70.2771.0050.72AATOM683OHTYRA231−34.64788.622−71.6241.0052.16AATOM684CTYRA231−34.80291.854−66.7051.0042.58AATOM685OTYRA231−35.98491.646−66.9761.0042.89AATOM686NALAA232−34.08892.814−67.2901.0042.00AATOM687CAALAA232−34.63793.653−68.3561.0041.81AATOM688CBALAA232−33.52794.416−69.0541.0041.02AATOM689CALAA232−35.34492.749−69.3511.0042.16AATOM690OALAA232−35.27091.537−69.2441.0043.74AATOM691NASNA233−36.00893.323−70.3431.0043.23AATOM692CAASNA233−36.75392.492−71.2881.0043.75AATOM693CBASNA233−38.20292.344−70.7961.0045.51AATOM694CGASNA233−38.85391.048−71.2371.0046.48AATOM695OD1ASNA233−38.32489.961−71.0181.0048.18AATOM696ND2ASNA233−40.02591.160−71.8401.0047.41AATOM697CASNA233−36.75193.075−72.6831.0042.66AATOM698OASNA233−37.11492.398−73.6421.0043.49AATOM699NGLYA234−36.34394.331−72.7951.0041.69AATOM700CAGLYA234−36.32694.961−74.0941.0041.95AATOM701CGLYA234−34.96395.268−74.6761.0041.82AATOM702OGLYA234−34.66196.423−74.9551.0041.22AATOM703NGLYA235−34.12594.250−74.8341.0042.45AATOM704CAGLYA235−32.82694.469−75.4421.0044.17AATOM705CGLYA235−31.56994.772−74.6411.0045.65AATOM706OGLYA235−31.59694.997−73.4331.0045.42AATOM707NGLUA236−30.45294.788−75.3701.0046.13AATOM708CAGLUA236−29.12395.041−74.8311.0045.84AATOM709CBGLUA236−28.24693.821−75.0731.0046.16AATOM710CGGLUA236−29.01292.502−75.0611.0049.28AATOM711CDGLUA236−29.17091.927−73.6611.0052.42AATOM712OE1GLUA236−28.22091.263−73.1701.0053.46AATOM713OE2GLUA236−30.24092.150−73.0501.0052.08AATOM714CGLUA236−28.54396.224−75.5821.0045.41AATOM715OGLUA236−28.09396.081−76.7071.0045.48AATOM716NLEUA237−28.55797.395−74.9661.0046.49AATOM717CALEUA237−28.03098.593−75.6001.0046.92AATOM718CBLEUA237−27.73099.635−74.5391.0046.39AATOM719CGLEUA237−27.505101.045−75.0721.0049.33AATOM720CD1LEUA237−27.954102.038−74.0101.0050.02AATOM721CD2LEUA237−26.036101.251−75.4591.0050.55AATOM722CLEUA237−26.78198.312−76.4351.0048.20AATOM723OLEUA237−26.61598.854−77.5191.0049.31AATOM724NPHEA238−25.90197.455−75.9441.0050.29AATOM725CAPHEA238−24.70297.138−76.6991.0051.06AATOM726CBPHEA238−23.92396.005−76.0421.0052.21AATOM727CGPHEA238−22.66395.653−76.7761.0055.02AATOM728CD1PHEA238−21.47196.325−76.5071.0056.03AATOM729CD2PHEA238−22.67894.694−77.7851.0054.88AATOM730CE1PHEA238−20.31796.050−77.2311.0056.01AATOM731CE2PHEA238−21.52894.412−78.5181.0055.49AATOM732CZPHEA238−20.34795.092−78.2401.0056.77AATOM733CPHEA238−25.08896.714−78.1111.0051.64AATOM734OPHEA238−24.48797.167−79.0861.0051.78AATOM735NPHEA239−26.08695.838−78.2141.0051.05AATOM736CAPHEA239−26.54195.355−79.5081.0050.34AATOM737CBPHEA239−27.06893.930−79.4001.0053.30AATOM738CGPHEA239−25.97692.886−79.3781.0055.81AATOM739CD1PHEA239−26.07391.773−78.5431.0055.46AATOM740CD2PHEA239−24.83393.040−80.1711.0055.37AATOM741CE1PHEA239−25.05790.842−78.4931.0056.34AATOM742CE2PHEA239−23.81792.118−80.1301.0056.41AATOM743CZPHEA239−23.91991.008−79.2861.0057.26AATOM744CPHEA239−27.57996.245−80.1381.0049.66AATOM745OPHEA239−27.93896.051−81.2971.0050.84AATOM746NHISA240−28.07497.216−79.3751.0047.54AATOM747CAHISA240−29.03398.174−79.9051.0043.90AATOM748CBHISA240−29.81998.842−78.7861.0042.16AATOM749CGHISA240−30.95498.016−78.2831.0041.30AATOM750CD2HISA240−31.18697.465−77.0701.0041.33AATOM751ND1HISA240−32.00897.641−79.0851.0041.24AATOM752CE1HISA240−32.84096.889−78.3891.0041.90AATOM753NE2HISA240−32.36596.767−77.1631.0040.71AATOM754CHISA240−28.20299.209−80.6431.0043.45AATOM755OHISA240−28.70999.953−81.4691.0045.30AATOM756NLEUA241−26.91499.244−80.3341.0041.54AATOM757CALEUA241−25.995100.161−80.9851.0041.67AATOM758CBLEUA241−24.853100.506−80.0411.0039.70AATOM759CGLEUA241−23.861101.533−80.5621.0039.41AATOM760CD1LEUA241−24.539102.894−80.5721.0038.38AATOM761CD2LEUA241−22.608101.545−79.6841.0037.59AATOM762CLEUA241−25.42799.488−82.2401.0043.22AATOM763OLEUA241−25.372100.083−83.3091.0044.67AATOM764NSERA242−25.00598.239−82.0941.0042.62AATOM765CASERA242−24.44497.459−83.1831.0041.93AATOM766CBSERA242−24.27996.028−82.7161.0042.54AATOM767OGSERA242−25.47595.622−82.0791.0044.02AATOM768CSERA242−25.30297.475−84.4421.0042.68AATOM769OSERA242−24.77797.353−85.5521.0044.22AATOM770NARGA243−26.61997.590−84.2791.0042.79AATOM771CAARGA243−27.51797.634−85.4341.0041.20AATOM772CBARGA243−28.94997.291−85.0451.0040.35AATOM773CGARGA243−29.16295.943−84.4081.0041.66AATOM774CDARGA243−30.66495.623−84.3461.0042.58AATOM775NEARGA243−31.50596.805−84.1111.0043.70AATOM776CZARGA243−31.56197.501−82.9741.0044.52AATOM777NH1ARGA243−30.82597.147−81.9281.0044.45AATOM778NH2ARGA243−32.34598.572−82.8901.0044.14AATOM779CARGA243−27.54099.030−86.0371.0040.60AATOM780OARGA243−27.83799.205−87.2131.0040.76AATOM781NGLUA244−27.218100.027−85.2271.0039.12AATOM782CAGLUA244−27.255101.401−85.6821.0038.02AATOM783CBGLUA244−28.285102.148−84.8611.0037.26AATOM784CGGLUA244−29.634101.496−84.9361.0034.08AATOM785CDGLUA244−30.661102.241−84.1561.0032.02AATOM786OE1GLUA244−30.710102.072−82.9221.0030.18AATOM787OE2GLUA244−31.414103.004−84.7871.0031.62AATOM788CGLUA244−25.938102.114−85.5811.0038.67AATOM789OGLUA244−25.848103.296−85.8721.0038.98AATOM790NARGA245−24.914101.369−85.1951.0039.02AATOM791CAARGA245−23.561101.884−84.9901.0038.77AATOM792CBARGA245−22.731101.873−86.2821.0038.30AATOM793CGARGA245−23.443102.207−87.5591.0039.67AATOM794CDARGA245−24.332101.049−88.0011.0041.10AATOM795NEARGA245−24.271100.822−89.4431.0041.51AATOM796CZARGA245−23.48899.920−90.0221.0042.11AATOM797NH1ARGA245−22.69799.151−89.2881.0043.11AATOM798NH2ARGA245−23.50399.777−91.3391.0042.47AATOM799CARGA245−23.419103.246−84.3341.0037.39AATOM800OARGA245−22.472103.450−83.5971.0039.64AATOM801NVALA246−24.323104.179−84.5791.0034.06AATOM802CAVALA246−24.168105.475−83.9611.0033.86AATOM803CBVALA246−23.364106.425−84.8601.0033.87AATOM804CG1VALA246−22.924107.607−84.0691.0034.38AATOM805CG2VALA246−22.160105.728−85.4261.0034.12AATOM806CVALA246−25.471106.166−83.5861.0034.38AATOM807OVALA246−26.060106.891−84.3811.0033.67AATOM808NPHEA247−25.910105.942−82.3541.0034.78AATOM809CAPHEA247−27.119106.553−81.8491.0032.44AATOM810CBPHEA247−27.241106.295−80.3511.0031.96AATOM811CGPHEA247−27.582104.878−79.9951.0032.09AATOM812CD1PHEA247−28.481104.149−80.7611.0031.38AATOM813CD2PHEA247−27.068104.298−78.8401.0033.87AATOM814CE1PHEA247−28.865102.867−80.3781.0032.81AATOM815CE2PHEA247−27.448103.015−78.4531.0033.44AATOM816CZPHEA247−28.350102.301−79.2241.0032.59AATOM817CPHEA247−27.012108.049−82.0971.0032.71AATOM818OPHEA247−25.931108.557−82.3931.0030.31AATOM819NTHRA248−28.132108.751−81.9701.0034.47AATOM820CATHRA248−28.166110.199−82.1701.0035.62AATOM821CBTHRA248−29.602110.694−82.4151.0038.60AATOM822OG1THRA248−30.311109.742−83.2251.0040.72AATOM823CG2THRA248−29.578112.050−83.1101.0037.55AATOM824CTHRA248−27.661110.887−80.9111.0034.79AATOM825OTHRA248−27.903110.410−79.8031.0034.05AATOM826NGLUA249−26.972112.008−81.0811.0034.51AATOM827CAGLUA249−26.449112.760−79.9441.0035.98AATOM828CBGLUA249−25.923114.117−80.4051.0034.13AATOM829CGGLUA249−24.432114.183−80.6521.0031.70AATOM830CDGLUA249−23.931115.615−80.7191.0030.48AATOM831OE1GLUA249−24.105116.350−79.7241.0026.58AATOM832OE2GLUA249−23.366116.000−81.7631.0027.76AATOM833CGLUA249−27.524112.972−78.8701.0039.20AATOM834OGLUA249−27.241113.423−77.7551.0039.80AATOM835NGLUA250−28.759112.645−79.2311.0041.58AATOM836CAGLUA250−29.912112.753−78.3521.0043.56AATOM837CBGLUA250−31.063113.352−79.1161.0045.82AATOM838CGGLUA250−30.930114.817−79.2441.0048.09AATOM839CDGLUA250−31.169115.469−77.9261.0047.68AATOM840OE1GLUA250−32.320115.377−77.4551.0046.05AATOM841OE2GLUA250−30.209116.041−77.3651.0047.24AATOM842CGLUA250−30.278111.364−77.9151.0044.41AATOM843OGLUA250−30.681111.135−76.7791.0045.34AATOM844NARGA251−30.134110.442−78.8581.0045.42AATOM845CAARGA251−30.394109.027−78.6431.0045.39AATOM846CBARGA251−30.031108.252−79.8911.0044.94AATOM847CGARGA251−31.130107.370−80.3951.0045.93AATOM848CDARGA251−31.338106.185−79.5121.0043.02AATOM849NEARGA251−31.711105.064−80.3521.0045.83AATOM850CZARGA251−31.936103.834−79.9101.0048.35AATOM851NH1ARGA251−31.825103.562−78.6191.0048.46AATOM852NH2ARGA251−32.262102.870−80.7641.0049.08AATOM853CARGA251−29.514108.568−77.4971.0044.99AATOM854OARGA251−29.847107.624−76.7821.0045.06AATOM855NALAA252−28.368109.229−77.3501.0042.22AATOM856CAALAA252−27.462108.928−76.2631.0040.76AATOM857CBALAA252−26.030109.281−76.6481.0039.88AATOM858CALAA252−27.946109.809−75.1231.0040.70AATOM859OALAA252−28.134109.344−74.0081.0041.22AATOM860NARGA253−28.167111.085−75.4291.0040.48AATOM861CAARGA253−28.637112.057−74.4531.0038.59AATOM862CBARGA253−29.344113.219−75.1731.0037.81AATOM863CGARGA253−29.896114.356−74.2811.0034.71AATOM864CDARGA253−28.965115.572−74.2261.0030.13AATOM865NEARGA253−28.727116.108−75.5591.0029.06AATOM866CZARGA253−27.731116.928−75.8801.0029.79AATOM867NH1ARGA253−26.879117.325−74.9551.0025.42AATOM868NH2ARGA253−27.551117.304−77.1421.0027.32AATOM869CARGA253−29.598111.377−73.4821.0038.51AATOM870OARGA253−29.452111.502−72.2631.0038.00AATOM871NPHEA254−30.563110.640−74.0181.0037.52AATOM872CAPHEA254−31.544109.961−73.1701.0038.28AATOM873CBPHEA254−32.545109.183−74.0211.0040.43AATOM874CGPHEA254−33.726108.671−73.2521.0042.97AATOM875CD1PHEA254−34.612109.557−72.6461.0044.15AATOM876CD2PHEA254−33.980107.308−73.1691.0044.39AATOM877CE1PHEA254−35.739109.096−71.9691.0044.57AATOM878CE2PHEA254−35.105106.834−72.4941.0046.74AATOM879CZPHEA254−35.991107.734−71.8941.0046.36AATOM880CPHEA254−30.876109.007−72.1971.0037.59AATOM881OPHEA254−30.984109.172−70.9831.0038.31AATOM882NTYRA255−30.187108.009−72.7441.0036.49AATOM883CATYRA255−29.481107.008−71.9551.0034.51AATOM884CBTYRA255−28.764106.031−72.8781.0034.38AATOM885CGTYRA255−29.697105.399−73.8671.0036.38AATOM886CD1TYRA255−30.861104.782−73.4401.0036.86AATOM887CE1TYRA255−31.754104.249−74.3411.0037.89AATOM888CD2TYRA255−29.445105.457−75.2311.0036.21AATOM889CE2TYRA255−30.336104.922−76.1431.0037.02AATOM890CZTYRA255−31.489104.326−75.6911.0036.90AATOM891OHTYRA255−32.414103.838−76.5711.0037.31AATOM892CTYRA255−28.470107.639−71.0251.0033.28AATOM893OTYRA255−28.510107.436−69.8211.0033.03AATOM894NGLYA256−27.560108.404−71.5961.0032.52AATOM895CAGLYA256−26.547109.041−70.7921.0033.15AATOM896CGLYA256−27.176109.791−69.6521.0033.67AATOM897OGLYA256−26.544110.007−68.6191.0034.79AATOM898NALAA257−28.424110.199−69.8351.0032.91AATOM899CAALAA257−29.116110.919−68.7811.0033.05AATOM900CBALAA257−30.291111.691−69.3471.0032.88AATOM901CALAA257−29.585109.942−67.7111.0031.96AATOM902OALAA257−29.381110.159−66.5291.0031.69AATOM903NGLUA258−30.207108.855−68.1261.0030.83AATOM904CAGLUA258−30.673107.880−67.1641.0032.74AATOM905CBGLUA258−31.424106.772−67.8881.0032.87AATOM906CGGLUA258−32.516107.302−68.7901.0034.21AATOM907CDGLUA258−33.530106.249−69.1161.0035.49AATOM908OE1GLUA258−33.111105.169−69.5601.0036.86AATOM909OE2GLUA258−34.739106.497−68.9261.0034.07AATOM910CGLUA258−29.539107.291−66.3191.0033.81AATOM911OGLUA258−29.720107.023−65.1291.0034.65AATOM912NILEA259−28.371107.105−66.9251.0033.33AATOM913CAILEA259−27.229106.552−66.2071.0032.69AATOM914CBILEA259−26.091106.159−67.1681.0032.27AATOM915CG2ILEA259−24.926105.569−66.3781.0031.18AATOM916CG1ILEA259−26.602105.158−68.2001.0029.40AATOM917CD1ILEA259−25.626104.896−69.2541.0029.61AATOM918CILEA259−26.671107.532−65.1831.0032.05AATOM919OILEA259−26.199107.126−64.1211.0031.97AATOM920NVALA260−26.711108.818−65.5231.0032.02AATOM921CAVALA260−26.229109.888−64.6311.0032.08AATOM922CBVALA260−26.093111.249−65.3841.0029.83AATOM923CG1VALA260−25.724112.352−64.4111.0025.00AATOM924CG2VALA260−25.056111.139−66.4851.0028.32AATOM925CVALA260−27.179110.096−63.4391.0031.55AATOM926OVALA260−26.763110.558−62.3891.0032.28AATOM927NSERA261−28.451109.757−63.6121.0029.94AATOM928CASERA261−29.424109.900−62.5451.0030.84AATOM929CBSERA261−30.833109.632−63.0841.0031.81AATOM930OGSERA261−31.828110.009−62.1511.0030.44AATOM931CSERA261−29.079108.858−61.4871.0031.10AATOM932OSERA261−29.088109.130−60.2911.0031.07AATOM933NALAA262−28.767107.657−61.9641.0030.84AATOM934CAALAA262−28.416106.533−61.1121.0027.97AATOM935CBALAA262−28.404105.262−61.9351.0028.46AATOM936CALAA262−27.078106.707−60.4151.0025.94AATOM937OALAA262−26.823106.079−59.4051.0026.90AATOM938NLEUA263−26.227107.564−60.9491.0023.62AATOM939CALEUA263−24.919107.773−60.3661.0024.02AATOM940CBLEUA263−23.887108.048−61.4521.0023.45AATOM941CGLEUA263−23.570106.878−62.3771.0022.05AATOM942CD1LEUA263−22.324107.208−63.1701.0021.25AATOM943CD2LEUA263−23.388105.621−61.5581.0020.13AATOM944CLEUA263−24.846108.865−59.3361.0026.44AATOM945OLEUA263−23.991108.814−58.4601.0026.99AATOM946NGLUA264−25.709109.873−59.4531.0028.99AATOM947CAGLUA264−25.732110.948−58.4621.0028.77AATOM948CBGLUA264−26.614112.103−58.9311.0028.24AATOM949CGGLUA264−26.605113.264−57.9551.0031.63AATOM950CDGLUA264−27.616114.338−58.2741.0032.30AATOM951OE1GLUA264−28.801113.996−58.4541.0032.81AATOM952OE2GLUA264−27.225115.524−58.3221.0033.53AATOM953CGLUA264−26.336110.291−57.2151.0028.46AATOM954OGLUA264−25.952110.568−56.0791.0026.27AATOM955NTYRA265−27.271109.384−57.4791.0027.85AATOM956CATYRA265−27.963108.612−56.4631.0029.34AATOM957CBTYRA265−29.099107.820−57.1001.0029.72AATOM958CGTYRA265−29.598106.710−56.2161.0033.41AATOM959CD1TYRA265−30.425106.970−55.1291.0034.71AATOM960CE1TYRA265−30.841105.945−54.2861.0035.99AATOM961CD2TYRA265−29.201105.396−56.4351.0037.60AATOM962CE2TYRA265−29.614104.362−55.5911.0037.88AATOM963CZTYRA265−30.429104.648−54.5261.0037.05AATOM964OHTYRA265−30.823103.630−53.7031.0039.24AATOM965CTYRA265−27.035107.635−55.7431.0029.17AATOM966OTYRA265−27.024107.578−54.5051.0029.69AATOM967NLEUA266−26.293106.846−56.5221.0026.54AATOM968CALEUA266−25.369105.862−55.9661.0024.17AATOM969CBLEUA266−24.856104.908−57.0381.0022.32AATOM970CGLEUA266−25.724103.728−57.4311.0022.72AATOM971CD1LEUA266−25.048102.968−58.5461.0020.84AATOM972CD2LEUA266−25.954102.847−56.2311.0022.60AATOM973CLEUA266−24.181106.497−55.3051.0023.04AATOM974OLEUA266−23.651105.963−54.3571.0021.67AATOM975NHISA267−23.753107.634−55.8191.0022.48AATOM976CAHISA267−22.609108.322−55.2451.0023.97AATOM977CBHISA267−22.023109.324−56.2591.0023.04AATOM978CGHISA267−21.332108.680−57.4291.0023.99AATOM979CD2HISA267−21.208107.379−57.7881.0022.90AATOM980ND1HISA267−20.618109.401−58.3611.0024.12AATOM981CE1HISA267−20.080108.573−59.2381.0022.93AATOM982NE2HISA267−20.423107.343−58.9121.0022.95AATOM983CHISA267−22.973109.042−53.9511.0024.92AATOM984OHISA267−22.099109.497−53.2341.0024.71AATOM985NSERA268−24.268109.153−53.6631.0028.48AATOM986CASERA268−24.722109.840−52.4621.0030.48AATOM987CBSERA268−26.092110.533−52.6741.0033.19AATOM988OGSERA268−27.135109.656−53.1071.0036.18AATOM989CSERA268−24.784108.852−51.3311.0030.30AATOM990OSERA268−24.966109.222−50.1821.0030.83AATOM991NARGA269−24.629107.583−51.6631.0031.41AATOM992CAARGA269−24.609106.546−50.6441.0034.82AATOM993CBARGA269−25.417105.312−51.0751.0036.65AATOM994CGARGA269−26.912105.562−51.2841.0040.81AATOM995CDARGA269−27.670104.245−51.5061.0043.17AATOM996NEARGA269−29.030104.277−50.9521.0046.03AATOM997CZARGA269−29.900103.270−51.0311.0046.64AATOM998NH1ARGA269−29.554102.139−51.6401.0047.74AATOM999NH2ARGA269−31.123103.400−50.5271.0045.34AATOM1000CARGA269−23.149106.145−50.4321.0035.15AATOM1001OARGA269−22.853105.332−49.5611.0037.64AATOM1002NASPA270−22.246106.730−51.2231.0033.55AATOM1003CAASPA270−20.821106.422−51.1531.0032.07AATOM1004CBASPA270−20.355106.364−49.7021.0034.09AATOM1005CGASPA270−19.942107.706−49.1871.0038.64AATOM1006OD1ASPA270−18.759108.086−49.3371.0039.23AATOM1007OD2ASPA270−20.814108.403−48.6421.0044.04AATOM1008CASPA270−20.539105.091−51.8381.0031.42AATOM1009OASPA270−19.536104.430−51.5611.0031.81AATOM1010NVALA271−21.437104.712−52.7371.0028.12AATOM1011CAVALA271−21.330103.472−53.4831.0025.52AATOM1012CBVALA271−22.697102.855−53.7021.0024.60AATOM1013CG1VALA271−22.565101.626−54.5541.0021.84AATOM1014CG2VALA271−23.357102.562−52.3751.0023.57AATOM1015CVALA271−20.732103.689−54.8591.0025.86AATOM1016OVALA271−21.446104.006−55.7861.0027.74AATOM1017NVALA272−19.423103.536−55.0061.0026.27AATOM1018CAVALA272−18.828103.707−56.3241.0025.25AATOM1019CBVALA272−17.305103.688−56.2681.0024.89AATOM1020CG1VALA272−16.739103.513−57.6651.0023.43AATOM1021CG2VALA272−16.807104.980−55.6371.0019.68AATOM1022CVALA272−19.328102.512−57.0841.0025.49AATOM1023OVALA272−19.458101.451−56.5021.0027.02AATOM1024NTYRA273−19.631102.671−58.3671.0026.39AATOM1025CATYRA273−20.154101.542−59.1381.0025.65AATOM1026CBTYRA273−21.158102.026−60.1881.0021.46AATOM1027CGTYRA273−22.014100.907−60.7281.0019.34AATOM1028CD1TYRA273−22.989100.320−59.9451.0015.37AATOM1029CE1TYRA273−23.73499.269−60.4141.0015.86AATOM1030CD2TYRA273−21.814100.407−62.0081.0019.42AATOM1031CE2TYRA273−22.56599.351−62.4901.0017.46AATOM1032CZTYRA273−23.51898.786−61.6881.0017.18AATOM1033OHTYRA273−24.25597.719−62.1471.0020.93AATOM1034CTYRA273−19.097100.658−59.8041.0025.88AATOM1035OTYRA273−19.18799.444−59.7311.0025.15AATOM1036NARGA274−18.114101.264−60.4601.0027.43AATOM1037CAARGA274−17.043100.507−61.1141.0031.42AATOM1038CBARGA274−16.42799.499−60.1291.0031.33AATOM1039CGARGA274−15.718100.127−58.9641.0035.00AATOM1040CDARGA274−15.39499.118−57.8871.0036.47AATOM1041NEARGA274−14.48098.077−58.3431.0038.77AATOM1042CZARGA274−13.79297.278−57.5301.0039.74AATOM1043NH1ARGA274−13.90897.404−56.2131.0040.96AATOM1044NH2ARGA274−12.99596.344−58.0321.0039.62AATOM1045CARGA274−17.39199.751−62.4061.0031.91AATOM1046OARGA274−16.52299.520−63.2331.0032.08AATOM1047NASPA275−18.64699.367−62.5861.0033.64AATOM1048CAASPA275−19.00098.608−63.7691.0035.02AATOM1049CBASPA275−19.60097.268−63.3531.0037.76AATOM1050CGASPA275−18.57396.347−62.7311.0040.90AATOM1051OD1ASPA275−18.00996.702−61.6751.0040.31AATOM1052OD2ASPA275−18.32895.265−63.3051.0044.05AATOM1053CASPA275−19.89599.263−64.8031.0035.21AATOM1054OASPA275−20.62998.570−65.5091.0034.29AATOM1055NILEA276−19.831100.588−64.9061.0034.89AATOM1056CAILEA276−20.630101.285−65.9001.0035.45AATOM1057CBILEA276−20.863102.772−65.5391.0035.25AATOM1058CG2ILEA276−21.467103.525−66.7461.0032.67AATOM1059CG1ILEA276−21.824102.860−64.3451.0034.05AATOM1060CD1ILEA276−22.086104.228−63.9101.0033.07AATOM1061CILEA276−19.893101.179−67.2171.0036.58AATOM1062OILEA276−18.872101.828−67.4321.0035.65AATOM1063NLYSA277−20.434100.325−68.0821.0037.98AATOM1064CALYSA277−19.880100.038−69.3971.0039.08AATOM1065CBLYSA277−18.71399.046−69.2631.0038.92AATOM1066CGLYSA277−19.09597.761−68.5451.0040.30AATOM1067CDLYSA277−17.98696.729−68.5431.0041.04AATOM1068CELYSA277−18.49195.371−68.0261.0042.56AATOM1069NZLYSA277−17.53494.248−68.2741.0040.96AATOM1070CLYSA277−21.01599.433−70.2311.0039.64AATOM1071OLYSA277−22.01798.980−69.6791.0040.48AATOM1072NLEUA278−20.83499.418−71.5491.0039.22AATOM1073CALEUA278−21.82298.940−72.5191.0038.63AATOM1074CBLEUA278−21.21298.943−73.9011.0038.08AATOM1075CGLEUA278−21.80599.976−74.8201.0037.92AATOM1076CD1LEUA278−20.695100.904−75.2401.0038.72AATOM1077CD2LEUA278−22.46299.305−75.9951.0037.44AATOM1078CLEUA278−22.53897.622−72.3701.0039.89AATOM1079OLEUA278−23.66097.470−72.8791.0039.13AATOM1080NGLUA279−21.89096.648−71.7361.0041.04AATOM1081CAGLUA279−22.52795.346−71.5611.0040.42AATOM1082CBGLUA279−21.47694.246−71.4731.0042.80AATOM1083CGGLUA279−21.72693.134−72.4691.0045.57AATOM1084CDGLUA279−22.03693.680−73.8581.0047.03AATOM1085OE1GLUA279−21.25094.536−74.3391.0046.93AATOM1086OE2GLUA279−23.05493.254−74.4581.0044.67AATOM1087CGLUA279−23.41095.357−70.3301.0037.93AATOM1088OGLUA279−24.31694.552−70.1831.0037.80AATOM1089NASNA280−23.14596.304−69.4531.0036.16AATOM1090CAASNA280−23.93696.443−68.2551.0036.11AATOM1091CBASNA280−23.13397.186−67.1821.0036.30AATOM1092CGASNA280−22.21896.269−66.4041.0034.57AATOM1093OD1ASNA280−22.57995.786−65.3451.0035.55AATOM1094ND2ASNA280−21.03996.014−66.9361.0033.27AATOM1095CASNA280−25.22297.190−68.5621.0034.76AATOM1096OASNA280−26.06197.338−67.6961.0034.70AATOM1097NLEUA281−25.37597.636−69.8051.0035.35AATOM1098CALEUA281−26.55698.398−70.2361.0035.38AATOM1099CBLEUA281−26.10699.657−70.9911.0034.23AATOM1100CGLEUA281−25.228100.592−70.1561.0035.27AATOM1101CD1LEUA281−24.698101.766−70.9821.0035.67AATOM1102CD2LEUA281−26.049101.091−68.9811.0037.36AATOM1103CLEUA281−27.57797.630−71.0891.0035.68AATOM1104OLEUA281−27.25197.072−72.1351.0034.57AATOM1105NMETA282−28.81697.603−70.6111.0036.34AATOM1106CAMETA282−29.92196.940−71.2981.0037.12AATOM1107CBMETA282−30.40895.722−70.5091.0037.66AATOM1108CGMETA282−29.47394.530−70.5241.0039.07AATOM1109SDMETA282−30.34092.945−70.1891.0042.02AATOM1110CEMETA282−30.03992.718−68.4221.0040.51AATOM1111CMETA282−31.05897.957−71.4151.0037.98AATOM1112OMETA282−30.85699.145−71.1411.0037.86AATOM1113NLEUA283−32.24297.492−71.8151.0037.15AATOM1114CALEUA283−33.42598.346−71.9651.0036.88AATOM1115CBLEUA283−33.56598.838−73.4121.0032.01AATOM1116CGLEUA283−32.47399.715−74.0311.0027.90AATOM1117CD1LEUA283−32.77399.914−75.4931.0027.78AATOM1118CD2LEUA283−32.399101.042−73.3341.0025.20AATOM1119CLEUA283−34.66397.535−71.5841.0039.75AATOM1120OLEUA283−34.79596.380−71.9911.0039.81AATOM1121NASPA284−35.57098.128−70.8061.0041.87AATOM1122CAASPA284−36.77297.415−70.3911.0043.84AATOM1123CBASPA284−37.25297.893−69.0121.0046.24AATOM1124CGASPA284−37.38999.410−68.9091.0048.50AATOM1125OD1ASPA284−37.751100.054−69.9171.0046.51AATOM1126OD2ASPA284−37.15299.945−67.7961.0048.37AATOM1127CASPA284−37.89797.539−71.4031.0045.15AATOM1128OASPA284−37.81898.344−72.3271.0044.64AATOM1129NLYSA285−38.94096.733−71.2241.0046.02AATOM1130CALYSA285−40.08696.734−72.1321.0046.07AATOM1131CBLYSA285−41.34196.168−71.4361.0045.21AATOM1132CGLYSA285−41.54694.643−71.5461.0045.28AATOM1133CDLYSA285−42.99294.262−71.1581.0044.25AATOM1134CELYSA285−43.28892.751−71.1901.0041.92AATOM1135NZLYSA285−42.78792.018−69.9941.0039.57AATOM1136CLYSA285−40.43098.087−72.7531.0045.07AATOM1137OLYSA285−40.82398.134−73.9141.0045.90AATOM1138NASPA286−40.26299.180−72.0081.0043.75AATOM1139CAASPA286−40.609100.516−72.5171.0042.99AATOM1140CBASPA286−41.235101.371−71.4001.0041.55AATOM1141CGASPA286−42.373100.665−70.6771.0042.05AATOM1142OD1ASPA286−43.357100.275−71.3461.0042.14AATOM1143OD2ASPA286−42.285100.500−69.4321.0042.02AATOM1144CASPA286−39.520101.357−73.1871.0042.82AATOM1145OASPA286−39.827102.405−73.7451.0044.03AATOM1146NGLYA287−38.262100.929−73.1271.0043.61AATOM1147CAGLYA287−37.184101.706−73.7341.0041.35AATOM1148CGLYA287−36.272102.442−72.7471.0039.84AATOM1149OGLYA287−35.457103.286−73.1351.0039.78AATOM1150NHISA288−36.400102.122−71.4641.0038.40AATOM1151CAHISA288−35.584102.741−70.4221.0036.35AATOM1152CBHISA288−36.444102.987−69.1841.0035.85AATOM1153CGHISA288−37.360104.157−69.3101.0036.47AATOM1154CD2HISA288−38.708104.229−69.3851.0036.42AATOM1155ND1HISA288−36.902105.455−69.3991.0036.41AATOM1156CE1HISA288−37.929106.272−69.5241.0037.52AATOM1157NE2HISA288−39.038105.552−69.5191.0036.25AATOM1158CHISA288−34.360101.891−70.0411.0034.72AATOM1159OHISA288−34.477100.695−69.8111.0034.41AATOM1160NILEA289−33.193102.522−69.9661.0032.41AATOM1161CAILEA289−31.955101.829−69.6101.0031.73AATOM1162CBILEA289−30.742102.782−69.6071.0030.57AATOM1163CG2ILEA289−30.056102.742−68.2291.0028.30AATOM1164CG1ILEA289−29.764102.401−70.7311.0029.20AATOM1165CD1ILEA289−28.489103.216−70.7561.0026.28AATOM1166CILEA289−32.018101.214−68.2271.0031.91AATOM1167OILEA289−32.737101.702−67.3591.0033.58AATOM1168NLYSA290−31.229100.159−68.0361.0031.19AATOM1169CALYSA290−31.11799.430−66.7661.0029.97AATOM1170CBLYSA290−31.89198.123−66.8071.0027.48AATOM1171CGLYSA290−33.36198.218−66.5971.0026.64AATOM1172CDLYSA290−33.73697.567−65.2941.0025.08AATOM1173CELYSA290−33.43298.474−64.1581.0025.34AATOM1174NZLYSA290−34.47799.510−64.0771.0024.39AATOM1175CLYSA290−29.65499.071−66.5611.0030.57AATOM1176OLYSA290−29.15898.168−67.2231.0031.66AATOM1177NILEA291−28.96399.781−65.6731.0030.15AATOM1178CAILEA291−27.57199.498−65.3921.0028.64AATOM1179CBILEA291−26.997100.504−64.4071.0028.60AATOM1180CG2ILEA291−25.578100.110−64.0341.0028.92AATOM1181CG1ILEA291−27.006101.904−65.0271.0028.24AATOM1182CD1ILEA291−26.860103.033−64.0081.0026.43AATOM1183CILEA291−27.67898.147−64.7411.0030.07AATOM1184OILEA291−28.47197.965−63.8461.0030.32AATOM1185NTHRA292−26.88597.187−65.1821.0032.81AATOM1186CATHRA292−27.01495.853−64.6341.0035.39AATOM1187CBTHRA292−27.74494.972−65.6801.0032.81AATOM1188OG1THRA292−28.19793.761−65.0821.0032.18AATOM1189CG2THRA292−26.85394.673−66.8201.0030.94AATOM1190CTHRA292−25.70895.200−64.1591.0039.46AATOM1191OTHRA292−24.77195.876−63.7281.0038.51AATOM1192NASPA293−25.68293.874−64.2051.0045.81AATOM1193CAASPA293−24.53293.068−63.7981.0051.59AATOM1194CBASPA293−23.49093.056−64.9191.0053.04AATOM1195CGASPA293−22.57191.843−64.8551.0054.41AATOM1196OD1ASPA293−23.09790.707−64.7051.0054.78AATOM1197OD2ASPA293−21.33492.036−64.9701.0053.19AATOM1198CASPA293−23.89893.549−62.5011.0054.71AATOM1199OASPA293−23.11694.502−62.4981.0055.17AATOM1200NPHEA294−24.24392.878−61.4031.0058.22AATOM1201CAPHEA294−23.71793.220−60.0911.0062.47AATOM1202CBPHEA294−24.81593.107−59.0361.0064.72AATOM1203CGPHEA294−25.45694.417−58.6591.0067.85AATOM1204CD1PHEA294−26.32395.070−59.5311.0068.79AATOM1205CD2PHEA294−25.22994.975−57.4031.0068.87AATOM1206CE1PHEA294−26.96296.254−59.1541.0069.30AATOM1207CE2PHEA294−25.86696.162−57.0181.0069.41AATOM1208CZPHEA294−26.73396.799−57.8961.0068.81AATOM1209CPHEA294−22.56292.303−59.6841.0064.77AATOM1210OPHEA294−22.78291.163−59.2641.0065.50AATOM1211NGLYA295−21.33292.797−59.7881.0065.64AATOM1212CAGLYA295−20.20291.979−59.3991.0066.77AATOM1213CGLYA295−19.08192.748−58.7321.0068.04AATOM1214OGLYA295−18.55392.326−57.7061.0067.55AATOM1215NLEUA296−18.72293.887−59.3151.0069.24AATOM1216CALEUA296−17.63694.714−58.7961.0069.80AATOM1217CBLEUA296−16.68395.040−59.9411.0068.99AATOM1218CGLEUA296−16.70293.978−61.0511.0069.63AATOM1219CD1LEUA296−15.74494.376−62.1581.0069.49AATOM1220CD2LEUA296−16.32192.612−60.4871.0069.24AATOM1221CLEUA296−18.12196.008−58.1181.0070.84AATOM1222OLEUA296−17.97497.103−58.6631.0071.52AATOM1223NCYSA297−18.69895.870−56.9271.0070.50AATOM1224CACYSA297−19.18297.014−56.1661.0070.35AATOM1225CBCYSA297−20.61797.346−56.5621.0070.19AATOM1226SGCYSA297−20.72298.245−58.1131.0070.43AATOM1227CCYSA297−19.10096.805−54.6531.0070.28AATOM1228OCYSA297−18.91295.692−54.1661.0070.03AATOM1229NLYSA298−19.26197.894−53.9131.0070.13AATOM1230CALYSA298−19.18697.847−52.4641.0069.38AATOM1231CBLYSA298−17.79297.391−52.0411.0068.44AATOM1232CGLYSA298−17.63497.221−50.5481.0069.24AATOM1233CDLYSA298−16.17597.100−50.1481.0068.56AATOM1234CELYSA298−16.01697.147−48.6321.0066.43AATOM1235NZLYSA298−14.60397.390−48.2381.0063.63AATOM1236CLYSA298−19.46099.239−51.9051.0069.46AATOM1237OLYSA298−19.586100.205−52.6561.0069.37AATOM1238NGLUA299−19.54199.339−50.5861.0069.37AATOM1239CAGLUA299−19.781100.617−49.9351.0070.45AATOM1240CBGLUA299−20.687100.423−48.7351.0069.62AATOM1241CGGLUA299−20.03699.732−47.5521.0067.24AATOM1242CDGLUA299−21.06099.321−46.5221.0064.27AATOM1243OE1GLUA299−20.76499.388−45.3131.0062.87AATOM1244OE2GLUA299−22.16898.925−46.9301.0061.93AATOM1245CGLUA299−18.468101.244−49.4701.0072.35AATOM1246OGLUA299−18.463102.257−48.7591.0072.33AATOM1247NVALA302−17.355100.625−49.8541.0073.46AATOM1248CAVALA302−16.046101.143−49.4891.0073.43AATOM1249CBVALA302−14.911100.262−50.0771.0072.36AATOM1250CG1VALA302−14.996100.251−51.5861.0070.53AATOM1251CG2VALA302−13.546100.759−49.5941.0071.14AATOM1252CVALA302−15.960102.566−50.0371.0074.40AATOM1253OVALA302−16.201102.805−51.2261.0074.16AATOM1254NALAA303−15.640103.505−49.1521.0075.32AATOM1255CAALAA303−15.534104.914−49.5091.0076.08AATOM1256CBALAA303−16.714105.682−48.9181.0075.56AATOM1257CALAA303−14.221105.530−49.0221.0076.47AATOM1258OALAA303−13.932106.698−49.3051.0076.25AATOM1259NGLYA304−13.435104.746−48.2851.0076.58AATOM1260CAGLYA304−12.169105.235−47.7671.0076.19AATOM1261CGLYA304−11.184105.537−48.8771.0076.64AATOM1262OGLYA304−10.771106.687−49.0591.0076.62AATOM1263NALAA305−10.812104.495−49.6201.0076.61AATOM1264CAALAA305−9.869104.604−50.7351.0075.64AATOM1265CBALAA305−8.622105.396−50.3081.0075.16AATOM1266CALAA305−9.459103.219−51.2401.0075.04AATOM1267OALAA305−8.422102.690−50.8471.0074.28AATOM1268NTHRA306−10.280102.644−52.1131.0074.75AATOM1269CATHRA306−10.014101.332−52.6971.0073.89AATOM1270CBTHRA306−11.309100.478−52.7491.0073.35AATOM1271OG1THRA306−11.04899.229−53.4021.0073.02AATOM1272OG2THRA306−12.404101.218−53.4941.0072.10AATOM1273CTHRA306−9.455101.520−54.1141.0074.01AATOM1274OTHRA306−9.854102.445−54.8281.0073.10AATOM1275NMETA307−8.530100.648−54.5131.0074.07AATOM1276CAMETA307−7.901100.726−55.8311.0074.12AATOM1277CBMETA307−6.632101.565−55.7121.0073.12AATOM1278CGMETA307−5.784101.217−54.4891.0070.93AATOM1279SDMETA307−4.511102.458−54.1041.0068.51AATOM1280CEMETA307−4.504102.352−52.2511.0066.70AATOM1281CMETA307−7.58599.334−56.4091.0075.82AATOM1282OMETA307−6.64999.165−57.2091.0074.61AATOM1283NTHRA309−8.39998.360−55.9931.0077.31AATOM1284CATHRA309−8.31496.947−56.3831.0078.49AATOM1285CBTHRA309−9.66196.244−56.0561.0078.84AATOM1286OG1THRA309−10.00896.517−54.6941.0079.62AATOM1287CG2THRA309−9.57294.733−56.2461.0078.86AATOM1288CTHRA309−7.95996.679−57.8521.0078.75AATOM1289OTHRA309−7.73597.604−58.6341.0078.84AATOM1290NPHEA310−7.89895.400−58.2131.0079.13AATOM1291CAPHEA310−7.58894.997−59.5791.0079.15AATOM1292CBPHEA310−6.23194.252−59.6431.0077.42AATOM1293CGPHEA310−5.02295.139−59.4201.0075.20AATOM1294CD1PHEA310−4.67195.569−58.1401.0074.27AATOM1295CD2PHEA310−4.25595.577−60.5001.0073.64AATOM1296CE1PHEA310−3.56396.428−57.9381.0071.91AATOM1297CE2PHEA310−3.15196.434−60.3111.0071.10AATOM1298CZPHEA310−2.81096.862−59.0261.0069.93AATOM1299CPHEA310−8.69694.109−60.1741.0080.19AATOM1300OPHEA310−8.95893.002−59.6901.0080.39AATOM1301NCYSA311−9.34394.635−61.2171.0080.36AATOM1302CACYSA311−10.40893.978−61.9941.0079.60AATOM1303CBCYSA311−11.60993.541−61.1311.0080.92AATOM1304SGCYSA311−12.94192.618−62.0811.0081.68AATOM1305CCYSA311−10.86295.035−62.9961.0078.12AATOM1306OCYSA311−11.00996.210−62.6371.0077.53AATOM1307NGLYA312−11.08494.633−64.2471.0076.21AATOM1308CAGLYA312−11.48695.616−65.2321.0072.84AATOM1309CGLYA312−12.18895.222−66.5171.0070.38AATOM1310OGLYA312−12.51594.070−66.7781.0069.42AATOM1311NTHRA313−12.42096.248−67.3211.0068.96AATOM1312CATHRA313−13.08296.131−68.6071.0068.24AATOM1313CBTHRA313−14.45896.839−68.5791.0067.34AATOM1314OG1THRA313−15.34496.121−67.7121.0065.56AATOM1315CG2THRA313−15.05396.919−69.9811.0067.08AATOM1316CTHRA313−12.19896.781−69.6801.0067.17AATOM1317OTHRA313−12.18398.004−69.8391.0066.98AATOM1318NPROA314−11.46895.958−70.4381.0065.72AATOM1319CDPROA314−11.84394.553−70.6881.0067.12AATOM1320CAPROA314−10.58396.436−71.4911.0065.27AATOM1321CBPROA314−11.03395.607−72.6771.0065.64AATOM1322CGPROA314−11.19894.260−72.0481.0067.64AATOM1323CPROA314−10.61897.937−71.7641.0063.03AATOM1324OPROA314−10.23898.754−70.9211.0062.60AATOM1325NGLUA315−11.07698.280−72.9601.0061.49AATOM1326CAGLUA315−11.19299.665−73.4361.0058.28AATOM1327CBGLUA315−11.86899.660−74.8151.0056.91AATOM1328CGGLUA315−11.52098.451−75.7081.0056.55AATOM1329CDGLUA315−11.87197.082−75.0901.0055.97AATOM1330OE1GLUA315−12.84596.976−74.3151.0054.66AATOM1331OE2GLUA315−11.17796.096−75.4011.0054.71AATOM1332CGLUA315−11.975100.605−72.4931.0055.25AATOM1333OGLUA315−12.296101.726−72.8711.0053.46AATOM1334NTYRA316−12.258100.147−71.2741.0053.16AATOM1335CATYRA316−13.021100.924−70.2981.0051.85AATOM1336CBTYRA316−14.293100.167−69.8871.0054.53AATOM1337CGTYRA316−15.527100.441−70.7191.0056.84AATOM1338CD1TYRA316−15.83899.647−71.8331.0056.81AATOM1339CE1TYRA316−16.98099.894−72.5961.0056.47AATOM1340CD2TYRA316−16.395101.492−70.3891.0056.21AATOM1341CE2TYRA316−17.539101.744−71.1511.0055.90AATOM1342CZTYRA316−17.821100.943−72.2531.0055.67AATOM1343OHTYRA316−18.921101.204−73.0371.0056.04AATOM1344CTYRA316−12.309101.329−69.0031.0047.86AATOM1345OTYRA316−12.642102.357−68.4211.0048.81AATOM1346NLEUA317−11.370100.525−68.5281.0041.96AATOM1347CALEUA317−10.702100.868−67.2831.0038.08AATOM1348CBLEUA317−9.55099.891−67.0011.0036.93AATOM1349CGLEUA317−9.94198.607−66.2561.0034.10AATOM1350CD1LEUA317−8.82098.231−65.2991.0033.28AATOM1351CD2LEUA317−11.21698.815−65.4711.0032.46AATOM1352CLEUA317−10.212102.319−67.2241.0035.05AATOM1353OLEUA317−9.776102.871−68.2231.0033.58AATOM1354NALAA318−10.304102.927−66.0441.0032.34AATOM1355CAALAA318−9.905104.310−65.8541.0034.07AATOM1356CBALAA318−10.747104.933−64.7481.0032.53AATOM1357CALAA318−8.410104.471−65.5431.0035.01AATOM1358OALAA318−7.841103.700−64.7731.0037.39AATOM1359NPROA319−7.755105.487−66.1291.0033.94AATOM1360CDPROA319−8.257106.556−67.0051.0034.01AATOM1361CAPROA319−6.329105.665−65.8571.0033.57AATOM1362CBPROA319−6.020107.053−66.4341.0033.33AATOM1363CGPROA319−7.367107.700−66.6111.0034.75AATOM1364CPROA319−5.924105.520−64.4041.0034.03AATOM1365OPROA319−5.033104.739−64.0951.0034.93AATOM1366NGLUA320−6.571106.254−63.5061.0035.74AATOM1367CAGLUA320−6.216106.168−62.0891.0036.67AATOM1368CBGLUA320−7.027107.166−61.2431.0036.20AATOM1369CGGLUA320−8.520106.843−61.1471.0036.13AATOM1370CDGLUA320−9.344107.541−62.2001.0036.06AATOM1371OE1GLUA320−8.959107.535−63.3831.0036.56AATOM1372OE2GLUA320−10.390108.096−61.8391.0035.80AATOM1373CGLUA320−6.443104.740−61.5761.0037.87AATOM1374OGLUA320−5.766104.289−60.6461.0038.06AATOM1375NVALA321−7.399104.030−62.1691.0036.31AATOM1376CAVALA321−7.638102.667−61.7551.0036.60AATOM1377CBVALA321−8.908102.086−62.3961.0036.12AATOM1378CG1VALA321−8.998100.595−62.1231.0033.41AATOM1379CG2VALA321−10.136102.787−61.8271.0035.14AATOM1380CVALA321−6.431101.884−62.2291.0038.65AATOM1381OVALA321−6.037100.902−61.6051.0041.18AATOM1382NLEUA322−5.821102.335−63.3221.0039.36AATOM1383CALEUA322−4.654101.649−63.8801.0039.61AATOM1384CBLEUA322−4.520101.940−65.3811.0037.36AATOM1385CGLEUA322−5.685101.511−66.2761.0035.40AATOM1386CD1LEUA322−5.399101.809−67.7551.0032.58AATOM1387CD2LEUA322−5.922100.042−66.0511.0033.55AATOM1388CLEUA322−3.348102.000−63.1861.0040.65AATOM1389OLEUA322−2.602101.124−62.7681.0040.96AATOM1390NGLUA323−3.065103.287−63.0711.0042.76AATOM1391CAGLUA323−1.831103.736−62.4341.0044.83AATOM1392CBGLUA323−1.688105.257−62.6241.0044.50AATOM1393CGGLUA323−0.305105.846−62.3811.0045.98AATOM1394CDGLUA323−0.173107.299−62.8921.0047.67AATOM1395OE1GLUA323−1.042108.160−62.5861.0047.60AATOM1396OE2GLUA3230.818107.592−63.5951.0046.81AATOM1397CGLUA323−1.906103.364−60.9581.0046.00AATOM1398OGLUA323−1.192103.917−60.1401.0046.72AATOM1399NASPA324−2.784102.417−60.6341.0047.83AATOM1400CAASPA324−2.994101.950−59.2611.0049.37AATOM1401CBASPA324−1.683101.529−58.6001.0051.34AATOM1402CGASPA324−0.872100.577−59.4501.0051.23AATOM1403OD1ASPA324−1.17499.348−59.4671.0049.81AATOM1404OD2ASPA3240.073101.078−60.0931.0050.14AATOM1405CASPA324−3.590103.048−58.4261.0049.80AATOM1406OASPA324−4.109102.787−57.3461.0048.34AATOM1407NASNA325−3.480104.276−58.9231.0052.04AATOM1408CAASNA325−4.002105.450−58.2341.0056.14AATOM1409CBASNA325−4.011106.655−59.1691.0058.77AATOM1410CGASNA325−2.976107.692−58.7891.0060.00AATOM1411OD1ASNA325−1.765107.401−58.7261.0059.63AATOM1412ND2ASNA325−3.446108.917−58.5251.0059.01AATOM1413CASNA325−5.404105.200−57.7131.0057.52AATOM1414OASNA325−6.342105.001−58.4801.0056.92AATOM1415NASPA326−5.532105.214−56.3921.0058.30AATOM1416CAASPA326−6.806104.958−55.7451.0057.19AATOM1417CBASPA326−6.778105.439−54.2931.0057.07AATOM1418CGASPA326−7.366104.422−53.3431.0056.28AATOM1419OD1ASPA326−8.436103.856−53.6751.0054.26AATOM1420OD2ASPA326−6.772104.197−52.2691.0056.03AATOM1421CASPA326−7.923105.640−56.4961.0055.86AATOM1422OASPA326−7.730106.702−57.0791.0056.11AATOM1423NTYRA327−9.092105.018−56.4811.0055.34AATOM1424CATYRA327−10.236105.574−57.1781.0054.96AATOM1425CBTYRA327−10.660104.630−58.3001.0055.94AATOM1426CGTYRA327−11.246103.330−57.8201.0055.51AATOM1427CD1TYRA327−12.449103.299−57.1261.0054.72AATOM1428CE1TYRA327−12.989102.114−56.6981.0056.28AATOM1429CD2TYRA327−10.601102.131−58.0711.0056.68AATOM1430CE2TYRA327−11.134100.933−57.6461.0057.44AATOM1431CZTYRA327−12.326100.930−56.9581.0057.63AATOM1432OHTYRA327−12.83599.734−56.5011.0059.73AATOM1433CTYRA327−11.439105.889−56.2841.0053.95AATOM1434OTYRA327−11.480105.544−55.1001.0055.45AATOM1435NGLYA328−12.422106.547−56.8751.0050.71AATOM1436CAGLYA328−13.612106.912−56.1411.0048.37AATOM1437CGLYA328−14.716107.059−57.1501.0046.26AATOM1438OGLYA328−14.754106.292−58.1111.0046.78AATOM1439NARGA329−15.591108.044−56.9661.0041.48AATOM1440CAARGA329−16.682108.219−57.9031.0037.24AATOM1441CBARGA329−17.587109.383−57.5131.0037.63AATOM1442CGARGA329−17.764109.646−56.0571.0036.06AATOM1443CDARGA329−16.844110.758−55.6291.0035.26AATOM1444NEARGA329−16.817111.840−56.6011.0033.75AATOM1445CZARGA329−16.106112.955−56.4561.0035.19AATOM1446NH1ARGA329−15.364113.145−55.3741.0034.20AATOM1447NH2ARGA329−16.121113.882−57.4001.0036.43AATOM1448CARGA329−16.149108.487−59.2981.0035.05AATOM1449OARGA329−16.646107.927−60.2631.0036.56AATOM1450NALAA330−15.136109.340−59.3931.0031.90AATOM1451CAALAA330−14.550109.723−60.6691.0030.63AATOM1452CBALAA330−13.257110.459−60.4411.0030.72AATOM1453CALAA330−14.336108.644−61.7151.0029.98AATOM1454OALAA330−14.145108.974−62.8671.0031.64AATOM1455NVALA331−14.342107.366−61.3521.0029.53AATOM1456CAVALA331−14.169106.318−62.3671.0027.58AATOM1457CBVALA331−13.489105.011−61.8081.0026.39AATOM1458CG1VALA331−12.252105.376−61.0371.0026.09AATOM1459CG2VALA331−14.454104.199−60.9551.0023.49AATOM1460CVALA331−15.529105.954−62.9621.0026.82AATOM1461OVALA331−15.608105.294−63.9991.0028.10AATOM1462NASPA332−16.596106.380−62.2961.0023.56AATOM1463CAASPA332−17.939106.120−62.7771.0024.79AATOM1464CBASPA332−18.950106.312−61.6471.0025.46AATOM1465CGASPA332−19.033105.123−60.7291.0027.62AATOM1466OD1ASPA332−19.285104.018−61.2151.0030.62AATOM1467OD2ASPA332−18.854105.276−59.5131.0029.68AATOM1468CASPA332−18.221107.115−63.8971.0025.01AATOM1469OASPA332−18.965106.854−64.8331.0026.25AATOM1470NTRPA333−17.594108.266−63.7771.0024.60AATOM1471CATRPA333−17.748109.336−64.7221.0023.25AATOM1472CBTRPA333−17.236110.606−64.0761.0025.29AATOM1473CGTRPA333−18.122111.016−62.9561.0026.30AATOM1474CD2TRPA333−19.558111.047−62.9751.0026.84AATOM1475CE2TRPA333−19.979111.535−61.7301.0027.00AATOM1476CE3TRPA333−20.530110.712−63.9341.0027.23AATOM1477CD1TRPA333−17.745111.465−61.7361.0027.59AATOM1478NE1TRPA333−18.854111.784−60.9881.0029.34AATOM1479CZ2TRPA333−21.330111.698−61.4121.0025.21AATOM1480CZ3TRPA333−21.867110.875−63.6161.0024.16AATOM1481CH2TRPA333−22.254111.366−62.3651.0023.45AATOM1482CTRPA333−17.004109.000−65.9651.0023.53AATOM1483OTRPA333−17.494109.228−67.0631.0023.81AATOM1484NTRPA334−15.807108.452−65.7721.0024.61AATOM1485CATRPA334−14.938107.993−66.8571.0022.69AATOM1486CBTRPA334−13.617107.483−66.2581.0023.94AATOM1487CGTRPA334−12.796106.588−67.1711.0027.74AATOM1488CD2TRPA334−11.743106.998−68.0491.0028.58AATOM1489CE2TRPA334−11.309105.852−68.7421.0027.50AATOM1490CE3TRPA334−11.125108.229−68.3211.0029.45AATOM1491CD1TRPA334−12.945105.233−67.3661.0024.94AATOM1492NE1TRPA334−12.059104.793−68.3021.0025.22AATOM1493CZ2TEPA334−10.288105.900−69.6861.0028.75AATOM1494CZ3TRPA334−10.109108.274−69.2591.0028.55AATOM1495CH2TRPA334−9.703107.120−69.9301.0029.40AATOM1496CTRPA334−15.682106.872−67.6071.0020.19AATOM1497OTRPA334−15.746106.845−68.8241.0017.98AATOM1498NGLYA335−16.265105.956−66.8551.0018.67AATOM1499CAGLYA335−17.004104.878−67.4671.0020.33AATOM1500CGLYA335−18.069105.391−68.4001.0021.63AATOM1501OGLYA335−18.236104.862−69.4891.0023.51AATOM1502NLEUA336−18.787106.421−67.9631.0023.99AATOM1503CALEUA336−19.863107.049−68.7261.0024.84AATOM1504CBLEUA336−20.535108.121−67.8731.0024.67AATOM1505CGLEUA336−21.839108.729−68.3941.0025.55AATOM1506CD1LEUA336−22.988107.739−68.1701.0025.24AATOM1507CD2LEUA336−22.103110.052−67.6851.0023.57AATOM1508CLEUA336−19.363107.687−70.0181.0026.87AATOM1509OLEUA336−19.949107.499−71.0781.0027.17AATOM1510NGLYA337−18.288108.458−69.9111.0027.61AATOM1511CAGLYA337−17.717109.106−71.0731.0029.23AATOM1512CGLYA337−17.258108.141−72.1491.0029.61AATOM1513OGLYA337−17.309108.459−73.3311.0030.14AATOM1514NVALA338−16.790106.966−71.7371.0030.37AATOM1515CAVALA338−16.342105.942−72.6791.0030.86AATOM1516CBVALA338−15.590104.784−71.9601.0031.23AATOM1517CG1VALA338−15.493103.583−72.8621.0029.09AATOM1518CG2VALA338−14.181105.224−71.5911.0030.70AATOM1519CVALA338−17.579105.403−73.3721.0030.82AATOM1520OVALA338−17.595105.235−74.5841.0031.75AATOM1521NVALA339−18.625105.152−72.5961.0031.86AATOM1522CAVALA339−19.879104.661−73.1491.0034.51AATOM1523CBVALA339−20.935104.438−72.0361.0034.77AATOM1524CG1VALA339−22.165103.763−72.6071.0033.66AATOM1525CG2VALA339−20.354103.587−70.9381.0034.82AATOM1526CVALA339−20.420105.697−74.1461.0036.29AATOM1527OVALA339−20.900105.353−75.2171.0036.95AATOM1528NMETA340−20.329106.972−73.7921.0037.21AATOM1529CAMETA340−20.818108.025−74.6681.0038.32AATOM1530CBMETA340−20.970109.322−73.9071.0037.63AATOM1531CGMETA340−22.325109.906−74.0681.0038.53AATOM1532SDMETA340−23.123109.959−72.5101.0039.47AATOM1533CEMETA340−21.792110.826−71.5821.0038.30AATOM1534CMETA340−19.911108.265−75.8551.0038.66AATOM1535OMETA340−20.297108.919−76.8201.0039.35AATOM1536NTYRA341−18.690107.761−75.7801.0037.91AATOM1537CATYRA341−17.792107.937−76.9021.0037.35AATOM1538CBTYRA341−16.362107.567−76.5481.0035.13AATOM1539CGTYRA341−15.423107.906−77.6621.0034.49AATOM1540CD1TYRA341−15.518107.270−78.8991.0033.81AATOM1541CE1TYRA341−14.680107.618−79.9501.0035.18AATOM1542CD2TYRA341−14.464108.900−77.5011.0035.70AATOM1543CE2TYRA341−13.615109.261−78.5471.0036.06AATOM1544CZTYRA341−13.726108.618−79.7681.0035.95AATOM1545OHTYRA341−12.888108.981−80.7971.0036.52AATOM1546CTYRA341−18.285106.987−77.9591.0037.38AATOM1547OTYRA341−18.443107.347−79.1181.0038.53AATOM1548NGLUA342−18.531105.760−77.5321.0035.93AATOM1549CAGLUA342−19.002104.728−78.4161.0035.30AATOM1550CBGLUA342−18.995103.402−77.6481.0036.37AATOM1551CGGLUA342−19.528102.192−78.3901.0038.72AATOM1552CDGLUA342−18.825100.898−77.9731.0042.11AATOM1553OE1GLUA342−18.517100.709−76.7691.0040.90AATOM1554OE2GLUA342−18.582100.058−78.8621.0044.17AATOM1555CGLUA342−20.390105.064−78.9581.0034.62AATOM1556OGLUA342−20.609105.087−80.1671.0033.33AATOM1557NMETA343−21.319105.363−78.0621.0034.80AATOM1558CAMETA343−22.686105.655−78.4591.0033.07AATOM1559CBMETA343−23.496106.155−77.2621.0032.99AATOM1560CGMETA343−23.962105.088−76.2861.0031.45AATOM1561SDMETA343−25.158105.770−75.0851.0034.71AATOM1562CEMETA343−26.066104.347−74.6371.0030.72AATOM1563CMETA343−22.823106.656−79.5931.0033.70AATOM1564OMETA343−23.675106.486−80.4531.0034.72AATOM1565NMETA344−21.989107.693−79.6041.0032.31AATOM1566CAMETA344−22.080108.728−80.6311.0031.25AATOM1567CBMETA344−21.996110.091−79.9601.0030.36AATOM1568CGMETA344−22.881110.196−78.7271.0030.78AATOM1569SDMETA344−23.399111.855−78.3201.0033.40AATOM1570CEMETA344−22.242112.378−77.0811.0027.81AATOM1571CMETA344−21.040108.639−81.7441.0033.24AATOM1572OMETA344−21.198109.244−82.8111.0033.06AATOM1573NCYSA345−19.970107.886−81.4911.0033.58AATOM1574CACYSA345−18.914107.721−82.4651.0030.35AATOM1575CBCYSA345−17.570108.071−81.8471.0029.51AATOM1576SGCYSA345−17.464109.713−81.1031.0028.81AATOM1577CCYSA345−18.890106.298−82.9821.0031.60AATOM1578OCYSA345−17.977105.926−83.6991.0032.43AATOM1579NGLYA346−19.895105.507−82.6121.0032.93AATOM1580CAGLYA346−20.002104.127−83.0681.0034.64AATOM1581CGLYA346−18.800103.236−82.8261.0037.57AATOM1582OGLYA346−18.863102.007−82.9761.0037.29AATOM1583NARGA347−17.705103.865−82.4171.0038.88AATOM1584CAARGA347−16.456103.177−82.1761.0040.60AATOM1585CBARGA347−15.498103.503−83.3301.0042.28AATOM1586CGARGA347−14.947104.928−83.2681.0045.81AATOM1587CDARGA347−14.730105.556−84.6351.0046.25AATOM1588NEARGA347−13.805106.693−84.5591.0048.33AATOM1589CZARGA347−13.709107.659−85.4741.0049.83AATOM1590NH1ARGA347−14.493107.647−86.5441.0048.95AATOM1591NH2ARGA347−12.799108.624−85.3431.0048.33AATOM1592CARGA347−15.868103.641−80.8431.0040.34AATOM1593OARGA347−16.241104.695−80.3261.0038.20AATOM1594NLEUA348−14.955102.848−80.2871.0040.05AATOM1595CALEUA348−14.311103.206−79.0321.0040.55AATOM1596CBLEUA348−13.954101.952−78.2461.0037.02AATOM1597CGLEUA348−15.058101.388−77.3571.0034.76AATOM1598CD1LEUA348−14.617100.083−76.7561.0033.49AATOM1599CD2LEUA348−15.381102.376−76.2641.0033.75AATOM1600CLEUA348−13.062104.017−79.3381.0042.53AATOM1601OLEUA348−12.307103.680−80.2391.0042.44AATOM1602NPROA349−12.817105.088−78.5721.0045.77AATOM1603CDPROA349−13.370105.301−77.2231.0045.24AATOM1604CAPROA349−11.639105.940−78.8011.0049.88AATOM1605CBPROA349−11.524106.746−77.4971.0048.25AATOM1606CGPROA349−12.201105.884−76.4851.0046.99AATOM1607CPROA349−10.373105.153−79.1401.0053.33AATOM1608OPROA349−9.553105.585−79.9511.0053.67AATOM1609NPHEA350−10.228103.994−78.5071.0057.43AATOM1610CAPHEA350−9.094103.113−78.7361.0061.40AATOM1611CBPHEA350−8.243102.938−77.4701.0060.86AATOM1612CGPHEA350−7.579104.197−76.9861.0059.81AATOM1613CD1PHEA350−7.126104.286−75.6691.0059.25AATOM1614CD2PHEA350−7.408105.285−77.8211.0058.02AATOM1615CE1PHEA350−6.525105.437−75.1971.0057.00AATOM1616CE2PHEA350−6.806106.441−77.3521.0057.83AATOM1617CZPHEA350−6.365106.514−76.0381.0057.19AATOM1618CPHEA350−9.715101.773−79.0881.0064.90AATOM1619OPHEA350−10.342101.117−78.2291.0064.17AATOM1620NTYRA351−9.550101.386−80.3511.0066.85AATOM1621CATYRA351−10.071100.123−80.8571.0068.83AATOM1622CBTYRA351−11.390100.355−81.6051.0068.47AATOM1623CGTYRA351−11.241100.959−82.9891.0068.33AATOM1624CD1TYRA351−11.138100.140−84.1161.0068.03AATOM1625CE1TYRA351−11.017100.680−85.3941.0067.30AATOM1626CD2TYRA351−11.213102.346−83.1761.0067.76AATOM1627CE2TYRA351−11.091102.904−84.4541.0066.51AATOM1628CZTYRA351−10.997102.061−85.5621.0067.80AATOM1629OHTYRA351−10.914102.580−86.8431.0066.85AATOM1630CTYRA351−9.01699.575−81.8041.0070.67AATOM1631OTYRA351−8.425100.338−82.5861.0071.18AATOM1632NASNA352−8.77098.266−81.7361.0071.80AATOM1633CAASNA352−7.76497.642−82.6031.0072.00AATOM1634CBASNA352−6.36297.727−81.9781.0069.26AATOM1635CGASNA352−5.70599.066−82.1851.0064.92AATOM1636OD1ASNA352−5.85899.696−83.2411.0062.88AATOM1637ND2ASNA352−4.94899.509−81.1801.0062.64AATOM1638CASNA352−7.97696.188−82.9861.0072.98AATOM1639OASNA352−9.09195.663−83.0251.0073.91AATOM1640NGLNA353−6.83895.565−83.2691.0073.41AATOM1641CAGLNA353−6.73194.177−83.6621.0073.01AATOM1642CBGLNA353−6.02394.072−85.0241.0072.45AATOM1643CGGLNA353−6.59394.959−86.1451.0072.29AATOM1644CDGLNA353−5.58995.194−87.2891.0071.25AATOM1645OE1GLNA353−4.89694.260−87.7331.0071.23AATOM1646NE2GLNA353−5.51596.442−87.7771.0069.34AATOM1647CGLNA353−5.85893.537−82.5831.0072.33AATOM1648OGLNA353−5.05192.654−82.8791.0073.66AATOM1649NASPA354−6.00793.999−81.3401.0070.59AATOM1650CAASPA354−5.22493.461−80.2231.0069.03AATOM1651CBASPA354−3.72793.585−80.5321.0067.78AATOM1652CGASPA354−3.03292.236−80.6461.0067.35AATOM1653OD1ASPA354−3.60891.310−81.2641.0067.99AATOM1654OD2ASPA354−1.89992.110−80.1291.0067.47AATOM1655CASPA354−5.51794.127−78.8751.0068.09AATOM1656OASPA354−5.40395.351−78.7321.0067.53AATOM1657NHISA355−5.89293.314−77.8891.0067.65AATOM1658CAHISA355−6.18293.816−76.5461.0067.60AATOM1659CBHISA355−6.74292.703−75.6521.0067.55AATOM1660CGHISA355−8.21092.460−75.8261.0067.24AATOM1661CD2HISA355−9.26192.746−75.0181.0067.09AATOM1662ND1HISA355−8.74591.871−76.9541.0067.46AATOM1663CE1HISA355−10.06291.807−76.8341.0066.78AATOM1664NE2HISA355−10.40092.330−75.6681.0067.42AATOM1665CHISA355−4.90894.375−75.9201.0067.46AATOM1666OHISA355−4.87595.532−75.5011.0067.39AATOM1667NGLUA356−3.86493.547−75.8561.0067.04AATOM1668CAGLUA356−2.57893.967−75.2951.0065.33AATOM1669CBGLUA356−1.61392.765−75.1831.0063.15AATOM1670CGGLUA356−2.22491.511−74.5081.0058.60AATOM1671CDGLUA356−1.19890.420−74.1231.0056.10AATOM1672OE1GLUA356−0.30890.081−74.9371.0052.87AATOM1673OE2GLUA356−1.30589.879−72.9981.0053.91AATOM1674CGLUA356−2.00795.040−76.2341.0064.93AATOM1675OGLUA356−1.08294.783−77.0061.0063.85AATOM1676NARGA357−2.58296.241−76.1511.0063.08AATOM1677CAARGA357−2.20097.376−76.9861.0060.83AATOM1678CBARGA357−3.04697.388−78.2591.0060.63AATOM1679CGARGA357−2.38596.856−79.5051.0061.39AATOM1680CDARGA357−3.36096.895−80.6791.0060.19AATOM1681NEARGA357−2.86796.093−81.7921.0058.45AATOM1682CZARGA357−1.76596.376−82.4741.0058.35AATOM1683NH1ARGA357−1.05497.456−82.1471.0057.33AATOM1684NH2ARGA357−1.36395.573−83.4691.0057.73AATOM1685CARGA357−2.44098.710−76.2971.0060.25AATOM1686OARGA357−1.62899.633−76.3951.0058.35AATOM1687NLEUA358−3.58198.790−75.6111.0058.90AATOM1688CALEUA358−4.036100.014−74.9581.0056.98AATOM1689CBLEUA358−5.533100.218−75.2711.0056.75AATOM1690CGLEUA358−6.61599.341−74.6051.0054.50AATOM1691CD1LEUA358−7.95499.621−75.2561.0053.65AATOM1692CD2LEUA358−6.27097.859−74.7221.0052.82AATOM1693CLEUA358−3.820100.168−73.4621.0056.02AATOM1694OLEUA358−4.244101.161−72.8841.0055.19AATOM1695NPHEA359−3.16299.203−72.8351.0056.21AATOM1696CAPHEA359−2.91399.265−71.3891.0055.48AATOM1697CBPHEA359−2.47397.885−70.8711.0058.44AATOM1698CGPHEA359−3.59596.876−70.7841.0060.94AATOM1699CD1PHEA359−4.44096.648−71.8741.0062.04AATOM1700CD2PHEA359−3.80396.151−69.6101.0061.26AATOM1701CE1PHEA359−5.48295.713−71.7931.0062.67AATOM1702CE2PHEA359−4.84195.213−69.5181.0062.59AATOM1703CZPHEA359−5.68294.993−70.6111.0062.70AATOM1704CPHEA359−1.878100.317−71.0011.0052.84AATOM1705OPHEA359−1.333100.284−69.9001.0051.58AATOM1706NGLUA360−1.615101.234−71.9291.0050.81AATOM1707CAGLUA360−0.659102.329−71.7541.0048.44AATOM1708CBGLUA3600.788101.846−71.9301.0048.67AATOM1709CGGLUA3600.945100.450−72.4951.0048.17AATOM1710CDGLUA3601.092100.454−73.9811.0048.83AATOM1711OE1GLUA3600.42999.636−74.6421.0051.50AATOM1712OE2GLUA3601.877101.271−74.4921.0049.43AATOM1713CGLUA360−0.969103.409−72.7761.0046.64AATOM1714OGLUA360−0.224104.377−72.9311.0046.72AATOM1715NLEUA361−2.082103.205−73.4741.0044.35AATOM1716CALEUA361−2.595104.126−74.4751.0041.50AATOM1717CBLEUA361−3.310103.345−75.5911.0039.48AATOM1718CGLEUA361−2.713103.296−77.0031.0036.25AATOM1719CD1LEUA361−3.603102.547−77.9581.0033.77AATOM1720CD2LEUA361−2.562104.677−77.5051.0034.78AATOM1721CLEUA361−3.596105.007−73.7251.0041.11AATOM1722OLEUA361−3.715106.194−73.9841.0041.16AATOM1723NILEA362−4.306104.397−72.7831.0040.61AATOM1724CAILEA362−5.297105.083−71.9581.0041.06AATOM1725CBILEA362−6.197104.061−71.2141.0039.14AATOM1726CG2ILEA362−7.057104.764−70.2011.0036.58AATOM1727CG1ILEA362−7.049103.284−72.2131.0036.16AATOM1728CD1ILEA362−7.828102.166−71.6001.0033.30AATOM1729CILEA362−4.643105.988−70.9081.0042.37AATOM1730OILEA362−5.263106.927−70.4171.0042.48AATOM1731NLEUA363−3.390105.705−70.5671.0043.15AATOM1732CALEUA363−2.682106.483−69.5601.0041.88AATOM1733CBLEUA363−1.797105.558−68.7261.0039.50AATOM1734CGLEUA363−2.484104.738−67.6241.0038.79AATOM1735CD1LEUA363−1.611103.558−67.2261.0037.68AATOM1736CD2LEUA363−2.779105.622−66.4171.0037.32AATOM1737CLEUA363−1.850107.642−70.0881.0043.44AATOM1738OLEUA363−1.427108.494−69.3131.0043.50AATOM1739NMETA364−1.621107.688−71.3991.0044.79AATOM1740CAMETA364−0.816108.759−71.9931.0045.39AATOM1741CBMETA3640.651108.325−72.0641.0044.16AATOM1742CGMETA3641.254107.978−70.7221.0042.09AATOM1743SDMETA3642.816107.070−70.8121.0040.78AATOM1744CEMETA3642.370105.550−70.0251.0040.87AATOM1745CMETA364−1.252109.230−73.3831.0046.56AATOM1746OMETA364−0.596110.084−73.9701.0047.17AATOM1747NGLUA365−2.338108.680−73.9191.0046.18AATOM1748CAGLUA365−2.794109.096−75.2421.0046.62AATOM1749CBGLUA365−3.069107.900−76.1421.0045.43AATOM1750CGCLDA365−1.974107.628−77.1481.0045.51AATOM1751CDGLUA365−1.858108.665−78.2591.0043.01AATOM1752OE1GLUA365−1.281109.756−78.0421.0042.64AATOM1753OE2GLUA365−2.339108.369−79.3631.0041.76AATOM1754CGLUA365−4.011109.988−75.2931.0047.27AATOM1755OGLUA365−4.920109.902−74.4741.0047.46AATOM1756NGLUA366−4.009110.828−76.3141.0048.61AATOM1757CAGLUA366−5.065111.778−76.5741.0050.19AATOM1758CBGLUA366−4.557112.821−77.5711.0052.21AATOM1759CGGLUA366−3.059113.108−77.4691.0052.47AATOM1760CDGLUA366−2.496113.737−78.7370.0051.77AATOM1761OE1GLUA366−2.503113.069−79.7891.0050.96AATOM1762OE2GLUA366−2.048114.900−78.6911.0052.02AATOM1763CGLUA366−6.262111.048−77.1771.0050.93AATOM1764OGLUA366−6.117110.270−78.1191.0051.55AATOM1765NILEA367−7.443111.287−76.6241.0050.06AATOM1766CAILEA367−8.644110.672−77.1601.0049.58AATOM1767CBILEA367−9.635110.286−76.0301.0048.32AATOM1768CG2ILEA367−11.040110.168−76.5751.0048.47AATOM1769CG1ILEA367−9.184108.955−75.4051.0048.00AATOM1770CD1ILEA367−9.969108.474−74.1871.0045.21AATOM1771CILEA367−9.239111.699−78.1241.0049.83AATOM1772OILEA367−9.702112.767−77.7151.0050.38AATOM1773NARGA368−9.171111.377−79.4151.0049.10AATOM1774CAARGA368−9.669112.250−80.4611.0047.08AATOM1775CBARGA368−8.817112.101−81.7201.0048.41AATOM1776CGARGA368−7.376112.542−81.5391.0050.42AATOM1777CDARGA368−6.605112.475−82.8440.0052.02AATOM1778NEARGA368−7.160113.376−83.8500.0053.60AATOM1779CZARGA368−6.650113.543−85.0650.0054.42AATOM1780NH1ARGA368−5.568112.868−85.4300.0054.95AATOM1781NH2ARGA368−7.220114.384−85.9160.0054.95AATOM1782CARGA368−11.112111.935−80.7801.0045.04AATOM1783OARGA368−11.563110.812−80.5971.0043.92AATOM1784NPHEA369−11.828112.946−81.2621.0044.17AATOM1785CAPHEA369−13.237112.822−81.6161.0042.41AATOM1786CBPHEA369−14.062113.787−80.7581.0041.47AATOM1787CGPHEA369−13.627113.835−79.3251.0041.31AATOM1788CD1PHEA369−14.081112.893−78.4081.0040.46AATOM1789CD2PHEA369−12.694114.773−78.9051.0040.29AATOM1790CE1PHEA369−13.604112.890−77.1051.0039.25AATOM1791CE2PHEA369−12.213114.770−77.5971.0038.36AATOM1792CZPHEA369−12.666113.834−76.7051.0038.31AATOM1793CPHEA369−13.447113.156−83.0971.0042.29AATOM1794OPHEA369−12.685113.916−83.7011.0042.06AATOM1795NPROA370−14.475112.571−83.7131.0042.63AATOM1796CDPROA370−15.369111.488−83.2691.0041.99AATOM1797CAPROA370−14.689112.892−85.1201.0043.64AATOM1798CBPROA370−15.960112.126−85.4471.0042.72AATOM1799CGPROA370−15.832110.907−84.5761.0042.44AATOM1800CPROA370−14.878114.395−85.2581.0045.92AATOM1801OPROA370−14.827115.127−84.2771.0045.82AATOM1802NARGA371−15.083114.861−86.4811.0049.54AATOM1803CAARGA371−15.319116.282−86.7121.0050.65AATOM1804CBARGA371−14.985116.649−88.1611.0051.72AATOM1805CGARGA371−14.061115.656−88.8731.0052.39AATOM1806CDARGA371−13.701116.170−90.2711.0054.02AATOM1807NEARGA371−13.275115.105−91.1751.0054.49AATOM1808CZARGA371−14.101114.351−91.9031.0053.61AATOM1809NH1ARGA371−15.420114.539−91.8501.0052.26AATOM1810NH2ARGA371−13.600113.398−92.6791.0052.07AATOM1811CARGA371−16.817116.447−86.4561.0051.39AATOM1812OARGA371−17.257117.411−85.8281.0051.37AATOM1813NTHRA372−17.570115.459−86.9411.0050.88AATOM1814CATHRA372−19.023115.356−86.8181.0050.83AATOM1815CBTHRA372−19.507114.071−87.4381.0050.23AATOM1816OG1THRA372−18.401113.414−88.0681.0049.03AATOM1817CG2THRA372−20.627114.346−88.4171.0049.67AATOM1818CTHRA372−19.545115.311−85.3821.0051.79AATOM1819OTHRA372−20.655114.818−85.1361.0051.82AATOM1820NLEUA373−18.753115.791−84.4341.0050.84AATOM1821CALEUA373−19.169115.762−83.0471.0048.92AATOM1822CBLEUA373−18.029115.247−82.1661.0047.97AATOM1823CGLEUA373−18.446114.519−80.8891.0046.19AATOM1824CD1LEUA373−19.127113.208−81.2421.0045.21AATOM1825CD2LEUA373−17.224114.266−80.0381.0047.17AATOM1826CLEUA373−19.540117.166−82.6471.0048.09AATOM1827OLEUA373−18.676118.040−82.6021.0048.56AATOM1828NSERA374−20.823117.379−82.3671.0047.93AATOM1829CASERA374−21.308118.691−81.9671.0049.03AATOM1830CBSERA374−22.617118.581−81.1931.0047.65AATOM1831OGSERA374−22.382118.167−79.8581.0046.63AATOM1832CSERA374−20.268119.332−81.0731.0050.48AATOM1833OSERA374−19.558118.647−80.3411.0050.96AATOM1834NPROA375−20.152120.662−81.1301.0051.38AATOM1835CDPROA375−20.942121.628−81.9151.0050.30AATOM1836CAPROA375−19.165121.337−80.2841.0051.78AATOM1837CBPROA375−19.373122.815−80.6221.0051.95AATOM1838CGPROA375−20.824122.876−81.0811.0051.37AATOM1839CPROA375−19.372121.021−78.8041.0051.12AATOM1840OPROA375−18.418120.716−78.0871.0050.68AATOM1841NGLUA376−20.622121.077−78.3551.0050.44AATOM1842CAGLUA376−20.940120.796−76.9591.0050.98AATOM1843CBGLUA376−22.413121.107−76.6821.0051.55AATOM1844CGGLUA376−22.744122.572−76.9331.0056.21AATOM1845CDGLUA376−24.226122.900−76.7871.0057.71AATOM1846OE1GLUA376−25.057122.171−77.4051.0058.41AATOM1847OE2GLUA376−24.554123.889−76.0691.0057.40AATOM1848CGLUA376−20.611119.359−76.5711.0050.65AATOM1849OGLUA376−19.955119.130−75.5551.0050.30AATOM1850NALAA377−21.047118.399−77.3881.0050.04AATOM1851CAALAA377−20.799116.978−77.1311.0049.23AATOM1852CBALAA377−21.682116.138−78.0331.0049.05AATOM1853CALAA377−19.323116.557−77.2851.0049.02AATOM1854OALAA377−18.966115.396−77.0941.0047.67AATOM1855NLYSA378−18.470117.511−77.6301.0049.27AATOM1856CALYSA378−17.048117.247−77.7851.0049.40AATOM1857CBLYSA378−16.505117.963−79.0261.0050.09AATOM1858CGLYSA378−15.056117.632−79.3441.0051.44AATOM1859CDLYSA378−14.620118.251−80.6601.0052.50AATOM1860CELYSA378−13.164117.926−80.9741.0052.00AATOM1861NZLYSA378−12.726118.550−82.2501.0049.98AATOM1862CLYSA378−16.380117.777−76.5281.0048.68AATOM1863OLYSA378−15.265117.393−76.1851.0048.48AATOM1864NSERA379−17.092118.670−75.8471.0048.49AATOM1865CASERA379−16.625119.267−74.5991.0046.75AATOM1866CBSERA379−17.388120.554−74.3091.0044.14AATOM1867OGSERA379−16.817121.223−73.2091.0039.06AATOM1868CSERA379−16.911118.249−73.5051.0046.36AATOM1869OSERA379−16.113118.060−72.5801.0044.88AATOM1870NLEUA380−18.066117.597−73.6351.0045.53AATOM1871CALEUA380−18.493116.565−72.7061.0044.33AATOM1872CBLEUA380−19.820115.966−73.1621.0042.39AATOM1873CGLEUA380−20.356114.907−72.2041.0041.20AATOM1874CD1LEUA380−20.698115.566−70.8631.0039.88AATOM1875CD2LEUA380−21.565114.222−72.8091.0040.47AATOM1876CLEUA380−17.449115.460−72.6641.0044.77AATOM1877OLEUA380−16.691115.337−71.7011.0044.52AATOM1878NLEUA381−17.433114.658−73.7291.0044.80AATOM1879CALEUA381−16.505113.533−73.8831.0044.13AATOM1880CBLEUA381−16.516113.052−75.3361.0043.54AATOM1881CGLEUA381−17.851112.475−75.8091.0044.44AATOM1882CD1LEUA381−17.940112.490−77.3151.0042.79AATOM1883CD2LEUA381−17.999111.072−75.2631.0045.30AATOM1884CLEUA381−15.081113.881−73.4761.0043.00AATOM1885OLEUA381−14.385113.081−72.8651.0042.58AATOM1886NALAA382−14.651115.083−73.8171.0042.31AATOM1887CAALAA382−13.312115.504−73.4831.0041.97AATOM1888CBALAA382−12.993116.797−74.1951.0042.13AATOM1889CALAA382−13.168115.683−71.9851.0042.03AATOM1890OALAA382−12.075115.557−71.4491.0042.73AATOM1891NGLYA383−14.278115.975−71.3141.0042.56AATOM1892CAGLYA383−14.254116.199−69.8761.0041.18AATOM1893CGLYA383−14.493114.964−69.0321.0039.86AATOM1894OGLYA383−13.974114.861−67.9201.0037.66AATOM1895NLEUA384−15.299114.042−69.5561.0038.27AATOM1896CALEUA384−15.593112.799−68.8661.0038.05AATOM1897CBLEUA384−16.868112.163−69.4101.0036.40AATOM1898CGLEUA384−18.208112.776−68.9881.0036.16AATOM1899CD1LEUA384−19.354112.028−69.6661.0035.25AATOM1900CD2LEUA384−18.353112.711−67.4711.0033.07AATOM1901CLEUA384−14.435111.837−69.0531.0038.84AATOM1902OLEUA384−14.378110.793−68.4131.0041.26AATOM1903NLEUA385−13.507112.199−69.9331.0038.54AATOM1904CALEUA385−12.338111.375−70.2131.0037.80AATOM1905CBLEUA385−12.260111.037−71.6991.0034.89AATOM1906CGLEUA385−13.354110.156−72.2831.0034.69AATOM1907CD1LEUA385−13.139110.037−73.7691.0036.09AATOM1908CD2LEUA385−13.327108.785−71.6461.0035.52AATOM1909CLEUA385−11.024112.015−69.7971.0039.02AATOM1910OLEUA385−9.970111.437−70.0311.0039.50AATOM1911NLYSA386−11.068113.204−69.1991.0041.43AATOM1912CALYSA386−9.831113.851−68.7781.0042.54AATOM1913CBLYSA386−10.099115.209−68.1221.0042.65AATOM1914CGLYSA386−10.494116.285−69.1311.0045.71AATOM1915CDLYSA386−10.054117.685−68.6941.0048.93AATOM1916CELYSA386−10.357118.770−69.7561.0048.50AATOM1917NZLYSA386−11.811119.053−69.9851.0047.77AATOM1918CLYSA386−9.158112.902−67.8151.0042.73AATOM1919OLYSA386−9.711112.575−66.7681.0042.71AATOM1920NLYSA387−7.969112.448−68.1971.0042.54AATOM1921CALYSA387−7.199111.491−67.4141.0043.21AATOM1922CBLYSA387−5.786111.387−67.9751.0043.49AATOM1923CGLYSA387−5.747111.162−69.4761.0041.60AATOM1924CDLYSA387−6.243109.800−69.8881.0040.78AATOM1925CELYSA387−6.094109.644−71.3901.0041.72AATOM1926NZLYSA387−4.809110.242−71.8611.0038.93AATOM1927CLYSA387−7.141111.766−65.9221.0043.35AATOM1928OLYSA387−7.398110.867−65.1231.0044.75AATOM1929NASPA388−6.789112.989−65.5401.0043.54AATOM1930CAASPA388−6.726113.335−64.1251.0044.15AATOM1931CBASPA388−6.209114.757−63.9511.0043.62AATOM1932CGASPA388−5.635115.005−62.5761.0043.61AATOM1933OD1ASPA388−6.302114.690−61.5701.0042.68AATOM1934OD2ASPA388−4.507115.530−62.5051.0044.42AATOM1935CASPA388−8.155113.247−63.6141.0045.46AATOM1936OASPA388−9.056113.825−64.2121.0046.61AATOM1937NPROA389−8.391112.531−62.5001.0046.10AATOM1938CDPROA389−7.468111.951−61.5061.0044.92AATOM1939CAPROA389−9.767112.448−62.0231.0046.39AATOM1940CBPROA389−9.688111.364−60.9651.0044.37AATOM1941CGPROA389−8.381111.657−60.3361.0045.26AATOM1942CPROA389−10.209113.783−61.4601.0047.88AATOM1943OPROA389−11.277114.278−61.7991.0048.62AATOM1944NLYSA390−9.365114.368−60.6171.0048.64AATOM1945CALYSA390−9.655115.649−59.9911.0049.76AATOM1946CBLYSA390−8.406116.176−59.2791.0051.91AATOM1947CGLYSA390−8.097115.471−57.9571.0051.28AATOM1948CDLYSA390−6.665115.718−57.5211.0051.94AATOM1949CELYSA390−6.346114.994−56.2201.0052.72AATOM1950NZLYSA390−4.869114.972−55.9481.0052.27AATOM1951CLYSA390−10.136116.661−61.0101.0050.10AATOM1952OLYSA390−10.845117.610−60.6741.0050.03AATOM1953NGLNA391−9.756116.441−62.2621.0050.17AATOM1954CAGLNA391−10.136117.324−63.3541.0049.69AATOM1955CBGLNA391−8.929117.548−64.2611.0049.67AATOM1956CGGLNA391−8.031118.674−63.8010.0049.20AATOM1957CDGLNA391−6.719118.695−64.5430.0048.71AATOM1958OE1GLNA391−6.678118.462−65.7581.0047.00AATOM1959NE2GLNA391−5.634118.984−63.8211.0048.83AATOM1960CGLNA391−11.332116.834−64.1761.0049.45AATOM1961OGLNA391−12.016117.630−64.8201.0050.24AATOM1962NARGA392−11.589115.530−64.1381.0048.09AATOM1963CAARGA392−12.695114.929−64.8781.0047.20AATOM1964CBARGA392−12.757113.441−64.5391.0046.04AATOM1965CGARGA392−13.458112.560−65.5611.0045.97AATOM1966CDARGA392−13.185111.099−65.2591.0044.98AATOM1967NEARGA392−11.764110.884−64.9951.0044.47AATOM1968CZARGA392−11.241109.756−64.5271.0043.95AATOM1969NH1ARGA392−12.014108.717−64.2661.0043.76AATOM1970NH2ARGA392−9.939109.671−64.3111.0043.88AATOM1971CARGA392−14.026115.606−64.5381.0046.76AATOM1972OARGA392−14.095116.386−63.5881.0047.44AATOM1973NLEUA393−15.070115.332−65.3281.0046.23AATOM1974CALEUA393−16.414115.883−65.0741.0044.99AATOM1975CBLEUA393−17.281115.834−66.3261.0043.19AATOM1976CGLEUA393−17.276117.067−67.2081.0041.49AATOM1977CD1LEUA393−18.281116.891−68.3281.0040.13AATOM1978CD2LEUA393−17.620118.270−66.3611.0042.02AATOM1979CLEUA393−17.080115.042−63.9941.0045.79AATOM1980OLEUA393−17.734114.046−64.2761.0045.67AATOM1981NGLYA394−16.920115.468−62.7531.0046.54AATOM1982CAGLYA394−17.449114.716−61.6391.0046.91AATOM1983CGLYA394−16.221114.425−60.8031.0047.02AATOM1984OGLYA394−16.155113.465−60.0481.0046.57AATOM1985NGLYA395−15.219115.270−60.9881.0047.22AATOM1986CAGLYA395−13.994115.139−60.2411.0049.50AATOM1987CGLYA395−14.081116.170−59.1441.0050.85AATOM1988OGLYA395−13.344116.118−58.1561.0053.00AATOM1989NGLYA396−15.000117.113−59.3291.0050.83AATOM1990CAGLYA396−15.201118.162−58.3491.0050.44AATOM1991CGLYA396−16.000117.677−57.1531.0050.19AATOM1992OGLYA396−16.692116.656−57.2351.0050.51AATOM1993NPROA397−15.937118.405−56.0261.0049.00AATOM1994CDPROA397−15.287119.722−55.9090.0048.69AATOM1995CAPROA397−16.645118.071−54.7881.0048.22AATOM1996CBPROA397−16.269119.224−53.8601.0047.31AATOM1997CGPROA397−16.083120.366−54.8040.0048.31AATOM1998CPROA397−18.159117.906−54.9381.0047.36AATOM1999OPROA397−18.786117.199−54.1491.0047.61AATOM2000NSERA398−18.731118.545−55.9611.0045.23AATOM2001CASERA398−20.169118.495−56.2271.0042.61AATOM2002CBSERA398−20.608119.771−56.9191.0043.28AATOM2003OGSERA398−19.939119.905−58.1551.0044.50AATOM2004CSERA398−20.621117.311−57.0711.0041.14AATOM2005OSERA398−21.785117.227−57.4391.0039.80AATOM2006NASPA399−19.695116.410−57.3861.0039.71AATOM2007CAASPA399−19.991115.210−58.1661.0038.56AATOM2008CBASPA399−20.703114.168−57.2861.0038.01AATOM2009CGASPA399−20.402112.733−57.7111.0038.48AATOM2010OD1ASPA399−21.315112.038−58.1931.0038.28AATOM2011OD2ASPA399−19.244112.289−57.5601.0038.15AATOM2012CASPA399−20.799115.446−59.4461.0037.24AATOM2013OASPA399−20.451116.293−60.2491.0037.13AATOM2014NALAA400−21.878114.699−59.6291.0034.67AATOM2015CAALAA400−22.684114.804−60.8371.0035.08AATOM2016CBALAA400−23.905113.910−60.7091.0033.43AATOM2017CALAA400−23.106116.209−61.2871.0036.56AATOM2018OALAA400−23.312116.444−62.4801.0036.63AATOM2019NLYSA401−23.234117.142−60.3481.0035.88AATOM2020CALYSA401−23.645118.494−60.6981.0034.95AATOM2021CBLYSA401−23.628119.397−59.4721.0032.50AATOM2022CGLYSA401−24.708119.078−58.4841.0031.43AATOM2023CDLYSA401−24.507119.886−57.2461.0028.22AATOM2024CELYSA401−25.278119.318−56.0891.0027.81AATOM2025NZLYSA401−24.727119.867−54.8301.0025.14AATOM2026CLYSA401−22.791119.106−61.7851.0034.81AATOM2027OLYSA401−23.160120.125−62.3631.0036.29AATOM2028NGLUA402−21.650118.492−62.0631.0034.06AATOM2029CAGLUA402−20.768118.993−63.1041.0035.31AATOM2030CBGLUA402−19.320118.574−62.8441.0035.15AATOM2031CGGLUA402−18.942118.522−61.3901.0035.78AATOM2032CDGLUA402−17.607119.159−61.0971.0036.09AATOM2033OE1GLUA402−16.573118.719−61.6351.0035.51AATOM2034OE2GLUA402−17.594120.114−60.3021.0037.27AATOM2035CGLUA402−21.225118.403−64.4251.0036.16AATOM2036OGLUA402−21.097119.024−65.4721.0037.83AATOM2037NVALA403−21.775117.196−64.3511.0036.13AATOM2038CAVALA403−22.243116.465−65.5201.0035.96AATOM2039CBVALA403−22.195114.948−65.2401.0032.70AATOM2040CG1VALA403−22.532114.164−66.4681.0030.74AATOM2041CG2VALA403−20.826114.569−64.7681.0032.27AATOM2042CVALA403−23.652116.873−65.9321.0038.49AATOM2043OVALA403−23.971116.923−67.1221.0040.23AATOM2044NMETA404−24.482117.180−64.9381.0040.98AATOM2045CAMETA404−25.873117.589−65.1451.0040.56AATOM2046CBMETA404−26.629117.556−63.8251.0038.94AATOM2047CGMETA404−26.923116.169−63.3401.0038.99AATOM2048SDMETA404−27.808116.211−61.8231.0036.34AATOM2049CEMETA404−26.589116.901−60.8051.0037.24AATOM2050CMETA404−26.001118.974−65.7201.0041.72AATOM2051OMETA404−26.781119.205−66.6351.0042.27AATOM2052NGLUA405−25.240119.900−65.1601.0043.19AATOM2053CAGLUA405−25.278121.277−65.6081.0045.78AATOM2054CBGLUA405−25.012122.207−64.4251.0046.91AATOM2055CGGLUA405−26.226122.431−63.5501.0048.97AATOM2056CDGLUA405−25.867122.541−62.0861.0048.81AATOM2057OE1GLUA405−24.936123.307−61.7641.0047.03AATOM2058OE2GLUA405−26.521121.858−61.2611.0050.16AATOM2059CGLUA405−24.292121.563−66.7261.0046.65AATOM2060OGLUA405−24.001122.724−67.0191.0047.70AATOM2061NHISA406−23.779120.510−67.3531.0046.55AATOM2062CAHISA406−22.834120.687−68.4481.0046.72AATOM2063CBHISA406−22.058119.398−68.7371.0044.99AATOM2064CGHISA406−21.113119.517−69.8951.0042.90AATOM2065CD2HISA406−19.763119.607−69.9401.0041.46AATOM2066ND1HISA406−21.543119.590−71.2031.0041.37AATOM2067CE1HISA406−20.500119.720−72.0021.0041.87AATOM2068NE2HISA406−19.408119.733−71.2611.0042.52AATOM2069CHISA406−23.583121.111−69.6951.0046.62AATOM2070OHISA406−24.686120.636−69.9491.0046.24AATOM2071NARGA407−22.967122.006−70.4631.0047.11AATOM2072CAARGA407−23.545122.528−71.6971.0047.66AATOM2073CBARGA407−22.448123.141−72.5801.0049.51AATOM2074CGARGA407−21.572124.152−71.8751.0052.53AATOM2075CDARGA407−22.414125.173−71.1291.0053.78AATOM2076NEARGA407−21.612126.235−70.5271.0055.27AATOM2077CZARGA407−20.951127.167−71.2171.0055.91AATOM2078NH1ARGA407−20.980127.175−72.5511.0055.67AATOM2079NH2ARGA407−20.283128.118−70.5681.0056.67AATOM2080CARGA407−24.275121.459−72.4921.0045.82AATOM2081OARGA407−25.354121.696−73.0321.0044.38AATOM2082NPHEA408−23.673120.281−72.5691.0044.29AATOM2083CAPHEA408−24.280119.203−73.3151.0042.94AATOM2084CBPHEA408−23.402117.949−73.2881.0041.05AATOM2085CGPHEA408−23.975116.812−74.0781.0039.45AATOM2086CD1PHEA408−23.995116.858−75.4611.0037.39AATOM2087CD2PHEA408−24.567115.725−73.4321.0038.00AATOM2088CE1PHEA408−24.600115.842−76.1891.0036.63AATOM2089CE2PHEA408−25.174114.705−74.1531.0036.63AATOM2090CZPHEA408−25.191114.763−75.5361.0035.56AATOM2091CPHEA408−25.636118.899−72.7231.0042.17AATOM2092OPHEA408−26.639118.901−73.4181.0043.14AATOM2093NPHEA409−25.665118.647−71.4281.0041.88AATOM2094CAPHEA409−26.913118.345−70.7611.0041.98AATOM2095CBPHEA409−26.622117.576−69.4811.0039.76AATOM2096CGPHEA409−26.320116.133−69.7141.0037.85AATOM2097CD1PHEA409−27.350115.243−70.0331.0036.86AATOM2098CD2PHEA409−25.015115.664−69.6441.0035.28AATOM2099CE1PHEA409−27.090113.911−70.2791.0035.98AATOM2100CE2PHEA409−24.735114.334−69.8881.0035.27AATOM2101CZPHEA409−25.776113.448−70.2081.0035.85AATOM2102CPHEA409−27.770119.579−70.4751.0042.86AATOM2103OPHEA409−28.807119.478−69.8371.0043.83AATOM2104NLEUA410−27.330120.733−70.9621.0043.73AATOM2105CALEUA410−28.047121.994−70.8011.0044.49AATOM2106CBLEUA410−27.252123.123−71.4961.0045.19AATOM2107CGLEUA410−26.668124.403−70.8451.0045.14AATOM2108CD1LEUA410−27.740125.483−70.7221.0043.41AATOM2109CD2LEUA410−26.024124.074−69.4991.0043.54AATOM2110CLEUA410−29.440121.853−71.4501.0044.57AATOM2111OLEUA410−30.097122.847−71.7561.0045.04AATOM2112NSERA411−29.878120.613−71.6511.0042.73AATOM2113CASERA411−31.168120.315−72.2691.0041.24AATOM2114CBSERA411−30.933119.605−73.6101.0041.27AATOM2115OGSERA411−31.886118.564−73.8361.0036.52AATOM2116CSERA411−32.125119.458−71.4321.0041.48AATOM2117OSERA411−33.326119.435−71.6971.0041.51AATOM2118NILEA412−31.610118.747−70.4311.0039.95AATOM2119CAILEA412−32.470117.874−69.6361.0037.71AATOM2120CBILEA412−31.795116.483−69.4121.0037.46AATOM2121CG2ILEA412−32.770115.531−68.7251.0036.37AATOM2122CG1ILEA412−31.325115.893−70.7511.0035.25AATOM2123CD1ILEA412−32.228114.820−71.3581.0031.16AATOM2124CILEA412−32.929118.405−68.2771.0036.84AATOM2125OILEA412−32.188119.093−67.5621.0034.95AATOM2126NASNA413−34.176118.068−67.9531.0037.15AATOM2127CAASNA413−34.822118.417−66.6951.0038.79AATOM2128CBASNA413−36.339118.546−66.8951.0039.70AATOM2129CGASNA413−37.090118.765−65.5891.0041.29AATOM2130OD1ASNA413−36.704119.602−64.7721.0045.08AATOM2131ND2ASNA413−38.168118.021−65.3901.0034.66AATOM2132CASNA413−34.506117.218−65.8171.0039.23AATOM2133OASNA413−35.165116.185−65.8981.0038.70AATOM2134NTRPA414−33.482117.365−64.9861.0040.55AATOM2135CATRPA414−33.016116.295−64.1161.0041.65AATOM2136CBTRPA414−31.706116.715−63.4541.0043.22AATOM2137CGTRPA414−30.563116.487−64.3841.0048.09AATOM2138CD2TRPA414−30.184115.233−64.9731.0049.22AATOM2139CE2TRPA414−29.105115.492−65.8451.0049.82AATOM2140CE3TRPA414−30.658113.916−64.8501.0048.90AATOM2141CD1TRPA414−29.722117.424−64.9041.0049.09AATOM2142NE1TRPA414−28.843116.833−65.7861.0050.48AATOM2143CZ2TRPA414−28.489114.482−66.5931.0050.23AATOM2144CZ3TRPA414−30.051112.913−65.6931.0048.84AATOM2145CH2TRPA414−28.975113.203−66.4551.0050.52AATOM2146CTRPA414−33.972115.759−63.0831.0041.45AATOM2147OTRPA414−33.559115.107−62.1291.0042.26AATOM2148NGLNA415−35.256115.996−63.2961.0040.99AATOM2149CAGLNA415−36.266115.538−62.3671.0040.33AATOM2150CBGLNA415−36.904116.746−61.6721.0038.84AATOM2151CGGLNA415−38.182116.447−60.9001.0035.87AATOM2152CDGLNA415−38.694117.651−60.1361.0033.90AATOM2153OE1GLNA415−39.843117.687−59.7261.0031.97AATOM2154NE2GLNA415−37.832118.636−59.9301.0031.91AATOM2155CGLNA415−37.309114.707−63.0871.0040.59AATOM2156OGLNA415−38.042113.967−62.4591.0040.18AATOM2157NASPA416−37.382114.840−64.4081.0041.53AATOM2158CAASPA416−38.335114.064−65.1971.0043.23AATOM2159CBASPA416−38.539114.661−66.5951.0044.45AATOM2160CGASPA416−39.248116.003−66.5681.0044.39AATOM2161OD1ASPA416−40.321116.080−65.9391.0045.82AATOM2162OD2ASPA416−38.737116.970−67.1721.0041.69AATOM2163CASPA416−37.679112.720−65.3451.0043.96AATOM2164OASPA416−38.322111.682−65.2511.0044.10AATOM2165NVALA417−36.374112.775−65.5791.0045.55AATOM2166CAVALA417−35.536111.599−65.7511.0045.69AATOM2167CBVALA417−34.050111.954−65.5831.0045.81AATOM2168CG1VALA417−33.196110.740−65.8821.0045.88AATOM2169CG2VALA417−33.678113.116−66.4911.0046.39AATOM2170CVALA417−35.881110.565−64.7071.0045.58AATOM2171OVALA417−36.372109.480−65.0181.0046.46AATOM2172NVALA418−35.626110.926−63.4581.0044.65AATOM2173CAVALA418−35.876110.055−62.3281.0045.15AATOM2174CBVALA418−35.600110.812−61.0181.0045.58AATOM2175CG1VALA418−35.572109.864−59.8631.0044.96AATOM2176CG2VALA418−34.263111.530−61.1181.0046.99AATOM2177CVALA418−37.289109.485−62.3211.0045.12AATOM2178OVALA418−37.522108.419−61.7621.0044.65AATOM2179NGLNA419−38.226110.182−62.9561.0046.35AATOM2180CAGLNA419−39.617109.728−63.0111.0047.06AATOM2181CBGLNA419−40.553110.925−62.8351.0048.45AATOM2182CGGLNA419−42.015110.669−63.2161.0052.74AATOM2183CDGLNA419−42.708109.632−62.3551.0054.02AATOM2184OE1GLNA419−42.256108.489−62.2481.0054.06AATOM2185NE2GLNA419−43.823110.024−61.7431.0053.61AATOM2186CGLNA419−39.981108.959−64.2891.0046.21AATOM2187OGLNA419−41.106108.470−64.4341.0044.30AATOM2188NLYSA420−39.018108.818−65.1961.0046.01AATOM2189CALYSA420−39.259108.128−66.4571.0044.73AATOM2190CBLYSA420−39.751106.700−66.2051.0043.74AATOM2191CGLYSA420−38.701105.746−65.6641.0040.89AATOM2192CDLYSA420−39.279104.355−65.4071.0037.22AATOM2193CELYSA420−38.152103.355−65.1731.0040.17AATOM2194NZLYSA420−38.566101.984−64.7591.0036.48AATOM2195CLYSA420−40.316108.916−67.2261.0044.79AATOM2196OLYSA420−41.038108.364−68.0581.0043.94AATOM2197NLYSA421−40.400110.211−66.9151.0045.23AATOM2198CALYSA421−41.337111.137−67.5491.0046.15AATOM2199CBLYSA421−41.333112.495−66.8361.0044.83AATOM2200CGLYSA421−42.157112.575−65.5691.0044.08AATOM2201CDLYSA421−42.246114.006−65.0451.0042.19AATOM2202CELYSA421−42.888114.928−66.0751.0043.13AATOM2203NZLYSA421−43.266116.261−65.5351.0039.02AATOM2204CLYSA421−40.898111.359−68.9831.0047.72AATOM2205OLYSA421−41.692111.727−69.8471.0047.61AATOM2206NLEUA422−39.609111.154−69.2141.0048.81AATOM2207CALEUA422−39.038111.327−70.5291.0050.06AATOM2208CBLEUA422−37.517111.262−70.4331.0050.15AATOM2209CGLEUA422−36.915112.248−69.4321.0050.34AATOM2210CD1LEUA422−35.404112.051−69.3361.0051.35AATOM2211CD2LEUA422−37.240113.660−69.8641.0049.35AATOM2212CLEUA422−39.565110.230−71.4411.0050.97AATOM2213OLEUA422−39.895109.139−70.9871.0050.98AATOM2214NLEUA423−39.661110.528−72.7291.0052.60AATOM2215CALEUA423−40.145109.553−73.6861.0054.55AATOM2216CBLEUA423−41.081110.226−74.6971.0053.81AATOM2217CGLEUA423−41.938111.411−74.2100.0052.10AATOM2218CD1LEUA423−42.644112.026−75.4161.0051.16AATOM2219CD2LEUA423−42.955110.983−73.1361.0050.78AATOM2220CLEUA423−38.912108.987−74.3931.0056.58AATOM2221OLEUA423−38.191109.712−75.0821.0056.59AATOM2222NPROA424−38.650107.682−74.2121.0056.63AATOM2223CDPROA424−39.513106.735−73.4851.0056.01AATOM2224CAPROA424−37.513106.983−74.8121.0058.90AATOM2225CBPROA424−37.642105.576−74.2391.0058.09AATOM2226CGPROA424−39.110105.411−74.0701.0056.04AATOM2227CPROA424−37.530106.997−76.3411.0059.64AATOM2228OPROA424−38.451106.479−76.9721.0058.94AATOM2229NPROA425−36.498107.588−76.9561.0059.31AATOM2230CDPROA425−35.304108.166−76.3161.0060.68AATOM2231CAPROA425−36.397107.671−78.4131.0059.90AATOM2232CBPROA425−35.212108.602−78.6171.0059.98AATOM2233CGPROA425−34.329108.239−77.4701.0061.61AATOM2234CPROA425−36.187106.312−79.0611.0059.43AATOM2235OPROA425−35.296106.137−79.8861.0060.86AATOM2236NPHEA426−37.018105.356−78.6791.0056.79AATOM2237CAPHEA426−36.948104.012−79.2091.0056.12AATOM2238CBPHEA426−35.493103.551−79.3431.0055.18AATOM2239CGPHEA426−35.347102.114−79.7521.0055.15AATOM2240CD1PHEA426−35.822101.672−80.9761.0055.09AATOM2241CD2PHEA426−34.763101.190−78.8901.0056.47AATOM2242CE1PHEA426−35.724100.337−81.3311.0056.49AATOM2243CE2PHEA426−34.66099.841−79.2391.0056.52AATOM2244CZPHEA426−35.14199.417−80.4591.0057.05AATOM2245CPHEA426−37.683103.121−78.2331.0057.34AATOM2246OPHEA426−37.504103.240−77.0221.0057.59AATOM2247NLYSA427−38.524102.240−78.7561.0057.52AATOM2248CALYSA427−39.274101.335−77.9111.0058.08AATOM2249CBLYSA427−40.709101.840−77.7241.0058.05AATOM2250CGLYSA427−40.887102.717−76.4881.0058.16AATOM2251CDLYSA427−41.882103.837−76.7181.0059.46AATOM2252CELYSA427−41.451104.719−77.8931.0058.92AATOM2253NZLYSA427−42.563105.617−78.3051.0059.73AATOM2254CLYSA427−39.27899.922−78.4521.0058.72AATOM2255OLYSA427−39.85299.644−79.4981.0058.34AATOM2256NPROA428−38.61099.009−77.7401.0060.79AATOM2257CDPROA428−37.75399.258−76.5651.0060.29AATOM2258CAPROA428−38.53997.609−78.1501.0062.03AATOM2259CBPROA428−37.86296.956−76.9591.0062.09AATOM2260CGPROA428−36.89098.029−76.5331.0060.55AATOM2261CPROA428−39.93697.071−78.4271.0063.87AATOM2262OPROA428−40.86197.313−77.6611.0064.43AATOM2263NGLNA429−40.07496.347−79.5311.0065.72AATOM2264CAGLNA429−41.35495.791−79.9641.0068.28AATOM2265CBGLNA429−41.25195.441−81.4521.0069.22AATOM2266CGGLNA429−40.83596.635−82.3040.0071.03AATOM2267CDGLNA429−40.63696.292−83.7670.0071.23AATOM2268OE1GLNA429−41.59095.928−84.4711.0071.28AATOM2269NE2GLNA429−39.38996.410−84.2371.0070.79AATOM2270CGLNA429−41.88694.597−79.1571.0067.62AATOM2271OGLNA429−41.12693.865−78.5281.0066.77AATOM2272NVALA430−43.20594.414−79.1890.0068.55AATOM2273CAVALA430−43.86693.336−78.4510.0069.19AATOM2274CBVALA430−44.68493.921−77.2620.0068.71AATOM2275CG1VALA430−45.49392.823−76.5761.0067.68AATOM2276CG2VALA430−43.74694.605−76.2651.0068.75AATOM2277CVALA430−44.80792.498−79.3270.0068.52AATOM2278OVALA430−45.68993.040−79.9930.0068.45AATOM2279NTHRA431−44.61591.179−79.3230.0069.17AATOM2280CATHRA431−45.46490.275−80.1010.0070.45AATOM2281CBTHRA431−44.66189.502−81.1940.0070.12AATOM2282OG1THRA431−45.51189.259−82.3291.0068.50AATOM2283CG2THRA431−44.14088.141−80.6461.0069.39AATOM2284CTHRA431−46.10189.259−79.1570.0071.64AATOM2285OTHRA431−47.09488.614−79.4970.0070.36AATOM2286NSERA432−45.51889.129−77.9680.0072.76AATOM2287CASERA432−46.00088.189−76.9590.0073.70AATOM2288CBSERA432−45.95386.760−77.5031.0075.55AATOM2289OGSERA432−46.05485.810−76.4481.0076.12AATOM2290CSERA432−45.16088.243−75.6910.0072.92AATOM2291OSERA432−43.93888.381−75.7580.0073.90AATOM2292NGLUA433−45.81088.134−74.5350.0073.20AATOM2293CAGLUA433−45.07588.129−73.2760.0073.44AATOM2294CBGLUA433−46.00587.883−72.0850.0073.69AATOM2295CGGLUA433−46.76889.101−71.5880.0071.40AATOM2296CDGLUA433−48.20189.140−72.0780.0069.94AATOM2297OE1GLUA433−49.09689.443−71.2591.0067.25AATOM2298OE2GLUA433−48.43688.878−73.2761.0068.23AATOM2299CGLUA433−44.10586.966−73.3960.0074.79AATOM2300OGLUA433−44.31186.078−74.2250.0074.19AATOM2301NVALA434−43.05586.959−72.5830.0074.23AATOM2302CAVALA434−42.08885.872−72.6541.0075.04AATOM2303CBVALA434−42.80684.505−72.4781.0074.65AATOM2304CG1VALA434−41.82483.354−72.6901.0074.90AATOM2305CG2VALA434−43.45184.434−71.0961.0073.65AATOM2306CVALA434−41.43285.946−74.0381.0074.75AATOM2307OVALA434−41.94185.382−75.0111.0076.78AATOM2308NASPA435−40.31086.655−74.1190.0073.96AATOM2309CAASPA435−39.59086.828−75.3781.0072.40AATOM2310CBASPA435−40.48587.560−76.3871.0072.75AATOM2311CGASPA435−39.73987.981−77.6471.0071.98AATOM2312OD1ASPA435−40.39488.478−78.5891.0071.33AATOM2313OD2ASPA435−38.50487.821−77.7001.0071.98AATOM2314CASPA435−38.32687.640−75.1311.0072.65AATOM2315OASPA435−38.38988.715−74.5321.0073.50AATOM2316NTHRA436−37.18387.134−75.5961.0071.32AATOM2317CATHRA436−35.90387.827−75.4121.0070.22AATOM2318CBTHRA436−34.97087.038−74.4521.0068.79AATOM2319OG1THRA436−34.42385.906−75.1391.0067.56AATOM2320CG2THRA436−35.74586.552−73.2261.0066.02AATOM2321CTHRA436−35.20487.980−76.7631.0069.55AATOM2322OTHRA436−33.97888.034−76.8411.0069.24AATOM2323NARGA437−36.02588.061−77.8081.0069.77AATOM2324CAARGA437−35.63188.177−79.2181.0068.79AATOM2325CBARGA437−36.91188.401−80.0461.0068.01AATOM2326CGARGA437−36.82888.059−81.5341.0066.69AATOM2327CDARGA437−38.21887.811−82.1271.0065.27AATOM2328NEARGA437−38.84386.610−81.5411.0063.62AATOM2329CZARGA437−39.92585.995−82.0291.0059.93AATOM2330NH1ARGA437−40.53486.456−83.1221.0058.41AATOM2331NH2ARGA437−40.37384.904−81.4361.0056.18AATOM2332CARGA437−34.56289.216−79.6011.0067.75AATOM2333OARGA437−34.00389.142−80.6961.0066.59AATOM2334NTYRA438−34.27690.171−78.7141.0068.22AATOM2335CATYRA438−33.27091.218−78.9841.0067.16AATOM2336CBTYRA438−33.61492.517−78.2361.0065.63AATOM2337CGTYRA438−34.99493.048−78.5171.0064.03AATOM2338CD1TYRA438−35.95493.098−77.5131.0063.19AATOM2339CE1TYRA438−37.24693.527−77.7721.0063.50AATOM2340CD2TYRA438−35.35793.453−79.8031.0064.73AATOM2341CE2TYRA438−36.65293.892−80.0831.0064.79AATOM2342CZTYRA438−37.59393.926−79.0591.0064.10AATOM2343OHTYRA438−38.87194.372−79.3231.0064.05AATOM2344CTYRA438−31.86590.793−78.5721.0067.56AATOM2345OTYRA438−30.91791.567−78.6641.0066.70AATOM2346NPHEA439−31.73989.556−78.1191.0068.41AATOM2347CAPHEA439−30.46489.033−77.6631.0069.60AATOM2348CBPHEA439−30.71288.179−76.4141.0068.48AATOM2349CGPHEA439−31.33188.957−75.2591.0067.67AATOM2350CD1PHEA439−32.21190.016−75.4951.0066.74AATOM2351CD2PHEA439−31.04388.621−73.9391.0066.90AATOM2352CE1PHEA439−32.79290.724−74.4401.0066.23AATOM2353CE2PHEA439−31.61989.321−72.8791.0065.64AATOM2354CZPHEA439−32.49590.376−73.1331.0065.83AATOM2355CPHEA439−29.71588.264−78.7621.0070.52AATOM2356OPHEA439−29.23488.880−79.7201.0070.33AATOM2357NASPA440−29.61486.940−78.6531.0071.72AATOM2358CAASPA440−28.88986.189−79.6871.0073.06AATOM2359CBASPA440−27.40486.606−79.6401.0071.34AATOM2360CGASPA440−26.66186.333−80.9351.0068.74AATOM2361OD1ASPA440−25.52786.844−81.0761.0066.33AATOM2362OD2ASPA440−27.20085.614−81.8001.0067.42AATOM2363CASPA440−29.02884.651−79.5991.0074.04AATOM2364OASPA440−29.45584.098−78.5721.0073.71AATOM2365NASPA441−28.66883.981−80.6971.0074.91AATOM2366CAASPA441−28.72682.522−80.7981.0075.49AATOM2367CBASPA441−28.89682.091−82.2571.0075.66AATOM2368CGASPA441−30.10782.719−82.9221.0076.58AATOM2369OD1ASPA441−30.38482.355−84.0901.0076.57AATOM2370OD2ASPA441−30.77383.572−82.2861.0075.89AATOM2371CASPA441−27.44481.891−80.2661.0075.57AATOM2372OASPA441−26.48481.715−81.0141.0075.00AATOM2373NALAA442−27.43081.546−78.9831.0075.85AATOM2374CAALAA442−26.25580.927−78.3651.0076.13AATOM2375CBALAA442−25.29882.008−77.8561.0074.63AATOM2376CALAA442−26.64379.975−77.2241.0076.57AATOM2377OALAA442−27.66679.270−77.3771.0076.87AATOM2378OXTALAA442−25.92079.929−76.2031.0075.20A

[0490]

14

TABLE 3

Coordinate data for pΔPH-PKBβ-ΔC (second batch)

REMARK coordinates from minimization refinement

REMARK refinement resolution: 500.0-2.3 A

REMARK starting r = 0.2431 free_r = 0.3043

REMARK final r = 0.2374 free_r = 0.3087

REMARK rmsd bonds = 0.010503 rmsd angles = 1.53593

REMARK wa = 4.5

REMARK target = mlf cycles = 1 steps = 80

REMARK sg = P4 (1) 2 (1) 2 a = 148.405 b = 148.405 c = 38.547 alpha = 90 beta = 90

gamma = 90

REMARK parameter file 1: CNS_TOPPAR: protein_rep.param

REMARK parameter file 2: CNS_TOPPAR: water_rep.param

REMARK molecular structure file: water_pick.mtf

REMARK input coordinates: water_pick.pdb

REMARK reflection file = pkb-33-all-new.fob

REMARK ncs = none

REMARK B-correction resolution: 6.0-2.3

REMARK initial B-factor correction applied to fobs:

REMARK B11 = −8.472 B22 = −8.472 B33 = 16.944

REMARK B12 = 0.000 B13 = 0.000 B23 = 0.000

REMARK B-factor correction applied to coordinate array B: −1.018

REMARK bulk solvent: density level = 0.335739 e/A{circumflex over ( )}3, B-factor = 54.1491 A{circumflex over ( )}2

REMARK reflections with |Fobs|/sigma_F < 0.0 rejected

REMARK reflections with |Fobs| > 10000 * rms (Fobs) rejected

REMARK theoretical total number of refl. in resol. range: 19801 (100.0%)

REMARK number of unobserved reflections (no entry or |F| =0): 827 (4.2%)

REMARK number of reflections rejected: 0 (0.0%)

REMARK total number of reflections used: 18974 (95.8%)

REMARK number of reflections in working set: 17576 (88.8%)

REMARK number of reflections in test set: 1398 (7.1%)

CRYST1 148.405 148.405 38.547 90.00 90.00 90.00 P 41 21 2

REMARK FILENAME = “minimize.pdb”

REMARK DATE: 23-Nov-01 19:15:46

REMARK VERSION: 1.1

ATOM
1
CB
ALA

146
−37.642
81.084
−46.450
1.00
75.24

ATOM
2
C
ALA

146
−38.383
81.091
−48.848
1.00
74.66

ATOM
3
O
ALA

146
−39.041
80.113
−49.229
1.00
76.10

ATOM
4
N
ALA

146
−40.033
81.409
−47.060
1.00
74.47

ATOM
5
CA
ALA

146
−38.626
81.691
−47.470
1.00
74.54

ATOM
6
N
ALA

147
−37.448
81.673
−49.600
1.00
72.95

ATOM
7
CA
ALA

147
−37.135
81.164
−50.931
1.00
69.87

ATOM
8
CB
ALA

147
−36.605
82.281
−51.822
1.00
69.59

ATOM
9
C
ALA

147
−36.107
80.051
−50.824
1.00
67.47

ATOM
10
O
ALA

147
−35.286
80.029
−49.909
1.00
66.70

ATOM
11
N
THR

148
−36.166
79.129
−51.773
1.00
65.70

ATOM
12
CA
THR

148
−35.249
77.999
−51.824
1.00
63.28

ATOM
13
CB
THR

148
−35.790
76.808
−51.001
1.00
63.55

ATOM
14
OG1
THR

148
−35.170
76.818
−49.709
1.00
64.84

ATOM
15
CG2
THR

148
−35.527
75.477
−51.687
1.00
62.78

ATOM
16
C
THR

148
−35.048
77.579
−53.268
1.00
62.60

ATOM
17
O
THR

148
−35.898
77.841
−54.128
1.00
61.96

ATOM
18
N
MET

149
−33.921
76.927
−53.527
1.00
60.64

ATOM
19
CA
MET

149
−33.597
76.474
−54.865
1.00
59.94

ATOM
20
CB
MET

149
−32.461
75.462
−54.816
1.00
59.38

ATOM
21
CG
MET

149
−31.139
76.109
−54.570
1.00
59.25

ATOM
22
SD
MET

149
−30.742
77.184
−55.938
1.00
56.44

ATOM
23
CE
MET

149
−28.996
76.720
−56.112
1.00
58.07

ATOM
24
C
MET

149
−34.762
75.864
−55.594
1.00
60.31

ATOM
25
O
MET

149
−34.903
76.031
−56.805
1.00
61.48

ATOM
26
N
ASN

150
−35.606
75.156
−54.857
1.00
62.05

ATOM
27
CA
ASN

150
−36.745
74.498
−55.470
1.00
62.17

ATOM
28
CB
ASN

150
−37.275
73.404
−54.549
1.00
64.49

ATOM
29
CG
ASN

150
−38.268
72.507
−55.245
1.00
66.43

ATOM
30
OD1
ASN

150
−39.189
71.991
−54.619
1.00
69.01

ATOM
31
ND2
ASN

150
−38.091
72.317
−56.554
1.00
66.61

ATOM
32
C
ASN

150
−37.868
75.444
−55.873
1.00
60.81

ATOM
33
O
ASN

150
−38.844
75.028
−56.478
1.00
61.24

ATOM
34
N
ASP

151
−37.731
76.718
−55.546
1.00
59.88

ATOM
35
CA
ASP

151
−38.738
77.700
−55.931
1.00
60.47

ATOM
36
CB
ASP

151
−38.676
78.926
−55.002
1.00
62.92

ATOM
37
CG
ASP

151
−39.337
78.690
−53.655
1.00
64.34

ATOM
38
OD1
ASP

151
−40.502
78.241
−53.661
1.00
67.09

ATOM
39
OD2
ASP

151
−38.711
78.969
−52.602
1.00
63.82

ATOM
40
C
ASP

151
−38.518
78.188
−57.374
1.00
60.17

ATOM
41
O
ASP

151
−39.284
79.009
−57.884
1.00
57.73

ATOM
42
N
PHE

152
−37.483
77.692
−58.047
1.00
60.29

ATOM
43
CA
PHE

152
−37.210
78.195
−59.388
1.00
59.56

ATOM
44
CB
PHE

152
−36.050
79.196
−59.305
1.00
56.60

ATOM
45
CG
PHE

152
−36.232
80.251
−58.245
1.00
53.19

ATOM
46
CD1
PHE

152
−37.003
81.385
−58.494
1.00
52.09

ATOM
47
CD2
PHE

152
−35.653
80.097
−56.984
1.00
50.65

ATOM
48
CE1
PHE

152
−37.199
82.363
−57.495
1.00
48.55

ATOM
49
CE2
PHE

152
−35.841
81.061
−55.983
1.00
50.10

ATOM
50
CZ
PHE

152
−36.620
82.201
−56.244
1.00
47.82

ATOM
51
C
PHE

152
−36.923
77.183
−60.493
1.00
60.88

ATOM
52
O
PHE

152
−36.413
76.086
−60.246
1.00
62.22

ATOM
53
N
ASP

153
−37.268
77.572
−61.721
1.00
62.21

ATOM
54
CA
ASP

153
−37.032
76.753
−62.904
1.00
62.60

ATOM
55
CB
ASP

153
−38.188
76.860
−63.902
1.00
66.09

ATOM
56
CG
ASP

153
−39.500
76.340
−63.349
1.00
69.91

ATOM
57
OD1
ASP

153
−39.570
75.140
−62.990
1.00
71.36

ATOM
58
OD2
ASP

153
−40.468
77.135
−63.284
1.00
72.40

ATOM
59
C
ASP

153
−35.798
77.320
−63.574
1.00
61.47

ATOM
60
O
ASP

153
−35.665
78.536
−63.706
1.00
60.46

ATOM
61
N
TYR

154
−34.897
76.447
−63.997
1.00
60.59

ATOM
62
CA
TYR

154
−33.692
76.894
−64.676
1.00
59.06

ATOM
63
CB
TYR

154
−32.619
75.826
−64.608
1.00
58.21

ATOM
64
CG
TYR

154
−31.473
76.086
−65.557
1.00
58.30

ATOM
65
CD1
TYR

154
−30.431
76.936
−65.209
1.00
57.17

ATOM
66
CE1
TYR

154
−29.362
77.135
−66.064
1.00
57.83

ATOM
67
CD2
TYR

154
−31.422
75.453
−66.794
1.00
57.54

ATOM
68
CE2
TYR

154
−30.367
75.640
−67.652
1.00
58.09

ATOM
69
CZ
TYR

154
−29.332
76.475
−67.287
1.00
59.85

ATOM
70
OH
TYR

154
−28.245
76.592
−68.129
1.00
61.95

ATOM
71
C
TYR

154
−33.948
77.204
−66.145
1.00
58.79

ATOM
72
O
TYR

154
−34.448
76.354
−66.878
1.00
60.40

ATOM
73
N
LEU

155
−33.588
78.410
−66.581
1.00
58.11

ATOM
74
CA
LEU

155
−33.763
78.784
−67.980
1.00
55.79

ATOM
75
CB
LEU

155
−34.390
80.163
−68.073
1.00
55.60

ATOM
76
CG
LEU

155
−35.886
79.883
−67.996
1.00
56.32

ATOM
77
CD1
LEU

155
−36.631
81.037
−67.446
1.00
54.90

ATOM
78
CD2
LEU

155
−36.381
79.522
−69.392
1.00
57.99

ATOM
79
C
LEU

155
−32.456
78.723
−68.736
1.00
53.65

ATOM
80
O
LEU

155
−32.336
77.986
−69.701
1.00
52.78

ATOM
81
N
LYS

156
−31.463
79.482
−68.301
1.00
53.65

ATOM
82
CA
LYS

156
−30.170
79.435
−68.972
1.00
54.02

ATOM
83
CB
LYS

156
−30.243
80.086
−70.357
1.00
55.68

ATOM
84
CG
LYS

156
−30.412
81.588
−70.335
1.00
58.53

ATOM
85
CD
LYS

156
−30.300
82.164
−71.738
1.00
60.28

ATOM
86
CE
LYS

156
−29.978
83.651
−71.688
1.00
60.98

ATOM
87
NZ
LYS

156
−29.678
84.179
−73.055
1.00
63.58

ATOM
88
C
LYS

156
−29.094
80.119
−68.164
1.00
53.71

ATOM
89
O
LYS

156
−29.366
80.790
−67.165
1.00
52.50

ATOM
90
N
LEU

157
−27.860
79.948
−68.605
1.00
54.56

ATOM
91
CA
LEU

157
−26.746
80.571
−67.921
1.00
56.09

ATOM
92
CB
LEU

157
−25.455
79.797
−68.185
1.00
56.31

ATOM
93
CG
LEU

157
−24.186
80.379
−67.559
1.00
55.75

ATOM
94
CD1
LEU

157
−24.387
80.695
−66.079
1.00
54.49

ATOM
95
CD2
LEU

157
−23.077
79.379
−67.753
1.00
58.24

ATOM
96
C
LEU

157
−26.574
82.002
−68.400
1.00
57.27

ATOM
97
O
LEU

157
−26.436
82.246
−69.592
1.00
57.09

ATOM
98
N
LEU

158
−26.588
82.949
−67.472
1.00
58.72

ATOM
99
CA
LEU

158
−26.406
84.339
−67.847
1.00
61.37

ATOM
100
CB
LEU

158
−27.269
85.246
−66.975
1.00
59.04

ATOM
101
CG
LEU

158
−28.732
85.225
−67.410
1.00
56.77

ATOM
102
CD1
LEU

158
−29.581
86.052
−66.461
1.00
57.48

ATOM
103
CD2
LEU

158
−28.829
85.772
−68.832
1.00
56.10

ATOM
104
C
LEU

158
−24.942
84.697
−67.713
1.00
63.74

ATOM
105
O
LEU

158
−24.428
85.520
−68.458
1.00
63.88

ATOM
106
N
GLY

159
−24.264
84.056
−66.772
1.00
67.31

ATOM
107
CA
GLY

159
−22.853
84.332
−66.589
1.00
71.22

ATOM
108
C
GLY

159
−22.125
83.436
−65.602
1.00
73.75

ATOM
109
O
GLY

159
−22.663
83.050
−64.564
1.00
73.51

ATOM
110
N
LYS

160
−20.891
83.092
−65.938
1.00
76.64

ATOM
111
CA
LYS

160
−20.070
82.274
−65.060
1.00
80.27

ATOM
112
CB
LYS

160
−19.468
81.096
−65.826
1.00
80.27

ATOM
113
CG
LYS

160
−18.685
80.125
−64.949
1.00
82.00

ATOM
114
CD
LYS

160
−18.167
78.934
−65.758
1.00
83.36

ATOM
115
CE
LYS

160
−17.410
77.928
−64.888
1.00
82.96

ATOM
116
NZ
LYS

160
−16.799
76.854
−65.724
1.00
81.28

ATOM
117
C
LYS

160
−18.968
83.214
−64.580
1.00
82.51

ATOM
118
O
LYS

160
−18.846
84.334
−65.081
1.00
83.54

ATOM
119
N
GLY

161
−18.168
82.782
−63.616
1.00
84.63

ATOM
120
CA
GLY

161
−17.112
83.655
−63.135
1.00
86.72

ATOM
121
C
GLY

161
−16.292
83.081
−61.999
1.00
87.97

ATOM
122
O
GLY

161
−16.583
81.992
−61.489
1.00
88.29

ATOM
123
N
THR

162
−15.262
83.824
−61.604
1.00
88.34

ATOM
124
CA
THR

162
−14.376
83.406
−60.525
1.00
88.46

ATOM
125
CB
THR

162
−13.221
84.393
−60.385
1.00
89.84

ATOM
126
OG1
THR

162
−12.916
84.938
−61.678
1.00
90.96

ATOM
127
CG2
THR

162
−11.985
83.690
−59.827
1.00
90.13

ATOM
128
C
THR

162
−15.170
83.376
−59.224
1.00
87.43

ATOM
129
O
THR

162
−15.015
82.476
−58.397
1.00
87.84

ATOM
130
N
PHE

163
−16.025
84.381
−59.074
1.00
85.83

ATOM
131
CA
PHE

163
−16.904
84.562
−57.923
1.00
84.10

ATOM
132
CB
PHE

163
−17.533
85.938
−58.047
1.00
84.86

ATOM
133
CG
PHE

163
−18.142
86.187
−59.403
1.00
85.76

ATOM
134
CD1
PHE

163
−19.508
85.984
−59.622
1.00
85.73

ATOM
135
CD2
PHE

163
−17.342
86.594
−60.475
1.00
86.08

ATOM
136
CE1
PHE

163
−20.074
86.184
−60.888
1.00
86.00

ATOM
137
CE2
PHE

163
−17.894
86.796
−61.745
1.00
86.68

ATOM
138
CZ
PHE

163
−19.265
86.591
−61.951
1.00
86.71

ATOM
139
C
PHE

163
−18.017
83.494
−57.849
1.00
82.58

ATOM
140
O
PHE

163
−18.457
83.100
−56.764
1.00
82.36

ATOM
141
N
GLY

164
−18.471
83.037
−59.012
1.00
79.86

ATOM
142
CA
GLY

164
−19.530
82.049
−59.056
1.00
76.17

ATOM
143
C
GLY

164
−20.227
82.093
−60.402
1.00
73.69

ATOM
144
O
GLY

164
−19.574
82.109
−61.448
1.00
74.26

ATOM
145
N
LYS

165
−21.553
82.133
−60.389
1.00
69.87

ATOM
146
CA
LYS

165
−22.312
82.154
−61.632
1.00
65.10

ATOM
147
CB
LYS

165
−22.612
80.709
−62.064
1.00
66.05

ATOM
148
CG
LYS

165
−23.469
79.912
−61.074
1.00
66.47

ATOM
149
CD
LYS

165
−23.502
78.419
−61.418
1.00
68.61

ATOM
150
CE
LYS

165
−22.228
77.699
−60.963
1.00
69.56

ATOM
151
NZ
LYS

165
−22.080
76.323
−61.531
1.00
69.28

ATOM
152
C
LYS

165
−23.619
82.933
−61.498
1.00
62.02

ATOM
153
O
LYS

165
−24.043
83.269
−60.388
1.00
59.79

ATOM
154
N
VAL

166
−24.248
83.224
−62.636
1.00
58.85

ATOM
155
CA
VAL

166
−25.520
83.936
−62.661
1.00
56.27

ATOM
156
CB
VAL

166
−25.372
85.413
−63.112
1.00
55.61

ATOM
157
CG1
VAL

166
−26.754
86.063
−63.228
1.00
53.77

ATOM
158
CG2
VAL

166
−24.515
86.197
−62.095
1.00
54.35

ATOM
159
C
VAL

166
−26.407
83.192
−63.637
1.00
56.59

ATOM
160
O
VAL

166
−26.075
83.022
−64.815
1.00
54.74

ATOM
161
N
ILE

167
−27.540
82.743
−63.120
1.00
55.92

ATOM
162
CA
ILE

167
−28.480
81.965
−63.898
1.00
55.67

ATOM
163
CB
ILE

167
−28.842
80.645
−63.158
1.00
55.84

ATOM
164
CG2
ILE

167
−29.868
79.876
−63.947
1.00
57.49

ATOM
165
CG1
ILE

167
−27.588
79.795
−62.911
1.00
57.15

ATOM
166
CD1
ILE

167
−26.852
79.362
−64.166
1.00
55.95

ATOM
167
C
ILE

167
−29.760
82.732
−64.108
1.00
54.34

ATOM
168
O
ILE

167
−30.172
83.522
−63.263
1.00
54.22

ATOM
169
N
LEU

168
−30.388
82.487
−65.244
1.00
53.57

ATOM
170
CA
LEU

168
−31.652
83.110
−65.553
1.00
54.21

ATOM
171
CB
LEU

168
−31.786
83.307
−67.068
1.00
53.94

ATOM
172
CG
LEU

168
−33.073
83.985
−67.557
1.00
54.53

ATOM
173
CD1
LEU

168
−33.264
85.300
−66.829
1.00
52.96

ATOM
174
CD2
LEU

168
−33.015
84.203
−69.064
1.00
53.85

ATOM
175
C
LEU

168
−32.682
82.106
−65.058
1.00
54.62

ATOM
176
O
LEU

168
−32.767
80.996
−65.579
1.00
55.68

ATOM
177
N
VAL

169
−33.458
82.479
−64.048
1.00
55.53

ATOM
178
CA
VAL

169
−34.471
81.562
−63.510
1.00
56.35

ATOM
179
CB
VAL

169
−34.188
81.185
−62.028
1.00
55.31

ATOM
180
CG1
VAL

169
−32.849
80.448
−61.907
1.00
52.24

ATOM
181
CG2
VAL

169
−34.199
82.439
−61.167
1.00
50.35

ATOM
182
C
VAL

169
−35.885
82.114
−63.537
1.00
58.43

ATOM
183
O
VAL

169
−36.111
83.292
−63.802
1.00
57.56

ATOM
184
N
ARG

170
−36.842
81.248
−63.243
1.00
61.25

ATOM
185
CA
ARG

170
−38.222
81.675
−63.186
1.00
63.27

ATOM
186
CB
ARG

170
−39.033
81.161
−64.371
1.00
65.66

ATOM
187
CG
ARG

170
−40.430
81.795
−64.434
1.00
68.73

ATOM
188
CD
ARG

170
−41.401
80.882
−65.136
1.00
71.75

ATOM
189
NE
ARG

170
−40.715
80.173
−66.203
1.00
74.18

ATOM
190
CZ
ARG

170
−40.838
78.870
−66.411
1.00
76.99

ATOM
191
NH1
ARG

170
−41.629
78.148
−65.620
1.00
78.12

ATOM
192
NH2
ARG

170
−40.158
78.287
−67.393
1.00
77.33

ATOM
193
C
ARG

170
−38.839
81.145
−61.920
1.00
63.88

ATOM
194
O
ARG

170
−38.826
79.943
−61.681
1.00
62.83

ATOM
195
N
GLU

171
−39.368
82.058
−61.117
1.00
65.09

ATOM
196
CA
GLU

171
−40.030
81.724
−59.868
1.00
66.62

ATOM
197
CB
GLU

171
−40.279
83.011
−59.069
1.00
66.66

ATOM
198
CG
GLU

171
−41.025
82.839
−57.743
1.00
68.07

ATOM
199
CD
GLU

171
−41.262
84.170
−57.029
1.00
68.86

ATOM
200
OE1
GLU

171
−41.790
85.098
−57.677
1.00
69.85

ATOM
201
OE2
GLU

171
−40.930
84.300
−55.831
1.00
67.30

ATOM
202
C
GLU

171
−41.356
81.047
−60.215
1.00
67.69

ATOM
203
O
GLU

171
−42.271
81.695
−60.708
1.00
67.97

ATOM
204
N
LYS

172
−41.449
79.744
−59.966
1.00
68.76

ATOM
205
CA
LYS

172
−42.663
78.980
−60.253
1.00
69.57

ATOM
206
CB
LYS

172
−42.498
77.547
−59.751
1.00
68.09

ATOM
207
CG
LYS

172
−41.690
76.689
−60.690
1.00
69.02

ATOM
208
CD
LYS

172
−41.285
75.359
−60.075
1.00
68.14

ATOM
209
CE
LYS

172
−40.239
75.554
−58.997
1.00
69.50

ATOM
210
NZ
LYS

172
−39.596
74.269
−58.604
1.00
68.90

ATOM
211
C
LYS

172
−43.947
79.574
−59.669
1.00
70.67

ATOM
212
O
LYS

172
−45.036
79.401
−60.221
1.00
70.71

ATOM
213
N
ALA

173
−43.818
80.284
−58.557
1.00
72.24

ATOM
214
CA
ALA

173
−44.975
80.877
−57.895
1.00
73.96

ATOM
215
CB
ALA

173
−44.610
81.276
−56.461
1.00
74.11

ATOM
216
C
ALA

173
−45.557
82.077
−58.631
1.00
74.82

ATOM
217
O
ALA

173
−46.768
82.284
−58.619
1.00
75.00

ATOM
218
N
THR

174
−44.707
82.862
−59.280
1.00
75.03

ATOM
219
CA
THR

174
−45.194
84.042
−59.968
1.00
74.48

ATOM
220
CB
THR

174
−44.458
85.293
−59.481
1.00
74.95

ATOM
221
OG1
THR

174
−43.072
85.187
−59.829
1.00
75.75

ATOM
222
CG2
THR

174
−44.589
85.434
−57.969
1.00
74.21

ATOM
223
C
THR

174
−45.031
83.962
−61.467
1.00
74.15

ATOM
224
O
THR

174
−45.641
84.736
−62.200
1.00
75.49

ATOM
225
N
GLY

175
−44.217
83.023
−61.929
1.00
73.18

ATOM
226
CA
GLY

175
−43.975
82.911
−63.355
1.00
70.33

ATOM
227
C
GLY

175
−43.052
84.045
−63.763
1.00
69.05

ATOM
228
O
GLY

175
−42.743
84.212
−64.937
1.00
69.75

ATOM
229
N
ARG

176
−42.610
84.823
−62.779
1.00
67.92

ATOM
230
CA
ARG

176
−41.719
85.960
−62.999
1.00
68.93

ATOM
231
CB
ARG

176
−41.817
86.915
−61.811
1.00
71.59

ATOM
232
CG
ARG

176
−43.150
87.625
−61.671
1.00
75.57

ATOM
233
CD
ARG

176
−43.366
88.603
−62.812
1.00
79.75

ATOM
234
NE
ARG

176
−44.674
89.255
−62.739
1.00
84.37

ATOM
235
CZ
ARG

176
−45.225
89.958
−63.730
1.00
86.47

ATOM
236
NH1
ARG

176
−44.583
90.108
−64.886
1.00
87.26

ATOM
237
NH2
ARG

176
−46.425
90.508
−63.568
1.00
87.79

ATOM
238
C
ARG

176
−40.242
85.576
−63.212
1.00
67.74

ATOM
239
O
ARG

176
−39.745
84.623
−62.620
1.00
67.72

ATOM
240
N
TYR

177
−39.537
86.337
−64.044
1.00
66.26

ATOM
241
CA
TYR

177
−38.132
86.061
−64.319
1.00
63.67

ATOM
242
CB
TYR

177
−37.806
86.317
−65.784
1.00
64.16

ATOM
243
CG
TYR

177
−38.470
85.356
−66.723
1.00
64.07

ATOM
244
CD1
TYR

177
−39.806
85.502
−67.075
1.00
64.56

ATOM
245
CE1
TYR

177
−40.433
84.590
−67.920
1.00
65.12

ATOM
246
CD2
TYR

177
−37.776
84.284
−67.235
1.00
64.52

ATOM
247
CE2
TYR

177
−38.395
83.372
−68.076
1.00
66.54

ATOM
248
CZ
TYR

177
−39.718
83.528
−68.411
1.00
65.13

ATOM
249
OH
TYR

177
−40.316
82.598
−69.220
1.00
63.95

ATOM
250
C
TYR

177
−37.160
86.854
−63.476
1.00
62.79

ATOM
251
O
TYR

177
−37.361
88.039
−63.198
1.00
62.55

ATOM
252
N
TYR

178
−36.092
86.179
−63.074
1.00
61.19

ATOM
253
CA
TYR

178
−35.052
86.798
−62.277
1.00
60.06

ATOM
254
CB
TYR

178
−35.244
86.527
−60.782
1.00
61.97

ATOM
255
CG
TYR

178
−36.565
86.987
−60.216
1.00
63.36

ATOM
256
CD1
TYR

178
−37.740
86.288
−60.491
1.00
62.38

ATOM
257
CE1
TYR

178
−38.958
86.708
−59.985
1.00
63.50

ATOM
258
CD2
TYR

178
−36.642
88.129
−59.411
1.00
63.43

ATOM
259
CE2
TYR

178
−37.866
88.563
−58.897
1.00
64.13

ATOM
260
CZ
TYR

178
−39.017
87.843
−59.194
1.00
64.76

ATOM
261
OH
TYR

178
−40.235
88.258
−58.713
1.00
67.74

ATOM
262
C
TYR

178
−33.714
86.237
−62.675
1.00
58.06

ATOM
263
O
TYR

178
−33.610
85.228
−63.370
1.00
56.48

ATOM
264
N
ALA

179
−32.685
86.926
−62.232
1.00
57.38

ATOM
265
CA
ALA

179
−31.340
86.484
−62.473
1.00
56.62

ATOM
266
CB
ALA

179
−30.493
87.626
−62.991
1.00
56.58

ATOM
267
C
ALA

179
−30.876
86.055
−61.087
1.00
55.18

ATOM
268
O
ALA

179
−31.051
86.789
−60.112
1.00
53.35

ATOM
269
N
MET

180
−30.325
84.851
−60.999
1.00
55.43

ATOM
270
CA
MET

180
−29.838
84.332
−59.724
1.00
55.24

ATOM
271
CB
MET

180
−30.410
82.940
−59.446
1.00
53.54

ATOM
272
CG
MET

180
−30.001
82.356
−58.100
1.00
54.72

ATOM
273
SD
MET

180
−30.551
80.638
−57.860
1.00
54.86

ATOM
274
CE
MET

180
−32.238
80.891
−57.326
1.00
52.28

ATOM
275
C
MET

180
−28.323
84.263
−59.741
1.00
55.40

ATOM
276
O
MET

180
−27.718
83.596
−60.585
1.00
55.12

ATOM
277
N
LYS

181
−27.727
84.983
−58.804
1.00
56.75

ATOM
278
CA
LYS

181
−26.287
85.039
−58.657
1.00
58.97

ATOM
279
CB
LYS

181
−25.882
86.432
−58.186
1.00
60.57

ATOM
280
CG
LYS

181
−24.399
86.712
−58.255
1.00
66.33

ATOM
281
CD
LYS

181
−24.120
88.222
−58.086
1.00
70.83

ATOM
282
CE
LYS

181
−22.663
88.570
−58.410
1.00
72.71

ATOM
283
NZ
LYS

181
−22.345
90.004
−58.147
1.00
73.68

ATOM
284
C
LYS

181
−25.929
83.990
−57.611
1.00
58.69

ATOM
285
O
LYS

181
−26.406
84.048
−56.475
1.00
58.27

ATOM
286
N
ILE

182
−25.105
83.027
−58.011
1.00
59.91

ATOM
287
CA
ILE

182
−24.678
81.933
−57.133
1.00
61.37

ATOM
288
CB
ILE

182
−24.906
80.567
−57.818
1.00
60.20

ATOM
289
CG2
ILE

182
−24.475
79.443
−56.906
1.00
60.60

ATOM
290
CG1
ILE

182
−26.385
80.407
−58.156
1.00
59.22

ATOM
291
CD1
ILE

182
−26.687
79.161
−58.947
1.00
57.26

ATOM
292
C
ILE

182
−23.209
82.068
−56.745
1.00
62.16

ATOM
293
O
ILE

182
−22.309
81.687
−57.495
1.00
61.70

ATOM
294
N
LEU

183
−22.980
82.614
−55.559
1.00
64.42

ATOM
295
CA
LEU

183
−21.632
82.828
−55.067
1.00
68.23

ATOM
296
CB
LEU

183
−21.565
84.124
−54.266
1.00
67.68

ATOM
297
CG
LEU

183
−21.808
85.409
−55.041
1.00
68.73

ATOM
298
CD1
LEU

183
−21.638
86.584
−54.098
1.00
68.65

ATOM
299
CD2
LEU

183
−20.835
85.500
−56.220
1.00
68.73

ATOM
300
C
LEU

183
−21.101
81.716
−54.189
1.00
70.99

ATOM
301
O
LEU

183
−21.739
81.339
−53.201
1.00
70.76

ATOM
302
N
ARG

184
−19.924
81.210
−54.543
1.00
73.48

ATOM
303
CA
ARG

184
−19.283
80.175
−53.753
1.00
76.54

ATOM
304
CB
ARG

184
−17.967
79.743
−54.397
1.00
76.87

ATOM
305
CG
ARG

184
−18.041
79.414
−55.881
1.00
79.16

ATOM
306
CD
ARG

184
−18.383
77.946
−56.135
1.00
80.34

ATOM
307
NE
ARG

184
−18.284
77.570
−57.554
1.00
82.37

ATOM
308
CZ
ARG

184
−18.920
78.183
−58.558
1.00
83.04

ATOM
309
NH1
ARG

184
−19.718
79.228
−58.331
1.00
82.96

ATOM
310
NH2
ARG

184
−18.777
77.738
−59.800
1.00
82.81

ATOM
311
C
ARG

184
−18.976
80.844
−52.414
1.00
78.39

ATOM
312
O
ARG

184
−18.497
81.977
−52.381
1.00
77.88

ATOM
313
N
LYS

185
−19.286
80.172
−51.311
1.00
81.21

ATOM
314
CA
LYS

185
−18.979
80.726
−49.997
1.00
83.85

ATOM
315
CB
LYS

185
−19.663
79.918
−48.886
1.00
82.70

ATOM
316
CG
LYS

185
−21.127
80.273
−48.646
1.00
82.88

ATOM
317
CD
LYS

185
−21.737
79.414
−47.532
1.00
82.13

ATOM
318
CE
LYS

185
−23.202
79.768
−47.259
1.00
80.52

ATOM
319
NZ
LYS

185
−23.902
78.757
−46.406
1.00
79.61

ATOM
320
C
LYS

185
−17.468
80.569
−49.903
1.00
86.31

ATOM
321
O
LYS

185
−16.755
81.439
−49.398
1.00
86.24

ATOM
322
N
GLU

186
−17.004
79.436
−50.425
1.00
88.89

ATOM
323
CA
GLU

186
−15.595
79.076
−50.457
1.00
91.04

ATOM
324
CB
GLU

186
−15.429
77.838
−51.331
1.00
91.80

ATOM
325
CG
GLU

186
−14.030
77.303
−51.396
1.00
93.01

ATOM
326
CD
GLU

186
−13.991
75.916
−51.987
1.00
93.49

ATOM
327
OE1
GLU

186
−14.374
75.754
−53.165
1.00
92.38

ATOM
328
OE2
GLU

186
−13.583
74.983
−51.262
1.00
94.32

ATOM
329
C
GLU

186
−14.759
80.226
−51.003
1.00
92.26

ATOM
330
O
GLU

186
−13.808
80.676
−50.361
1.00
93.52

ATOM
331
N
VAL

187
−15.125
80.700
−52.191
1.00
93.66

ATOM
332
CA
VAL

187
−14.430
81.810
−52.836
1.00
94.85

ATOM
333
CB
VAL

187
−15.129
82.202
−54.165
1.00
95.02

ATOM
334
CG1
VAL

187
−14.700
83.605
−54.597
1.00
94.99

ATOM
335
CG2
VAL

187
−14.792
81.182
−55.247
1.00
94.32

ATOM
336
C
VAL

187
−14.363
83.036
−51.927
1.00
95.77

ATOM
337
O
VAL

187
−13.284
83.575
−51.691
1.00
96.57

ATOM
338
N
ILE

188
−15.516
83.471
−51.423
1.00
96.66

ATOM
339
CA
ILE

188
−15.588
84.634
−50.539
1.00
97.25

ATOM
340
CB
ILE

188
−17.052
85.166
−50.409
1.00
97.70

ATOM
341
CG2
ILE

188
−17.997
84.034
−50.014
1.00
98.38

ATOM
342
CG1
ILE

188
−17.108
86.302
−49.381
1.00
97.42

ATOM
343
CD1
ILE

188
−18.504
86.790
−49.062
1.00
96.61

ATOM
344
C
ILE

188
−15.061
84.294
−49.146
1.00
97.74

ATOM
345
O
ILE

188
−14.751
85.183
−48.345
1.00
98.04

ATOM
346
N
ALA

198
−18.217
91.398
−48.874
1.00
112.30

ATOM
347
CA
ALA

198
−19.344
92.061
−48.228
1.00
112.68

ATOM
348
CB
ALA

198
−18.944
92.535
−46.839
1.00
111.86

ATOM
349
C
ALA

198
−19.841
93.242
−49.057
1.00
113.24

ATOM
350
O
ALA

198
−21.048
93.456
−49.184
1.00
112.83

ATOM
351
N
ALA

199
−18.908
94.005
−49.622
1.00
114.02

ATOM
352
CA
ALA

199
−19.255
95.170
−50.438
1.00
114.16

ATOM
353
CB
ALA

199
−17.989
95.795
−51.030
1.00
113.26

ATOM
354
C
ALA

199
−20.221
94.796
−51.559
1.00
114.23

ATOM
355
O
ALA

199
−20.779
95.669
−52.224
1.00
114.58

ATOM
356
N
ALA

200
−20.418
93.496
−51.759
1.00
114.26

ATOM
357
CA
ALA

200
−21.309
93.003
−52.804
1.00
114.40

ATOM
358
CB
ALA

200
−20.589
91.932
−53.633
1.00
114.28

ATOM
359
C
ALA

200
−22.625
92.445
−52.247
1.00
114.21

ATOM
360
O
ALA

200
−23.589
92.244
−52.988
1.00
114.12

ATOM
361
N
ALA

201
−22.667
92.205
−50.940
1.00
113.54

ATOM
362
CA
ALA

201
−23.863
91.664
−50.305
1.00
112.74

ATOM
363
CB
ALA

201
−23.510
90.409
−49.513
1.00
112.58

ATOM
364
C
ALA

201
−24.482
92.706
−49.388
1.00
112.67

ATOM
365
O
ALA

201
−23.796
93.623
−48.936
1.00
113.41

ATOM
366
N
ALA

202
−25.777
92.553
−49.112
1.00
111.66

ATOM
367
CA
ALA

202
−26.520
93.475
−48.253
1.00
109.46

ATOM
368
CB
ALA

202
−25.917
93.503
−46.845
1.00
109.54

ATOM
369
C
ALA

202
−26.524
94.873
−48.860
1.00
107.99

ATOM
370
O
ALA

202
−27.585
95.470
−49.053
1.00
107.70

ATOM
371
N
ALA

203
−25.332
95.386
−49.163
1.00
106.33

ATOM
372
CA
ALA

203
−25.189
96.711
−49.759
1.00
104.82

ATOM
373
CB
ALA

203
−23.759
96.915
−50.279
1.00
104.06

ATOM
374
C
ALA

203
−26.185
96.789
−50.902
1.00
103.73

ATOM
375
O
ALA

203
−27.143
97.558
−50.849
1.00
103.87

ATOM
376
N
ALA

204
−25.959
95.972
−51.925
1.00
102.19

ATOM
377
CA
ALA

204
−26.843
95.929
−53.078
1.00
100.05

ATOM
378
CB
ALA

204
−26.277
94.995
−54.148
1.00
100.32

ATOM
379
C
ALA

204
−28.210
95.440
−52.628
1.00
98.98

ATOM
380
O
ALA

204
−29.234
95.845
−53.185
1.00
99.48

ATOM
381
N
ALA

205
−28.219
94.575
−51.612
1.00
96.81

ATOM
382
CA
ALA

205
−29.459
94.016
−51.079
1.00
93.77

ATOM
383
CB
ALA

205
−29.171
93.174
−49.847
1.00
93.47

ATOM
384
C
ALA

205
−30.442
95.122
−50.730
1.00
91.99

ATOM
385
O
ALA

205
−31.663
94.956
−50.847
1.00
92.30

ATOM
386
N
ALA

206
−29.911
96.260
−50.306
1.00
88.38

ATOM
387
CA
ALA

206
−30.778
97.360
−49.948
1.00
84.60

ATOM
388
CB
ALA

206
−30.428
97.858
−48.568
1.00
85.09

ATOM
389
C
ALA

206
−30.771
98.511
−50.947
1.00
81.63

ATOM
390
O
ALA

206
−31.811
99.146
−51.150
1.00
82.52

ATOM
391
N
THR

207
−29.633
98.789
−51.583
1.00
77.52

ATOM
392
CA
THR

207
−29.610
99.901
−52.537
1.00
73.18

ATOM
393
CB
THR

207
−28.264
100.054
−53.262
1.00
73.37

ATOM
394
OG1
THR

207
−27.940
98.830
−53.934
1.00
73.63

ATOM
395
CG2
THR

207
−27.166
100.443
−52.273
1.00
71.60

ATOM
396
C
THR

207
−30.703
99.705
−53.559
1.00
69.95

ATOM
397
O
THR

207
−30.618
98.872
−54.460
1.00
71.26

ATOM
398
N
ARG

208
−31.752
100.482
−53.382
1.00
66.22

ATOM
399
CA
ARG

208
−32.903
100.424
−54.249
1.00
62.60

ATOM
400
CB
ARG

208
−34.161
100.336
−53.392
1.00
65.54

ATOM
401
CG
ARG

208
−35.441
100.224
−54.168
1.00
71.05

ATOM
402
CD
ARG

208
−35.830
98.778
−54.390
1.00
74.90

ATOM
403
NE
ARG

208
−37.066
98.710
−55.161
1.00
78.98

ATOM
404
CZ
ARG

208
−37.885
97.664
−55.192
1.00
80.71

ATOM
405
NH1
ARG

208
−37.608
96.571
−54.486
1.00
81.00

ATOM
406
NH2
ARG

208
−38.993
97.722
−55.926
1.00
81.70

ATOM
407
C
ARG

208
−32.904
101.707
−55.061
1.00
57.41

ATOM
408
O
ARG

208
−32.743
102.789
−54.512
1.00
57.88

ATOM
409
N
HIS

209
−33.075
101.592
−56.368
1.00
51.12

ATOM
410
CA
HIS

209
−33.107
102.765
−57.211
1.00
44.06

ATOM
411
CB
HIS

209
−31.703
103.287
−57.410
1.00
40.97

ATOM
412
CG
HIS

209
−31.619
104.544
−58.206
1.00
39.71

ATOM
413
CD2
HIS

209
−31.229
105.796
−57.852
1.00
40.44

ATOM
414
ND1
HIS

209
−31.847
104.582
−59.566
1.00
38.76

ATOM
415
CE1
HIS

209
−31.588
105.797
−60.017
1.00
39.10

ATOM
416
NE2
HIS

209
−31.209
106.552
−58.999
1.00
38.77

ATOM
417
C
HIS

209
−33.705
102.334
−58.518
1.00
43.50

ATOM
418
O
HIS

209
−33.585
101.188
−58.906
1.00
42.53

ATOM
419
N
PRO

210
−34.404
103.253
−59.200
1.00
43.01

ATOM
420
CD
PRO

210
−34.750
104.591
−58.677
1.00
39.86

ATOM
421
CA
PRO

210
−35.051
103.018
−60.486
1.00
41.13

ATOM
422
CB
PRO

210
−35.417
104.427
−60.947
1.00
39.59

ATOM
423
CG
PRO

210
−35.777
105.085
−59.669
1.00
39.43

ATOM
424
C
PRO

210
−34.169
102.333
−61.507
1.00
41.97

ATOM
425
O
PRO

210
−34.638
101.461
−62.245
1.00
41.73

ATOM
426
N
PHE

211
−32.908
102.736
−61.574
1.00
40.52

ATOM
427
CA
PHE

211
−32.040
102.155
−62.569
1.00
43.90

ATOM
428
CB
PHE

211
−31.304
103.275
−63.278
1.00
44.90

ATOM
429
CG
PHE

211
−32.213
104.384
−63.724
1.00
47.06

ATOM
430
CD1
PHE

211
−33.322
104.107
−64.509
1.00
45.32

ATOM
431
CD2
PHE

211
−31.998
105.697
−63.301
1.00
46.48

ATOM
432
CE1
PHE

211
−34.209
105.119
−64.862
1.00
47.55

ATOM
433
CE2
PHE

211
−32.876
106.707
−63.647
1.00
44.53

ATOM
434
CZ
PHE

211
−33.985
106.418
−64.427
1.00
44.53

ATOM
435
C
PHE

211
−31.077
101.097
−62.053
1.00
45.03

ATOM
436
O
PHE

211
−30.200
100.625
−62.781
1.00
45.88

ATOM
437
N
LEU

212
−31.234
100.716
−60.796
1.00
45.41

ATOM
438
CA
LEU

212
−30.387
99.677
−60.259
1.00
46.32

ATOM
439
CB
LEU

212
−29.823
100.097
−58.906
1.00
45.21

ATOM
440
CG
LEU

212
−28.689
101.126
−58.969
1.00
46.08

ATOM
441
CD1
LEU

212
−28.195
101.433
−57.580
1.00
42.17

ATOM
442
CD2
LEU

212
−27.561
100.575
−59.816
1.00
44.69

ATOM
443
C
LEU

212
−31.204
98.398
−60.139
1.00
47.20

ATOM
444
O
LEU

212
−32.345
98.419
−59.696
1.00
46.29

ATOM
445
N
THR

213
−30.628
97.293
−60.589
1.00
49.03

ATOM
446
CA
THR

213
−31.271
95.989
−60.508
1.00
50.07

ATOM
447
CB
THR

213
−30.291
94.895
−60.952
1.00
52.26

ATOM
448
OG1
THR

213
−29.718
95.257
−62.215
1.00
52.98

ATOM
449
CG2
THR

213
−31.006
93.559
−61.087
1.00
52.62

ATOM
450
C
THR

213
−31.638
95.746
−59.039
1.00
49.24

ATOM
451
O
THR

213
−30.822
95.962
−58.148
1.00
49.43

ATOM
452
N
ALA

214
−32.851
95.291
−58.770
1.00
49.28

ATOM
453
CA
ALA

214
−33.247
95.076
−57.383
1.00
50.03

ATOM
454
CB
ALA

214
−34.693
95.471
−57.191
1.00
49.20

ATOM
455
C
ALA

214
−33.050
93.654
−56.913
1.00
50.38

ATOM
456
O
ALA

214
−33.210
92.709
−57.681
1.00
50.97

ATOM
457
N
LEU

215
−32.709
93.515
−55.639
1.00
51.62

ATOM
458
CA
LEU

215
−32.495
92.209
−55.018
1.00
53.41

ATOM
459
CB
LEU

215
−31.604
92.336
−53.794
1.00
52.18

ATOM
460
CG
LEU

215
−31.541
91.025
−53.023
1.00
55.10

ATOM
461
CD1
LEU

215
−30.601
90.071
−53.751
1.00
53.62

ATOM
462
CD2
LEU

215
−31.083
91.272
−51.598
1.00
52.91

ATOM
463
C
LEU

215
−33.839
91.727
−54.552
1.00
55.19

ATOM
464
O
LEU

215
−34.366
92.261
−53.601
1.00
55.13

ATOM
465
N
LYS

216
−34.405
90.729
−55.213
1.00
58.13

ATOM
466
CA
LYS

216
−35.706
90.231
−54.799
1.00
60.30

ATOM
467
CB
LYS

216
−36.348
89.456
−55.932
1.00
61.60

ATOM
468
CG
LYS

216
−37.769
89.099
−55.658
1.00
65.28

ATOM
469
CD
LYS

216
−38.609
90.335
−55.480
1.00
66.80

ATOM
470
CE
LYS

216
−40.077
89.974
−55.595
1.00
69.41

ATOM
471
NZ
LYS

216
−40.406
88.781
−54.766
1.00
71.09

ATOM
472
C
LYS

216
−35.574
89.356
−53.544
1.00
60.92

ATOM
473
O
LYS

216
−36.178
89.657
−52.515
1.00
61.66

ATOM
474
N
TYR

217
−34.798
88.279
−53.617
1.00
60.52

ATOM
475
CA
TYR

217
−34.590
87.440
−52.437
1.00
61.22

ATOM
476
CB
TYR

217
−35.256
86.070
−52.539
1.00
59.98

ATOM
477
CG
TYR

217
−36.693
86.089
−52.944
1.00
60.82

ATOM
478
CD1
TYR

217
−37.054
85.919
−54.272
1.00
58.85

ATOM
479
CE1
TYR

217
−38.383
85.948
−54.657
1.00
62.01

ATOM
480
CD2
TYR

217
−37.697
86.290
−51.997
1.00
60.67

ATOM
481
CE2
TYR

217
−39.037
86.317
−52.370
1.00
60.66

ATOM
482
CZ
TYR

217
−39.372
86.144
−53.698
1.00
62.10

ATOM
483
OH
TYR

217
−40.692
86.126
−54.072
1.00
64.17

ATOM
484
C
TYR

217
−33.120
87.178
−52.269
1.00
61.56

ATOM
485
O
TYR

217
−32.366
87.197
−53.242
1.00
62.12

ATOM
486
N
ALA

218
−32.733
86.923
−51.026
1.00
62.02

ATOM
487
CA
ALA

218
−31.363
86.595
−50.676
1.00
63.28

ATOM
488
CB
ALA

218
−30.697
87.751
−49.955
1.00
61.87

ATOM
489
C
ALA

218
−31.412
85.384
−49.759
1.00
63.85

ATOM
490
O
ALA

218
−31.782
85.504
−48.589
1.00
64.79

ATOM
491
N
PHE

219
−31.070
84.216
−50.293
1.00
64.05

ATOM
492
CA
PHE

219
−31.041
83.008
−49.483
1.00
63.40

ATOM
493
CB
PHE

219
−32.173
82.039
−49.860
1.00
61.42

ATOM
494
CG
PHE

219
−31.980
81.343
−51.169
1.00
61.44

ATOM
495
CD1
PHE

219
−32.354
81.948
−52.355
1.00
60.16

ATOM
496
CD2
PHE

219
−31.418
80.072
−51.218
1.00
60.74

ATOM
497
CE1
PHE

219
−32.173
81.296
−53.577
1.00
60.41

ATOM
498
CE2
PHE

219
−31.234
79.413
−52.433
1.00
61.58

ATOM
499
CZ
PHE

219
−31.611
80.024
−53.614
1.00
60.89

ATOM
500
C
PHE

219
−29.683
82.348
−49.672
1.00
65.35

ATOM
501
O
PHE

219
−28.892
82.758
−50.530
1.00
65.66

ATOM
502
N
GLN

220
−29.396
81.343
−48.857
1.00
66.57

ATOM
503
CA
GLN

220
−28.125
80.660
−48.971
1.00
68.74

ATOM
504
CB
GLN

220
−27.131
81.209
−47.943
1.00
72.76

ATOM
505
CG
GLN

220
−27.559
81.061
−46.486
1.00
76.92

ATOM
506
CD
GLN

220
−26.375
81.159
−45.524
1.00
80.40

ATOM
507
OE1
GLN

220
−25.585
82.111
−45.581
1.00
82.71

ATOM
508
NE2
GLN

220
−26.246
80.171
−44.636
1.00
81.00

ATOM
509
C
GLN

220
−28.248
79.160
−48.796
1.00
67.66

ATOM
510
O
GLN

220
−29.077
78.683
−48.027
1.00
66.84

ATOM
511
N
THR

221
−27.427
78.421
−49.536
1.00
66.83

ATOM
512
CA
THR

221
−27.409
76.975
−49.436
1.00
64.35

ATOM
513
CB
THR

221
−27.016
76.297
−50.778
1.00
62.50

ATOM
514
OG1
THR

221
−25.718
76.730
−51.192
1.00
59.24

ATOM
515
CG2
THR

221
−28.007
76.645
−51.856
1.00
61.99

ATOM
516
C
THR

221
−26.316
76.768
−48.409
1.00
65.53

ATOM
517
O
THR

221
−25.758
77.743
−47.912
1.00
66.18

ATOM
518
N
HIS

222
−26.009
75.523
−48.073
1.00
66.98

ATOM
519
CA
HIS

222
−24.955
75.265
−47.099
1.00
68.87

ATOM
520
CB
HIS

222
−25.074
73.831
−46.556
1.00
69.00

ATOM
521
CG
HIS

222
−23.844
72.999
−46.767
1.00
69.74

ATOM
522
CD2
HIS

222
−22.959
72.471
−45.886
1.00
69.08

ATOM
523
ND1
HIS

222
−23.378
72.670
−48.022
1.00
68.15

ATOM
524
CE1
HIS

222
−22.259
71.979
−47.905
1.00
69.85

ATOM
525
NE2
HIS

222
−21.982
71.843
−46.619
1.00
70.10

ATOM
526
C
HIS

222
−23.604
75.455
−47.795
1.00
69.04

ATOM
527
O
HIS

222
−22.539
75.431
−47.173
1.00
70.34

ATOM
528
N
ASP

223
−23.657
75.658
−49.098
1.00
67.92

ATOM
529
CA
ASP

223
−22.445
75.808
−49.878
1.00
67.17

ATOM
530
CB
ASP

223
−22.479
74.806
−51.043
1.00
67.71

ATOM
531
CG
ASP

223
−21.118
74.538
−51.619
1.00
66.74

ATOM
532
OD1
ASP

223
−21.034
74.122
−52.800
1.00
67.60

ATOM
533
OD2
ASP

223
−20.136
74.729
−50.880
1.00
66.85

ATOM
534
C
ASP

223
−22.257
77.210
−50.444
1.00
66.50

ATOM
535
O
ASP

223
−21.161
77.768
−50.389
1.00
66.77

ATOM
536
N
ARG

224
−23.334
77.781
−50.974
1.00
64.39

ATOM
537
CA
ARG

224
−23.239
79.070
−51.625
1.00
62.77

ATOM
538
CB
ARG

224
−23.387
78.831
−53.118
1.00
61.74

ATOM
539
CG
ARG

224
−22.711
77.528
−53.515
1.00
60.66

ATOM
540
CD
ARG

224
−22.760
77.254
−54.970
1.00
60.28

ATOM
541
NE
ARG

224
−21.849
76.175
−55.315
1.00
62.03

ATOM
542
CZ
ARG

224
−21.550
75.828
−56.559
1.00
63.12

ATOM
543
NH1
ARG

224
−22.097
76.472
−57.581
1.00
64.62

ATOM
544
NH2
ARG

224
−20.683
74.853
−56.790
1.00
65.79

ATOM
545
C
ARG

224
−24.230
80.106
−51.161
1.00
63.89

ATOM
546
O
ARG

224
−25.103
79.828
−50.332
1.00
65.57

ATOM
547
N
LEU

225
−24.070
81.316
−51.690
1.00
64.38

ATOM
548
CA
LEU

225
−24.958
82.430
−51.375
1.00
64.19

ATOM
549
CB
LEU

225
−24.155
83.675
−51.006
1.00
64.97

ATOM
550
CG
LEU

225
−23.191
83.535
−49.825
1.00
65.82

ATOM
551
CD1
LEU

225
−22.392
84.820
−49.678
1.00
66.26

ATOM
552
CD2
LEU

225
−23.964
83.235
−48.543
1.00
65.86

ATOM
553
C
LEU

225
−25.776
82.692
−52.632
1.00
63.53

ATOM
554
O
LEU

225
−25.238
82.692
−53.748
1.00
63.44

ATOM
555
N
CYS

226
−27.075
82.900
−52.461
1.00
62.16

ATOM
556
CA
CYS

226
−27.925
83.132
−53.613
1.00
61.86

ATOM
557
CB
CYS

226
−28.878
81.962
−53.805
1.00
61.51

ATOM
558
SG
CYS

226
−27.987
80.479
−54.257
1.00
67.89

ATOM
559
C
CYS

226
−28.695
84.432
−53.568
1.00
60.26

ATOM
560
O
CYS

226
−29.355
84.766
−52.586
1.00
60.82

ATOM
561
N
PHE

227
−28.592
85.167
−54.663
1.00
58.36

ATOM
562
CA
PHE

227
−29.264
86.438
−54.782
1.00
56.02

ATOM
563
CB
PHE

227
−28.227
87.539
−54.846
1.00
55.72

ATOM
564
CG
PHE

227
−27.247
87.499
−53.708
1.00
55.63

ATOM
565
CD1
PHE

227
−26.140
86.659
−53.757
1.00
56.15

ATOM
566
CD2
PHE

227
−27.424
88.304
−52.594
1.00
54.88

ATOM
567
CE1
PHE

227
−25.220
86.628
−52.715
1.00
55.00

ATOM
568
CE2
PHE

227
−26.507
88.279
−51.545
1.00
56.51

ATOM
569
CZ
PHE

227
−25.403
87.441
−51.609
1.00
55.60

ATOM
570
C
PHE

227
−30.134
86.431
−56.016
1.00
54.03

ATOM
571
O
PHE

227
−29.658
86.369
−57.142
1.00
52.89

ATOM
572
N
VAL

228
−31.429
86.449
−55.781
1.00
52.44

ATOM
573
CA
VAL

228
−32.372
86.445
−56.865
1.00
52.04

ATOM
574
CB
VAL

228
−33.651
85.726
−56.445
1.00
51.79

ATOM
575
CG1
VAL

228
−34.632
85.715
−57.578
1.00
51.78

ATOM
576
CG2
VAL

228
−33.314
84.310
−56.017
1.00
53.18

ATOM
577
C
VAL

228
−32.649
87.911
−57.110
1.00
52.53

ATOM
578
O
VAL

228
−33.119
88.616
−56.212
1.00
51.60

ATOM
579
N
MET

229
−32.333
88.391
−58.307
1.00
53.03

ATOM
580
CA
MET

229
−32.569
89.799
−58.592
1.00
53.34

ATOM
581
CB
MET

229
−31.242
90.536
−58.712
1.00
56.21

ATOM
582
CG
MET

229
−30.322
90.228
−57.557
1.00
61.27

ATOM
583
SD
MET

229
−28.661
90.744
−57.952
1.00
73.99

ATOM
584
CE
MET

229
−28.454
90.022
−59.617
1.00
68.07

ATOM
585
C
MET

229
−33.409
89.997
−59.828
1.00
51.78

ATOM
586
O
MET

229
−33.460
89.146
−60.715
1.00
50.70

ATOM
587
N
GLU

230
−34.087
91.131
−59.864
1.00
53.04

ATOM
588
CA
GLU

230
−34.952
91.462
−60.979
1.00
54.78

ATOM
589
CB
GLU

230
−35.549
92.868
−60.782
1.00
57.38

ATOM
590
CG
GLU

230
−34.583
93.987
−61.149
1.00
61.76

ATOM
591
CD
GLU

230
−35.195
95.382
−61.083
1.00
62.98

ATOM
592
OE1
GLU

230
−36.266
95.603
−61.690
1.00
64.36

ATOM
593
OE2
GLU

230
−34.586
96.260
−60.431
1.00
64.01

ATOM
594
C
GLU

230
−34.168
91.400
−62.293
1.00
52.88

ATOM
595
O
GLU

230
−32.988
91.775
−62.352
1.00
48.54

ATOM
596
N
TYR

231
−34.831
90.918
−63.338
1.00
52.60

ATOM
597
CA
TYR

231
−34.205
90.826
−64.637
1.00
53.84

ATOM
598
CB
TYR

231
−34.105
89.368
−65.092
1.00
54.55

ATOM
599
CG
TYR

231
−33.307
89.190
−66.376
1.00
56.70

ATOM
600
CD1
TYR

231
−31.947
89.516
−66.431
1.00
55.49

ATOM
601
CE1
TYR

231
−31.205
89.327
−67.608
1.00
57.10

ATOM
602
CD2
TYR

231
−33.909
88.678
−67.530
1.00
58.25

ATOM
603
CE2
TYR

231
−33.181
88.487
−68.706
1.00
57.41

ATOM
604
CZ
TYR

231
−31.832
88.808
−68.745
1.00
57.81

ATOM
605
OH
TYR

231
−31.115
88.598
−69.918
1.00
59.03

ATOM
606
C
TYR

231
−34.929
91.625
−65.717
1.00
54.12

ATOM
607
O
TYR

231
−36.075
91.332
−66.069
1.00
55.07

ATOM
608
N
ALA

232
−34.230
92.623
−66.248
1.00
53.26

ATOM
609
CA
ALA

232
−34.739
93.472
−67.319
1.00
54.44

ATOM
610
CB
ALA

232
−33.718
94.546
−67.640
1.00
51.99

ATOM
611
C
ALA

232
−34.965
92.599
−68.542
1.00
55.27

ATOM
612
O
ALA

232
−34.065
91.856
−68.943
1.00
56.46

ATOM
613
N
ASN

233
−36.146
92.682
−69.146
1.00
55.12

ATOM
614
CA
ASN

233
−36.401
91.856
−70.318
1.00
55.88

ATOM
615
CB
ASN

233
−37.672
91.025
−70.113
1.00
58.18

ATOM
616
CG
ASN

233
−38.899
91.879
−69.978
1.00
56.33

ATOM
617
OD1
ASN

233
−39.520
92.223
−70.963
1.00
56.92

ATOM
618
ND2
ASN

233
−39.239
92.247
−68.747
1.00
58.52

ATOM
619
C
ASN

233
−36.486
92.633
−71.625
1.00
55.79

ATOM
620
O
ASN

233
−37.086
92.167
−72.589
1.00
56.57

ATOM
621
N
GLY

234
−35.879
93.816
−71.654
1.00
55.96

ATOM
622
CA
GLY

234
−35.874
94.619
−72.865
1.00
54.78

ATOM
623
C
GLY

234
−34.549
94.503
−73.616
1.00
55.90

ATOM
624
O
GLY

234
−34.223
95.348
−74.462
1.00
55.67

ATOM
625
N
GLY

235
−33.773
93.461
−73.307
1.00
53.62

ATOM
626
CA
GLY

235
−32.505
93.266
−73.981
1.00
50.27

ATOM
627
C
GLY

235
−31.361
94.058
−73.399
1.00
49.88

ATOM
628
O
GLY

235
−31.562
94.983
−72.611
1.00
48.36

ATOM
629
N
GLU

236
−30.147
93.692
−73.789
1.00
50.89

ATOM
630
CA
GLU

236
−28.952
94.368
−73.296
1.00
52.45

ATOM
631
CB
GLU

236
−27.805
93.369
−73.108
1.00
55.02

ATOM
632
CG
GLU

236
−27.858
92.179
−74.044
1.00
61.22

ATOM
633
CD
GLU

236
−28.458
90.912
−73.408
1.00
65.08

ATOM
634
OE1
GLU

236
−29.513
90.428
−73.896
1.00
67.00

ATOM
635
OE2
GLU

236
−27.863
90.397
−72.432
1.00
66.21

ATOM
636
C
GLU

236
−28.508
95.484
−74.217
1.00
51.78

ATOM
637
O
GLU

236
−28.652
95.395
−75.439
1.00
50.86

ATOM
638
N
LEU

237
−27.964
96.538
−73.619
1.00
52.51

ATOM
639
CA
LEU

237
−27.508
97.679
−74.380
1.00
54.32

ATOM
640
CB
LEU

237
−26.891
98.726
−73.467
1.00
53.44

ATOM
641
CG
LEU

237
−27.775
99.944
−73.202
1.00
53.88

ATOM
642
CD1
LEU

237
−26.850
101.115
−72.909
1.00
53.26

ATOM
643
CD2
LEU

237
−28.676
100.274
−74.409
1.00
51.94

ATOM
644
C
LEU

237
−26.523
97.319
−75.475
1.00
55.07

ATOM
645
O
LEU

237
−26.622
97.824
−76.591
1.00
56.10

ATOM
646
N
PHE

238
−25.566
96.460
−75.158
1.00
57.14

ATOM
647
CA
PHE

238
−24.589
96.048
−76.151
1.00
58.66

ATOM
648
CB
PHE

238
−23.763
94.887
−75.608
1.00
63.00

ATOM
649
CG
PHE

238
−23.122
94.064
−76.680
1.00
68.23

ATOM
650
CD1
PHE

238
−22.068
94.585
−77.441
1.00
70.20

ATOM
651
CD2
PHE

238
−23.608
92.791
−76.978
1.00
69.62

ATOM
652
CE1
PHE

238
−21.504
93.854
−78.487
1.00
71.02

ATOM
653
CE2
PHE

238
−23.057
92.044
−78.023
1.00
71.85

ATOM
654
CZ
PHE

238
−22.000
92.577
−78.782
1.00
72.24

ATOM
655
C
PHE

238
−25.326
95.627
−77.433
1.00
58.33

ATOM
656
O
PHE

238
−25.061
96.144
−78.523
1.00
58.19

ATOM
657
N
PHE

239
−26.272
94.706
−77.301
1.00
57.11

ATOM
658
CA
PHE

239
−27.031
94.249
−78.458
1.00
56.89

ATOM
659
CB
PHE

239
−28.108
93.239
−78.014
1.00
59.51

ATOM
660
CG
PHE

239
−29.150
92.922
−79.082
1.00
62.72

ATOM
661
CD1
PHE

239
−28.826
92.140
−80.199
1.00
63.57

ATOM
662
CD2
PHE

239
−30.464
93.412
−78.966
1.00
63.29

ATOM
663
CE1
PHE

239
−29.796
91.849
−81.188
1.00
63.48

ATOM
664
CE2
PHE

239
−31.439
93.130
−79.945
1.00
64.34

ATOM
665
CZ
PHE

239
−31.102
92.346
−81.058
1.00
64.06

ATOM
666
C
PHE

239
−27.684
95.393
−79.256
1.00
55.15

ATOM
667
O
PHE

239
−27.582
95.416
−80.488
1.00
55.59

ATOM
668
N
HIS

240
−28.363
96.316
−78.562
1.00
52.53

ATOM
669
CA
HIS

240
−29.043
97.447
−79.209
1.00
50.62

ATOM
670
CB
HIS

240
−29.870
98.241
−78.191
1.00
49.40

ATOM
671
CG
HIS

240
−31.047
97.493
−77.660
1.00
44.72

ATOM
672
CD2
HIS

240
−31.345
97.072
−76.409
1.00
46.34

ATOM
673
ND1
HIS

240
−32.058
97.032
−78.472
1.00
44.43

ATOM
674
CE1
HIS

240
−32.928
96.351
−77.748
1.00
44.08

ATOM
675
NE2
HIS

240
−32.519
96.359
−76.492
1.00
48.10

ATOM
676
C
HIS

240
−28.031
98.379
−79.861
1.00
51.18

ATOM
677
O
HIS

240
−28.158
98.753
−81.018
1.00
51.15

ATOM
678
N
LEU

241
−27.018
98.759
−79.103
1.00
51.15

ATOM
679
CA
LEU

241
−25.996
99.615
−79.645
1.00
50.61

ATOM
680
CB
LEU

241
−24.833
99.747
−78.664
1.00
45.73

ATOM
681
CG
LEU

241
−23.839
100.798
−79.168
1.00
44.27

ATOM
682
CD1
LEU

241
−24.560
102.140
−79.451
1.00
42.06

ATOM
683
CD2
LEU

241
−22.726
100.964
−78.142
1.00
43.07

ATOM
684
C
LEU

241
−25.477
99.044
−80.958
1.00
53.54

ATOM
685
O
LEU

241
−25.604
99.673
−82.016
1.00
54.97

ATOM
686
N
SER

242
−24.898
97.847
−80.890
1.00
56.14

ATOM
687
CA
SER

242
−24.335
97.214
−82.075
1.00
58.25

ATOM
688
CB
SER

242
−23.868
95.804
−81.746
1.00
57.13

ATOM
689
OG
SER

242
−24.967
94.935
−81.719
1.00
59.66

ATOM
690
C
SER

242
−25.301
97.178
−83.257
1.00
59.57

ATOM
691
O
SER

242
−24.866
97.190
−84.401
1.00
60.46

ATOM
692
N
ARG

243
−26.606
97.143
−82.998
1.00
61.59

ATOM
693
CA
ARG

243
−27.563
97.134
−84.099
1.00
64.36

ATOM
694
CB
ARG

243
−28.916
96.585
−83.651
1.00
66.54

ATOM
695
CG
ARG

243
−28.887
95.112
−83.217
1.00
71.68

ATOM
696
CD
ARG

243
−30.302
94.528
−83.134
1.00
73.05

ATOM
697
NE
ARG

243
−30.893
94.274
−84.450
1.00
76.62

ATOM
698
CZ
ARG

243
−32.146
93.875
−84.642
1.00
76.35

ATOM
699
NH1
ARG

243
−32.942
93.688
−83.598
1.00
76.98

ATOM
700
NH2
ARG

243
−32.600
93.656
−85.873
1.00
74.86

ATOM
701
C
ARG

243
−27.774
98.525
−84.679
1.00
65.42

ATOM
702
O
ARG

243
−28.709
98.744
−85.441
1.00
66.61

ATOM
703
N
GLU

244
−26.911
99.468
−84.318
1.00
64.38

ATOM
704
CA
GLU

244
−27.042
100.833
−84.807
1.00
64.41

ATOM
705
CB
GLU

244
−27.862
101.674
−83.828
1.00
65.97

ATOM
706
CG
GLU

244
−29.054
100.950
−83.237
1.00
69.18

ATOM
707
CD
GLU

244
−30.265
101.847
−83.078
1.00
72.03

ATOM
708
OE1
GLU

244
−30.913
101.795
−82.005
1.00
74.67

ATOM
709
OE2
GLU

244
−30.574
102.598
−84.034
1.00
73.95

ATOM
710
C
GLU

244
−25.668
101.457
−84.943
1.00
63.51

ATOM
711
O
GLU

244
−25.534
102.582
−85.435
1.00
62.57

ATOM
712
N
ARG

245
−24.661
100.708
−84.495
1.00
61.39

ATOM
713
CA
ARG

245
−23.260
101.120
−84.508
1.00
60.43

ATOM
714
CB
ARG

245
−22.809
101.543
−85.912
1.00
61.28

ATOM
715
CG
ARG

245
−21.581
102.453
−85.911
1.00
64.32

ATOM
716
CD
ARG

245
−20.242
101.748
−85.697
1.00
67.77

ATOM
717
NE
ARG

245
−19.673
101.274
−86.959
1.00
71.50

ATOM
718
CZ
ARG

245
−19.872
100.058
−87.470
1.00
73.03

ATOM
719
NH1
ARG

245
−20.622
99.165
−86.825
1.00
72.40

ATOM
720
NH2
ARG

245
−19.340
99.741
−88.647
1.00
72.90

ATOM
721
C
ARG

245
−23.058
102.260
−83.524
1.00
58.48

ATOM
722
O
ARG

245
−22.064
102.301
−82.801
1.00
58.83

ATOM
723
N
VAL

246
−23.998
103.196
−83.513
1.00
56.29

ATOM
724
CA
VAL

246
−23.924
104.309
−82.591
1.00
54.40

ATOM
725
CB
VAL

246
−23.131
105.506
−83.150
1.00
54.63

ATOM
726
CG1
VAL

246
−22.577
106.312
−82.016
1.00
55.47

ATOM
727
CG2
VAL

246
−22.008
105.054
−84.036
1.00
57.36

ATOM
728
C
VAL

246
−25.320
104.799
−82.247
1.00
52.78

ATOM
729
O
VAL

246
−26.304
104.487
−82.920
1.00
49.96

ATOM
730
N
PHE

247
−25.379
105.550
−81.164
1.00
50.53

ATOM
731
CA
PHE

247
−26.614
106.118
−80.690
1.00
50.80

ATOM
732
CB
PHE

247
−26.774
105.906
−79.180
1.00
49.27

ATOM
733
CG
PHE

247
−27.254
104.559
−78.792
1.00
46.81

ATOM
734
CD1
PHE

247
−27.982
103.784
−79.673
1.00
48.42

ATOM
735
CD2
PHE

247
−27.037
104.092
−77.512
1.00
46.55

ATOM
736
CE1
PHE

247
−28.493
102.556
−79.277
1.00
47.03

ATOM
737
CE2
PHE

247
−27.544
102.863
−77.103
1.00
47.99

ATOM
738
CZ
PHE

247
−28.275
102.095
−77.992
1.00
47.33

ATOM
739
C
PHE

247
−26.542
107.623
−80.918
1.00
51.95

ATOM
740
O
PHE

247
−25.461
108.223
−80.874
1.00
50.17

ATOM
741
N
THR

248
−27.703
108.224
−81.138
1.00
52.44

ATOM
742
CA
THR

248
−27.809
109.669
−81.297
1.00
55.16

ATOM
743
CB
THR

248
−29.254
110.050
−81.510
1.00
55.99

ATOM
744
OG1
THR

248
−29.546
109.992
−82.910
1.00
58.05

ATOM
745
CG2
THR

248
−29.539
111.419
−80.939
1.00
58.66

ATOM
746
C
THR

248
−27.317
110.312
−80.007
1.00
53.97

ATOM
747
O
THR

248
−27.478
109.745
−78.940
1.00
53.89

ATOM
748
N
GLU

249
−26.710
111.484
−80.093
1.00
54.54

ATOM
749
CA
GLU

249
−26.229
112.116
−78.881
1.00
56.50

ATOM
750
CB
GLU

249
−25.561
113.442
−79.195
1.00
55.39

ATOM
751
CG
GLU

249
−24.268
113.279
−79.920
1.00
58.70

ATOM
752
CD
GLU

249
−23.445
114.543
−79.909
1.00
60.05

ATOM
753
OE1
GLU

249
−23.380
115.180
−78.841
1.00
62.42

ATOM
754
OE2
GLU

249
−22.852
114.895
−80.951
1.00
60.76

ATOM
755
C
GLU

249
−27.350
112.319
−77.874
1.00
57.15

ATOM
756
O
GLU

249
−27.111
112.420
−76.678
1.00
57.59

ATOM
757
N
GLU

250
−28.579
112.378
−78.344
1.00
57.29

ATOM
758
CA
GLU

250
−29.665
112.558
−77.408
1.00
59.02

ATOM
759
CB
GLU

250
−30.881
113.184
−78.083
1.00
60.37

ATOM
760
CG
GLU

250
−30.920
114.707
−77.961
1.00
63.15

ATOM
761
CD
GLU

250
−30.865
115.198
−76.505
1.00
63.92

ATOM
762
OE1
GLU

250
−29.747
115.503
−76.015
1.00
62.09

ATOM
763
OE2
GLU

250
−31.942
115.268
−75.853
1.00
63.53

ATOM
764
C
GLU

250
−30.043
111.237
−76.777
1.00
58.15

ATOM
765
O
GLU

250
−30.572
111.210
−75.665
1.00
59.23

ATOM
766
N
ARG

251
−29.794
110.147
−77.492
1.00
55.14

ATOM
767
CA
ARG

251
−30.075
108.829
−76.956
1.00
51.68

ATOM
768
CB
ARG

251
−29.975
107.771
−78.046
1.00
54.80

ATOM
769
CG
ARG

251
−31.236
106.944
−78.221
1.00
55.47

ATOM
770
CD
ARG

251
−30.932
105.468
−78.046
1.00
57.40

ATOM
771
NE
ARG

251
−31.620
104.635
−79.030
1.00
60.32

ATOM
772
CZ
ARG

251
−31.667
103.303
−78.996
1.00
61.07

ATOM
773
NH1
ARG

251
−31.069
102.631
−78.023
1.00
61.67

ATOM
774
NH2
ARG

251
−32.309
102.637
−79.944
1.00
61.79

ATOM
775
C
ARG

251
−28.985
108.612
−75.914
1.00
48.74

ATOM
776
O
ARG

251
−29.267
108.281
−74.770
1.00
48.32

ATOM
777
N
ALA

252
−27.734
108.817
−76.296
1.00
46.02

ATOM
778
CA
ALA

252
−26.654
108.642
−75.333
1.00
46.47

ATOM
779
CB
ALA

252
−25.376
109.340
−75.800
1.00
44.07

ATOM
780
C
ALA

252
−27.183
109.324
−74.089
1.00
45.73

ATOM
781
O
ALA

252
−27.374
108.699
−73.044
1.00
47.17

ATOM
782
N
ALA

253
−27.421
110.622
−74.240
1.00
43.78

ATOM
783
CA
ALA

253
−27.948
111.491
−73.199
1.00
38.33

ATOM
784
CB
ALA

253
−28.493
112.720
−73.840
1.00
37.71

ATOM
785
C
ALA

253
−29.034
110.815
−72.396
1.00
35.92

ATOM
786
O
ALA

253
−28.969
110.708
−71.181
1.00
37.83

ATOM
787
N
PHE

254
−30.054
110.336
−73.065
1.00
33.51

ATOM
788
CA
PHE

254
−31.092
109.718
−72.304
1.00
35.15

ATOM
789
CB
PHE

254
−32.128
109.129
−73.202
1.00
36.77

ATOM
790
CG
PHE

254
−33.197
108.427
−72.455
1.00
43.38

ATOM
791
CD1
PHE

254
−34.253
109.143
−71.903
1.00
42.17

ATOM
792
CD2
PHE

254
−33.144
107.041
−72.287
1.00
44.22

ATOM
793
CE1
PHE

254
−35.261
108.493
−71.192
1.00
44.09

ATOM
794
CE2
PHE

254
−34.140
106.367
−71.581
1.00
46.95

ATOM
795
CZ
PHE

254
−35.212
107.098
−71.028
1.00
46.80

ATOM
796
C
PHE

254
−30.555
108.618
−71.398
1.00
38.34

ATOM
797
O
PHE

254
−30.915
108.574
−70.227
1.00
39.59

ATOM
798
N
TYR

255
−29.710
107.726
−71.932
1.00
38.81

ATOM
799
CA
TYR

255
−29.138
106.622
−71.128
1.00
37.31

ATOM
800
CB
TYR

255
−28.457
105.555
−72.016
1.00
33.21

ATOM
801
CG
TYR

255
−29.437
104.850
−72.934
1.00
32.18

ATOM
802
CD1
TYR

255
−30.628
104.364
−72.445
1.00
31.36

ATOM
803
CE1
TYR

255
−31.548
103.785
−73.283
1.00
34.88

ATOM
804
CD2
TYR

255
−29.191
104.726
−74.299
1.00
32.34

ATOM
805
CE2
TYR

255
−30.117
104.144
−75.144
1.00
29.63

ATOM
806
CZ
TYR

255
−31.286
103.681
−74.627
1.00
31.05

ATOM
807
OH
TYR

255
−32.218
103.100
−75.431
1.00
34.60

ATOM
808
C
TYR

255
−28.145
107.113
−70.096
1.00
36.47

ATOM
809
O
TYR

255
−28.168
106.687
−68.950
1.00
40.42

ATOM
810
N
GLY

256
−27.278
108.028
−70.479
1.00
35.21

ATOM
811
CA
GLY

256
−26.302
108.482
−69.521
1.00
33.66

ATOM
812
C
GLY

256
−26.908
109.108
−68.291
1.00
38.33

ATOM
813
O
GLY

256
−26.409
108.899
−67.172
1.00
41.37

ATOM
814
N
ALA

257
−27.970
109.894
−68.477
1.00
36.89

ATOM
815
CA
ALA

257
−28.599
110.570
−67.354
1.00
34.76

ATOM
816
CB
ALA

257
−29.688
111.565
−67.862
1.00
36.88

ATOM
817
C
ALA

257
−29.205
109.567
−66.361
1.00
33.00

ATOM
818
O
ALA

257
−29.072
109.749
−65.170
1.00
35.08

ATOM
819
N
GLU

258
−29.864
108.520
−66.830
1.00
33.02

ATOM
820
CA
GLU

258
−30.424
107.563
−65.896
1.00
36.92

ATOM
821
CB
GLU

258
−31.248
106.489
−66.627
1.00
38.50

ATOM
822
CG
GLU

258
−32.366
107.082
−67.499
1.00
38.85

ATOM
823
CD
GLU

258
−33.535
106.114
−67.769
1.00
44.40

ATOM
824
OE1
GLU

258
−33.271
104.923
−68.061
1.00
45.03

ATOM
825
OE2
GLU

258
−34.728
106.540
−67.698
1.00
43.40

ATOM
826
C
GLU

258
−29.249
106.949
−65.099
1.00
39.65

ATOM
827
O
GLU

258
−29.373
106.663
−63.893
1.00
43.01

ATOM
828
N
ILE

259
−28.097
106.815
−65.749
1.00
36.89

ATOM
829
CA
ILE

259
−26.929
106.268
−65.085
1.00
36.09

ATOM
830
CB
ILE

259
−25.794
105.895
−66.118
1.00
35.08

ATOM
831
CG2
ILE

259
−24.466
105.704
−65.416
1.00
36.36

ATOM
832
CG1
ILE

259
−26.170
104.624
−66.868
1.00
33.56

ATOM
833
CD1
ILE

259
−25.203
104.279
−68.021
1.00
36.34

ATOM
834
C
ILE

259
−26.414
107.273
−64.079
1.00
35.91

ATOM
835
O
ILE

259
−26.079
106.918
−62.944
1.00
36.63

ATOM
836
N
VAL

260
−26.335
108.535
−64.475
1.00
36.67

ATOM
837
CA
VAL

260
−25.849
109.551
−63.537
1.00
34.46

ATOM
838
CB
VAL

260
−25.840
110.964
−64.156
1.00
32.53

ATOM
839
CG1
VAL

260
−25.309
111.951
−63.137
1.00
30.91

ATOM
840
CG2
VAL

260
−24.933
110.996
−65.353
1.00
26.79

ATOM
841
C
VAL

260
−26.694
109.594
−62.279
1.00
33.98

ATOM
842
O
VAL

260
−26.186
109.803
−61.164
1.00
33.13

ATOM
843
N
SER

261
−27.988
109.371
−62.473
1.00
35.21

ATOM
844
CA
SER

261
−28.961
109.363
−61.375
1.00
36.44

ATOM
845
CB
SER

261
−30.367
109.154
−61.957
1.00
34.12

ATOM
846
OG
SER

261
−31.335
109.138
−60.941
1.00
37.38

ATOM
847
C
SER

261
−28.618
108.261
−60.351
1.00
36.60

ATOM
848
O
SER

261
−28.585
108.499
−59.123
1.00
34.41

ATOM
849
N
ALA

262
−28.356
107.061
−60.875
1.00
36.24

ATOM
850
CA
ALA

262
−27.988
105.898
−60.055
1.00
36.35

ATOM
851
CB
ALA

262
−27.822
104.679
−60.928
1.00
37.72

ATOM
852
C
ALA

262
−26.701
106.178
−59.317
1.00
35.05

ATOM
853
O
ALA

262
−26.626
106.041
−58.106
1.00
39.79

ATOM
854
N
LEU

263
−25.687
106.591
−60.049
1.00
36.70

ATOM
855
CA
LEU

263
−24.406
106.889
−59.433
1.00
37.91

ATOM
856
CB
LEU

263
−23.385
107.255
−60.522
1.00
35.37

ATOM
857
CG
LEU

263
−22.971
106.076
−61.423
1.00
38.91

ATOM
858
CD1
LEU

263
−21.907
106.537
−62.445
1.00
33.32

ATOM
859
CD2
LEU

263
−22.422
104.934
−60.572
1.00
34.51

ATOM
860
C
LEU

263
−24.468
107.978
−58.348
1.00
38.63

ATOM
861
O
LEU

263
−23.790
107.870
−57.313
1.00
40.82

ATOM
862
N
GLU

264
−25.243
109.033
−58.585
1.00
39.29

ATOM
863
CA
GLU

264
−25.380
110.108
−57.591
1.00
39.52

ATOM
864
CB
GLU

264
−26.394
111.162
−58.051
1.00
43.65

ATOM
865
CG
GLU

264
−26.881
112.048
−56.899
1.00
49.73

ATOM
866
CD
GLU

264
−27.767
113.216
−57.346
1.00
52.93

ATOM
867
OE1
GLU

264
−28.758
113.004
−58.078
1.00
54.86

ATOM
868
OE2
GLU

264
−27.472
114.356
−56.941
1.00
54.54

ATOM
869
C
GLU

264
−25.906
109.485
−56.305
1.00
37.10

ATOM
870
O
GLU

264
−25.491
109.830
−55.197
1.00
32.98

ATOM
871
N
TYR

265
−26.834
108.555
−56.493
1.00
37.40

ATOM
872
CA
TYR

265
−27.465
107.861
−55.406
1.00
37.88

ATOM
873
CB
TYR

265
−28.609
106.993
−55.918
1.00
43.44

ATOM
874
CG
TYR

265
−29.424
106.466
−54.768
1.00
48.31

ATOM
875
CD1
TYR

265
−30.166
107.340
−53.982
1.00
53.35

ATOM
876
CE1
TYR

265
−30.876
106.899
−52.863
1.00
55.97

ATOM
877
CD2
TYR

265
−29.412
105.124
−54.416
1.00
50.34

ATOM
878
CE2
TYR

265
−30.130
104.668
−53.296
1.00
53.43

ATOM
879
CZ
TYR

265
−30.861
105.572
−52.525
1.00
55.06

ATOM
880
OH
TYR

265
−31.602
105.189
−51.416
1.00
59.22

ATOM
881
C
TYR

265
−26.479
106.984
−54.663
1.00
38.40

ATOM
882
O
TYR

265
−26.371
107.069
−53.440
1.00
38.68

ATOM
883
N
LEU

266
−25.765
106.129
−55.397
1.00
36.66

ATOM
884
CA
LEU

266
−24.800
105.241
−54.756
1.00
34.81

ATOM
885
CB
LEU

266
−24.179
104.280
−55.778
1.00
33.68

ATOM
886
CG
LEU

266
−25.120
103.207
−56.359
1.00
34.62

ATOM
887
CD1
LEU

266
−24.512
102.522
−57.548
1.00
33.12

ATOM
888
CD2
LEU

266
−25.439
102.176
−55.286
1.00
35.25

ATOM
889
C
LEU

266
−23.731
106.057
−54.047
1.00
32.09

ATOM
890
O
LEU

266
−23.404
105.779
−52.915
1.00
28.47

ATOM
891
N
HIS

267
−23.227
107.105
−54.678
1.00
34.14

ATOM
892
CA
HIS

267
−22.190
107.871
−54.008
1.00
36.06

ATOM
893
CB
HIS

267
−21.556
108.895
−54.954
1.00
37.44

ATOM
894
CG
HIS

267
−20.822
108.265
−56.099
1.00
39.63

ATOM
895
CD2
HIS

267
−20.728
106.970
−56.484
1.00
37.04

ATOM
896
ND1
HIS

267
−20.123
108.993
−57.037
1.00
39.82

ATOM
897
CE1
HIS

267
−19.637
108.173
−57.954
1.00
37.38

ATOM
898
NE2
HIS

267
−19.993
106.941
−57.641
1.00
36.45

ATOM
899
C
HIS

267
−22.690
108.547
−52.758
1.00
39.21

ATOM
900
O
HIS

267
−21.916
108.743
−51.818
1.00
40.44

ATOM
901
N
SER

268
−23.972
108.902
−52.718
1.00
39.67

ATOM
902
CA
SER

268
−24.492
109.539
−51.514
1.00
42.53

ATOM
903
CB
SER

268
−25.934
110.007
−51.709
1.00
42.69

ATOM
904
OG
SER

268
−26.823
108.908
−51.645
1.00
47.00

ATOM
905
C
SER

268
−24.432
108.559
−50.342
1.00
42.62

ATOM
906
O
SER

268
−24.422
108.976
−49.196
1.00
42.09

ATOM
907
N
ARG

269
−24.413
107.262
−50.640
1.00
45.09

ATOM
908
CA
ARG

269
−24.327
106.224
−49.626
1.00
48.53

ATOM
909
CB
ARG

269
−25.195
105.029
−50.013
1.00
51.99

ATOM
910
CG
ARG

269
−26.672
105.309
−50.120
1.00
57.10

ATOM
911
CD
ARG

269
−27.251
105.588
−48.746
1.00
62.32

ATOM
912
NE
ARG

269
−28.707
105.763
−48.740
1.00
67.05

ATOM
913
CZ
ARG

269
−29.373
106.699
−49.424
1.00
68.97

ATOM
914
NH1
ARG

269
−28.730
107.566
−50.201
1.00
69.91

ATOM
915
NH2
ARG

269
−30.691
106.794
−49.302
1.00
69.33

ATOM
916
C
ARG

269
−22.877
105.734
−49.505
1.00
50.09

ATOM
917
O
ARG

269
−22.649
104.611
−49.060
1.00
49.03

ATOM
918
N
ASP

270
−21.915
106.558
−49.924
1.00
50.68

ATOM
919
CA
ASP

270
−20.492
106.206
−49.871
1.00
52.09

ATOM
920
CB
ASP

270
−20.010
106.164
−48.417
1.00
57.80

ATOM
921
CG
ASP

270
−18.635
106.833
−48.217
1.00
63.46

ATOM
922
OD1
ASP

270
−17.708
106.571
−49.030
1.00
64.87

ATOM
923
OD2
ASP

270
−18.480
107.611
−47.232
1.00
66.66

ATOM
924
C
ASP

270
−20.218
104.845
−50.539
1.00
50.49

ATOM
925
O
ASP

270
−19.346
104.084
−50.116
1.00
51.23

ATOM
926
N
VAL

271
−20.985
104.542
−51.574
1.00
45.87

ATOM
927
CA
VAL

271
−20.831
103.304
−52.300
1.00
44.41

ATOM
928
CB
VAL

271
−22.163
102.633
−52.559
1.00
42.09

ATOM
929
CG1
VAL

271
−21.989
101.524
−53.568
1.00
40.36

ATOM
930
CG2
VAL

271
−22.721
102.114
−51.276
1.00
43.19

ATOM
931
C
VAL

271
−20.213
103.557
−53.666
1.00
46.59

ATOM
932
O
VAL

271
−20.705
104.400
−54.427
1.00
45.80

ATOM
933
N
VAL

272
−19.150
102.810
−53.974
1.00
45.19

ATOM
934
CA
VAL

272
−18.469
102.930
−55.253
1.00
42.21

ATOM
935
CB
VAL

272
−16.957
102.802
−55.093
1.00
40.51

ATOM
936
CG1
VAL

272
−16.313
102.730
−56.476
1.00
42.91

ATOM
937
CG2
VAL

272
−16.405
104.001
−54.326
1.00
38.71

ATOM
938
C
VAL

272
−18.983
101.788
−56.100
1.00
41.41

ATOM
939
O
VAL

272
−18.947
100.644
−55.682
1.00
42.62

ATOM
940
N
TYR

273
−19.464
102.059
−57.295
1.00
40.02

ATOM
941
CA
TYR

273
−19.997
100.938
−58.038
1.00
40.54

ATOM
942
CB
TYR

273
−20.982
101.428
−59.092
1.00
37.31

ATOM
943
CG
TYR

273
−21.854
100.323
−59.594
1.00
33.65

ATOM
944
CD1
TYR

273
−22.811
99.729
−58.770
1.00
36.03

ATOM
945
CE1
TYR

273
−23.602
98.665
−59.234
1.00
37.71

ATOM
946
CD2
TYR

273
−21.702
99.842
−60.872
1.00
34.61

ATOM
947
CE2
TYR

273
−22.479
98.794
−61.345
1.00
38.18

ATOM
948
CZ
TYR

273
−23.422
98.210
−60.528
1.00
36.31

ATOM
949
OH
TYR

273
−24.167
97.177
−61.040
1.00
40.78

ATOM
950
C
TYR

273
−18.962
100.001
−58.695
1.00
41.21

ATOM
951
O
TYR

273
−19.210
98.799
−58.812
1.00
39.04

ATOM
952
N
ARG

274
−17.849
100.567
−59.151
1.00
40.96

ATOM
953
CA
ARG

274
−16.772
99.824
−59.812
1.00
44.77

ATOM
954
CB
ARG

274
−16.198
98.756
−58.871
1.00
44.32

ATOM
955
CG
ARG

274
−15.573
99.267
−57.569
1.00
45.68

ATOM
956
CD
ARG

274
−15.067
98.053
−56.759
1.00
47.47

ATOM
957
NE
ARG

274
−14.406
98.397
−55.497
1.00
52.46

ATOM
958
CZ
ARG

274
−13.355
97.739
−55.002
1.00
51.71

ATOM
959
NH1
ARG

274
−12.839
96.710
−55.666
1.00
50.62

ATOM
960
NH2
ARG

274
−12.827
98.099
−53.838
1.00
49.56

ATOM
961
C
ARG

274
−17.114
99.136
−61.139
1.00
45.03

ATOM
962
O
ARG

274
−16.225
98.858
−61.933
1.00
45.38

ATOM
963
N
ASP

275
−18.391
98.860
−61.384
1.00
46.86

ATOM
964
CA
ASP

275
−18.796
98.160
−62.605
1.00
47.22

ATOM
965
CB
ASP

275
−19.534
96.872
−62.227
1.00
50.91

ATOM
966
CG
ASP

275
−18.600
95.798
−61.674
1.00
55.90

ATOM
967
OD1
ASP

275
−17.746
96.099
−60.804
1.00
55.33

ATOM
968
OD2
ASP

275
−18.734
94.632
−62.117
1.00
61.84

ATOM
969
C
ASP

275
−19.629
98.898
−63.649
1.00
46.70

ATOM
970
O
ASP

275
−20.512
98.300
−64.276
1.00
46.88

ATOM
971
N
ILE

276
−19.375
100.182
−63.859
1.00
45.39

ATOM
972
CA
ILE

276
−20.139
100.865
−64.890
1.00
42.27

ATOM
973
CB
ILE

276
−20.120
102.415
−64.728
1.00
44.44

ATOM
974
CG2
ILE

276
−20.910
103.055
−65.867
1.00
40.81

ATOM
975
CG1
ILE

276
−20.751
102.842
−63.389
1.00
41.78

ATOM
976
CD1
ILE

276
−22.138
102.296
−63.147
1.00
39.09

ATOM
977
C
ILE

276
−19.501
100.521
−66.225
1.00
42.12

ATOM
978
O
ILE

276
−18.404
100.958
−66.522
1.00
41.23

ATOM
979
N
LYS

277
−20.169
99.713
−67.031
1.00
42.85

ATOM
980
CA
LYS

277
−19.630
99.379
−68.336
1.00
44.14

ATOM
981
CB
LYS

277
−18.410
98.445
−68.210
1.00
47.06

ATOM
982
CG
LYS

277
−18.561
97.203
−67.357
1.00
49.66

ATOM
983
CD
LYS

277
−17.188
96.507
−67.310
1.00
57.47

ATOM
984
CE
LYS

277
−17.163
95.206
−66.516
1.00
58.16

ATOM
985
NZ
LYS

277
−17.881
94.084
−67.215
1.00
61.79

ATOM
986
C
LYS

277
−20.737
98.787
−69.174
1.00
43.44

ATOM
987
O
LYS

277
−21.646
98.178
−68.644
1.00
47.32

ATOM
988
N
LEU

278
−20.669
98.986
−70.481
1.00
42.84

ATOM
989
CA
LEU

278
−21.712
98.551
−71.400
1.00
42.92

ATOM
990
CB
LEU

278
−21.201
98.664
−72.841
1.00
45.02

ATOM
991
CG
LEU

278
−22.217
98.490
−73.981
1.00
49.27

ATOM
992
CD1
LEU

278
−23.288
99.584
−73.900
1.00
49.33

ATOM
993
CD2
LEU

278
−21.495
98.562
−75.347
1.00
49.44

ATOM
994
C
LEU

278
−22.329
97.178
−71.186
1.00
45.54

ATOM
995
O
LEU

278
−23.536
97.005
−71.345
1.00
45.54

ATOM
996
N
GLU

279
−21.508
96.194
−70.834
1.00
45.98

ATOM
997
CA
GLU

279
−21.993
94.832
−70.625
1.00
45.74

ATOM
998
CB
GLU

279
−20.795
93.898
−70.397
1.00
49.69

ATOM
999
CG
GLU

279
−19.574
94.156
−71.318
1.00
55.11

ATOM
1000
CD
GLU

279
−18.863
95.478
−71.020
1.00
58.90

ATOM
1001
OE1
GLU

279
−18.900
95.923
−69.859
1.00
63.47

ATOM
1002
OE2
GLU

279
−18.248
96.074
−71.932
1.00
60.83

ATOM
1003
C
GLU

279
−22.951
94.769
−69.423
1.00
44.36

ATOM
1004
O
GLU

279
−23.839
93.914
−69.348
1.00
41.91

ATOM
1005
N
ASN

280
−22.766
95.672
−68.470
1.00
42.34

ATOM
1006
CA
ASN

280
−23.629
95.685
−67.322
1.00
42.85

ATOM
1007
CB
ASN

280
−22.851
96.205
−66.120
1.00
45.62

ATOM
1008
CG
ASN

280
−21.818
95.186
−65.608
1.00
48.24

ATOM
1009
OD1
ASN

280
−21.001
94.708
−66.358
1.00
50.55

ATOM
1010
ND2
ASN

280
−21.869
94.865
−64.330
1.00
48.97

ATOM
1011
C
ASN

280
−24.896
96.519
−67.562
1.00
42.89

ATOM
1012
O
ASN

280
−25.646
96.790
−66.635
1.00
44.04

ATOM
1013
N
LEU

281
−25.155
96.911
−68.803
1.00
41.26

ATOM
1014
CA
LEU

281
−26.341
97.718
−69.080
1.00
40.35

ATOM
1015
CB
LEU

281
−25.993
99.011
−69.842
1.00
35.92

ATOM
1016
CG
LEU

281
−25.004
99.939
−69.121
1.00
35.39

ATOM
1017
CD1
LEU

281
−24.662
101.111
−69.992
1.00
32.28

ATOM
1018
CD2
LEU

281
−25.579
100.372
−67.790
1.00
33.88

ATOM
1019
C
LEU

281
−27.385
96.987
−69.868
1.00
41.54

ATOM
1020
O
LEU

281
−27.092
96.360
−70.907
1.00
40.29

ATOM
1021
N
MET

282
−28.609
97.074
−69.355
1.00
40.75

ATOM
1022
CA
MET

282
−29.765
96.481
−70.002
1.00
44.50

ATOM
1023
CB
MET

282
−30.222
95.240
−69.235
1.00
46.49

ATOM
1024
CG
MET

282
−29.137
94.171
−69.092
1.00
51.07

ATOM
1025
SD
MET

282
−29.909
92.558
−69.088
1.00
57.33

ATOM
1026
CE
MET

282
−30.611
92.576
−67.423
1.00
56.55

ATOM
1027
C
MET

282
−30.913
97.504
−70.057
1.00
45.24

ATOM
1028
O
MET

282
−30.831
98.588
−69.464
1.00
42.96

ATOM
1029
N
LEU

283
−31.975
97.156
−70.775
1.00
45.25

ATOM
1030
CA
LEU

283
−33.142
98.014
−70.854
1.00
45.02

ATOM
1031
CB
LEU

283
−33.456
98.374
−72.290
1.00
42.75

ATOM
1032
CG
LEU

283
−32.475
99.150
−73.135
1.00
42.36

ATOM
1033
CD1
LEU

283
−33.134
99.402
−74.492
1.00
41.24

ATOM
1034
CD2
LEU

283
−32.088
100.440
−72.452
1.00
41.01

ATOM
1035
C
LEU

283
−34.303
97.197
−70.316
1.00
46.71

ATOM
1036
O
LEU

283
−34.357
95.984
−70.528
1.00
44.94

ATOM
1037
N
ASP

284
−35.235
97.834
−69.613
1.00
48.53

ATOM
1038
CA
ASP

284
−36.391
97.078
−69.146
1.00
50.53

ATOM
1039
CB
ASP

284
−36.951
97.624
−67.822
1.00
52.33

ATOM
1040
CG
ASP

284
−37.398
99.066
−67.907
1.00
52.25

ATOM
1041
OD1
ASP

284
−37.813
99.541
−68.987
1.00
52.03

ATOM
1042
OD2
ASP

284
−37.348
99.724
−66.852
1.00
54.97

ATOM
1043
C
ASP

284
−37.465
97.120
−70.233
1.00
50.52

ATOM
1044
O
ASP

284
−37.286
97.758
−71.266
1.00
48.72

ATOM
1045
N
LYS

285
−38.570
96.433
−70.001
1.00
51.98

ATOM
1046
CA
LYS

285
−39.651
96.391
−70.973
1.00
54.76

ATOM
1047
CB
LYS

285
−40.889
95.751
−70.338
1.00
55.91

ATOM
1048
CG
LYS

285
−41.266
96.363
−69.003
1.00
58.33

ATOM
1049
CD
LYS

285
−42.302
95.524
−68.289
1.00
60.68

ATOM
1050
CE
LYS

285
−42.334
95.866
−66.809
1.00
62.11

ATOM
1051
NZ
LYS

285
−41.058
95.456
−66.129
1.00
62.92

ATOM
1052
C
LYS

285
−40.023
97.756
−71.560
1.00
54.80

ATOM
1053
O
LYS

285
−40.461
97.834
−72.710
1.00
55.83

ATOM
1054
N
ASP

286
−39.834
98.825
−70.788
1.00
54.22

ATOM
1055
CA
ASP

286
−40.203
100.160
−71.247
1.00
54.53

ATOM
1056
CB
ASP

286
−40.831
100.947
−70.101
1.00
55.42

ATOM
1057
CG
ASP

286
−42.065
100.277
−69.552
1.00
56.65

ATOM
1058
OD1
ASP

286
−42.930
99.908
−70.374
1.00
58.04

ATOM
1059
OD2
ASP

286
−42.169
100.124
−68.310
1.00
56.41

ATOM
1060
C
ASP

286
−39.141
101.040
−71.876
1.00
54.31

ATOM
1061
O
ASP

286
−39.387
102.220
−72.101
1.00
58.59

ATOM
1062
N
GLY

287
−37.965
100.516
−72.161
1.00
51.01

ATOM
1063
CA
GLY

287
−36.962
101.378
−72.753
1.00
48.45

ATOM
1064
C
GLY

287
−36.064
102.006
−71.714
1.00
47.14

ATOM
1065
O
GLY

287
−35.092
102.673
−72.066
1.00
48.27

ATOM
1066
N
HIS

288
−36.378
101.803
−70.435
1.00
47.24

ATOM
1067
CA
HIS

288
−35.551
102.342
−69.347
1.00
47.36

ATOM
1068
CB
HIS

288
−36.411
102.565
−68.114
1.00
47.39

ATOM
1069
CG
HIS

288
−37.181
103.840
−68.161
1.00
48.56

ATOM
1070
CD2
HIS

288
−38.513
104.078
−68.209
1.00
46.05

ATOM
1071
ND1
HIS

288
−36.565
105.073
−68.166
1.00
50.60

ATOM
1072
CE1
HIS

288
−37.488
106.019
−68.211
1.00
50.41

ATOM
1073
NE2
HIS

288
−38.677
105.441
−68.236
1.00
46.30

ATOM
1074
C
HIS

288
−34.309
101.490
−68.972
1.00
46.61

ATOM
1075
O
HIS

288
−34.331
100.252
−69.031
1.00
44.63

ATOM
1076
N
ILE

289
−33.234
102.173
−68.581
1.00
44.71

ATOM
1077
CA
ILE

289
−31.985
101.518
−68.213
1.00
43.43

ATOM
1078
CB
ILE

289
−30.820
102.522
−68.191
1.00
43.26

ATOM
1079
CG2
ILE

289
−30.061
102.415
−66.861
1.00
42.64

ATOM
1080
CG1
ILE

289
−29.934
102.306
−69.432
1.00
43.34

ATOM
1081
CD1
ILE

289
−28.522
102.939
−69.357
1.00
46.39

ATOM
1082
C
ILE

289
−31.970
100.769
−66.876
1.00
44.25

ATOM
1083
O
ILE

289
−32.575
101.200
−65.882
1.00
44.29

ATOM
1084
N
LYS

290
−31.264
99.641
−66.866
1.00
42.98

ATOM
1085
CA
LYS

290
−31.123
98.833
−65.666
1.00
41.38

ATOM
1086
CB
LYS

290
−31.941
97.545
−65.750
1.00
39.02

ATOM
1087
CG
LYS

290
−33.361
97.681
−65.368
1.00
40.24

ATOM
1088
CD
LYS

290
−33.484
97.938
−63.870
1.00
41.83

ATOM
1089
CE
LYS

290
−34.893
98.339
−63.545
1.00
40.44

ATOM
1090
NZ
LYS

290
−34.963
98.747
−62.141
1.00
42.96

ATOM
1091
C
LYS

290
−29.674
98.457
−65.552
1.00
40.99

ATOM
1092
O
LYS

290
−29.194
97.656
−66.319
1.00
40.05

ATOM
1093
N
ILE

291
−28.979
99.053
−64.597
1.00
42.46

ATOM
1094
CA
ILE

291
−27.589
98.748
−64.354
1.00
42.00

ATOM
1095
CB
ILE

291
−26.970
99.846
−63.530
1.00
41.72

ATOM
1096
CG2
ILE

291
−25.624
99.425
−63.022
1.00
39.30

ATOM
1097
CG1
ILE

291
−26.911
101.125
−64.379
1.00
41.56

ATOM
1098
CD1
ILE

291
−26.386
102.329
−63.638
1.00
40.40

ATOM
1099
C
ILE

291
−27.544
97.415
−63.602
1.00
45.01

ATOM
1100
O
ILE

291
−28.018
97.285
−62.482
1.00
40.95

ATOM
1101
N
THR

292
−26.970
96.426
−64.264
1.00
49.33

ATOM
1102
CA
THR

292
−26.855
95.073
−63.758
1.00
53.20

ATOM
1103
CB
THR

292
−26.859
94.118
−64.941
1.00
54.04

ATOM
1104
OG1
THR

292
−27.852
93.116
−64.747
1.00
52.48

ATOM
1105
CG2
THR

292
−25.502
93.507
−65.137
1.00
53.65

ATOM
1106
C
THR

292
−25.581
94.913
−62.963
1.00
58.02

ATOM
1107
O
THR

292
−24.707
95.773
−62.990
1.00
59.64

ATOM
1108
N
ASP

293
−25.469
93.801
−62.257
1.00
64.16

ATOM
1109
CA
ASP

293
−24.291
93.537
−61.428
1.00
69.42

ATOM
1110
CB
ASP

293
−24.722
93.339
−59.962
1.00
72.22

ATOM
1111
CG
ASP

293
−23.631
93.708
−58.971
1.00
75.85

ATOM
1112
OD1
ASP

293
−22.477
93.246
−59.147
1.00
79.23

ATOM
1113
OD2
ASP

293
−23.927
94.461
−58.010
1.00
77.35

ATOM
1114
C
ASP

293
−23.582
92.273
−61.909
1.00
71.22

ATOM
1115
O
ASP

293
−23.439
91.323
−61.140
1.00
73.99

ATOM
1116
N
PHE

294
−23.149
92.250
−63.167
1.00
72.25

ATOM
1117
CA
PHE

294
−22.475
91.077
−63.728
1.00
73.70

ATOM
1118
CB
PHE

294
−23.204
89.804
−63.303
1.00
72.45

ATOM
1119
CG
PHE

294
−24.660
89.793
−63.672
1.00
70.33

ATOM
1120
CD1
PHE

294
−25.061
89.453
−64.959
1.00
67.51

ATOM
1121
CD2
PHE

294
−25.636
90.131
−62.727
1.00
69.26

ATOM
1122
CE1
PHE

294
−26.420
89.447
−65.306
1.00
67.84

ATOM
1123
CE2
PHE

294
−26.998
90.127
−63.063
1.00
68.34

ATOM
1124
CZ
PHE

294
−27.392
89.784
−64.357
1.00
67.45

ATOM
1125
C
PHE

294
−22.445
91.135
−65.247
1.00
75.40

ATOM
1126
O
PHE

294
−23.320
91.738
−65.871
1.00
76.19

ATOM
1127
N
GLY

295
−21.459
90.481
−65.849
1.00
76.43

ATOM
1128
CA
GLY

295
−21.371
90.504
−67.295
1.00
77.74

ATOM
1129
C
GLY

295
−21.782
89.222
−67.991
1.00
78.56

ATOM
1130
O
GLY

295
−21.533
88.125
−67.498
1.00
78.40

ATOM
1131
N
ALA

296
−22.408
89.370
−69.155
1.00
79.85

ATOM
1132
CA
ALA

296
−22.851
88.230
−69.947
1.00
80.07

ATOM
1133
CB
ALA

296
−23.711
88.714
−71.116
1.00
78.65

ATOM
1134
C
ALA

296
−21.637
87.448
−70.468
1.00
80.65

ATOM
1135
O
ALA

296
−21.490
86.246
−70.221
1.00
79.69

ATOM
1136
N
THR

313
−14.667
91.536
−75.055
1.00
64.50

ATOM
1137
CA
THR

313
−14.516
92.943
−74.706
1.00
63.57

ATOM
1138
CB
THR

313
−15.812
93.497
−74.037
1.00
64.19

ATOM
1139
OG1
THR

313
−16.126
92.731
−72.865
1.00
63.91

ATOM
1140
CG2
THR

313
−16.997
93.422
−75.014
1.00
65.19

ATOM
1141
C
THR

313
−13.314
93.198
−73.775
1.00
62.47

ATOM
1142
O
THR

313
−13.105
92.490
−72.789
1.00
61.71

ATOM
1143
N
PRO

314
−12.481
94.191
−74.114
1.00
60.78

ATOM
1144
CD
PRO

314
−12.345
94.703
−75.485
1.00
60.25

ATOM
1145
CA
PRO

314
−11.304
94.542
−73.307
1.00
60.12

ATOM
1146
CB
PRO

314
−10.421
95.313
−74.292
1.00
58.86

ATOM
1147
CG
PRO

314
−10.849
94.810
−75.622
1.00
61.26

ATOM
1148
C
PRO

314
−11.714
95.424
−72.122
1.00
59.62

ATOM
1149
O
PRO

314
−12.561
96.304
−72.275
1.00
61.90

ATOM
1150
N
GLU

315
−11.130
95.194
−70.951
1.00
58.34

ATOM
1151
CA
GLU

315
−11.444
96.004
−69.776
1.00
57.56

ATOM
1152
CB
GLU

315
−10.955
95.337
−68.494
1.00
60.10

ATOM
1153
CG
GLU

315
−11.839
94.246
−67.961
1.00
66.09

ATOM
1154
CD
GLU

315
−11.955
94.301
−66.441
1.00
68.46

ATOM
1155
OE1
GLU

315
−12.651
95.213
−65.929
1.00
69.22

ATOM
1156
OE2
GLU

315
−11.349
93.440
−65.762
1.00
69.03

ATOM
1157
C
GLU

315
−10.798
97.387
−69.844
1.00
56.14

ATOM
1158
O
GLU

315
−9.649
97.528
−70.241
1.00
54.63

ATOM
1159
N
TYR

316
−11.538
98.412
−69.447
1.00
52.66

ATOM
1160
CA
TYR

316
−10.987
99.746
−69.452
1.00
48.79

ATOM
1161
CB
TYR

316
−11.782
100.657
−70.372
1.00
46.62

ATOM
1162
CG
TYR

316
−11.294
100.677
−71.793
1.00
43.91

ATOM
1163
CD1
TYR

316
−11.606
99.650
−72.674
1.00
41.71

ATOM
1164
CE1
TYR

316
−11.224
99.715
−74.026
1.00
43.79

ATOM
1165
CD2
TYR

316
−10.571
101.769
−72.275
1.00
44.76

ATOM
1166
CE2
TYR

316
−10.183
101.850
−73.610
1.00
43.33

ATOM
1167
CZ
TYR

316
−10.514
100.834
−74.485
1.00
42.50

ATOM
1168
OH
TYR

316
−10.189
100.967
−75.818
1.00
43.57

ATOM
1169
C
TYR

316
−11.035
100.272
−68.040
1.00
48.58

ATOM
1170
O
TYR

316
−11.866
101.127
−67.707
1.00
49.20

ATOM
1171
N
LEU

317
−10.154
99.745
−67.202
1.00
45.40

ATOM
1172
CA
LEU

317
−10.113
100.178
−65.825
1.00
45.80

ATOM
1173
CB
LEU

317
−9.159
99.311
−64.991
1.00
44.82

ATOM
1174
CG
LEU

317
−9.614
97.878
−64.736
1.00
47.19

ATOM
1175
CD1
LEU

317
−8.574
97.186
−63.873
1.00
46.19

ATOM
1176
CD2
LEU

317
−10.983
97.859
−64.027
1.00
44.93

ATOM
1177
C
LEU

317
−9.663
101.612
−65.767
1.00
45.03

ATOM
1178
O
LEU

317
−8.963
102.082
−66.655
1.00
44.87

ATOM
1179
N
ALA

318
−10.067
102.305
−64.710
1.00
43.87

ATOM
1180
CA
ALA

318
−9.683
103.686
−64.554
1.00
44.02

ATOM
1181
CB
ALA

318
−10.475
104.343
−63.434
1.00
44.38

ATOM
1182
C
ALA

318
−8.210
103.769
−64.246
1.00
43.01

ATOM
1183
O
ALA

318
−7.665
102.963
−63.497
1.00
44.82

ATOM
1184
N
PRO

319
−7.541
104.758
−64.815
1.00
42.59

ATOM
1185
CD
PRO

319
−8.016
105.783
−65.749
1.00
43.21

ATOM
1186
CA
PRO

319
−6.114
104.908
−64.555
1.00
42.84

ATOM
1187
CB
PRO

319
−5.782
106.290
−65.157
1.00
43.35

ATOM
1188
CG
PRO

319
−7.112
106.935
−65.379
1.00
45.27

ATOM
1189
C
PRO

319
−5.721
104.805
−63.091
1.00
43.49

ATOM
1190
O
PRO

319
−4.710
104.187
−62.774
1.00
44.53

ATOM
1191
N
GLU

320
−6.493
105.393
−62.182
1.00
43.03

ATOM
1192
CA
GLU

320
−6.079
105.312
−60.790
1.00
44.76

ATOM
1193
CB
GLU

320
−6.808
106.355
−59.893
1.00
48.10

ATOM
1194
CG
GLU

320
−8.326
106.204
−59.762
1.00
46.52

ATOM
1195
CD
GLU

320
−9.071
106.821
−60.926
1.00
48.46

ATOM
1196
OE1
GLU

320
−8.493
106.872
−62.040
1.00
47.31

ATOM
1197
OE2
GLU

320
−10.237
107.235
−60.723
1.00
47.04

ATOM
1198
C
GLU

320
−6.263
103.894
−60.262
1.00
44.72

ATOM
1199
O
GLU

320
−5.746
103.530
−59.215
1.00
43.21

ATOM
1200
N
VAL

321
−7.016
103.081
−60.975
1.00
46.54

ATOM
1201
CA
VAL

321
−7.154
101.715
−60.522
1.00
49.76

ATOM
1202
CB
VAL

321
−8.401
101.062
−61.087
1.00
50.16

ATOM
1203
CG1
VAL

321
−8.314
99.545
−60.908
1.00
48.56

ATOM
1204
CG2
VAL

321
−9.627
101.626
−60.374
1.00
50.78

ATOM
1205
C
VAL

321
−5.904
100.949
−60.980
1.00
51.61

ATOM
1206
O
VAL

321
−5.328
100.190
−60.199
1.00
53.12

ATOM
1207
N
LEU

322
−5.492
101.168
−62.235
1.00
50.45

ATOM
1208
CA
LEU

322
−4.291
100.537
−62.804
1.00
49.32

ATOM
1209
CB
LEU

322
−4.119
100.915
−64.272
1.00
47.27

ATOM
1210
CG
LEU

322
−5.229
100.509
−65.231
1.00
46.23

ATOM
1211
CD1
LEU

322
−4.944
101.014
−66.650
1.00
46.57

ATOM
1212
CD2
LEU

322
−5.341
98.997
−65.194
1.00
47.37

ATOM
1213
C
LEU

322
−3.041
100.994
−62.062
1.00
49.93

ATOM
1214
O
LEU

322
−2.205
100.196
−61.676
1.00
50.30

ATOM
1215
N
GLU

323
−2.907
102.285
−61.840
1.00
50.92

ATOM
1216
CA
GLU

323
−1.712
102.736
−61.160
1.00
53.42

ATOM
1217
CB
GLU

323
−1.429
104.196
−61.515
1.00
51.33

ATOM
1218
CG
GLU

323
−0.210
104.753
−60.819
1.00
52.71

ATOM
1219
CD
GLU

323
0.208
106.094
−61.364
1.00
54.31

ATOM
1220
OE1
GLU

323
−0.658
106.825
−61.899
1.00
53.42

ATOM
1221
OE2
GLU

323
1.406
106.422
−61.240
1.00
54.99

ATOM
1222
C
GLU

323
−1.688
102.539
−59.638
1.00
54.99

ATOM
1223
O
GLU

323
−0.654
102.178
−59.074
1.00
56.42

ATOM
1224
N
ASP

324
−2.812
102.748
−58.967
1.00
55.14

ATOM
1225
CA
ASP

324
−2.823
102.608
−57.530
1.00
54.80

ATOM
1226
CB
ASP

324
−2.933
103.980
−56.895
1.00
57.17

ATOM
1227
CG
ASP

324
−1.637
104.719
−56.952
1.00
60.24

ATOM
1228
OD1
ASP

324
−0.632
104.083
−56.548
1.00
61.08

ATOM
1229
OD2
ASP

324
−1.620
105.898
−57.395
1.00
58.44

ATOM
1230
C
ASP

324
−3.854
101.701
−56.917
1.00
54.98

ATOM
1231
O
ASP

324
−3.970
101.658
−55.696
1.00
54.52

ATOM
1232
N
ASN

325
−4.612
100.984
−57.734
1.00
55.35

ATOM
1233
CA
ASN

325
−5.606
100.089
−57.166
1.00
55.66

ATOM
1234
CB
ASN

325
−4.882
99.039
−56.340
1.00
55.33

ATOM
1235
CG
ASN

325
−5.795
97.986
−55.834
1.00
57.26

ATOM
1236
OD1
ASN

325
−6.543
97.380
−56.608
1.00
56.07

ATOM
1237
ND2
ASN

325
−5.749
97.741
−54.526
1.00
58.55

ATOM
1238
C
ASN

325
−6.530
100.918
−56.265
1.00
55.25

ATOM
1239
O
ASN

325
−6.901
100.502
−55.172
1.00
53.76

ATOM
1240
N
ASP

326
−6.896
102.096
−56.752
1.00
56.48

ATOM
1241
CA
ASP

326
−7.726
103.040
−56.007
1.00
57.01

ATOM
1242
CB
ASP

326
−7.046
104.412
−56.046
1.00
60.51

ATOM
1243
CG
ASP

326
−7.879
105.494
−55.403
1.00
64.02

ATOM
1244
OD1
ASP

326
−7.706
106.683
−55.764
1.00
64.46

ATOM
1245
OD2
ASP

326
−8.699
105.150
−54.529
1.00
66.73

ATOM
1246
C
ASP

326
−9.165
103.162
−56.525
1.00
54.60

ATOM
1247
O
ASP

326
−9.460
103.977
−57.398
1.00
54.57

ATOM
1248
N
TYR

327
−10.057
102.355
−55.969
1.00
51.99

ATOM
1249
CA
TYR

327
−11.453
102.376
−56.364
1.00
50.16

ATOM
1250
CB
TYR

327
−12.096
101.007
−56.168
1.00
49.27

ATOM
1251
CG
TYR

327
−11.586
99.951
−57.109
1.00
50.05

ATOM
1252
CD1
TYR

327
−10.366
99.315
−56.879
1.00
48.99

ATOM
1253
CE1
TYR

327
−9.893
98.360
−57.746
1.00
48.59

ATOM
1254
CD2
TYR

327
−12.313
99.597
−58.240
1.00
48.52

ATOM
1255
CE2
TYR

327
−11.842
98.640
−59.124
1.00
49.50

ATOM
1256
CZ
TYR

327
−10.630
98.025
−58.872
1.00
50.76

ATOM
1257
OH
TYR

327
−10.140
97.087
−59.766
1.00
51.99

ATOM
1258
C
TYR

327
−12.272
103.408
−55.598
1.00
49.40

ATOM
1259
O
TYR

327
−13.166
103.053
−54.833
1.00
50.18

ATOM
1260
N
GLY

328
−11.956
104.679
−55.813
1.00
48.90

ATOM
1261
CA
GLY

328
−12.686
105.757
−55.186
1.00
46.25

ATOM
1262
C
GLY

328
−13.806
106.160
−56.126
1.00
46.83

ATOM
1263
O
GLY

328
−13.874
105.679
−57.272
1.00
47.34

ATOM
1264
N
ARG

329
−14.669
107.048
−55.651
1.00
45.65

ATOM
1265
CA
ARG

329
−15.816
107.525
−56.407
1.00
44.38

ATOM
1266
CB
ARG

329
−16.361
108.810
−55.785
1.00
44.43

ATOM
1267
CG
ARG

329
−16.333
108.891
−54.284
1.00
49.59

ATOM
1268
CD
ARG

329
−16.128
110.355
−53.849
1.00
51.17

ATOM
1269
NE
ARG

329
−16.659
111.214
−54.890
1.00
51.31

ATOM
1270
CZ
ARG

329
−16.190
112.410
−55.212
1.00
52.20

ATOM
1271
NH1
ARG

329
−15.166
112.936
−54.555
1.00
48.17

ATOM
1272
NH2
ARG

329
−16.720
113.044
−56.257
1.00
53.25

ATOM
1273
C
ARG

329
−15.542
107.822
−57.872
1.00
42.12

ATOM
1274
O
ARG

329
−16.340
107.523
−58.743
1.00
43.69

ATOM
1275
N
ALA

330
−14.426
108.462
−58.144
1.00
42.72

ATOM
1276
CA
ALA

330
−14.101
108.829
−59.507
1.00
43.00

ATOM
1277
CB
ALA

330
−12.729
109.445
−59.541
1.00
43.84

ATOM
1278
C
ALA

330
−14.192
107.714
−60.542
1.00
42.15

ATOM
1279
O
ALA

330
−14.655
107.948
−61.654
1.00
44.24

ATOM
1280
N
VAL

331
−13.765
106.507
−60.197
1.00
40.09

ATOM
1281
CA
VAL

331
−13.799
105.438
−61.188
1.00
40.14

ATOM
1282
CB
VAL

331
−13.295
104.083
−60.599
1.00
39.98

ATOM
1283
CG1
VAL

331
−11.942
104.288
−59.892
1.00
36.42

ATOM
1284
CG2
VAL

331
−14.339
103.500
−59.661
1.00
37.20

ATOM
1285
C
VAL

331
−15.170
105.233
−61.816
1.00
40.34

ATOM
1286
O
VAL

331
−15.285
104.727
−62.937
1.00
43.22

ATOM
1287
N
ASP

332
−16.219
105.622
−61.104
1.00
38.59

ATOM
1288
CA
ASP

332
−17.553
105.469
−61.648
1.00
35.94

ATOM
1289
CB
ASP

332
−18.621
105.649
−60.545
1.00
37.31

ATOM
1290
CG
ASP

332
−18.774
104.413
−59.649
1.00
39.08

ATOM
1291
OD1
ASP

332
−18.465
103.304
−60.134
1.00
39.92

ATOM
1292
OD2
ASP

332
−19.223
104.535
−58.477
1.00
38.85

ATOM
1293
C
ASP

332
−17.770
106.473
−62.757
1.00
30.82

ATOM
1294
O
ASP

332
−18.439
106.181
−63.748
1.00
31.25

ATOM
1295
N
TRP

333
−17.223
107.668
−62.587
1.00
31.26

ATOM
1296
CA
TRP

333
−17.379
108.720
−63.594
1.00
33.91

ATOM
1297
CB
TRP

333
−16.964
110.096
−63.015
1.00
35.02

ATOM
1298
CG
TRP

333
−17.919
110.550
−61.926
1.00
32.79

ATOM
1299
CD2
TRP

333
−19.351
110.529
−61.991
1.00
30.04

ATOM
1300
CE2
TRP

333
−19.830
110.827
−60.706
1.00
31.33

ATOM
1301
CE3
TRP

333
−20.276
110.268
−63.013
1.00
28.23

ATOM
1302
CD1
TRP

333
−17.601
110.871
−60.647
1.00
33.52

ATOM
1303
NE1
TRP

333
−18.739
111.038
−59.904
1.00
34.35

ATOM
1304
CZ2
TRP

333
−21.202
110.864
−60.402
1.00
27.84

ATOM
1305
CZ3
TRP

333
−21.635
110.306
−62.709
1.00
28.48

ATOM
1306
CH2
TRP

333
−22.080
110.599
−61.408
1.00
23.78

ATOM
1307
C
TRP

333
−16.542
108.336
−64.808
1.00
35.02

ATOM
1308
O
TRP

333
−16.960
108.555
−65.942
1.00
35.03

ATOM
1309
N
TRP

334
−15.378
107.731
−64.562
1.00
36.30

ATOM
1310
CA
TRP

334
−14.524
107.258
−65.646
1.00
35.62

ATOM
1311
CB
TRP

334
−13.216
106.715
−65.052
1.00
37.90

ATOM
1312
CG
TRP

334
−12.411
105.806
−65.990
1.00
43.98

ATOM
1313
CD2
TRP

334
−11.457
106.215
−66.977
1.00
43.83

ATOM
1314
CE2
TRP

334
−11.017
105.048
−67.644
1.00
44.87

ATOM
1315
CE3
TRP

334
−10.930
107.454
−67.365
1.00
45.29

ATOM
1316
CD1
TRP

334
−12.504
104.447
−66.094
1.00
42.68

ATOM
1317
NE1
TRP

334
−11.672
103.987
−67.083
1.00
44.91

ATOM
1318
CZ2
TRP

334
−10.081
105.080
−68.683
1.00
42.82

ATOM
1319
CZ3
TRP

334
−9.984
107.487
−68.416
1.00
45.27

ATOM
1320
CH2
TRP

334
−9.579
106.306
−69.054
1.00
42.67

ATOM
1321
C
TRP

334
−15.326
106.183
−66.396
1.00
34.52

ATOM
1322
O
TRP

334
−15.389
106.158
−67.631
1.00
37.86

ATOM
1323
N
GLY

335
−15.995
105.316
−65.655
1.00
31.85

ATOM
1324
CA
GLY

335
−16.782
104.301
−66.311
1.00
30.60

ATOM
1325
C
GLY

335
−17.915
104.888
−67.118
1.00
33.86

ATOM
1326
O
GLY

335
−18.303
104.347
−68.171
1.00
34.29

ATOM
1327
N
LEU

336
−18.482
105.984
−66.618
1.00
34.61

ATOM
1328
CA
LEU

336
−19.583
106.641
−67.321
1.00
34.46

ATOM
1329
CB
LEU

336
−20.166
107.826
−66.504
1.00
31.10

ATOM
1330
CG
LEU

336
−21.191
108.610
−67.333
1.00
30.58

ATOM
1331
CD1
LEU

336
−22.347
107.686
−67.703
1.00
28.91

ATOM
1332
CD2
LEU

336
−21.704
109.809
−66.564
1.00
31.32

ATOM
1333
C
LEU

336
−19.059
107.163
−68.657
1.00
33.73

ATOM
1334
O
LEU

336
−19.701
106.989
−69.699
1.00
33.15

ATOM
1335
N
GLY

337
−17.896
107.805
−68.618
1.00
32.09

ATOM
1336
CA
GLY

337
−17.323
108.318
−69.849
1.00
35.61

ATOM
1337
C
GLY

337
−17.013
107.276
−70.923
1.00
36.20

ATOM
1338
O
GLY

337
−17.314
107.484
−72.109
1.00
35.81

ATOM
1339
N
VAL

338
−16.406
106.162
−70.518
1.00
35.93

ATOM
1340
CA
VAL

338
−16.096
105.084
−71.457
1.00
34.99

ATOM
1341
CB
VAL

338
−15.373
103.917
−70.744
1.00
35.15

ATOM
1342
CG1
VAL

338
−15.287
102.716
−71.696
1.00
35.32

ATOM
1343
CG2
VAL

338
−14.010
104.370
−70.249
1.00
29.80

ATOM
1344
C
VAL

338
−17.391
104.542
−72.064
1.00
36.10

ATOM
1345
O
VAL

338
−17.439
104.198
−73.221
1.00
35.73

ATOM
1346
N
VAL

339
−18.448
104.475
−71.269
1.00
37.38

ATOM
1347
CA
VAL

339
−19.725
103.983
−71.761
1.00
38.24

ATOM
1348
CB
VAL

339
−20.707
103.767
−70.600
1.00
38.51

ATOM
1349
CG1
VAL

339
−22.118
103.527
−71.141
1.00
39.32

ATOM
1350
CG2
VAL

339
−20.242
102.629
−69.746
1.00
36.32

ATOM
1351
C
VAL

339
−20.389
104.935
−72.769
1.00
41.68

ATOM
1352
O
VAL

339
−20.982
104.496
−73.753
1.00
42.94

ATOM
1353
N
MET

340
−20.337
106.235
−72.526
1.00
43.29

ATOM
1354
CA
MET

340
−20.954
107.139
−73.488
1.00
47.13

ATOM
1355
CB
MET

340
−21.355
108.429
−72.808
1.00
47.27

ATOM
1356
CG
MET

340
−22.494
108.158
−71.888
1.00
50.00

ATOM
1357
SD
MET

340
−22.930
109.585
−70.972
1.00
58.78

ATOM
1358
CE
MET

340
−21.327
110.067
−70.266
1.00
57.23

ATOM
1359
C
MET

340
−20.068
107.395
−74.697
1.00
47.39

ATOM
1360
O
MET

340
−20.570
107.714
−75.776
1.00
48.38

ATOM
1361
N
TYR

341
−18.756
107.261
−74.518
1.00
47.83

ATOM
1362
CA
TYR

341
−17.820
107.397
−75.638
1.00
47.94

ATOM
1363
CB
TYR

341
−16.381
107.168
−75.175
1.00
48.36

ATOM
1364
CG
TYR

341
−15.347
107.294
−76.274
1.00
50.05

ATOM
1365
CD1
TYR

341
−15.342
106.428
−77.376
1.00
50.85

ATOM
1366
CE1
TYR

341
−14.383
106.550
−78.390
1.00
49.93

ATOM
1367
CD2
TYR

341
−14.364
108.277
−76.209
1.00
50.28

ATOM
1368
CE2
TYR

341
−13.400
108.407
−77.201
1.00
49.75

ATOM
1369
CZ
TYR

341
−13.418
107.547
−78.289
1.00
50.14

ATOM
1370
OH
TYR

341
−12.481
107.722
−79.273
1.00
49.73

ATOM
1371
C
TYR

341
−18.185
106.302
−76.645
1.00
47.92

ATOM
1372
O
TYR

341
−18.215
106.543
−77.850
1.00
47.96

ATOM
1373
N
GLU

342
−18.501
105.104
−76.155
1.00
46.58

ATOM
1374
CA
GLU

342
−18.839
104.033
−77.068
1.00
46.00

ATOM
1375
CB
GLU

342
−18.758
102.660
−76.376
1.00
47.87

ATOM
1376
CG
GLU

342
−18.397
101.539
−77.352
1.00
48.85

ATOM
1377
CD
GLU

342
−18.527
100.096
−76.802
1.00
51.28

ATOM
1378
OE1
GLU

342
−18.160
99.817
−75.632
1.00
49.65

ATOM
1379
OE2
GLU

342
−18.984
99.223
−77.578
1.00
50.90

ATOM
1380
C
GLU

342
−20.210
104.220
−77.677
1.00
45.28

ATOM
1381
O
GLU

342
−20.423
103.854
−78.828
1.00
46.44

ATOM
1382
N
MET

343
−21.151
104.768
−76.915
1.00
45.59

ATOM
1383
CA
MET

343
−22.521
104.990
−77.419
1.00
45.57

ATOM
1384
CB
MET

343
−23.434
105.507
−76.317
1.00
45.82

ATOM
1385
CG
MET

343
−23.647
104.552
−75.212
1.00
46.42

ATOM
1386
SD
MET

343
−24.664
105.261
−73.950
1.00
42.59

ATOM
1387
CE
MET

343
−26.008
104.169
−74.111
1.00
42.20

ATOM
1388
C
MET

343
−22.575
106.009
−78.527
1.00
46.54

ATOM
1389
O
MET

343
−23.347
105.874
−79.470
1.00
46.11

ATOM
1390
N
MET

344
−21.766
107.048
−78.379
1.00
48.19

ATOM
1391
CA
MET

344
−21.725
108.124
−79.337
1.00
52.87

ATOM
1392
CB
MET

344
−21.468
109.441
−78.583
1.00
54.70

ATOM
1393
CG
MET

344
−22.732
109.950
−77.819
1.00
53.79

ATOM
1394
SD
MET

344
−22.469
111.313
−76.629
1.00
53.65

ATOM
1395
CE
MET

344
−20.927
111.957
−77.209
1.00
55.26

ATOM
1396
C
MET

344
−20.741
107.922
−80.496
1.00
55.14

ATOM
1397
O
MET

344
−20.982
108.421
−81.585
1.00
56.82

ATOM
1398
C
CYS

345
−19.659
107.172
−80.278
1.00
56.22

ATOM
1399
CA
CYS

345
−18.664
106.907
−81.327
1.00
54.43

ATOM
1400
CB
CYS

345
−17.266
107.057
−80.757
1.00
53.88

ATOM
1401
SG
CYS

345
−17.096
108.616
−79.854
1.00
55.65

ATOM
1402
C
CYS

345
−18.832
105.520
−81.967
1.00
53.79

ATOM
1403
O
CYS

345
−18.521
105.334
−83.139
1.00
54.14

ATOM
1404
N
GLY

346
−19.345
104.561
−81.202
1.00
53.60

ATOM
1405
CA
GLY

346
−19.583
103.221
−81.724
1.00
53.07

ATOM
1406
C
GLY

346
−18.442
102.236
−81.509
1.00
54.24

ATOM
1407
O
GLY

346
−18.529
101.072
−81.904
1.00
54.77

ATOM
1408
N
ARG

347
−17.385
102.695
−80.856
1.00
52.18

ATOM
1409
CA
ARG

347
−16.216
101.882
−80.625
1.00
52.52

ATOM
1410
CB
ARG

347
−15.282
102.036
−81.825
1.00
53.58

ATOM
1411
CG
ARG

347
−14.898
103.488
−82.028
1.00
56.50

ATOM
1412
CD
ARG

347
−13.855
103.693
−83.108
1.00
60.38

ATOM
1413
NE
ARG

347
−13.384
105.084
−83.188
1.00
62.75

ATOM
1414
CZ
ARG

347
−14.052
106.088
−83.761
1.00
63.87

ATOM
1415
NH1
ARG

347
−15.241
105.875
−84.321
1.00
62.78

ATOM
1416
NH2
ARG

347
−13.525
107.312
−83.780
1.00
64.47

ATOM
1417
C
ARG

347
−15.537
102.435
−79.380
1.00
51.29

ATOM
1418
O
ARG

347
−15.779
103.588
−79.017
1.00
52.32

ATOM
1419
N
LEU

348
−14.688
101.628
−78.738
1.00
48.98

ATOM
1420
CA
LEU

348
−13.954
102.064
−77.550
1.00
46.80

ATOM
1421
CB
LEU

348
−13.391
100.855
−76.797
1.00
42.70

ATOM
1422
CG
LEU

348
−14.472
100.098
−76.001
1.00
41.56

ATOM
1423
CD1
LEU

348
−14.061
98.674
−75.719
1.00
40.62

ATOM
1424
CD2
LEU

348
−14.727
100.812
−74.690
1.00
41.06

ATOM
1425
C
LEU

348
−12.857
103.047
−77.964
1.00
47.61

ATOM
1426
O
LEU

348
−12.566
103.186
−79.139
1.00
51.11

ATOM
1427
N
PRO

349
−12.245
103.757
−77.013
1.00
47.51

ATOM
1428
CD
PRO

349
−12.581
103.882
−75.592
1.00
46.67

ATOM
1429
CA
PRO

349
−11.205
104.716
−77.385
1.00
47.57

ATOM
1430
CB
PRO

349
−10.901
105.436
−76.075
1.00
47.25

ATOM
1431
CG
PRO

349
−11.319
104.493
−75.056
1.00
47.82

ATOM
1432
C
PRO

349
−9.953
104.221
−78.060
1.00
51.21

ATOM
1433
O
PRO

349
−9.329
104.949
−78.826
1.00
50.75

ATOM
1434
N
PHE

350
−9.557
102.996
−77.770
1.00
53.02

ATOM
1435
CA
PHE

350
−8.355
102.466
−78.390
1.00
54.38

ATOM
1436
CB
PHE

350
−7.325
102.172
−77.304
1.00
50.15

ATOM
1437
CG
PHE

350
−7.020
103.350
−76.425
1.00
46.03

ATOM
1438
CD1
PHE

350
−7.210
103.274
−75.047
1.00
43.07

ATOM
1439
CD2
PHE

350
−6.464
104.505
−76.960
1.00
43.87

ATOM
1440
CE1
PHE

350
−6.845
104.319
−74.210
1.00
38.42

ATOM
1441
CE2
PHE

350
−6.095
105.553
−76.140
1.00
38.64

ATOM
1442
CZ
PHE

350
−6.282
105.460
−74.754
1.00
41.34

ATOM
1443
C
PHE

350
−8.726
101.197
−79.144
1.00
57.61

ATOM
1444
O
PHE

350
−7.941
100.259
−79.232
1.00
57.75

ATOM
1445
N
TYR

351
−9.934
101.191
−79.697
1.00
62.81

ATOM
1446
CA
TYR

351
−10.468
100.028
−80.396
1.00
67.96

ATOM
1447
CB
TYR

351
−11.808
100.368
−81.052
1.00
69.37

ATOM
1448
CG
TYR

351
−11.685
100.990
−82.423
1.00
72.39

ATOM
1449
CD1
TYR

351
−12.414
100.479
−83.504
1.00
73.37

ATOM
1450
CE1
TYR

351
−12.300
101.034
−84.777
1.00
74.61

ATOM
1451
CD2
TYR

351
−10.836
102.081
−82.650
1.00
72.88

ATOM
1452
CE2
TYR

351
−10.717
102.647
−83.922
1.00
73.95

ATOM
1453
CZ
TYR

351
−11.454
102.118
−84.979
1.00
74.79

ATOM
1454
OH
TYR

351
−11.372
102.676
−86.238
1.00
76.57

ATOM
1455
C
TYR

351
−9.544
99.404
−81.433
1.00
70.44

ATOM
1456
O
TYR

351
−9.595
98.196
−81.655
1.00
71.41

ATOM
1457
N
ASN

352
−8.718
100.208
−82.087
1.00
72.22

ATOM
1458
CA
ASN

352
−7.815
99.638
−83.071
1.00
76.18

ATOM
1459
CB
ASN

352
−7.629
100.581
−84.268
1.00
77.45

ATOM
1460
CG
ASN

352
−7.433
102.021
−83.857
1.00
79.51

ATOM
1461
OD1
ASN

352
−7.062
102.863
−84.678
1.00
80.45

ATOM
1462
ND2
ASN

352
−7.687
102.320
−82.585
1.00
80.65

ATOM
1463
C
ASN

352
−6.466
99.289
−82.449
1.00
77.72

ATOM
1464
O
ASN

352
−6.016
98.146
−82.564
1.00
79.04

ATOM
1465
N
GLN

353
−5.837
100.251
−81.773
1.00
78.39

ATOM
1466
CA
GLN

353
−4.542
100.018
−81.150
1.00
79.59

ATOM
1467
CB
GLN

353
−4.189
101.156
−80.209
1.00
79.95

ATOM
1468
CG
GLN

353
−3.895
102.458
−80.902
1.00
82.10

ATOM
1469
CD
GLN

353
−2.971
103.349
−80.082
1.00
84.82

ATOM
1470
OE1
GLN

353
−1.763
103.100
−79.991
1.00
84.86

ATOM
1471
NE2
GLN

353
−3.537
104.389
−79.470
1.00
85.81

ATOM
1472
C
GLN

353
−4.460
98.699
−80.395
1.00
81.13

ATOM
1473
O
GLN

353
−4.997
98.564
−79.301
1.00
82.46

ATOM
1474
N
ASP

354
−3.764
97.740
−80.996
1.00
82.13

ATOM
1475
CA
ASP

354
−3.569
96.402
−80.449
1.00
83.41

ATOM
1476
CB
ASP

354
−2.105
96.210
−80.042
1.00
85.22

ATOM
1477
CG
ASP

354
−1.671
94.748
−80.088
1.00
86.43

ATOM
1478
OD1
ASP

354
−2.390
93.884
−79.525
1.00
87.08

ATOM
1479
OD2
ASP

354
−0.606
94.467
−80.686
1.00
86.75

ATOM
1480
C
ASP

354
−4.483
96.079
−79.273
1.00
83.06

ATOM
1481
O
ASP

354
−5.701
96.095
−79.417
1.00
83.88

ATOM
1482
N
HIS

355
−3.905
95.786
−78.112
1.00
82.18

ATOM
1483
CA
HIS

355
−4.711
95.460
−76.950
1.00
81.42

ATOM
1484
CB
HIS

355
−5.566
94.239
−77.230
1.00
83.37

ATOM
1485
CG
HIS

355
−6.197
93.675
−76.003
1.00
86.62

ATOM
1486
CD2
HIS

355
−6.418
92.398
−75.613
1.00
88.45

ATOM
1487
ND1
HIS

355
−6.672
94.474
−74.985
1.00
88.33

ATOM
1488
CE1
HIS

355
−7.155
93.714
−74.019
1.00
89.36

ATOM
1489
NE2
HIS

355
−7.014
92.449
−74.375
1.00
89.98

ATOM
1490
C
HIS

355
−3.936
95.230
−75.662
1.00
80.28

ATOM
1491
O
HIS

355
−4.452
95.461
−74.570
1.00
79.78

ATOM
1492
N
GLU

356
−2.710
94.741
−75.774
1.00
78.69

ATOM
1493
CA
GLU

356
−1.894
94.533
−74.589
1.00
77.64

ATOM
1494
CB
GLU

356
−0.815
93.496
−74.868
1.00
81.61

ATOM
1495
CG
GLU

356
−1.343
92.213
−75.448
1.00
84.72

ATOM
1496
CD
GLU

356
−0.260
91.445
−76.163
1.00
87.70

ATOM
1497
OE1
GLU

356
0.395
92.041
−77.054
1.00
89.08

ATOM
1498
OE2
GLU

356
−0.061
90.253
−75.840
1.00
89.45

ATOM
1499
C
GLU

356
−1.251
95.882
−74.289
1.00
75.04

ATOM
1500
O
GLU

356
−0.439
96.019
−73.374
1.00
73.95

ATOM
1501
N
ARG

357
−1.633
96.869
−75.095
1.00
72.08

ATOM
1502
CA
ARG

357
−1.153
98.231
−74.972
1.00
69.60

ATOM
1503
CB
ARG

357
−1.078
98.867
−76.353
1.00
71.43

ATOM
1504
CG
ARG

357
0.094
98.346
−77.125
1.00
76.13

ATOM
1505
CD
ARG

357
0.055
98.637
−78.604
1.00
78.63

ATOM
1506
NE
ARG

357
1.141
97.902
−79.249
1.00
80.96

ATOM
1507
CZ
ARG

357
1.347
97.865
−80.557
1.00
82.63

ATOM
1508
NH1
ARG

357
0.533
98.534
−81.368
1.00
82.83

ATOM
1509
NH2
ARG

357
2.354
97.148
−81.049
1.00
82.20

ATOM
1510
C
ARG

357
−2.058
99.052
−74.078
1.00
66.85

ATOM
1511
O
ARG

357
−1.690
100.143
−73.632
1.00
66.26

ATOM
1512
N
LEU

358
−3.240
98.510
−73.806
1.00
63.02

ATOM
1513
CA
LEU

358
−4.222
99.197
−72.983
1.00
59.37

ATOM
1514
CB
LEU

358
−5.409
98.291
−72.688
1.00
58.41

ATOM
1515
CG
LEU

358
−6.414
98.354
−73.833
1.00
57.85

ATOM
1516
CD1
LEU

358
−7.578
97.420
−73.549
1.00
56.87

ATOM
1517
CD2
LEU

358
−6.885
99.795
−74.004
1.00
55.74

ATOM
1518
C
LEU

358
−3.682
99.746
−71.698
1.00
57.04

ATOM
1519
O
LEU

358
−4.055
100.839
−71.308
1.00
55.89

ATOM
1520
N
PHE

359
−2.798
99.005
−71.043
1.00
55.87

ATOM
1521
CA
PHE

359
−2.240
99.479
−69.785
1.00
55.06

ATOM
1522
CB
PHE

359
−1.221
98.495
−69.214
1.00
51.89

ATOM
1523
CG
PHE

359
−0.671
98.915
−67.881
1.00
51.13

ATOM
1524
CD1
PHE

359
−1.391
98.693
−66.715
1.00
48.78

ATOM
1525
CD2
PHE

359
0.553
99.567
−67.797
1.00
51.18

ATOM
1526
CE1
PHE

359
−0.902
99.114
−65.483
1.00
50.68

ATOM
1527
CE2
PHE

359
1.055
99.993
−66.572
1.00
50.67

ATOM
1528
CZ
PHE

359
0.327
99.769
−65.409
1.00
51.77

ATOM
1529
C
PHE

359
−1.578
100.842
−69.959
1.00
55.16

ATOM
1530
O
PHE

359
−1.881
101.776
−69.205
1.00
57.22

ATOM
1531
N
GLU

360
−0.696
100.963
−70.951
1.00
53.44

ATOM
1532
CA
GLU

360
−0.001
102.229
−71.182
1.00
53.14

ATOM
1533
CB
GLU

360
1.252
102.050
−72.046
1.00
54.80

ATOM
1534
CG
GLU

360
2.070
100.799
−71.810
1.00
58.70

ATOM
1535
CD
GLU

360
1.473
99.577
−72.494
1.00
58.32

ATOM
1536
OE1
GLU

360
0.856
98.753
−71.790
1.00
57.65

ATOM
1537
OE2
GLU

360
1.617
99.451
−73.733
1.00
58.10

ATOM
1538
C
GLU

360
−0.872
103.280
−71.863
1.00
51.75

ATOM
1539
O
GLU

360
−0.661
104.478
−71.680
1.00
50.13

ATOM
1540
N
LEU

361
−1.825
102.835
−72.673
1.00
50.27

ATOM
1541
CA
LEU

361
−2.686
103.771
−73.365
1.00
50.68

ATOM
1542
CB
LEU

361
−3.478
103.054
−74.461
1.00
50.12

ATOM
1543
CG
LEU

361
−2.623
102.536
−75.628
1.00
51.08

ATOM
1544
CD1
LEU

361
−3.549
101.911
−76.651
1.00
49.83

ATOM
1545
CD2
LEU

361
−1.803
103.687
−76.275
1.00
48.70

ATOM
1546
C
LEU

361
−3.622
104.481
−72.379
1.00
50.93

ATOM
1547
O
LEU

361
−3.717
105.709
−72.374
1.00
52.21

ATOM
1548
N
ILE

362
−4.293
103.706
−71.537
1.00
49.07

ATOM
1549
CA
ILE

362
−5.197
104.262
−70.551
1.00
47.02

ATOM
1550
CB
ILE

362
−5.867
103.135
−69.731
1.00
45.45

ATOM
1551
CG2
ILE

362
−6.513
103.702
−68.460
1.00
42.01

ATOM
1552
CG1
ILE

362
−6.873
102.400
−70.623
1.00
41.50

ATOM
1553
CD1
ILE

362
−7.453
101.158
−69.981
1.00
41.44

ATOM
1554
C
ILE

362
−4.432
105.185
−69.625
1.00
47.66

ATOM
1555
O
ILE

362
−4.887
106.285
−69.293
1.00
48.84

ATOM
1556
N
LEU

363
−3.250
104.754
−69.218
1.00
46.30

ATOM
1557
CA
LEU

363
−2.485
105.578
−68.326
1.00
46.39

ATOM
1558
CB
LEU

363
−1.436
104.750
−67.618
1.00
46.12

ATOM
1559
CG
LEU

363
−2.077
103.829
−66.591
1.00
48.62

ATOM
1560
CD1
LEU

363
−1.044
102.819
−66.105
1.00
47.35

ATOM
1561
CD2
LEU

363
−2.668
104.685
−65.435
1.00
45.18

ATOM
1562
C
LEU

363
−1.822
106.773
−68.952
1.00
47.90

ATOM
1563
O
LEU

363
−1.711
107.804
−68.299
1.00
50.11

ATOM
1564
N
MET

364
−1.396
106.674
−70.206
1.00
48.50

ATOM
1565
CA
MET

364
−0.676
107.800
−70.782
1.00
50.98

ATOM
1566
CB
MET

364
0.834
107.530
−70.714
1.00
50.87

ATOM
1567
CG
MET

364
1.317
107.145
−69.322
1.00
53.98

ATOM
1568
SD
MET

364
3.045
106.570
−69.216
1.00
59.08

ATOM
1569
CE
MET

364
2.882
104.919
−69.800
1.00
56.15

ATOM
1570
C
MET

364
−1.036
108.234
−72.179
1.00
52.24

ATOM
1571
O
MET

364
−0.392
109.111
−72.721
1.00
53.82

ATOM
1572
N
GLU

365
−2.055
107.643
−72.770
1.00
53.37

ATOM
1573
CA
GLU

365
−2.422
108.045
−74.115
1.00
57.40

ATOM
1574
CB
GLU

365
−2.799
106.818
−74.933
1.00
60.60

ATOM
1575
CG
GLU

365
−3.279
107.139
−76.310
1.00
64.02

ATOM
1576
CD
GLU

365
−2.184
107.689
−77.168
1.00
68.42

ATOM
1577
OE1
GLU

365
−1.590
108.721
−76.783
1.00
70.32

ATOM
1578
OE2
GLU

365
−1.918
107.084
−78.232
1.00
72.08

ATOM
1579
C
GLU

365
−3.590
109.021
−74.096
1.00
58.80

ATOM
1580
O
GLU

365
−4.532
108.851
−73.331
1.00
56.60

ATOM
1581
N
GLU

366
−3.543
110.043
−74.942
1.00
60.64

ATOM
1582
CA
GLU

366
−4.634
110.997
−74.967
1.00
61.98

ATOM
1583
CB
GLU

366
−4.179
112.310
−75.567
1.00
65.32

ATOM
1584
CG
GLU

366
−3.699
112.176
−76.996
1.00
71.72

ATOM
1585
CD
GLU

366
−3.615
113.524
−77.709
1.00
75.29

ATOM
1586
OE1
GLU

366
−4.674
114.200
−77.851
1.00
75.91

ATOM
1587
OE2
GLU

366
−2.488
113.903
−78.118
1.00
76.74

ATOM
1588
C
GLU

366
−5.771
110.435
−75.796
1.00
60.77

ATOM
1589
O
GLU

366
−5.580
110.022
−76.938
1.00
61.00

ATOM
1590
N
ILE

367
−6.960
110.402
−75.220
1.00
58.76

ATOM
1591
CA
ILE

367
−8.088
109.891
−75.959
1.00
58.98

ATOM
1592
CB
ILE

367
−9.241
109.558
−75.025
1.00
56.06

ATOM
1593
CG2
ILE

367
−10.427
109.109
−75.822
1.00
53.24

ATOM
1594
CG1
ILE

367
−8.795
108.470
−74.037
1.00
55.06

ATOM
1595
CD1
ILE

367
−9.794
108.162
−72.932
1.00
52.27

ATOM
1596
C
ILE

367
−8.508
110.950
−76.971
1.00
61.65

ATOM
1597
O
ILE

367
−8.640
112.130
−76.635
1.00
64.27

ATOM
1598
N
ARG

368
−8.705
110.516
−78.212
1.00
63.12

ATOM
1599
CA
ARG

368
−9.096
111.383
−79.312
1.00
64.31

ATOM
1600
CB
ARG

368
−8.247
111.044
−80.553
1.00
68.59

ATOM
1601
CG
ARG

368
−8.693
111.737
−81.842
1.00
76.42

ATOM
1602
CD
ARG

368
−7.540
112.463
−82.591
1.00
82.03

ATOM
1603
NE
ARG

368
−6.996
113.629
−81.879
1.00
85.84

ATOM
1604
CZ
ARG

368
−6.175
114.527
−82.427
1.00
87.53

ATOM
1605
NH1
ARG

368
−5.802
114.405
−83.699
1.00
88.04

ATOM
1606
NH2
ARG

368
−5.715
115.542
−81.703
1.00
87.35

ATOM
1607
C
ARG

368
−10.587
111.204
−79.603
1.00
63.44

ATOM
1608
O
ARG

368
−11.112
110.099
−79.493
1.00
63.88

ATOM
1609
N
PHE

369
−11.266
112.284
−79.987
1.00
61.31

ATOM
1610
CA
PHE

369
−12.700
112.224
−80.247
1.00
59.41

ATOM
1611
CB
PHE

369
−13.449
113.249
−79.380
1.00
58.28

ATOM
1612
CG
PHE

369
−13.006
113.275
−77.944
1.00
54.21

ATOM
1613
CD1
PHE

369
−13.448
112.310
−77.046
1.00
52.84

ATOM
1614
CD2
PHE

369
−12.102
114.232
−77.506
1.00
53.02

ATOM
1615
CE1
PHE

369
−12.996
112.295
−75.742
1.00
49.33

ATOM
1616
CE2
PHE

369
−11.641
114.223
−76.203
1.00
51.92

ATOM
1617
CZ
PHE

369
−12.091
113.248
−75.316
1.00
49.73

ATOM
1618
C
PHE

369
−13.056
112.503
−81.684
1.00
58.66

ATOM
1619
O
PHE

369
−12.484
113.378
−82.314
1.00
58.34

ATOM
1620
N
PRO

370
−14.018
111.765
−82.221
1.00
58.55

ATOM
1621
CD
PRO

370
−14.726
110.621
−81.635
1.00
58.83

ATOM
1622
CA
PRO

370
−14.425
111.988
−83.606
1.00
61.42

ATOM
1623
CB
PRO

370
−15.632
111.076
−83.752
1.00
60.56

ATOM
1624
CG
PRO

370
−15.276
109.935
−82.848
1.00
60.53

ATOM
1625
C
PRO

370
−14.772
113.467
−83.807
1.00
63.94

ATOM
1626
O
PRO

370
−15.074
114.171
−82.841
1.00
65.21

ATOM
1627
N
ARG

371
−14.730
113.934
−85.054
1.00
66.21

ATOM
1628
CA
ARG

371
−15.027
115.334
−85.362
1.00
66.42

ATOM
1629
CB
ARG

371
−14.433
115.724
−86.720
1.00
69.22

ATOM
1630
CG
ARG

371
−12.920
115.489
−86.879
1.00
72.19

ATOM
1631
CD
ARG

371
−12.432
115.882
−88.296
1.00
74.81

ATOM
1632
NE
ARG

371
−13.090
115.121
−89.369
1.00
76.73

ATOM
1633
CZ
ARG

371
−12.692
113.928
−89.811
1.00
78.18

ATOM
1634
NH1
ARG

371
−11.621
113.336
−89.287
1.00
78.15

ATOM
1635
NH2
ARG

371
−13.377
113.318
−90.772
1.00
78.08

ATOM
1636
C
ARG

371
−16.529
115.571
−85.400
1.00
65.40

ATOM
1637
O
ARG

371
−17.004
116.656
−85.084
1.00
65.17

ATOM
1638
N
THR

372
−17.265
114.540
−85.780
1.00
64.11

ATOM
1639
CA
THR

372
−18.718
114.599
−85.891
1.00
64.88

ATOM
1640
CB
THR

372
−19.194
113.370
−86.716
1.00
65.04

ATOM
1641
OG1
THR

372
−20.506
113.612
−87.236
1.00
68.26

ATOM
1642
CG2
THR

372
−19.199
112.106
−85.863
1.00
63.65

ATOM
1643
C
THR

372
−19.466
114.661
−84.531
1.00
65.27

ATOM
1644
O
THR

372
−20.667
114.390
−84.442
1.00
64.03

ATOM
1645
N
LEU

373
−18.754
115.036
−83.473
1.00
66.41

ATOM
1646
CA
LEU

373
−19.341
115.107
−82.135
1.00
65.61

ATOM
1647
CB
LEU

373
−18.399
114.482
−81.108
1.00
64.92

ATOM
1648
CG
LEU

373
−18.850
113.336
−80.194
1.00
64.67

ATOM
1649
CD1
LEU

373
−19.581
112.265
−80.975
1.00
63.41

ATOM
1650
CD2
LEU

373
−17.618
112.756
−79.519
1.00
63.52

ATOM
1651
C
LEU

373
−19.593
116.530
−81.724
1.00
65.19

ATOM
1652
O
LEU

373
−18.703
117.370
−81.812
1.00
63.80

ATOM
1653
N
SER

374
−20.810
116.799
−81.271
1.00
65.94

ATOM
1654
CA
SER

374
−21.147
118.132
−80.809
1.00
65.15

ATOM
1655
CB
SER

374
−22.511
118.123
−80.115
1.00
64.69

ATOM
1656
OG
SER

374
−22.419
117.514
−78.841
1.00
63.95

ATOM
1657
C
SER

374
−20.051
118.457
−79.802
1.00
63.92

ATOM
1658
O
SER

374
−19.584
117.575
−79.093
1.00
65.77

ATOM
1659
N
PRO

375
−19.624
119.720
−79.731
1.00
63.66

ATOM
1660
CD
PRO

375
−20.142
120.861
−80.505
1.00
63.53

ATOM
1661
CA
PRO

375
−18.572
120.149
−78.805
1.00
62.49

ATOM
1662
CB
PRO

375
−18.295
121.579
−79.249
1.00
62.86

ATOM
1663
CG
PRO

375
−19.645
122.031
−79.705
1.00
63.02

ATOM
1664
C
PRO

375
−18.945
120.045
−77.327
1.00
62.04

ATOM
1665
O
PRO

375
−18.074
120.040
−76.461
1.00
61.06

ATOM
1666
N
GLU

376
−20.233
119.988
−77.017
1.00
61.15

ATOM
1667
CA
GLU

376
−20.599
119.833
−75.614
1.00
61.95

ATOM
1668
CB
GLU

376
−22.081
120.133
−75.386
1.00
62.71

ATOM
1669
CG
GLU

376
−23.019
119.521
−76.405
1.00
65.90

ATOM
1670
CD
GLU

376
−23.304
120.456
−77.579
1.00
67.70

ATOM
1671
OE1
GLU

376
−22.372
121.159
−78.046
1.00
68.57

ATOM
1672
OE2
GLU

376
−24.465
120.470
−78.039
1.00
67.01

ATOM
1673
C
GLU

376
−20.287
118.372
−75.263
1.00
61.17

ATOM
1674
O
GLU

376
−19.558
118.091
−74.301
1.00
60.59

ATOM
1675
N
ALA

377
−20.830
117.456
−76.073
1.00
59.85

ATOM
1676
CA
ALA

377
−20.603
116.017
−75.905
1.00
57.71

ATOM
1677
CB
ALA

377
−21.238
115.249
−77.037
1.00
57.77

ATOM
1678
C
ALA

377
−19.106
115.764
−75.893
1.00
55.75

ATOM
1679
O
ALA

377
−18.605
114.949
−75.132
1.00
52.94

ATOM
1680
N
LYS

378
−18.387
116.480
−76.741
1.00
56.05

ATOM
1681
CA
LYS

378
−16.956
116.313
−76.767
1.00
57.51

ATOM
1682
CB
LYS

378
−16.337
117.087
−77.935
1.00
59.91

ATOM
1683
CG
LYS

378
−14.802
116.987
−77.963
1.00
63.45

ATOM
1684
CD
LYS

378
−14.169
117.946
−78.970
1.00
65.36

ATOM
1685
CE
LYS

378
−12.635
117.887
−78.920
1.00
67.38

ATOM
1686
NZ
LYS

378
−11.967
118.978
−79.722
1.00
67.76

ATOM
1687
C
LYS

378
−16.389
116.803
−75.444
1.00
55.87

ATOM
1688
O
LYS

378
−15.407
116.257
−74.937
1.00
58.72

ATOM
1689
N
SER

379
−17.009
117.822
−74.862
1.00
54.70

ATOM
1690
CA
SER

379
−16.511
118.359
−73.594
1.00
52.54

ATOM
1691
CB
SER

379
−17.189
119.703
−73.277
1.00
53.44

ATOM
1692
OG
SER

379
−16.486
120.400
−72.248
1.00
53.25

ATOM
1693
C
SER

379
−16.755
117.378
−72.444
1.00
50.71

ATOM
1694
O
SER

379
−15.905
117.184
−71.561
1.00
47.73

ATOM
1695
N
LEU

380
−17.936
116.772
−72.459
1.00
48.78

ATOM
1696
CA
LEU

380
−18.301
115.814
−71.435
1.00
47.66

ATOM
1697
CB
LEU

380
−19.698
115.280
−71.736
1.00
47.18

ATOM
1698
CG
LEU

380
−20.295
114.313
−70.726
1.00
46.47

ATOM
1699
CD1
LEU

380
−20.622
115.048
−69.442
1.00
45.13

ATOM
1700
CD2
LEU

380
−21.527
113.672
−71.322
1.00
44.51

ATOM
1701
C
LEU

380
−17.280
114.668
−71.401
1.00
47.62

ATOM
1702
O
LEU

380
−16.659
114.385
−70.364
1.00
45.83

ATOM
1703
N
LEU

381
−17.099
114.023
−72.549
1.00
47.58

ATOM
1704
CA
LEU

381
−16.169
112.908
−72.654
1.00
46.38

ATOM
1705
CB
LEU

381
−16.132
112.417
−74.082
1.00
46.15

ATOM
1706
CG
LEU

381
−17.520
111.971
−74.502
1.00
47.47

ATOM
1707
CD1
LEU

381
−17.548
111.593
−75.970
1.00
46.79

ATOM
1708
CD2
LEU

381
−17.942
110.808
−73.624
1.00
47.47

ATOM
1709
C
LEU

381
−14.786
113.316
−72.213
1.00
46.18

ATOM
1710
O
LEU

381
−14.136
112.620
−71.441
1.00
47.28

ATOM
1711
N
ALA

382
−14.324
114.460
−72.683
1.00
47.23

ATOM
1712
CA
ALA

382
−12.991
114.881
−72.289
1.00
47.82

ATOM
1713
CB
ALA

382
−12.627
116.208
−72.945
1.00
47.82

ATOM
1714
C
ALA

382
−12.938
114.997
−70.781
1.00
46.91

ATOM
1715
O
ALA

382
−11.916
114.713
−70.176
1.00
48.30

ATOM
1716
N
GLY

383
−14.055
115.391
−70.171
1.00
47.90

ATOM
1717
CA
GLY

383
−14.082
115.542
−68.720
1.00
45.67

ATOM
1718
C
GLY

383
−14.214
114.249
−67.922
1.00
44.89

ATOM
1719
O
GLY

383
−13.576
114.063
−66.873
1.00
42.07

ATOM
1720
N
LEU

384
−15.066
113.357
−68.405
1.00
43.92

ATOM
1721
CA
LEU

384
−15.252
112.092
−67.732
1.00
45.87

ATOM
1722
CB
LEU

384
−16.458
111.368
−68.326
1.00
42.85

ATOM
1723
CG
LEU

384
−17.816
112.028
−68.087
1.00
39.24

ATOM
1724
CD1
LEU

384
−18.874
111.269
−68.856
1.00
38.96

ATOM
1725
CD2
LEU

384
−18.138
112.047
−66.590
1.00
40.88

ATOM
1726
C
LEU

384
−13.997
111.231
−67.894
1.00
48.25

ATOM
1727
O
LEU

384
−13.687
110.401
−67.038
1.00
50.20

ATOM
1728
N
LEU

385
−13.262
111.434
−68.980
1.00
49.92

ATOM
1729
CA
LEU

385
−12.077
110.630
−69.207
1.00
50.81

ATOM
1730
CB
LEU

385
−11.973
110.246
−70.670
1.00
50.57

ATOM
1731
CG
LEU

385
−13.207
109.482
−71.145
1.00
51.27

ATOM
1732
CD1
LEU

385
−13.112
109.264
−72.648
1.00
54.08

ATOM
1733
CD2
LEU

385
−13.322
108.158
−70.413
1.00
51.68

ATOM
1734
C
LEU

385
−10.778
111.246
−68.749
1.00
51.61

ATOM
1735
O
LEU

385
−9.735
110.850
−69.221
1.00
53.44

ATOM
1736
N
LYS

386
−10.832
112.209
−67.836
1.00
52.32

ATOM
1737
CA
LYS

386
−9.614
112.806
−67.296
1.00
54.25

ATOM
1738
CB
LYS

386
−9.964
113.930
−66.312
1.00
55.53

ATOM
1739
CG
LYS

386
−9.973
115.337
−66.890
1.00
59.35

ATOM
1740
CD
LYS

386
−8.586
115.737
−67.379
1.00
61.57

ATOM
1741
CE
LYS

386
−8.476
117.225
−67.729
1.00
62.40

ATOM
1742
NZ
LYS

386
−8.110
118.106
−66.554
1.00
64.25

ATOM
1743
C
LYS

386
−8.837
111.689
−66.563
1.00
55.28

ATOM
1744
O
LYS

386
−9.412
110.912
−65.797
1.00
55.21

ATOM
1745
N
LYS

387
−7.532
111.614
−66.783
1.00
56.62

ATOM
1746
CA
LYS

387
−6.734
110.567
−66.161
1.00
57.65

ATOM
1747
CB
LYS

387
−5.431
110.371
−66.941
1.00
57.20

ATOM
1748
CG
LYS

387
−5.629
109.607
−68.233
1.00
54.57

ATOM
1749
CD
LYS

387
−4.520
109.849
−69.228
1.00
57.32

ATOM
1750
CE
LYS

387
−4.495
108.784
−70.325
1.00
56.45

ATOM
1751
NZ
LYS

387
−5.787
108.581
−71.027
1.00
54.02

ATOM
1752
C
LYS

387
−6.457
110.808
−64.700
1.00
58.92

ATOM
1753
O
LYS

387
−6.108
109.891
−63.970
1.00
58.52

ATOM
1754
N
ASP

388
−6.622
112.050
−64.270
1.00
61.81

ATOM
1755
CA
ASP

388
−6.399
112.402
−62.872
1.00
62.16

ATOM
1756
CB
ASP

388
−5.855
113.821
−62.746
1.00
62.17

ATOM
1757
CG
ASP

388
−5.111
114.047
−61.446
1.00
61.91

ATOM
1758
OD1
ASP

388
−5.446
113.405
−60.428
1.00
60.36

ATOM
1759
OD2
ASP

388
−4.187
114.888
−61.447
1.00
65.14

ATOM
1760
C
ASP

388
−7.754
112.357
−62.193
1.00
63.15

ATOM
1761
O
ASP

388
−8.635
113.159
−62.520
1.00
62.45

ATOM
1762
N
PRO

389
−7.953
111.417
−61.250
1.00
63.99

ATOM
1763
CD
PRO

389
−7.053
110.472
−60.564
1.00
63.69

ATOM
1764
CA
PRO

389
−9.278
111.427
−60.630
1.00
64.65

ATOM
1765
CB
PRO

389
−9.157
110.368
−59.527
1.00
63.51

ATOM
1766
CG
PRO

389
−7.699
110.350
−59.214
1.00
63.39

ATOM
1767
C
PRO

389
−9.550
112.833
−60.111
1.00
64.89

ATOM
1768
O
PRO

389
−10.602
113.406
−60.379
1.00
65.71

ATOM
1769
N
LYS

390
−8.574
113.413
−59.425
1.00
64.17

ATOM
1770
CA
LYS

390
−8.755
114.750
−58.896
1.00
65.12

ATOM
1771
CB
LYS

390
−7.502
115.210
−58.162
1.00
66.88

ATOM
1772
CG
LYS

390
−7.480
114.745
−56.723
1.00
69.54

ATOM
1773
CD
LYS

390
−6.348
115.373
−55.924
1.00
74.47

ATOM
1774
CE
LYS

390
−6.468
115.015
−54.438
1.00
77.11

ATOM
1775
NZ
LYS

390
−6.509
113.535
−54.182
1.00
78.67

ATOM
1776
C
LYS

390
−9.181
115.812
−59.895
1.00
64.23

ATOM
1777
O
LYS

390
−9.512
116.927
−59.501
1.00
64.56

ATOM
1778
N
GLN

391
−9.187
115.490
−61.181
1.00
62.47

ATOM
1779
CA
GLN

391
−9.611
116.485
−62.162
1.00
60.75

ATOM
1780
CB
GLN

391
−8.477
116.866
−63.084
1.00
62.53

ATOM
1781
CG
GLN

391
−7.246
117.347
−62.412
1.00
67.86

ATOM
1782
CD
GLN

391
−6.152
117.548
−63.434
1.00
73.05

ATOM
1783
OE1
GLN

391
−6.320
118.332
−64.388
1.00
74.71

ATOM
1784
NE2
GLN

391
−5.025
116.833
−63.263
1.00
73.43

ATOM
1785
C
CLN

391
−10.744
115.994
−63.032
1.00
58.42

ATOM
1786
O
GLN

391
−11.208
116.711
−63.919
1.00
58.65

ATOM
1787
N
ARG

392
−11.193
114.774
−62.797
1.00
54.84

ATOM
1788
CA
ARG

392
−12.259
114.246
−63.618
1.00
52.67

ATOM
1789
CB
ARG

392
−12.384
112.745
−63.396
1.00
49.94

ATOM
1790
CG
ARG

392
−13.290
112.012
−64.376
1.00
48.29

ATOM
1791
CD
ARG

392
−13.054
110.500
−64.206
1.00
48.02

ATOM
1792
NE
ARG

392
−11.617
110.210
−64.177
1.00
46.31

ATOM
1793
CZ
ARG

392
−11.052
109.274
−63.426
1.00
44.20

ATOM
1794
NH1
ARG

392
−11.801
108.520
−62.636
1.00
44.34

ATOM
1795
NH2
ARG

392
−9.737
109.121
−63.440
1.00
42.60

ATOM
1796
C
ARG

392
−13.588
114.932
−63.344
1.00
50.78

ATOM
1797
O
ARG

392
−13.861
115.393
−62.251
1.00
52.37

ATOM
1798
N
LEU

393
−14.399
115.016
−64.375
1.00
49.90

ATOM
1799
CA
LEU

393
−15.709
115.586
−64.256
1.00
50.17

ATOM
1800
CB
LEU

393
−16.406
115.541
−65.610
1.00
48.71

ATOM
1801
CG
LEU

393
−17.595
116.450
−65.879
1.00
47.91

ATOM
1802
CD1
LEU

393
−18.567
115.731
−66.796
1.00
47.02

ATOM
1803
CD2
LEU

393
−18.259
116.816
−64.576
1.00
49.63

ATOM
1804
C
LEU

393
−16.432
114.653
−63.288
1.00
52.41

ATOM
1805
O
LEU

393
−16.839
113.549
−63.671
1.00
53.23

ATOM
1806
N
GLY

394
−16.581
115.081
−62.037
1.00
53.32

ATOM
1807
CA
GLY

394
−17.277
114.261
−61.070
1.00
53.52

ATOM
1808
C
GLY

394
−16.340
113.821
−59.981
1.00
54.11

ATOM
1809
O
GLY

394
−16.772
113.291
−58.956
1.00
53.36

ATOM
1810
N
GLY

395
−15.053
114.047
−60.214
1.00
54.86

ATOM
1811
CA
GLY

395
−14.040
113.678
−59.248
1.00
56.24

ATOM
1812
C
GLY

395
−13.876
114.765
−58.201
1.00
58.65

ATOM
1813
O
GLY

395
−13.037
114.656
−57.297
1.00
59.43

ATOM
1814
N
GLY

396
−14.664
115.828
−58.329
1.00
59.28

ATOM
1815
CA
GLY

396
−14.597
116.912
−57.362
1.00
59.27

ATOM
1816
C
GLY

396
−15.568
116.660
−56.218
1.00
59.64

ATOM
1817
O
GLY

396
−16.538
115.920
−56.398
1.00
58.40

ATOM
1818
N
PRO

397
−15.347
117.270
−55.031
1.00
59.85

ATOM
1819
CD
PRO

397
−14.322
118.293
−54.770
1.00
59.44

ATOM
1820
CA
PRO

397
−16.213
117.098
−53.853
1.00
59.00

ATOM
1821
CB
PRO

397
−15.695
118.155
−52.878
1.00
59.15

ATOM
1822
CG
PRO

397
−15.006
119.161
−53.762
1.00
59.13

ATOM
1823
C
PRO

397
−17.711
117.212
−54.095
1.00
59.00

ATOM
1824
O
PRO

397
−18.514
116.724
−53.298
1.00
59.48

ATOM
1825
N
SER

398
−18.084
117.841
−55.201
1.00
58.44

ATOM
1826
CA
SER

398
−19.479
118.013
−55.542
1.00
58.58

ATOM
1827
CB
SER

398
−19.636
119.226
−56.451
1.00
62.15

ATOM
1828
OG
SER

398
−20.991
119.394
−56.846
1.00
66.14

ATOM
1829
C
SER

398
−20.024
116.781
−56.247
1.00
57.44

ATOM
1830
O
SER

398
−21.188
116.754
−56.642
1.00
56.72

ATOM
1831
N
ASP

399
−19.167
115.777
−56.419
1.00
56.57

ATOM
1832
CA
ASP

399
−19.527
114.515
−57.076
1.00
54.02

ATOM
1833
CB
ASP

399
−20.107
113.528
−56.041
1.00
54.67

ATOM
1834
CG
ASP

399
−20.177
112.096
−56.558
1.00
53.89

ATOM
1835
OD1
ASP

399
−21.288
111.628
−56.860
1.00
55.72

ATOM
1836
OD2
ASP

399
−19.123
111.435
−56.663
1.00
53.25

ATOM
1837
C
ASP

399
−20.492
114.681
−58.254
1.00
52.23

ATOM
1838
O
ASP

399
−20.250
115.490
−59.146
1.00
51.65

ATOM
1839
N
ALA

400
−21.585
113.926
−58.256
1.00
50.05

ATOM
1840
CA
ALA

400
−22.541
114.000
−59.350
1.00
50.76

ATOM
1841
CB
ALA

400
−23.817
113.245
−58.981
1.00
48.57

ATOM
1842
C
ALA

400
−22.888
115.419
−59.834
1.00
51.21

ATOM
1843
O
ALA

400
−23.028
115.653
−61.028
1.00
50.70

ATOM
1844
N
LYS

401
−23.026
116.372
−58.927
1.00
52.29

ATOM
1845
CA
LYS

401
−23.373
117.722
−59.355
1.00
54.73

ATOM
1846
CB
LYS

401
−23.317
118.664
−58.159
1.00
56.85

ATOM
1847
CG
LYS

401
−24.401
118.358
−57.136
1.00
59.67

ATOM
1848
CD
LYS

401
−24.009
118.894
−55.754
1.00
63.33

ATOM
1849
CE
LYS

401
−25.081
118.675
−54.699
1.00
61.16

ATOM
1850
NZ
LYS

401
−24.682
119.357
−53.437
1.00
60.07

ATOM
1851
C
LYS

401
−22.538
118.258
−60.529
1.00
53.87

ATOM
1852
O
LYS

401
−23.100
118.718
−61.510
1.00
54.65

ATOM
1853
N
GLU

402
−21.216
118.192
−60.458
1.00
54.04

ATOM
1854
CA
GLU

402
−20.424
118.663
−61.587
1.00
56.21

ATOM
1855
CB
GLU

402
−18.967
118.276
−61.408
1.00
57.34

ATOM
1856
CG
GLU

402
−18.248
118.977
−60.285
1.00
61.35

ATOM
1857
CD
GLU

402
−16.812
118.470
−60.133
1.00
67.08

ATOM
1858
OE1
GLU

402
−16.136
118.249
−61.168
1.00
71.46

ATOM
1859
OE2
GLU

402
−16.343
118.295
−58.988
1.00
69.45

ATOM
1860
C
GLU

402
−20.930
118.078
−62.918
1.00
56.01

ATOM
1861
O
GLU

402
−20.962
118.757
−63.939
1.00
58.61

ATOM
1862
N
VAL

403
−21.339
116.818
−62.896
1.00
55.01

ATOM
1863
CA
VAL

403
−21.818
116.126
−64.087
1.00
54.30

ATOM
1864
CB
VAL

403
−21.745
114.577
−63.869
1.00
52.34

ATOM
1865
CG1
VAL

403
−22.260
113.806
−65.096
1.00
49.97

ATOM
1866
CG2
VAL

403
−20.338
114.191
−63.547
1.00
48.55

ATOM
1867
C
VAL

403
−23.249
116.506
−64.477
1.00
55.72

ATOM
1868
O
VAL

403
−23.579
116.631
−65.665
1.00
55.85

ATOM
1869
N
MET

404
−24.109
116.665
−63.479
1.00
56.07

ATOM
1870
CA
MET

404
−25.500
117.018
−63.752
1.00
56.54

ATOM
1871
CB
MET

404
−26.326
116.934
−62.470
1.00
55.56

ATOM
1872
CG
MET

404
−26.808
115.543
−62.127
1.00
56.38

ATOM
1873
SD
MET

404
−27.379
115.534
−60.461
1.00
53.80

ATOM
1874
CE
MET

404
−25.837
115.738
−59.667
1.00
54.96

ATOM
1875
C
MET

404
−25.635
118.418
−64.339
1.00
55.41

ATOM
1876
O
MET

404
−26.583
118.709
−65.057
1.00
53.73

ATOM
1877
N
GLU

405
−24.673
119.273
−64.022
1.00
55.58

ATOM
1878
CA
GLU

405
−24.688
120.640
−64.483
1.00
58.04

ATOM
1879
CB
GLU

405
−24.334
121.561
−63.328
1.00
59.78

ATOM
1880
CG
GLU

405
−25.120
121.309
−62.074
1.00
63.57

ATOM
1881
CD
GLU

405
−24.559
122.097
−60.910
1.00
66.97

ATOM
1882
OE1
GLU

405
−23.353
122.442
−60.977
1.00
66.24

ATOM
1883
OE2
GLU

405
−25.309
122.359
−59.937
1.00
69.08

ATOM
1884
C
GLU

405
−23.707
120.896
−65.620
1.00
59.79

ATOM
1885
O
GLU

405
−23.284
122.046
−65.837
1.00
60.33

ATOM
1886
N
HIS

406
−23.319
119.845
−66.341
1.00
58.09

ATOM
1887
CA
HIS

406
−22.377
120.057
−67.420
1.00
52.85

ATOM
1888
CB
HIS

406
−21.558
118.794
−67.742
1.00
48.84

ATOM
1889
CG
HIS

406
−20.579
118.978
−68.864
1.00
40.92

ATOM
1890
CD2
HIS

406
−19.263
119.296
−68.855
1.00
38.08

ATOM
1891
ND1
HIS

406
−20.938
118.885
−70.196
1.00
40.72

ATOM
1892
CE1
HIS

406
−19.889
119.136
−70.953
1.00
34.51

ATOM
1893
NE2
HIS

406
−18.859
119.391
−70.165
1.00
36.37

ATOM
1894
C
HIS

406
−23.146
120.483
−68.628
1.00
54.12

ATOM
1895
O
HIS

406
−24.302
120.093
−68.838
1.00
52.18

ATOM
1896
N
ARG

407
−22.479
121.321
−69.404
1.00
55.55

ATOM
1897
CA
ARG

407
−23.001
121.846
−70.640
1.00
58.47

ATOM
1898
CB
ARG

407
−21.816
122.218
−71.517
1.00
62.44

ATOM
1899
CG
ARG

407
−22.120
122.712
−72.902
1.00
66.15

ATOM
1900
CD
ARG

407
−20.781
122.911
−73.581
1.00
69.94

ATOM
1901
NE
ARG

407
−20.881
123.436
−74.934
1.00
75.38

ATOM
1902
CZ
ARG

407
−19.828
123.780
−75.674
1.00
77.07

ATOM
1903
NH1
ARG

407
−18.599
123.653
−75.179
1.00
77.19

ATOM
1904
NH2
ARG

407
−20.006
124.243
−76.907
1.00
78.05

ATOM
1905
C
ARG

407
−23.835
120.774
−71.307
1.00
58.60

ATOM
1906
O
ARG

407
−25.030
120.967
−71.546
1.00
58.90

ATOM
1907
N
PHE

408
−23.209
119.628
−71.579
1.00
57.25

ATOM
1908
CA
PHE

408
−23.921
118.539
−72.243
1.00
56.47

ATOM
1909
CB
PHE

408
−23.056
117.267
−72.290
1.00
56.76

ATOM
1910
CG
PHE

408
−23.709
116.129
−73.027
1.00
54.26

ATOM
1911
CD1
PHE

408
−23.666
116.071
−74.410
1.00
53.88

ATOM
1912
CD2
PHE

408
−24.434
115.164
−72.335
1.00
53.15

ATOM
1913
CE1
PHE

408
−24.335
115.077
−75.097
1.00
55.74

ATOM
1914
CE2
PHE

408
−25.114
114.165
−73.008
1.00
54.60

ATOM
1915
CZ
PHE

408
−25.067
114.117
−74.398
1.00
57.66

ATOM
1916
C
PHE

408
−25.255
118.221
−71.566
1.00
55.42

ATOM
1917
O
PHE

408
−26.179
117.726
−72.205
1.00
53.41

ATOM
1918
N
PHE

409
−25.348
118.516
−70.271
1.00
55.79

ATOM
1919
CA
PHE

409
−26.558
118.253
−69.509
1.00
56.18

ATOM
1920
CB
PHE

409
−26.225
117.407
−68.245
1.00
53.73

ATOM
1921
CG
PHE

409
−25.870
115.940
−68.528
1.00
47.14

ATOM
1922
CD1
PHE

409
−26.801
115.075
−69.107
1.00
44.58

ATOM
1923
CD2
PHE

409
−24.616
115.442
−68.213
1.00
44.43

ATOM
1924
CE1
PHE

409
−26.482
113.748
−69.367
1.00
44.98

ATOM
1925
CE2
PHE

409
−24.277
114.093
−68.471
1.00
44.11

ATOM
1926
CZ
PHE

409
−25.210
113.252
−69.050
1.00
42.55

ATOM
1927
C
PHE

409
−27.292
119.552
−69.101
1.00
59.74

ATOM
1928
O
PHE

409
−27.103
120.069
−67.990
1.00
59.58

ATOM
1929
N
LEU

410
−28.134
120.076
−69.998
1.00
61.57

ATOM
1930
CA
LEU

410
−28.922
121.279
−69.712
1.00
63.20

ATOM
1931
CB
LEU

410
−28.606
122.400
−70.703
1.00
64.81

ATOM
1932
CG
LEU

410
−29.718
123.442
−70.916
1.00
64.28

ATOM
1933
CD1
LEU

410
−29.124
124.805
−71.188
1.00
63.37

ATOM
1934
CD2
LEU

410
−30.609
123.003
−72.074
1.00
62.40

ATOM
1935
C
LEU

410
−30.399
120.953
−69.791
1.00
63.34

ATOM
1936
O
LEU

410
−31.151
121.165
−68.855
1.00
64.71

ATOM
1937
N
SER

411
−30.797
120.434
−70.931
1.00
63.38

ATOM
1938
CA
SER

411
−32.168
120.061
−71.189
1.00
63.86

ATOM
1939
CB
SER

411
−32.222
119.362
−72.540
1.00
65.46

ATOM
1940
OG
SER

411
−31.246
118.319
−72.586
1.00
65.31

ATOM
1941
C
SER

411
−32.747
119.124
−70.141
1.00
63.97

ATOM
1942
O
SER

411
−33.963
118.919
−70.090
1.00
65.56

ATOM
1943
N
ILE

412
−31.882
118.550
−69.308
1.00
63.16

ATOM
1944
CA
ILE

412
−32.324
117.576
−68.315
1.00
59.72

ATOM
1945
CB
ILE

412
−31.176
116.621
−67.886
1.00
59.74

ATOM
1946
CG2
ILE

412
−31.732
115.541
−66.969
1.00
60.46

ATOM
1947
CG1
ILE

412
−30.554
115.943
−69.111
1.00
58.99

ATOM
1948
CD1
ILE

412
−31.553
115.171
−69.950
1.00
60.50

ATOM
1949
C
ILE

412
−32.990
118.037
−67.041
1.00
57.34

ATOM
1950
O
ILE

412
−32.588
118.988
−66.384
1.00
55.60

ATOM
1951
N
ASN

413
−34.018
117.293
−66.687
1.00
55.66

ATOM
1952
CA
ASN

413
−34.742
117.547
−65.481
1.00
54.01

ATOM
1953
CB
ASN

413
−36.209
117.699
−65.813
1.00
57.97

ATOM
1954
CG
ASN

413
−36.880
118.676
−64.904
1.00
62.55

ATOM
1955
OD1
ASN

413
−37.468
118.295
−63.877
1.00
62.35

ATOM
1956
ND2
ASN

413
−36.773
119.969
−65.252
1.00
64.77

ATOM
1957
C
ASN

413
−34.495
116.339
−64.581
1.00
50.15

ATOM
1958
O
ASN

413
−35.194
115.327
−64.664
1.00
46.05

ATOM
1959
N
TRP

414
−33.495
116.471
−63.717
1.00
49.18

ATOM
1960
CA
TRP

414
−33.082
115.393
−62.827
1.00
50.10

ATOM
1961
CB
TRP

414
−31.928
115.864
−61.957
1.00
49.14

ATOM
1962
CG
TRP

414
−30.794
116.301
−62.825
1.00
53.71

ATOM
1963
CD2
TRP

414
−29.905
115.450
−63.590
1.00
56.49

ATOM
1964
CE2
TRP

414
−29.069
116.296
−64.359
1.00
55.49

ATOM
1965
CE3
TRP

414
−29.738
114.058
−63.699
1.00
56.94

ATOM
1966
CD1
TRP

414
−30.462
117.578
−63.151
1.00
54.04

ATOM
1967
NE1
TRP

414
−29.428
117.587
−64.077
1.00
56.41

ATOM
1968
CZ2
TRP

414
−28.082
115.799
−65.217
1.00
56.63

ATOM
1969
CZ3
TRP

414
−28.746
113.561
−64.563
1.00
57.11

ATOM
1970
CH2
TRP

414
−27.936
114.434
−65.307
1.00
56.43

ATOM
1971
C
TRP

414
−34.167
114.753
−62.008
1.00
51.80

ATOM
1972
O
TRP

414
−34.085
113.566
−61.690
1.00
54.04

ATOM
1973
N
GLN

415
−35.204
115.516
−61.682
1.00
52.38

ATOM
1974
CA
GLN

415
−36.305
114.963
−60.921
1.00
51.12

ATOM
1975
CB
GLN

415
−37.241
116.064
−60.455
1.00
50.32

ATOM
1976
CG
GLN

415
−37.102
116.392
−59.004
1.00
48.51

ATOM
1977
CD
CLN

415
−38.256
117.229
−58.503
1.00
44.92

ATOM
1978
OE1
GLN

415
−39.405
116.818
−58.569
1.00
45.16

ATOM
1979
NE2
GLN

415
−37.949
118.406
−58.004
1.00
41.65

ATOM
1980
C
GLN

415
−37.037
114.061
−61.875
1.00
53.28

ATOM
1981
O
GLN

415
−37.503
112.973
−61.520
1.00
53.75

ATOM
1982
N
ASP

416
−37.134
114.535
−63.106
1.00
54.15

ATOM
1983
CA
ASP

416
−37.815
113.793
−64.146
1.00
55.69

ATOM
1984
CB
ASP

416
−37.837
114.613
−65.442
1.00
60.37

ATOM
1985
CG
ASP

416
−38.998
115.599
−65.490
1.00
65.00

ATOM
1986
OD1
ASP

416
−40.169
115.141
−65.488
1.00
66.07

ATOM
1987
OD2
ASP

416
−38.737
116.824
−65.521
1.00
66.23

ATOM
1988
C
ASP

416
−37.074
112.499
−64.366
1.00
53.11

ATOM
1989
O
ASP

416
−37.668
111.434
−64.496
1.00
52.07

ATOM
1990
N
VAL

417
−35.759
112.627
−64.404
1.00
52.21

ATOM
1991
CA
VAL

417
−34.863
111.501
−64.610
1.00
51.80

ATOM
1992
CB
VAL

417
−33.412
111.961
−64.467
1.00
49.97

ATOM
1993
CG1
VAL

417
−32.472
110.762
−64.483
1.00
51.02

ATOM
1994
CG2
VAL

417
−33.100
112.908
−65.604
1.00
45.80

ATOM
1995
C
VAL

417
−35.158
110.384
−63.627
1.00
50.42

ATOM
1996
O
VAL

417
−35.576
109.298
−64.028
1.00
50.11

ATOM
1997
N
VAL

418
−35.003
110.674
−62.340
1.00
50.05

ATOM
1998
CA
VAL

418
−35.252
109.672
−61.320
1.00
50.83

ATOM
1999
CB
VAL

418
−34.743
110.146
−59.955
1.00
52.90

ATOM
2000
CG1
VAL

418
−33.496
110.981
−60.158
1.00
54.38

ATOM
2001
CG2
VAL

418
−35.820
110.936
−59.219
1.00
53.52

ATOM
2002
C
VAL

418
−36.720
109.296
−61.218
1.00
52.01

ATOM
2003
O
VAL

418
−37.071
108.281
−60.615
1.00
52.28

ATOM
2004
N
GLN

419
−37.592
110.101
−61.802
1.00
52.94

ATOM
2005
CA
GLN

419
−39.001
109.765
−61.745
1.00
55.18

ATOM
2006
CB
GLN

419
−39.863
111.032
−61.754
1.00
57.66

ATOM
2007
CG
GLN

419
−39.825
111.869
−60.460
1.00
59.36

ATOM
2008
CD
GLN

419
−40.442
111.155
−59.276
1.00
62.06

ATOM
2009
OE1
GLN

419
−41.601
110.737
−59.321
1.00
64.62

ATOM
2010
NE2
GLN

419
−39.670
111.012
−58.202
1.00
64.83

ATOM
2011
C
GLN

419
−39.421
108.845
−62.889
1.00
56.26

ATOM
2012
O
GLN

419
−40.572
108.409
−62.934
1.00
57.06

ATOM
2013
N
LYS

420
−38.490
108.517
−63.790
1.00
56.08

ATOM
2014
CA
LYS

420
−38.814
107.657
−64.931
1.00
55.57

ATOM
2015
CB
LYS

420
−39.320
106.287
−64.471
1.00
54.42

ATOM
2016
CG
LYS

420
−38.255
105.261
−64.104
1.00
55.72

ATOM
2017
CD
LYS

420
−38.819
103.826
−64.034
1.00
55.51

ATOM
2018
CE
LYS

420
−37.677
102.805
−63.774
1.00
59.38

ATOM
2019
NZ
LYS

420
−38.076
101.362
−63.591
1.00
58.45

ATOM
2020
C
LYS

420
−39.926
108.356
−65.724
1.00
57.42

ATOM
2021
O
LYS

420
−40.726
107.716
−66.424
1.00
56.09

ATOM
2022
N
LYS

421
−39.971
109.678
−65.585
1.00
58.45

ATOM
2023
CA
LYS

421
−40.969
110.499
−66.243
1.00
60.43

ATOM
2024
CB
LYS

421
−41.145
111.808
−65.463
1.00
63.06

ATOM
2025
CG
LYS

421
−42.569
112.092
−65.016
1.00
66.83

ATOM
2026
CD
LYS

421
−43.152
110.957
−64.175
1.00
68.90

ATOM
2027
CE
LYS

421
−44.627
111.224
−63.855
1.00
71.68

ATOM
2028
NZ
LYS

421
−44.839
112.504
−63.115
1.00
71.58

ATOM
2029
C
LYS

421
−40.562
110.792
−67.689
1.00
61.55

ATOM
2030
O
LYS

421
−41.394
111.164
−68.516
1.00
61.24

ATOM
2031
N
LEU

422
−39.279
110.625
−67.992
1.00
61.71

ATOM
2032
CA
LEU

422
−38.795
110.870
−69.343
1.00
61.12

ATOM
2033
CB
LEU

422
−37.273
111.024
−69.358
1.00
58.69

ATOM
2034
CG
LEU

422
−36.793
112.227
−68.551
1.00
57.09

ATOM
2035
CD1
LEU

422
−35.328
112.468
−68.787
1.00
55.92

ATOM
2036
CD2
LEU

422
−37.591
113.449
−68.962
1.00
58.70

ATOM
2037
C
LEU

422
−39.197
109.703
−70.216
1.00
61.35

ATOM
2038
O
LEU

422
−39.262
108.575
−69.748
1.00
62.11

ATOM
2039
N
LEU

423
−39.491
109.977
−71.481
1.00
62.29

ATOM
2040
CA
LEU

423
−39.868
108.920
−72.410
1.00
62.77

ATOM
2041
CB
LEU

423
−40.817
109.480
−73.481
1.00
62.00

ATOM
2042
CG
LEU

423
−41.542
108.475
−74.382
1.00
63.36

ATOM
2043
CD1
LEU

423
−42.505
107.628
−73.551
1.00
61.18

ATOM
2044
CD2
LEU

423
−42.289
109.224
−75.483
1.00
63.05

ATOM
2045
C
LEU

423
−38.584
108.341
−73.044
1.00
61.73

ATOM
2046
O
LEU

423
−37.677
109.066
−73.452
1.00
61.55

ATOM
2047
N
PRO

424
−38.476
107.018
−73.097
1.00
62.47

ATOM
2048
CD
PRO

424
−39.311
105.961
−72.495
1.00
63.37

ATOM
2049
CA
PRO

424
−37.255
106.472
−73.700
1.00
62.30

ATOM
2050
CB
PRO

424
−37.243
105.029
−73.198
1.00
62.87

ATOM
2051
CG
PRO

424
−38.707
104.694
−73.079
1.00
62.90

ATOM
2052
C
PRO

424
−37.251
106.575
−75.231
1.00
61.64

ATOM
2053
O
PRO

424
−38.209
106.163
−75.897
1.00
61.35

ATOM
2054
N
PRO

425
−36.167
107.126
−75.806
1.00
60.32

ATOM
2055
CD
PRO

425
−34.925
107.498
−75.121
1.00
59.42

ATOM
2056
CA
PRO

425
−36.004
107.298
−77.251
1.00
60.15

ATOM
2057
CB
PRO

425
−34.623
107.916
−77.368
1.00
59.16

ATOM
2058
CG
PRO

425
−33.924
107.335
−76.226
1.00
59.65

ATOM
2059
C
PRO

425
−36.118
106.001
−78.040
1.00
60.95

ATOM
2060
O
PRO

425
−35.993
106.002
−79.269
1.00
61.28

ATOM
2061
N
PHE

426
−36.359
104.902
−77.332
1.00
59.85

ATOM
2062
CA
PHE

426
−36.504
103.604
−77.964
1.00
59.45

ATOM
2063
CB
PHE

426
−35.149
103.014
−78.319
1.00
60.30

ATOM
2064
CG
PHE

426
−35.213
101.553
−78.647
1.00
61.86

ATOM
2065
CD1
PHE

426
−35.996
101.100
−79.699
1.00
62.98

ATOM
2066
CD2
PHE

426
−34.518
100.622
−77.886
1.00
61.05

ATOM
2067
CE1
PHE

426
−36.082
99.738
−79.984
1.00
63.40

ATOM
2068
CE2
PHE

426
−34.598
99.269
−78.163
1.00
60.51

ATOM
2069
CZ
PHE

426
−35.380
98.824
−79.211
1.00
61.73

ATOM
2070
C
PHE

426
−37.231
102.613
−77.089
1.00
59.96

ATOM
2071
O
PHE

426
−36.870
102.400
−75.936
1.00
60.41

ATOM
2072
N
LYS

427
−38.248
101.978
−77.635
1.00
60.95

ATOM
2073
CA
LYS

427
−38.956
101.019
−76.834
1.00
64.11

ATOM
2074
CB
LYS

427
−40.449
101.315
−76.817
1.00
66.80

ATOM
2075
CG
LYS

427
−41.223
100.379
−75.906
1.00
69.63

ATOM
2076
CD
LYS

427
−42.583
100.941
−75.606
1.00
73.24

ATOM
2077
CE
LYS

427
−43.325
100.103
−74.583
1.00
75.62

ATOM
2078
NZ
LYS

427
−44.685
100.695
−74.329
1.00
78.61

ATOM
2079
C
LYS

427
−38.718
99.619
−77.334
1.00
65.11

ATOM
2080
O
LYS

427
−38.968
99.311
−78.490
1.00
63.93

ATOM
2081
N
PRO

428
−38.203
98.752
−76.460
1.00
67.83

ATOM
2082
CD
PRO

428
−37.755
99.068
−75.095
1.00
67.46

ATOM
2083
CA
PRO

428
−37.920
97.354
−76.796
1.00
69.61

ATOM
2084
CB
PRO

428
−37.394
96.793
−75.484
1.00
69.12

ATOM
2085
CG
PRO

428
−36.726
98.003
−74.859
1.00
68.49

ATOM
2086
C
PRO

428
−39.230
96.708
−77.235
1.00
72.00

ATOM
2087
O
PRO

428
−40.306
97.111
−76.779
1.00
71.52

ATOM
2088
N
GLN

429
−39.144
95.704
−78.097
1.00
74.15

ATOM
2089
CA
GLN

429
−40.343
95.067
−78.613
1.00
79.21

ATOM
2090
CB
GLN

429
−40.092
94.660
−80.078
1.00
81.34

ATOM
2091
CG
GLN

429
−39.762
95.862
−80.998
1.00
83.36

ATOM
2092
CD
GLN

429
−38.427
95.726
−81.758
1.00
84.49

ATOM
2093
OE1
GLN

429
−37.441
95.201
−81.233
1.00
84.83

ATOM
2094
NE2
GLN

429
−38.394
96.229
−82.990
1.00
84.60

ATOM
2095
C
GLN

429
−40.900
93.890
−77.799
1.00
81.25

ATOM
2096
O
GLN

429
−41.217
92.841
−78.358
1.00
81.88

ATOM
2097
N
VAL

430
−41.049
94.076
−76.487
1.00
83.33

ATOM
2098
CA
VAL

430
−41.575
93.022
−75.607
1.00
84.98

ATOM
2099
CB
VAL

430
−40.690
92.858
−74.342
1.00
83.81

ATOM
2100
CG1
VAL

430
−39.398
92.181
−74.706
1.00
82.55

ATOM
2101
CG2
VAL

430
−40.395
94.213
−73.727
1.00
82.81

ATOM
2102
C
VAL

430
−43.031
93.269
−75.168
1.00
87.28

ATOM
2103
O
VAL

430
−43.430
94.416
−74.927
1.00
88.31

ATOM
2104
N
THR

431
−43.819
92.196
−75.068
1.00
88.25

ATOM
2105
CA
THR

431
−45.232
92.300
−74.667
1.00
89.29

ATOM
2106
CB
THR

431
−45.928
90.908
−74.636
1.00
89.30

ATOM
2107
OG1
THR

431
−45.791
90.259
−75.908
1.00
90.23

ATOM
2108
CG2
THR

431
−47.406
91.060
−74.306
1.00
89.06

ATOM
2109
C
THR

431
−45.340
92.883
−73.263
1.00
89.57

ATOM
2110
O
THR

431
−45.818
93.998
−73.046
1.00
88.88

ATOM
2111
N
SER

432
−44.890
92.085
−72.311
1.00
90.05

ATOM
2112
CA
SER

432
−44.896
92.452
−70.916
1.00
90.57

ATOM
2113
CB
SER

432
−46.073
91.781
−70.221
1.00
91.71

ATOM
2114
OG
SER

432
−46.052
90.383
−70.467
1.00
92.70

ATOM
2115
C
SER

432
−43.590
91.893
−70.386
1.00
90.68

ATOM
2116
O
SER

432
−42.878
91.192
−71.111
1.00
90.77

ATOM
2117
N
GLU

433
−43.266
92.193
−69.134
1.00
90.44

ATOM
2118
CA
GLU

433
−42.035
91.677
−68.568
1.00
90.51

ATOM
2119
CB
GLU

433
−41.873
92.168
−67.129
1.00
91.44

ATOM
2120
CG
GLU

433
−43.165
92.298
−66.370
1.00
93.97

ATOM
2121
CD
GLU

433
−43.077
93.334
−65.263
1.00
95.97

ATOM
2122
OE1
GLU

433
−42.108
93.279
−64.472
1.00
95.47

ATOM
2123
OE2
GLU

433
−43.981
94.204
−65.188
1.00
97.07

ATOM
2124
C
GLU

433
−42.003
90.150
−68.651
1.00
89.80

ATOM
2125
O
GLU

433
−40.965
89.529
−68.447
1.00
89.98

ATOM
2126
N
VAL

434
−43.145
89.561
−68.989
1.00
89.02

ATOM
2127
CA
VAL

434
−43.276
88.114
−69.122
1.00
87.58

ATOM
2128
CB
VAL

434
−44.762
87.677
−69.051
1.00
87.60

ATOM
2129
CG1
VAL

434
−44.863
86.181
−68.774
1.00
86.18

ATOM
2130
CG2
VAL

434
−45.495
88.484
−67.990
1.00
87.26

ATOM
2131
C
VAL

434
−42.724
87.701
−70.476
1.00
86.78

ATOM
2132
O
VAL

434
−42.287
86.567
−70.664
1.00
86.37

ATOM
2133
N
ASP

435
−42.756
88.632
−71.422
1.00
86.52

ATOM
2134
CA
ASP

435
−42.257
88.362
−72.758
1.00
86.28

ATOM
2135
CB
ASP

435
−42.355
89.613
−73.629
1.00
86.61

ATOM
2136
CG
ASP

435
−41.944
89.350
−75.062
1.00
87.61

ATOM
2137
OD1
ASP

435
−42.491
88.411
−75.679
1.00
87.73

ATOM
2138
OD2
ASP

435
−41.070
90.078
−75.574
1.00
88.49

ATOM
2139
C
ASP

435
−40.809
87.892
−72.676
1.00
85.62

ATOM
2140
O
ASP

435
−39.937
88.611
−72.180
1.00
84.77

ATOM
2141
N
THR

436
−40.562
86.686
−73.178
1.00
85.48

ATOM
2142
CA
THR

436
−39.229
86.085
−73.138
1.00
85.33

ATOM
2143
CB
THR

436
−39.323
84.597
−72.743
1.00
84.60

ATOM
2144
OG1
THR

436
−39.815
83.843
−73.857
1.00
83.80

ATOM
2145
CG2
THR

436
−40.270
84.417
−71.566
1.00
82.29

ATOM
2146
C
THR

436
−38.455
86.160
−74.455
1.00
85.27

ATOM
2147
O
THR

436
−37.513
85.390
−74.669
1.00
84.76

ATOM
2148
N
ARG

437
−38.820
87.092
−75.326
1.00
85.80

ATOM
2149
CA
ARG

437
−38.146
87.170
−76.613
1.00
86.96

ATOM
2150
CB
ARG

437
−39.005
87.931
−77.626
1.00
87.46

ATOM
2151
CG
ARG

437
−38.985
89.432
−77.509
1.00
88.62

ATOM
2152
CD
ARG

437
−39.638
90.034
−78.749
1.00
90.99

ATOM
2153
NE
ARG

437
−40.987
89.502
−78.970
1.00
92.25

ATOM
2154
CZ
ARG

437
−41.689
89.666
−80.090
1.00
92.57

ATOM
2155
NH1
ARG

437
−41.181
90.351
−81.109
1.00
93.15

ATOM
2156
NH2
ARG

437
−42.901
89.138
−80.195
1.00
92.65

ATOM
2157
C
ARG

437
−36.712
87.695
−76.670
1.00
86.99

ATOM
2158
O
ARG

437
−36.017
87.418
−77.643
1.00
87.72

ATOM
2159
N
TYR

438
−36.249
88.442
−75.669
1.00
86.84

ATOM
2160
CA
TYR

438
−34.868
88.928
−75.713
1.00
86.83

ATOM
2161
CB
TYR

438
−34.727
90.299
−75.042
1.00
86.68

ATOM
2162
CG
TYR

438
−35.112
91.450
−75.945
1.00
87.90

ATOM
2163
CD1
TYR

438
−36.343
92.097
−75.803
1.00
87.81

ATOM
2164
CE1
TYR

438
−36.723
93.135
−76.663
1.00
87.32

ATOM
2165
CD2
TYR

438
−34.262
91.872
−76.973
1.00
87.74

ATOM
2166
CE2
TYR

438
−34.629
92.910
−77.841
1.00
86.99

ATOM
2167
CZ
TYR

438
−35.863
93.534
−77.679
1.00
87.49

ATOM
2168
OH
TYR

438
−36.244
94.545
−78.536
1.00
87.87

ATOM
2169
C
TYR

438
−33.903
87.951
−75.064
1.00
86.82

ATOM
2170
O
TYR

438
−32.692
88.165
−75.066
1.00
87.00

ATOM
2171
N
PHE

439
−34.441
86.864
−74.528
1.00
87.29

ATOM
2172
CA
PHE

439
−33.620
85.865
−73.863
1.00
88.45

ATOM
2173
CB
PHE

439
−34.498
85.037
−72.920
1.00
86.80

ATOM
2174
CG
PHE

439
−35.133
85.846
−71.813
1.00
85.58

ATOM
2175
CD1
PHE

439
−36.068
85.270
−70.959
1.00
85.32

ATOM
2176
CD2
PHE

439
−34.803
87.189
−71.628
1.00
85.46

ATOM
2177
CE1
PHE

439
−36.664
86.015
−69.940
1.00
85.22

ATOM
2178
CE2
PHE

439
−35.393
87.940
−70.615
1.00
85.05

ATOM
2179
CZ
PHE

439
−36.325
87.354
−69.769
1.00
85.55

ATOM
2180
C
PHE

439
−32.841
84.958
−74.817
1.00
89.81

ATOM
2181
O
PHE

439
−32.724
83.761
−74.581
1.00
90.39

ATOM
2182
N
ASP

440
−32.308
85.549
−75.888
1.00
92.18

ATOM
2183
CA
ASP

440
−31.505
84.851
−76.906
1.00
93.77

ATOM
2184
CB
ASP

440
−32.378
84.402
−78.085
1.00
94.49

ATOM
2185
CG
ASP

440
−33.503
83.476
−77.665
1.00
95.46

ATOM
2186
OD1
ASP

440
−34.347
83.889
−76.838
1.00
95.57

ATOM
2187
OD2
ASP

440
−33.549
82.335
−78.170
1.00
95.83

ATOM
2188
C
ASP

440
−30.462
85.858
−77.414
1.00
94.78

ATOM
2189
O
ASP

440
−30.043
86.747
−76.657
1.00
95.43

ATOM
2190
N
ASP

441
−30.051
85.729
−78.680
1.00
95.03

ATOM
2191
CA
ASP

441
−29.075
86.656
−79.279
1.00
95.25

ATOM
2192
CB
ASP

441
−27.915
85.901
−79.960
1.00
95.91

ATOM
2193
CG
ASP

441
−26.870
85.376
−78.966
1.00
97.03

ATOM
2194
OD1
ASP

441
−27.176
84.396
−78.239
1.00
97.59

ATOM
2195
OD2
ASP

441
−25.744
85.945
−78.915
1.00
95.54

ATOM
2196
C
ASP

441
−29.749
87.569
−80.310
1.00
95.02

ATOM
2197
O
ASP

441
−29.416
87.547
−81.498
1.00
94.55

ATOM
2198
OH2
TIP

1
−17.565
102.189
−62.350
1.00
37.43

ATOM
2199
OH2
TIP

2
−33.587
91.116
−71.760
1.00
41.39

ATOM
2200
OH2
TIP

3
−17.875
100.298
−70.868
1.00
46.03

ATOM
2201
OH2
TIP

4
−25.044
95.430
−72.610
1.00
42.52

ATOM
2202
OH2
TIP

5
−23.822
111.358
−54.564
1.00
45.34

ATOM
2203
OH2
TIP

6
−39.172
106.198
−60.025
1.00
45.47

ATOM
2204
OH2
TIP

7
−17.966
101.207
−52.051
1.00
55.19

ATOM
2205
OH2
TIP

8
−14.825
102.146
−63.563
1.00
36.22

ATOM
2206
OH2
TIP

9
−12.646
109.426
−56.476
1.00
39.70

ATOM
2207
OH2
TIP

10
−26.220
112.515
−82.519
1.00
54.10

ATOM
2208
OH2
TIP

11
−21.056
96.909
−58.004
1.00
50.75

ATOM
2209
OH2
TIP

12
−12.363
100.866
−62.927
1.00
41.26

ATOM
2210
OH2
TIP

13
−1.321
111.343
−71.328
1.00
80.10

ATOM
2211
OH2
TIP

14
−15.955
100.816
−65.204
1.00
40.00

ATOM
2212
OH2
TIP

15
−38.264
94.351
−68.026
1.00
56.00

ATOM
2213
OH2
TIP

16
−34.747
103.092
−74.730
1.00
54.31

ATOM
2214
OH2
TIP

17
−36.658
81.314
−74.149
1.00
71.15

ATOM
2215
OH2
TIP

18
−16.949
98.679
−85.728
1.00
87.62

ATOM
2216
OH2
TIP

21
−18.846
109.431
−51.863
1.00
51.80

ATOM
2217
OH2
TIP

22
−19.808
89.557
−73.154
1.00
50.02

ATOM
2218
OH2
TIP

23
−15.508
95.436
−70.540
1.00
88.56

ATOM
2219
OH2
TIP

24
−14.481
98.173
−68.748
1.00
55.20

ATOM
2220
OH2
TIP

25
−12.701
111.957
−87.032
1.00
60.67

ATOM
2221
OH2
TIP

26
−16.126
117.347
−81.325
1.00
92.19

ATOM
2222
OH2
TIP

28
−32.498
88.797
−82.315
1.00
63.65

ATOM
2223
OH2
TIP

29
−27.830
77.286
−70.926
1.00
64.26

ATOM
2224
OH2
TIP

30
−18.104
75.804
−72.803
1.00
62.36

ATOM
2225
OH2
TIP

31
−4.498
114.218
−69.024
1.00
50.34

ATOM
2226
OH2
TIP

32
−27.549
116.364
−75.607
1.00
38.10

ATOM
2227
OH2
TIP

33
−20.441
122.193
−68.960
1.00
57.93

ATOM
2228
OH2
TIP

34
−38.352
98.016
−64.877
1.00
48.98

ATOM
2229
OH2
TIP

35
−25.169
109.804
−72.683
1.00
62.00

ATOM
2230
OH2
TIP

36
−15.952
120.584
−76.396
1.00
60.49

ATOM
2231
OH2
TIP

37
−31.772
109.042
−81.185
1.00
61.74

ATOM
2232
OH2
TIP

38
−26.023
117.180
−77.997
1.00
45.99

ATOM
2233
OH2
TIP

39
−30.417
119.656
−66.158
1.00
57.36

ATOM
2234
OH2
TIP

40
−31.769
114.324
−58.313
1.00
54.48

ATOM
2235
OH2
TIP

41
−21.640
114.988
−52.575
1.00
59.03

ATOM
2236
OH2
TIP

42
−46.473
91.759
−56.427
1.00
61.38

ATOM
2237
OH2
TIP

43
−42.689
114.142
−63.306
1.00
81.90

ATOM
2238
OH2
TIP

44
−14.015
126.468
−54.963
1.00
61.90

ATOM
2239
OH2
TIP

45
−27.585
121.073
−60.489
1.00
62.27

ATOM
2240
OH2
TIP

46
−16.865
101.333
−68.880
1.00
55.82

ATOM
2241
OH2
TIP

47
−34.735
117.310
−60.322
1.00
60.49

ATOM
2242
OH2
TIP

48
−9.234
93.074
−70.733
1.00
72.22

ATOM
2243
OH2
TIP

49
−40.289
91.726
−57.862
1.00
50.18

ATOM
2244
OH2
TIP

50
−9.221
112.888
−55.496
1.00
54.20

ATOM
2245
OH2
TIP

51
−38.906
112.515
−66.710
1.00
78.66

ATOM
2246
OH2
TIP

52
2.529
96.809
−74.765
1.00
69.23

ATOM
2247
OH2
TIP

53
−24.199
72.889
−78.644
1.00
59.85

ATOM
2248
OH2
TIP

54
−31.754
89.026
−72.509
1.00
62.94

ATOM
2249
OH2
TIP

55
−20.971
74.991
−59.317
1.00
61.24

ATOM
2250
OH2
TIP

56
−26.546
125.032
−70.146
1.00
62.26

ATOM
2251
OH2
TIP

57
−47.392
111.329
−65.455
1.00
63.14

ATOM
2252
OH2
TIP

58
−32.406
116.433
−73.716
1.00
52.36

ATOM
2253
OH2
TIP

59
−23.830
94.667
−52.040
1.00
75.89

ATOM
2254
OH2
TIP

60
−30.049
91.062
−63.135
1.00
59.19

ATOM
2255
OH2
TIP

61
−20.767
90.050
−71.065
1.00
61.77

ATOM
2256
OH2
TIP

62
−14.383
86.763
−62.584
1.00
66.17

ATOM
2257
OH2
TIP

63
−24.503
106.816
−84.818
1.00
46.19

ATOM
2258
OH2
TIP

64
−47.457
95.958
−60.114
1.00
64.05

ATOM
2259
OH2
TIP

65
−33.015
107.500
−54.598
1.00
57.09

ATOM
2260
OH2
TIP

66
−19.177
72.293
−58.651
1.00
65.08

ATOM
2261
OH2
TIP

67
−42.245
87.048
−85.668
1.00
80.22

ATOM
2262
OH2
TIP

68
−41.110
105.176
−75.745
1.00
55.61

ATOM
2263
OH2
TIP

69
−17.900
101.391
−73.416
1.00
50.26

ATOM
2264
OH2
TIP

70
−15.112
122.752
−72.280
1.00
62.23

ATOM
2265
OH2
TIP

71
−10.897
110.554
−88.353
1.00
59.35

ATOM
2266
OH2
TIP

72
−15.863
87.894
−40.536
1.00
76.19

ATOM
2267
OH2
TIP

73
−13.269
89.222
−73.978
1.00
72.37

ATOM
2268
OH2
TIP

74
−12.819
125.509
−83.766
1.00
61.65

ATOM
2269
OH2
TIP

75
−17.556
97.431
−73.936
1.00
45.20

ATOM
2270
OH2
TIP

76
2.814
106.071
−59.216
1.00
62.17

ATOM
2271
OH2
TIP

77
−20.096
74.736
−45.657
1.00
56.01

ATOM
2272
OH2
TIP

78
−12.837
81.660
−39.897
1.00
61.24

ATOM
2273
OH2
TIP

79
−6.887
83.385
−69.442
1.00
83.46

ATOM
2274
OH2
TIP

80
−40.679
99.898
−84.715
1.00
69.12

ATOM
2275
OH2
TIP

81
−17.993
123.292
−72.716
1.00
53.42

ATOM
2276
OH2
TIP

82
−46.988
106.360
−64.908
1.00
60.82

ATOM
2277
OH2
TIP

83
−6.977
83.446
−75.179
1.00
64.46

ATOM
2278
OH2
TIP

84
−15.030
112.332
−88.404
1.00
68.15

ATOM
2279
OH2
TIP

85
−40.535
89.123
−65.466
1.00
66.73

ATOM
2280
OH2
TIP

86
−23.943
109.923
−81.328
1.00
53.47

ATOM
2281
OH2
TIP

87
−28.039
92.419
−61.573
1.00
60.22

ATOM
2282
OH2
TIP

88
−13.595
91.555
−61.879
1.00
65.84

ATOM
2283
OH2
TIP

89
−16.436
81.809
−39.142
1.00
61.00

ATOM
2284
OH2
TIP

90
−7.960
78.226
−49.496
1.00
56.06

ATOM
2285
OH2
TIP

91
−27.922
85.717
−46.157
1.00
63.49

ATOM
2286
OH2
TIP

92
−25.252
85.080
−70.790
1.00
87.29

ATOM
2287
OH2
TIP

93
−44.520
99.048
−63.477
1.00
66.02

ATOM
2288
OH2
TIP

94
−14.400
81.735
−70.409
1.00
58.67

ATOM
2289
OH2
TIP

95
−22.737
126.809
−60.364
1.00
68.49

ATOM
2290
OH2
TIP

96
−36.302
116.540
−69.002
1.00
67.72

ATOM
2291
OH2
TIP

97
−9.993
98.758
−77.341
1.00
60.73

ATOM
2292
OH2
TIP

98
−5.198
107.622
−56.586
1.00
62.27

ATOM
2293
OH2
TIP

99
−42.156
87.741
−57.066
1.00
66.15

ATOM
2294
OH2
TIP

100
−24.999
97.737
−53.947
1.00
67.24

ATOM
2295
OH2
TIP

101
−34.330
85.565
−83.609
1.00
107.86

ATOM
2296
OH2
TIP

102
−46.299
88.604
−57.149
1.00
63.80

ATOM
2297
OH2
TIP

103
−41.265
81.337
−55.536
1.00
56.91

ATOM
2298
OH2
TIP

104
−26.510
109.042
−46.918
1.00
40.04

ATOM
2299
OH2
TIP

105
−40.249
113.287
−69.629
1.00
90.25

ATOM
2300
OH2
TIP

106
−8.724
94.018
−77.530
1.00
56.35

ATOM
2301
OH2
TIP

107
−25.587
92.031
−67.802
1.00
64.34

ATOM
2302
OH2
TIP

108
−6.596
117.195
−52.572
1.00
72.27

ATOM
2303
OH2
TIP

109
−10.888
107.185
−57.545
1.00
53.02

ATOM
2304
OH2
TIP

110
−0.502
119.304
−51.158
1.00
61.37

ATOM
2305
OH2
TIP

111
−1.110
111.586
−79.546
1.00
63.31

ATOM
2306
OH2
TIP

112
−9.865
114.401
−80.681
1.00
75.67

ATOM
2307
OH2
TIP

113
−46.370
79.300
−40.951
1.00
73.70

ATOM
2308
OH2
TIP

114
−29.421
87.726
−46.003
1.00
69.76

ATOM
2309
OH2
TIP

115
−3.726
84.683
−75.163
1.00
76.57

ATOM
2310
OH2
TIP

116
−40.377
85.114
−48.505
1.00
69.00

ATOM
2311
OH2
TIP

117
−43.021
94.888
−57.265
1.00
75.05

ATOM
2312
OH2
TIP

118
−26.757
89.010
−44.248
1.00
71.82

ATOM
2313
OH2
TIP

119
−26.088
90.870
−77.910
1.00
73.49

ATOM
2314
OH2
TIP

120
−51.720
94.496
−56.733
1.00
73.77

ATOM
2315
OH2
TIP

121
−22.597
90.054
−55.639
1.00
68.81

ATOM
2316
OH2
TIP

122
−48.699
74.961
−56.253
1.00
74.57

ATOM
2317
OH2
TIP

123
−48.606
76.242
−50.583
1.00
70.48

ATOM
2318
OH2
TIP

124
−34.958
81.995
−72.529
1.00
70.39

ATOM
2319
OH2
TIP
S
1
−24.874
75.096
−52.563
1.00
100.64
S

ATOM
2320
OH2
TIP
S
2
−27.640
116.193
−73.338
1.00
64.47
S

ATOM
2321
OH2
TIP
S
3
−33.593
103.889
−70.517
1.00
140.05
S

ATOM
2322
OH2
TIP
S
4
−6.592
112.901
−69.231
1.00
63.69
S

ATOM
2323
OH2
TIP
S
5
−29.756
115.038
−73.461
1.00
97.42
S

ATOM
2324
OH2
TIP
S
6
−38.105
119.752
−67.515
1.00
53.94
S

ATOM
2325
OH2
TIP
S
7
−32.981
119.061
−63.624
1.00
60.23
S

ATOM
2326
OH2
TIP
S
8
−35.040
108.034
−58.557
1.00
102.55
S

ATOM
2327
OH2
TIP
S
9
−31.599
98.109
−46.064
1.00
83.62
S

ATOM
2328
OH2
TIP
S
10
−28.319
116.523
−78.734
1.00
64.87
S

ATOM
2329
OH2
TIP
S
11
−17.321
112.989
−83.893
1.00
92.65
S

ATOM
2330
OH2
TIP
S
12
−24.476
91.578
−44.694
1.00
55.22
S

ATOM
2331
OH2
TIP
S
13
−29.554
118.607
−68.303
1.00
61.65
S

ATOM
2332
OH2
TIP
S
14
−16.299
98.303
−65.370
1.00
144.76
S

ATOM
2333
OH2
TIP
S
15
−1.478
95.998
−77.354
1.00
131.79
S

ATOM
2334
OH2
TIP
S
16
−29.686
102.563
−51.767
1.00
75.73
S

ATOM
2335
OH2
TIP
S
17
−36.744
110.842
−72.109
1.00
118.16
S

ATOM
2336
OH2
TIP
S
18
−29.348
79.309
−60.792
1.00
122.86
S

ATOM
2337
OH2
TIP
S
19
−34.282
105.373
−55.136
1.00
65.27
S

ATOM
2338
OH2
TIP
S
20
−30.975
89.345
−60.958
1.00
91.03
S

ATOM
2339
OH2
TIP
S
21
2.308
96.056
−77.529
1.00
85.89
S

ATOM
2340
OH2
TIP
S
22
−21.670
122.591
−62.938
1.00
78.79
S

ATOM
2341
OH2
TIP
S
23
−26.498
116.728
−56.181
1.00
62.33
S

ATOM
2342
OH2
TIP
S
24
−24.379
90.799
−69.404
1.00
120.16
S

ATOM
2343
OH2
TIP
S
25
−15.600
92.352
−50.584
1.00
63.36
S

ATOM
2344
OH2
TIP
S
26
−30.058
91.485
−47.678
1.00
68.28
S

ATOM
2345
OH2
TIP
S
27
−22.559
96.748
−63.089
1.00
149.69
S

ATOM
2346
OH2
TIP
S
28
−39.576
76.992
−44.850
1.00
64.31
S

ATOM
2347
OH2
TIP
S
29
−34.518
120.744
−73.343
1.00
119.94
S

ATOM
2348
OH2
TIP
S
30
−16.840
119.987
−56.087
1.00
126.22
S

ATOM
2349
OH2
TIP
S
31
−29.914
106.013
−81.685
1.00
60.80
S

ATOM
2350
OH2
TIP
S
32
−43.945
108.903
−62.310
1.00
61.73
S

ATOM
2351
OH2
TIP
S
33
−4.901
113.071
−67.218
1.00
86.69
S

ATOM
2352
OH2
TIP
S
34
−20.068
100.803
−74.311
1.00
130.96
S

ATOM
2353
OH2
TIP
S
35
−31.212
112.368
−60.484
1.00
63.96
S

ATOM
2354
OH2
TIP
S
36
−38.783
102.197
−60.426
1.00
61.22
S

ATOM
2355
OH2
TIP
S
37
−26.422
114.665
−76.950
1.00
142.66
S

ATOM
2356
OH2
TIP
S
38
−15.042
117.523
−50.310
1.00
81.99
S

ATOM
2357
OH2
TIP
S
39
−21.749
124.273
−64.985
1.00
53.70
S

ATOM
2358
OH2
TIP
S
40
−13.125
89.749
−52.101
1.00
66.80
S

ATOM
2359
OH2
TIP
S
41
−18.963
109.880
−54.656
1.00
121.15
S

ATOM
2360
OH2
TIP
S
42
−15.531
109.411
−73.950
1.00
108.80
S

ATOM
2361
OH2
TIP
S
43
−38.932
116.811
−62.960
1.00
87.34
S

ATOM
2362
OH2
TIP
S
44
−35.799
75.151
−68.750
1.00
68.27
S

ATOM
2363
OH2
TIP
S
45
−14.248
108.177
−52.675
1.00
57.76
S

ATOM
2364
OH2
TIP
S
46
−42.016
79.620
−57.106
1.00
58.01
S

ATOM
2365
OH2
TIP
S
47
−37.376
89.555
−73.417
1.00
56.77
S

ATOM
2366
OH2
TIP
S
48
−16.662
98.182
−50.524
1.00
72.07
S

ATOM
2367
OH2
TIP
S
49
−31.363
113.752
−80.911
1.00
115.84
S

ATOM
2368
OH2
TIP
S
50
−35.870
110.266
−74.588
1.00
86.77
S

ATOM
2369
OH2
TIP
S
51
−18.880
88.423
−71.504
1.00
71.73
S

ATOM
2370
OH2
TIP
S
52
−18.696
74.787
−59.072
1.00
96.03
S

ATOM
2371
OH2
TIP
S
53
−1.450
92.204
−72.489
1.00
82.54
S

ATOM
2372
OH2
TIP
S
54
−25.703
117.997
−74.653
1.00
140.68
S

ATOM
2373
OH2
TIP
S
55
−5.538
113.841
−87.337
1.00
63.97
S

ATOM
2374
OH2
TIP
S
56
−24.002
99.399
−87.296
1.00
70.42
S

ATOM
2375
OH2
TIP
S
57
−35.685
115.383
−71.829
1.00
59.90
S

ATOM
2376
OH2
TIP
S
58
−11.949
109.303
−85.222
1.00
64.78
S

ATOM
2377
OH2
TIP
S
59
−17.979
122.996
−70.462
1.00
66.48
S

ATOM
2378
OH2
TIP
S
60
−18.897
76.383
−47.330
1.00
69.81
S

ATOM
2379
OH2
TIP
S
61
−3.494
95.718
−66.750
1.00
57.69
S

ATOM
2380
OH2
TIP
S
62
−21.232
72.773
−60.409
1.00
101.51
S

ATOM
2381
OH2
TIP
S
63
−24.848
72.699
−43.896
1.00
69.30
S

ATOM
2382
OH2
TIP
S
64
−15.885
97.828
−71.257
1.00
110.31
S

ATOM
2383
OH2
TIP
S
65
−50.982
93.901
−66.391
1.00
77.23
S

ATOM
2384
OH2
TIP
S
66
−1.936
111.255
−73.689
1.00
117.10
S

ATOM
2385
OH2
TIP
S
67
−36.839
95.982
−64.530
1.00
66.26
S

ATOM
2386
OH2
TIP
S
68
−22.433
97.386
−85.175
1.00
60.50
S

ATOM
2387
OH2
TIP
S
69
−13.273
99.571
−64.786
1.00
80.33
S

ATOM
2388
OH2
TIP
S
70
−33.962
108.924
−56.388
1.00
134.83
S

ATOM
2389
OH2
TIP
S
71
−18.557
98.422
−71.902
1.00
99.04
S

ATOM
2390
OH2
TIP
S
72
−45.868
106.075
−62.475
1.00
70.05
S

ATOM
2391
OH2
TIP
S
73
−51.210
97.539
−68.618
1.00
66.94
S

ATOM
2392
OH2
TIP
S
74
−28.905
119.910
−72.319
1.00
87.40
S

ATOM
2393
OH2
TIP
S
75
−28.722
122.818
−67.249
1.00
79.82
S

ATOM
2394
OH2
TIP
S
76
0.389
101.944
−79.250
1.00
82.60
S

ATOM
2395
OH2
TIP
S
77
−46.387
108.440
−61.129
1.00
68.36
S

ATOM
2396
OH2
TIP
S
78
−7.776
89.350
−50.825
1.00
62.37
S

ATOM
2397
OH2
TIP
S
79
−49.244
72.524
−53.967
1.00
69.82
S

ATOM
2398
OH2
TIP
S
80
−15.802
77.724
−43.188
1.00
77.26
S

ATOM
2399
OH2
TIP
S
81
−20.198
84.415
−71.895
1.00
74.18
S

ATOM
2400
OH2
TIP
S
82
−17.441
96.031
−54.591
1.00
87.05
S

ATOM
2401
OH2
TIP
S
83
−13.713
79.061
−53.525
1.00
103.17
S

ATOM
2402
OH2
TIP
S
84
−10.825
80.730
−74.575
1.00
65.97
S

ATOM
2403
OH2
TIP
S
85
−10.354
92.500
−58.649
1.00
62.83
S

ATOM
2404
OH2
TIP
S
86
−23.321
115.846
−54.320
1.00
65.53
S

ATOM
2405
OH2
TIP
S
87
−16.844
106.078
−51.616
1.00
63.10
S

ATOM
2406
OH2
TIP
S
88
−8.169
131.138
−53.890
1.00
54.83
S

ATOM
2407
OH2
TIP
S
89
−21.698
115.219
−88.740
1.00
71.18
S

ATOM
2408
OH2
TIP
S
90
−16.070
109.682
−51.162
1.00
90.41
S

ATOM
2409
OH2
TIP
S
91
−49.578
96.512
−57.361
1.00
94.26
S

ATOM
2410
OH2
TIP
S
92
−25.989
115.973
−80.132
1.00
120.09
S

ATOM
2411
OH2
TIP
S
93
−25.659
128.045
−67.099
1.00
62.69
S

ATOM
2412
OH2
TIP
S
94
−58.940
73.355
−44.774
1.00
67.40
S

ATOM
2413
OH2
TIP
S
95
−7.341
139.735
−51.730
1.00
67.88
S

ATOM
2414
OH2
TIP
S
96
−4.375
111.380
−80.697
1.00
80.04
S

ATOM
2415
OH2
TIP
S
97
1.015
101.593
−74.683
1.00
95.35
S

ATOM
2416
OH2
TIP
S
98
−26.446
122.591
−69.117
1.00
62.28
S

ATOM
2417
OH2
TIP
S
99
−13.214
95.620
−57.763
1.00
59.86
S

ATOM
2418
OH2
TIP
S
100
−33.522
79.708
−82.091
1.00
61.83
S

ATOM
2419
OH2
TIP
S
101
−28.979
113.146
−60.493
1.00
64.27
S

ATOM
2420
OH2
TIP
S
102
−30.165
105.293
−68.877
1.00
129.21
S

ATOM
2421
OH2
TIP
S
103
−20.187
108.049
−60.809
1.00
95.32
S

ATOM
2422
OH2
TIP
S
104
−4.038
78.620
−74.193
1.00
66.01
S

ATOM
2423
OH2
TIP
S
105
−44.998
72.537
−48.705
1.00
66.95
S

ATOM
2424
OH2
TIP
S
106
−17.364
90.923
−76.639
1.00
85.80
S

ATOM
2425
OH2
TIP
S
107
−24.311
109.750
−67.949
1.00
125.44
S

ATOM
2426
OH2
TIP
S
108
−4.458
112.991
−71.248
1.00
80.75
S

ATOM
2427
OH2
TIP
S
109
−19.788
112.078
−52.627
1.00
73.74
S

ATOM
2428
OH2
TIP
S
110
−25.141
86.545
−46.263
1.00
73.13
S

ATOM
2429
OH2
TIP
S
111
−9.626
114.187
−70.875
1.00
47.58
S

ATOM
2430
OH2
TIP
S
112
−33.019
104.690
−82.096
1.00
65.61
S

ATOM
2431
OH2
TIP
S
113
−30.915
103.388
−49.239
1.00
74.91
S

ATOM
2432
OH2
TIP
S
114
−2.840
112.339
−68.829
1.00
106.76
S

ATOM
2433
OH2
TIP
S
115
−5.612
114.639
−65.699
1.00
93.56
S

ATOM
2434
OH2
TIP
S
116
−27.879
114.149
−71.735
1.00
131.93
S

ATOM
2435
OH2
TIP
S
117
−19.800
76.358
−64.870
1.00
86.29
S

ATOM
2436
OH2
TIP
S
118
−6.170
112.309
−79.263
1.00
127.11
S

ATOM
2437
OH2
TIP
S
119
−17.424
93.166
−52.153
1.00
116.00
S

ATOM
2438
OH2
TIP
S
120
−6.256
114.887
−70.663
1.00
94.77
S

ATOM
2439
OH2
TIP
S
121
−5.429
109.637
−82.500
1.00
107.88
S

ATOM
2440
OH2
TIP
S
122
−9.489
110.380
−84.271
1.00
96.46
S

ATOM
2441
OH2
TIP
S
123
−34.145
116.425
−70.273
1.00
113.00
S

ATOM
2442
OH2
TIP
S
124
−8.365
114.107
−78.064
1.00
92.92
S

ATOM
2443
OH2
TIP
S
125
−20.890
121.095
−65.288
1.00
97.32
S

ATOM
2444
OH2
TIP
S
126
−26.405
122.091
−66.588
1.00
118.46
S

ATOM
2445
OH2
TIP
S
127
−38.874
104.293
−58.332
1.00
97.42
S

ATOM
2446
OH2
TIP
S
128
−14.102
135.951
−44.531
1.00
71.88
S

ATOM
2447
OH2
TIP
S
129
−21.085
97.000
−78.847
1.00
87.18
S

ATOM
2448
OH2
TIP
S
130
−17.557
111.295
−88.049
1.00
92.93
S

ATOM
2449
OH2
TIP
S
131
−20.722
89.291
−49.320
1.00
68.70
S

ATOM
2450
OH2
TIP
S
132
−35.203
83.232
−65.991
1.00
127.96
S

ATOM
2451
OH2
TIP
S
133
1.796
94.625
−79.513
1.00
110.26
S

ATOM
2452
OH2
TIP
S
134
−32.464
106.775
−81.054
1.00
134.58
S

ATOM
2453
OH2
TIP
S
135
−17.472
75.316
−55.073
1.00
67.49
S

ATOM
2454
OH2
TIP
S
136
−45.283
112.927
−67.518
1.00
87.86
S

ATOM
2455
OH2
TIP
S
137
−35.109
94.164
−63.986
1.00
86.94
S

ATOM
2456
OH2
TIP
S
138
−16.086
89.526
−50.510
1.00
70.01
S

ATOM
2457
OH2
TIP
S
139
−23.362
108.488
−64.225
1.00
154.27
S

ATOM
2458
OH2
TIP
S
140
−43.122
87.160
−66.507
1.00
98.37
S

ATOM
2459
OH2
TIP
S
141
−2.776
109.674
−79.736
1.00
95.96
S

ATOM
2460
OH2
TIP
S
142
−15.663
95.312
−52.990
1.00
83.86
S

ATOM
2461
OH2
TIP
S
143
−14.744
122.625
−70.042
1.00
100.44
S

ATOM
2462
OH2
TIP
S
144
−28.506
117.021
−70.975
1.00
124.41
S

ATOM
2463
OH2
TIP
S
145
−27.738
90.826
−49.482
1.00
110.44
S

ATOM
2464
OH2
TIP
S
146
−28.136
120.622
−65.210
1.00
96.26
S

ATOM
2465
OH2
TIP
S
147
−20.842
71.154
−62.384
1.00
111.91
S

ATOM
2466
OH2
TIP
S
148
−20.450
74.731
−48.346
1.00
147.09
S

ATOM
2467
OH2
TIP
S
149
−49.750
90.607
−50.890
1.00
70.14
S

ATOM
2468
OH2
TIP
S
150
−25.722
76.682
−66.927
1.00
83.48
S

ATOM
2469
OH2
TIP
S
151
−10.014
90.765
−70.005
1.00
67.99
S

ATOM
2470
OH2
TIP
S
152
−23.364
92.000
−46.848
1.00
116.71
S

ATOM
2471
OH2
TIP
S
153
−49.912
95.518
−54.399
1.00
80.82
S

ATOM
2472
OH2
TIP
S
154
−8.294
109.516
−68.131
1.00
130.96
S

ATOM
2473
OH2
TIP
S
155
−35.512
119.480
−62.035
1.00
92.04
S

ATOM
2474
OH2
TIP
S
156
−7.634
97.609
−77.316
1.00
70.83
S

ATOM
2475
OH2
TIP
S
157
−17.429
105.471
−57.223
1.00
106.41
S

ATOM
2476
OH2
TIP
S
158
−16.526
98.965
−54.259
1.00
76.99
S

ATOM
2477
OH2
TIP
S
159
−11.631
105.626
−81.492
1.00
72.26
S

ATOM
2478
OH2
TIP
S
160
−59.947
80.639
−42.270
1.00
76.82
S

ATOM
2479
OH2
TIP
S
161
−26.927
80.699
−78.815
1.00
68.78
S

ATOM
2480
OH2
TIP
S
162
−4.676
96.323
−52.755
1.00
73.60
S

ATOM
2481
OH2
TIP
S
163
−27.740
95.995
−59.978
1.00
102.27
S

ATOM
2482
OH2
TIP
S
164
−8.963
82.489
−73.329
1.00
78.96
S

ATOM
2483
OH2
TIP
S
165
−39.727
100.726
−66.210
1.00
67.68
S

ATOM
2484
OH2
TIP
S
166
−11.859
106.429
−87.378
1.00
84.13
S

ATOM
2485
OH2
TIP
S
167
−18.852
85.938
−39.462
1.00
70.52
S

ATOM
2486
OH2
TIP
S
168
−0.694
110.380
−68.264
1.00
69.04
S

ATOM
2487
OH2
TIP
S
169
−38.128
78.343
−75.080
1.00
65.00
S

ATOM
2488
OH2
TIP
S
170
−46.764
91.241
−66.819
1.00
74.30
S

ATOM
2489
OH2
TIP
S
171
3.183
99.399
−79.141
1.00
128.67
S

ATOM
2490
OH2
TIP
S
172
−63.975
70.259
−33.320
1.00
65.69
S

ATOM
2491
OH2
TIP
S
173
−11.493
123.888
−52.294
1.00
79.10
S

ATOM
2492
OH2
TIP
S
174
−27.059
111.341
−70.316
1.00
150.68
S

ATOM
2493
OH2
TIP
S
175
−15.936
88.989
−62.024
1.00
97.30
S

ATOM
2494
OH2
TIP
S
176
−14.875
100.243
−85.307
1.00
87.07
S

ATOM
2495
OH2
TIP
S
177
−18.037
70.966
−56.508
1.00
77.36
S

ATOM
2496
OH2
TIP
S
178
−6.470
80.004
−76.016
1.00
71.26
S

ATOM
2497
OH2
TIP
S
179
−49.811
109.689
−67.021
1.00
63.51
S

ATOM
2498
OH2
TIP
S
180
−40.676
92.496
−84.033
1.00
64.95
S

ATOM
2499
OH2
TIP
S
181
−18.587
98.632
−52.482
1.00
90.86
S

ATOM
2500
OH2
TIP
S
182
−17.583
119.509
−49.763
1.00
70.51
S

ATOM
2501
OH2
TIP
S
183
−11.655
73.314
−55.139
1.00
75.57
S

ATOM
2502
OH2
TIP
S
184
−9.477
87.156
−65.728
1.00
60.46
S

ATOM
2503
OH2
TIP
S
185
−13.688
110.861
−90.110
1.00
94.57
S

ATOM
2504
OH2
TIP
S
186
−23.785
112.222
−71.430
1.00
136.94
S

ATOM
2505
OH2
TIP
S
187
−39.708
96.995
−50.710
1.00
81.92
S

ATOM
2506
OH2
TIP
S
188
−36.265
93.471
−86.062
1.00
69.78
S

ATOM
2507
OH2
TIP
S
189
−13.807
119.103
−74.658
1.00
124.21
S

ATOM
2508
OH2
TIP
S
190
2.032
95.724
−83.054
1.00
74.44
S

ATOM
2509
OH2
TIP
S
191
−33.006
112.815
−70.272
1.00
113.66
S

ATOM
2510
OH2
TIP
S
192
−40.901
76.884
−74.050
1.00
86.83
S

ATOM
2511
OH2
TIP
S
193
−46.882
97.000
−55.824
1.00
65.96
S

ATOM
2512
OH2
TIP
S
194
−15.147
95.684
−76.401
1.00
95.85
S

ATOM
2513
OH2
TIP
S
195
−13.498
80.649
−60.434
1.00
102.97
S

ATOM
2514
OH2
TIP
S
196
−22.522
78.860
−64.110
1.00
121.19
S

ATOM
2515
OH2
TIP
S
197
−29.314
84.793
−82.436
1.00
84.45
S

END

[0491]

15

TABLE 4

Coordinate data for ΔPH-PKBβ-ΔC

CRYST1 149.703 149.703 39.185 90.00 90.00 90.00 P 41 21 2

REMARK FILENAME = “dph-pkb-dc.pdb”

REMARK DATE: 30-Nov-01 15:41:04

REMARK VERSION: 1.1

ATOM
1
CB
ALA

146
−38.368
81.177
−47.423
1.00
72.10

ATOM
2
C
ALA

146
−38.291
81.513
−49.914
1.00
73.26

ATOM
3
O
ALA

146
−38.678
80.383
−50.231
1.00
74.20

ATOM
4
N
ALA

146
−40.134
82.542
−48.532
1.00
72.62

ATOM
5
CA
ALA

146
−38.688
82.145
−48.572
1.00
73.27

ATOM
6
N
ALA

147
−37.512
82.257
−50.696
1.00
72.37

ATOM
7
CA
ALA

147
−37.051
81.793
−51.995
1.00
70.36

ATOM
8
CB
ALA

147
−36.169
82.851
−52.631
1.00
70.01

ATOM
9
C
ALA

147
−36.275
80.488
−51.849
1.00
69.01

ATOM
10
O
ALA

147
−35.807
80.142
−50.764
1.00
68.52

ATOM
11
N
THR

148
−36.147
79.771
−52.957
1.00
67.57

ATOM
12
CA
THR

148
−35.416
78.514
−52.995
1.00
66.30

ATOM
13
CB
THR

148
−36.130
77.423
−52.159
1.00
66.09

ATOM
14
OG1
THR

148
−35.396
77.229
−50.947
1.00
67.43

ATOM
15
CG2
THR

148
−36.220
76.101
−52.907
1.00
64.34

ATOM
16
C
THR

148
−35.268
78.077
−54.443
1.00
66.26

ATOM
17
O
THR

148
−36.141
78.339
−55.271
1.00
65.96

ATOM
18
N
MET

149
−34.154
77.424
−54.746
1.00
65.69

ATOM
19
CA
MET

149
−33.882
76.969
−56.099
1.00
65.90

ATOM
20
CB
MET

149
−32.779
75.923
−56.075
1.00
65.89

ATOM
21
CG
MET

149
−31.452
76.489
−55.657
1.00
66.44

ATOM
22
SD
MET

149
−30.870
77.680
−56.856
1.00
65.10

ATOM
23
CE
MET

149
−29.158
77.222
−56.912
1.00
67.52

ATOM
24
C
MET

149
−35.098
76.405
−56.805
1.00
66.12

ATOM
25
O
MET

149
−35.324
76.688
−57.980
1.00
66.35

ATOM
26
N
ASN

150
−35.886
75.619
−56.077
1.00
66.02

ATOM
27
CA
ASN

150
−37.073
74.989
−56.641
1.00
65.30

ATOM
28
CB
ASN

150
−37.574
73.882
−55.718
1.00
64.72

ATOM
29
CG
ASN

150
−38.585
72.996
−56.399
1.00
66.37

ATOM
30
OD1
ASN

150
−39.424
72.371
−55.753
1.00
68.35

ATOM
31
ND2
ASN

150
−38.510
72.932
−57.725
1.00
66.81

ATOM
32
C
ASN

150
−38.231
75.947
−56.964
1.00
64.97

ATOM
33
O
ASN

150
−39.215
75.552
−57.591
1.00
64.68

ATOM
34
N
ASP

151
−38.125
77.199
−56.539
1.00
64.20

ATOM
35
CA
ASP

151
−39.173
78.152
−56.831
1.00
64.01

ATOM
36
CB
ASP

151
−39.178
79.279
−55.800
1.00
65.85

ATOM
37
CG
ASP

151
−39.625
78.816
−54.426
1.00
67.83

ATOM
38
OD1
ASP

151
−40.580
78.011
−54.361
1.00
69.12

ATOM
39
OD2
ASP

151
−39.041
79.268
−53.413
1.00
68.47

ATOM
40
C
ASP

151
−38.979
78.746
−58.221
1.00
63.35

ATOM
41
O
ASP

151
−39.803
79.536
−58.679
1.00
63.55

ATOM
42
N
PHE

152
−37.901
78.359
−58.902
1.00
62.43

ATOM
43
CA
PHE

152
−37.608
78.904
−60.233
1.00
61.46

ATOM
44
CB
PHE

152
−36.387
79.842
−60.174
1.00
60.80

ATOM
45
CG
PHE

152
−36.484
80.896
−59.123
1.00
59.27

ATOM
46
CD1
PHE

152
−37.244
82.029
−59.333
1.00
58.29

ATOM
47
CD2
PHE

152
−35.878
80.714
−57.887
1.00
59.08

ATOM
48
CE1
PHE

152
−37.411
82.968
−58.324
1.00
58.92

ATOM
49
CE2
PHE

152
−36.041
81.641
−56.877
1.00
58.79

ATOM
50
CZ
PHE

152
−36.813
82.773
−57.095
1.00
58.93

ATOM
51
C
PHE

152
−37.331
77.865
−61.313
1.00
61.40

ATOM
52
O
PHE

152
−36.913
76.734
−61.028
1.00
61.27

ATOM
53
N
ASP

153
−37.551
78.281
−62.560
1.00
59.89

ATOM
54
CA
ASP

153
−37.298
77.449
−63.723
1.00
58.75

ATOM
55
CB
ASP

153
−38.509
77.446
−64.667
1.00
62.22

ATOM
56
CG
ASP

153
−39.670
76.575
−64.156
1.00
63.93

ATOM
57
OD1
ASP

153
−39.507
75.338
−64.029
1.00
63.98

ATOM
58
OD2
ASP

153
−40.755
77.136
−63.888
1.00
64.53

ATOM
59
C
ASP

153
−36.089
78.019
−64.461
1.00
57.30

ATOM
60
O
ASP

153
−35.975
79.234
−64.644
1.00
57.33

ATOM
61
N
TYR

154
−35.190
77.136
−64.881
1.00
55.23

ATOM
62
CA
TYR

154
−33.995
77.530
−65.611
1.00
53.89

ATOM
63
CB
TYR

154
−32.969
76.411
−65.565
1.00
51.68

ATOM
64
CG
TYR

154
−31.788
76.648
−66.476
1.00
52.25

ATOM
65
CD1
TYR

154
−30.763
77.530
−66.124
1.00
53.16

ATOM
66
CE1
TYR

154
−29.662
77.724
−66.960
1.00
52.88

ATOM
67
CD2
TYR

154
−31.681
75.976
−67.679
1.00
51.34

ATOM
68
CE2
TYR

154
−30.593
76.154
−68.511
1.00
52.96

ATOM
69
CZ
TYR

154
−29.583
77.022
−68.154
1.00
53.56

ATOM
70
OH
TYR

154
−28.485
77.141
−68.987
1.00
54.21

ATOM
71
C
TYR

154
−34.306
77.835
−67.071
1.00
54.58

ATOM
72
O
TYR

154
−35.036
77.099
−67.710
1.00
58.05

ATOM
73
N
LEU

155
−33.758
78.913
−67.611
1.00
54.64

ATOM
74
CA
LEU

155
−33.990
79.234
−69.011
1.00
53.24

ATOM
75
CB
LEU

155
−34.665
80.590
−69.164
1.00
52.10

ATOM
76
CG
LEU

155
−36.138
80.449
−68.807
1.00
52.18

ATOM
77
CD1
LEU

155
−36.824
81.788
−68.842
1.00
53.57

ATOM
78
CD2
LEU

155
−36.782
79.508
−69.785
1.00
53.33

ATOM
79
C
LEU

155
−32.681
79.226
−69.744
1.00
53.55

ATOM
80
O
LEU

155
−32.469
78.417
−70.643
1.00
53.03

ATOM
81
N
LYS

156
−31.781
80.118
−69.371
1.00
53.89

ATOM
82
CA
LYS

156
−30.513
80.114
−70.058
1.00
55.50

ATOM
83
CB
LYS

156
−30.667
80.746
−71.443
1.00
56.37

ATOM
84
CG
LYS

156
−31.083
82.208
−71.429
1.00
57.54

ATOM
85
CD
LYS

156
−30.759
82.836
−72.769
1.00
58.31

ATOM
86
CE
LYS

156
−30.520
84.321
−72.634
1.00
57.68

ATOM
87
NZ
LYS

156
−29.917
84.844
−73.888
1.00
58.86

ATOM
88
C
LYS

156
−29.402
80.799
−69.297
1.00
56.19

ATOM
89
O
LYS

156
−29.629
81.458
−68.278
1.00
55.60

ATOM
90
N
LEU

157
−28.188
80.623
−69.795
1.00
57.43

ATOM
91
CA
LEU

157
−27.050
81.243
−69.168
1.00
59.59

ATOM
92
CB
LEU

157
−25.772
80.504
−69.533
1.00
58.98

ATOM
93
CG
LEU

157
−24.501
81.061
−68.892
1.00
58.30

ATOM
94
CD1
LEU

157
−24.764
81.446
−67.457
1.00
58.21

ATOM
95
CD2
LEU

157
−23.406
80.017
−68.963
1.00
58.74

ATOM
96
C
LEU

157
−26.969
82.672
−69.666
1.00
61.07

ATOM
97
O
LEU

157
−27.146
82.927
−70.857
1.00
61.45

ATOM
98
N
LEU

158
−26.729
83.597
−68.743
1.00
61.77

ATOM
99
CA
LEU

158
−26.603
85.004
−69.074
1.00
63.79

ATOM
100
CB
LEU

158
−27.477
85.862
−68.161
1.00
63.54

ATOM
101
CG
LEU

158
−28.985
85.959
−68.361
1.00
62.03

ATOM
102
CD1
LEU

158
−29.582
86.501
−67.080
1.00
63.45

ATOM
103
CD2
LEU

158
−29.331
86.859
−69.536
1.00
61.08

ATOM
104
C
LEU

158
−25.155
85.409
−68.878
1.00
65.26

ATOM
105
O
LEU

158
−24.663
86.298
−69.564
1.00
64.54

ATOM
106
N
GLY

159
−24.474
84.760
−67.934
1.00
68.01

ATOM
107
CA
GLY

159
−23.078
85.091
−67.678
1.00
71.21

ATOM
108
C
GLY

159
−22.361
84.198
−66.678
1.00
73.75

ATOM
109
O
GLY

159
−22.970
83.688
−65.736
1.00
73.94

ATOM
110
N
LYS

160
−21.058
84.016
−66.883
1.00
76.25

ATOM
111
CA
LYS

160
−20.222
83.178
−66.011
1.00
78.92

ATOM
112
CB
LYS

160
−19.635
82.023
−66.851
1.00
78.80

ATOM
113
CG
LYS

160
−19.312
80.735
−66.086
1.00
79.84

ATOM
114
CD
LYS

160
−18.660
79.651
−66.992
1.00
79.69

ATOM
115
CE
LYS

160
−18.214
78.394
−66.183
1.00
79.04

ATOM
116
NZ
LYS

160
−17.218
77.517
−66.886
1.00
75.82

ATOM
117
C
LYS

160
−19.096
84.059
−65.399
1.00
80.46

ATOM
118
O
LYS

160
−19.049
85.271
−65.647
1.00
81.00

ATOM
119
N
GLY

161
−18.199
83.481
−64.597
1.00
81.61

ATOM
120
CA
GLY

161
−17.131
84.301
−64.032
1.00
82.86

ATOM
121
C
GLY

161
−16.242
83.756
−62.918
1.00
83.67

ATOM
122
O
GLY

161
−16.419
82.639
−62.426
1.00
83.60

ATOM
123
N
THR

162
−15.273
84.573
−62.519
1.00
84.29

ATOM
124
CA
THR

162
−14.335
84.215
−61.460
1.00
85.61

ATOM
125
CB
THR

162
−13.167
85.245
−61.391
1.00
87.59

ATOM
126
OG1
THR

162
−13.056
85.934
−62.648
1.00
89.49

ATOM
127
CG2
THR

162
−11.837
84.543
−61.087
1.00
88.57

ATOM
128
C
THR

162
−15.080
84.230
−60.122
1.00
84.92

ATOM
129
O
THR

162
−14.579
83.753
−59.105
1.00
84.61

ATOM
130
N
PHE

163
−16.286
84.786
−60.148
1.00
84.72

ATOM
131
CA
PHE

163
−17.145
84.914
−58.968
1.00
84.07

ATOM
132
CB
PHE

163
−17.718
86.338
−58.947
1.00
84.30

ATOM
133
CG
PHE

163
−18.371
86.753
−60.251
1.00
85.54

ATOM
134
CD1
PHE

163
−19.759
86.669
−60.419
1.00
85.14

ATOM
135
CD2
PHE

163
−17.597
87.221
−61.315
1.00
85.78

ATOM
136
CE1
PHE

163
−20.371
87.048
−61.623
1.00
85.09

ATOM
137
CE2
PHE

163
−18.197
87.602
−62.526
1.00
86.86

ATOM
138
CZ
PHE

163
−19.591
87.516
−62.677
1.00
86.20

ATOM
139
C
PHE

163
−18.291
83.867
−58.929
1.00
82.93

ATOM
140
O
PHE

163
−18.651
83.340
−57.864
1.00
82.41

ATOM
141
N
GLY

164
−18.849
83.573
−60.100
1.00
80.55

ATOM
142
CA
GLY

164
−19.936
82.618
−60.202
1.00
77.40

ATOM
143
C
GLY

164
−20.599
82.701
−61.569
1.00
75.05

ATOM
144
O
GLY

164
−19.925
82.648
−62.606
1.00
75.87

ATOM
145
N
LYS

165
−21.918
82.836
−61.593
1.00
72.00

ATOM
146
CA
LYS

165
−22.593
82.923
−62.871
1.00
68.85

ATOM
147
CB
LYS

165
−22.699
81.524
−63.488
1.00
70.37

ATOM
148
CG
LYS

165
−23.766
80.630
−62.864
1.00
71.00

ATOM
149
CD
LYS

165
−23.663
79.198
−63.358
1.00
72.16

ATOM
150
CE
LYS

165
−22.585
78.449
−62.588
1.00
74.70

ATOM
151
NZ
LYS

165
−22.532
77.000
−62.927
1.00
76.05

ATOM
152
C
LYS

165
−23.974
83.524
−62.712
1.00
66.56

ATOM
153
O
LYS

165
−24.522
83.553
−61.610
1.00
65.74

ATOM
154
N
VAL

166
−24.520
84.027
−63.815
1.00
63.53

ATOM
155
CA
VAL

166
−25.862
84.583
−63.803
1.00
61.12

ATOM
156
CB
VAL

166
−25.894
86.080
−64.173
1.00
62.20

ATOM
157
CG1
VAL

166
−27.339
86.566
−64.227
1.00
61.08

ATOM
158
CG2
VAL

166
−25.120
86.891
−63.135
1.00
62.28

ATOM
159
C
VAL

166
−26.689
83.792
−64.798
1.00
58.96

ATOM
160
O
VAL

166
−26.345
83.686
−65.972
1.00
56.35

ATOM
161
N
ILE

167
−27.771
83.224
−64.282
1.00
58.40

ATOM
162
CA
ILE

167
−28.714
82.403
−65.026
1.00
57.37

ATOM
163
CB
ILE

167
−29.121
81.170
−64.170
1.00
56.62

ATOM
164
CG2
ILE

167
−30.181
80.366
−64.857
1.00
58.67

ATOM
165
CG1
ILE

167
−27.922
80.276
−63.941
1.00
56.70

ATOM
166
CD1
ILE

167
−27.326
79.765
−65.237
1.00
57.59

ATOM
167
C
ILE

167
−29.968
83.229
−65.287
1.00
56.93

ATOM
168
O
ILE

167
−30.276
84.155
−64.533
1.00
57.78

ATOM
169
N
LEU

168
−30.682
82.913
−66.359
1.00
55.71

ATOM
170
CA
LEU

168
−31.942
83.588
−66.656
1.00
55.34

ATOM
171
CB
LEU

168
−32.086
83.818
−68.159
1.00
54.97

ATOM
172
CG
LEU

168
−33.334
84.504
−68.725
1.00
55.00

ATOM
173
CD1
LEU

168
−33.637
85.838
−68.041
1.00
54.88

ATOM
174
CD2
LEU

168
−33.073
84.724
−70.197
1.00
55.25

ATOM
175
C
LEU

168
−32.981
82.577
−66.186
1.00
55.65

ATOM
176
O
LEU

168
−33.072
81.488
−66.750
1.00
56.14

ATOM
177
N
VAL

169
−33.743
82.914
−65.149
1.00
56.28

ATOM
178
CA
VAL

169
−34.744
81.991
−64.606
1.00
56.68

ATOM
179
CB
VAL

169
−34.394
81.567
−63.153
1.00
55.72

ATOM
180
CG1
VAL

169
−33.016
80.927
−63.105
1.00
53.79

ATOM
181
CG2
VAL

169
−34.444
82.776
−62.231
1.00
52.73

ATOM
182
C
VAL

169
−36.133
82.605
−64.575
1.00
58.31

ATOM
183
O
VAL

169
−36.277
83.810
−64.750
1.00
57.96

ATOM
184
N
ARG

170
−37.145
81.771
−64.335
1.00
60.42

ATOM
185
CA
ARG

170
−38.535
82.222
−64.256
1.00
62.62

ATOM
186
CB
ARG

170
−39.344
81.620
−65.405
1.00
64.57

ATOM
187
CG
ARG

170
−40.685
82.328
−65.671
1.00
68.47

ATOM
188
CD
ARG

170
−41.696
81.470
−66.464
1.00
69.77

ATOM
189
NE
ARG

170
−41.088
80.712
−67.562
1.00
71.23

ATOM
190
CZ
ARG

170
−40.826
79.406
−67.514
1.00
71.25

ATOM
191
NH1
ARG

170
−41.122
78.706
−66.424
1.00
70.34

ATOM
192
NH2
ARG

170
−40.259
78.802
−68.553
1.00
70.83

ATOM
193
C
ARG

170
−39.198
81.813
−62.930
1.00
63.43

ATOM
194
O
ARG

170
−39.399
80.632
−62.688
1.00
64.23

ATOM
195
N
GLU

171
−39.541
82.774
−62.074
1.00
64.60

ATOM
196
CA
GLU

171
−40.199
82.444
−60.809
1.00
66.03

ATOM
197
CB
GLU

171
−40.527
83.720
−60.014
1.00
66.33

ATOM
198
CG
GLU

171
−41.455
83.497
−58.804
1.00
66.72

ATOM
199
CD
GLU

171
−41.511
84.693
−57.842
1.00
67.61

ATOM
200
OE1
GLU

171
−41.639
85.855
−58.311
1.00
66.75

ATOM
201
OE2
GLU

171
−41.442
84.457
−56.612
1.00
65.68

ATOM
202
C
GLU

171
−41.481
81.669
−61.118
1.00
67.13

ATOM
203
O
GLU

171
−42.431
82.226
−61.680
1.00
67.09

ATOM
204
N
LYS

172
−41.510
80.391
−60.734
1.00
67.98

ATOM
205
CA
LYS

172
−42.655
79.523
−61.011
1.00
68.77

ATOM
206
CB
LYS

172
−42.374
78.107
−60.511
1.00
67.84

ATOM
207
CG
LYS

172
−41.981
77.172
−61.634
1.00
68.40

ATOM
208
CD
LYS

172
−41.645
75.766
−61.157
1.00
68.66

ATOM
209
CE
LYS

172
−40.306
75.704
−60.454
1.00
68.13

ATOM
210
NZ
LYS

172
−40.126
74.417
−59.745
1.00
66.77

ATOM
211
C
LYS

172
−44.046
79.951
−60.548
1.00
69.73

ATOM
212
O
LYS

172
−45.037
79.630
−61.199
1.00
69.61

ATOM
213
N
ALA

173
−44.139
80.663
−59.433
1.00
71.28

ATOM
214
CA
ALA

173
−45.449
81.089
−58.949
1.00
72.19

ATOM
215
CB
ALA

173
−45.330
81.689
−57.545
1.00
72.40

ATOM
216
C
ALA

173
−46.046
82.115
−59.899
1.00
72.23

ATOM
217
O
ALA

173
−47.053
81.856
−60.564
1.00
71.61

ATOM
218
N
THR

174
−45.400
83.276
−59.960
1.00
71.76

ATOM
219
CA
THR

174
−45.858
84.365
−60.799
1.00
71.25

ATOM
220
CB
THR

174
−45.088
85.660
−60.488
1.00
71.18

ATOM
221
OG1
THR

174
−43.845
85.668
−61.195
1.00
70.70

ATOM
222
CG2
THR

174
−44.804
85.756
−58.998
1.00
71.39

ATOM
223
C
THR

174
−45.712
84.044
−62.278
1.00
71.45

ATOM
224
O
THR

174
−46.703
83.867
−62.989
1.00
73.06

ATOM
225
N
GLY

175
−44.475
83.955
−62.737
1.00
71.40

ATOM
226
CA
GLY

175
−44.224
83.682
−64.134
1.00
71.12

ATOM
227
C
GLY

175
−43.263
84.738
−64.624
1.00
71.06

ATOM
228
O
GLY

175
−42.784
84.680
−65.757
1.00
71.69

ATOM
229
N
ARG

176
−42.979
85.703
−63.752
1.00
70.93

ATOM
230
CA
ARG

176
−42.067
86.795
−64.063
1.00
72.13

ATOM
231
CB
ARG

176
−42.083
87.836
−62.930
1.00
75.41

ATOM
232
CG
ARG

176
−43.441
88.495
−62.650
1.00
79.99

ATOM
233
CD
ARG

176
−43.962
89.314
−63.842
1.00
84.22

ATOM
234
NE
ARG

176
−45.334
89.793
−63.623
1.00
87.99

ATOM
235
CZ
ARG

176
−46.092
90.395
−64.543
1.00
88.86

ATOM
236
NH1
ARG

176
−45.625
90.607
−65.772
1.00
89.64

ATOM
237
NH2
ARG

176
−47.327
90.783
−64.233
1.00
88.39

ATOM
238
C
ARG

176
−40.636
86.271
−64.272
1.00
71.38

ATOM
239
O
ARG

176
−40.294
85.178
−63.818
1.00
71.09

ATOM
240
N
TYR

177
−39.805
87.067
−64.948
1.00
69.68

ATOM
241
CA
TYR

177
−38.419
86.701
−65.242
1.00
67.28

ATOM
242
CB
TYR

177
−38.129
86.903
−66.727
1.00
67.29

ATOM
243
CG
TYR

177
−38.865
85.978
−67.648
1.00
68.57

ATOM
244
CD1
TYR

177
−40.249
85.907
−67.637
1.00
68.90

ATOM
245
CE1
TYR

177
−40.925
85.056
−68.498
1.00
69.12

ATOM
246
CD2
TYR

177
−38.174
85.168
−68.542
1.00
69.83

ATOM
247
CE2
TYR

177
−38.845
84.318
−69.406
1.00
69.44

ATOM
248
CZ
TYR

177
−40.214
84.266
−69.374
1.00
68.87

ATOM
249
OH
TYR

177
−40.877
83.426
−70.226
1.00
70.45

ATOM
250
C
TYR

177
−37.363
87.476
−64.456
1.00
66.16

ATOM
251
O
TYR

177
−37.376
88.712
−64.406
1.00
65.73

ATOM
252
N
TYR

178
−36.430
86.741
−63.865
1.00
65.15

ATOM
253
CA
TYR

178
−35.342
87.359
−63.121
1.00
63.26

ATOM
254
CB
TYR

178
−35.492
87.108
−61.622
1.00
62.91

ATOM
255
CG
TYR

178
−36.817
87.567
−61.062
1.00
63.24

ATOM
256
CD1
TYR

178
−37.991
86.857
−61.327
1.00
63.61

ATOM
257
CE1
TYR

178
−39.225
87.300
−60.850
1.00
63.23

ATOM
258
CD2
TYR

178
−36.909
88.734
−60.299
1.00
63.38

ATOM
259
CE2
TYR

178
−38.137
89.183
−59.819
1.00
63.89

ATOM
260
CZ
TYR

178
−39.289
88.459
−60.100
1.00
63.86

ATOM
261
OH
TYR

178
−40.506
88.893
−59.632
1.00
66.00

ATOM
262
C
TYR

178
−34.017
86.785
−63.598
1.00
62.05

ATOM
263
O
TYR

178
−33.967
85.775
−64.303
1.00
61.10

ATOM
264
N
ALA

179
−32.943
87.460
−63.241
1.00
60.77

ATOM
265
CA
ALA

179
−31.630
86.987
−63.606
1.00
60.99

ATOM
266
CB
ALA

179
−30.807
88.114
−64.165
1.00
62.12

ATOM
267
C
ALA

179
−31.083
86.550
−62.274
1.00
60.52

ATOM
268
O
ALA

179
−31.094
87.339
−61.327
1.00
60.98

ATOM
269
N
MET

180
−30.627
85.304
−62.179
1.00
59.47

ATOM
270
CA
MET

180
−30.104
84.818
−60.909
1.00
57.96

ATOM
271
CB
MET

180
−30.636
83.436
−60.591
1.00
55.07

ATOM
272
CG
MET

180
−30.452
83.096
−59.142
1.00
53.62

ATOM
273
SD
MET

180
−30.652
81.376
−58.824
1.00
51.13

ATOM
274
CE
MET

180
−32.386
81.183
−59.120
1.00
54.25

ATOM
275
C
MET

180
−28.594
84.765
−60.873
1.00
58.77

ATOM
276
O
MET

180
−27.975
84.039
−61.648
1.00
60.13

ATOM
277
N
LYS

181
−28.013
85.535
−59.958
1.00
58.72

ATOM
278
CA
LYS

181
−26.572
85.603
−59.788
1.00
59.60

ATOM
279
CB
LYS

181
−26.187
87.005
−59.319
1.00
61.96

ATOM
280
CG
LYS

181
−24.713
87.331
−59.448
1.00
65.96

ATOM
281
CD
LYS

181
−24.435
88.802
−59.115
1.00
69.70

ATOM
282
CE
LYS

181
−22.954
89.170
−59.317
1.00
69.92

ATOM
283
NZ
LYS

181
−22.638
90.606
−59.012
1.00
70.79

ATOM
284
C
LYS

181
−26.167
84.566
−58.742
1.00
59.64

ATOM
285
O
LYS

181
−26.525
84.689
−57.569
1.00
59.52

ATOM
286
N
ILE

182
−25.426
83.546
−59.170
1.00
59.53

ATOM
287
CA
ILE

182
−24.982
82.469
−58.280
1.00
59.64

ATOM
288
CR
ILE

182
−25.313
81.081
−58.895
1.00
58.23

ATOM
289
CG2
ILE

182
−24.940
79.975
−57.933
1.00
55.70

ATOM
290
CG1
ILE

182
−26.806
80.996
−59.218
1.00
57.10

ATOM
291
CD1
ILE

182
−27.180
79.776
−60.026
1.00
56.15

ATOM
292
C
ILE

182
−23.479
82.530
−57.987
1.00
60.78

ATOM
293
O
ILE

182
−22.656
82.252
−58.858
1.00
61.27

ATOM
294
N
LEU

183
−23.137
82.866
−56.747
1.00
62.07

ATOM
295
CA
LEU

183
−21.744
82.985
−56.317
1.00
64.98

ATOM
296
CB
LEU

183
−21.571
84.278
−55.519
1.00
63.44

ATOM
297
CG
LEU

183
−21.966
85.574
−56.201
1.00
61.23

ATOM
298
CD1
LEU

183
−21.741
86.707
−55.230
1.00
58.89

ATOM
299
CD2
LEU

183
−21.161
85.760
−57.475
1.00
59.81

ATOM
300
C
LEU

183
−21.195
81.833
−55.461
1.00
67.22

ATOM
301
O
LEU

183
−21.814
81.444
−54.459
1.00
66.64

ATOM
302
N
ARG

184
−20.025
81.313
−55.839
1.00
69.55

ATOM
303
CA
ARG

184
−19.387
80.236
−55.074
1.00
73.02

ATOM
304
CB
ARG

184
−18.086
79.774
−55.757
1.00
74.15

ATOM
305
CG
ARG

184
−18.166
79.378
−57.246
1.00
77.69

ATOM
306
CD
ARG

184
−18.491
77.888
−57.458
1.00
79.90

ATOM
307
NE
ARG

184
−18.364
77.439
−58.855
1.00
82.50

ATOM
308
CZ
ARG

184
−18.975
77.994
−59.912
1.00
84.72

ATOM
309
NH1
ARG

184
−19.777
79.049
−59.774
1.00
85.63

ATOM
310
NH2
ARG

184
−18.800
77.477
−61.123
1.00
84.83

ATOM
311
C
ARG

184
−19.033
80.810
−53.686
1.00
74.65

ATOM
312
O
ARG

184
−18.373
81.839
−53.597
1.00
74.63

ATOM
313
N
LYS

185
−19.480
80.176
−52.605
1.00
76.64

ATOM
314
CA
LYS

185
−19.134
80.674
−51.271
1.00
78.41

ATOM
315
CB
LYS

185
−19.851
79.882
−50.169
1.00
75.30

ATOM
316
CG
LYS

185
−21.260
80.331
−49.833
1.00
73.34

ATOM
317
CD
LYS

185
−21.873
79.438
−48.754
1.00
71.48

ATOM
318
CE
LYS

185
−23.277
79.893
−48.349
1.00
70.10

ATOM
319
NZ
LYS

185
−23.934
78.985
−47.355
1.00
67.84

ATOM
320
C
LYS

185
−17.629
80.460
−51.135
1.00
81.73

ATOM
321
O
LYS

185
−16.971
81.033
−50.265
1.00
82.47

ATOM
322
N
GLU

186
−17.101
79.627
−52.025
1.00
85.05

ATOM
323
CA
GLU

186
−15.687
79.267
−52.059
1.00
88.41

ATOM
324
CB
GLU

186
−15.537
77.990
−52.887
1.00
89.94

ATOM
325
CG
GLU

186
−14.140
77.401
−52.970
1.00
92.22

ATOM
326
CD
GLU

186
−14.165
75.989
−53.535
1.00
93.16

ATOM
327
OE1
GLU

186
−14.633
75.811
−54.684
1.00
92.42

ATOM
328
OE2
GLU

186
−13.728
75.057
−52.822
1.00
94.10

ATOM
329
C
GLU

186
−14.795
80.377
−52.621
1.00
90.23

ATOM
330
O
GLU

186
−13.661
80.556
−52.183
1.00
91.51

ATOM
331
N
VAL

187
−15.305
81.116
−53.597
1.00
91.46

ATOM
332
CA
VAL

187
−14.546
82.207
−54.192
1.00
92.72

ATOM
333
CB
VAL

187
−15.153
82.614
−55.561
1.00
93.10

ATOM
334
CG1
VAL

187
−14.672
84.015
−55.976
1.00
92.86

ATOM
335
CG2
VAL

187
−14.774
81.570
−56.616
1.00
92.89

ATOM
336
C
VAL

187
−14.515
83.409
−53.248
1.00
93.50

ATOM
337
O
VAL

187
−13.470
84.021
−53.043
1.00
93.75

ATOM
338
N
ILE

188
−15.660
83.744
−52.668
1.00
94.77

ATOM
339
CA
ILE

188
−15.729
84.867
−51.744
1.00
96.38

ATOM
340
CB
ILE

188
−17.106
85.583
−51.817
1.00
97.58

ATOM
341
CG2
ILE

188
−18.202
84.653
−51.323
1.00
97.46

ATOM
342
CG1
ILE

188
−17.093
86.853
−50.956
1.00
98.72

ATOM
343
CD1
ILE

188
−18.323
87.755
−51.143
1.00
99.63

ATOM
344
C
ILE

188
−15.515
84.350
−50.327
1.00
96.39

ATOM
345
O
ILE

188
−14.548
84.716
−49.665
1.00
97.59

ATOM
346
N
ALA

198
−20.044
91.656
−49.943
1.00
111.27

ATOM
347
CA
ALA

198
−20.100
92.787
−49.020
1.00
111.39

ATOM
348
CB
ALA

198
−18.767
92.924
−48.288
1.00
111.17

ATOM
349
C
ALA

198
−20.433
94.091
−49.745
1.00
111.44

ATOM
350
O
ALA

198
−21.557
94.586
−49.677
1.00
110.50

ATOM
351
N
ALA

199
−19.439
94.644
−50.435
1.00
112.22

ATOM
352
CA
ALA

199
−19.611
95.887
−51.184
1.00
112.15

ATOM
353
CB
ALA

199
−18.274
96.324
−51.806
1.00
111.66

ATOM
354
C
ALA

199
−20.659
95.689
−52.272
1.00
111.80

ATOM
355
O
ALA

199
−21.257
96.652
−52.750
1.00
111.96

ATOM
356
N
ALA

200
−20.875
94.434
−52.659
1.00
111.30

ATOM
357
CA
ALA

200
−21.861
94.095
−53.687
1.00
110.31

ATOM
358
CB
ALA

200
−21.427
92.823
−54.430
1.00
109.64

ATOM
359
C
ALA

200
−23.235
93.892
−53.038
1.00
109.45

ATOM
360
O
ALA

200
−24.164
94.681
−53.235
1.00
109.02

ATOM
361
N
ALA

201
−23.352
92.828
−52.254
1.00
108.62

ATOM
362
CA
ALA

201
−24.597
92.525
−51.568
1.00
107.31

ATOM
363
CB
ALA

201
−24.485
91.182
−50.856
1.00
107.26

ATOM
364
C
ALA

201
−24.870
93.635
−50.560
1.00
106.33

ATOM
365
O
ALA

201
−24.094
94.586
−50.459
1.00
106.70

ATOM
366
N
ALA

202
−25.974
93.498
−49.823
1.00
104.62

ATOM
367
CA
ALA

202
−26.393
94.460
−48.798
1.00
102.14

ATOM
368
CB
ALA

202
−25.391
94.457
−47.640
1.00
102.24

ATOM
369
C
ALA

202
−26.565
95.876
−49.346
1.00
100.18

ATOM
370
O
ALA

202
−27.661
96.436
−49.323
1.00
99.14

ATOM
371
N
ALA

203
−25.467
96.443
−49.831
1.00
98.53

ATOM
372
CA
ALA

203
−25.448
97.783
−50.399
1.00
96.44

ATOM
373
CB
ALA

203
−24.049
98.102
−50.933
1.00
96.12

ATOM
374
C
ALA

203
−26.467
97.881
−51.522
1.00
95.16

ATOM
375
O
ALA

203
−27.372
98.713
−51.473
1.00
94.87

ATOM
376
N
ALA

204
−26.311
97.015
−52.524
1.00
93.35

ATOM
377
CA
ALA

204
−27.189
96.983
−53.689
1.00
90.99

ATOM
378
CB
ALA

204
−26.498
96.249
−54.826
1.00
90.77

ATOM
379
C
ALA

204
−28.546
96.349
−53.410
1.00
89.70

ATOM
380
O
ALA

204
−29.471
96.485
−54.201
1.00
89.55

ATOM
381
N
ALA

205
−28.668
95.653
−52.288
1.00
88.45

ATOM
382
CA
ALA

205
−29.929
95.009
−51.940
1.00
86.63

ATOM
383
CB
ALA

205
−29.695
93.931
−50.892
1.00
87.44

ATOM
384
C
ALA

205
−30.945
96.027
−51.427
1.00
85.01

ATOM
385
O
ALA

205
−32.140
95.909
−51.701
1.00
85.23

ATOM
386
N
ALA

206
−30.476
97.021
−50.677
1.00
82.62

ATOM
387
CA
ALA

206
−31.373
98.044
−50.149
1.00
79.56

ATOM
388
CB
ALA

206
−31.006
98.380
−48.696
1.00
78.86

ATOM
389
C
ALA

206
−31.389
99.317
−51.014
1.00
77.67

ATOM
390
O
ALA

206
−32.217
100.210
−50.782
1.00
77.42

ATOM
391
N
THR

207
−30.491
99.413
−52.003
1.00
74.84

ATOM
392
CA
THR

207
−30.485
100.589
−52.887
1.00
71.87

ATOM
393
CB
THR

207
−29.097
100.925
−53.484
1.00
72.74

ATOM
394
OG1
THR

207
−28.555
99.752
−54.106
1.00
73.95

ATOM
395
CG2
THR

207
−28.149
101.488
−52.408
1.00
71.32

ATOM
396
C
THR

207
−31.444
100.377
−54.052
1.00
68.91

ATOM
397
O
THR

207
−31.238
99.527
−54.919
1.00
68.62

ATOM
398
N
ARG

208
−32.495
101.183
−54.035
1.00
66.01

ATOM
399
CA
ARG

208
−33.569
101.181
−55.009
1.00
62.69

ATOM
400
CB
ARG

208
−34.880
101.401
−54.251
1.00
65.69

ATOM
401
CG
ARG

208
−36.133
101.250
−55.073
1.00
70.98

ATOM
402
CD
ARG

208
−36.384
99.777
−55.385
1.00
74.29

ATOM
403
NE
ARG

208
−37.662
99.572
−56.060
1.00
76.66

ATOM
404
CZ
ARG

208
−38.209
98.380
−56.273
1.00
78.00

ATOM
405
NH1
ARG

208
−37.589
97.277
−55.863
1.00
78.03

ATOM
406
NH2
ARG

208
−39.381
98.294
−56.889
1.00
79.20

ATOM
407
C
ARG

208
−33.323
102.351
−55.963
1.00
57.98

ATOM
408
O
ARG

208
−32.701
103.330
−55.570
1.00
59.11

ATOM
409
N
HIS

209
−33.789
102.251
−57.205
1.00
51.68

ATOM
410
CA
HIS

209
−33.643
103.345
−58.162
1.00
46.72

ATOM
411
CB
HIS

209
−32.200
103.778
−58.280
1.00
43.33

ATOM
412
CG
HIS

209
−32.018
105.063
−59.026
1.00
42.75

ATOM
413
CD2
HIS

209
−31.578
106.278
−58.616
1.00
41.65

ATOM
414
ND1
HIS

209
−32.254
105.179
−60.380
1.00
42.43

ATOM
415
CE1
HIS

209
−31.959
106.407
−60.774
1.00
41.53

ATOM
416
NE2
HIS

209
−31.546
107.094
−59.723
1.00
41.40

ATOM
417
C
HIS

209
−34.177
103.007
−59.542
1.00
45.78

ATOM
418
O
HIS

209
−33.909
101.942
−60.080
1.00
46.54

ATOM
419
N
PRO

210
−34.962
103.919
−60.137
1.00
45.04

ATOM
420
CD
PRO

210
−35.199
105.284
−59.639
1.00
44.80

ATOM
421
CA
PRO

210
−35.559
103.748
−61.465
1.00
43.86

ATOM
422
CB
PRO

210
−35.790
105.174
−61.923
1.00
42.99

ATOM
423
CG
PRO

210
−36.110
105.860
−60.687
1.00
43.79

ATOM
424
C
PRO

210
−34.676
103.024
−62.453
1.00
43.47

ATOM
425
O
PRO

210
−35.125
102.104
−63.119
1.00
43.96

ATOM
426
N
PHE

211
−33.421
103.458
−62.531
1.00
42.97

ATOM
427
CA
PHE

211
−32.459
102.920
−63.487
1.00
43.73

ATOM
428
CB
PHE

211
−31.731
104.080
−64.166
1.00
43.15

ATOM
429
CG
PHE

211
−32.644
105.180
−64.592
1.00
43.15

ATOM
430
CD1
PHE

211
−33.798
104.898
−65.327
1.00
43.74

ATOM
431
CD2
PHE

211
−32.405
106.490
−64.206
1.00
43.08

ATOM
432
CE1
PHE

211
−34.699
105.908
−65.660
1.00
40.39

ATOM
433
CE2
PHE

211
−33.310
107.501
−64.538
1.00
40.15

ATOM
434
CZ
PHE

211
−34.449
107.197
−65.262
1.00
38.77

ATOM
435
C
PHE

211
−31.431
101.905
−62.991
1.00
44.53

ATOM
436
O
PHE

211
−30.522
101.540
−63.736
1.00
46.25

ATOM
437
N
LEU

212
−31.543
101.483
−61.735
1.00
44.20

ATOM
438
CA
LEU

212
−30.653
100.464
−61.193
1.00
42.38

ATOM
439
CB
LEU

212
−30.135
100.831
−59.807
1.00
39.21

ATOM
440
CG
LEU

212
−29.022
101.872
−59.692
1.00
39.56

ATOM
441
CD1
LEU

212
−28.523
101.885
−58.262
1.00
39.36

ATOM
442
CD2
LEU

212
−27.860
101.545
−60.604
1.00
39.12

ATOM
443
C
LEU

212
−31.489
99.202
−61.088
1.00
43.32

ATOM
444
O
LEU

212
−32.662
99.248
−60.701
1.00
43.07

ATOM
445
N
THR

213
−30.898
98.078
−61.468
1.00
44.44

ATOM
446
CA
THR

213
−31.579
96.795
−61.389
1.00
45.26

ATOM
447
CB
THR

213
−30.646
95.699
−61.849
1.00
45.78

ATOM
448
OG1
THR

213
−29.792
96.220
−62.866
1.00
49.66

ATOM
449
CG2
THR

213
−31.415
94.530
−62.387
1.00
44.85

ATOM
450
C
THR

213
−31.908
96.532
−59.912
1.00
45.99

ATOM
451
O
THR

213
−31.066
96.766
−59.039
1.00
45.57

ATOM
452
N
ALA

214
−33.112
96.043
−59.625
1.00
46.07

ATOM
453
CA
ALA

214
−33.486
95.757
−58.236
1.00
46.22

ATOM
454
CB
ALA

214
−34.947
96.059
−58.009
1.00
43.78

ATOM
455
C
ALA

214
−33.208
94.315
−57.836
1.00
46.04

ATOM
456
O
ALA

214
−33.315
93.391
−58.645
1.00
44.74

ATOM
457
N
LEU

215
−32.856
94.127
−56.574
1.00
47.88

ATOM
458
CA
LEU

215
−32.583
92.802
−56.055
1.00
50.44

ATOM
459
CB
LEU

215
−31.614
92.875
−54.903
1.00
51.79

ATOM
460
CG
LEU

215
−31.518
91.485
−54.297
1.00
53.08

ATOM
461
CD1
LEU

215
−30.496
90.672
−55.109
1.00
53.05

ATOM
462
CD2
LEU

215
−31.139
91.590
−52.820
1.00
52.91

ATOM
463
C
LEU

215
−33.871
92.279
−55.509
1.00
51.40

ATOM
464
O
LEU

215
−34.264
92.675
−54.424
1.00
52.98

ATOM
465
N
LYS

216
−34.513
91.371
−56.223
1.00
53.23

ATOM
466
CA
LYS

216
−35.790
90.841
−55.770
1.00
55.65

ATOM
467
CB
LYS

216
−36.493
90.144
−56.925
1.00
55.96

ATOM
468
CG
LYS

216
−37.897
89.721
−56.602
1.00
58.54

ATOM
469
CD
LYS

216
−38.681
90.848
−55.952
1.00
59.83

ATOM
470
CE
LYS

216
−40.184
90.539
−55.985
1.00
63.13

ATOM
471
NZ
LYS

216
−40.549
89.164
−55.477
1.00
63.74

ATOM
472
C
LYS

216
−35.734
89.917
−54.546
1.00
57.23

ATOM
473
O
LYS

216
−36.483
90.120
−53.596
1.00
58.03

ATOM
474
N
TYR

217
−34.870
88.903
−54.569
1.00
59.20

ATOM
475
CA
TYR

217
−34.722
87.975
−53.443
1.00
60.12

ATOM
476
CB
TYR

217
−35.318
86.607
−53.735
1.00
61.60

ATOM
477
CG
TYR

217
−36.750
86.557
−54.161
1.00
63.87

ATOM
478
CD1
TYR

217
−37.119
85.794
−55.264
1.00
63.97

ATOM
479
CE1
TYR

217
−38.438
85.681
−55.654
1.00
66.51

ATOM
480
CD2
TYR

217
−37.744
87.218
−53.448
1.00
65.03

ATOM
481
CE2
TYR

217
−39.087
87.114
−53.833
1.00
66.62

ATOM
482
CZ
TYR

217
−39.421
86.341
−54.941
1.00
66.84

ATOM
483
OH
TYR

217
−40.721
86.236
−55.362
1.00
66.74

ATOM
484
C
TYR

217
−33.245
87.725
−53.217
1.00
60.58

ATOM
485
O
TYR

217
−32.437
87.818
−54.146
1.00
62.04

ATOM
486
N
ALA

218
−32.893
87.382
−51.987
1.00
59.36

ATOM
487
CA
ALA

218
−31.510
87.069
−51.669
1.00
59.06

ATOM
488
CB
ALA

218
−30.836
88.249
−50.982
1.00
59.17

ATOM
489
C
ALA

218
−31.535
85.852
−50.752
1.00
58.60

ATOM
490
O
ALA

218
−32.074
85.910
−49.642
1.00
58.70

ATOM
491
N
PHE

219
−30.989
84.739
−51.218
1.00
57.97

ATOM
492
CA
PHE

219
−30.983
83.551
−50.397
1.00
57.83

ATOM
493
CB
PHE

219
−32.179
82.647
−50.721
1.00
56.56

ATOM
494
CG
PHE

219
−32.047
81.884
−52.011
1.00
56.06

ATOM
495
CD1
PHE

219
−32.502
82.415
−53.200
1.00
57.08

ATOM
496
CD2
PHE

219
−31.479
80.625
−52.033
1.00
55.89

ATOM
497
CE1
PHE

219
−32.396
81.703
−54.390
1.00
56.64

ATOM
498
CE2
PHE

219
−31.373
79.923
−53.209
1.00
55.25

ATOM
499
CZ
PHE

219
−31.835
80.465
−54.388
1.00
55.98

ATOM
500
C
PHE

219
−29.706
82.784
−50.581
1.00
58.69

ATOM
501
O
PHE

219
−28.958
83.027
−51.521
1.00
59.00

ATOM
502
N
GLN

220
−29.450
81.852
−49.677
1.00
60.19

ATOM
503
CA
GLN

220
−28.246
81.054
−49.795
1.00
62.39

ATOM
504
CB
GLN

220
−27.206
81.489
−48.767
1.00
64.75

ATOM
505
CG
GLN

220
−27.666
81.361
−47.328
1.00
68.63

ATOM
506
CD
GLN

220
−26.492
81.319
−46.366
1.00
71.92

ATOM
507
OE1
GLN

220
−25.490
82.023
−46.563
1.00
73.88

ATOM
508
NE2
GLN

220
−26.607
80.501
−45.312
1.00
72.13

ATOM
509
C
GLN

220
−28.469
79.550
−49.661
1.00
62.03

ATOM
510
O
GLN

220
−29.420
79.078
−49.027
1.00
62.34

ATOM
511
N
THR

221
−27.562
78.814
−50.285
1.00
60.95

ATOM
512
CA
THR

221
−27.568
77.381
−50.247
1.00
59.41

ATOM
513
CB
THR

221
−27.254
76.834
−51.636
1.00
59.17

ATOM
514
OG1
THR

221
−26.002
77.361
−52.088
1.00
58.38

ATOM
515
CG2
THR

221
−28.340
77.253
−52.618
1.00
58.65

ATOM
516
C
THR

221
−26.458
77.052
−49.242
1.00
60.17

ATOM
517
O
THR

221
−25.880
77.951
−48.633
1.00
60.99

ATOM
518
N
HIS

222
−26.156
75.781
−49.039
1.00
60.76

ATOM
519
CA
HIS

222
−25.102
75.453
−48.087
1.00
61.77

ATOM
520
CB
HIS

222
−25.298
74.008
−47.584
1.00
60.58

ATOM
521
CG
HIS

222
−24.067
73.162
−47.656
1.00
56.94

ATOM
522
CD2
HIS

222
−23.278
72.649
−46.681
1.00
55.38

ATOM
523
ND1
HIS

222
−23.517
72.754
−48.851
1.00
55.90

ATOM
524
CE1
HIS

222
−22.440
72.024
−48.612
1.00
55.82

ATOM
525
NE2
HIS

222
−22.275
71.946
−47.302
1.00
55.59

ATOM
526
C
HIS

222
−23.710
75.639
−48.714
1.00
61.88

ATOM
527
O
HIS

222
−22.682
75.609
−48.035
1.00
60.39

ATOM
528
N
ASP

223
−23.699
75.897
−50.009
1.00
62.01

ATOM
529
CA
ASP

223
−22.461
76.016
−50.739
1.00
62.36

ATOM
530
CB
ASP

223
−22.353
74.737
−51.572
1.00
62.94

ATOM
531
CG
ASP

223
−21.436
74.868
−52.737
1.00
63.63

ATOM
532
OD1
ASP

223
−21.921
74.826
−53.894
1.00
63.16

ATOM
533
OD2
ASP

223
−20.226
75.009
−52.481
1.00
65.54

ATOM
534
C
ASP

223
−22.353
77.273
−51.615
1.00
62.99

ATOM
535
O
ASP

223
−21.313
77.513
−52.242
1.00
63.19

ATOM
536
N
ARG

224
−23.413
78.082
−51.659
1.00
62.05

ATOM
537
CA
ARG

224
−23.407
79.272
−52.509
1.00
60.21

ATOM
538
CB
ARG

224
−23.827
78.911
−53.939
1.00
58.56

ATOM
539
CG
ARG

224
−23.235
77.626
−54.449
1.00
57.87

ATOM
540
CD
ARG

224
−23.091
77.648
−55.926
1.00
56.29

ATOM
541
NE
ARG

224
−22.321
76.512
−56.389
1.00
55.08

ATOM
542
CZ
ARG

224
−21.966
76.333
−57.656
1.00
57.33

ATOM
543
NH1
ARG

224
−22.311
77.217
−58.587
1.00
57.43

ATOM
544
NH2
ARG

224
−21.263
75.264
−58.001
1.00
59.13

ATOM
545
C
ARG

224
−24.311
80.392
−52.053
1.00
60.29

ATOM
546
O
ARG

224
−25.144
80.222
−51.157
1.00
59.45

ATOM
547
N
LEU

225
−24.137
81.538
−52.706
1.00
60.51

ATOM
548
CA
LEU

225
−24.947
82.721
−52.450
1.00
61.55

ATOM
549
CB
LEU

225
−24.071
83.916
−52.058
1.00
63.02

ATOM
550
CG
LEU

225
−23.521
83.920
−50.623
1.00
64.17

ATOM
551
CD1
LEU

225
−22.911
85.286
−50.320
1.00
63.56

ATOM
552
CD2
LEU

225
−24.649
83.614
−49.622
1.00
64.04

ATOM
553
C
LEU

225
−25.724
83.027
−53.731
1.00
61.30

ATOM
554
O
LEU

225
−25.155
83.010
−54.827
1.00
61.77

ATOM
555
N
CYS

226
−27.021
83.295
−53.586
1.00
59.68

ATOM
556
CA
CYS

226
−27.877
83.578
−54.725
1.00
58.60

ATOM
557
CB
CYS

226
−28.920
82.476
−54.870
1.00
59.17

ATOM
558
SG
CYS

226
−28.211
80.907
−55.333
1.00
59.56

ATOM
559
C
CYS

226
−28.595
84.909
−54.645
1.00
58.03

ATOM
560
O
CYS

226
−29.187
85.241
−53.623
1.00
58.16

ATOM
561
N
PHE

227
−28.556
85.667
−55.736
1.00
57.36

ATOM
562
CA
PHE

227
−29.249
86.950
−55.791
1.00
56.31

ATOM
563
CB
PHE

227
−28.249
88.097
−55.884
1.00
57.09

ATOM
564
CG
PHE

227
−27.318
88.189
−54.699
1.00
55.74

ATOM
565
CD1
PHE

227
−26.040
87.654
−54.762
1.00
54.75

ATOM
566
CD2
PHE

227
−27.730
88.807
−53.522
1.00
55.28

ATOM
567
CE1
PHE

227
−25.187
87.736
−53.676
1.00
55.81

ATOM
568
CE2
PHE

227
−26.887
88.895
−52.434
1.00
55.49

ATOM
569
CZ
PHE

227
−25.613
88.361
−52.507
1.00
56.68

ATOM
570
C
PHE

227
−30.166
86.952
−57.002
1.00
56.05

ATOM
571
O
PHE

227
−29.719
87.127
−58.129
1.00
56.45

ATOM
572
N
VAL

228
−31.448
86.710
−56.757
1.00
55.64

ATOM
573
CA
VAL

228
−32.458
86.680
−57.797
1.00
55.27

ATOM
574
CB
VAL

228
−33.716
85.999
−57.288
1.00
55.66

ATOM
575
CG1
VAL

228
−34.839
86.140
−58.313
1.00
55.60

ATOM
576
CG2
VAL

228
−33.422
84.551
−56.967
1.00
54.36

ATOM
577
C
VAL

228
−32.812
88.112
−58.092
1.00
56.00

ATOM
578
O
VAL

228
−33.421
88.765
−57.257
1.00
55.89

ATOM
579
N
MET

229
−32.454
88.611
−59.270
1.00
57.58

ATOM
580
CA
MET

229
−32.750
90.008
−59.594
1.00
58.37

ATOM
581
CB
MET

229
−31.475
90.793
−59.652
1.00
59.57

ATOM
582
CG
MET

229
−30.745
90.725
−58.372
1.00
63.19

ATOM
583
SD
MET

229
−29.202
91.470
−58.688
1.00
70.23

ATOM
584
CE
MET

229
−28.769
90.676
−60.338
1.00
67.31

ATOM
585
C
MET

229
−33.531
90.292
−60.844
1.00
57.66

ATOM
586
O
MET

229
−33.457
89.547
−61.812
1.00
58.68

ATOM
587
N
GLU

230
−34.260
91.405
−60.804
1.00
57.78

ATOM
588
CA
GLU

230
−35.110
91.860
−61.904
1.00
57.98

ATOM
589
CB
GLU

230
−35.741
93.217
−61.556
1.00
60.35

ATOM
590
CG
GLU

230
−34.744
94.370
−61.480
1.00
63.42

ATOM
591
CD
GLU

230
−35.380
95.749
−61.716
1.00
65.17

ATOM
592
OE1
GLU

230
−36.017
95.968
−62.781
1.00
65.34

ATOM
593
OE2
GLU

230
−35.222
96.621
−60.838
1.00
65.88

ATOM
594
C
GLU

230
−34.395
91.965
−63.251
1.00
56.10

ATOM
595
O
GLU

230
−33.313
92.549
−63.350
1.00
53.79

ATOM
596
N
TYR

231
−35.025
91.410
−64.288
1.00
55.38

ATOM
597
CA
TYR

231
−34.449
91.424
−65.624
1.00
56.06

ATOM
598
CB
TYR

231
−34.368
90.000
−66.158
1.00
57.59

ATOM
599
CG
TYR

231
−33.509
89.855
−67.393
1.00
58.75

ATOM
600
CD1
TYR

231
−32.154
90.220
−67.373
1.00
59.60

ATOM
601
CE1
TYR

231
−31.340
90.052
−68.505
1.00
61.01

ATOM
602
CD2
TYR

231
−34.037
89.323
−68.575
1.00
58.59

ATOM
603
CE2
TYR

231
−33.239
89.153
−69.708
1.00
60.96

ATOM
604
CZ
TYR

231
−31.892
89.514
−69.672
1.00
62.62

ATOM
605
OH
TYR

231
−31.101
89.307
−70.794
1.00
64.40

ATOM
606
C
TYR

231
−35.190
92.293
−66.642
1.00
56.11

ATOM
607
O
TYR

231
−36.364
92.068
−66.941
1.00
54.71

ATOM
608
N
ALA

232
−34.477
93.280
−67.181
1.00
56.15

ATOM
609
CA
ALA

232
−35.021
94.192
−68.185
1.00
55.56

ATOM
610
CB
ALA

232
−34.036
95.301
−68.448
1.00
54.61

ATOM
611
C
ALA

232
−35.229
93.394
−69.449
1.00
55.59

ATOM
612
O
ALA

232
−34.376
92.587
−69.795
1.00
55.66

ATOM
613
N
ASN

233
−36.336
93.605
−70.153
1.00
56.51

ATOM
614
CA
ASN

233
−36.545
92.836
−71.377
1.00
57.65

ATOM
615
CB
ASN

233
−37.793
91.943
−71.274
1.00
59.23

ATOM
616
CG
ASN

233
−39.009
92.691
−70.824
1.00
60.87

ATOM
617
OD1
ASN

233
−39.677
93.344
−71.622
1.00
62.75

ATOM
618
ND2
ASN

233
−39.301
92.621
−69.528
1.00
63.07

ATOM
619
C
ASN

233
−36.576
93.664
−72.643
1.00
56.89

ATOM
620
O
ASN

233
−37.218
93.306
−73.620
1.00
57.27

ATOM
621
N
GLY

234
−35.851
94.770
−72.623
1.00
56.49

ATOM
622
CA
GLY

234
−35.768
95.613
−73.794
1.00
56.62

ATOM
623
C
GLY

234
−34.437
95.431
−74.505
1.00
56.75

ATOM
624
O
GLY

234
−34.007
96.309
−75.255
1.00
57.72

ATOM
625
N
GLY

235
−33.774
94.299
−74.274
1.00
55.93

ATOM
626
CA
GLY

235
−32.499
94.049
−74.926
1.00
55.04

ATOM
627
C
GLY

235
−31.347
94.831
−74.329
1.00
54.89

ATOM
628
O
GLY

235
−31.528
95.587
−73.377
1.00
54.91

ATOM
629
N
GLU

236
−30.154
94.670
−74.885
1.00
55.24

ATOM
630
CA
GLU

236
−29.004
95.368
−74.328
1.00
55.07

ATOM
631
CB
GLU

236
−27.852
94.404
−74.112
1.00
56.18

ATOM
632
CG
GLU

236
−27.842
93.269
−75.080
1.00
59.38

ATOM
633
CD
GLU

236
−28.404
92.007
−74.471
1.00
62.42

ATOM
634
OE1
GLU

236
−29.574
91.653
−74.791
1.00
62.53

ATOM
635
OE2
GLU

236
−27.665
91.380
−73.662
1.00
62.54

ATOM
636
C
GLU

236
−28.534
96.510
−75.175
1.00
54.13

ATOM
637
O
GLU

236
−28.433
96.382
−76.387
1.00
54.23

ATOM
638
N
LEU

237
−28.234
97.628
−74.529
1.00
53.71

ATOM
639
CA
LEU

237
−27.783
98.788
−75.265
1.00
54.93

ATOM
640
CB
LEU

237
−27.252
99.857
−74.329
1.00
54.04

ATOM
641
CG
LEU

237
−28.248
100.998
−74.338
1.00
53.95

ATOM
642
CD1
LEU

237
−27.709
102.156
−73.522
1.00
54.66

ATOM
643
CD2
LEU

237
−28.500
101.409
−75.784
1.00
53.81

ATOM
644
C
LEU

237
−26.725
98.420
−76.291
1.00
56.21

ATOM
645
O
LEU

237
−26.824
98.812
−77.456
1.00
56.21

ATOM
646
N
PHE

238
−25.717
97.667
−75.864
1.00
58.45

ATOM
647
CA
PHE

238
−24.687
97.238
−76.792
1.00
59.89

ATOM
648
CB
PHE

238
−23.792
96.165
−76.162
1.00
63.73

ATOM
649
CG
PHE

238
−23.289
95.200
−77.160
1.00
68.93

ATOM
650
CD1
PHE

238
−22.333
95.601
−78.100
1.00
71.68

ATOM
651
CD2
PHE

238
−23.908
93.955
−77.305
1.00
70.77

ATOM
652
CE1
PHE

238
−22.003
94.782
−79.193
1.00
74.10

ATOM
653
CE2
PHE

238
−23.596
93.120
−78.386
1.00
73.70

ATOM
654
CZ
PHE

238
−22.639
93.536
−79.340
1.00
74.73

ATOM
655
C
PHE

238
−25.374
96.661
−78.066
1.00
59.02

ATOM
656
O
PHE

238
−24.983
96.969
−79.201
1.00
58.51

ATOM
657
N
PHE

239
−26.387
95.822
−77.866
1.00
57.17

ATOM
658
CA
PHE

239
−27.116
95.238
−78.980
1.00
56.51

ATOM
659
CB
PHE

239
−28.324
94.445
−78.471
1.00
58.38

ATOM
660
CG
PHE

239
−29.260
93.985
−79.566
1.00
58.40

ATOM
661
CD1
PHE

239
−28.957
92.862
−80.342
1.00
59.15

ATOM
662
CD2
PHE

239
−30.430
94.683
−79.830
1.00
57.90

ATOM
663
CE1
PHE

239
−29.812
92.443
−81.369
1.00
59.43

ATOM
664
CE2
PHE

239
−31.293
94.270
−80.859
1.00
59.40

ATOM
665
CZ
PHE

239
−30.984
93.151
−81.628
1.00
59.17

ATOM
666
C
PHE

239
−27.618
96.329
−79.920
1.00
55.27

ATOM
667
O
PHE

239
−27.177
96.426
−81.060
1.00
55.80

ATOM
668
N
HIS

240
−28.558
97.134
−79.420
1.00
53.43

ATOM
669
CA
HIS

240
−29.171
98.228
−80.172
1.00
51.94

ATOM
670
CB
HIS

240
−30.103
99.043
−79.257
1.00
50.17

ATOM
671
CG
HIS

240
−31.250
98.258
−78.691
1.00
46.78

ATOM
672
CD2
HIS

240
−31.564
97.936
−77.412
1.00
46.08

ATOM
673
ND1
HIS

240
−32.233
97.700
−79.478
1.00
45.57

ATOM
674
CE1
HIS

240
−33.103
97.066
−78.710
1.00
45.18

ATOM
675
NE2
HIS

240
−32.720
97.194
−77.454
1.00
45.22

ATOM
676
C
HIS

240
−28.135
99.165
−80.815
1.00
51.95

ATOM
677
O
HIS

240
−28.259
99.520
−81.993
1.00
52.45

ATOM
678
N
LEU

241
−27.123
99.573
−80.052
1.00
50.66

ATOM
679
CA
LEU

241
−26.090
100.439
−80.595
1.00
51.66

ATOM
680
CB
LEU

241
−25.000
100.715
−79.555
1.00
48.76

ATOM
681
CG
LEU

241
−23.880
101.590
−80.112
1.00
46.97

ATOM
682
CD1
LEU

241
−24.521
102.823
−80.697
1.00
48.02

ATOM
683
CD2
LEU

241
−22.854
101.969
−79.049
1.00
47.08

ATOM
684
C
LEU

241
−25.442
99.829
−81.842
1.00
54.73

ATOM
685
O
LEU

241
−25.232
100.516
−82.847
1.00
55.64

ATOM
686
N
SER

242
−25.119
98.544
−81.802
1.00
56.62

ATOM
687
CA
SER

242
−24.494
97.949
−82.968
1.00
59.11

ATOM
688
CB
SER

242
−23.920
96.580
−82.632
1.00
58.85

ATOM
689
OG
SER

242
−24.802
95.876
−81.797
1.00
62.13

ATOM
690
C
SER

242
−25.434
97.848
−84.166
1.00
61.10

ATOM
691
O
SER

242
−24.978
97.767
−85.310
1.00
61.61

ATOM
692
N
ARG

243
−26.740
97.861
−83.923
1.00
62.64

ATOM
693
CA
ARG

243
−27.687
97.787
−85.030
1.00
64.71

ATOM
694
CB
ARG

243
−29.046
97.264
−84.563
1.00
66.18

ATOM
695
CG
ARG

243
−29.021
95.813
−84.068
1.00
70.06

ATOM
696
CD
ARG

243
−30.424
95.242
−84.090
1.00
73.49

ATOM
697
NE
ARG

243
−30.942
95.238
−85.455
1.00
78.42

ATOM
698
CZ
ARG

243
−32.214
95.033
−85.783
1.00
79.64

ATOM
699
NH1
ARG

243
−33.117
94.813
−84.831
1.00
81.30

ATOM
700
NH2
ARG

243
−32.581
95.047
−87.063
1.00
79.34

ATOM
701
C
ARG

243
−27.862
99.167
−85.631
1.00
64.74

ATOM
702
O
ARG

243
−28.608
99.353
−86.587
1.00
65.12

ATOM
703
N
GLU

244
−27.153
100.136
−85.072
1.00
64.07

ATOM
704
CA
GLU

244
−27.264
101.498
−85.550
1.00
63.44

ATOM
705
CB
GLU

244
−28.160
102.304
−84.623
1.00
63.93

ATOM
706
CG
GLU

244
−29.603
101.920
−84.755
1.00
65.33

ATOM
707
CD
GLU

244
−30.505
102.799
−83.939
1.00
67.27

ATOM
708
OE1
GLU

244
−30.580
102.588
−82.705
1.00
67.76

ATOM
709
OE2
GLU

244
−31.128
103.708
−84.539
1.00
68.46

ATOM
710
C
GLU

244
−25.958
102.216
−85.701
1.00
62.23

ATOM
711
O
GLU

244
−25.961
103.408
−86.000
1.00
63.17

ATOM
712
N
ARG

245
−24.854
101.501
−85.489
1.00
60.84

ATOM
713
CA
ARG

245
−23.502
102.066
−85.605
1.00
58.99

ATOM
714
CB
ARG

245
−23.236
102.486
−87.069
1.00
58.85

ATOM
715
CG
ARG

245
−21.846
103.050
−87.362
1.00
60.59

ATOM
716
CD
ARG

245
−20.726
102.072
−87.020
1.00
63.59

ATOM
717
NE
ARG

245
−19.936
101.635
−88.180
1.00
67.49

ATOM
718
CZ
ARG

245
−20.165
100.534
−88.902
1.00
68.65

ATOM
719
NH1
ARG

245
−21.173
99.722
−88.608
1.00
70.75

ATOM
720
NH2
ARG

245
−19.368
100.229
−89.920
1.00
69.78

ATOM
721
C
ARG

245
−23.255
103.236
−84.626
1.00
56.71

ATOM
722
O
ARG

245
−22.246
103.234
−83.900
1.00
56.07

ATOM
723
N
VAL

246
−24.175
104.207
−84.607
1.00
53.86

ATOM
724
CA
VAL

246
−24.095
105.363
−83.727
1.00
53.06

ATOM
725
CB
VAL

246
−23.407
106.571
−84.401
1.00
54.68

ATOM
726
CG1
VAL

246
−22.668
107.425
−83.338
1.00
52.61

ATOM
727
CG2
VAL

246
−22.446
106.097
−85.495
1.00
56.84

ATOM
728
C
VAL

246
−25.483
105.819
−83.324
1.00
52.80

ATOM
729
O
VAL

246
−26.440
105.584
−84.033
1.00
53.52

ATOM
730
N
PHE

247
−25.584
106.462
−82.166
1.00
53.24

ATOM
731
CA
PHE

247
−26.844
106.994
−81.661
1.00
52.35

ATOM
732
CB
PHE

247
−26.976
106.756
−80.154
1.00
51.14

ATOM
733
CG
PHE

247
−27.508
105.395
−79.777
1.00
51.57

ATOM
734
CD1
PHE

247
−28.268
104.649
−80.667
1.00
50.67

ATOM
735
CD2
PHE

247
−27.293
104.888
−78.490
1.00
51.25

ATOM
736
CE1
PHE

247
−28.805
103.426
−80.279
1.00
51.34

ATOM
737
CE2
PHE

247
−27.822
103.669
−78.100
1.00
50.31

ATOM
738
CZ
PHE

247
−28.580
102.935
−78.989
1.00
50.52

ATOM
739
C
PHE

247
−26.820
108.509
−81.908
1.00
54.13

ATOM
740
O
PHE

247
−25.791
109.073
−82.300
1.00
53.35

ATOM
741
N
THR

248
−27.940
109.178
−81.660
1.00
55.42

ATOM
742
CA
THR

248
−28.012
110.617
−81.866
1.00
56.42

ATOM
743
CB
THR

248
−29.418
111.048
−82.231
1.00
58.86

ATOM
744
OG1
THR

248
−29.704
110.625
−83.573
1.00
60.69

ATOM
745
CG2
THR

248
−29.554
112.568
−82.109
1.00
59.43

ATOM
746
C
THR

248
−27.608
111.354
−80.619
1.00
56.27

ATOM
747
O
THR

248
−27.994
110.956
−79.518
1.00
57.63

ATOM
748
N
GLU

249
−26.863
112.443
−80.790
1.00
55.72

ATOM
749
CA
GLU

249
−26.395
113.208
−79.648
1.00
56.33

ATOM
750
CB
GLU

249
−25.773
114.523
−80.092
1.00
57.14

ATOM
751
CG
GLU

249
−24.423
114.380
−80.750
1.00
58.64

ATOM
752
CD
GLU

249
−23.690
115.710
−80.817
1.00
60.38

ATOM
753
OE1
GLU

249
−23.628
116.384
−79.776
1.00
62.11

ATOM
754
OE2
GLU

249
−23.172
116.087
−81.886
1.00
61.08

ATOM
755
C
GLU

249
−27.486
113.468
−78.612
1.00
56.82

ATOM
756
O
GLU

249
−27.213
113.962
−77.517
1.00
57.02

ATOM
757
N
GLU

250
−28.721
113.144
−78.960
1.00
57.10

ATOM
758
CA
GLU

250
−29.814
113.318
−78.030
1.00
59.34

ATOM
759
CB
GLU

250
−31.072
113.823
−78.730
1.00
62.10

ATOM
760
CG
GLU

250
−31.276
115.328
−78.624
1.00
65.60

ATOM
761
CD
GLU

250
−31.330
115.805
−77.183
1.00
67.27

ATOM
762
OE1
GLU

250
−30.255
115.869
−76.530
1.00
68.52

ATOM
763
OE2
GLU

250
−32.451
116.105
−76.709
1.00
66.68

ATOM
764
C
GLU

250
−30.095
111.974
−77.414
1.00
58.83

ATOM
765
O
GLU

250
−30.177
111.852
−76.187
1.00
60.92

ATOM
766
N
ARG

251
−30.233
110.966
−78.268
1.00
56.44

ATOM
767
CA
ARG

251
−30.501
109.619
−77.797
1.00
54.72

ATOM
768
CB
ARG

251
−30.474
108.631
−78.948
1.00
54.18

ATOM
769
CG
ARG

251
−31.385
107.465
−78.709
1.00
54.07

ATOM
770
CD
ARG

251
−30.722
106.182
−79.096
1.00
53.40

ATOM
771
NE
ARG

251
−31.487
105.437
−80.082
1.00
53.76

ATOM
772
CZ
ARG

251
−32.032
104.246
−79.860
1.00
55.64

ATOM
773
NH1
ARG

251
−31.896
103.660
−78.680
1.00
55.82

ATOM
774
NH2
ARG

251
−32.717
103.632
−80.820
1.00
56.77

ATOM
775
C
ARG

251
−29.407
109.264
−76.800
1.00
53.82

ATOM
776
O
ARG

251
−29.657
108.695
−75.741
1.00
52.67

ATOM
777
N
ALA

252
−28.182
109.609
−77.148
1.00
52.30

ATOM
778
CA
ALA

252
−27.093
109.340
−76.247
1.00
52.96

ATOM
779
CB
ALA

252
−25.782
109.939
−76.782
1.00
54.05

ATOM
780
C
ALA

252
−27.509
110.044
−74.983
1.00
52.90

ATOM
781
O
ALA

252
−27.744
109.410
−73.967
1.00
54.24

ATOM
782
N
ALA

253
−27.621
111.369
−75.077
1.00
51.69

ATOM
783
CA
ALA

253
−27.994
112.219
−73.952
1.00
48.08

ATOM
784
CB
ALA

253
−28.328
113.607
−74.437
1.00
49.27

ATOM
785
C
ALA

253
−29.146
111.654
−73.134
1.00
46.00

ATOM
786
O
ALA

253
−29.112
111.732
−71.907
1.00
45.85

ATOM
787
N
PHE

254
−30.160
111.100
−73.791
1.00
42.03

ATOM
788
CA
PHE

254
−31.266
110.529
−73.042
1.00
41.60

ATOM
789
CB
PHE

254
−32.210
109.778
−73.941
1.00
44.00

ATOM
790
CG
PHE

254
−33.337
109.124
−73.209
1.00
48.04

ATOM
791
CD1
PHE

254
−34.345
109.886
−72.638
1.00
49.95

ATOM
792
CD2
PHE

254
−33.422
107.736
−73.137
1.00
50.49

ATOM
793
CE1
PHE

254
−35.439
109.271
−72.006
1.00
51.92

ATOM
794
CE2
PHE

254
−34.503
107.102
−72.511
1.00
51.03

ATOM
795
CZ
PHE

254
−35.514
107.865
−71.947
1.00
52.65

ATOM
796
C
PHE

254
−30.674
109.557
−72.045
1.00
41.01

ATOM
797
O
PHE

254
−30.805
109.745
−70.842
1.00
41.53

ATOM
798
N
TYR

255
−29.999
108.529
−72.560
1.00
40.14

ATOM
799
CA
TYR

255
−29.332
107.515
−71.747
1.00
36.58

ATOM
800
CB
TYR

255
−28.635
106.511
−72.638
1.00
37.23

ATOM
801
CG
TYR

255
−29.594
105.830
−73.563
1.00
39.49

ATOM
802
CD1
TYR

255
−30.778
105.317
−73.082
1.00
38.77

ATOM
803
CE1
TYR

255
−31.680
104.716
−73.932
1.00
42.51

ATOM
804
CD2
TYR

255
−29.332
105.725
−74.930
1.00
40.34

ATOM
805
CE2
TYR

255
−30.227
105.132
−75.789
1.00
40.12

ATOM
806
CZ
TYR

255
−31.400
104.618
−75.286
1.00
41.95

ATOM
807
OH
TYR

255
−32.279
103.937
−76.098
1.00
41.80

ATOM
808
C
TYR

255
−28.316
108.106
−70.797
1.00
34.60

ATOM
809
O
TYR

255
−28.265
107.739
−69.630
1.00
34.46

ATOM
810
N
GLY

256
−27.510
109.024
−71.303
1.00
33.03

ATOM
811
CA
GLY

256
−26.502
109.646
−70.481
1.00
34.98

ATOM
812
C
GLY

256
−27.112
110.248
−69.242
1.00
37.28

ATOM
813
O
GLY

256
−26.511
110.221
−68.157
1.00
36.19

ATOM
814
N
ALA

257
−28.319
110.790
−69.408
1.00
38.76

ATOM
815
CA
ALA

257
−29.040
111.417
−68.316
1.00
39.95

ATOM
816
CB
ALA

257
−30.154
112.298
−68.864
1.00
39.05

ATOM
817
C
ALA

257
−29.601
110.395
−67.310
1.00
40.20

ATOM
818
O
ALA

257
−29.477
110.600
−66.100
1.00
41.01

ATOM
819
N
GLU

258
−30.211
109.308
−67.774
1.00
38.83

ATOM
820
CA
GLU

258
−30.723
108.348
−66.802
1.00
41.08

ATOM
821
CB
GLU

258
−31.524
107.215
−67.474
1.00
40.29

ATOM
822
CG
GLU

258
−32.521
107.739
−68.512
1.00
42.23

ATOM
823
CD
GLU

258
−33.741
106.852
−68.742
1.00
46.18

ATOM
824
OE1
GLU

258
−33.585
105.619
−68.855
1.00
46.61

ATOM
825
OE2
GLU

258
−34.876
107.391
−68.839
1.00
49.04

ATOM
826
C
GLU

258
−29.527
107.801
−66.019
1.00
41.79

ATOM
827
O
GLU

258
−29.601
107.600
−64.798
1.00
41.76

ATOM
828
N
ILE

259
−28.403
107.610
−66.705
1.00
41.38

ATOM
829
CA
ILE

259
−27.234
107.101
−66.016
1.00
40.33

ATOM
830
CB
ILE

259
−26.045
106.804
−66.969
1.00
40.56

ATOM
831
CG2
ILE

259
−24.789
106.440
−66.149
1.00
39.49

ATOM
832
CG1
ILE

259
−26.394
105.642
−67.900
1.00
39.49

ATOM
833
CD1
ILE

259
−25.353
105.415
−68.934
1.00
39.15

ATOM
834
C
ILE

259
−26.776
108.096
−64.978
1.00
40.77

ATOM
835
O
ILE

259
−26.598
107.722
−63.822
1.00
41.79

ATOM
836
N
VAL

260
−26.583
109.355
−65.387
1.00
40.24

ATOM
837
CA
VAL

260
−26.125
110.415
−64.468
1.00
37.59

ATOM
838
CB
VAL

260
−26.185
111.823
−65.129
1.00
34.92

ATOM
839
CG1
VAL

260
−25.857
112.883
−64.114
1.00
32.77

ATOM
840
CG2
VAL

260
−25.176
111.918
−66.253
1.00
34.85

ATOM
841
C
VAL

260
−26.970
110.429
−63.202
1.00
37.07

ATOM
842
O
VAL

260
−26.455
110.626
−62.102
1.00
34.02

ATOM
843
N
SER

261
−28.271
110.194
−63.377
1.00
36.64

ATOM
844
CA
SER

261
−29.215
110.152
−62.267
1.00
36.77

ATOM
845
CB
SER

261
−30.636
109.969
−62.785
1.00
37.47

ATOM
846
OG
SER

261
−31.528
109.766
−61.706
1.00
39.68

ATOM
847
C
SER

261
−28.874
109.006
−61.320
1.00
36.39

ATOM
848
O
SER

261
−28.740
109.206
−60.116
1.00
35.60

ATOM
849
N
ALA

262
−28.736
107.809
−61.882
1.00
35.91

ATOM
850
CA
ALA

262
−28.384
106.621
−61.110
1.00
34.56

ATOM
851
CB
ALA

262
−28.198
105.437
−62.035
1.00
33.00

ATOM
852
C
ALA

262
−27.112
106.863
−60.320
1.00
34.18

ATOM
853
O
ALA

262
−27.017
106.524
−59.156
1.00
35.06

ATOM
854
N
LEU

263
−26.137
107.473
−60.951
1.00
34.74

ATOM
855
CA
LEU

263
−24.874
107.705
−60.291
1.00
37.11

ATOM
856
CB
LEU

263
−23.796
108.072
−61.321
1.00
37.01

ATOM
857
CG
LEU

263
−23.457
106.927
−62.259
1.00
35.53

ATOM
858
CD1
LEU

263
−22.346
107.311
−63.188
1.00
34.02

ATOM
859
CD2
LEU

263
−23.075
105.738
−61.396
1.00
35.69

ATOM
860
C
LEU

263
−24.921
108.754
−59.219
1.00
38.74

ATOM
861
O
LEU

263
−24.185
108.665
−58.235
1.00
40.59

ATOM
862
N
GLU

264
−25.750
109.772
−59.410
1.00
41.02

ATOM
863
CA
GLU

264
−25.840
110.807
−58.393
1.00
42.25

ATOM
864
CB
GLU

264
−26.791
111.903
−58.801
1.00
43.68

ATOM
865
CG
GLU

264
−27.085
112.811
−57.647
1.00
48.37

ATOM
866
CD
GLU

264
−27.950
113.972
−58.033
1.00
52.87

ATOM
867
OE1
GLU

264
−29.130
113.757
−58.408
1.00
55.43

ATOM
868
OE2
GLU

264
−27.436
115.107
−57.963
1.00
56.01

ATOM
869
C
GLU

264
−26.377
110.155
−57.140
1.00
41.62

ATOM
870
O
GLU

264
−25.903
110.405
−56.036
1.00
39.43

ATOM
871
N
TYR

265
−27.374
109.304
−57.334
1.00
41.96

ATOM
872
CA
TYR

265
−27.982
108.620
−56.224
1.00
43.36

ATOM
873
CB
TYR

265
−29.099
107.706
−56.696
1.00
46.93

ATOM
874
CG
TYR

265
−29.949
107.250
−55.535
1.00
54.20

ATOM
875
CD1
TYR

265
−30.771
108.173
−54.850
1.00
58.79

ATOM
876
CE1
TYR

265
−31.545
107.791
−53.731
1.00
58.88

ATOM
877
CD2
TYR

265
−29.915
105.926
−55.081
1.00
53.90

ATOM
878
CE2
TYR

265
−30.683
105.526
−53.964
1.00
56.95

ATOM
879
CZ
TYR

265
−31.498
106.466
−53.288
1.00
58.96

ATOM
880
OH
TYR

265
−32.256
106.102
−52.170
1.00
58.88

ATOM
881
C
TYR

265
−26.939
107.801
−55.467
1.00
42.79

ATOM
882
O
TYR

265
−26.759
107.978
−54.252
1.00
41.77

ATOM
883
N
LEU

266
−26.256
106.910
−56.193
1.00
40.98

ATOM
884
CA
LEU

266
−25.232
106.045
−55.608
1.00
36.65

ATOM
885
CB
LEU

266
−24.601
105.144
−56.660
1.00
35.25

ATOM
886
CG
LEU

266
−25.523
104.107
−57.291
1.00
34.78

ATOM
887
CD1
LEU

266
−24.845
103.565
−58.495
1.00
34.51

ATOM
888
CD2
LEU

266
−25.841
102.987
−56.322
1.00
35.50

ATOM
889
C
LEU

266
−24.146
106.834
−54.936
1.00
35.02

ATOM
890
O
LEU

266
−23.752
106.500
−53.843
1.00
33.78

ATOM
891
N
HIS

267
−23.655
107.885
−55.569
1.00
34.64

ATOM
892
CA
HIS

267
−22.602
108.639
−54.921
1.00
35.63

ATOM
893
CB
HIS

267
−21.964
109.646
−55.875
1.00
35.65

ATOM
894
CG
HIS

267
−21.273
109.027
−57.046
1.00
36.53

ATOM
895
CD2
HIS

267
−21.221
107.748
−57.478
1.00
37.02

ATOM
896
ND1
HIS

267
−20.546
109.766
−57.951
1.00
37.83

ATOM
897
CE1
HIS

267
−20.078
108.967
−58.894
1.00
37.83

ATOM
898
NE2
HIS

267
−20.472
107.738
−58.631
1.00
37.12

ATOM
899
C
HIS

267
−23.107
109.385
−53.699
1.00
37.37

ATOM
900
O
HIS

267
−22.321
109.787
−52.862
1.00
37.40

ATOM
901
N
SER

268
−24.410
109.612
−53.603
1.00
40.64

ATOM
902
CA
SER

268
−24.928
110.329
−52.447
1.00
42.75

ATOM
903
CB
SER

268
−26.351
110.833
−52.695
1.00
43.40

ATOM
904
OG
SER

268
−27.255
109.754
−52.870
1.00
46.67

ATOM
905
C
SER

268
−24.912
109.358
−51.285
1.00
43.85

ATOM
906
O
SER

268
−24.706
109.757
−50.139
1.00
42.93

ATOM
907
N
ARG

269
−25.142
108.085
−51.597
1.00
45.20

ATOM
908
CA
ARG

269
−25.122
107.028
−50.597
1.00
47.42

ATOM
909
CB
ARG

269
−25.911
105.812
−51.074
1.00
49.68

ATOM
910
CG
ARG

269
−27.399
106.019
−51.078
1.00
55.46

ATOM
911
CD
ARG

269
−27.854
106.411
−49.687
1.00
58.44

ATOM
912
NE
ARG

269
−29.232
106.886
−49.656
1.00
61.49

ATOM
913
CZ
ARG

269
−29.721
107.845
−50.440
1.00
63.34

ATOM
914
NH1
ARG

269
−28.946
108.440
−51.341
1.00
63.40

ATOM
915
NH2
ARG

269
−30.988
108.224
−50.304
1.00
63.31

ATOM
916
C
ARG

269
−23.675
106.603
−50.358
1.00
47.89

ATOM
917
O
ARG

269
−23.424
105.589
−49.704
1.00
48.73

ATOM
918
N
ASP

270
−22.731
107.360
−50.916
1.00
46.60

ATOM
919
CA
ASP

270
−21.320
107.059
−50.753
1.00
47.20

ATOM
920
CB
ASP

270
−20.955
107.159
−49.270
1.00
51.45

ATOM
921
CG
ASP

270
−19.463
107.258
−49.054
1.00
56.02

ATOM
922
OD1
ASP

270
−18.735
106.794
−49.952
1.00
59.22

ATOM
923
OD2
ASP

270
−19.003
107.786
−48.014
1.00
58.08

ATOM
924
C
ASP

270
−20.960
105.656
−51.282
1.00
45.77

ATOM
925
O
ASP

270
−20.291
104.890
−50.598
1.00
47.78

ATOM
926
N
VAL

271
−21.400
105.336
−52.498
1.00
41.94

ATOM
927
CA
VAL

271
−21.183
104.045
−53.146
1.00
37.02

ATOM
928
CB
VAL

271
−22.484
103.341
−53.365
1.00
35.61

ATOM
929
CG1
VAL

271
−22.333
102.319
−54.452
1.00
32.84

ATOM
930
CG2
VAL

271
−22.935
102.714
−52.107
1.00
35.19

ATOM
931
C
VAL

271
−20.615
104.242
−54.528
1.00
38.27

ATOM
932
O
VAL

271
−21.261
104.865
−55.348
1.00
39.48

ATOM
933
N
VAL

272
−19.441
103.684
−54.818
1.00
39.56

ATOM
934
CA
VAL

272
−18.835
103.864
−56.141
1.00
38.29

ATOM
935
CB
VAL

272
−17.290
103.882
−56.096
1.00
37.80

ATOM
936
CG1
VAL

272
−16.751
103.924
−57.510
1.00
37.97

ATOM
937
CG2
VAL

272
−16.785
105.095
−55.326
1.00
34.59

ATOM
938
C
VAL

272
−19.254
102.728
−57.015
1.00
38.29

ATOM
939
O
VAL

272
−18.962
101.592
−56.712
1.00
40.46

ATOM
940
N
TYR

273
−19.919
103.007
−58.123
1.00
37.53

ATOM
941
CA
TYR

273
−20.354
101.890
−58.932
1.00
36.67

ATOM
942
CB
TYR

273
−21.281
102.355
−60.040
1.00
30.76

ATOM
943
CG
TYR

273
−22.145
101.215
−60.507
1.00
31.04

ATOM
944
CD1
TYR

273
−23.066
100.619
−59.656
1.00
28.51

ATOM
945
CE1
TYR

273
−23.840
99.543
−60.080
1.00
29.65

ATOM
946
CD2
TYR

273
−22.018
100.708
−61.781
1.00
30.83

ATOM
947
CE2
TYR

273
−22.781
99.633
−62.215
1.00
31.32

ATOM
948
CZ
TYR

273
−23.687
99.052
−61.368
1.00
31.70

ATOM
949
OH
TYR

273
−24.420
97.962
−61.824
1.00
32.78

ATOM
950
C
TYR

273
−19.278
100.951
−59.513
1.00
37.18

ATOM
951
O
TYR

273
−19.470
99.740
−59.488
1.00
37.07

ATOM
952
N
ARG

274
−18.181
101.503
−60.034
1.00
38.28

ATOM
953
CA
ARG

274
−17.086
100.729
−60.646
1.00
40.89

ATOM
954
CB
ARG

274
−16.598
99.623
−59.718
1.00
43.17

ATOM
955
CG
ARG

274
−15.851
100.074
−58.502
1.00
48.37

ATOM
956
CD
ARG

274
−15.646
98.887
−57.598
1.00
50.53

ATOM
957
NE
ARG

274
−14.866
99.192
−56.400
1.00
52.73

ATOM
958
CZ
ARG

274
−13.646
98.710
−56.176
1.00
54.09

ATOM
959
NH1
ARG

274
−13.065
97.912
−57.083
1.00
53.66

ATOM
960
NH2
ARG

274
−13.027
98.986
−55.029
1.00
52.88

ATOM
961
C
ARG

274
−17.384
100.057
−61.979
1.00
40.25

ATOM
962
O
ARG

274
−16.485
99.809
−62.744
1.00
40.06

ATOM
963
N
ASP

275
−18.640
99.745
−62.252
1.00
41.62

ATOM
964
CA
ASP

275
−18.989
99.042
−63.480
1.00
42.56

ATOM
965
CB
ASP

275
−19.701
97.731
−63.130
1.00
47.02

ATOM
966
CG
ASP

275
−18.755
96.664
−62.591
1.00
52.05

ATOM
967
OD1
ASP

275
−18.081
96.896
−61.560
1.00
52.75

ATOM
968
OD2
ASP

275
−18.694
95.574
−63.209
1.00
56.41

ATOM
969
C
ASP

275
−19.838
99.776
−64.513
1.00
41.87

ATOM
970
O
ASP

275
−20.625
99.146
−65.227
1.00
41.73

ATOM
971
N
ILE

276
−19.711
101.089
−64.619
1.00
40.20

ATOM
972
CA
ILE

276
−20.506
101.760
−65.632
1.00
38.96

ATOM
973
CB
ILE

276
−20.609
103.265
−65.377
1.00
38.40

ATOM
974
CG2
ILE

276
−21.168
103.971
−66.601
1.00
35.75

ATOM
975
CG1
ILE

276
−21.486
103.514
−64.140
1.00
36.92

ATOM
976
CD1
ILE

276
−22.840
102.866
−64.216
1.00
35.84

ATOM
977
C
ILE

276
−19.836
101.526
−66.972
1.00
39.53

ATOM
978
O
ILE

276
−18.831
102.153
−67.287
1.00
39.09

ATOM
979
N
LYS

277
−20.378
100.604
−67.758
1.00
39.04

ATOM
980
CA
LYS

277
−19.801
100.318
−69.055
1.00
40.33

ATOM
981
CB
LYS

277
−18.631
99.350
−68.896
1.00
42.59

ATOM
982
CG
LYS

277
−18.928
98.073
−68.127
1.00
43.91

ATOM
983
CD
LYS

277
−17.606
97.384
−67.779
1.00
48.02

ATOM
984
CE
LYS

277
−17.758
95.972
−67.203
1.00
49.19

ATOM
985
NZ
LYS

277
−17.436
94.948
−68.257
1.00
49.33

ATOM
986
C
LYS

277
−20.892
99.762
−69.947
1.00
40.01

ATOM
987
O
LYS

277
−21.810
99.117
−69.467
1.00
41.30

ATOM
988
N
LEU

278
−20.780
100.010
−71.245
1.00
39.68

ATOM
989
CA
LEU

278
−21.801
99.615
−72.215
1.00
40.09

ATOM
990
CB
LEU

278
−21.264
99.813
−73.645
1.00
38.12

ATOM
991
CG
LEU

278
−22.126
99.491
−74.877
1.00
37.37

ATOM
992
CD1
LEU

278
−23.466
100.158
−74.821
1.00
39.03

ATOM
993
CD2
LEU

278
−21.388
99.958
−76.105
1.00
37.19

ATOM
994
C
LEU

278
−22.407
98.236
−72.085
1.00
40.69

ATOM
995
O
LEU

278
−23.583
98.030
−72.385
1.00
40.65

ATOM
996
N
GLU

279
−21.606
97.292
−71.626
1.00
42.71

ATOM
997
CA
GLU

279
−22.054
95.910
−71.488
1.00
44.42

ATOM
998
CB
GLU

279
−20.832
94.996
−71.352
1.00
47.35

ATOM
999
CG
GLU

279
−19.664
95.380
−72.283
1.00
51.14

ATOM
1000
CD
GLU

279
−18.950
96.657
−71.812
1.00
55.38

ATOM
1001
OE1
GLU

279
−18.934
96.864
−70.574
1.00
57.08

ATOM
1002
OE2
GLU

279
−18.402
97.438
−72.646
1.00
57.18

ATOM
1003
C
GLU

279
−23.003
95.738
−70.307
1.00
43.66

ATOM
1004
O
GLU

279
−23.809
94.814
−70.265
1.00
44.78

ATOM
1005
N
ASN

280
−22.913
96.648
−69.353
1.00
42.86

ATOM
1006
CA
ASN

280
−23.771
96.605
−68.187
1.00
43.61

ATOM
1007
CB
ASN

280
−23.032
97.219
−66.988
1.00
44.97

ATOM
1008
CG
ASN

280
−22.262
96.195
−66.159
1.00
46.33

ATOM
1009
OD1
ASN

280
−21.285
95.605
−66.599
1.00
49.39

ATOM
1010
ND2
ASN

280
−22.706
96.000
−64.933
1.00
49.29

ATOM
1011
C
ASN

280
−25.079
97.391
−68.434
1.00
43.20

ATOM
1012
O
ASN

280
−25.821
97.641
−67.498
1.00
44.95

ATOM
1013
N
LEU

281
−25.374
97.783
−69.672
1.00
40.99

ATOM
1014
CA
LEU

281
−26.581
98.568
−69.916
1.00
39.76

ATOM
1015
CB
LEU

281
−26.222
99.902
−70.585
1.00
36.50

ATOM
1016
CG
LEU

281
−25.347
100.750
−69.651
1.00
37.63

ATOM
1017
CD1
LEU

281
−24.798
101.997
−70.320
1.00
34.48

ATOM
1018
CD2
LEU

281
−26.169
101.104
−68.451
1.00
38.95

ATOM
1019
C
LEU

281
−27.642
97.871
−70.722
1.00
41.40

ATOM
1020
O
LEU

281
−27.373
97.350
−71.797
1.00
41.39

ATOM
1021
N
MET

282
−28.858
97.857
−70.183
1.00
43.20

ATOM
1022
CA
MET

282
−30.014
97.256
−70.851
1.00
44.72

ATOM
1023
CB
MET

282
−30.422
95.996
−70.123
1.00
43.76

ATOM
1024
CG
MET

282
−29.466
94.890
−70.334
1.00
46.63

ATOM
1025
SD
MET

282
−30.291
93.309
−70.088
1.00
50.69

ATOM
1026
CE
MET

282
−30.382
93.294
−68.257
1.00
51.55

ATOM
1027
C
MET

282
−31.207
98.241
−70.901
1.00
45.67

ATOM
1028
O
MET

282
−31.231
99.245
−70.177
1.00
46.72

ATOM
1029
N
LEU

283
−32.180
97.979
−71.765
1.00
44.26

ATOM
1030
CA
LEU

283
−33.356
98.835
−71.840
1.00
44.16

ATOM
1031
CB
LEU

283
−33.662
99.237
−73.291
1.00
41.73

ATOM
1032
CG
LEU

283
−32.705
100.063
−74.164
1.00
41.56

ATOM
1033
CD1
LEU

283
−33.409
100.385
−75.477
1.00
39.31

ATOM
1034
CD2
LEU

283
−32.294
101.359
−73.474
1.00
39.00

ATOM
1035
C
LEU

283
−34.535
98.027
−71.305
1.00
46.47

ATOM
1036
O
LEU

283
−34.590
96.814
−71.510
1.00
44.43

ATOM
1037
N
ASP

284
−35.469
98.674
−70.605
1.00
48.97

ATOM
1038
CA
ASP

284
−36.650
97.937
−70.140
1.00
51.54

ATOM
1039
CB
ASP

284
−37.173
98.436
−68.771
1.00
51.43

ATOM
1040
CG
ASP

284
−37.637
99.898
−68.773
1.00
51.84

ATOM
1041
OD1
ASP

284
−37.973
100.454
−69.838
1.00
50.58

ATOM
1042
OD2
ASP

284
−37.683
100.483
−67.665
1.00
52.12

ATOM
1043
C
ASP

284
−37.764
98.005
−71.210
1.00
53.72

ATOM
1044
O
ASP

284
−37.669
98.774
−72.178
1.00
52.20

ATOM
1045
N
LYS

285
−38.798
97.183
−71.048
1.00
55.54

ATOM
1046
CA
LYS

285
−39.910
97.136
−72.000
1.00
56.99

ATOM
1047
CB
LYS

285
−41.120
96.496
−71.330
1.00
57.83

ATOM
1048
CG
LYS

285
−41.527
97.200
−70.058
1.00
60.93

ATOM
1049
CD
LYS

285
−42.642
96.446
−69.371
1.00
63.52

ATOM
1050
CE
LYS

285
−42.950
97.044
−68.008
1.00
66.90

ATOM
1051
NZ
LYS

285
−41.877
96.789
−66.997
1.00
67.28

ATOM
1052
C
LYS

285
−40.310
98.496
−72.574
1.00
56.20

ATOM
1053
O
LYS

285
−40.818
98.580
−73.694
1.00
55.97

ATOM
1054
N
ASP

286
−40.062
99.556
−71.815
1.00
55.50

ATOM
1055
CA
ASP

286
−40.426
100.894
−72.249
1.00
56.10

ATOM
1056
CB
ASP

286
−40.989
101.678
−71.060
1.00
57.07

ATOM
1057
CG
ASP

286
−42.273
101.076
−70.513
1.00
58.89

ATOM
1058
OD1
ASP

286
−43.227
100.908
−71.307
1.00
60.61

ATOM
1059
OD2
ASP

286
−42.328
100.782
−69.291
1.00
58.93

ATOM
1060
C
ASP

286
−39.345
101.734
−72.929
1.00
55.50

ATOM
1061
O
ASP

286
−39.646
102.770
−73.502
1.00
56.75

ATOM
1062
N
GLY

287
−38.090
101.316
−72.863
1.00
54.81

ATOM
1063
CA
GLY

287
−37.037
102.098
−73.500
1.00
51.56

ATOM
1064
C
GLY

287
−36.178
102.825
−72.484
1.00
50.79

ATOM
1065
O
GLY

287
−35.283
103.592
−72.845
1.00
50.78

ATOM
1066
N
HIS

288
−36.457
102.593
−71.205
1.00
49.54

ATOM
1067
CA
HIS

288
−35.700
103.211
−70.117
1.00
48.54

ATOM
1068
CB
HIS

288
−36.607
103.414
−68.911
1.00
50.42

ATOM
1069
CG
HIS

288
−37.503
104.594
−69.035
1.00
51.68

ATOM
1070
CD2
HIS

288
−38.828
104.684
−69.285
1.00
52.15

ATOM
1071
ND1
HIS

288
−37.037
105.888
−68.938
1.00
52.82

ATOM
1072
CE1
HIS

288
−38.043
106.724
−69.122
1.00
54.05

ATOM
1073
NE2
HIS

288
−39.142
106.018
−69.335
1.00
52.91

ATOM
1074
C
HIS

288
−34.488
102.366
−69.704
1.00
46.68

ATOM
1075
O
HIS

288
−34.597
101.152
−69.499
1.00
45.61

ATOM
1076
N
ILE

289
−33.341
103.023
−69.562
1.00
44.04

ATOM
1077
CA
ILE

289
−32.124
102.328
−69.196
1.00
43.16

ATOM
1078
CB
ILE

289
−30.914
103.271
−69.247
1.00
43.33

ATOM
1079
CG2
ILE

289
−30.311
103.442
−67.857
1.00
43.11

ATOM
1080
CG1
ILE

289
−29.907
102.722
−70.263
1.00
45.10

ATOM
1081
CD1
ILE

289
−28.589
103.483
−70.385
1.00
46.75

ATOM
1082
C
ILE

289
−32.140
101.607
−67.851
1.00
42.02

ATOM
1083
O
ILE

289
−32.802
102.022
−66.893
1.00
42.42

ATOM
1084
N
LYS

290
−31.416
100.498
−67.807
1.00
40.39

ATOM
1085
CA
LYS

290
−31.290
99.711
−66.596
1.00
39.28

ATOM
1086
CB
LYS

290
−32.146
98.455
−66.666
1.00
38.03

ATOM
1087
CG
LYS

290
−33.543
98.601
−66.124
1.00
36.87

ATOM
1088
CD
LYS

290
−33.506
98.866
−64.648
1.00
37.88

ATOM
1089
CE
LYS

290
−34.900
99.067
−64.100
1.00
38.01

ATOM
1090
NZ
LYS

290
−34.888
99.219
−62.604
1.00
38.30

ATOM
1091
C
LYS

290
−29.846
99.306
−66.478
1.00
38.75

ATOM
1092
O
LYS

290
−29.388
98.468
−67.248
1.00
39.10

ATOM
1093
N
ILE

291
−29.127
99.936
−65.552
1.00
39.18

ATOM
1094
CA
ILE

291
−27.729
99.616
−65.280
1.00
40.53

ATOM
1095
CB
ILE

291
−27.102
100.659
−64.371
1.00
40.48

ATOM
1096
CG2
ILE

291
−25.636
100.353
−64.175
1.00
41.38

ATOM
1097
CG1
ILE

291
−27.296
102.050
−64.980
1.00
40.46

ATOM
1098
CD1
ILE

291
−26.629
103.149
−64.222
1.00
37.02

ATOM
1099
C
ILE

291
−27.739
98.275
−64.546
1.00
42.36

ATOM
1100
O
ILE

291
−28.198
98.160
−63.417
1.00
40.43

ATOM
1101
N
THR

292
−27.242
97.255
−65.215
1.00
46.18

ATOM
1102
CA
THR

292
−27.212
95.915
−64.685
1.00
50.40

ATOM
1103
CB
THR

292
−27.356
94.967
−65.826
1.00
50.36

ATOM
1104
OG1
THR

292
−28.352
94.004
−65.504
1.00
51.44

ATOM
1105
CG2
THR

292
−26.031
94.303
−66.124
1.00
51.92

ATOM
1106
C
THR

292
−25.923
95.629
−63.930
1.00
53.75

ATOM
1107
O
THR

292
−24.962
96.386
−64.023
1.00
54.59

ATOM
1108
N
ASP

293
−25.893
94.538
−63.174
1.00
58.48

ATOM
1109
CA
ASP

293
−24.682
94.209
−62.411
1.00
62.70

ATOM
1110
CB
ASP

293
−25.012
94.041
−60.917
1.00
64.65

ATOM
1111
CG
ASP

293
−23.760
94.011
−60.029
1.00
67.21

ATOM
1112
OD1
ASP

293
−22.766
93.321
−60.391
1.00
68.04

ATOM
1113
OD2
ASP

293
−23.779
94.678
−58.962
1.00
66.05

ATOM
1114
C
ASP

293
−23.963
92.954
−62.913
1.00
63.92

ATOM
1115
O
ASP

293
−23.813
91.981
−62.181
1.00
64.24

ATOM
1116
N
PHE

294
−23.539
92.979
−64.168
1.00
65.83

ATOM
1117
CA
PHE

294
−22.806
91.868
−64.757
1.00
68.53

ATOM
1118
CB
PHE

294
−23.521
90.530
−64.491
1.00
67.38

ATOM
1119
CG
PHE

294
−24.991
90.534
−64.811
1.00
65.59

ATOM
1120
CD1
PHE

294
−25.433
90.424
−66.124
1.00
63.34

ATOM
1121
CD2
PHE

294
−25.940
90.626
−63.783
1.00
65.16

ATOM
1122
CE1
PHE

294
−26.801
90.404
−66.419
1.00
64.24

ATOM
1123
CE2
PHE

294
−27.316
90.605
−64.059
1.00
64.73

ATOM
1124
CZ
PHE

294
−27.750
90.494
−65.385
1.00
63.90

ATOM
1125
C
PHE

294
−22.551
92.046
−66.254
1.00
71.35

ATOM
1126
O
PHE

294
−23.113
92.943
−66.899
1.00
73.04

ATOM
1127
N
GLY

295
−21.679
91.196
−66.793
1.00
72.68

ATOM
1128
CA
GLY

295
−21.356
91.245
−68.205
1.00
73.62

ATOM
1129
C
GLY

295
−22.030
90.094
−68.928
1.00
74.66

ATOM
1130
O
GLY

295
−22.020
88.958
−68.449
1.00
73.51

ATOM
1131
N
ALA

296
−22.623
90.394
−70.080
1.00
75.77

ATOM
1132
CA
ALA

296
−23.312
89.384
−70.871
1.00
76.34

ATOM
1133
CB
ALA

296
−24.361
90.050
−71.752
1.00
75.21

ATOM
1134
C
ALA

296
−22.313
88.596
−71.733
1.00
77.70

ATOM
1135
O
ALA

296
−22.126
87.378
−71.560
1.00
77.57

ATOM
1136
N
THR

313
−14.819
92.287
−75.520
1.00
61.26

ATOM
1137
CA
THR

313
−14.683
93.743
−75.449
1.00
61.34

ATOM
1138
CB
THR

313
−16.018
94.393
−74.946
1.00
62.47

ATOM
1139
OG1
THR

313
−16.491
93.701
−73.780
1.00
61.36

ATOM
1140
CG2
THR

313
−17.105
94.324
−76.048
1.00
63.50

ATOM
1141
C
THR

313
−13.497
94.217
−74.576
1.00
59.67

ATOM
1142
O
THR

313
−13.333
93.780
−73.438
1.00
59.35

ATOM
1143
N
PRO

314
−12.657
95.119
−75.116
1.00
57.55

ATOM
1144
CD
PRO

314
−12.756
95.646
−76.488
1.00
56.93

ATOM
1145
CA
PRO

314
−11.480
95.677
−74.429
1.00
55.87

ATOM
1146
CB
PRO

314
−10.828
96.559
−75.504
1.00
55.86

ATOM
1147
CG
PRO

314
−11.319
95.995
−76.790
1.00
57.18

ATOM
1148
C
PRO

314
−11.859
96.498
−73.196
1.00
54.26

ATOM
1149
O
PRO

314
−12.676
97.407
−73.291
1.00
55.26

ATOM
1150
N
GLU

315
−11.264
96.194
−72.048
1.00
52.49

ATOM
1151
CA
GLU

315
−11.561
96.934
−70.828
1.00
51.35

ATOM
1152
CB
GLU

315
−10.957
96.252
−69.616
1.00
53.09

ATOM
1153
CG
GLU

315
−11.694
95.032
−69.164
1.00
60.50

ATOM
1154
CD
GLU

315
−11.734
94.927
−67.643
1.00
65.03

ATOM
1155
OE1
GLU

315
−12.688
95.482
−67.023
1.00
65.47

ATOM
1156
OE2
GLU

315
−10.797
94.304
−67.073
1.00
67.26

ATOM
1157
C
GLU

315
−11.030
98.355
−70.865
1.00
50.05

ATOM
1158
O
GLU

315
−9.906
98.591
−71.284
1.00
51.67

ATOM
1159
N
TYR

316
−11.834
99.314
−70.428
1.00
47.11

ATOM
1160
CA
TYR

316
−11.365
100.685
−70.402
1.00
43.35

ATOM
1161
CB
TYR

316
−12.167
101.573
−71.360
1.00
40.98

ATOM
1162
CG
TYR

316
−11.678
101.609
−72.786
1.00
40.11

ATOM
1163
CD1
TYR

316
−12.024
100.610
−73.685
1.00
41.02

ATOM
1164
CE1
TYR

316
−11.627
100.660
−75.021
1.00
42.06

ATOM
1165
CD2
TYR

316
−10.903
102.679
−73.255
1.00
42.01

ATOM
1166
CE2
TYR

316
−10.489
102.754
−74.609
1.00
41.47

ATOM
1167
CZ
TYR

316
−10.859
101.736
−75.492
1.00
44.04

ATOM
1168
OH
TYR

316
−10.487
101.776
−76.844
1.00
44.56

ATOM
1169
C
TYR

316
−11.474
101.212
−68.974
1.00
41.97

ATOM
1170
O
TYR

316
−12.354
102.030
−68.648
1.00
41.74

ATOM
1171
N
LEU

317
−10.601
100.709
−68.113
1.00
38.94

ATOM
1172
CA
LEU

317
−10.572
101.165
−66.733
1.00
38.79

ATOM
1173
CB
LEU

317
−9.578
100.336
−65.920
1.00
37.70

ATOM
1174
CG
LEU

317
−9.799
98.842
−65.770
1.00
36.96

ATOM
1175
CD1
LEU

317
−8.726
98.351
−64.804
1.00
34.85

ATOM
1176
CD2
LEU

317
−11.207
98.517
−65.258
1.00
34.60

ATOM
1177
C
LEU

317
−10.123
102.633
−66.655
1.00
36.86

ATOM
1178
O
LEU

317
−9.390
103.107
−67.515
1.00
36.87

ATOM
1179
N
ALA

318
−10.540
103.346
−65.618
1.00
35.70

ATOM
1180
CA
ALA

318
−10.116
104.728
−65.474
1.00
37.61

ATOM
1181
CB
ALA

318
−10.755
105.345
−64.259
1.00
37.33

ATOM
1182
C
ALA

318
−8.604
104.736
−65.304
1.00
38.70

ATOM
1183
O
ALA

318
−8.026
103.777
−64.798
1.00
40.54

ATOM
1184
N
PRO

319
−7.934
105.807
−65.734
1.00
38.80

ATOM
1185
CD
PRO

319
−8.351
106.906
−66.606
1.00
39.29

ATOM
1186
CA
PRO

319
−6.487
105.813
−65.561
1.00
38.47

ATOM
1187
CB
PRO

319
−6.052
107.101
−66.245
1.00
37.53

ATOM
1188
CG
PRO

319
−7.287
107.900
−66.314
1.00
39.33

ATOM
1189
C
PRO

319
−6.046
105.739
−64.114
1.00
39.51

ATOM
1190
O
PRO

319
−5.009
105.149
−63.820
1.00
38.97

ATOM
1191
N
GLU

320
−6.820
106.309
−63.198
1.00
40.43

ATOM
1192
CA
GLU

320
−6.417
106.251
−61.792
1.00
43.60

ATOM
1193
CB
GLU

320
−7.214
107.259
−60.931
1.00
44.36

ATOM
1194
CG
GLU

320
−8.720
107.052
−60.916
1.00
47.85

ATOM
1195
CD
GLU

320
−9.455
107.815
−62.020
1.00
48.76

ATOM
1196
OE1
GLU

320
−8.982
107.821
−63.179
1.00
50.53

ATOM
1197
OE2
GLU

320
−10.522
108.395
−61.723
1.00
48.20

ATOM
1198
C
GLU

320
−6.580
104.815
−61.263
1.00
44.50

ATOM
1199
O
GLU

320
−6.010
104.434
−60.232
1.00
45.42

ATOM
1200
N
VAL

321
−7.370
104.015
−61.967
1.00
44.14

ATOM
1201
CA
VAL

321
−7.540
102.638
−61.567
1.00
45.55

ATOM
1202
CB
VAL

321
−8.818
102.032
−62.206
1.00
45.38

ATOM
1203
CG1
VAL

321
−8.820
100.525
−62.069
1.00
42.63

ATOM
1204
CG2
VAL

321
−10.038
102.607
−61.530
1.00
45.16

ATOM
1205
C
VAL

321
−6.271
101.898
−62.041
1.00
47.14

ATOM
1206
O
VAL

321
−5.714
101.074
−61.308
1.00
47.99

ATOM
1207
N
LEU

322
−5.812
102.222
−63.254
1.00
46.59

ATOM
1208
CA
LEU

322
−4.609
101.634
−63.841
1.00
45.62

ATOM
1209
CB
LEU

322
−4.481
102.057
−65.295
1.00
42.44

ATOM
1210
CG
LEU

322
−5.494
101.455
−66.250
1.00
40.66

ATOM
1211
CD1
LEU

322
−5.222
101.899
−67.698
1.00
39.43

ATOM
1212
CD2
LEU

322
−5.410
99.965
−66.116
1.00
38.54

ATOM
1213
C
LEU

322
−3.312
102.023
−63.131
1.00
46.94

ATOM
1214
O
LEU

322
−2.427
101.191
−62.905
1.00
47.93

ATOM
1215
N
GLU

323
−3.188
103.290
−62.782
1.00
48.12

ATOM
1216
CA
GLU

323
−1.967
103.745
−62.144
1.00
50.05

ATOM
1217
CB
GLU

323
−1.677
105.211
−62.545
1.00
48.81

ATOM
1218
CG
GLU

323
−0.359
105.785
−62.024
1.00
50.87

ATOM
1219
CD
GLU

323
0.023
107.151
−62.641
1.00
52.66

ATOM
1220
OE1
GLU

323
−0.859
108.010
−62.882
1.00
51.24

ATOM
1221
OE2
GLU

323
1.227
107.384
−62.862
1.00
53.66

ATOM
1222
C
GLU

323
−1.952
103.575
−60.627
1.00
51.25

ATOM
1223
O
GLU

323
−0.906
103.304
−60.055
1.00
54.36

ATOM
1224
N
ASP

324
−3.084
103.697
−59.953
1.00
50.61

ATOM
1225
CA
ASP

324
−3.037
103.554
−58.512
1.00
50.05

ATOM
1226
CB
ASP

324
−3.044
104.925
−57.846
1.00
52.30

ATOM
1227
CG
ASP

324
−1.834
105.750
−58.219
1.00
55.74

ATOM
1228
OD1
ASP

324
−0.725
105.159
−58.232
1.00
58.08

ATOM
1229
OD2
ASP

324
−1.978
106.975
−58.488
1.00
56.37

ATOM
1230
C
ASP

324
−4.129
102.717
−57.927
1.00
49.96

ATOM
1231
O
ASP

324
−4.458
102.865
−56.755
1.00
50.47

ATOM
1232
N
ASN

325
−4.694
101.830
−58.731
1.00
49.93

ATOM
1233
CA
ASN

325
−5.772
100.970
−58.255
1.00
49.22

ATOM
1234
CB
ASN

325
−5.184
99.796
−57.495
1.00
46.61

ATOM
1235
CG
ASN

325
−6.211
98.775
−57.158
1.00
47.05

ATOM
1236
OD1
ASN

325
−6.958
98.324
−58.033
1.00
47.61

ATOM
1237
ND2
ASN

325
−6.269
98.389
−55.888
1.00
44.60

ATOM
1238
C
ASN

325
−6.754
101.742
−57.352
1.00
49.53

ATOM
1239
O
ASN

325
−7.311
101.204
−56.393
1.00
49.05

ATOM
1240
N
ASP

326
−6.962
103.008
−57.704
1.00
50.17

ATOM
1241
CA
ASP

326
−7.831
103.937
−56.975
1.00
50.18

ATOM
1242
CB
ASP

326
−7.149
105.309
−56.995
1.00
53.10

ATOM
1243
CG
ASP

326
−7.929
106.362
−56.273
1.00
56.35

ATOM
1244
OD1
ASP

326
−7.509
107.537
−56.325
1.00
58.45

ATOM
1245
OD2
ASP

326
−8.955
106.024
−55.655
1.00
58.70

ATOM
1246
C
ASP

326
−9.273
104.030
−57.540
1.00
48.15

ATOM
1247
O
ASP

326
−9.510
104.626
−58.591
1.00
47.03

ATOM
1248
N
TYR

327
−10.228
103.433
−56.836
1.00
45.99

ATOM
1249
CA
TYR

327
−11.616
103.447
−57.281
1.00
45.38

ATOM
1250
CB
TYR

327
−12.271
102.063
−57.137
1.00
43.12

ATOM
1251
CG
TYR

327
−11.819
101.000
−58.118
1.00
42.93

ATOM
1252
CD1
TYR

327
−10.610
100.306
−57.946
1.00
42.61

ATOM
1253
CE1
TYR

327
−10.225
99.290
−58.835
1.00
42.42

ATOM
1254
CD2
TYR

327
−12.614
100.658
−59.203
1.00
42.05

ATOM
1255
CE2
TYR

327
−12.238
99.657
−60.100
1.00
41.56

ATOM
1256
CZ
TYR

327
−11.048
98.970
−59.919
1.00
42.45

ATOM
1257
OH
TYR

327
−10.694
97.968
−60.826
1.00
41.82

ATOM
1258
C
TYR

327
−12.465
104.444
−56.496
1.00
46.49

ATOM
1259
O
TYR

327
−13.230
104.042
−55.614
1.00
46.90

ATOM
1260
N
GLY

328
−12.333
105.733
−56.807
1.00
45.77

ATOM
1261
CA
GLY

328
−13.149
106.738
−56.142
1.00
45.22

ATOM
1262
C
GLY

328
−14.339
107.091
−57.033
1.00
45.48

ATOM
1263
O
GLY

328
−14.499
106.496
−58.114
1.00
45.70

ATOM
1264
N
ARG

329
−15.173
108.037
−56.591
1.00
43.69

ATOM
1265
CA
ARG

329
−16.339
108.486
−57.361
1.00
42.80

ATOM
1266
CB
ARG

329
−16.799
109.864
−56.888
1.00
44.61

ATOM
1267
CG
ARG

329
−17.258
110.041
−55.457
1.00
44.55

ATOM
1268
CD
ARG

329
−16.877
111.454
−55.025
1.00
43.18

ATOM
1269
NE
ARG

329
−16.989
112.379
−56.143
1.00
41.78

ATOM
1270
CZ
ARG

329
−16.297
113.511
−56.280
1.00
43.13

ATOM
1271
NH1
ARG

329
−15.409
113.903
−55.368
1.00
40.29

ATOM
1272
NH2
ARG

329
−16.497
114.263
−57.355
1.00
44.31

ATOM
1273
C
ARG

329
−16.014
108.652
−58.845
1.00
42.35

ATOM
1274
O
ARG

329
−16.679
108.105
−59.713
1.00
42.55

ATOM
1275
N
ALA

330
−14.996
109.464
−59.109
1.00
41.66

ATOM
1276
CA
ALA

330
−14.552
109.782
−60.453
1.00
41.23

ATOM
1277
CB
ALA

330
−13.212
110.456
−60.386
1.00
40.72

ATOM
1278
C
ALA

330
−14.513
108.637
−61.471
1.00
41.72

ATOM
1279
O
ALA

330
−14.745
108.868
−62.649
1.00
43.52

ATOM
1280
N
VAL

331
−14.235
107.408
−61.049
1.00
41.60

ATOM
1281
CA
VAL

331
−14.193
106.309
−62.017
1.00
40.30

ATOM
1282
CB
VAL

331
−13.656
104.980
−61.391
1.00
38.70

ATOM
1283
CG1
VAL

331
−12.310
105.224
−60.787
1.00
38.40

ATOM
1284
CG2
VAL

331
−14.604
104.436
−60.355
1.00
38.50

ATOM
1285
C
VAL

331
−15.552
106.049
−62.654
1.00
39.89

ATOM
1286
O
VAL

331
−15.632
105.459
−63.733
1.00
40.50

ATOM
1287
N
ASP

332
−16.615
106.487
−61.984
1.00
38.53

ATOM
1288
CA
ASP

332
−17.958
106.304
−62.515
1.00
39.28

ATOM
1289
CB
ASP

332
−19.007
106.559
−61.441
1.00
40.53

ATOM
1290
CG
ASP

332
−19.059
105.468
−60.439
1.00
42.03

ATOM
1291
OD1
ASP

332
−18.868
104.312
−60.876
1.00
44.04

ATOM
1292
OD2
ASP

332
−19.294
105.758
−59.241
1.00
42.18

ATOM
1293
C
ASP

332
−18.222
107.243
−63.679
1.00
38.44

ATOM
1294
O
ASP

332
−18.936
106.901
−64.630
1.00
36.56

ATOM
1295
N
TRP

333
−17.630
108.427
−63.595
1.00
37.75

ATOM
1296
CA
TRP

333
−17.811
109.449
−64.607
1.00
37.81

ATOM
1297
CB
TRP

333
−17.399
110.803
−64.025
1.00
36.84

ATOM
1298
CG
TRP

333
−18.360
111.209
−62.930
1.00
35.29

ATOM
1299
CD2
TRP

333
−19.794
111.187
−63.007
1.00
32.65

ATOM
1300
CE2
TRP

333
−20.284
111.584
−61.744
1.00
32.66

ATOM
1301
CE3
TRP

333
−20.704
110.885
−64.023
1.00
32.50

ATOM
1302
CD1
TRP

333
−18.048
111.605
−61.662
1.00
33.63

ATOM
1303
NE1
TRP

333
−19.202
111.826
−60.941
1.00
33.21

ATOM
1304
CZ2
TRP

333
−21.659
111.682
−61.467
1.00
32.05

ATOM
1305
CZ3
TRP

333
−22.075
110.984
−63.749
1.00
33.26

ATOM
1306
CH2
TRP

333
−22.536
111.385
−62.476
1.00
30.12

ATOM
1307
C
TRP

333
−17.035
109.095
−65.849
1.00
39.56

ATOM
1308
O
TRP

333
−17.500
109.328
−66.973
1.00
40.91

ATOM
1309
N
TRP

334
−15.864
108.504
−65.637
1.00
39.04

ATOM
1310
CA
TRP

334
−15.028
108.051
−66.720
1.00
37.22

ATOM
1311
CB
TRP

334
−13.735
107.505
−66.121
1.00
40.96

ATOM
1312
CG
TRP

334
−12.918
106.669
−67.041
1.00
42.79

ATOM
1313
CD2
TRP

334
−11.938
107.140
−67.955
1.00
43.52

ATOM
1314
CE2
TRP

334
−11.464
106.020
−68.673
1.00
43.53

ATOM
1315
CE3
TRP

334
−11.420
108.406
−68.251
1.00
44.18

ATOM
1316
CD1
TRP

334
−12.995
105.317
−67.217
1.00
41.70

ATOM
1317
NE1
TRP

334
−12.124
104.918
−68.198
1.00
42.64

ATOM
1318
CZ2
TRP

334
−10.488
106.127
−69.667
1.00
43.97

ATOM
1319
CZ3
TRP

334
−10.454
108.514
−69.236
1.00
43.63

ATOM
1320
CH2
TRP

334
−10.000
107.379
−69.938
1.00
42.90

ATOM
1321
C
TRP

334
−15.841
106.971
−67.442
1.00
35.47

ATOM
1322
O
TRP

334
−15.970
106.961
−68.661
1.00
36.91

ATOM
1323
N
GLY

335
−16.425
106.072
−66.674
1.00
34.13

ATOM
1324
CA
GLY

335
−17.221
105.030
−67.277
1.00
33.20

ATOM
1325
C
GLY

335
−18.317
105.669
−68.081
1.00
34.33

ATOM
1326
O
GLY

335
−18.660
105.208
−69.176
1.00
34.34

ATOM
1327
N
LEU

336
−18.872
106.745
−67.535
1.00
33.92

ATOM
1328
CA
LEU

336
−19.943
107.457
−68.211
1.00
33.63

ATOM
1329
CB
LEU

336
−20.366
108.695
−67.430
1.00
33.05

ATOM
1330
CG
LEU

336
−21.493
109.476
−68.121
1.00
30.46

ATOM
1331
CD1
LEU

336
−22.685
108.555
−68.460
1.00
31.04

ATOM
1332
CD2
LEU

336
−21.898
110.613
−67.216
1.00
28.30

ATOM
1333
C
LEU

336
−19.469
107.897
−69.565
1.00
33.40

ATOM
1334
O
LEU

336
−20.042
107.516
−70.592
1.00
33.66

ATOM
1335
N
GLY

337
−18.420
108.713
−69.537
1.00
32.38

ATOM
1336
CA
GLY

337
−17.821
109.237
−70.742
1.00
32.93

ATOM
1337
C
GLY

337
−17.460
108.178
−71.762
1.00
34.46

ATOM
1338
O
GLY

337
−17.879
108.281
−72.924
1.00
36.54

ATOM
1339
N
VAL

338
−16.670
107.182
−71.374
1.00
32.43

ATOM
1340
CA
VAL

338
−16.345
106.136
−72.341
1.00
33.15

ATOM
1341
CB
VAL

338
−15.505
104.962
−71.707
1.00
32.41

ATOM
1342
CG1
VAL

338
−15.446
103.780
−72.680
1.00
27.57

ATOM
1343
CG2
VAL

338
−14.083
105.438
−71.373
1.00
30.48

ATOM
1344
C
VAL

338
−17.636
105.557
−72.944
1.00
32.28

ATOM
1345
O
VAL

338
−17.672
105.215
−74.106
1.00
31.83

ATOM
1346
N
VAL

339
−18.694
105.455
−72.158
1.00
33.11

ATOM
1347
CA
VAL

339
−19.926
104.898
−72.694
1.00
37.56

ATOM
1348
CB
VAL

339
−20.964
104.598
−71.598
1.00
36.78

ATOM
1349
CG1
VAL

339
−22.313
104.291
−72.226
1.00
34.38

ATOM
1350
CG2
VAL

339
−20.506
103.436
−70.769
1.00
34.72

ATOM
1351
C
VAL

339
−20.548
105.866
−73.674
1.00
41.60

ATOM
1352
O
VAL

339
−20.890
105.509
−74.794
1.00
43.18

ATOM
1353
N
MET

340
−20.710
107.105
−73.272
1.00
44.34

ATOM
1354
CA
MET

340
−21.305
107.998
−74.217
1.00
47.85

ATOM
1355
CB
MET

340
−21.634
109.312
−73.541
1.00
48.32

ATOM
1356
CG
MET

340
−22.880
109.147
−72.735
1.00
51.33

ATOM
1357
SD
MET

340
−23.443
110.658
−72.056
1.00
59.88

ATOM
1358
CE
MET

340
−22.191
110.901
−70.873
1.00
58.75

ATOM
1359
C
MET

340
−20.435
108.160
−75.464
1.00
50.14

ATOM
1360
O
MET

340
−20.967
108.305
−76.579
1.00
52.11

ATOM
1361
N
TYR

341
−19.114
108.100
−75.301
1.00
49.46

ATOM
1362
CA
TYR

341
−18.229
108.223
−76.455
1.00
48.67

ATOM
1363
CB
TYR

341
−16.766
108.132
−76.045
1.00
48.69

ATOM
1364
CG
TYR

341
−15.774
108.344
−77.181
1.00
47.70

ATOM
1365
CD1
TYR

341
−15.734
107.493
−78.299
1.00
46.57

ATOM
1366
CE1
TYR

341
−14.791
107.668
−79.308
1.00
45.67

ATOM
1367
CD2
TYR

341
−14.847
109.377
−77.110
1.00
47.95

ATOM
1368
CE2
TYR

341
−13.900
109.564
−78.105
1.00
48.62

ATOM
1369
CZ
TYR

341
−13.869
108.715
−79.202
1.00
48.25

ATOM
1370
OH
TYR

341
−12.900
108.947
−80.164
1.00
46.56

ATOM
1371
C
TYR

341
−18.499
107.126
−77.467
1.00
48.36

ATOM
1372
O
TYR

341
−18.438
107.354
−78.669
1.00
48.58

ATOM
1373
N
GLU

342
−18.793
105.926
−76.998
1.00
47.95

ATOM
1374
CA
GLU

342
−19.029
104.874
−77.949
1.00
48.49

ATOM
1375
CB
GLU

342
−19.093
103.512
−77.274
1.00
50.95

ATOM
1376
CG
GLU

342
−18.572
102.395
−78.172
1.00
54.82

ATOM
1377
CD
GLU

342
−18.836
101.005
−77.608
1.00
57.85

ATOM
1378
OE1
GLU

342
−18.663
100.818
−76.382
1.00
59.56

ATOM
1379
OE2
GLU

342
−19.206
100.094
−78.390
1.00
57.97

ATOM
1380
C
GLU

342
−20.332
105.178
−78.612
1.00
48.20

ATOM
1381
O
GLU

342
−20.476
105.012
−79.812
1.00
48.67

ATOM
1382
N
MET

343
−21.275
105.673
−77.826
1.00
49.06

ATOM
1383
CA
MET

343
−22.607
105.984
−78.336
1.00
48.83

ATOM
1384
CB
MET

343
−23.518
106.434
−77.192
1.00
48.54

ATOM
1385
CG
MET

343
−24.128
105.302
−76.390
1.00
47.29

ATOM
1386
SD
MET

343
−25.065
105.970
−75.026
1.00
47.95

ATOM
1387
CE
MET

343
−26.127
104.620
−74.632
1.00
45.95

ATOM
1388
C
MET

343
−22.691
107.006
−79.467
1.00
49.03

ATOM
1389
O
MET

343
−23.331
106.772
−80.494
1.00
47.16

ATOM
1390
N
MET

344
−22.053
108.149
−79.274
1.00
49.81

ATOM
1391
CA
MET

344
−22.091
109.194
−80.277
1.00
50.59

ATOM
1392
CB
MET

344
−21.991
110.552
−79.571
1.00
50.34

ATOM
1393
CG
MET

344
−23.211
110.906
−78.688
1.00
49.99

ATOM
1394
SD
MET

344
−22.884
112.235
−77.445
1.00
50.65

ATOM
1395
CE
MET

344
−21.609
113.102
−78.152
1.00
51.66

ATOM
1396
C
MET

344
−20.993
109.033
−81.344
1.00
52.24

ATOM
1397
O
MET

344
−20.998
109.744
−82.353
1.00
52.10

ATOM
1398
N
CYS

345
−20.066
108.090
−81.133
1.00
52.55

ATOM
1399
CA
CYS

345
−18.983
107.863
−82.086
1.00
51.46

ATOM
1400
CB
CYS

345
−17.639
108.112
−81.425
1.00
52.21

ATOM
1401
SG
CYS

345
−17.325
109.829
−80.872
1.00
52.31

ATOM
1402
C
CYS

345
−18.984
106.472
−82.725
1.00
53.00

ATOM
1403
O
CYS

345
−18.323
106.263
−83.747
1.00
53.87

ATOM
1404
N
GLY

346
−19.724
105.528
−82.132
1.00
53.88

ATOM
1405
CA
GLY

346
−19.820
104.162
−82.660
1.00
54.16

ATOM
1406
C
GLY

346
−18.594
103.258
−82.487
1.00
55.22

ATOM
1407
O
GLY

346
−18.526
102.127
−82.996
1.00
54.37

ATOM
1408
N
ARG

347
−17.622
103.735
−81.730
1.00
55.38

ATOM
1409
CA
ARG

347
−16.408
102.972
−81.559
1.00
56.01

ATOM
1410
CB
ARG

347
−15.562
103.138
−82.817
1.00
57.25

ATOM
1411
CG
ARG

347
−15.291
104.588
−83.115
1.00
59.86

ATOM
1412
CD
ARG

347
−14.333
104.760
−84.255
1.00
64.85

ATOM
1413
NE
ARG

347
−13.725
106.094
−84.271
1.00
70.18

ATOM
1414
CZ
ARG

347
−14.316
107.196
−84.741
1.00
73.20

ATOM
1415
NH1
ARG

347
−15.553
107.134
−85.244
1.00
73.23

ATOM
1416
NH2
ARG

347
−13.662
108.365
−84.720
1.00
74.67

ATOM
1417
C
ARG

347
−15.674
103.518
−80.345
1.00
54.82

ATOM
1418
O
ARG

347
−15.829
104.704
−80.000
1.00
54.57

ATOM
1419
N
LEU

348
−14.873
102.664
−79.705
1.00
52.56

ATOM
1420
CA
LEU

348
−14.136
103.085
−78.515
1.00
50.40

ATOM
1421
CB
LEU

348
−13.570
101.869
−77.791
1.00
47.48

ATOM
1422
CG
LEU

348
−14.693
100.992
−77.231
1.00
45.56

ATOM
1423
CD1
LEU

348
−14.148
99.664
−76.836
1.00
44.34

ATOM
1424
CD2
LEU

348
−15.354
101.671
−76.041
1.00
45.21

ATOM
1425
C
LEU

348
−13.043
104.076
−78.866
1.00
50.04

ATOM
1426
O
LEU

348
−12.529
104.088
−79.976
1.00
48.92

ATOM
1427
N
PRO

349
−12.683
104.939
−77.917
1.00
51.10

ATOM
1428
CD
PRO

349
−13.202
105.059
−76.548
1.00
50.72

ATOM
1429
CA
PRO

349
−11.642
105.935
−78.185
1.00
52.64

ATOM
1430
CB
PRO

349
−11.346
106.542
−76.798
1.00
51.49

ATOM
1431
CG
PRO

349
−12.012
105.631
−75.823
1.00
51.83

ATOM
1432
C
PRO

349
−10.400
105.444
−78.917
1.00
53.85

ATOM
1433
O
PRO

349
−9.817
106.185
−79.706
1.00
53.86

ATOM
1434
N
PHE

350
−10.006
104.201
−78.686
1.00
56.07

ATOM
1435
CA
PHE

350
−8.825
103.663
−79.350
1.00
59.34

ATOM
1436
CB
PHE

350
−7.741
103.367
−78.303
1.00
55.77

ATOM
1437
CG
PHE

350
−7.378
104.546
−77.417
1.00
52.76

ATOM
1438
CD1
PHE

350
−7.568
104.479
−76.033
1.00
51.68

ATOM
1439
CD2
PHE

350
−6.749
105.677
−77.944
1.00
48.51

ATOM
1440
CE1
PHE

350
−7.124
105.513
−75.194
1.00
48.61

ATOM
1441
CE2
PHE

350
−6.309
106.703
−77.116
1.00
46.48

ATOM
1442
CZ
PHE

350
−6.492
106.622
−75.739
1.00
47.76

ATOM
1443
C
PHE

350
−9.178
102.367
−80.105
1.00
63.66

ATOM
1444
O
PHE

350
−8.379
101.437
−80.170
1.00
65.35

ATOM
1445
N
TYR

351
−10.367
102.318
−80.691
1.00
68.61

ATOM
1446
CA
TYR

351
−10.858
101.121
−81.386
1.00
73.08

ATOM
1447
CB
TYR

351
−12.190
101.415
−82.076
1.00
74.99

ATOM
1448
CG
TYR

351
−12.014
102.042
−83.441
1.00
77.23

ATOM
1449
CD1
TYR

351
−12.362
101.340
−84.604
1.00
78.33

ATOM
1450
CE1
TYR

351
−12.205
101.917
−85.869
1.00
79.59

ATOM
1451
CD2
TYR

351
−11.497
103.334
−83.574
1.00
77.34

ATOM
1452
CE2
TYR

351
−11.337
103.920
−84.829
1.00
79.10

ATOM
1453
CZ
TYR

351
−11.697
103.211
−85.970
1.00
80.28

ATOM
1454
OH
TYR

351
−11.601
103.815
−87.202
1.00
82.10

ATOM
1455
C
TYR

351
−9.962
100.449
−82.414
1.00
75.11

ATOM
1456
O
TYR

351
−10.107
99.246
−82.654
1.00
76.83

ATOM
1457
N
ASN

352
−9.067
101.196
−83.050
1.00
75.74

ATOM
1458
CA
ASN

352
−8.216
100.575
−84.056
1.00
77.97

ATOM
1459
CB
ASN

352
−8.127
101.479
−85.276
1.00
79.00

ATOM
1460
CG
ASN

352
−7.847
102.900
−84.909
1.00
80.39

ATOM
1461
OD1
ASN

352
−8.034
103.806
−85.714
1.00
80.82

ATOM
1462
ND2
ASN

352
−7.390
103.112
−83.683
1.00
81.68

ATOM
1463
C
ASN

352
−6.819
100.177
−83.574
1.00
79.11

ATOM
1464
O
ASN

352
−6.396
99.041
−83.792
1.00
79.92

ATOM
1465
N
GLN

353
−6.110
101.090
−82.917
1.00
79.23

ATOM
1466
CA
GLN

353
−4.773
100.797
−82.408
1.00
79.53

ATOM
1467
CB
GLN

353
−4.298
101.949
−81.519
1.00
78.93

ATOM
1468
CG
GLN

353
−4.329
103.304
−82.207
1.00
78.41

ATOM
1469
CD
GLN

353
−3.652
104.395
−81.391
1.00
79.43

ATOM
1470
OE1
GLN

353
−2.433
104.374
−81.175
1.00
79.09

ATOM
1471
NE2
GLN

353
−4.444
105.359
−80.931
1.00
79.05

ATOM
1472
C
GLN

353
−4.706
99.462
−81.640
1.00
80.21

ATOM
1473
O
GLN

353
−5.408
99.257
−80.652
1.00
80.41

ATOM
1474
N
ASP

354
−3.836
98.573
−82.113
1.00
81.30

ATOM
1475
CA
ASP

354
−3.630
97.229
−81.561
1.00
82.19

ATOM
1476
CB
ASP

354
−2.186
97.069
−81.045
1.00
82.85

ATOM
1477
CG
ASP

354
−1.707
95.603
−81.059
1.00
83.70

ATOM
1478
OD1
ASP

354
−2.412
94.722
−80.500
1.00
84.53

ATOM
1479
OD2
ASP

354
−0.620
95.337
−81.624
1.00
82.33

ATOM
1480
C
ASP

354
−4.618
96.764
−80.483
1.00
81.95

ATOM
1481
O
ASP

354
−5.694
96.258
−80.813
1.00
82.11

ATOM
1482
N
HIS

355
−4.250
96.924
−79.210
1.00
81.03

ATOM
1483
CA
HIS

355
−5.094
96.489
−78.096
1.00
80.71

ATOM
1484
CB
HIS

355
−5.745
95.142
−78.415
1.00
82.86

ATOM
1485
CG
HIS

355
−6.471
94.531
−77.254
1.00
85.76

ATOM
1486
CD2
HIS

355
−6.160
93.475
−76.467
1.00
87.26

ATOM
1487
ND1
HIS

355
−7.660
95.032
−76.769
1.00
87.41

ATOM
1488
CE1
HIS

355
−8.050
94.311
−75.733
1.00
87.85

ATOM
1489
NE2
HIS

355
−7.159
93.359
−75.527
1.00
87.74

ATOM
1490
C
HIS

355
−4.260
96.338
−76.833
1.00
79.81

ATOM
1491
O
HIS

355
−4.703
96.661
−75.730
1.00
79.19

ATOM
1492
N
GLU

356
−3.055
95.810
−77.005
1.00
79.13

ATOM
1493
CA
GLU

356
−2.133
95.617
−75.896
1.00
77.59

ATOM
1494
CB
GLU

356
−1.061
94.615
−76.289
1.00
80.02

ATOM
1495
CG
GLU

356
−1.624
93.352
−76.907
1.00
83.48

ATOM
1496
CD
GLU

356
−0.573
92.577
−77.683
1.00
86.23

ATOM
1497
OE1
GLU

356
−0.023
93.137
−78.661
1.00
86.65

ATOM
1498
OE2
GLU

356
−0.296
91.412
−77.315
1.00
87.72

ATOM
1499
C
GLU

356
−1.511
96.980
−75.633
1.00
75.49

ATOM
1500
O
GLU

356
−0.698
97.156
−74.723
1.00
74.40

ATOM
1501
N
ARG

357
−1.916
97.937
−76.461
1.00
72.73

ATOM
1502
CA
ARG

357
−1.466
99.306
−76.361
1.00
70.48

ATOM
1503
CB
ARG

357
−1.546
99.964
−77.735
1.00
72.58

ATOM
1504
CG
ARG

357
−0.207
100.160
−78.398
1.00
77.63

ATOM
1505
CD
ARG

357
−0.169
99.604
−79.814
1.00
80.59

ATOM
1506
NE
ARG

357
1.165
99.077
−80.109
1.00
83.88

ATOM
1507
CZ
ARG

357
1.518
98.504
−81.257
1.00
84.74

ATOM
1508
NH1
ARG

357
0.631
98.383
−82.240
1.00
85.51

ATOM
1509
NH2
ARG

357
2.754
98.040
−81.417
1.00
84.34

ATOM
1510
C
ARG

357
−2.343
100.077
−75.376
1.00
67.76

ATOM
1511
O
ARG

357
−2.035
101.214
−75.021
1.00
67.91

ATOM
1512
N
LEU

358
−3.432
99.457
−74.925
1.00
63.63

ATOM
1513
CA
LEU

358
−4.355
100.137
−74.016
1.00
60.15

ATOM
1514
CB
LEU

358
−5.553
99.236
−73.669
1.00
57.26

ATOM
1515
CG
LEU

358
−6.684
99.227
−74.713
1.00
54.60

ATOM
1516
CD1
LEU

358
−7.908
98.554
−74.161
1.00
53.63

ATOM
1517
CD2
LEU

358
−7.029
100.647
−75.095
1.00
52.19

ATOM
1518
C
LEU

358
−3.765
100.735
−72.747
1.00
58.49

ATOM
1519
O
LEU

358
−3.945
101.922
−72.508
1.00
58.73

ATOM
1520
N
PHE

359
−3.072
99.939
−71.937
1.00
56.63

ATOM
1521
CA
PHE

359
−2.477
100.452
−70.703
1.00
54.30

ATOM
1522
CB
PHE

359
−1.462
99.453
−70.140
1.00
51.83

ATOM
1523
CG
PHE

359
−0.861
99.870
−68.828
1.00
49.28

ATOM
1524
CD1
PHE

359
−1.503
99.577
−67.629
1.00
48.65

ATOM
1525
CD2
PHE

359
0.331
100.583
−68.790
1.00
48.91

ATOM
1526
CE1
PHE

359
−0.969
99.992
−66.403
1.00
47.05

ATOM
1527
CE2
PHE

359
0.880
101.005
−67.568
1.00
48.51

ATOM
1528
CZ
PHE

359
0.225
100.709
−66.372
1.00
48.33

ATOM
1529
C
PHE

359
−1.783
101.802
−70.947
1.00
54.90

ATOM
1530
O
PHE

359
−2.099
102.794
−70.288
1.00
55.02

ATOM
1531
N
GLU

360
−0.848
101.846
−71.896
1.00
55.38

ATOM
1532
CA
GLU

360
−0.123
103.089
−72.202
1.00
55.56

ATOM
1533
CB
GLU

360
1.065
102.819
−73.136
1.00
57.15

ATOM
1534
CG
GLU

360
1.748
101.460
−72.982
1.00
62.38

ATOM
1535
CD
GLU

360
1.157
100.399
−73.908
1.00
65.01

ATOM
1536
OE1
GLU

360
0.171
99.743
−73.494
1.00
66.75

ATOM
1537
OE2
GLU

360
1.667
100.235
−75.050
1.00
64.31

ATOM
1538
C
GLU

360
−1.021
104.158
−72.862
1.00
54.55

ATOM
1539
O
GLU

360
−0.868
105.361
−72.626
1.00
53.90

ATOM
1540
N
LEU

361
−1.943
103.716
−73.703
1.00
53.09

ATOM
1541
CA
LEU

361
−2.835
104.633
−74.385
1.00
52.99

ATOM
1542
CB
LEU

361
−3.697
103.856
−75.381
1.00
53.03

ATOM
1543
CG
LEU

361
−2.966
103.371
−76.633
1.00
51.61

ATOM
1544
CD1
LEU

361
−3.926
102.631
−77.512
1.00
52.09

ATOM
1545
CD2
LEU

361
−2.385
104.558
−77.391
1.00
52.42

ATOM
1546
C
LEU

361
−3.720
105.413
−73.411
1.00
52.83

ATOM
1547
O
LEU

361
−3.628
106.632
−73.309
1.00
52.67

ATOM
1548
N
ILE

362
−4.574
104.691
−72.694
1.00
51.97

ATOM
1549
CA
ILE

362
−5.482
105.283
−71.732
1.00
50.58

ATOM
1550
CB
ILE

362
−6.208
104.195
−70.937
1.00
49.70

ATOM
1551
CG2
ILE

362
−7.104
104.819
−69.860
1.00
47.94

ATOM
1552
CG1
ILE

362
−7.004
103.321
−71.898
1.00
47.22

ATOM
1553
CD1
ILE

362
−7.508
102.076
−71.252
1.00
47.62

ATOM
1554
C
ILE

362
−4.752
106.171
−70.753
1.00
51.35

ATOM
1555
O
ILE

362
−5.290
107.157
−70.285
1.00
52.23

ATOM
1556
N
LEU

363
−3.519
105.835
−70.428
1.00
51.85

ATOM
1557
CA
LEU

363
−2.816
106.657
−69.474
1.00
52.24

ATOM
1558
CB
LEU

363
−1.749
105.843
−68.760
1.00
50.66

ATOM
1559
CG
LEU

363
−2.313
104.876
−67.722
1.00
50.68

ATOM
1560
CD1
LEU

363
−1.325
103.767
−67.441
1.00
49.35

ATOM
1561
CD2
LEU

363
−2.649
105.640
−66.453
1.00
49.87

ATOM
1562
C
LEU

363
−2.188
107.880
−70.082
1.00
53.84

ATOM
1563
O
LEU

363
−2.310
108.962
−69.524
1.00
54.29

ATOM
1564
N
MET

364
−1.550
107.729
−71.240
1.00
55.93

ATOM
1565
CA
MET

364
−0.835
108.851
−71.848
1.00
57.84

ATOM
1566
CB
MET

364
0.673
108.561
−71.792
1.00
57.41

ATOM
1567
CG
MET

364
1.113
107.908
−70.495
1.00
58.69

ATOM
1568
SD
MET

364
2.879
107.503
−70.396
1.00
61.01

ATOM
1569
CE
MET

364
2.879
105.770
−70.850
1.00
59.26

ATOM
1570
C
MET

364
−1.196
109.277
−73.268
1.00
58.73

ATOM
1571
O
MET

364
−0.449
110.014
−73.892
1.00
60.34

ATOM
1572
N
GLU

365
−2.322
108.832
−73.791
1.00
59.20

ATOM
1573
CA
GLU

365
−2.695
109.218
−75.141
1.00
60.03

ATOM
1574
CB
GLU

365
−2.982
107.977
−75.979
1.00
61.60

ATOM
1575
CG
GLU

365
−3.395
108.284
−77.405
1.00
61.85

ATOM
1576
CD
GLU

365
−2.208
108.436
−78.298
1.00
62.17

ATOM
1577
OE1
GLU

365
−1.359
109.282
−77.961
1.00
62.61

ATOM
1578
OE2
GLU

365
−2.119
107.712
−79.319
1.00
63.68

ATOM
1579
C
GLU

365
−3.935
110.103
−75.138
1.00
60.53

ATOM
1580
O
GLU

365
−4.940
109.775
−74.495
1.00
59.82

ATOM
1581
N
GLU

366
−3.871
111.216
−75.866
1.00
61.00

ATOM
1582
CA
GLU

366
−5.005
112.129
−75.941
1.00
61.39

ATOM
1583
CB
GLU

366
−4.597
113.450
−76.591
1.00
63.37

ATOM
1584
CG
GLU

366
−4.258
113.348
−78.087
1.00
67.78

ATOM
1585
CD
GLU

366
−4.383
114.685
−78.820
1.00
69.43

ATOM
1586
OE1
GLU

366
−5.508
115.259
−78.847
1.00
69.67

ATOM
1587
OE2
GLU

366
−3.361
115.157
−79.368
1.00
69.98

ATOM
1588
C
GLU

366
−6.120
111.490
−76.760
1.00
61.39

ATOM
1589
O
GLU

366
−5.886
110.976
−77.858
1.00
60.86

ATOM
1590
N
ILE

367
−7.328
111.501
−76.213
1.00
61.54

ATOM
1591
CA
ILE

367
−8.471
110.942
−76.906
1.00
61.47

ATOM
1592
CB
ILE

367
−9.606
110.686
−75.943
1.00
60.89

ATOM
1593
CG2
ILE

367
−10.885
110.501
−76.713
1.00
61.95

ATOM
1594
CG1
ILE

367
−9.261
109.462
−75.081
1.00
60.19

ATOM
1595
CD1
ILE

367
−10.249
109.124
−73.986
1.00
56.88

ATOM
1596
C
ILE

367
−8.888
111.950
−77.965
1.00
63.20

ATOM
1597
O
ILE

367
−8.911
113.163
−77.717
1.00
63.34

ATOM
1598
N
ARG

368
−9.201
111.438
−79.150
1.00
64.36

ATOM
1599
CA
ARG

368
−9.556
112.264
−80.299
1.00
65.23

ATOM
1600
CB
ARG

368
−8.658
111.846
−81.474
1.00
69.04

ATOM
1601
CG
ARG

368
−8.856
112.574
−82.790
1.00
76.89

ATOM
1602
CD
ARG

368
−7.506
112.969
−83.416
1.00
82.05

ATOM
1603
NE
ARG

368
−6.914
114.116
−82.725
1.00
87.01

ATOM
1604
CZ
ARG

368
−6.646
115.294
−83.290
1.00
88.75

ATOM
1605
NH1
ARG

368
−6.906
115.506
−84.577
1.00
89.73

ATOM
1606
NH2
ARG

368
−6.133
116.276
−82.557
1.00
90.35

ATOM
1607
C
ARG

368
−11.029
112.091
−80.633
1.00
63.45

ATOM
1608
O
ARG

368
−11.560
110.988
−80.515
1.00
62.89

ATOM
1609
N
PHE

369
−11.686
113.177
−81.047
1.00
62.26

ATOM
1610
CA
PHE

369
−13.120
113.141
−81.376
1.00
60.85

ATOM
1611
CB
PHE

369
−13.894
114.147
−80.521
1.00
58.47

ATOM
1612
CG
PHE

369
−13.475
114.171
−79.098
1.00
55.69

ATOM
1613
CD1
PHE

369
−13.898
113.182
−78.224
1.00
53.89

ATOM
1614
CD2
PHE

369
−12.588
115.135
−78.651
1.00
54.16

ATOM
1615
CE1
PHE

369
−13.435
113.147
−76.921
1.00
53.32

ATOM
1616
CE2
PHE

369
−12.115
115.112
−77.353
1.00
53.82

ATOM
1617
CZ
PHE

369
−12.534
114.116
−76.481
1.00
52.90

ATOM
1618
C
PHE

369
−13.452
113.451
−82.825
1.00
61.47

ATOM
1619
O
PHE

369
−12.764
114.238
−83.481
1.00
60.78

ATOM
1620
N
PRO

370
−14.529
112.841
−83.337
1.00
62.58

ATOM
1621
CD
PRO

370
−15.245
111.734
−82.686
1.00
62.83

ATOM
1622
CA
PRO

370
−15.014
113.024
−84.708
1.00
64.77

ATOM
1623
CB
PRO

370
−16.273
112.165
−84.742
1.00
63.67

ATOM
1624
CG
PRO

370
−15.900
111.038
−83.862
1.00
62.77

ATOM
1625
C
PRO

370
−15.325
114.499
−84.960
1.00
67.04

ATOM
1626
O
PRO

370
−15.846
115.188
−84.075
1.00
66.93

ATOM
1627
N
ARG

371
−14.995
114.987
−86.155
1.00
69.45

ATOM
1628
CA
ARG

371
−15.249
116.383
−86.492
1.00
70.54

ATOM
1629
CB
ARG

371
−14.745
116.674
−87.913
1.00
73.31

ATOM
1630
CG
ARG

371
−13.262
116.315
−88.161
1.00
76.94

ATOM
1631
CD
ARG

371
−12.774
116.710
−89.589
1.00
80.18

ATOM
1632
NE
ARG

371
−13.485
115.988
−90.653
1.00
83.53

ATOM
1633
CZ
ARG

371
−13.091
114.836
−91.205
1.00
85.07

ATOM
1634
NH1
ARG

371
−11.963
114.238
−90.822
1.00
85.98

ATOM
1635
NH2
ARG

371
−13.854
114.256
−92.126
1.00
84.82

ATOM
1636
C
ARG

371
−16.762
116.628
−86.376
1.00
69.82

ATOM
1637
O
ARG

371
−17.203
117.636
−85.832
1.00
68.81

ATOM
1638
N
THR

372
−17.538
115.665
−86.862
1.00
69.75

ATOM
1639
CA
THR

372
−19.003
115.694
−86.841
1.00
71.11

ATOM
1640
CB
THR

372
−19.524
114.599
−87.794
1.00
71.17

ATOM
1641
OG1
THR

372
−20.880
114.278
−87.476
1.00
73.09

ATOM
1642
CG2
THR

372
−18.670
113.334
−87.666
1.00
71.70

ATOM
1643
C
THR

372
−19.619
115.477
−85.428
1.00
71.80

ATOM
1644
O
THR

372
−20.414
114.547
−85.219
1.00
72.12

ATOM
1645
N
LEU

373
−19.276
116.342
−84.469
1.00
71.42

ATOM
1646
CA
LEU

373
−19.758
116.190
−83.089
1.00
69.80

ATOM
1647
CB
LEU

373
−18.698
115.433
−82.279
1.00
70.86

ATOM
1648
CG
LEU

373
−19.076
114.509
−81.117
1.00
71.23

ATOM
1649
CD1
LEU

373
−19.837
113.303
−81.653
1.00
70.31

ATOM
1650
CD2
LEU

373
−17.816
114.061
−80.392
1.00
70.52

ATOM
1651
C
LEU

373
−19.994
117.558
−82.455
1.00
68.53

ATOM
1652
O
LEU

373
−19.044
118.321
−82.279
1.00
68.27

ATOM
1653
N
SER

374
−21.241
117.860
−82.098
1.00
67.32

ATOM
1654
CA
SER

374
−21.571
119.166
−81.514
1.00
67.55

ATOM
1655
CB
SER

374
−22.919
119.115
−80.797
1.00
66.97

ATOM
1656
OG
SER

374
−22.788
118.583
−79.489
1.00
67.60

ATOM
1657
C
SER

374
−20.486
119.627
−80.541
1.00
67.21

ATOM
1658
O
SER

374
−20.059
118.883
−79.669
1.00
69.14

ATOM
1659
N
PRO

375
−20.037
120.874
−80.668
1.00
65.82

ATOM
1660
CD
PRO

375
−20.692
121.978
−81.380
1.00
65.36

ATOM
1661
CA
PRO

375
−18.985
121.376
−79.773
1.00
64.80

ATOM
1662
CB
PRO

375
−18.886
122.853
−80.149
1.00
64.82

ATOM
1663
CG
PRO

375
−20.300
123.170
−80.532
1.00
66.04

ATOM
1664
C
PRO

375
−19.229
121.160
−78.280
1.00
63.31

ATOM
1665
O
PRO

375
−18.268
121.163
−77.489
1.00
61.84

ATOM
1666
N
GLU

376
−20.497
120.987
−77.892
1.00
61.85

ATOM
1667
CA
GLU

376
−20.819
120.753
−76.480
1.00
62.01

ATOM
1668
CB
GLU

376
−22.276
121.106
−76.147
1.00
61.80

ATOM
1669
CG
GLU

376
−23.296
120.418
−77.005
1.00
64.69

ATOM
1670
CD
GLU

376
−23.834
121.325
−78.113
1.00
66.85

ATOM
1671
OE1
GLU

376
−23.108
122.248
−78.564
1.00
67.43

ATOM
1672
OE2
GLU

376
−24.983
121.095
−78.546
1.00
65.89

ATOM
1673
C
GLU

376
−20.547
119.286
−76.162
1.00
61.28

ATOM
1674
O
GLU

376
−19.997
118.973
−75.094
1.00
61.94

ATOM
1675
N
ALA

377
−20.924
118.392
−77.082
1.00
58.93

ATOM
1676
CA
ALA

377
−20.663
116.957
−76.912
1.00
56.68

ATOM
1677
CB
ALA

377
−21.267
116.186
−78.065
1.00
55.69

ATOM
1678
C
ALA

377
−19.135
116.717
−76.839
1.00
55.03

ATOM
1679
O
ALA

377
−18.647
115.929
−76.038
1.00
52.86

ATOM
1680
N
LYS

378
−18.386
117.411
−77.682
1.00
54.47

ATOM
1681
CA
LYS

378
−16.946
117.290
−77.660
1.00
54.99

ATOM
1682
CB
LYS

378
−16.322
118.023
−78.868
1.00
57.80

ATOM
1683
CG
LYS

378
−14.778
118.182
−78.821
1.00
61.35

ATOM
1684
CD
LYS

378
−14.214
118.776
−80.137
1.00
64.11

ATOM
1685
CE
LYS

378
−12.696
119.099
−80.062
1.00
65.84

ATOM
1686
NZ
LYS

378
−12.139
119.690
−81.333
1.00
64.38

ATOM
1687
C
LYS

378
−16.492
117.928
−76.352
1.00
53.95

ATOM
1688
O
LYS

378
−15.357
117.731
−75.901
1.00
54.88

ATOM
1689
N
SER

379
−17.391
118.682
−75.731
1.00
52.17

ATOM
1690
CA
SER

379
−17.064
119.352
−74.475
1.00
49.37

ATOM
1691
CB
SER

379
−18.011
120.534
−74.224
1.00
48.67

ATOM
1692
OG
SER

379
−17.529
121.359
−73.169
1.00
47.44

ATOM
1693
C
SER

379
−17.171
118.364
−73.328
1.00
47.02

ATOM
1694
O
SER

379
−16.280
118.274
−72.479
1.00
43.80

ATOM
1695
N
LEU

380
−18.284
117.639
−73.329
1.00
45.31

ATOM
1696
CA
LEU

380
−18.589
116.632
−72.330
1.00
45.01

ATOM
1697
CB
LEU

380
−19.936
115.981
−72.677
1.00
42.73

ATOM
1698
CG
LEU

380
−20.567
115.047
−71.650
1.00
42.08

ATOM
1699
CD1
LEU

380
−20.777
115.803
−70.344
1.00
39.85

ATOM
1700
CD2
LEU

380
−21.873
114.459
−72.186
1.00
40.06

ATOM
1701
C
LEU

380
−17.472
115.570
−72.287
1.00
45.96

ATOM
1702
O
LEU

380
−16.728
115.449
−71.286
1.00
45.21

ATOM
1703
N
LEU

381
−17.348
114.806
−73.368
1.00
44.53

ATOM
1704
CA
LEU

381
−16.328
113.774
−73.419
1.00
43.33

ATOM
1705
CB
LEU

381
−16.241
113.199
−74.802
1.00
41.46

ATOM
1706
CG
LEU

381
−17.643
112.869
−75.242
1.00
41.01

ATOM
1707
CD1
LEU

381
−17.614
112.364
−76.674
1.00
39.08

ATOM
1708
CD2
LEU

381
−18.233
111.876
−74.270
1.00
40.64

ATOM
1709
C
LEU

381
−14.978
114.315
−73.020
1.00
43.61

ATOM
1710
O
LEU

381
−14.323
113.788
−72.128
1.00
43.42

ATOM
1711
N
ALA

382
−14.540
115.372
−73.672
1.00
44.81

ATOM
1712
CA
ALA

382
−13.243
115.903
−73.307
1.00
46.42

ATOM
1713
CB
ALA

382
−13.042
117.276
−73.939
1.00
46.11

ATOM
1714
C
ALA

382
−13.151
115.989
−71.781
1.00
46.76

ATOM
1715
O
ALA

382
−12.072
115.836
−71.212
1.00
47.69

ATOM
1716
N
GLY

383
−14.302
116.178
−71.129
1.00
46.94

ATOM
1717
CA
GLY

383
−14.339
116.330
−69.674
1.00
46.89

ATOM
1718
C
GLY

383
−14.605
115.087
−68.843
1.00
46.16

ATOM
1719
O
GLY

383
−14.119
114.944
−67.715
1.00
44.69

ATOM
1720
N
LEU

384
−15.409
114.190
−69.380
1.00
44.84

ATOM
1721
CA
LEU

384
−15.660
112.970
−68.663
1.00
44.28

ATOM
1722
CB
LEU

384
−16.835
112.218
−69.295
1.00
42.32

ATOM
1723
CG
LEU

384
−18.192
112.901
−69.109
1.00
41.84

ATOM
1724
CD1
LEU

384
−19.295
112.121
−69.807
1.00
39.23

ATOM
1725
CD2
LEU

384
−18.475
113.001
−67.611
1.00
40.93

ATOM
1726
C
LEU

384
−14.395
112.124
−68.735
1.00
45.06

ATOM
1727
O
LEU

384
−14.207
111.236
−67.915
1.00
46.62

ATOM
1728
N
LEU

385
−13.519
112.430
−69.695
1.00
44.98

ATOM
1729
CA
LEU

385
−12.294
111.653
−69.921
1.00
43.46

ATOM
1730
CB
LEU

385
−12.198
111.267
−71.385
1.00
40.19

ATOM
1731
CG
LEU

385
−13.448
110.502
−71.784
1.00
40.02

ATOM
1732
CD1
LEU

385
−13.576
110.453
−73.302
1.00
39.91

ATOM
1733
CD2
LEU

385
−13.391
109.138
−71.159
1.00
40.44

ATOM
1734
C
LEU

385
−10.963
112.240
−69.485
1.00
43.65

ATOM
1735
O
LEU

385
−9.908
111.747
−69.880
1.00
43.05

ATOM
1736
N
LYS

386
−10.999
113.295
−68.685
1.00
44.64

ATOM
1737
CA
LYS

386
−9.765
113.861
−68.183
1.00
46.79

ATOM
1738
CB
LYS

386
−10.074
115.018
−67.227
1.00
48.36

ATOM
1739
CG
LYS

386
−10.220
116.375
−67.909
1.00
52.10

ATOM
1740
CD
LYS

386
−8.891
116.759
−68.584
1.00
56.86

ATOM
1741
CE
LYS

386
−8.843
118.214
−69.092
1.00
58.05

ATOM
1742
NZ
LYS

386
−8.448
119.203
−68.027
1.00
59.99

ATOM
1743
C
LYS

386
−9.035
112.718
−67.458
1.00
47.37

ATOM
1744
O
LYS

386
−9.620
112.013
−66.640
1.00
47.60

ATOM
1745
N
LYS

387
−7.764
112.519
−67.767
1.00
47.79

ATOM
1746
CA
LYS

387
−7.033
111.439
−67.128
1.00
48.42

ATOM
1747
CB
LYS

387
−5.699
111.213
−67.843
1.00
48.01

ATOM
1748
CG
LYS

387
−5.875
110.641
−69.243
1.00
46.81

ATOM
1749
CD
LYS

387
−4.663
110.912
−70.117
1.00
46.36

ATOM
1750
CE
LYS

387
−4.658
110.026
−71.359
1.00
46.26

ATOM
1751
NZ
LYS

387
−5.956
109.963
−72.100
1.00
44.08

ATOM
1752
C
LYS

387
−6.819
111.711
−65.651
1.00
49.30

ATOM
1753
O
LYS

387
−6.690
110.794
−64.850
1.00
48.51

ATOM
1754
N
ASP

388
−6.789
112.976
−65.274
1.00
51.05

ATOM
1755
CA
ASP

388
−6.610
113.289
−63.866
1.00
53.06

ATOM
1756
CB
ASP

388
−5.966
114.661
−63.706
1.00
53.15

ATOM
1757
CG
ASP

388
−5.602
114.960
−62.277
1.00
53.88

ATOM
1758
OD1
ASP

388
−6.273
114.411
−61.382
1.00
54.59

ATOM
1759
OD2
ASP

388
−4.662
115.750
−62.045
1.00
55.38

ATOM
1760
C
ASP

388
−7.988
113.269
−63.194
1.00
54.47

ATOM
1761
O
ASP

388
−8.852
114.085
−63.503
1.00
54.45

ATOM
1762
N
PRO

389
−8.218
112.316
−62.280
1.00
56.07

ATOM
1763
CD
PRO

389
−7.371
111.211
−61.798
1.00
56.72

ATOM
1764
CA
PRO

389
−9.533
112.289
−61.634
1.00
56.52

ATOM
1765
CB
PRO

389
−9.400
111.154
−60.607
1.00
55.95

ATOM
1766
CG
PRO

389
−7.904
111.008
−60.409
1.00
56.22

ATOM
1767
C
PRO

389
−9.907
113.625
−61.010
1.00
56.98

ATOM
1768
O
PRO

389
−11.050
114.073
−61.126
1.00
56.98

ATOM
1769
N
LYS

390
−8.936
114.264
−60.368
1.00
57.25

ATOM
1770
CA
LYS

390
−9.160
115.553
−59.732
1.00
58.61

ATOM
1771
CB
LYS

390
−7.867
116.073
−59.108
1.00
60.51

ATOM
1772
CG
LYS

390
−7.667
115.682
−57.649
1.00
63.58

ATOM
1773
CD
LYS

390
−6.332
116.196
−57.102
1.00
66.33

ATOM
1774
CE
LYS

390
−6.366
116.325
−55.575
1.00
69.42

ATOM
1775
NZ
LYS

390
−6.791
115.062
−54.860
1.00
71.82

ATOM
1776
C
LYS

390
−9.688
116.577
−60.721
1.00
58.91

ATOM
1777
O
LYS

390
−10.438
117.490
−60.350
1.00
59.35

ATOM
1778
N
GLN

391
−9.309
116.428
−61.983
1.00
58.86

ATOM
1779
CA
GLN

391
−9.765
117.365
−62.996
1.00
58.63

ATOM
1780
CB
GLN

391
−8.660
117.655
−64.003
1.00
61.12

ATOM
1781
CG
GLN

391
−7.457
118.404
−63.457
1.00
65.85

ATOM
1782
CD
GLN

391
−6.403
118.596
−64.542
1.00
70.16

ATOM
1783
OE1
GLN

391
−6.587
119.394
−65.480
1.00
71.02

ATOM
1784
NE2
GLN

391
−5.301
117.841
−64.440
1.00
70.27

ATOM
1785
C
GLN

391
−11.003
116.932
−63.760
1.00
57.14

ATOM
1786
O
GLN

391
−11.706
117.778
−64.288
1.00
59.42

ATOM
1787
N
ARG

392
−11.287
115.638
−63.831
1.00
53.89

ATOM
1788
CA
ARG

392
−12.459
115.191
−64.581
1.00
52.12

ATOM
1789
CB
ARG

392
−12.671
113.705
−64.375
1.00
51.68

ATOM
1790
CG
ARG

392
−13.589
113.031
−65.379
1.00
51.30

ATOM
1791
CD
ARG

392
−13.307
111.535
−65.331
1.00
51.76

ATOM
1792
NE
ARG

392
−11.858
111.316
−65.235
1.00
49.83

ATOM
1793
CZ
ARG

392
−11.281
110.411
−64.457
1.00
47.76

ATOM
1794
NH1
ARG

392
−12.027
109.618
−63.703
1.00
46.43

ATOM
1795
NH2
ARG

392
−9.958
110.331
−64.408
1.00
47.65

ATOM
1796
C
ARG

392
−13.761
115.923
−64.241
1.00
51.08

ATOM
1797
O
ARG

392
−13.915
116.485
−63.162
1.00
50.36

ATOM
1798
N
LEU

393
−14.693
115.908
−65.186
1.00
49.96

ATOM
1799
CA
LEU

393
−15.986
116.542
−65.014
1.00
49.55

ATOM
1800
CB
LEU

393
−16.672
116.669
−66.377
1.00
48.34

ATOM
1801
CG
LEU

393
−17.687
117.778
−66.684
1.00
49.19

ATOM
1802
CD1
LEU

393
−18.839
117.184
−67.497
1.00
49.83

ATOM
1803
CD2
LEU

393
−18.214
118.417
−65.412
1.00
50.60

ATOM
1804
C
LEU

393
−16.796
115.617
−64.096
1.00
51.24

ATOM
1805
O
LEU

393
−17.141
114.494
−64.479
1.00
52.00

ATOM
1806
N
GLY

394
−17.113
116.078
−62.891
1.00
51.09

ATOM
1807
CA
GLY

394
−17.863
115.229
−61.975
1.00
50.50

ATOM
1808
C
GLY

394
−16.866
114.686
−60.974
1.00
49.64

ATOM
1809
O
GLY

394
−17.197
113.919
−60.075
1.00
47.57

ATOM
1810
N
GLY

395
−15.624
115.128
−61.155
1.00
49.62

ATOM
1811
CA
GLY

395
−14.533
114.726
−60.297
1.00
50.44

ATOM
1812
C
GLY

395
−14.325
115.762
−59.227
1.00
51.76

ATOM
1813
O
GLY

395
−13.457
115.592
−58.367
1.00
52.68

ATOM
1814
N
GLY

396
−15.118
116.836
−59.281
1.00
52.01

ATOM
1815
CA
GLY

396
−15.034
117.897
−58.286
1.00
53.00

ATOM
1816
C
GLY

396
−15.975
117.650
−57.116
1.00
53.59

ATOM
1817
O
GLY

396
−16.932
116.895
−57.252
1.00
54.24

ATOM
1818
N
PRO

397
−15.751
118.291
−55.959
1.00
54.28

ATOM
1819
CD
PRO

397
−14.835
119.434
−55.823
1.00
54.32

ATOM
1820
CA
PRO

397
−16.577
118.141
−54.747
1.00
54.47

ATOM
1821
CB
PRO

397
−16.054
119.245
−53.836
1.00
54.97

ATOM
1822
CG
PRO

397
−15.549
120.278
−54.813
1.00
55.09

ATOM
1823
C
PRO

397
−18.093
118.225
−54.954
1.00
55.41

ATOM
1824
O
PRO

397
−18.874
117.742
−54.122
1.00
56.14

ATOM
1825
N
SER

398
−18.500
118.830
−56.070
1.00
55.16

ATOM
1826
CA
SER

398
−19.905
118.972
−56.425
1.00
52.76

ATOM
1827
CB
SER

398
−20.077
120.149
−57.376
1.00
54.19

ATOM
1828
OG
SER

398
−21.404
120.170
−57.885
1.00
57.17

ATOM
1829
C
SER

398
−20.448
117.717
−57.109
1.00
51.78

ATOM
1830
O
SER

398
−21.658
117.604
−57.355
1.00
52.25

ATOM
1831
N
ASP

399
−19.543
116.801
−57.453
1.00
49.40

ATOM
1832
CA
ASP

399
−19.888
115.534
−58.102
1.00
47.59

ATOM
1833
CB
ASP

399
−20.400
114.521
−57.050
1.00
48.09

ATOM
1834
CG
ASP

399
−20.297
113.066
−57.521
1.00
48.96

ATOM
1835
OD1
ASP

399
−21.344
112.440
−57.792
1.00
48.69

ATOM
1836
OD2
ASP

399
−19.161
112.543
−57.620
1.00
49.08

ATOM
1837
C
ASP

399
−20.897
115.692
−59.239
1.00
45.55

ATOM
1838
O
ASP

399
−20.773
116.589
−60.047
1.00
45.59

ATOM
1839
N
ALA

400
−21.896
114.823
−59.288
1.00
45.15

ATOM
1840
CA
ALA

400
−22.896
114.842
−60.346
1.00
46.94

ATOM
1841
CB
ALA

400
−24.009
113.870
−60.012
1.00
43.68

ATOM
1842
C
ALA

400
−23.497
116.199
−60.740
1.00
49.95

ATOM
1843
O
ALA

400
−24.223
116.293
−61.745
1.00
51.57

ATOM
1844
N
LYS

401
−23.228
117.258
−59.981
1.00
52.07

ATOM
1845
CA
LYS

401
−23.809
118.528
−60.378
1.00
53.83

ATOM
1846
CB
LYS

401
−23.809
119.518
−59.225
1.00
55.19

ATOM
1847
CG
LYS

401
−25.013
119.298
−58.315
1.00
59.36

ATOM
1848
CD
LYS

401
−24.866
120.046
−56.995
1.00
61.63

ATOM
1849
CE
LYS

401
−25.722
119.436
−55.884
1.00
61.07

ATOM
1850
NZ
LYS

401
−25.331
120.004
−54.554
1.00
60.54

ATOM
1851
C
LYS

401
−23.073
119.067
−61.577
1.00
53.82

ATOM
1852
O
LYS

401
−23.686
119.535
−62.528
1.00
54.37

ATOM
1853
N
GLU

402
−21.757
118.971
−61.553
1.00
53.25

ATOM
1854
CA
GLU

402
−20.984
119.444
−62.676
1.00
53.58

ATOM
1855
CB
GLU

402
−19.504
119.147
−62.445
1.00
54.86

ATOM
1856
CG
GLU

402
−18.880
120.014
−61.379
1.00
57.21

ATOM
1857
CD
GLU

402
−17.666
119.380
−60.726
1.00
60.57

ATOM
1858
OE1
GLU

402
−16.808
118.836
−61.461
1.00
61.15

ATOM
1859
OE2
GLU

402
−17.568
119.436
−59.473
1.00
61.74

ATOM
1860
C
GLU

402
−21.493
118.761
−63.950
1.00
53.81

ATOM
1861
O
GLU

402
−21.674
119.407
−64.983
1.00
54.59

ATOM
1862
N
VAL

403
−21.765
117.466
−63.881
1.00
53.03

ATOM
1863
CA
VAL

403
−22.233
116.773
−65.073
1.00
52.97

ATOM
1864
CB
VAL

403
−22.083
115.243
−64.907
1.00
50.93

ATOM
1865
CG1
VAL

403
−22.741
114.491
−66.070
1.00
47.49

ATOM
1866
CG2
VAL

403
−20.601
114.908
−64.814
1.00
49.93

ATOM
1867
C
VAL

403
−23.670
117.137
−65.458
1.00
54.53

ATOM
1868
O
VAL

403
−24.008
117.206
−66.648
1.00
55.78

ATOM
1869
N
MET

404
−24.513
117.382
−64.462
1.00
55.12

ATOM
1870
CA
MET

404
−25.903
117.741
−64.728
1.00
56.16

ATOM
1871
CB
MET

404
−26.717
117.629
−63.446
1.00
56.98

ATOM
1872
CG
MET

404
−26.993
116.206
−63.038
1.00
57.98

ATOM
1873
SD
MET

404
−27.908
116.121
−61.526
1.00
59.07

ATOM
1874
CE
MET

404
−26.647
116.771
−60.384
1.00
57.66

ATOM
1875
C
MET

404
−26.006
119.154
−65.274
1.00
56.24

ATOM
1876
O
MET

404
−26.874
119.461
−66.088
1.00
54.90

ATOM
1877
N
GLU

405
−25.097
120.000
−64.807
1.00
56.49

ATOM
1878
CA
GLU

405
−25.030
121.392
−65.193
1.00
57.03

ATOM
1879
CB
GLU

405
−24.706
122.249
−63.982
1.00
57.28

ATOM
1880
CG
GLU

405
−25.876
122.502
−63.088
1.00
60.66

ATOM
1881
CD
GLU

405
−25.431
122.776
−61.688
1.00
62.93

ATOM
1882
OE1
GLU

405
−24.283
123.254
−61.539
1.00
61.54

ATOM
1883
OE2
GLU

405
−26.219
122.513
−60.747
1.00
65.44

ATOM
1884
C
GLU

405
−23.967
121.637
−66.236
1.00
58.00

ATOM
1885
O
GLU

405
−23.217
122.623
−66.141
1.00
59.39

ATOM
1886
N
HIS

406
−23.858
120.746
−67.211
1.00
56.91

ATOM
1887
CA
HIS

406
−22.873
120.962
−68.248
1.00
55.53

ATOM
1888
CB
HIS

406
−22.061
119.699
−68.550
1.00
53.24

ATOM
1889
CG
HIS

406
−21.139
119.838
−69.729
1.00
50.16

ATOM
1890
CD2
HIS

406
−19.831
120.192
−69.804
1.00
48.59

ATOM
1891
ND1
HIS

406
−21.557
119.642
−71.034
1.00
49.62

ATOM
1892
CE1
HIS

406
−20.546
119.870
−71.858
1.00
48.28

ATOM
1893
NE2
HIS

406
−19.487
120.206
−71.139
1.00
48.59

ATOM
1894
C
HIS

406
−23.613
121.396
−69.479
1.00
55.78

ATOM
1895
O
HIS

406
−24.787
121.071
−69.668
1.00
53.92

ATOM
1896
N
ARG

407
−22.904
122.168
−70.293
1.00
57.33

ATOM
1897
CA
ARG

407
−23.401
122.697
−71.551
1.00
57.68

ATOM
1898
CB
ARG

407
−22.182
123.067
−72.402
1.00
61.12

ATOM
1899
CG
ARG

407
−22.411
123.709
−73.766
1.00
66.54

ATOM
1900
CD
ARG

407
−21.026
123.834
−74.450
1.00
72.28

ATOM
1901
NE
ARG

407
−20.978
124.757
−75.594
1.00
77.56

ATOM
1902
CZ
ARG

407
−19.851
125.217
−76.156
1.00
79.95

ATOM
1903
NH1
ARG

407
−18.653
124.849
−75.690
1.00
79.70

ATOM
1904
NH2
ARG

407
−19.920
126.058
−77.189
1.00
80.94

ATOM
1905
C
ARG

407
−24.270
121.635
−72.233
1.00
56.17

ATOM
1906
O
ARG

407
−25.441
121.882
−72.544
1.00
56.34

ATOM
1907
N
PHE

408
−23.701
120.442
−72.418
1.00
53.99

ATOM
1908
CA
PHE

408
−24.394
119.336
−73.087
1.00
51.30

ATOM
1909
CB
PHE

408
−23.521
118.053
−73.063
1.00
47.78

ATOM
1910
CG
PHE

408
−24.156
116.874
−73.782
1.00
43.10

ATOM
1911
CD1
PHE

408
−24.176
116.820
−75.176
1.00
40.46

ATOM
1912
CD2
PHE

408
−24.837
115.879
−73.061
1.00
39.68

ATOM
1913
CE1
PHE

408
−24.871
115.798
−75.852
1.00
40.23

ATOM
1914
CE2
PHE

408
−25.537
114.856
−73.725
1.00
39.16

ATOM
1915
CZ
PHE

408
−25.555
114.815
−75.129
1.00
39.59

ATOM
1916
C
PHE

408
−25.782
119.024
−72.516
1.00
51.33

ATOM
1917
O
PHE

408
−26.700
118.632
−73.252
1.00
50.34

ATOM
1918
N
PHE

409
−25.924
119.222
−71.209
1.00
51.69

ATOM
1919
CA
PHE

409
−27.159
118.928
−70.498
1.00
53.34

ATOM
1920
CB
PHE

409
−26.835
118.087
−69.247
1.00
52.49

ATOM
1921
CG
PHE

409
−26.514
116.636
−69.536
1.00
49.84

ATOM
1922
CD1
PHE

409
−27.509
115.766
−70.000
1.00
47.15

ATOM
1923
CD2
PHE

409
−25.215
116.138
−69.336
1.00
46.48

ATOM
1924
CE1
PHE

409
−27.218
114.416
−70.262
1.00
44.93

ATOM
1925
CE2
PHE

409
−24.920
114.808
−69.593
1.00
43.99

ATOM
1926
CZ
PHE

409
−25.927
113.944
−70.058
1.00
43.30

ATOM
1927
C
PHE

409
−28.007
120.138
−70.076
1.00
55.22

ATOM
1928
O
PHE

409
−28.365
120.275
−68.896
1.00
55.90

ATOM
1929
N
LEU

410
−28.330
121.018
−71.018
1.00
56.10

ATOM
1930
CA
LEU

410
−29.185
122.158
−70.688
1.00
55.66

ATOM
1931
CB
LEU

410
−28.881
123.355
−71.598
1.00
56.88

ATOM
1932
CG
LEU

410
−30.061
124.263
−71.967
1.00
57.63

ATOM
1933
CD1
LEU

410
−29.522
125.592
−72.450
1.00
58.73

ATOM
1934
CD2
LEU

410
−30.955
123.605
−73.045
1.00
56.93

ATOM
1935
C
LEU

410
−30.664
121.744
−70.814
1.00
54.17

ATOM
1936
O
LEU

410
−31.462
122.007
−69.916
1.00
54.11

ATOM
1937
N
SER

411
−31.016
121.081
−71.910
1.00
52.16

ATOM
1938
CA
SER

411
−32.389
120.640
−72.150
1.00
52.53

ATOM
1939
CB
SER

411
−32.495
120.044
−73.548
1.00
53.52

ATOM
1940
OG
SER

411
−31.890
118.751
−73.607
1.00
50.84

ATOM
1941
C
SER

411
−32.870
119.579
−71.170
1.00
53.03

ATOM
1942
O
SER

411
−33.795
118.811
−71.468
1.00
52.87

ATOM
1943
N
ILE

412
−32.297
119.550
−69.981
1.00
53.34

ATOM
1944
CA
ILE

412
−32.648
118.480
−69.071
1.00
52.85

ATOM
1945
CB
ILE

412
−31.334
117.739
−68.701
1.00
52.94

ATOM
1946
CG2
ILE

412
−31.575
116.638
−67.692
1.00
52.69

ATOM
1947
CG1
ILE

412
−30.728
117.154
−69.988
1.00
52.08

ATOM
1948
CD1
ILE

412
−31.728
116.302
−70.822
1.00
49.42

ATOM
1949
C
ILE

412
−33.452
118.801
−67.837
1.00
52.20

ATOM
1950
O
ILE

412
−33.138
119.728
−67.106
1.00
53.49

ATOM
1951
N
ASN

413
−34.505
118.028
−67.608
1.00
52.27

ATOM
1952
CA
ASN

413
−35.329
118.214
−66.420
1.00
52.73

ATOM
1953
CB
ASN

413
−36.825
118.077
−66.741
1.00
56.07

ATOM
1954
CG
ASN

413
−37.698
118.919
−65.801
1.00
59.17

ATOM
1955
OD1
ASN

413
−38.601
118.412
−65.118
1.00
58.30

ATOM
1956
OD2
ASN

413
−37.416
120.225
−65.764
1.00
60.58

ATOM
1957
C
ASN

413
−34.926
117.114
−65.461
1.00
51.48

ATOM
1958
O
ASN

413
−35.598
116.080
−65.369
1.00
49.23

ATOM
1959
N
TRP

414
−33.827
117.329
−64.749
1.00
51.21

ATOM
1960
CA
TRP

414
−33.338
116.309
−63.836
1.00
52.23

ATOM
1961
CB
TRP

414
−32.142
116.843
−63.040
1.00
52.76

ATOM
1962
CG
TRP

414
−30.919
117.040
−63.916
1.00
56.33

ATOM
1963
CD2
TRP

414
−30.173
116.019
−64.622
1.00
57.44

ATOM
1964
CE2
TRP

414
−29.133
116.675
−65.333
1.00
58.16

ATOM
1965
CE3
TRP

414
−30.274
114.622
−64.710
1.00
57.73

ATOM
1966
CD1
TRP

414
−30.321
118.226
−64.226
1.00
57.64

ATOM
1967
NE1
TRP

414
−29.249
118.015
−65.080
1.00
58.59

ATOM
1968
CZ2
TRP

414
−28.208
115.981
−66.134
1.00
57.67

ATOM
1969
CZ3
TRP

414
−29.349
113.930
−65.510
1.00
57.83

ATOM
1970
CH2
TRP

414
−28.326
114.617
−66.204
1.00
57.14

ATOM
1971
C
TRP

414
−34.403
115.709
−62.917
1.00
52.00

ATOM
1972
O
TRP

414
−34.186
114.669
−62.318
1.00
53.55

ATOM
1973
N
GLN

415
−35.557
116.350
−62.806
1.00
53.02

ATOM
1974
CA
GLN

415
−36.628
115.808
−61.979
1.00
52.35

ATOM
1975
CB
GLN

415
−37.586
116.896
−61.510
1.00
51.85

ATOM
1976
CG
GLN

415
−37.357
117.413
−60.128
1.00
50.98

ATOM
1977
CD
GLN

415
−38.597
118.074
−59.581
1.00
49.35

ATOM
1978
OE1
GLN

415
−39.702
117.610
−59.829
1.00
49.48

ATOM
1979
NE2
GLN

415
−38.422
119.148
−58.823
1.00
48.14

ATOM
1980
C
GLN

415
−37.412
114.853
−62.845
1.00
52.80

ATOM
1981
O
GLN

415
−37.889
113.832
−62.379
1.00
53.07

ATOM
1982
N
ASP

416
−37.559
115.211
−64.112
1.00
53.66

ATOM
1983
CA
ASP

416
−38.293
114.387
−65.055
1.00
56.63

ATOM
1984
CB
ASP

416
−38.441
115.099
−66.395
1.00
61.15

ATOM
1985
CG
ASP

416
−39.645
116.005
−66.436
1.00
64.26

ATOM
1986
OD1
ASP

416
−40.757
115.527
−66.084
1.00
67.64

ATOM
1987
OD2
ASP

416
−39.472
117.180
−66.828
1.00
64.63

ATOM
1988
C
ASP

416
−37.597
113.072
−65.274
1.00
55.71

ATOM
1989
O
ASP

416
−38.245
112.058
−65.503
1.00
54.51

ATOM
1990
N
VAL

417
−36.268
113.114
−65.228
1.00
55.85

ATOM
1991
CA
VAL

417
−35.439
111.925
−65.391
1.00
55.28

ATOM
1992
CB
VAL

417
−33.936
112.238
−65.172
1.00
55.40

ATOM
1993
CG1
VAL

417
−33.145
110.943
−65.138
1.00
55.85

ATOM
1994
CG2
VAL

417
−33.409
113.162
−66.273
1.00
53.47

ATOM
1995
C
VAL

417
−35.843
110.879
−64.359
1.00
55.08

ATOM
1996
O
VAL

417
−36.481
109.884
−64.691
1.00
54.28

ATOM
1997
N
VAL

418
−35.499
111.124
−63.099
1.00
54.29

ATOM
1998
CA
VAL

418
−35.795
110.153
−62.056
1.00
55.72

ATOM
1999
CB
VAL

418
−35.348
110.662
−60.674
1.00
55.31

ATOM
2000
CG1
VAL

418
−34.048
111.438
−60.813
1.00
56.68

ATOM
2001
CG2
VAL

418
−36.416
111.528
−60.064
1.00
56.29

ATOM
2002
C
VAL

418
−37.257
109.767
−61.997
1.00
56.54

ATOM
2003
O
VAL

418
−37.622
108.728
−61.420
1.00
55.83

ATOM
2004
N
GLN

419
−38.094
110.600
−62.603
1.00
58.05

ATOM
2005
CA
GLN

419
−39.525
110.354
−62.603
1.00
60.00

ATOM
2006
CB
GLN

419
−40.273
111.691
−62.624
1.00
60.59

ATOM
2007
CG
GLN

419
−40.145
112.531
−61.347
1.00
60.61

ATOM
2008
CD
GLN

419
−41.070
112.054
−60.251
1.00
61.81

ATOM
2009
OE1
GLN

419
−42.288
112.234
−60.324
1.00
63.44

ATOM
2010
NE2
GLN

419
−40.503
111.430
−59.233
1.00
61.86

ATOM
2011
C
GLN

419
−39.967
109.489
−63.781
1.00
61.10

ATOM
2012
O
GLN

419
−41.143
109.155
−63.893
1.00
61.80

ATOM
2013
N
LYS

420
−39.015
109.101
−64.633
1.00
62.64

ATOM
2014
CA
LYS

420
−39.305
108.306
−65.836
1.00
63.79

ATOM
2015
CB
LYS

420
−39.859
106.919
−65.475
1.00
63.30

ATOM
2016
CG
LYS

420
−38.812
105.910
−65.107
1.00
61.93

ATOM
2017
CD
LYS

420
−39.356
104.487
−65.106
1.00
61.18

ATOM
2018
CE
LYS

420
−38.194
103.506
−64.904
1.00
63.83

ATOM
2019
NZ
LYS

420
−38.544
102.054
−64.991
1.00
64.72

ATOM
2020
C
LYS

420
−40.328
109.071
−66.686
1.00
64.94

ATOM
2021
O
LYS

420
−41.038
108.499
−67.520
1.00
65.21

ATOM
2022
N
LYS

421
−40.389
110.375
−66.454
1.00
65.55

ATOM
2023
CA
LYS

421
−41.305
111.243
−67.157
1.00
66.82

ATOM
2024
CB
LYS

421
−41.375
112.602
−66.448
1.00
69.10

ATOM
2025
CG
LYS

421
−42.722
112.866
−65.761
1.00
71.17

ATOM
2026
CD
LYS

421
−43.160
111.712
−64.841
1.00
73.41

ATOM
2027
CE
LYS

421
−44.649
111.810
−64.441
1.00
74.24

ATOM
2028
NZ
LYS

421
−45.029
113.065
−63.704
1.00
74.43

ATOM
2029
C
LYS

421
−40.880
111.405
−68.606
1.00
67.07

ATOM
2030
O
LYS

421
−41.719
111.535
−69.493
1.00
67.37

ATOM
2031
N
LEU

422
−39.576
111.389
−68.850
1.00
66.80

ATOM
2032
CA
LEU

422
−39.073
111.511
−70.215
1.00
66.69

ATOM
2033
CB
LEU

422
−37.543
111.507
−70.230
1.00
66.44

ATOM
2034
CG
LEU

422
−36.956
112.734
−69.534
1.00
67.01

ATOM
2035
CD1
LEU

422
−35.499
112.889
−69.926
1.00
66.42

ATOM
2036
CD2
LEU

422
−37.751
113.982
−69.938
1.00
66.61

ATOM
2037
C
LEU

422
−39.593
110.390
−71.107
1.00
66.24

ATOM
2038
O
LEU

422
−40.064
109.359
−70.635
1.00
65.39

ATOM
2039
N
LEU

423
−39.515
110.612
−72.409
1.00
66.58

ATOM
2040
CA
LEU

423
−39.976
109.628
−73.364
1.00
66.62

ATOM
2041
CB
LEU

423
−40.843
110.306
−74.438
1.00
66.42

ATOM
2042
CG
LEU

423
−41.560
109.422
−75.476
1.00
68.09

ATOM
2043
CD1
LEU

423
−42.789
108.747
−74.838
1.00
67.26

ATOM
2044
CD2
LEU

423
−41.979
110.258
−76.683
1.00
66.82

ATOM
2045
C
LEU

423
−38.755
108.959
−74.002
1.00
66.65

ATOM
2046
O
LEU

423
−37.840
109.629
−74.500
1.00
66.10

ATOM
2047
N
PRO

424
−38.708
107.621
−73.959
1.00
66.46

ATOM
2048
CD
PRO

424
−39.698
106.650
−73.455
1.00
66.23

ATOM
2049
CA
PRO

424
−37.563
106.943
−74.564
1.00
66.89

ATOM
2050
CB
PRO

424
−37.826
105.477
−74.232
1.00
66.75

ATOM
2051
CG
PRO

424
−39.334
105.406
−74.205
1.00
66.65

ATOM
2052
C
PRO

424
−37.644
107.231
−76.062
1.00
67.60

ATOM
2053
O
PRO

424
−38.714
107.079
−76.671
1.00
67.91

ATOM
2054
N
PRO

425
−36.531
107.680
−76.670
1.00
67.38

ATOM
2055
CD
PRO

425
−35.258
108.039
−76.023
1.00
67.26

ATOM
2056
CA
PRO

425
−36.498
107.990
−78.106
1.00
66.27

ATOM
2057
CB
PRO

425
−35.223
108.806
−78.254
1.00
66.59

ATOM
2058
CG
PRO

425
−34.336
108.213
−77.214
1.00
67.16

ATOM
2059
C
PRO

425
−36.503
106.745
−78.980
1.00
66.14

ATOM
2060
O
PRO

425
−36.358
106.826
−80.202
1.00
65.38

ATOM
2061
N
PHE

426
−36.671
105.595
−78.339
1.00
65.30

ATOM
2062
CA
PHE

426
−36.726
104.317
−79.027
1.00
65.63

ATOM
2063
CB
PHE

426
−35.322
103.782
−79.325
1.00
65.22

ATOM
2064
CG
PHE

426
−35.297
102.322
−79.685
1.00
63.93

ATOM
2065
CD1
PHE

426
−35.632
101.901
−80.963
1.00
63.23

ATOM
2066
CD2
PHE

426
−35.017
101.358
−78.716
1.00
65.40

ATOM
2067
CE1
PHE

426
−35.699
100.550
−81.274
1.00
62.86

ATOM
2068
CE2
PHE

426
−35.082
99.996
−79.017
1.00
64.40

ATOM
2069
CZ
PHE

426
−35.425
99.597
−80.299
1.00
63.95

ATOM
2070
C
PHE

426
−37.422
103.354
−78.101
1.00
66.77

ATOM
2071
O
PHE

426
−36.981
103.141
−76.974
1.00
67.75

ATOM
2072
N
LYS

427
−38.517
102.773
−78.553
1.00
68.26

ATOM
2073
CA
LYS

427
−39.184
101.826
−77.698
1.00
71.07

ATOM
2074
CB
LYS

427
−40.684
102.075
−77.609
1.00
73.34

ATOM
2075
CG
LYS

427
−41.421
100.969
−76.845
1.00
76.46

ATOM
2076
CD
LYS

427
−42.730
101.483
−76.267
1.00
79.30

ATOM
2077
CE
LYS

427
−43.315
100.524
−75.244
1.00
80.07

ATOM
2078
NZ
LYS

427
−44.509
101.121
−74.569
1.00
81.44

ATOM
2079
C
LYS

427
−38.963
100.438
−78.214
1.00
72.16

ATOM
2080
O
LYS

427
−39.269
100.141
−79.362
1.00
72.45

ATOM
2081
N
PRO

428
−38.412
99.566
−77.364
1.00
73.23

ATOM
2082
CD
PRO

428
−37.908
99.901
−76.024
1.00
72.33

ATOM
2083
CA
PRO

428
−38.129
98.168
−77.687
1.00
74.21

ATOM
2084
CB
PRO

428
−37.604
97.632
−76.370
1.00
73.62

ATOM
2085
CG
PRO

428
−36.904
98.823
−75.801
1.00
72.83

ATOM
2086
C
PRO

428
−39.448
97.530
−78.096
1.00
75.76

ATOM
2087
O
PRO

428
−40.505
98.013
−77.695
1.00
76.36

ATOM
2088
N
GLN

429
−39.400
96.457
−78.879
1.00
77.72

ATOM
2089
CA
GLN

429
−40.633
95.824
−79.338
1.00
80.67

ATOM
2090
CB
GLN

429
−40.477
95.347
−80.795
1.00
81.80

ATOM
2091
CG
GLN

429
−40.279
96.476
−81.816
1.00
83.38

ATOM
2092
CD
GLN

429
−38.905
96.442
−82.489
1.00
85.42

ATOM
2093
OE1
GLN

429
−37.916
96.005
−81.891
1.00
87.30

ATOM
2094
NE2
GLN

429
−38.837
96.926
−83.731
1.00
84.87

ATOM
2095
C
GLN

429
−41.118
94.669
−78.476
1.00
81.74

ATOM
2096
O
GLN

429
−40.983
93.511
−78.865
1.00
82.91

ATOM
2097
N
VAL

430
−41.702
94.976
−77.320
1.00
82.78

ATOM
2098
CA
VAL

430
−42.204
93.932
−76.420
1.00
84.69

ATOM
2099
CB
VAL

430
−41.168
93.618
−75.284
1.00
84.62

ATOM
2100
CG1
VAL

430
−39.900
93.018
−75.877
1.00
84.85

ATOM
2101
CG2
VAL

430
−40.822
94.880
−74.515
1.00
84.52

ATOM
2102
C
VAL

430
−43.566
94.258
−75.773
1.00
85.71

ATOM
2103
O
VAL

430
−43.749
95.333
−75.188
1.00
86.15

ATOM
2104
N
THR

431
−44.512
93.321
−75.884
1.00
86.28

ATOM
2105
CA
THR

431
−45.862
93.477
−75.314
1.00
86.70

ATOM
2106
CB
THR

431
−46.700
92.163
−75.454
1.00
86.82

ATOM
2107
OG1
THR

431
−46.569
91.632
−76.779
1.00
86.80

ATOM
2108
CG2
THR

431
−48.171
92.432
−75.169
1.00
85.55

ATOM
2109
C
THR

431
−45.738
93.775
−73.819
1.00
86.81

ATOM
2110
O
THR

431
−45.720
94.927
−73.381
1.00
85.92

ATOM
2111
N
SER

432
−45.664
92.694
−73.052
1.00
88.08

ATOM
2112
CA
SER

432
−45.515
92.743
−71.606
1.00
89.37

ATOM
2113
CB
SER

432
−46.410
91.683
−70.940
1.00
89.59

ATOM
2114
OG
SER

432
−46.114
90.373
−71.413
1.00
88.93

ATOM
2115
C
SER

432
−44.051
92.433
−71.300
1.00
90.26

ATOM
2116
O
SER

432
−43.324
91.917
−72.161
1.00
90.49

ATOM
2117
N
GLU

433
−43.623
92.752
−70.082
1.00
90.53

ATOM
2118
CA
GLU

433
−42.253
92.483
−69.661
1.00
90.91

ATOM
2119
CB
GLU

433
−42.077
92.887
−68.197
1.00
90.87

ATOM
2120
CG
GLU

433
−43.355
92.807
−67.388
1.00
91.01

ATOM
2121
CD
GLU

433
−43.538
94.017
−66.483
1.00
91.12

ATOM
2122
OE1
GLU

433
−42.690
94.220
−65.584
1.00
90.23

ATOM
2123
OE2
GLU

433
−44.526
94.767
−66.675
1.00
90.80

ATOM
2124
C
GLU

433
−41.963
90.995
−69.859
1.00
90.98

ATOM
2125
O
GLU

433
−40.809
90.580
−70.026
1.00
90.47

ATOM
2126
N
VAL

434
−43.035
90.206
−69.859
1.00
90.73

ATOM
2127
CA
VAL

434
−42.950
88.769
−70.049
1.00
89.79

ATOM
2128
CB
VAL

434
−44.265
88.093
−69.629
1.00
90.32

ATOM
2129
CG1
VAL

434
−44.234
86.614
−69.958
1.00
89.56

ATOM
2130
CG2
VAL

434
−44.472
88.288
−68.141
1.00
91.06

ATOM
2131
C
VAL

434
−42.625
88.419
−71.496
1.00
89.19

ATOM
2132
O
VAL

434
−42.378
87.258
−71.812
1.00
89.05

ATOM
2133
N
ASP

435
−42.618
89.411
−72.381
0.00
89.50

ATOM
2134
CA
ASP

435
−42.287
89.119
−73.767
1.00
89.74

ATOM
2135
CB
ASP

435
−42.537
90.319
−74.683
1.00
89.77

ATOM
2136
CG
ASP

435
−42.274
89.985
−76.145
1.00
90.31

ATOM
2137
OD1
ASP

435
−42.890
89.020
−76.641
1.00
90.76

ATOM
2138
OD2
ASP

435
−41.453
90.667
−76.796
1.00
89.77

ATOM
2139
C
ASP

435
−40.813
88.728
−73.802
1.00
89.83

ATOM
2140
O
ASP

435
−39.933
89.522
−73.471
1.00
89.50

ATOM
2141
N
THR

436
−40.551
87.495
−74.213
1.00
90.03

ATOM
2142
CA
THR

436
−39.193
86.974
−74.245
1.00
90.44

ATOM
2143
CB
THR

436
−39.164
85.530
−73.725
1.00
89.61

ATOM
2144
OG1
THR

436
−39.768
84.674
−74.702
1.00
88.62

ATOM
2145
CG2
THR

436
−39.925
85.417
−72.404
1.00
88.03

ATOM
2146
C
THR

436
−38.552
86.964
−75.624
1.00
91.23

ATOM
2147
O
THR

436
−37.872
86.002
−75.981
1.00
91.04

ATOM
2148
N
ARG

437
−38.742
88.019
−76.403
1.00
92.58

ATOM
2149
CA
ARG

437
−38.148
88.006
−77.727
1.00
94.08

ATOM
2150
CB
ARG

437
−39.012
88.785
−78.732
1.00
95.34

ATOM
2151
CG
ARG

437
−38.907
90.293
−78.701
1.00
97.36

ATOM
2152
CD
ARG

437
−39.504
90.871
−79.993
1.00
99.69

ATOM
2153
NE
ARG

437
−40.923
90.533
−80.159
1.00
101.02

ATOM
2154
CZ
ARG

437
−41.573
90.556
−81.321
1.00
100.67

ATOM
2155
NH1
ARG

437
−40.941
90.899
−82.437
1.00
100.49

ATOM
2156
NH2
ARG

437
−42.858
90.229
−81.369
1.00
100.57

ATOM
2157
C
ARG

437
−36.708
88.499
−77.742
1.00
93.94

ATOM
2158
O
ARG

437
−35.910
88.050
−78.563
1.00
94.51

ATOM
2159
N
TYR

438
−36.360
89.405
−76.835
1.00
93.65

ATOM
2160
CA
TYR

438
−34.985
89.893
−76.788
1.00
93.41

ATOM
2161
CB
TYR

438
−34.900
91.280
−76.147
1.00
92.61

ATOM
2162
CG
TYR

438
−35.288
92.417
−77.061
1.00
92.18

ATOM
2163
CD1
TYR

438
−36.580
92.944
−77.046
1.00
91.98

ATOM
2164
CE1
TYR

438
−36.945
93.978
−77.903
1.00
91.83

ATOM
2165
CD2
TYR

438
−34.365
92.957
−77.960
1.00
91.59

ATOM
2166
CE2
TYR

438
−34.717
93.992
−78.821
1.00
90.95

ATOM
2167
CZ
TYR

438
−36.009
94.496
−78.790
1.00
91.35

ATOM
2168
OH
TYR

438
−36.370
95.505
−79.657
1.00
91.56

ATOM
2169
C
TYR

438
−34.116
88.937
−75.988
1.00
93.68

ATOM
2170
O
TYR

438
−33.101
89.355
−75.421
1.00
94.37

ATOM
2171
N
PHE

439
−34.516
87.664
−75.935
1.00
93.70

ATOM
2172
CA
PHE

439
−33.765
86.654
−75.190
1.00
93.63

ATOM
2173
CB
PHE

439
−34.698
85.891
−74.232
1.00
92.31

ATOM
2174
CG
PHE

439
−35.246
86.736
−73.096
1.00
91.84

ATOM
2175
CD1
PHE

439
−36.241
86.239
−72.255
1.00
91.77

ATOM
2176
CD2
PHE

439
−34.788
88.039
−72.882
1.00
91.11

ATOM
2177
CE1
PHE

439
−36.777
87.028
−71.213
1.00
91.16

ATOM
2178
CE2
PHE

439
−35.314
88.833
−71.848
1.00
90.75

ATOM
2179
CZ
PHE

439
−36.313
88.325
−71.015
1.00
90.31

ATOM
2180
C
PHE

439
−33.006
85.671
−76.082
1.00
94.41

ATOM
2181
O
PHE

439
−32.915
84.488
−75.778
1.00
95.17

ATOM
2182
N
ASP

440
−32.466
86.178
−77.185
1.00
95.67

ATOM
2183
CA
ASP

440
−31.671
85.394
−78.131
1.00
97.43

ATOM
2184
CB
ASP

440
−32.530
84.911
−79.297
1.00
98.16

ATOM
2185
CG
ASP

440
−33.751
84.140
−78.841
1.00
98.95

ATOM
2186
OD1
ASP

440
−34.674
84.766
−78.269
1.00
98.96

ATOM
2187
OD2
ASP

440
−33.785
82.906
−79.051
1.00
99.24

ATOM
2188
C
ASP

440
−30.626
86.387
−78.635
1.00
98.95

ATOM
2189
O
ASP

440
−30.140
87.207
−77.853
1.00
99.32

ATOM
2190
N
ASP

441
−30.280
86.337
−79.922
1.00
99.92

ATOM
2191
CA
ASP

441
−29.299
87.289
−80.465
1.00
100.41

ATOM
2192
CB
ASP

441
−28.272
86.586
−81.370
1.00
100.96

ATOM
2193
CG
ASP

441
−27.259
85.755
−80.590
1.00
101.62

ATOM
2194
OD1
ASP

441
−27.650
84.708
−80.020
1.00
102.78

ATOM
2195
OD2
ASP

441
−26.070
86.155
−80.553
1.00
101.62

ATOM
2196
C
ASP

441
−29.979
88.403
−81.267
1.00
99.97

ATOM
2197
O
ASP

441
−29.457
88.722
−82.363
1.00
100.19

ATOM
2198
OXT
ASP

441
−31.006
88.949
−80.788
1.00
99.08

ATOM
2199
OH2
TIP
S
1
−28.279
117.130
−75.119
1.00
34.27
S

ATOM
2200
OH2
TIP
S
2
−20.338
90.232
−73.418
1.00
37.56
S

ATOM
2201
OH2
TIP
S
3
−40.040
69.855
−59.741
1.00
51.84
S

ATOM
2202
OH2
TIP
S
4
−25.225
75.462
−53.383
1.00
92.94
S

ATOM
2203
OH2
TIP
S
5
−10.577
83.823
−50.768
1.00
52.45
S

ATOM
2204
OH2
TIP
S
6
−20.050
83.628
−46.136
1.00
40.14
S

ATOM
2205
OH2
TIP
S
8
−25.025
95.943
−72.991
1.00
54.25
S

ATOM
2206
OH2
TIP
S
9
−16.147
93.778
−51.712
1.00
57.82
S

ATOM
2207
OH2
TIP
S
10
−14.459
99.445
−70.266
1.00
55.95
S

ATOM
2208
OH2
TIP
S
11
−29.240
120.386
−73.296
1.00
60.45
S

ATOM
2209
OH2
TIP
S
12
−17.965
101.307
−71.613
1.00
46.85
S

ATOM
2210
OH2
TIP
S
13
−15.267
108.531
−72.968
1.00
91.70
S

ATOM
2211
OH2
TIP
S
14
−35.604
84.032
−67.027
1.00
80.01
S

ATOM
2212
OH2
TIP
S
16
−24.325
112.109
−55.117
1.00
48.28
S

ATOM
2213
OH2
TIP
S
17
−19.694
85.685
−75.442
1.00
49.20
S

ATOM
2214
OH2
TIP
S
18
−14.471
111.840
−92.040
1.00
66.51
S

ATOM
2215
OH2
TIP
S
19
−29.978
105.957
−69.758
1.00
65.82
S

ATOM
2216
OH2
TIP
S
21
−34.418
119.302
−75.361
1.00
77.64
S

ATOM
2217
OH2
TIP
S
22
−38.864
101.588
−60.192
1.00
58.22
S

ATOM
2218
OH2
TIP
S
23
−24.772
100.358
−49.592
1.00
64.47
S

ATOM
2219
OH2
TIP
S
25
−17.774
102.854
−63.371
1.00
40.15
S

ATOM
2220
OH2
TIP
S
26
−25.095
110.786
−74.186
1.00
77.99
S

ATOM
2221
OH2
TIP
S
27
−6.339
113.185
−80.728
1.00
75.97
S

ATOM
2222
OH2
TIP
S
28
2.253
106.824
−60.404
1.00
62.87
S

ATOM
2223
OH2
TIP
S
29
−21.066
90.649
−77.276
1.00
54.35
S

ATOM
2224
OH2
TIP
S
30
−25.931
91.782
−59.896
1.00
79.95
S

ATOM
2225
OH2
TIP
S
31
−38.876
102.793
−82.070
1.00
35.31
S

ATOM
2226
OH2
TIP
S
32
−28.265
121.697
−61.510
1.00
73.14
S

ATOM
2227
OH2
TIP
S
33
−17.629
102.276
−52.451
1.00
50.42
S

ATOM
2228
OH2
TIP
S
36
−19.186
69.946
−50.434
1.00
55.26
S

ATOM
2229
OH2
TIP
S
37
−34.577
104.057
−75.386
1.00
59.33
S

ATOM
2230
OH2
TIP
S
39
−43.307
97.845
−75.637
1.00
84.67
S

ATOM
2231
OH2
TIP
S
40
−38.231
91.930
−61.441
1.00
67.57
S

ATOM
2232
OH2
TIP
S
42
−13.260
92.477
−62.358
1.00
47.45
S

ATOM
2233
OH2
TIP
S
43
−30.252
120.215
−67.130
1.00
63.27
S

ATOM
2234
OH2
TIP
S
45
−12.970
112.336
−88.089
1.00
61.99
S

ATOM
2235
OH2
TIP
S
46
−3.233
95.832
−73.294
1.00
70.30
S

ATOM
2236
OH2
TIP
S
47
−33.354
91.917
−73.019
1.00
50.21
S

ATOM
2237
OH2
TIP
S
48
−47.678
112.329
−66.053
1.00
58.36
S

ATOM
2238
OH2
TIP
S
49
−18.930
76.549
−47.815
1.00
36.97
S

ATOM
2239
OH2
TIP
S
50
−17.946
91.866
−77.524
1.00
67.78
S

ATOM
2240
OH2
TIP
S
51
−15.059
118.345
−90.201
1.00
68.42
S

ATOM
2241
OH2
TIP
S
52
−30.824
114.259
−74.515
1.00
91.39
S

ATOM
2242
OH2
TIP
S
53
−31.532
108.464
−82.347
1.00
61.82
S

ATOM
2243
OH2
TIP
S
54
−37.057
103.213
−57.306
1.00
55.29
S

ATOM
2244
OH2
TIP
S
55
−15.159
89.223
−47.068
1.00
62.08
S

ATOM
2245
OH2
TIP
S
56
−15.327
96.363
−53.985
1.00
63.66
S

ATOM
2246
OH2
TIP
S
57
−8.763
96.325
−78.630
1.00
68.63
S

ATOM
2247
OH2
TIP
S
58
−3.897
124.612
−68.352
1.00
54.99
S

ATOM
2248
OH2
TIP
S
59
−21.553
74.980
−60.637
1.00
66.26
S

ATOM
2249
OH2
TIP
S
60
−16.332
117.985
−81.778
1.00
82.09
S

ATOM
2250
OH2
TIP
S
62
−10.541
92.931
−60.120
1.00
61.28
S

ATOM
2251
OH2
TIP
S
63
−19.368
110.784
−52.826
1.00
57.63
S

ATOM
2252
OH2
TIP
S
65
−2.246
124.598
−64.545
1.00
61.06
S

ATOM
2253
OH2
TIP
S
66
−19.885
95.377
−47.136
1.00
94.88
S

ATOM
2254
OH2
TIP
S
67
−33.235
105.665
−77.851
1.00
93.94
S

ATOM
2255
OH2
TIP
S
68
−16.225
88.770
−80.454
1.00
52.18
S

ATOM
2256
OH2
TIP
S
69
−22.493
124.406
−77.955
1.00
77.26
S

ATOM
2257
OH2
TIP
S
70
−45.802
113.820
−68.412
1.00
56.85
S

ATOM
2258
OH2
TIP
S
73
−29.372
123.275
−68.017
1.00
77.12
S

ATOM
2259
OH2
TIP
S
74
−20.194
110.647
−75.811
1.00
72.87
S

ATOM
2260
OH2
TIP
S
75
−13.474
110.285
−57.377
1.00
52.18
S

ATOM
2261
OH2
TIP
S
76
−18.889
122.892
−58.058
1.00
63.85
S

ATOM
2262
OH2
TIP
S
77
−33.242
114.790
−69.241
1.00
90.71
S

ATOM
2263
OH2
TIP
S
78
−37.240
99.603
−86.817
1.00
65.07
S

ATOM
2264
OH2
TIP
S
79
−42.916
107.508
−66.443
1.00
71.85
S

ATOM
2265
OH2
TIP
S
80
−12.507
89.539
−53.003
1.00
52.98
S

ATOM
2266
OH2
TIP
S
81
−22.124
125.331
−65.900
1.00
37.55
S

ATOM
2267
OH2
TIP
S
82
−32.136
110.814
−81.456
1.00
93.66
S

ATOM
2268
OH2
TIP
S
83
−34.216
117.264
−58.785
1.00
49.62
S

ATOM
2269
OH2
TIP
S
84
−22.066
110.808
−48.305
1.00
68.96
S

ATOM
2270
OH2
TIP
S
85
1.915
96.956
−78.632
1.00
75.10
S

ATOM
2271
OH2
TIP
S
86
−6.991
109.235
−79.459
1.00
57.41
S

ATOM
2272
OH2
TIP
S
87
−22.550
116.451
−54.448
1.00
63.30
S

ATOM
2273
OH2
TIP
S
88
−47.364
94.770
−65.585
1.00
50.84
S

ATOM
2274
OH2
TIP
S
89
−18.529
102.462
−73.721
1.00
67.48
S

ATOM
2275
OH2
TIP
S
90
−40.581
100.708
−87.003
1.00
63.83
S

ATOM
2276
OH2
TIP
S
91
−44.190
104.278
−63.609
1.00
68.23
S

ATOM
2277
OH2
TIP
S
93
−39.737
97.108
−52.484
1.00
62.42
S

ATOM
2278
OH2
TIP
S
95
−18.784
124.281
−72.546
1.00
69.88
S

ATOM
2279
OH2
TIP
S
96
−22.323
77.228
−65.503
1.00
81.91
S

ATOM
2280
OH2
TIP
S
97
−41.947
112.253
−72.797
1.00
80.67
S

ATOM
2281
OH2
TIP
S
98
−30.279
91.655
−64.299
1.00
61.84
S

ATOM
2282
OH2
TIP
S
99
−10.995
81.597
−40.763
1.00
56.49
S

ATOM
2283
OH2
TIP
S
101
−30.653
85.509
−82.750
1.00
56.57
S

ATOM
2284
OH2
TIP
S
102
−31.914
113.319
−61.166
1.00
72.30
S

ATOM
2285
OH2
TIP
S
103
−6.815
129.917
−62.463
1.00
51.33
S

ATOM
2286
OH2
TIP
S
104
−15.562
102.708
−65.118
1.00
42.22
S

ATOM
2287
OH2
TIP
S
105
−46.346
107.948
−63.277
1.00
69.86
S

ATOM
2288
OH2
TIP
S
106
−18.087
70.972
−46.270
1.00
66.12
S

ATOM
2289
OH2
TIP
S
107
−43.366
115.216
−64.598
1.00
88.46
S

ATOM
2290
OH2
TIP
S
108
−49.436
89.111
−72.407
1.00
59.04
S

ATOM
2291
OH2
TIP
S
109
−24.747
104.973
−79.131
1.00
94.41
S

ATOM
2292
OH2
TIP
S
110
−14.831
88.579
−50.161
1.00
51.01
S

ATOM
2293
OH2
TIP
S
111
−20.775
93.910
−63.673
1.00
67.89
S

ATOM
2294
OH2
TIP
S
112
−27.551
89.850
−85.485
1.00
62.96
S

ATOM
2295
OH2
TIP
S
113
−9.610
113.671
−56.246
1.00
64.18
S

ATOM
2296
OH2
TIP
S
114
−13.054
116.811
−83.710
1.00
88.12
S

ATOM
2297
OH2
TIP
S
115
−36.908
72.261
−51.629
1.00
52.10
S

ATOM
2298
OH2
TIP
S
117
−6.237
137.377
−67.390
1.00
52.76
5

ATOM
2299
OH2
TIP
S
118
−41.941
80.782
−57.338
1.00
73.11
S

ATOM
2300
OH2
TIP
S
119
−10.771
115.633
−81.759
1.00
85.64
S

ATOM
2301
OH2
TIP
S
120
−8.339
89.553
−70.396
1.00
53.46
S

ATOM
2302
OH2
TIP
S
122
−48.014
76.217
−64.376
1.00
45.72
S

ATOM
2303
OH2
TIP
S
123
−13.904
127.700
−55.955
1.00
55.62
S

ATOM
2304
OH2
TIP
S
124
−17.611
112.118
−90.078
1.00
65.69
S

ATOM
2305
OH2
TIP
S
125
−50.470
95.953
−55.357
1.00
54.87
S

END

[0492]

16

TABLE 5

Coordinate data for ΔPH-PKBβ

CRYST1 149.523 149.523 39.055 90.00 90.00 90.00 P 41 21 2

REMARK FILENAME = “dph-pkb.pdb”

REMARK DATE: 23-Nov-01 19:09:37

REMARK VERSION: 1.1

ATOM
1
CB
ALA

146
−38.038
81.194
−46.909
1.00
73.30

ATOM
2
C
ALA

146
−38.368
81.486
−49.380
1.00
72.38

ATOM
3
O
ALA

146
−38.974
80.443
−49.651
1.00
72.14

ATOM
4
N
ALA

146
−39.973
82.494
−47.814
1.00
72.57

ATOM
5
CA
ALA

146
−38.532
82.146
−48.018
1.00
73.03

ATOM
6
N
ALA

147
−37.552
82.101
−50.235
1.00
71.08

ATOM
7
CA
ALA

147
−37.311
81.581
−51.575
1.00
68.29

ATOM
8
CB
ALA

147
−36.701
82.650
−52.443
1.00
68.54

ATOM
9
C
ALA

147
−36.379
80.400
−51.494
1.00
67.18

ATOM
10
O
ALA

147
−35.737
80.164
−50.473
1.00
66.81

ATOM
11
N
THR

148
−36.294
79.656
−52.581
1.00
66.55

ATOM
12
CA
THR

148
−35.418
78.506
−52.610
1.00
66.31

ATOM
13
CB
THR

148
−36.000
77.352
−51.749
1.00
67.26

ATOM
14
OG1
THR

148
−35.147
77.143
−50.621
1.00
67.64

ATOM
15
CG2
THR

148
−36.119
76.049
−52.542
1.00
66.47

ATOM
16
C
THR

148
−35.204
78.058
−54.039
1.00
66.45

ATOM
17
O
THR

148
−35.996
78.380
−54.926
1.00
66.16

ATOM
18
N
MET

149
−34.124
77.317
−54.251
1.00
65.81

ATOM
19
CA
MET

149
−33.780
76.809
−55.564
1.00
66.24

ATOM
20
CB
MET

149
−32.709
75.732
−55.436
1.00
65.07

ATOM
21
CG
MET

149
−31.299
76.285
−55.380
1.00
63.77

ATOM
22
SD
MET

149
−30.919
77.222
−56.876
1.00
63.06

ATOM
23
CE
MET

149
−29.920
78.511
−56.204
1.00
63.24

ATOM
24
C
MET

149
−34.965
76.251
−56.326
1.00
67.08

ATOM
25
O
MET

149
−35.168
76.573
−57.494
1.00
67.93

ATOM
26
N
ASN

150
−35.759
75.429
−55.651
1.00
68.71

ATOM
27
CA
ASN

150
−36.910
74.785
−56.265
1.00
68.51

ATOM
28
CB
ASN

150
−37.387
73.659
−55.361
1.00
70.67

ATOM
29
CG
ASN

150
−38.132
72.592
−56.118
1.00
74.10

ATOM
30
OD1
ASN

150
−38.586
71.614
−55.533
1.00
77.27

ATOM
31
ND2
ASN

150
−38.260
72.767
−57.433
1.00
76.43

ATOM
32
C
ASN

150
−38.085
75.701
−56.616
1.00
67.77

ATOM
33
O
ASN

150
−39.083
75.248
−57.183
1.00
67.35

ATOM
34
N
ASP

151
−37.982
76.981
−56.276
1.00
65.96

ATOM
35
CA
ASP

151
−39.049
77.919
−56.595
1.00
65.30

ATOM
36
CB
ASP

151
−39.020
79.128
−55.652
1.00
66.76

ATOM
37
CG
ASP

151
−39.490
78.802
−54.238
1.00
68.61

ATOM
38
OD1
ASP

151
−40.554
78.164
−54.090
1.00
69.24

ATOM
39
OD2
ASP

151
−38.807
79.206
−53.267
1.00
70.04

ATOM
40
C
ASP

151
−38.909
78.439
−58.023
1.00
64.65

ATOM
41
O
ASP

151
−39.786
79.147
−58.506
1.00
65.43

ATOM
42
N
PHE

152
−37.822
78.086
−58.706
1.00
63.65

ATOM
43
CA
PHE

152
−37.579
78.603
−60.052
1.00
62.25

ATOM
44
CB
PHE

152
−36.379
79.565
−60.044
1.00
60.50

ATOM
45
CG
PHE

152
−36.425
80.620
−58.974
1.00
57.88

ATOM
46
CD1
PHE

152
−37.115
81.801
−59.173
1.00
56.75

ATOM
47
CD2
PHE

152
−35.750
80.432
−57.768
1.00
57.33

ATOM
48
CE1
PHE

152
−37.136
82.786
−58.179
1.00
56.94

ATOM
49
CE2
PHE

152
−35.760
81.400
−56.774
1.00
56.46

ATOM
50
CZ
PHE

152
−36.452
82.579
−56.978
1.00
57.58

ATOM
51
C
PHE

152
−37.284
77.556
−61.118
1.00
63.50

ATOM
52
O
PHE

152
−36.883
76.426
−60.816
1.00
64.19

ATOM
53
N
ASP

153
−37.458
77.973
−62.375
1.00
63.33

ATOM
54
CA
ASP

153
−37.178
77.150
−63.545
1.00
62.04

ATOM
55
CB
ASP

153
−38.379
77.111
−64.493
1.00
64.71

ATOM
56
CG
ASP

153
−39.517
76.236
−63.973
1.00
67.74

ATOM
57
OD1
ASP

153
−39.297
75.021
−63.764
1.00
68.84

ATOM
58
OD2
ASP

153
−40.636
76.763
−63.779
1.00
68.99

ATOM
59
C
ASP

153
−35.992
77.774
−64.272
1.00
60.87

ATOM
60
O
ASP

153
−35.891
78.998
−64.387
1.00
60.45

ATOM
61
N
TYR

154
−35.099
76.925
−64.760
1.00
58.73

ATOM
62
CA
TYR

154
−33.918
77.366
−65.475
1.00
57.74

ATOM
63
CB
TYR

154
−32.856
76.282
−65.405
1.00
57.78

ATOM
64
CG
TYR

154
−31.632
76.579
−66.248
1.00
58.77

ATOM
65
CD1
TYR

154
−30.660
77.485
−65.813
1.00
59.49

ATOM
66
CE1
TYR

154
−29.515
77.711
−66.553
1.00
60.96

ATOM
67
CD2
TYR

154
−31.423
75.918
−67.451
1.00
57.76

ATOM
68
CE2
TYR

154
−30.278
76.133
−68.193
1.00
59.31

ATOM
69
CZ
TYR

154
−29.327
77.024
−67.739
1.00
61.22

ATOM
70
OH
TYR

154
−28.165
77.185
−68.452
1.00
62.54

ATOM
71
C
TYR

154
−34.146
77.694
−66.949
1.00
57.85

ATOM
72
O
TYR

154
−34.715
76.898
−67.682
1.00
59.77

ATOM
73
N
LEU

155
−33.678
78.849
−67.405
1.00
57.45

ATOM
74
CA
LEU

155
−33.836
79.179
−68.816
1.00
55.82

ATOM
75
CB
LEU

155
−34.554
80.519
−68.981
1.00
53.85

ATOM
76
CG
LEU

155
−35.982
80.397
−68.459
1.00
54.19

ATOM
77
CD1
LEU

155
−36.671
81.722
−68.473
1.00
53.47

ATOM
78
CD2
LEU

155
−36.738
79.377
−69.306
1.00
54.40

ATOM
79
C
LEU

155
−32.498
79.199
−69.527
1.00
55.26

ATOM
80
O
LEU

155
−32.247
78.384
−70.412
1.00
53.81

ATOM
81
N
LYS

156
−31.622
80.111
−69.125
1.00
56.86

ATOM
82
CA
LYS

156
−30.319
80.210
−69.774
1.00
57.99

ATOM
83
CB
LYS

156
−30.438
81.052
−71.056
1.00
58.45

ATOM
84
CG
LYS

156
−31.162
82.394
−70.854
1.00
59.97

ATOM
85
CD
LYS

156
−31.156
83.250
−72.125
1.00
60.20

ATOM
86
CE
LYS

156
−29.778
83.830
−72.408
1.00
59.49

ATOM
87
NZ
LYS

156
−29.771
84.739
−73.587
1.00
60.88

ATOM
88
C
LYS

156
−29.213
80.796
−68.914
1.00
57.53

ATOM
89
O
LYS

156
−29.447
81.368
−67.843
1.00
56.57

ATOM
90
N
LEU

157
−28.000
80.644
−69.418
1.00
57.95

ATOM
91
CA
LEU

157
−26.819
81.162
−68.764
1.00
60.12

ATOM
92
CB
LEU

157
−25.604
80.336
−69.161
1.00
59.27

ATOM
93
CG
LEU

157
−24.256
80.791
−68.607
1.00
58.35

ATOM
94
CD1
LEU

157
−24.330
80.986
−67.101
1.00
57.36

ATOM
95
CD2
LEU

157
−23.211
79.742
−68.966
1.00
58.09

ATOM
96
C
LEU

157
−26.644
82.592
−69.244
1.00
61.72

ATOM
97
O
LEU

157
−26.534
82.826
−70.441
1.00
62.13

ATOM
98
N
LEU

158
−26.632
83.541
−68.311
1.00
63.84

ATOM
99
CA
LEU

158
−26.480
84.954
−68.647
1.00
65.91

ATOM
100
CB
LEU

158
−27.291
85.832
−67.689
1.00
64.45

ATOM
101
CG
LEU

158
−28.814
85.750
−67.821
1.00
64.01

ATOM
102
CD1
LEU

158
−29.457
86.404
−66.607
1.00
64.00

ATOM
103
CD2
LEU

158
−29.270
86.421
−69.109
1.00
61.97

ATOM
104
C
LEU

158
−25.024
85.359
−68.582
1.00
67.50

ATOM
105
O
LEU

158
−24.566
86.154
−69.385
1.00
68.41

ATOM
106
N
GLY

159
−24.298
84.804
−67.625
1.00
70.15

ATOM
107
CA
GLY

159
−22.895
85.139
−67.494
1.00
74.03

ATOM
108
C
GLY

159
−22.215
84.276
−66.456
1.00
76.35

ATOM
109
O
GLY

159
−22.840
83.849
−65.490
1.00
76.38

ATOM
110
N
LYS

160
−20.934
84.006
−66.657
1.00
79.22

ATOM
111
CA
LYS

160
−20.186
83.188
−65.710
1.00
82.44

ATOM
112
CB
LYS

160
−19.600
81.968
−66.428
1.00
83.26

ATOM
113
CG
LYS

160
−19.286
80.795
−65.512
1.00
85.18

ATOM
114
CD
LYS

160
−18.705
79.613
−66.283
1.00
86.35

ATOM
115
CE
LYS

160
−18.593
78.367
−65.396
1.00
87.69

ATOM
116
NZ
LYS

160
−17.868
77.240
−66.058
1.00
87.72

ATOM
117
C
LYS

160
−19.072
84.052
−65.100
1.00
84.24

ATOM
118
O
LYS

160
−19.025
85.263
−65.340
1.00
84.74

ATOM
119
N
GLY

161
−18.189
83.452
−64.304
1.00
85.47

ATOM
120
CA
GLY

161
−17.116
84.235
−63.715
1.00
86.79

ATOM
121
C
GLY

161
−16.253
83.558
−62.666
1.00
87.65

ATOM
122
O
GLY

161
−16.388
82.366
−62.394
1.00
87.66

ATOM
123
N
THR

162
−15.352
84.341
−62.079
1.00
88.86

ATOM
124
CA
THR

162
−14.442
83.859
−61.042
1.00
89.23

ATOM
125
CB
THR

162
−13.109
84.639
−61.078
1.00
90.45

ATOM
126
OG1
THR

162
−12.755
84.919
−62.442
1.00
91.39

ATOM
127
CG2
THR

162
−12.000
83.821
−60.438
1.00
90.70

ATOM
128
C
THR

162
−15.119
84.083
−59.688
1.00
88.56

ATOM
129
O
THR

162
−14.593
83.718
−58.635
1.00
89.01

ATOM
130
N
PHE

163
−16.298
84.694
−59.743
1.00
87.18

ATOM
131
CA
PHE

163
−17.098
84.983
−58.562
1.00
85.60

ATOM
132
CB
PHE

163
−17.620
86.409
−58.663
1.00
86.54

ATOM
133
CG
PHE

163
−18.367
86.686
−59.943
1.00
88.12

ATOM
134
CD1
PHE

163
−19.706
86.313
−60.083
1.00
88.11

ATOM
135
CD2
PHE

163
−17.729
87.308
−61.013
1.00
88.99

ATOM
136
CE1
PHE

163
−20.403
86.560
−61.262
1.00
88.63

ATOM
137
CE2
PHE

163
−18.416
87.561
−62.201
1.00
89.91

ATOM
138
CZ
PHE

163
−19.761
87.183
−62.325
1.00
89.59

ATOM
139
C
PHE

163
−18.269
83.990
−58.512
1.00
83.93

ATOM
140
O
PHE

163
−18.797
83.678
−57.441
1.00
82.94

ATOM
141
N
GLY

164
−18.654
83.499
−59.691
1.00
81.62

ATOM
142
CA
GLY

164
−19.751
82.552
−59.807
1.00
78.46

ATOM
143
C
GLY

164
−20.414
82.557
−61.181
1.00
75.60

ATOM
144
O
GLY

164
−19.757
82.319
−62.203
1.00
75.33

ATOM
145
N
LYS

165
−21.721
82.808
−61.212
1.00
72.45

ATOM
46
CA
LYS

165
−22.457
82.844
−62.471
1.00
69.28

ATOM
147
CB
LYS

165
−22.642
81.420
−63.023
1.00
69.65

ATOM
148
CG
LYS

165
−23.791
80.627
−62.431
1.00
70.80

ATOM
149
CD
LYS

165
−23.723
79.153
−62.824
1.00
73.65

ATOM
150
CE
LYS

165
−22.523
78.462
−62.159
1.00
75.99

ATOM
151
NZ
LYS

165
−22.550
76.965
−62.206
1.00
75.49

ATOM
152
C
LYS

165
−23.818
83.521
−62.316
1.00
67.03

ATOM
153
O
LYS

165
−24.328
83.676
−61.205
1.00
65.82

ATOM
154
N
VAL

166
−24.386
83.940
−63.442
1.00
64.70

ATOM
155
CA
VAL

166
−25.697
84.579
−63.460
1.00
62.03

ATOM
156
CB
VAL

166
−25.633
86.040
−63.936
1.00
60.81

ATOM
157
CG1
VAL

166
−26.987
86.689
−63.762
1.00
60.12

ATOM
158
CG2
VAL

166
−24.573
86.800
−63.163
1.00
59.49

ATOM
159
C
VAL

166
−26.553
83.780
−64.430
1.00
61.42

ATOM
160
O
VAL

166
−26.161
83.530
−65.570
1.00
59.35

ATOM
161
N
ILE

167
−27.728
83.389
−63.957
1.00
61.73

ATOM
162
CA
ILE

167
−28.656
82.581
−64.730
1.00
61.19

ATOM
163
CB
ILE

167
−28.970
81.289
−63.979
1.00
60.19

ATOM
164
CG2
ILE

167
−29.944
80.464
−64.768
1.00
61.63

ATOM
165
CG1
ILE

167
−27.685
80.518
−63.696
1.00
60.81

ATOM
166
CD1
ILE

167
−26.997
79.990
−64.930
1.00
61.62

ATOM
167
C
ILE

167
−29.975
83.297
−64.945
1.00
61.83

ATOM
168
O
ILE

167
−30.381
84.128
−64.134
1.00
63.36

ATOM
169
N
LEU

168
−30.651
82.969
−66.036
1.00
61.16

ATOM
170
CA
LEU

168
−31.957
83.553
−66.313
1.00
59.71

ATOM
171
CB
LEU

168
−32.152
83.764
−67.820
1.00
59.59

ATOM
172
CG
LEU

168
−33.463
84.396
−68.300
1.00
59.38

ATOM
173
CD1
LEU

168
−33.747
85.672
−67.521
1.00
58.51

ATOM
174
CD2
LEU

168
−33.366
84.690
−69.790
1.00
60.52

ATOM
175
C
LEU

168
−32.934
82.506
−65.807
1.00
59.39

ATOM
176
O
LEU

168
−32.858
81.344
−66.210
1.00
60.09

ATOM
177
N
VAL

169
−33.830
82.900
−64.908
1.00
58.74

ATOM
178
CA
VAL

169
−34.819
81.967
−64.367
1.00
57.54

ATOM
179
CB
VAL

169
−34.457
81.502
−62.931
1.00
56.13

ATOM
180
CG1
VAL

169
−33.076
80.892
−62.916
1.00
53.50

ATOM
181
CG2
VAL

169
−34.544
82.668
−61.965
1.00
52.21

ATOM
182
C
VAL

169
−36.215
82.566
−64.319
1.00
58.69

ATOM
183
O
VAL

169
−36.400
83.778
−64.458
1.00
56.03

ATOM
184
N
ARG

170
−37.194
81.691
−64.120
1.00
60.60

ATOM
185
CA
ARG

170
−38.582
82.090
−64.026
1.00
63.17

ATOM
186
CB
ARG

170
−39.410
81.449
−65.148
1.00
64.23

ATOM
187
CG
ARG

170
−40.825
82.053
−65.318
1.00
65.59

ATOM
188
CD
ARG

170
−41.746
81.157
−66.154
1.00
66.11

ATOM
189
NE
ARG

170
−41.068
80.639
−67.342
1.00
67.53

ATOM
190
CZ
ARG

170
−40.827
79.347
−67.572
1.00
67.14

ATOM
191
NH1
ARG

170
−41.213
78.427
−66.693
1.00
66.28

ATOM
192
NH2
ARG

170
−40.194
78.976
−68.682
1.00
66.92

ATOM
193
C
ARG

170
−39.131
81.629
−62.686
1.00
64.75

ATOM
194
O
ARG

170
−39.107
80.439
−62.385
1.00
65.77

ATOM
195
N
GLU

171
−39.609
82.563
−61.875
1.00
66.65

ATOM
196
CA
GLU

171
−40.200
82.198
−60.599
1.00
68.87

ATOM
197
CB
GLU

171
−40.559
83.454
−59.808
1.00
68.24

ATOM
198
CG
CLU

171
−41.489
83.212
−58.645
1.00
69.67

ATOM
199
CD
GLU

171
−41.577
84.399
−57.692
1.00
71.08

ATOM
200
OE1
GLU

171
−41.646
85.567
−58.160
1.00
70.33

ATOM
201
OE2
GLU

171
−41.586
84.151
−56.466
1.00
70.60

ATOM
202
C
GLU

171
−41.451
81.415
−60.981
1.00
71.35

ATOM
203
O
GLU

171
−42.307
81.922
−61.701
1.00
72.05

ATOM
204
N
LYS

172
−41.552
80.171
−60.529
1.00
73.13

ATOM
205
CA
LYS

172
−42.703
79.355
−60.875
1.00
74.23

ATOM
206
CB
LYS

172
−42.483
77.922
−60.399
1.00
74.29

ATOM
207
CG
LYS

172
−41.471
77.214
−61.274
1.00
75.99

ATOM
208
CD
LYS

172
−41.241
75.757
−60.912
1.00
76.76

ATOM
209
CE
LYS

172
−40.397
75.598
−59.660
1.00
76.33

ATOM
210
NZ
LYS

172
−39.910
74.195
−59.515
1.00
75.41

ATOM
211
C
LYS

172
−44.037
79.891
−60.379
1.00
75.60

ATOM
212
O
LYS

172
−45.072
79.663
−61.004
1.00
76.21

ATOM
213
N
ALA

173
−44.023
80.612
−59.265
1.00
77.07

ATOM
214
CA
ALA

173
−45.258
81.174
−58.729
1.00
78.78

ATOM
215
CB
ALA

173
−45.016
81.745
−57.330
1.00
78.63

ATOM
216
C
ALA

173
−45.770
82.272
−59.661
1.00
79.50

ATOM
217
O
ALA

173
−46.722
82.068
−60.419
1.00
79.63

ATOM
218
N
THR

174
−45.106
83.427
−59.610
1.00
79.51

ATOM
219
CA
THR

174
−45.474
84.588
−60.414
1.00
78.86

ATOM
220
CB
THR

174
−44.739
85.874
−59.929
1.00
79.44

ATOM
221
OG1
THR

174
−43.332
85.759
−60.187
1.00
79.70

ATOM
222
CG2
THR

174
−44.965
86.097
−58.437
1.00
79.83

ATOM
223
C
THR

174
−45.237
84.476
−61.918
1.00
78.33

ATOM
224
O
THR

174
−45.724
85.306
−62.675
1.00
79.01

ATOM
225
N
GLY

175
−44.496
83.470
−62.361
1.00
77.74

ATOM
226
CA
GLY

175
−44.233
83.350
−63.784
1.00
76.56

ATOM
227
C
GLY

175
−43.262
84.417
−64.268
1.00
76.35

ATOM
228
O
GLY

175
−42.861
84.413
−65.431
1.00
76.58

ATOM
229
N
ARG

176
−42.881
85.323
−63.370
1.00
75.54

ATOM
230
CA
ARG

176
−41.957
86.411
−63.680
1.00
75.88

ATOM
231
CB
ARG

176
−41.906
87.392
−62.505
1.00
79.56

ATOM
232
CG
ARG

176
−43.242
88.006
−62.109
1.00
84.08

ATOM
233
CD
ARG

176
−43.796
88.927
−63.190
1.00
88.26

ATOM
234
NE
ARG

176
−45.072
89.523
−62.788
1.00
92.52

ATOM
235
CZ
ARG

176
−45.910
90.140
−63.621
1.00
94.75

ATOM
236
NH1
ARG

176
−45.610
90.243
−64.912
1.00
95.39

ATOM
237
NH2
ARG

176
−47.048
90.659
−63.165
1.00
95.28

ATOM
238
C
ARG

176
−40.524
85.936
−63.997
1.00
74.64

ATOM
239
O
ARG

176
−40.163
84.791
−63.725
1.00
74.48

ATOM
240
N
TYR

177
−39.712
86.836
−64.556
1.00
71.66

ATOM
241
CA
TYR

177
−38.330
86.529
−64.915
1.00
68.53

ATOM
242
CB
TYR

177
−38.078
86.842
−66.390
1.00
69.30

ATOM
243
CG
TYR

177
−38.757
85.900
−67.346
1.00
71.43

ATOM
244
CD1
TYR

177
−40.141
85.889
−67.483
1.00
73.14

ATOM
245
CE1
TYR

177
−40.770
85.008
−68.358
1.00
73.22

ATOM
246
CD2
TYR

177
−38.018
85.007
−68.110
1.00
72.26

ATOM
247
CE2
TYR

177
−38.640
84.126
−68.986
1.00
73.17

ATOM
248
CZ
TYR

177
−40.012
84.131
−69.102
1.00
73.66

ATOM
249
OH
TYR

177
−40.625
83.249
−69.958
1.00
75.02

ATOM
250
C
TYR

177
−37.304
87.288
−64.082
1.00
65.96

ATOM
251
O
TYR

177
−37.422
88.490
−63.863
1.00
66.11

ATOM
252
N
TYR

178
−36.284
86.575
−63.626
1.00
62.93

ATOM
253
CA
TYR

178
−35.226
87.176
−62.833
1.00
60.28

ATOM
254
CB
TYR

178
−35.401
86.848
−61.346
1.00
60.14

ATOM
255
CG
TYR

178
−36.695
87.370
−60.759
1.00
60.36

ATOM
256
CD1
TYR

178
−37.903
86.683
−60.948
1.00
59.37

ATOM
257
CE1
TYR

178
−39.101
87.203
−60.482
1.00
59.43

ATOM
258
CD2
TYR

178
−36.726
88.591
−60.078
1.00
59.40

ATOM
259
CE2
TYR

178
−37.917
89.119
−59.609
1.00
60.14

ATOM
260
CZ
TYR

178
−39.100
88.422
−59.816
1.00
60.79

ATOM
261
OH
TYR

178
−40.279
88.963
−59.366
1.00
64.02

ATOM
262
C
TYR

178
−33.900
86.642
−63.311
1.00
58.68

ATOM
263
O
TYR

178
−33.844
85.715
−64.107
1.00
56.28

ATOM
264
N
ALA

179
−32.835
87.261
−62.834
1.00
59.19

ATOM
265
CA
ALA

179
−31.483
86.849
−63.167
1.00
61.40

ATOM
266
CB
ALA

179
−30.692
88.012
−63.758
1.00
60.64

ATOM
267
C
ALA

179
−30.897
86.427
−61.835
1.00
63.02

ATOM
268
O
ALA

179
−30.706
87.252
−60.938
1.00
65.07

ATOM
269
N
MET

180
−30.632
85.137
−61.695
1.00
63.09

ATOM
270
CA
MET

180
−30.103
84.617
−60.444
1.00
63.02

ATOM
271
CB
MET

180
−30.634
83.202
−60.223
1.00
61.42

ATOM
272
CG
MET

180
−30.405
82.667
−58.837
1.00
61.56

ATOM
273
SD
MET

180
−30.840
80.947
−58.736
1.00
60.07

ATOM
274
CE
MET

180
−32.520
81.084
−58.339
1.00
61.93

ATOM
275
C
MET

180
−28.575
84.624
−60.398
1.00
63.37

ATOM
276
O
MET

180
−27.924
83.813
−61.053
1.00
64.64

ATOM
277
N
LYS

181
−28.011
85.554
−59.634
1.00
63.37

ATOM
278
CA
LYS

181
−26.565
85.655
−59.485
1.00
63.94

ATOM
279
CB
LYS

181
−26.171
87.067
−59.034
1.00
64.76

ATOM
280
CG
LYS

181
−24.668
87.288
−58.867
1.00
67.65

ATOM
281
CD
LYS

181
−24.298
88.765
−58.618
1.00
68.44

ATOM
282
CE
LYS

181
−22.782
88.973
−58.688
1.00
69.54

ATOM
283
NZ
LYS

181
−22.348
90.393
−58.617
1.00
69.40

ATOM
284
C
LYS

181
−26.174
84.633
−58.420
1.00
64.61

ATOM
285
O
LYS

181
−26.638
84.709
−57.279
1.00
64.31

ATOM
286
N
ILE

182
−25.334
83.672
−58.794
1.00
64.41

ATOM
287
CA
ILE

182
−24.908
82.627
−57.866
1.00
65.06

ATOM
288
CB
ILE

182
−25.222
81.227
−58.447
1.00
63.16

ATOM
289
CG2
ILE

182
−25.096
80.166
−57.359
1.00
63.49

ATOM
290
CG1
ILE

182
−26.653
81.202
−58.994
1.00
61.58

ATOM
291
CD1
ILE

182
−27.053
79.869
−59.563
1.00
58.80

ATOM
292
C
ILE

182
−23.412
82.712
−57.532
1.00
66.90

ATOM
293
O
ILE

182
−22.560
82.616
−58.413
1.00
66.62

ATOM
294
N
LEU

183
−23.098
82.873
−56.252
1.00
68.62

ATOM
295
CA
LEU

183
−21.707
82.985
−55.820
1.00
71.25

ATOM
296
CB
LEU

183
−21.515
84.307
−55.079
1.00
70.08

ATOM
297
CG
LEU

183
−21.909
85.553
−55.859
1.00
70.20

ATOM
298
CD1
LEU

183
−21.690
86.766
−54.988
1.00
69.25

ATOM
299
CD2
LEU

183
−21.089
85.643
−57.136
1.00
69.20

ATOM
300
C
LEU

183
−21.210
81.848
−54.920
1.00
73.26

ATOM
301
O
LEU

183
−21.897
81.450
−53.980
1.00
72.60

ATOM
302
N
ARG

184
−20.011
81.341
−55.206
1.00
76.22

ATOM
303
CA
ARG

184
−19.419
80.281
−54.388
1.00
80.60

ATOM
304
CB
ARG

184
−18.155
79.713
−55.050
1.00
80.79

ATOM
305
CG
ARG

184
−18.268
79.293
−56.510
1.00
83.12

ATOM
306
CD
ARG

184
−18.797
77.878
−56.657
1.00
84.80

ATOM
307
NE
ARG

184
−18.527
77.272
−57.971
1.00
87.21

ATOM
308
CZ
ARG

184
−18.831
77.815
−59.152
1.00
88.61

ATOM
309
NH1
ARG

184
−19.418
79.005
−59.231
1.00
89.57

ATOM
310
NH2
ARG

184
−18.572
77.148
−60.268
1.00
88.97

ATOM
311
C
ARG

184
−19.011
80.912
−53.044
1.00
82.32

ATOM
312
O
ARG

184
−18.384
81.969
−53.029
1.00
82.47

ATOM
313
N
LYS

185
−19.375
80.285
−51.925
1.00
84.93

ATOM
314
CA
LYS

185
−18.993
80.798
−50.606
1.00
87.47

ATOM
315
CB
LYS

185
−19.742
80.056
−49.497
1.00
86.74

ATOM
316
CG
LYS

185
−21.219
80.385
−49.403
1.00
88.14

ATOM
317
CD
LYS

185
−21.881
79.652
−48.230
1.00
88.29

ATOM
318
CE
LYS

185
−23.367
79.996
−48.113
1.00
88.05

ATOM
319
NZ
LYS

185
−24.098
79.175
−47.103
1.00
86.65

ATOM
320
C
LYS

185
−17.489
80.550
−50.457
1.00
89.82

ATOM
321
O
LYS

185
−16.768
81.280
−49.760
1.00
89.49

ATOM
322
N
GLU

186
−17.050
79.498
−51.144
1.00
91.98

ATOM
323
CA
GLU

186
−15.667
79.043
−51.184
1.00
93.99

ATOM
324
CB
GLU

186
−15.618
77.738
−51.989
1.00
95.74

ATOM
325
CG
GLU

186
−14.247
77.095
−52.150
1.00
97.28

ATOM
326
CD
GLU

186
−14.316
75.782
−52.925
1.00
97.52

ATOM
327
OE1
GLU

186
−14.841
75.784
−54.064
1.00
97.04

ATOM
328
OE2
GLU

186
−13.845
74.752
−52.391
1.00
97.90

ATOM
329
C
GLU

186
−14.751
80.101
−51.808
1.00
94.24

ATOM
330
O
GLU

186
−13.632
80.311
−51.346
1.00
94.97

ATOM
331
N
VAL

187
−15.227
80.760
−52.859
1.00
94.74

ATOM
332
CA
VAL

187
−14.451
81.806
−53.525
1.00
95.50

ATOM
333
CB
VAL

187
−15.155
82.287
−54.813
1.00
95.76

ATOM
334
CG1
VAL

187
−14.562
83.618
−55.277
1.00
95.48

ATOM
335
CG2
VAL

187
−15.014
81.225
−55.902
1.00
95.91

ATOM
336
C
VAL

187
−14.249
82.999
−52.592
1.00
95.59

ATOM
337
O
VAL

187
−13.149
83.538
−52.495
1.00
95.85

ATOM
338
N
ILE

188
−15.317
83.405
−51.912
1.00
95.86

ATOM
339
CA
ILE

188
−15.251
84.520
−50.974
1.00
96.27

ATOM
340
CB
ILE

188
−16.533
85.390
−51.038
1.00
96.69

ATOM
341
CG2
ILE

188
−17.765
84.521
−50.815
1.00
96.39

ATOM
342
CG1
ILE

188
−16.456
86.511
−49.991
1.00
97.39

ATOM
343
CD1
ILE

188
−17.633
87.478
−49.997
1.00
97.60

ATOM
344
C
ILE

188
−15.082
84.000
−49.543
1.00
96.43

ATOM
345
O
ILE

188
−14.092
83.338
−49.216
1.00
96.41

ATOM
346
N
ALA

198
−18.432
91.977
−49.977
1.00
117.70

ATOM
347
CA
ALA

198
−19.657
92.421
−49.318
1.00
117.91

ATOM
348
CB
ALA

198
−19.440
92.483
−47.809
1.00
117.84

ATOM
349
C
ALA

198
−20.108
93.785
−49.838
1.00
117.87

ATOM
350
O
ALA

198
−21.090
94.347
−49.353
1.00
116.79

ATOM
351
N
ALA

199
−19.383
94.304
−50.830
1.00
118.49

ATOM
352
CA
ALA

199
−19.679
95.608
−51.432
1.00
118.40

ATOM
353
CB
ALA

199
−18.422
96.179
−52.095
1.00
118.07

ATOM
354
C
ALA

199
−20.810
95.530
−52.452
1.00
118.10

ATOM
355
O
ALA

199
−21.239
96.552
−52.996
1.00
118.77

ATOM
356
N
ALA

200
−21.279
94.314
−52.717
1.00
117.30

ATOM
357
CA
ALA

200
−22.372
94.091
−53.660
1.00
116.57

ATOM
358
CB
ALA

200
−21.991
92.987
−54.656
1.00
116.07

ATOM
359
C
ALA

200
−23.613
93.684
−52.862
1.00
116.02

ATOM
360
O
ALA

200
−24.727
94.145
−53.124
1.00
115.51

ATOM
361
N
ALA

201
−23.391
92.819
−51.877
1.00
115.78

ATOM
362
CA
ALA

201
−24.449
92.316
−51.007
1.00
115.19

ATOM
363
CB
ALA

201
−23.954
91.075
−50.261
1.00
115.46

ATOM
364
C
ALA

201
−24.886
93.387
−50.008
1.00
114.36

ATOM
365
O
ALA

201
−24.098
94.260
−49.644
1.00
114.73

ATOM
366
N
ALA

202
−26.139
93.305
−49.564
1.00
112.87

ATOM
367
CA
ALA

202
−26.701
94.261
−48.610
1.00
110.91

ATOM
368
CB
ALA

202
−25.936
94.196
−47.292
1.00
110.82

ATOM
369
C
ALA

202
−26.695
95.691
−49.159
1.00
109.43

ATOM
370
O
ALA

202
−27.748
96.316
−49.280
1.00
108.79

ATOM
371
N
ALA

203
−25.509
96.200
−49.487
1.00
107.83

ATOM
372
CA
ALA

203
−25.353
97.551
−50.026
1.00
105.87

ATOM
373
CB
ALA

203
−23.883
97.817
−50.363
1.00
105.05

ATOM
374
C
ALA

203
−26.216
97.731
−51.272
1.00
104.62

ATOM
375
O
ALA

203
−27.076
98.615
−51.315
1.00
104.45

ATOM
376
N
ALA

204
−25.980
96.888
−52.278
1.00
102.74

ATOM
377
CA
ALA

204
−26.733
96.939
−53.527
1.00
100.15

ATOM
378
CB
ALA

204
−25.961
96.229
−54.628
1.00
99.98

ATOM
379
C
ALA

204
−28.120
96.312
−53.379
1.00
98.72

ATOM
380
O
ALA

204
−28.937
96.392
−54.290
1.00
98.28

ATOM
381
N
ALA

205
−28.381
95.690
−52.232
1.00
97.13

ATOM
382
CA
ALA

205
−29.671
95.049
−51.975
1.00
94.82

ATOM
383
CB
ALA

205
−29.505
93.932
−50.955
1.00
95.03

ATOM
384
C
ALA

205
−30.721
96.040
−51.480
1.00
93.24

ATOM
385
O
ALA

205
−31.908
95.894
−51.775
1.00
93.26

ATOM
386
N
ALA

206
−30.279
97.045
−50.726
1.00
90.80

ATOM
387
CA
ALA

206
−31.183
98.053
−50.178
1.00
87.61

ATOM
388
CB
ALA

206
−30.801
98.360
−48.721
1.00
87.13

ATOM
389
C
ALA

206
−31.217
99.346
−51.006
1.00
85.44

ATOM
390
O
ALA

206
−32.114
100.179
−50.834
1.00
85.50

ATOM
391
N
THR

207
−30.248
99.520
−51.899
1.00
82.56

ATOM
392
CA
THR

207
−30.231
100.712
−52.735
1.00
79.10

ATOM
393
CB
THR

207
−28.823
101.026
−53.286
1.00
79.91

ATOM
394
OG1
THR

207
−28.258
99.834
−53.848
1.00
81.31

ATOM
395
CG2
THR

207
−27.918
101.576
−52.185
1.00
77.84

ATOM
396
C
THR

207
−31.184
100.490
−53.900
1.00
76.04

ATOM
397
O
THR

207
−30.847
99.845
−54.897
1.00
76.19

ATOM
398
N
ARG

208
−32.392
101.015
−53.733
1.00
72.56

ATOM
399
CA
ARG

208
−33.450
100.934
−54.725
1.00
68.12

ATOM
400
CB
ARG

208
−34.805
101.004
−54.014
1.00
70.61

ATOM
401
CG
ARG

208
−36.005
100.761
−54.912
1.00
76.14

ATOM
402
CD
ARG

208
−36.284
99.268
−55.079
1.00
79.38

ATOM
403
NE
ARG

208
−37.338
99.008
−56.060
1.00
82.09

ATOM
404
CZ
ARG

208
−37.984
97.849
−56.187
1.00
82.92

ATOM
405
NH1
ARG

208
−37.696
96.822
−55.392
1.00
81.74

ATOM
406
NH2
ARG

208
−38.922
97.716
−57.116
1.00
84.03

ATOM
407
C
ARG

208
−33.257
102.162
−55.614
1.00
62.90

ATOM
408
O
ARG

208
−32.694
103.146
−55.163
1.00
62.14

ATOM
409
N
HIS

209
−33.693
102.091
−56.871
1.00
58.01

ATOM
410
CA
HIS

209
−33.596
103.216
−57.808
1.00
51.56

ATOM
411
CB
HIS

209
−32.180
103.743
−57.869
1.00
48.75

ATOM
412
CG
HIS

209
−32.029
104.974
−58.700
1.00
45.36

ATOM
413
CD2
HIS

209
−31.525
106.195
−58.398
1.00
46.04

ATOM
414
ND1
HIS

209
−32.323
105.004
−60.047
1.00
44.41

ATOM
415
CE1
HIS

209
−31.996
106.186
−60.540
1.00
44.49

ATOM
416
NE2
HIS

209
−31.507
106.927
−59.561
1.00
44.97

ATOM
417
C
HIS

209
−34.051
102.883
−59.224
1.00
49.66

ATOM
418
O
HIS

209
−33.667
101.874
−59.792
1.00
49.96

ATOM
419
N
PRO

210
−34.884
103.746
−59.813
1.00
48.82

ATOM
420
CD
PRO

210
−35.383
104.998
−59.215
1.00
48.63

ATOM
421
CA
PRO

210
−35.419
103.594
−61.163
1.00
47.87

ATOM
422
CB
PRO

210
−35.758
105.026
−61.544
1.00
46.95

ATOM
423
CG
PRO

210
−36.306
105.535
−60.293
1.00
47.55

ATOM
424
C
PRO

210
−34.502
102.943
−62.188
1.00
46.22

ATOM
425
O
PRO

210
−34.944
102.085
−63.941
1.00
46.47

ATOM
426
N
PHE

211
−33.236
103.338
−62.239
1.00
44.18

ATOM
427
CA
PHE

211
−32.382
102.749
−63.255
1.00
46.44

ATOM
428
CB
PHE

211
−31.700
103.856
−64.063
1.00
47.76

ATOM
429
CG
PHE

211
−32.607
105.030
−64.370
1.00
48.19

ATOM
430
CD1
PHE

211
−33.765
104.861
−65.118
1.00
47.07

ATOM
431
CD2
PHE

211
−32.311
106.298
−63.880
1.00
47.92

ATOM
432
CE1
PHE

211
−34.612
105.933
−65.370
1.00
45.67

ATOM
433
CE2
PHE

211
−33.158
107.378
−64.129
1.00
46.63

ATOM
434
CZ
PHE

211
−34.305
107.189
−64.874
1.00
45.23

ATOM
435
C
PHE

211
−31.352
101.730
−62.782
1.00
46.35

ATOM
436
O
PHE

211
−30.536
101.294
−63.570
1.00
45.82

ATOM
437
N
LEU

212
−31.376
101.366
−61.502
1.00
47.14

ATOM
438
CA
LEU

212
−30.456
100.355
−60.986
1.00
46.76

ATOM
439
CB
LEU

212
−29.932
100.715
−59.600
1.00
46.32

ATOM
440
CG
LEU

212
−28.978
101.901
−59.401
1.00
48.02

ATOM
441
CD1
LEU

212
−28.542
101.926
−57.944
1.00
46.97

ATOM
442
CD2
LEU

212
−27.753
101.797
−60.292
1.00
44.88

ATOM
443
C
LEU

212
−31.300
99.098
−60.887
1.00
47.83

ATOM
444
O
LEU

212
−32.479
99.175
−60.560
1.00
48.46

ATOM
445
N
THR

213
−30.721
97.952
−61.214
1.00
48.26

ATOM
446
CA
THR

213
−31.443
96.682
−61.135
1.00
49.99

ATOM
447
CB
THR

213
−30.578
95.530
−61.691
1.00
51.36

ATOM
448
OG1
THR

213
−30.281
95.780
−63.072
1.00
54.33

ATOM
449
CG2
THR

213
−31.299
94.201
−61.560
1.00
50.71

ATOM
450
C
THR

213
−31.830
96.335
−59.683
1.00
49.59

ATOM
451
O
THR

213
−30.996
96.357
−58.769
1.00
47.56

ATOM
452
N
ALA

214
−33.096
96.001
−59.473
1.00
50.39

ATOM
453
CA
ALA

214
−33.577
95.660
−58.131
1.00
52.38

ATOM
454
CB
ALA

214
−35.075
95.911
−58.030
1.00
50.72

ATOM
455
C
ALA

214
−33.289
94.222
−57.723
1.00
51.99

ATOM
456
O
ALA

214
−33.410
93.300
−58.523
1.00
51.79

ATOM
457
N
LEU

215
−32.915
94.043
−56.467
1.00
53.66

ATOM
458
CA
LEU

215
−32.654
92.717
−55.934
1.00
55.95

ATOM
459
CB
LEU

215
−31.605
92.789
−54.854
1.00
57.54

ATOM
460
CG
LEU

215
−31.542
91.471
−54.114
1.00
59.86

ATOM
461
CD1
LEU

215
−31.035
90.396
−55.080
1.00
61.69

ATOM
462
CD2
LEU

215
−30.637
91.617
−52.903
1.00
60.97

ATOM
463
C
LEU

215
−33.936
92.232
−55.304
1.00
57.19

ATOM
464
O
LEU

215
−34.271
92.662
−54.218
1.00
58.06

ATOM
465
N
LYS

216
−34.650
91.341
−55.974
1.00
60.03

ATOM
466
CA
LYS

216
−35.920
90.832
−55.456
1.00
63.02

ATOM
467
CB
LYS

216
−36.669
90.102
−56.577
1.00
63.60

ATOM
468
CG
LYS

216
−38.104
89.755
−56.260
1.00
67.22

ATOM
469
CD
LYS

216
−38.818
90.910
−55.545
1.00
70.35

ATOM
470
CE
LYS

216
−40.336
90.820
−55.730
1.00
72.53

ATOM
471
NZ
LYS

216
−40.855
89.419
−55.593
1.00
75.06

ATOM
472
C
LYS

216
−35.789
89.932
−54.209
1.00
64.87

ATOM
473
O
LYS

216
−36.374
90.244
−53.175
1.00
65.85

ATOM
474
N
TYR

217
−35.041
88.827
−54.303
1.00
66.23

ATOM
475
CA
TYR

217
−34.836
87.915
−53.162
1.00
66.97

ATOM
476
CB
TYR

217
−35.464
86.540
−53.382
1.00
67.30

ATOM
477
CG
TYR

217
−36.864
86.505
−53.916
1.00
70.63

ATOM
478
CD1
TYR

217
−37.221
85.555
−54.871
1.00
71.10

ATOM
479
CE1
TYR

217
−38.507
85.493
−55.377
1.00
73.55

ATOM
480
CD2
TYR

217
−37.839
87.400
−53.469
1.00
71.96

ATOM
481
CE2
TYR

217
−39.142
87.349
−53.972
1.00
73.20

ATOM
482
CZ
TYR

217
−39.464
86.392
−54.931
1.00
74.31

ATOM
483
OH
TYR

217
−40.725
86.350
−55.479
1.00
74.98

ATOM
484
C
TYR

217
−33.356
87.635
−52.974
1.00
67.49

ATOM
485
O
TYR

217
−32.584
87.654
−53.928
1.00
68.35

ATOM
486
N
ALA

218
−32.970
87.332
−51.743
1.00
67.82

ATOM
487
CA
ALA

218
−31.586
86.982
−51.450
1.00
68.73

ATOM
488
CB
ALA

218
−30.854
88.166
−50.830
1.00
68.56

ATOM
489
C
ALA

218
−31.573
85.783
−50.494
1.00
68.25

ATOM
490
O
ALA

218
−32.059
85.874
−49.366
1.00
68.81

ATOM
491
N
PHE

219
−31.043
84.654
−50.954
1.00
67.51

ATOM
492
CA
PHE

219
−30.969
83.470
−50.116
1.00
66.91

ATOM
493
CB
PHE

219
−32.091
82.485
−50.454
1.00
66.69

ATOM
494
CG
PHE

219
−31.932
81.783
−51.783
1.00
66.57

ATOM
495
CD1
PHE

219
−32.509
82.302
−52.936
1.00
66.88

ATOM
496
CD2
PHE

219
−31.254
80.568
−51.870
1.00
67.08

ATOM
497
CE1
PHE

219
−32.422
81.617
−54.161
1.00
67.21

ATOM
498
CE2
PHE

219
−31.162
79.881
−53.084
1.00
66.87

ATOM
499
CZ
PHE

219
−31.752
80.409
−54.233
1.00
66.88

ATOM
500
C
PHE

219
−29.630
82.766
−50.242
1.00
68.12

ATOM
501
O
PHE

219
−28.763
83.176
−51.008
1.00
67.85

ATOM
502
N
GLN

220
−29.462
81.697
−49.480
1.00
69.46

ATOM
503
CA
GLN

220
−28.224
80.944
−49.542
1.00
70.77

ATOM
504
CB
GLN

220
−27.263
81.403
−48.448
1.00
72.88

ATOM
505
CG
GLN

220
−27.842
81.326
−47.058
1.00
76.22

ATOM
506
CD
GLN

220
−26.798
80.964
−46.013
1.00
78.98

ATOM
507
OE1
GLN

220
−25.706
81.555
−45.958
1.00
79.29

ATOM
508
NE2
GLN

220
−27.131
79.989
−45.167
1.00
79.95

ATOM
509
C
GLN

220
−28.425
79.441
−49.419
1.00
69.62

ATOM
510
O
GLN

220
−29.275
78.970
−48.666
1.00
69.23

ATOM
511
N
THR

221
−27.630
78.703
−50.182
1.00
67.81

ATOM
512
CA
THR

221
−27.661
77.263
−50.141
1.00
66.82

ATOM
513
CB
THR

221
−27.335
76.637
−51.513
1.00
66.59

ATOM
514
OG1
THR

221
−26.037
77.065
−51.946
1.00
65.71

ATOM
515
CG2
THR

221
−28.374
77.037
−52.541
1.00
65.82

ATOM
516
C
THR

221
−26.565
76.895
−49.153
1.00
67.45

ATOM
517
O
THR

221
−26.013
77.751
−48.466
1.00
67.42

ATOM
518
N
HIS

222
−26.237
75.618
−49.084
1.00
68.27

ATOM
519
CA
HIS

222
−25.211
75.173
−48.159
1.00
68.63

ATOM
520
CB
HIS

222
−25.294
73.646
−48.033
1.00
67.27

ATOM
521
CG
HIS

222
−24.006
72.994
−47.649
1.00
65.84

ATOM
522
CD2
HIS

222
−23.502
72.654
−46.439
1.00
63.40

ATOM
523
ND1
HIS

222
−23.053
72.637
−48.579
1.00
64.42

ATOM
524
CE1
HIS

222
−22.016
72.103
−47.959
1.00
64.14

ATOM
525
NE2
HIS

222
−22.263
72.102
−46.659
1.00
64.39

ATOM
526
C
HIS

222
−23.792
75.633
−48.536
1.00
68.55

ATOM
527
O
HIS

222
−22.905
75.669
−47.686
1.00
88.63

ATOM
528
N
ASP

223
−23.572
76.008
−49.792
1.00
68.37

ATOM
529
CA
ASP

223
−22.235
76.440
−50.186
1.00
68.77

ATOM
530
CB
ASP

223
−21.414
75.226
−50.629
1.00
70.58

ATOM
531
CG
ASP

223
−21.555
74.931
−52.114
1.00
73.04

ATOM
532
OD1
ASP

223
−22.658
75.130
−52.673
1.00
75.26

ATOM
533
OD2
ASP

223
−20.561
74.490
−52.726
1.00
74.49

ATOM
534
C
ASP

223
−22.213
77.503
−51.289
1.00
67.78

ATOM
535
O
ASP

223
−21.252
77.591
−52.054
1.00
67.27

ATOM
536
N
ARG

224
−23.265
78.308
−51.371
1.00
66.12

ATOM
537
CA
ARG

224
−23.338
79.344
−52.390
1.00
64.62

ATOM
538
CB
ARG

224
−23.817
78.756
−53.727
1.00
64.01

ATOM
539
CG
ARG

224
−22.984
77.588
−54.244
1.00
63.37

ATOM
540
CD
ARG

224
−23.124
77.399
−55.734
1.00
64.16

ATOM
541
NE
ARG

224
−22.335
76.268
−56.207
1.00
65.27

ATOM
542
CZ
ARG

224
−22.020
76.057
−57.482
1.00
68.32

ATOM
543
NH1
ARG

224
−22.421
76.903
−58.425
1.00
68.36

ATOM
544
NH2
ARG

224
−21.301
74.995
−57.823
1.00
69.71

ATOM
545
C
ARG

224
−24.286
80.450
−51.969
1.00
64.24

ATOM
546
O
ARG

224
−25.214
80.227
−51.189
1.00
65.02

ATOM
547
N
LEU

225
−24.043
81.655
−52.472
1.00
63.20

ATOM
548
CA
LEU

225
−24.921
82.779
−52.172
1.00
62.23

ATOM
549
CB
LEU

225
−24.102
84.001
−51.753
1.00
61.58

ATOM
550
CG
LEU

225
−23.503
83.911
−50.345
1.00
62.50

ATOM
551
CD1
LEU

225
−22.685
85.158
−50.037
1.00
59.60

ATOM
552
CD2
LEU

225
−24.630
83.739
−49.329
1.00
60.22

ATOM
553
C
LEU

225
−25.755
83.075
−53.424
1.00
61.43

ATOM
554
O
LEU

225
−25.226
83.122
−54.532
1.00
61.26

ATOM
555
N
CYS

226
−27.060
83.252
−53.246
1.00
60.03

ATOM
556
CA
CYS

226
−27.944
83.522
−54.371
1.00
58.96

ATOM
557
CB
CYS

226
−28.967
82.405
−54.509
1.00
57.08

ATOM
558
SG
CYS

226
−28.212
80.855
−54.887
1.00
58.85

ATOM
559
C
CYS

226
−28.686
84.839
−54.277
1.00
58.68

ATOM
560
O
CYS

226
−29.344
85.120
−53.276
1.00
58.96

ATOM
561
N
PHE

227
−28.586
85.641
−55.332
1.00
58.33

ATOM
562
CA
PHE

227
−29.286
86.920
−55.387
1.00
57.69

ATOM
563
CB
PHE

227
−28.287
88.079
−55.422
1.00
58.43

ATOM
564
CG
PHE

227
−27.312
88.061
−54.284
1.00
58.45

ATOM
565
CD1
PHE

227
−26.098
87.394
−54.406
1.00
58.64

ATOM
566
CD2
PHE

227
−27.633
88.661
−53.071
1.00
57.57

ATOM
567
CE1
PHE

227
−25.218
87.323
−53.335
1.00
59.42

ATOM
568
CE2
PHE

227
−26.765
88.595
−51.992
1.00
58.69

ATOM
569
CZ
PHE

227
−25.554
87.926
−52.120
1.00
59.88

ATOM
570
C
PHE

227
−30.169
86.933
−56.623
1.00
57.25

ATOM
571
O
PHE

227
−29.690
87.051
−57.747
1.00
57.19

ATOM
572
N
VAL

228
−31.467
86.769
−56.413
1.00
57.99

ATOM
573
CA
VAL

228
−32.412
86.756
−57.520
1.00
58.10

ATOM
574
CB
VAL

228
−33.701
86.055
−57.114
1.00
57.27

ATOM
575
CG1
VAL

228
−34.648
85.996
−58.278
1.00
55.74

ATOM
576
CG2
VAL

228
−33.380
84.675
−56.586
1.00
56.18

ATOM
577
C
VAL

228
−32.715
88.198
−57.855
1.00
60.10

ATOM
578
O
VAL

228
−33.132
88.966
−56.990
1.00
60.07

ATOM
579
N
MET

229
−32.503
88.586
−59.105
1.00
61.45

ATOM
580
CA
MET

229
−32.771
89.968
−59.452
1.00
62.54

ATOM
581
CB
MET

229
−31.461
90.721
−59.549
1.00
65.03

ATOM
582
CG
MET

229
−30.643
90.590
−58.306
1.00
67.47

ATOM
583
SD
MET

229
−29.164
91.540
−58.504
1.00
76.13

ATOM
584
CE
MET

229
−28.364
90.629
−59.918
1.00
71.82

ATOM
585
C
MET

229
−33.614
90.215
−60.689
1.00
62.39

ATOM
586
O
MET

229
−33.666
89.405
−61.608
1.00
59.76

ATOM
587
N
GLU

230
−34.295
91.356
−60.672
1.00
64.12

ATOM
588
CA
GLU

230
−35.166
91.784
−61.757
1.00
65.04

ATOM
589
CB
GLU

230
−35.790
93.141
−61.414
1.00
67.87

ATOM
590
CG
GLU

230
−34.762
94.247
−61.183
1.00
70.27

ATOM
591
CD
GLU

230
−35.252
95.636
−61.612
1.00
72.06

ATOM
592
OE1
GLU

230
−35.747
95.779
−62.757
1.00
71.89

ATOM
593
OE2
GLU

230
−35.121
96.590
−60.813
1.00
71.80

ATOM
594
C
GLU

230
−34.408
91.886
−63.083
1.00
64.01

ATOM
595
O
GLU

230
−33.374
92.564
−63.180
1.00
61.86

ATOM
596
N
TYR

231
−34.946
91.214
−64.099
1.00
62.96

ATOM
597
CA
TYR

231
−34.344
91.192
−65.423
1.00
62.88

ATOM
598
CB
TYR

231
−34.292
89.748
−65.939
1.00
64.32

ATOM
599
CG
TYR

231
−33.449
89.561
−67.178
1.00
65.66

ATOM
600
CD1
TYR

231
−32.097
89.907
−67.186
1.00
66.23

ATOM
601
CE1
TYR

231
−31.309
89.729
−68.331
1.00
66.82

ATOM
602
CD2
TYR

231
−33.998
89.033
−68.340
1.00
66.65

ATOM
603
CE2
TYR

231
−33.224
88.850
−69.485
1.00
67.80

ATOM
604
CZ
TYR

231
−31.882
89.201
−69.480
1.00
68.02

ATOM
605
OH
TYR

231
−31.133
89.040
−70.634
1.00
69.12

ATOM
606
C
TYR

231
−35.099
92.070
−66.428
1.00
61.93

ATOM
607
O
TYR

231
−36.259
91.807
−66.768
1.00
61.07

ATOM
608
N
ALA

232
−34.424
93.119
−66.886
1.00
60.67

ATOM
609
CA
ALA

232
−34.978
94.040
−67.868
1.00
59.12

ATOM
610
CB
ALA

232
−34.019
95.188
−68.095
1.00
55.69

ATOM
611
C
ALA

232
−35.137
93.239
−69.142
1.00
59.78

ATOM
612
O
ALA

232
−34.228
92.518
−69.539
1.00
60.55

ATOM
613
N
ASN

233
−36.282
93.351
−69.795
1.00
60.97

ATOM
614
CA
ASN

233
−36.480
92.577
−71.011
1.00
62.16

ATOM
615
CB
ASN

233
−37.747
91.738
−70.891
1.00
62.76

ATOM
616
CG
ASN

233
−38.967
92.585
−70.651
1.00
64.97

ATOM
617
OD1
ASN

233
−39.462
93.241
−71.560
1.00
65.94

ATOM
618
ND2
ASN

233
−39.449
92.595
−69.416
1.00
66.63

ATOM
619
C
ASN

233
−36.516
93.423
−72.276
1.00
61.44

ATOM
620
O
ASN

233
−37.156
93.057
−73.256
1.00
62.23

ATOM
621
N
GLY

234
−35.833
94.559
−72.252
1.00
60.69

ATOM
622
CA
GLY

234
−35.772
95.391
−73.437
1.00
60.43

ATOM
623
C
GLY

234
−34.464
95.150
−74.188
1.00
59.89

ATOM
624
O
GLY

234
−34.115
95.916
−75.087
1.00
60.92

ATOM
625
N
GLY

235
−33.739
94.086
−73.836
1.00
58.89

ATOM
626
CA
GLY

235
−32.479
93.791
−74.499
1.00
57.90

ATOM
627
C
GLY

235
−31.341
94.707
−74.058
1.00
58.49

ATOM
628
O
GLY

235
−31.579
95.820
−73.565
1.00
57.13

ATOM
629
N
GLU

236
−30.097
94.263
−74.246
1.00
57.67

ATOM
630
CA
GLU

236
−28.964
95.069
−73.818
1.00
57.69

ATOM
631
CB
GLU

236
−27.746
94.193
−73.452
1.00
59.66

ATOM
632
CG
GLU

236
−27.375
93.077
−74.411
1.00
63.88

ATOM
633
CD
GLU

236
−28.072
91.754
−74.100
1.00
66.30

ATOM
634
OE1
GLU

236
−29.250
91.600
−74.489
1.00
68.95

ATOM
635
OE2
GLU

236
−27.444
90.872
−73.464
1.00
66.50

ATOM
636
C
GLU

236
−28.561
96.142
−74.803
1.00
55.83

ATOM
637
O
GLU

236
−28.650
95.964
−76.006
1.00
54.26

ATOM
638
N
LEU

237
−28.137
97.276
−74.265
1.00
56.29

ATOM
639
CA
LEU

237
−27.723
98.394
−75.087
1.00
58.37

ATOM
640
CB
LEU

237
−27.106
99.494
−74.235
1.00
58.34

ATOM
641
CG
LEU

237
−28.152
100.550
−73.958
1.00
59.37

ATOM
642
CD1
LEU

237
−27.529
101.709
−73.212
1.00
60.88

ATOM
643
CD2
LEU

237
−28.739
101.003
−75.284
1.00
60.06

ATOM
644
C
LEU

237
−26.744
97.979
−76.157
1.00
58.43

ATOM
645
O
LEU

237
−26.962
98.271
−77.331
1.00
57.83

ATOM
646
N
PHE

238
−25.666
97.309
−75.752
1.00
60.01

ATOM
647
CA
PHE

238
−24.662
96.843
−76.700
1.00
61.53

ATOM
648
CB
PHE

238
−23.785
95.771
−76.066
1.00
65.08

ATOM
649
CG
PHE

238
−23.085
94.932
−77.064
1.00
69.50

ATOM
650
CD1
PHE

238
−22.148
95.501
−77.926
1.00
72.18

ATOM
651
CD2
PHE

238
−23.418
93.592
−77.212
1.00
71.82

ATOM
652
CE1
PHE

238
−21.548
94.754
−78.933
1.00
73.89

ATOM
653
CE2
PHE

238
−22.828
92.821
−78.215
1.00
75.14

ATOM
654
CZ
PHE

238
−21.887
93.406
−79.083
1.00
76.46

ATOM
655
C
PHE

238
−25.337
96.271
−77.957
1.00
60.98

ATOM
656
O
PHE

238
−24.963
96.604
−79.088
1.00
60.58

ATOM
657
N
PHE

239
−26.328
95.408
−77.754
1.00
58.82

ATOM
658
CA
PHE

239
−27.048
94.832
−78.873
1.00
59.06

ATOM
659
CB
PHE

239
−28.184
93.935
−78.357
1.00
61.11

ATOM
660
CG
PHE

239
−29.231
93.605
−79.394
1.00
60.03

ATOM
661
CD1
PHE

239
−29.021
92.591
−80.318
1.00
60.34

ATOM
662
CD2
PHE

239
−30.408
94.349
−79.469
1.00
59.71

ATOM
663
CE1
PHE

239
−29.963
92.324
−81.315
1.00
60.57

ATOM
664
CE2
PHE

239
−31.357
94.095
−80.456
1.00
59.34

ATOM
665
CZ
PHE

239
−31.135
93.079
−81.385
1.00
60.69

ATOM
666
C
PHE

239
−27.613
95.961
−79.749
1.00
59.66

ATOM
667
O
PHE

239
−27.362
95.989
−80.959
1.00
59.72

ATOM
668
N
HIS

240
−28.365
96.882
−79.125
1.00
57.95

ATOM
669
CA
HIS

240
−28.981
98.023
−79.816
1.00
56.69

ATOM
670
CB
HIS

240
−29.832
98.858
−78.851
1.00
56.30

ATOM
671
CG
HIS

240
−31.104
98.192
−78.439
1.00
52.58

ATOM
672
CD2
HIS

240
−31.538
97.772
−77.229
1.00
52.51

ATOM
673
ND1
HIS

240
−32.061
97.801
−79.349
1.00
52.75

ATOM
674
CE1
HIS

240
−33.027
97.155
−78.719
1.00
52.02

ATOM
675
NE2
HIS

240
−32.734
97.123
−77.432
1.00
54.37

ATOM
676
C
HIS

240
−27.977
98.951
−80.489
1.00
56.52

ATOM
677
O
HIS

240
−28.146
99.314
−81.657
1.00
55.95

ATOM
678
N
LEU

241
−26.942
99.346
−79.759
1.00
56.06

ATOM
679
CA
LEU

241
−25.937
100.226
−80.333
1.00
57.24

ATOM
680
CB
LEU

241
−24.851
100.540
−79.315
1.00
54.85

ATOM
681
CG
LEU

241
−23.814
101.485
−79.922
1.00
53.60

ATOM
682
CD1
LEU

241
−24.461
102.838
−80.219
1.00
54.00

ATOM
683
CD2
LEU

241
−22.644
101.641
−78.980
1.00
53.68

ATOM
684
C
LEU

241
−25.276
99.631
−81.587
1.00
60.01

ATOM
685
O
LEU

241
−25.051
100.340
−82.579
1.00
59.83

ATOM
686
N
SER

242
−24.950
98.340
−81.544
1.00
61.36

ATOM
687
CA
SER

242
−24.313
97.705
−82.685
1.00
62.66

ATOM
688
CB
SER

242
−23.945
96.264
−82.350
1.00
63.23

ATOM
689
OG
SER

242
−25.104
95.454
−82.301
1.00
64.02

ATOM
690
C
SER

242
−25.246
97.725
−83.895
1.00
63.78

ATOM
691
O
SER

242
−24.793
97.840
−85.030
1.00
63.77

ATOM
692
N
ARG

243
−26.549
97.613
−83.651
1.00
65.15

ATOM
693
CA
ARG

243
−27.524
97.624
−84.740
1.00
67.42

ATOM
694
CB
ARG

243
−28.920
97.246
−84.225
1.00
68.67

ATOM
695
CG
ARG

243
−29.062
95.800
−83.756
1.00
73.40

ATOM
696
CD
ARG

243
−30.487
95.301
−83.978
1.00
75.73

ATOM
697
NE
ARG

243
−30.846
95.409
−85.392
1.00
80.29

ATOM
698
CZ
ARG

243
−31.959
94.928
−85.944
1.00
81.51

ATOM
699
NH1
ARG

243
−32.857
94.289
−85.201
1.00
83.68

ATOM
700
NH2
ARG

243
−32.169
95.081
−87.249
1.00
79.94

ATOM
701
C
ARG

243
−27.602
98.989
−85.434
1.00
67.41

ATOM
702
O
ARG

243
−27.903
99.091
−86.625
1.00
69.08

ATOM
703
N
GLU

244
−27.321
100.040
−84.683
1.00
66.72

ATOM
704
CA
GLU

244
−27.387
101.379
−85.225
1.00
66.11

ATOM
705
CB
GLU

244
−28.246
102.255
−84.315
1.00
67.57

ATOM
706
CG
GLU

244
−29.719
101.911
−84.408
1.00
70.44

ATOM
707
CD
GLU

244
−30.519
102.489
−83.268
1.00
73.07

ATOM
708
OE1
GLU

244
−30.407
101.962
−82.136
1.00
74.17

ATOM
709
OE2
GLU

244
−31.257
103.472
−83.505
1.00
75.33

ATOM
710
C
GLU

244
−26.036
102.020
−85.428
1.00
64.24

ATOM
711
O
GLU

244
−25.969
103.169
−85.861
1.00
64.90

ATOM
712
N
ARG

245
−24.971
101.280
−85.133
1.00
61.38

ATOM
713
CA
ARG

245
−23.615
101.792
−85.283
1.00
60.26

ATOM
714
CB
ARG

245
−23.356
102.182
−86.744
1.00
60.57

ATOM
715
CG
ARG

245
−22.008
102.841
−86.994
1.00
62.54

ATOM
716
CD
ARG

245
−20.823
101.908
−86.739
1.00
66.16

ATOM
717
NE
ARG

245
−20.294
101.255
−87.946
1.00
69.11

ATOM
718
CZ
ARG

245
−20.907
100.293
−88.643
1.00
70.48

ATOM
719
NH1
ARG

245
−22.106
99.837
−88.276
1.00
72.21

ATOM
720
NH2
ARG

245
−20.310
99.770
−89.711
1.00
70.06

ATOM
721
C
ARG

245
−23.358
102.986
−84.358
1.00
58.76

ATOM
722
O
ARG

245
−22.300
103.074
−83.736
1.00
59.27

ATOM
723
N
VAL

246
−24.327
103.898
−84.273
1.00
56.88

ATOM
724
CA
VAL

246
−24.231
105.079
−83.425
1.00
56.30

ATOM
725
CB
VAL

246
−23.514
106.234
−84.128
1.00
56.75

ATOM
726
CG1
VAL

246
−23.012
107.211
−83.110
1.00
55.87

ATOM
727
CG2
VAL

246
−22.368
105.728
−84.938
1.00
58.09

ATOM
728
C
VAL

246
−25.614
105.591
−83.015
1.00
56.68

ATOM
729
O
VAL

246
−26.624
105.216
−83.599
1.00
56.87

ATOM
730
N
PHE

247
−25.633
106.454
−82.002
1.00
55.57

ATOM
731
CA
PHE

247
−26.849
107.048
−81.462
1.00
54.79

ATOM
732
CB
PHE

247
−26.962
106.771
−79.960
1.00
53.15

ATOM
733
CG
PHE

247
−27.359
105.363
−79.613
1.00
52.02

ATOM
734
CD1
PHE

247
−28.332
104.697
−80.344
1.00
49.77

ATOM
735
CD2
PHE

247
−26.812
104.730
−78.492
1.00
53.62

ATOM
736
CE1
PHE

247
−28.761
103.434
−79.967
1.00
48.10

ATOM
737
CE2
PHE

247
−27.242
103.452
−78.107
1.00
51.99

ATOM
738
CZ
PHE

247
−28.219
102.809
−78.849
1.00
50.19

ATOM
739
C
PHE

247
−26.821
108.565
−81.648
1.00
56.44

ATOM
740
O
PHE

247
−25.744
109.163
−81.763
1.00
55.30

ATOM
741
N
THR

248
−28.000
109.186
−81.645
1.00
56.67

ATOM
742
CA
THR

248
−28.104
110.633
−81.792
1.00
58.42

ATOM
743
CB
THR

248
−29.547
111.063
−81.957
1.00
62.03

ATOM
744
OG1
THR

248
−29.983
110.739
−83.280
1.00
65.64

ATOM
745
CG2
THR

248
−29.701
112.564
−81.699
1.00
64.81

ATOM
746
C
THR

248
−27.595
111.270
−80.535
1.00
57.20

ATOM
747
O
THR

248
−27.885
110.783
−79.457
1.00
58.47

ATOM
748
N
GLU

249
−26.852
112.362
−80.662
1.00
57.14

ATOM
749
CA
GLU

249
−26.322
113.044
−79.489
1.00
58.07

ATOM
750
CB
GLU

249
−25.697
114.371
−79.879
1.00
57.49

ATOM
751
CG
GLU

249
−24.435
114.251
−80.671
1.00
60.71

ATOM
752
CD
GLU

249
−23.588
115.496
−80.526
1.00
62.96

ATOM
753
OE1
GLU

249
−23.859
116.250
−79.575
1.00
64.86

ATOM
754
OE2
GLU

249
−22.656
115.722
−81.333
1.00
64.89

ATOM
755
C
GLU

249
−27.405
113.283
−78.435
1.00
58.76

ATOM
756
O
GLU

249
−27.112
113.574
−77.275
1.00
59.17

ATOM
757
N
GLU

250
−28.659
113.184
−78.848
1.00
58.27

ATOM
758
CA
GLU

250
−29.751
113.358
−77.921
1.00
58.77

ATOM
759
CB
GLU

250
−31.032
113.731
−78.660
1.00
62.56

ATOM
760
CG
GLU

250
−31.430
115.197
−78.537
1.00
62.89

ATOM
761
CD
GLU

250
−31.662
115.600
−77.106
1.00
62.79

ATOM
762
OE1
GLU

250
−30.666
115.956
−76.439
1.00
62.66

ATOM
763
OE2
GLU

250
−32.830
115.534
−76.657
1.00
62.48

ATOM
764
C
GLU

250
−29.924
112.019
−77.238
1.00
58.14

ATOM
765
O
GLU

250
−30.025
111.947
−76.002
1.00
58.42

ATOM
766
N
ARG

251
−29.959
110.963
−78.053
1.00
56.39

ATOM
767
CA
ARG

251
−30.073
109.586
−77.554
1.00
52.97

ATOM
768
CB
ARG

251
−29.866
108.588
−78.692
1.00
52.89

ATOM
769
CG
ARG

251
−31.075
107.734
−79.023
1.00
54.14

ATOM
770
CD
ARG

251
−30.792
106.241
−78.788
1.00
56.02

ATOM
771
NE
ARG

251
−31.509
105.381
−79.727
1.00
55.82

ATOM
772
CZ
ARG

251
−31.772
104.094
−79.528
1.00
56.02

ATOM
773
NH1
ARG

251
−31.386
103.496
−78.418
1.00
56.87

ATOM
774
NH2
ARG

251
−32.420
103.398
−80.445
1.00
59.05

ATOM
775
C
ARG

251
−29.005
109.367
−76.478
1.00
50.39

ATOM
776
O
ARG

251
−29.300
109.000
−75.341
1.00
47.70

ATOM
777
N
ALA

252
−27.755
109.610
−76.828
1.00
49.25

ATOM
778
CA
ALA

252
−26.708
109.436
−75.838
1.00
50.43

ATOM
779
CB
ALA

252
−25.374
109.994
−76.337
1.00
48.80

ATOM
780
C
ALA

252
−27.215
110.236
−74.651
1.00
50.42

ATOM
781
O
ALA

252
−27.503
109.671
−73.603
1.00
51.77

ATOM
782
N
ALA

253
−27.351
111.550
−74.834
1.00
50.34

ATOM
783
CA
ALA

253
−27.850
112.436
−73.783
1.00
47.84

ATOM
784
CB
ALA

253
−28.379
113.721
−74.395
1.00
49.11

ATOM
785
C
ALA

253
−28.946
111.748
−72.958
1.00
45.27

ATOM
786
O
ALA

253
−28.860
111.687
−71.739
1.00
44.68

ATOM
787
N
PHE

254
−29.964
111.211
−73.605
1.00
41.73

ATOM
788
CA
PHE

254
−31.004
110.548
−72.841
1.00
42.16

ATOM
789
CB
PHE

254
−31.966
109.856
−73.777
1.00
45.56

ATOM
790
CG
PHE

254
−33.084
109.171
−73.075
1.00
50.41

ATOM
791
CD1
PHE

254
−34.144
109.908
−72.559
1.00
50.78

ATOM
792
CD2
PHE

254
−33.098
107.783
−72.953
1.00
51.98

ATOM
793
CE1
PHE

254
−35.212
109.281
−71.932
1.00
53.54

ATOM
794
CE2
PHE

254
−34.167
107.137
−72.325
1.00
52.46

ATOM
795
CZ
PHE

254
−35.228
107.890
−71.816
1.00
53.65

ATOM
796
C
PHE

254
−30.448
109.517
−71.830
1.00
41.57

ATOM
797
O
PHE

254
−30.562
109.717
−70.618
1.00
41.69

ATOM
798
N
TYR

255
−29.860
108.420
−72.336
1.00
40.48

ATOM
799
CA
TYR

255
−29.263
107.327
−71.525
1.00
32.92

ATOM
800
CB
TYR

255
−28.545
106.320
−72.423
1.00
31.84

ATOM
801
CG
TYR

255
−29.498
105.630
−73.390
1.00
32.14

ATOM
802
CD1
TYR

255
−30.676
105.070
−72.938
1.00
31.97

ATOM
803
CE1
TYR

255
−31.586
104.494
−73.828
1.00
34.25

ATOM
804
CD2
TYR

255
−29.238
105.592
−74.758
1.00
30.32

ATOM
805
CE2
TYR

255
−30.130
105.029
−75.647
1.00
30.67

ATOM
806
CZ
TYR

255
−31.309
104.484
−75.180
1.00
33.24

ATOM
807
OH
TYR

255
−32.236
103.968
−76.058
1.00
31.95

ATOM
808
C
TYR

255
−28.287
107.870
−70.525
1.00
31.24

ATOM
809
O
TYR

255
−28.308
107.513
−69.350
1.00
31.52

ATOM
810
N
GLY

256
−27.443
108.770
−70.984
1.00
27.74

ATOM
811
CA
GLY

256
−26.474
109.351
−70.098
1.00
29.40

ATOM
812
C
GLY

256
−27.112
109.949
−68.868
1.00
34.13

ATOM
813
O
GLY

256
−26.577
109.746
−67.753
1.00
36.09

ATOM
814
N
ALA

257
−28.241
110.670
−69.048
1.00
33.48

ATOM
815
CA
ALA

257
−28.923
111.323
−67.933
1.00
32.60

ATOM
816
CB
ALA

257
−30.041
112.328
−68.450
1.00
34.66

ATOM
817
C
ALA

257
−29.514
110.319
−66.936
1.00
34.67

ATOM
818
O
ALA

257
−29.375
110.514
−65.726
1.00
32.71

ATOM
819
N
GLU

258
−30.174
109.264
−67.418
1.00
33.09

ATOM
820
CA
GLU

258
−30.703
108.280
−66.487
1.00
37.82

ATOM
821
CB
GLU

258
−31.513
107.204
−67.227
1.00
38.53

ATOM
822
CG
GLU

258
−32.633
107.806
−68.066
1.00
41.10

ATOM
823
CD
GLU

258
−33.728
106.821
−68.411
1.00
44.29

ATOM
824
OE1
GLU

258
−33.406
105.642
−68.711
1.00
43.99

ATOM
825
OE2
GLU

258
−34.916
107.225
−68.391
1.00
41.43

ATOM
826
C
GLU

258
−29.516
107.661
−65.717
1.00
40.77

ATOM
827
O
GLU

258
−29.586
107.446
−64.480
1.00
41.98

ATOM
828
N
ILE

259
−28.410
107.427
−66.427
1.00
39.37

ATOM
829
CA
ILE

259
−27.246
106.862
−65.769
1.00
41.44

ATOM
830
CB
ILE

259
−26.061
106.538
−66.743
1.00
40.57

ATOM
831
CG2
ILE

259
−24.909
105.968
−65.969
1.00
37.79

ATOM
832
CG1
ILE

259
−26.493
105.531
−67.800
1.00
40.69

ATOM
833
CD1
ILE

259
−25.437
105.291
−68.852
1.00
45.72

ATOM
834
C
ILE

259
−26.754
107.871
−64.753
1.00
41.09

ATOM
835
O
ILE

259
−26.461
107.494
−63.614
1.00
42.53

ATOM
836
N
VAL

260
−26.656
109.144
−65.164
1.00
40.14

ATOM
837
CA
VAL

260
−26.176
110.200
−64.254
1.00
38.43

ATOM
838
CB
VAL

260
−26.066
111.595
−64.954
1.00
37.91

ATOM
839
CG1
VAL

260
−25.551
112.633
−63.980
1.00
34.74

ATOM
840
CG2
VAL

260
−25.111
111.532
−66.149
1.00
34.85

ATOM
841
C
VAL

260
−27.100
110.305
−63.039
1.00
38.63

ATOM
842
O
VAL

260
−26.676
110.673
−61.949
1.00
36.65

ATOM
843
N
SER

261
−28.366
109.948
−63.226
1.00
40.78

ATOM
844
CA
SER

261
−29.316
109.992
−62.128
1.00
42.94

ATOM
845
CB
SER

261
−30.750
109.902
−62.652
1.00
41.46

ATOM
846
OG
SER

261
−31.672
109.806
−61.591
1.00
38.11

ATOM
847
C
SER

261
−29.023
108.826
−61.183
1.00
43.11

ATOM
848
O
SER

261
−29.071
108.965
−59.963
1.00
43.59

ATOM
849
N
ALA

262
−28.705
107.676
−61.764
1.00
45.11

ATOM
850
CA
ALA

262
−28.395
106.486
−60.971
1.00
42.89

ATOM
851
CB
ALA

262
−28.224
105.289
−61.880
1.00
42.22

ATOM
852
C
ALA

262
−27.152
106.697
−60.117
1.00
42.66

ATOM
853
O
ALA

262
−27.131
106.329
−58.940
1.00
45.22

ATOM
854
N
LEU

263
−26.129
107.317
−60.680
1.00
41.70

ATOM
855
CA
LEU

263
−24.910
107.534
−59.919
1.00
42.13

ATOM
856
CB
LEU

263
−23.708
107.744
−60.833
1.00
40.05

ATOM
857
CG
LEU

263
−23.493
106.752
−61.964
1.00
41.42

ATOM
858
CD1
LEU

263
−22.215
107.141
−62.723
1.00
39.22

ATOM
859
CD2
LEU

263
−23.411
105.349
−61.393
1.00
40.79

ATOM
860
C
LEU

263
−24.969
108.689
−58.943
1.00
43.19

ATOM
861
O
LEU

263
−24.247
108.669
−57.954
1.00
45.28

ATOM
862
N
GLU

264
−25.768
109.721
−59.212
1.00
44.12

ATOM
863
CA
GLU

264
−25.852
110.821
−58.239
1.00
44.00

ATOM
864
CB
GLU

264
−26.829
111.903
−58.680
1.00
45.06

ATOM
865
CG
GLU

264
−26.912
113.061
−57.671
1.00
51.94

ATOM
866
CD
GLU

264
−28.131
113.968
−57.861
1.00
53.09

ATOM
867
OE1
GLU

264
−29.238
113.454
−58.170
1.00
52.09

ATOM
868
OE2
GLU

264
−27.982
115.195
−57.672
1.00
53.73

ATOM
869
C
GLU

264
−26.382
110.190
−56.953
1.00
42.94

ATOM
870
O
GLU

264
−25.895
110.474
−55.848
1.00
39.40

ATOM
871
N
TYR

265
−27.372
109.307
−57.136
1.00
43.31

ATOM
872
CA
TYR

265
−28.005
108.608
−56.041
1.00
43.11

ATOM
873
CB
TYR

265
−29.120
107.687
−56.543
1.00
47.99

ATOM
874
CG
TYR

265
−30.016
107.222
−55.405
1.00
55.41

ATOM
875
CD1
TYR

265
−30.944
108.110
−54.826
1.00
58.93

ATOM
876
CE1
TYR

265
−31.756
107.729
−53.757
1.00
59.78

ATOM
877
CD2
TYR

265
−29.925
105.928
−54.878
1.00
56.06

ATOM
878
CE2
TYR

265
−30.736
105.527
−53.803
1.00
59.29

ATOM
879
CZ
TYR

265
−31.655
106.441
−53.246
1.00
61.52

ATOM
880
OH
TYR

265
−32.488
106.103
−52.187
1.00
60.96

ATOM
881
C
TYR

265
−27.009
107.763
−55.254
1.00
41.53

ATOM
882
O
TYR

265
−26.976
107.846
−54.015
1.00
37.07

ATOM
883
N
LEU

266
−26.224
106.951
−55.986
1.00
40.89

ATOM
884
CA
LEU

266
−25.225
106.047
−55.395
1.00
38.93

ATOM
885
CB
LEU

266
−24.625
105.101
−56.444
1.00
37.40

ATOM
886
CG
LEU

266
−25.576
103.988
−56.927
1.00
36.00

ATOM
887
CD1
LEU

266
−25.211
103.561
−58.332
1.00
36.05

ATOM
888
CD2
LEU

266
−25.551
102.810
−55.979
1.00
34.11

ATOM
889
C
LEU

266
−24.129
106.786
−54.685
1.00
37.15

ATOM
890
O
LEU

266
−23.849
106.508
−53.550
1.00
35.44

ATOM
891
N
HIS

267
−23.523
107.751
−55.344
1.00
38.59

ATOM
892
CA
HIS

267
−22.468
108.502
−54.713
1.00
40.15

ATOM
893
CB
HIS

267
−21.913
109.539
−55.671
1.00
41.44

ATOM
894
CG
HIS

267
−21.177
108.961
−56.835
1.00
42.88

ATOM
895
CD2
HIS

267
−21.001
107.683
−57.234
1.00
42.55

ATOM
896
ND1
HIS

267
−20.524
109.745
−57.759
1.00
41.97

ATOM
897
CE1
HIS

267
−19.978
108.973
−58.680
1.00
43.09

ATOM
898
NE2
HIS

267
−20.253
107.717
−58.384
1.00
43.80

ATOM
899
C
HIS

267
−22.974
109.212
−53.478
1.00
43.29

ATOM
900
O
HIS

267
−22.187
109.612
−52.628
1.00
42.37

ATOM
901
N
SER

268
−24.287
109.406
−53.384
1.00
47.54

ATOM
902
CA
SER

268
−24.829
110.110
−52.232
1.00
51.53

ATOM
903
CB
SER

268
−26.224
110.671
−52.527
1.00
52.10

ATOM
904
OG
SER

268
−27.199
109.637
−52.556
1.00
59.22

ATOM
905
C
SER

268
−24.871
109.149
−51.062
1.00
51.38

ATOM
906
O
SER

268
−24.747
109.553
−49.916
1.00
52.88

ATOM
907
N
ARG

269
−25.056
107.875
−51.355
1.00
51.82

ATOM
908
CA
ARG

269
−25.060
106.869
−50.312
1.00
53.73

ATOM
909
CB
ARG

269
−25.949
105.693
−50.712
1.00
57.67

ATOM
910
CG
ARG

269
−27.399
106.037
−50.921
1.00
63.45

ATOM
911
CD
ARG

269
−28.018
106.576
−49.645
1.00
68.29

ATOM
912
NE
ARG

269
−29.466
106.764
−49.759
1.00
73.68

ATOM
913
CZ
ARG

269
−30.064
107.657
−50.552
1.00
75.36

ATOM
914
NH1
ARG

269
−29.349
108.472
−51.326
1.00
77.14

ATOM
915
NH2
ARG

269
−31.389
107.741
−50.569
1.00
75.25

ATOM
916
C
ARG

269
−23.613
106.382
−50.143
1.00
53.04

ATOM
917
O
ARG

269
−23.389
105.247
−49.745
1.00
51.54

ATOM
918
N
ASP

270
−22.646
107.236
−50.487
1.00
52.95

ATOM
919
CA
ASP

270
−21.218
106.921
−50.381
1.00
53.19

ATOM
920
CB
ASP

270
−20.827
106.915
−48.894
1.00
56.60

ATOM
921
CG
ASP

270
−19.328
107.150
−48.655
1.00
61.82

ATOM
922
OD1
ASP

270
−18.507
106.243
−48.926
1.00
65.60

ATOM
923
OD2
ASP

270
−18.965
108.250
−48.185
1.00
62.55

ATOM
924
C
ASP

270
−20.845
105.572
−51.051
1.00
52.23

ATOM
925
O
ASP

270
−19.967
104.857
−50.579
1.00
53.37

ATOM
926
N
VAL

271
−21.500
105.246
−52.164
1.00
48.97

ATOM
927
CA
VAL

271
−21.282
103.999
−52.896
1.00
46.17

ATOM
928
CB
VAL

271
−22.597
103.308
−53.150
1.00
45.22

ATOM
929
CG1
VAL

271
−22.411
102.187
−54.152
1.00
46.54

ATOM
930
CG2
VAL

271
−23.158
102.816
−51.868
1.00
46.65

ATOM
931
C
VAL

271
−20.655
104.189
−54.268
1.00
46.38

ATOM
932
O
VAL

271
−21.259
104.830
−55.118
1.00
47.00

ATOM
933
N
VAL

272
−19.475
103.613
−54.504
1.00
46.10

ATOM
934
CA
VAL

272
−18.802
103.732
−55.812
1.00
43.83

ATOM
935
CB
VAL

272
−17.265
103.711
−55.695
1.00
43.04

ATOM
936
CG1
VAL

272
−16.650
103.699
−57.095
1.00
42.62

ATOM
937
CG2
VAL

272
−16.779
104.907
−54.920
1.00
40.14

ATOM
938
C
VAL

272
−19.195
102.568
−56.701
1.00
42.40

ATOM
939
O
VAL

272
−18.938
101.421
−56.376
1.00
43.41

ATOM
940
N
TYR

273
−19.790
102.842
−57.844
1.00
40.51

ATOM
941
CA
TYR

273
−20.202
101.732
−58.678
1.00
37.57

ATOM
942
CB
TYR

273
−21.125
102.229
−59.766
1.00
32.36

ATOM
943
CG
TYR

273
−22.007
101.116
−60.224
1.00
28.72

ATOM
944
CD1
TYR

273
−22.905
100.536
−59.354
1.00
28.66

ATOM
945
CE1
TYR

273
−23.703
99.472
−59.756
1.00
29.61

ATOM
946
CD2
TYR

273
−21.917
100.613
−61.511
1.00
27.83

ATOM
947
CE2
TYR

273
−22.714
99.550
−61.923
1.00
29.06

ATOM
948
CZ
TYR

273
−23.608
98.988
−61.035
1.00
27.75

ATOM
949
OH
TYR

273
−24.438
97.962
−61.443
1.00
31.99

ATOM
950
C
TYR

273
−19.148
100.794
−59.311
1.00
36.59

ATOM
951
O
TYR

273
−19.391
99.593
−59.426
1.00
34.01

ATOM
952
N
ARG

274
−18.032
101.347
−59.771
1.00
37.36

ATOM
953
CA
ARG

274
−16.952
100.573
−60.400
1.00
41.86

ATOM
954
CB
ARG

274
−16.509
99.420
−59.490
1.00
42.11

ATOM
955
CG
ARG

274
−15.915
99.829
−58.157
1.00
44.64

ATOM
956
CD
ARG

274
−15.293
98.607
−57.485
1.00
47.09

ATOM
957
NE
ARG

274
−14.693
98.910
−56.188
1.00
48.75

ATOM
958
CZ
ARG

274
−13.499
98.474
−55.796
1.00
47.29

ATOM
959
NH1
ARG

274
−12.765
97.716
−56.608
1.00
48.77

ATOM
960
NH2
ARG

274
−13.048
98.780
−54.588
1.00
45.02

ATOM
961
C
ARG

274
−17.244
99.968
−61.769
1.00
43.19

ATOM
962
O
ARG

274
−16.346
99.832
−62.604
1.00
44.18

ATOM
963
N
ASP

275
−18.498
99.594
−61.993
1.00
45.10

ATOM
964
CA
ASP

275
−18.877
98.934
−63.231
1.00
43.85

ATOM
965
CB
ASP

275
−19.548
97.603
−62.910
1.00
48.48

ATOM
966
CG
ASP

275
−18.578
96.578
−62.322
1.00
54.54

ATOM
967
OD1
ASP

275
−17.969
96.835
−61.252
1.00
53.37

ATOM
968
OD2
ASP

275
−18.433
95.493
−62.939
1.00
60.03

ATOM
969
C
ASP

275
−19.752
99.681
−64.219
1.00
41.01

ATOM
970
O
ASP

275
−20.620
99.074
−64.844
1.00
40.47

ATOM
971
N
ILE

276
−19.563
100.982
−64.381
1.00
37.54

ATOM
972
CA
ILE

276
−20.376
101.616
−65.392
1.00
35.19

ATOM
973
CB
ILE

276
−20.452
103.147
−65.234
1.00
36.23

ATOM
974
CG2
ILE

276
−21.139
103.741
−66.479
1.00
31.78

ATOM
975
CG1
ILE

276
−21.172
103.516
−63.920
1.00
32.64

ATOM
976
CD1
ILE

276
−22.513
102.917
−63.772
1.00
28.27

ATOM
977
C
ILE

276
−19.757
101.302
−66.764
1.00
34.89

ATOM
978
O
ILE

276
−18.703
101.837
−67.122
1.00
33.85

ATOM
979
N
LYS

277
−20.405
100.442
−67.538
1.00
33.22

ATOM
980
CA
LYS

277
−19.865
100.132
−68.833
1.00
37.67

ATOM
981
CB
LYS

277
−18.602
99.230
−68.694
1.00
40.12

ATOM
982
CG
LYS

277
−18.758
97.959
−67.894
1.00
40.43

ATOM
983
CD
LYS

277
−17.397
97.537
−67.358
1.00
49.81

ATOM
984
CE
LYS

277
−17.280
96.033
−67.084
1.00
49.65

ATOM
985
NZ
LYS

277
−17.231
95.212
−68.335
1.00
50.73

ATOM
986
C
LYS

277
−20.945
99.493
−69.652
1.00
37.96

ATOM
987
O
LYS

277
−21.787
98.779
−69.120
1.00
38.70

ATOM
988
N
LEU

278
−20.892
99.745
−70.956
1.00
41.01

ATOM
989
CA
LEU

278
−21.901
99.300
−71.921
1.00
43.27

ATOM
990
CB
LEU

278
−21.344
99.464
−73.341
1.00
45.84

ATOM
991
CG
LEU

278
−22.252
99.148
−74.535
1.00
47.04

ATOM
992
CD1
LEU

278
−23.423
100.103
−74.582
1.00
47.73

ATOM
993
CD2
LEU

278
−21.430
99.245
−75.820
1.00
49.67

ATOM
994
C
LEU

278
−22.514
97.915
−71.765
1.00
44.93

ATOM
995
O
LEU

278
−23.717
97.712
−72.009
1.00
43.40

ATOM
996
N
GLU

279
−21.684
96.953
−71.382
1.00
46.75

ATOM
997
CA
GLU

279
−22.139
95.576
−71.210
1.00
46.80

ATOM
998
CB
GLU

279
−20.931
94.662
−70.943
1.00
51.26

ATOM
999
CG
GLU

279
−19.682
94.964
−71.808
1.00
54.97

ATOM
1000
CD
GLU

279
−19.043
96.309
−71.458
1.00
60.05

ATOM
1001
OE1
GLU

279
−19.369
96.848
−70.374
1.00
61.29

ATOM
1002
OE2
GLU

279
−18.214
96.826
−72.250
1.00
63.32

ATOM
1003
C
GLU

279
−23.131
95.509
−70.056
1.00
44.42

ATOM
1004
O
GLU

279
−24.081
94.751
−70.100
1.00
44.41

ATOM
1005
N
ASN

280
−22.906
96.318
−69.027
1.00
42.54

ATOM
1006
CA
ASN

280
−23.795
96.357
−67.878
1.00
43.63

ATOM
1007
CB
ASN

280
−23.067
96.910
−66.635
1.00
44.99

ATOM
1008
CG
ASN

280
−21.964
96.003
−66.130
1.00
47.56

ATOM
1009
OD1
ASN

280
−21.175
95.489
−66.896
1.00
52.55

ATOM
1010
ND2
ASN

280
−21.889
95.833
−64.829
1.00
48.82

ATOM
1011
C
ASN

280
−25.007
97.272
−68.142
1.00
43.42

ATOM
1012
O
ASN

280
−25.556
97.807
−67.194
1.00
44.40

ATOM
1013
N
LEU

281
−25.414
97.487
−69.390
1.00
42.51

ATOM
1014
CA
LEU

281
−26.565
98.375
−69.637
1.00
42.52

ATOM
1015
CB
LEU

281
−26.170
99.688
−70.343
1.00
38.94

ATOM
1016
CG
LEU

281
−25.149
100.642
−69.685
1.00
40.96

ATOM
1017
CD1
LEU

281
−24.893
101.863
−70.562
1.00
36.16

ATOM
1018
CD2
LEU

281
−25.652
101.071
−68.330
1.00
39.50

ATOM
1019
C
LEU

281
−27.634
97.710
−70.465
1.00
43.42

ATOM
1020
O
LEU

281
−27.381
97.229
−71.563
1.00
43.54

ATOM
1021
N
MET

282
−28.837
97.666
−69.924
1.00
44.23

ATOM
1022
CA
MET

282
−29.945
97.091
−70.655
1.00
48.65

ATOM
1023
CB
MET

282
−30.410
95.828
−69.966
1.00
48.44

ATOM
1024
CG
MET

282
−29.524
94.663
−70.284
1.00
49.57

ATOM
1025
SD
MET

282
−30.209
93.186
−69.538
1.00
49.53

ATOM
1026
CE
MET

282
−29.278
93.263
−68.055
1.00
50.05

ATOM
1027
C
MET

282
−31.086
98.112
−70.770
1.00
49.94

ATOM
1028
O
MET

282
−30.938
99.274
−70.362
1.00
50.74

ATOM
1029
N
LEU

283
−32.202
97.686
−71.344
1.00
48.61

ATOM
1030
CA
LEU

283
−33.344
98.564
−71.500
1.00
48.61

ATOM
1031
CB
LEU

283
−33.541
98.923
−72.979
1.00
45.53

ATOM
1032
CG
LEU

283
−32.426
99.762
−73.629
1.00
46.07

ATOM
1033
CD1
LEU

283
−32.831
100.189
−75.043
1.00
46.26

ATOM
1034
CD2
LEU

283
−32.158
101.005
−72.796
1.00
46.21

ATOM
1035
C
LEU

283
−34.554
97.828
−70.964
1.00
50.44

ATOM
1036
O
LEU

283
−34.693
96.632
−71.194
1.00
49.45

ATOM
1037
N
ASP

284
−35.417
98.511
−70.216
1.00
53.04

ATOM
1038
CA
ASP

284
−36.606
97.829
−69.716
1.00
56.45

ATOM
1039
CB
ASP

284
−37.127
98.448
−68.398
1.00
56.47

ATOM
1040
CG
ASP

284
−37.609
99.892
−68.548
1.00
56.20

ATOM
1041
OD1
ASP

284
−38.024
100.291
−69.657
1.00
55.37

ATOM
1042
OD2
ASP

284
−37.593
100.623
−67.530
1.00
56.55

ATOM
1043
C
ASP

284
−37.677
97.878
−70.809
1.00
57.77

ATOM
1044
O
ASP

284
−37.495
98.527
−71.832
1.00
56.14

ATOM
1045
N
LYS

285
−38.785
97.185
−70.589
1.00
60.53

ATOM
1046
CA
LYS

285
−39.870
97.136
−71.562
1.00
62.34

ATOM
1047
CB
LYS

285
−41.027
96.323
−70.983
1.00
64.39

ATOM
1048
CG
LYS

285
−41.474
96.804
−69.621
1.00
67.74

ATOM
1049
CD
LYS

285
−42.522
95.868
−69.033
1.00
69.58

ATOM
1050
CE
LYS

285
−42.837
96.237
−67.587
1.00
71.14

ATOM
1051
NZ
LYS

285
−41.661
96.089
−66.665
1.00
71.01

ATOM
1052
C
LYS

285
−40.399
98.477
−72.085
1.00
61.37

ATOM
1053
O
LYS

285
−41.191
98.489
−73.018
1.00
62.10

ATOM
1054
N
ASP

286
−39.972
99.594
−71.504
1.00
59.71

ATOM
1055
CA
ASP

286
−40.450
100.902
−71.955
1.00
58.63

ATOM
1056
CB
ASP

286
−41.104
101.685
−70.796
1.00
55.55

ATOM
1057
CG
ASP

286
−42.263
100.924
−70.147
1.00
54.69

ATOM
1058
OD1
ASP

286
−43.056
100.323
−70.906
1.00
53.87

ATOM
1059
OD2
ASP

286
−42.386
100.927
−68.892
1.00
52.13

ATOM
1060
C
ASP

286
−39.318
101.725
−72.550
1.00
58.98

ATOM
1061
O
ASP

286
−39.468
102.922
−72.818
1.00
59.33

ATOM
1062
N
GLY

287
−38.177
101.082
−72.749
1.00
58.42

ATOM
1063
CA
GLY

287
−37.045
101.776
−73.321
1.00
55.33

ATOM
1064
C
GLY

287
−36.218
102.535
−72.313
1.00
55.12

ATOM
1065
O
GLY

287
−35.337
103.302
−72.706
1.00
55.89

ATOM
1066
N
HIS

288
−36.503
102.364
−71.021
1.00
53.99

ATOM
1067
CA
HIS

288
−35.700
103.031
−69.985
1.00
52.87

ATOM
1068
CB
HIS

288
−36.535
103.298
−68.735
1.00
54.12

ATOM
1069
CG
HIS

288
−37.412
104.500
−68.849
1.00
54.36

ATOM
1070
CD2
HIS

288
−38.754
104.620
−68.949
1.00
54.12

ATOM
1071
ND1
HIS

288
−36.906
105.783
−68.882
1.00
54.49

ATOM
1072
CE1
HIS

288
−37.904
106.642
−68.993
1.00
55.05

ATOM
1073
NE2
HIS

288
−39.037
105.962
−69.035
1.00
54.04

ATOM
1074
C
HIS

288
−34.468
102.199
−69.620
1.00
50.81

ATOM
1075
O
HIS

288
−34.501
100.967
−69.649
1.00
49.80

ATOM
1076
N
ILE

289
−33.388
102.882
−69.270
1.00
48.66

ATOM
1077
CA
ILE

289
−32.133
102.231
−68.928
1.00
45.41

ATOM
1078
CB
ILE

289
−31.022
103.293
−68.889
1.00
46.00

ATOM
1079
CG2
ILE

289
−30.430
103.389
−67.495
1.00
46.37

ATOM
1080
CG1
ILE

289
−29.994
103.011
−69.984
1.00
47.38

ATOM
1081
CD1
ILE

289
−28.768
103.925
−69.940
1.00
48.92

ATOM
1082
C
ILE

289
−32.132
101.434
−67.604
1.00
45.12

ATOM
1083
O
ILE

289
−32.836
101.778
−66.648
1.00
44.61

ATOM
1084
N
LYS

290
−31.341
100.359
−67.564
1.00
42.74

ATOM
1085
CA
LYS

290
−31.213
99.537
−66.361
1.00
40.63

ATOM
1086
CB
LYS

290
−32.108
98.286
−66.403
1.00
38.79

ATOM
1087
CG
LYS

290
−33.506
98.445
−65.867
1.00
40.40

ATOM
1088
CD
LYS

290
−33.569
98.783
−64.376
1.00
40.88

ATOM
1089
CE
LYS

290
−35.040
98.949
−63.917
1.00
41.34

ATOM
1090
NZ
LYS

290
−35.202
99.399
−62.491
1.00
41.88

ATOM
1091
C
LYS

290
−29.780
99.076
−66.203
1.00
40.58

ATOM
1092
O
LYS

290
−29.315
98.213
−66.959
1.00
38.39

ATOM
1093
N
ILE

291
−29.095
99.659
−65.221
1.00
40.94

ATOM
1094
CA
ILE

291
−27.726
99.314
−64.899
1.00
42.72

ATOM
1095
CB
ILE

291
−27.135
100.321
−63.935
1.00
41.62

ATOM
1096
CG2
ILE

291
−25.725
99.908
−63.581
1.00
43.00

ATOM
1097
CG1
ILE

291
−27.179
101.715
−64.579
1.00
44.50

ATOM
1098
CD1
ILE

291
−26.529
102.835
−63.793
1.00
39.86

ATOM
1099
C
ILE

291
−27.760
97.937
−64.242
1.00
42.95

ATOM
1100
O
ILE

291
−28.153
97.791
−63.099
1.00
42.12

ATOM
1101
N
THR

292
−27.355
96.933
−65.001
1.00
46.30

ATOM
1102
CA
THR

292
−27.341
95.543
−64.579
1.00
50.75

ATOM
1103
CB
THR

292
−27.473
94.688
−65.814
1.00
49.64

ATOM
1104
OG1
THR

292
−28.211
93.514
−65.489
1.00
50.14

ATOM
1105
CG2
THR

292
−26.108
94.330
−66.360
1.00
50.90

ATOM
1106
C
THR

292
−26.045
95.219
−63.844
1.00
53.08

ATOM
1107
O
THR

292
−25.023
95.744
−64.205
1.00
54.20

ATOM
1108
N
ASP

293
−26.065
94.357
−62.832
1.00
58.90

ATOM
1109
CA
ASP

293
−24.821
94.066
−62.078
1.00
65.40

ATOM
1110
CB
ASP

293
−25.132
93.760
−60.602
1.00
68.31

ATOM
1111
CG
ASP

293
−23.910
93.957
−59.688
1.00
71.75

ATOM
1112
OD1
ASP

293
−22.797
93.515
−60.066
1.00
72.43

ATOM
1113
OD2
ASP

293
−24.066
94.558
−58.588
1.00
72.94

ATOM
1114
C
ASP

293
−23.898
92.954
−62.585
1.00
66.34

ATOM
1115
O
ASP

293
−23.428
92.142
−61.795
1.00
67.07

ATOM
1116
N
PHE

294
−23.619
92.922
−63.881
1.00
68.29

ATOM
1117
CA
PHE

294
−22.743
91.888
−64.429
1.00
71.15

ATOM
1118
CB
PHE

294
−23.363
90.512
−64.170
1.00
70.29

ATOM
1119
CG
PHE

294
−24.852
90.465
−64.391
1.00
68.39

ATOM
1120
CD1
PHE

294
−25.374
90.204
−65.653
1.00
67.64

ATOM
1121
CD2
PHE

294
−25.733
90.702
−63.334
1.00
67.17

ATOM
1122
CE1
PHE

294
−26.752
90.171
−65.864
1.00
67.40

ATOM
1123
CE2
PHE

294
−27.112
90.672
−63.527
1.00
67.56

ATOM
1124
CZ
PHE

294
−27.624
90.405
−64.801
1.00
67.17

ATOM
1125
C
PHE

294
−22.446
92.054
−65.921
1.00
74.06

ATOM
1126
O
PHE

294
−23.146
92.787
−66.637
1.00
74.81

ATOM
1127
N
GLY

295
−21.405
91.370
−66.387
1.00
75.03

ATOM
1128
CA
GLY

295
−21.057
91.448
−67.794
1.00
77.37

ATOM
1129
C
GLY

295
−21.847
90.436
−68.605
1.00
78.99

ATOM
1130
O
GLY

295
−21.644
89.232
−68.449
1.00
77.61

ATOM
1131
N
ALA

296
−22.744
90.923
−69.468
1.00
81.84

ATOM
1132
CA
ALA

296
−23.589
90.056
−70.301
1.00
83.30

ATOM
1133
CB
ALA

296
−24.207
90.857
−71.446
1.00
82.28

ATOM
1134
C
ALA

296
−22.814
88.866
−70.859
1.00
84.74

ATOM
1135
O
ALA

296
−22.495
87.925
−70.129
1.00
85.55

ATOM
1136
N
THR

313
−14.714
92.203
−75.369
1.00
60.91

ATOM
1137
CA
THR

313
−14.670
93.623
−75.035
1.00
60.64

ATOM
1138
CB
THR

313
−15.922
94.044
−74.210
1.00
63.10

ATOM
1139
OG1
THR

313
−16.167
93.077
−73.179
1.00
64.44

ATOM
1140
CG2
THR

313
−17.153
94.165
−75.111
1.00
65.78

ATOM
1141
C
THR

313
−13.420
94.061
−74.252
1.00
58.49

ATOM
1142
O
THR

313
−13.128
93.540
−73.176
1.00
57.70

ATOM
1143
N
PRO

314
−12.661
95.022
−74.803
1.00
55.65

ATOM
1144
CD
PRO

314
−12.751
95.465
−76.206
1.00
54.61

ATOM
1145
CA
PRO

314
−11.447
95.537
−74.149
1.00
55.15

ATOM
1146
CB
PRO

314
−10.831
96.445
−75.212
1.00
53.14

ATOM
1147
CG
PRO

314
−11.326
95.856
−76.510
1.00
55.07

ATOM
1148
C
PRO

314
−11.816
96.331
−72.891
1.00
55.44

ATOM
1149
O
PRO

314
−12.652
97.240
−72.954
1.00
58.62

ATOM
1150
N
GLU

315
−11.217
95.992
−71.752
1.00
54.65

ATOM
1151
CA
GLU

315
−11.486
96.709
−70.498
1.00
52.63

ATOM
1152
CB
GLU

315
−10.772
96.041
−69.326
1.00
55.03

ATOM
1153
CG
GLU

315
−11.462
94.835
−68.718
1.00
59.66

ATOM
1154
CD
GLU

315
−11.720
95.019
−67.225
1.00
61.87

ATOM
1155
OE1
GLU

315
−12.813
95.521
−66.858
1.00
64.01

ATOM
1156
OE2
GLU

315
−10.821
94.681
−66.422
1.00
62.85

ATOM
1157
C
GLU

315
−10.973
98.141
−70.578
1.00
51.76

ATOM
1158
O
GLU

315
−9.901
98.381
−71.126
1.00
50.53

ATOM
1159
N
TYR

316
−11.723
99.099
−70.037
1.00
49.20

ATOM
1160
CA
TYR

316
−11.262
100.487
−70.037
1.00
45.83

ATOM
1161
CB
TYR

316
−12.120
101.355
−70.954
1.00
45.08

ATOM
1162
CG
TYR

316
−11.603
101.488
−72.365
1.00
43.63

ATOM
1163
CD1
TYR

316
−11.992
100.596
−73.353
1.00
42.33

ATOM
1164
CE1
TYR

316
−11.590
100.765
−74.671
1.00
42.22

ATOM
1165
CD2
TYR

316
−10.773
102.563
−72.731
1.00
43.91

ATOM
1166
CE2
TYR

316
−10.363
102.743
−74.056
1.00
40.77

ATOM
1167
CZ
TYR

316
−10.782
101.837
−75.014
1.00
41.68

ATOM
1168
OH
TYR

316
−10.400
101.988
−76.327
1.00
44.89

ATOM
1169
C
TYR

316
−11.312
101.038
−68.614
1.00
46.24

ATOM
1170
O
TYR

316
−12.122
101.930
−68.287
1.00
46.53

ATOM
1171
N
LEU

317
−10.472
100.468
−67.759
1.00
43.22

ATOM
1172
CA
LEU

317
−10.397
100.902
−66.377
1.00
41.82

ATOM
1173
CB
LEU

317
−9.395
100.053
−65.582
1.00
38.88

ATOM
1174
CG
LEU

317
−9.778
98.578
−65.467
1.00
39.79

ATOM
1175
CD1
LEU

317
−8.704
97.838
−64.631
1.00
35.92

ATOM
1176
CD2
LEU

317
−11.196
98.444
−64.855
1.00
33.82

ATOM
1177
C
LEU

317
−9.955
102.349
−66.354
1.00
41.08

ATOM
1178
O
LEU

317
−9.159
102.777
−67.188
1.00
40.65

ATOM
1179
N
ALA

318
−10.470
103.098
−65.393
1.00
40.28

ATOM
1180
CA
ALA

318
−10.109
104.494
−65.280
1.00
40.73

ATOM
1181
CB
ALA

318
−10.853
105.129
−64.092
1.00
38.50

ATOM
1182
C
ALA

318
−8.604
104.570
−65.061
1.00
39.60

ATOM
1183
O
ALA

318
−8.029
103.712
−64.432
1.00
40.78

ATOM
1184
N
PRO

319
−7.950
105.604
−65.582
1.00
39.37

ATOM
1185
CD
PRO

319
−8.415
106.643
−66.505
1.00
39.04

ATOM
1186
CA
PRO

319
−6.511
105.711
−65.377
1.00
39.03

ATOM
1187
CB
PRO

319
−6.155
107.065
−66.012
1.00
39.95

ATOM
1188
CG
PRO

319
−7.466
107.750
−66.171
1.00
42.09

ATOM
1189
C
PRO

319
−6.068
105.611
−63.928
1.00
39.88

ATOM
1190
O
PRO

319
−5.090
104.906
−63.616
1.00
41.07

ATOM
1191
N
GLU

320
−6.766
106.288
−63.020
1.00
41.42

ATOM
1192
CA
GLU

320
−6.338
106.211
−61.616
1.00
42.37

ATOM
1193
CB
GLU

320
−7.040
107.272
−60.729
1.00
43.77

ATOM
1194
CG
GLU

320
−8.528
107.061
−60.511
1.00
44.04

ATOM
1195
CD
GLU

320
−9.384
107.677
−61.606
1.00
46.60

ATOM
1196
OE1
GLU

320
−8.905
107.784
−62.759
1.00
46.24

ATOM
1197
OE2
GLU

320
−10.547
108.029
−61.314
1.00
45.58

ATOM
1198
C
GLU

320
−6.555
104.785
−61.068
1.00
43.26

ATOM
1199
O
GLU

S320
−6.004
104.416
−60.026
1.00
43.06

ATOM
1200
N
VAL

321
−7.368
103.983
−61.752
1.00
43.24

ATOM
1201
CA
VAL

321
−7.527
102.616
−61.303
1.00
45.22

ATOM
1202
CB
VAL

321
−8.793
101.942
−61.886
1.00
44.66

ATOM
1203
CG1
VAL

321
−8.723
100.458
−61.658
1.00
42.53

ATOM
1204
CG2
VAL

321
−10.056
102.509
−61.224
1.00
43.26

ATOM
1205
C
VAL

321
−6.272
101.877
−61.807
1.00
47.72

ATOM
1206
O
VAL

321
−5.638
101.142
−61.052
1.00
47.80

ATOM
1207
N
LEU

322
−5.896
102.093
−63.070
1.00
47.95

ATOM
1208
CA
LEU

322
−4.715
101.428
−63.624
1.00
49.76

ATOM
1209
CB
LEU

322
−4.532
101.776
−65.098
1.00
47.04

ATOM
1210
CG
LEU

322
−5.572
101.131
−65.995
1.00
46.64

ATOM
1211
CD1
LEU

322
−5.338
101.564
−67.424
1.00
45.36

ATOM
1212
CD2
LEU

322
−5.482
99.601
−65.844
1.00
47.97

ATOM
1213
C
LEU

322
−3.419
101.770
−62.898
1.00
50.74

ATOM
1214
O
LEU

322
−2.587
100.890
−62.624
1.00
50.48

ATOM
1215
N
GLU

323
−3.246
103.046
−62.584
1.00
50.19

ATOM
1216
CA
GLU

323
−2.024
103.473
−61.931
1.00
50.50

ATOM
1217
CB
GLU

323
−1.723
104.930
−62.303
1.00
49.54

ATOM
1218
CG
GLU

323
−0.531
105.544
−61.605
1.00
51.05

ATOM
1219
CD
GLU

323
−0.121
106.897
−62.196
1.00
52.86

ATOM
1220
OE1
GLU

323
−0.996
107.667
−62.659
1.00
51.36

ATOM
1221
OE2
GLU

323
1.088
107.199
−62.173
1.00
53.36

ATOM
1222
C
GLU

323
−1.976
103.279
−60.423
1.00
51.07

ATOM
1223
O
GLU

323
−1.038
102.670
−59.924
1.00
53.24

ATOM
1224
N
ASP

324
−2.976
103.758
−59.689
1.00
51.06

ATOM
1225
CA
ASP

324
−2.935
103.625
−58.242
1.00
51.85

ATOM
1226
CB
ASP

324
−2.998
105.000
−57.569
1.00
53.82

ATOM
1227
CG
ASP

324
−1.834
105.890
−57.953
1.00
56.66

ATOM
1228
OD1
ASP

324
−0.719
105.351
−58.197
1.00
58.19

ATOM
1229
OD2
ASP

324
−2.030
107.132
−57.999
1.00
56.61

ATOM
1230
C
ASP

324
−3.988
102.746
−57.624
1.00
51.70

ATOM
1231
O
ASP

324
−4.235
102.840
−56.425
1.00
52.09

ATOM
1232
N
ASN

325
−4.599
101.886
−58.424
1.00
51.98

ATOM
1233
CA
ASN

325
−5.650
100.995
−57.930
1.00
52.58

ATOM
1234
CB
ASN

325
−5.045
99.844
−57.145
1.00
51.16

ATOM
1235
CG
ASN

325
−6.033
98.728
−56.940
1.00
52.85

ATOM
1236
OD1
ASN

325
−6.692
98.301
−57.891
1.00
51.88

ATOM
1237
ND2
ASN

325
−6.143
98.239
−55.709
1.00
53.08

ATOM
1238
C
ASN

325
−6.677
101.719
−57.046
1.00
53.38

ATOM
1239
O
ASN

325
−7.292
101.126
−56.156
1.00
53.07

ATOM
1240
N
ASP

326
−6.860
103.003
−57.320
1.00
53.86

ATOM
1241
CA
ASP

326
−7.778
103.855
−56.578
1.00
54.16

ATOM
1242
CB
ASP

326
−7.126
105.233
−56.459
1.00
57.67

ATOM
1243
CG
ASP

326
−8.052
106.279
−55.921
1.00
59.69

ATOM
1244
OD1
ASP

326
−7.591
107.424
−55.741
1.00
62.38

ATOM
1245
OD2
ASP

326
−9.231
105.974
−55.686
1.00
63.13

ATOM
1246
C
ASP

326
−9.175
103.941
−57.228
1.00
52.75

ATOM
1247
O
ASP

326
−9.360
104.610
−58.246
1.00
53.16

ATOM
1248
N
TYR

327
−10.145
103.255
−56.621
1.00
49.27

ATOM
1249
CA
TYR

327
−11.521
103.229
−57.104
1.00
47.81

ATOM
1250
CB
TYR

327
−12.174
101.844
−56.887
1.00
46.28

ATOM
1251
CG
TYR

327
−11.801
100.745
−57.861
1.00
45.89

ATOM
1252
CD1
TYR

327
−10.607
100.030
−57.726
1.00
46.18

ATOM
1253
CE1
TYR

327
−10.265
99.026
−58.620
1.00
45.79

ATOM
1254
CD2
TYR

327
−12.642
100.421
−58.924
1.00
45.64

ATOM
1255
CE2
TYR

327
−12.305
99.420
−59.828
1.00
46.87

ATOM
1256
CZ
TYR

327
−11.113
98.722
−59.672
1.00
48.27

ATOM
1257
OH
TYR

327
−10.775
97.734
−60.583
1.00
49.49

ATOM
1258
C
TYR

327
−12.406
104.263
−56.388
1.00
48.05

ATOM
1259
O
TYR

327
−13.294
103.873
−55.617
1.00
47.57

ATOM
1260
N
GLY

328
−12.182
105.555
−56.642
1.00
47.18

ATOM
1261
CA
GLY

328
−13.003
106.592
−56.028
1.00
46.32

ATOM
1262
C
GLY

328
−14.168
107.043
−56.905
1.00
46.65

ATOM
1263
O
GLY

328
−14.212
106.706
−58.091
1.00
47.60

ATOM
1264
N
ARG

329
−15.100
107.806
−56.332
1.00
45.55

ATOM
1265
CA
ARG

329
−16.280
108.314
−57.057
1.00
46.76

ATOM
1266
CB
ARG

329
−16.745
109.667
−56.494
1.00
48.48

ATOM
1267
CG
ARG

329
−16.740
109.839
−54.996
1.00
52.56

ATOM
1268
CD
ARG

329
−16.236
111.251
−54.601
1.00
54.15

ATOM
1269
NE
ARG

329
−16.644
112.263
−55.563
1.00
55.37

ATOM
1270
CZ
ARG

329
−16.066
113.450
−55.706
1.00
55.95

ATOM
1271
NH1
ARG

329
−15.038
113.807
−54.948
1.00
55.06

ATOM
1272
NH2
ARG

329
−16.520
114.280
−56.630
1.00
59.49

ATOM
1273
C
ARG

329
−16.017
108.549
−58.548
1.00
46.10

ATOM
1274
O
ARG

329
−16.807
108.160
−59.418
1.00
46.43

ATOM
1275
N
ALA

330
−14.904
109.231
−58.806
1.00
46.16

ATOM
1276
CA
ALA

330
−14.463
109.614
−60.134
1.00
45.40

ATOM
1277
CB
ALA

330
−13.052
110.143
−60.053
1.00
44.79

ATOM
1278
C
ALA

330
−14.551
108.554
−61.218
1.00
44.25

ATOM
1279
O
ALA

330
−14.952
108.843
−62.339
1.00
45.35

ATOM
1280
N
VAL

331
−14.193
107.323
−60.903
1.00
43.40

ATOM
1281
CA
VAL

331
−14.235
106.295
−61.938
1.00
42.86

ATOM
1282
CB
VAL

331
−13.607
104.964
−61.440
1.00
42.39

ATOM
1283
CG1
VAL

331
−12.330
105.257
−60.703
1.00
40.94

ATOM
1284
CG2
VAL

331
−14.576
104.212
−60.563
1.00
41.02

ATOM
1285
C
VAL

331
−15.621
106.018
−62.527
1.00
42.04

ATOM
1286
O
VAL

331
−15.728
105.397
−63.596
1.00
42.24

ATOM
1287
N
ASP

332
−16.687
106.458
−61.865
1.00
38.49

ATOM
1288
CA
ASP

332
−17.983
106.192
−62.457
1.00
39.57

ATOM
1289
CB
ASP

332
−19.117
106.275
−61.430
1.00
41.24

ATOM
1290
CG
ASP

332
−19.090
105.143
−60.432
1.00
43.04

ATOM
1291
OD1
ASP

332
−18.807
104.002
−60.846
1.00
44.33

ATOM
1292
OD2
ASP

332
−19.371
105.388
−59.236
1.00
42.62

ATOM
1293
C
ASP

332
−18.231
107.187
−63.588
1.00
37.82

ATOM
1294
O
ASP

332
−18.927
106.888
−64.568
1.00
37.16

ATOM
1295
N
TRP

333
−17.652
108.371
−63.446
1.00
37.40

ATOM
1296
CA
TRP

333
−17.817
109.414
−64.434
1.00
38.54

ATOM
1297
CB
TRP

333
−17.321
110.745
−63.853
1.00
40.23

ATOM
1298
CG
TRP

333
−18.209
111.198
−62.715
1.00
41.98

ATOM
1299
CD2
TRP

333
−19.644
111.173
−62.688
1.00
39.22

ATOM
1300
CE2
TRP

333
−20.050
111.582
−61.402
1.00
40.30

ATOM
1301
CE3
TRP

333
−20.629
110.829
−63.625
1.00
38.40

ATOM
1302
CD1
TRP

333
−17.811
111.630
−61.473
1.00
43.77

ATOM
1303
NE1
TRP

333
−18.912
111.859
−60.680
1.00
42.72

ATOM
1304
CZ2
TRP

333
−21.397
111.670
−61.026
1.00
39.06

ATOM
1305
CZ3
TRP

333
−21.967
110.915
−63.254
1.00
38.33

ATOM
1306
CH2
TRP

333
−22.337
111.330
−61.960
1.00
36.53

ATOM
1307
C
TRP

333
−17.060
108.981
−65.681
1.00
38.67

ATOM
1308
O
TRP

333
−17.605
109.055
−66.801
1.00
36.29

ATOM
1309
N
TRP

334
−15.824
108.508
−65.470
1.00
38.23

ATOM
1310
CA
TRP

334
−14.979
107.985
−66.546
1.00
35.70

ATOM
1311
CB
TRP

334
−13.684
107.430
−65.945
1.00
40.15

ATOM
1312
CG
TRP

334
−12.897
106.601
−66.905
1.00
45.37

ATOM
1313
CD2
TRP

334
−11.885
107.059
−67.802
1.00
46.40

ATOM
1314
CE2
TRP

334
−11.478
105.951
−68.572
1.00
47.80

ATOM
1315
CE3
TRP

334
−11.287
108.303
−68.039
1.00
47.17

ATOM
1316
CD1
TRP

334
−13.054
105.266
−67.154
1.00
46.66

ATOM
1317
NE1
TRP

334
−12.203
104.871
−68.154
1.00
49.45

ATOM
1318
CZ2
TRP

334
−10.496
106.045
−69.556
1.00
48.28

ATOM
1319
CZ3
TRP

334
−10.312
108.398
−69.017
1.00
47.44

ATOM
1320
CH2
TRP

334
−9.927
107.276
−69.767
1.00
47.35

ATOM
1321
C
TRP

334
−15.814
106.882
−67.206
1.00
32.98

ATOM
1322
O
TRP

334
−15.976
106.805
−68.446
1.00
29.28

ATOM
1323
N
GLY

335
−16.388
106.040
−66.359
1.00
32.62

ATOM
1324
CA
GLY

335
−17.246
104.975
−66.847
1.00
31.24

ATOM
1325
C
GLY

335
−18.265
105.585
−67.767
1.00
32.09

ATOM
1326
O
GLY

335
−18.422
105.124
−68.883
1.00
35.03

ATOM
1327
N
LEU

336
−18.950
106.630
−67.302
1.00
32.31

ATOM
1328
CA
LEU

336
−19.966
107.316
−68.103
1.00
31.74

ATOM
1329
CB
LEU

336
−20.548
108.517
−67.346
1.00
34.73

ATOM
1330
CG
LEU

336
−21.643
109.289
−68.099
1.00
35.62

ATOM
1331
CD1
LEU

336
−22.851
108.369
−68.323
1.00
39.53

ATOM
1332
CD2
LEU

336
−22.039
110.545
−67.321
1.00
38.52

ATOM
1333
C
LEU

336
−19.299
107.801
−69.376
1.00
32.10

ATOM
1334
O
LEU

336
−19.747
107.488
−70.486
1.00
30.32

ATOM
1335
N
GLY

337
−18.231
108.578
−69.198
1.00
30.47

ATOM
1336
CA
GLY

337
−17.477
109.061
−70.329
1.00
33.11

ATOM
1337
C
GLY

337
−17.185
107.988
−71.375
1.00
36.30

ATOM
1338
O
GLY

337
−17.617
108.136
−72.527
1.00
39.45

ATOM
1339
N
VAL

338
−16.479
106.914
−71.011
1.00
35.68

ATOM
1340
CA
VAL

338
−16.186
105.844
−71.987
1.00
34.88

ATOM
1341
CB
VAL

338
−15.401
104.640
−71.340
1.00
31.93

ATOM
1342
CG1
VAL

338
−15.010
103.655
−72.393
1.00
29.67

ATOM
1343
CG2
VAL

338
−14.177
105.137
−70.605
1.00
26.65

ATOM
1344
C
VAL

338
−17.481
105.308
−72.639
1.00
36.09

ATOM
1345
O
VAL

338
−17.538
105.071
−73.863
1.00
32.07

ATOM
1346
N
VAL

339
−18.525
105.132
−71.830
1.00
37.68

ATOM
1347
CA
VAL

339
−19.805
104.657
−72.378
1.00
39.88

ATOM
1348
CB
VAL

339
−20.863
104.396
−71.283
1.00
39.09

ATOM
1349
CG1
VAL

339
−22.073
103.703
−71.881
1.00
39.83

ATOM
1350
CG2
VAL

339
−20.275
103.573
−70.166
1.00
41.28

ATOM
1351
C
VAL

339
−20.395
105.698
−73.324
1.00
40.15

ATOM
1352
O
VAL

339
−21.040
105.359
−74.302
1.00
42.13

ATOM
1353
N
MET

340
−20.184
106.973
−73.042
1.00
42.58

ATOM
1354
CA
MET

340
−20.744
107.986
−73.923
1.00
46.52

ATOM
1355
CB
MET

340
−21.231
109.194
−73.131
1.00
45.49

ATOM
1356
CG
MET

340
−22.389
108.841
−72.275
1.00
49.72

ATOM
1357
SD
MET

340
−23.278
110.256
−71.668
1.00
53.94

ATOM
1358
CE
MET

340
−21.879
111.190
−70.904
1.00
54.43

ATOM
1359
C
MET

340
−19.815
108.409
−75.045
1.00
46.60

ATOM
1360
O
MET

340
−20.173
109.222
−75.910
1.00
47.26

ATOM
1361
N
TYR

341
−18.606
107.887
−75.035
1.00
45.25

ATOM
1362
CA
TYR

341
−17.761
108.207
−76.150
1.00
45.45

ATOM
1363
CB
TYR

341
−16.292
108.076
−75.787
1.00
44.57

ATOM
1364
CG
TYR

341
−15.357
108.298
−76.945
1.00
44.38

ATOM
1365
CD1
TYR

341
−15.388
107.468
−78.071
1.00
44.83

ATOM
1366
CE1
TYR

341
−14.490
107.628
−79.118
1.00
43.03

ATOM
1367
CD2
TYR

341
−14.403
109.298
−76.895
1.00
46.38

ATOM
1368
CE2
TYR

341
−13.486
109.475
−77.939
1.00
44.56

ATOM
1369
CZ
TYR

341
−13.538
108.641
−79.041
1.00
44.25

ATOM
1370
OH
TYR

341
−12.652
108.844
−80.063
1.00
41.93

ATOM
1371
C
TYR

341
−18.177
107.170
−77.188
1.00
45.21

ATOM
1372
O
TYR

341
−18.176
107.451
−78.382
1.00
44.90

ATOM
1373
N
GLU

342
−18.608
105.993
−76.729
1.00
45.89

ATOM
1374
CA
GLU

342
−18.999
104.938
−77.664
1.00
46.56

ATOM
1375
CB
GLU

342
−19.023
103.555
−77.006
1.00
47.47

ATOM
1376
CG
GLU

342
−18.486
102.458
−77.930
1.00
51.19

ATOM
1377
CD
GLU

342
−18.742
101.013
−77.446
1.00
53.52

ATOM
1378
OE1
GLU

342
−18.360
100.648
−76.303
1.00
55.05

ATOM
1379
OE2
GLU

342
−19.316
100.232
−78.233
1.00
51.05

ATOM
1380
C
GLU

342
−20.311
105.165
−78.353
1.00
45.51

ATOM
1381
O
GLU

342
−20.346
105.169
−79.566
1.00
47.31

ATOM
1382
N
MET

343
−21.387
105.360
−77.596
1.00
46.13

ATOM
1383
CA
MET

343
−22.736
105.558
−78.163
1.00
45.97

ATOM
1384
CB
MET

343
−23.738
105.975
−77.076
1.00
45.96

ATOM
1385
CG
MET

343
−24.381
104.877
−76.274
1.00
45.04

ATOM
1386
SD
MET

343
−25.048
105.637
−74.779
1.00
44.87

ATOM
1387
CE
MET

343
−26.173
104.315
−74.111
1.00
44.54

ATOM
1388
C
MET

343
−22.830
106.589
−79.277
1.00
47.60

ATOM
1389
O
MET

343
−23.570
106.379
−80.243
1.00
45.42

ATOM
1390
N
MET

344
−22.113
107.707
−79.114
1.00
48.72

ATOM
1391
CA
MET

344
−22.120
108.800
−80.083
1.00
51.33

ATOM
1392
CB
MET

344
−21.906
110.152
−79.363
1.00
50.03

ATOM
1393
CG
MET

344
−23.080
110.600
−78.422
1.00
51.59

ATOM
1394
SD
MET

344
−22.914
112.225
−77.512
1.00
51.38

ATOM
1395
CE
MET

344
−21.418
111.976
−76.565
1.00
50.37

ATOM
1396
C
MET

344
−21.060
108.598
−81.186
1.00
54.81

ATOM
1397
O
MET

344
−21.308
108.906
−82.357
1.00
55.93

ATOM
1398
N
CYS

345
−19.881
108.085
−80.806
1.00
56.27

ATOM
1399
CA
CYS

345
−18.792
107.826
−81.745
1.00
53.60

ATOM
1400
CB
CYS

345
−17.446
107.898
−81.033
1.00
53.35

ATOM
1401
SG
CYS

345
−16.911
109.518
−80.366
1.00
51.93

ATOM
1402
C
CYS

345
−18.930
106.460
−82.434
1.00
54.34

ATOM
1403
O
CYS

345
−18.421
106.275
−83.532
1.00
54.10

ATOM
1404
N
GLY

346
−19.630
105.519
−81.797
1.00
55.46

ATOM
1405
CA
GLY

346
−19.823
104.182
−82.359
1.00
56.53

ATOM
1406
C
GLY

346
−18.639
103.222
−82.176
1.00
58.54

ATOM
1407
O
GLY

346
−18.619
102.110
−82.711
1.00
58.51

ATOM
1408
N
ARG

347
−17.648
103.643
−81.400
1.00
59.41

ATOM
1409
CA
ARG

347
−16.457
102.832
−81.187
1.00
60.48

ATOM
1410
CB
ARG

347
−15.565
102.910
−82.426
1.00
62.58

ATOM
1411
CG
ARG

347
−15.306
104.335
−82.851
1.00
65.67

ATOM
1412
CD
ARG

347
−14.072
104.457
−83.713
1.00
70.23

ATOM
1413
NE
ARG

347
−13.477
105.793
−83.627
1.00
74.54

ATOM
1414
CZ
ARG

347
−14.030
106.899
−84.124
1.00
77.20

ATOM
1415
NH1
ARG

347
−15.201
106.834
−84.751
1.00
75.57

ATOM
1416
NH2
ARG

347
−13.408
108.075
−84.001
1.00
78.60

ATOM
1417
C
ARG

347
−15.717
103.403
−79.982
1.00
59.56

ATOM
1418
O
ARG

347
−15.957
104.554
−79.596
1.00
58.79

ATOM
1419
N
LEU

348
−14.813
102.616
−79.402
1.00
57.45

ATOM
1420
CA
LEU

348
−14.080
103.053
−78.224
1.00
55.76

ATOM
1421
CB
LEU

348
−13.539
101.834
−77.486
1.00
53.62

ATOM
1422
CG
LEU

348
−14.603
100.859
−76.953
1.00
52.62

ATOM
1423
CD1
LEU

348
−13.980
99.518
−76.642
1.00
54.33

ATOM
1424
CD2
LEU

348
−15.253
101.425
−75.707
1.00
54.19

ATOM
1425
C
LEU

348
−12.971
104.037
−78.586
1.00
58.09

ATOM
1426
O
LEU

348
−12.520
104.098
−79.719
1.00
59.07

ATOM
1427
N
PRO

349
−12.517
104.835
−77.625
1.00
59.01

ATOM
1428
CD
PRO

349
−12.930
105.013
−76.230
1.00
59.70

ATOM
1429
CA
PRO

349
−11.464
105.777
−77.993
1.00
61.12

ATOM
1430
CB
PRO

349
−11.156
106.502
−76.671
1.00
60.60

ATOM
1431
CG
PRO

349
−11.694
105.606
−75.620
1.00
60.92

ATOM
1432
C
PRO

349
−10.225
105.212
−78.671
1.00
62.77

ATOM
1433
O
PRO

349
−9.471
105.945
−79.300
1.00
63.54

ATOM
1434
N
PHE

350
−10.008
103.914
−78.576
1.00
64.60

ATOM
1435
CA
PHE

350
−8.819
103.351
−79.205
1.00
66.55

ATOM
1436
CB
PHE

350
−7.768
103.028
−78.130
1.00
63.72

ATOM
1437
CG
PHE

350
−7.373
104.204
−77.264
1.00
61.36

ATOM
1438
CD1
PHE

350
−7.537
104.151
−75.880
1.00
61.07

ATOM
1439
CD2
PHE

350
−6.765
105.331
−77.815
1.00
61.06

ATOM
1440
CE1
PHE

350
−7.097
105.200
−75.057
1.00
59.73

ATOM
1441
CE2
PHE

350
−6.319
106.385
−76.998
1.00
58.34

ATOM
1442
CZ
PHE

350
−6.483
106.316
−75.620
1.00
58.70

ATOM
1443
C
PHE

350
−9.173
102.076
−79.974
1.00
69.12

ATOM
1444
O
PHE

350
−8.336
101.197
−80.134
1.00
69.42

ATOM
1445
N
TYR

351
−10.414
101.990
−80.447
1.00
72.87

ATOM
1446
CA
TYR

351
−10.928
100.814
−81.162
1.00
76.20

ATOM
1447
CB
TYR

351
−12.249
101.146
−81.860
1.00
77.72

ATOM
1448
CG
TYR

351
−12.068
101.741
−83.240
1.00
80.61

ATOM
1449
CD1
TYR

351
−12.807
101.265
−84.323
1.00
80.64

ATOM
1450
CE1
TYR

351
−12.640
101.804
−85.595
1.00
81.66

ATOM
1451
CD2
TYR

351
−11.154
102.777
−83.467
1.00
80.71

ATOM
1452
CE2
TYR

351
−10.982
103.321
−84.734
1.00
81.04

ATOM
1453
CZ
TYR

351
−11.727
102.831
−85.787
1.00
81.43

ATOM
1454
OH
TYR

351
−11.578
103.376
−87.033
1.00
82.80

ATOM
1455
C
TYR

351
−9.991
100.174
−82.187
1.00
77.87

ATOM
1456
O
TYR

351
−10.102
98.975
−82.470
1.00
78.58

ATOM
1457
N
ASN

352
−9.093
100.960
−82.768
1.00
78.54

ATOM
1458
CA
ASN

352
−8.168
100.394
−83.734
1.00
80.51

ATOM
1459
CB
ASN

352
−7.914
101.381
−84.874
1.00
81.11

ATOM
1460
CG
ASN

352
−7.613
102.771
−84.382
1.00
81.90

ATOM
1461
OD1
ASN

352
−7.431
103.688
−85.173
1.00
81.64

ATOM
1462
ND2
ASN

352
−7.561
102.939
−83.067
1.00
82.39

ATOM
1463
C
ASN

352
−6.853
99.971
−83.070
1.00
81.13

ATOM
1464
O
ASN

352
−6.638
98.783
−82.830
1.00
81.84

ATOM
1465
N
GLN

353
−5.991
100.932
−82.753
1.00
81.20

ATOM
1466
CA
GLN

353
−4.704
100.640
−82.124
1.00
81.66

ATOM
1467
CB
GLN

353
−4.330
101.762
−81.165
1.00
81.11

ATOM
1468
CG
GLN

353
−4.343
103.105
−81.834
1.00
81.13

ATOM
1469
CD
GLN

353
−3.603
104.136
−81.040
1.00
83.01

ATOM
1470
OE1
GLN

353
−2.406
103.992
−80.786
1.00
82.60

ATOM
1471
NE2
GLN

353
−4.305
105.191
−80.638
1.00
83.18

ATOM
1472
C
GLN

353
−4.640
99.298
−81.401
1.00
82.23

ATOM
1473
O
GLN

353
−5.395
99.046
−80.468
1.00
82.60

ATOM
1474
N
ASP

354
−3.724
98.450
−81.866
1.00
83.56

ATOM
1475
CA
ASP

354
−3.486
97.104
−81.342
1.00
84.13

ATOM
1476
CB
ASP

354
−2.036
96.999
−80.852
1.00
85.68

ATOM
1477
CG
ASP

354
−1.518
95.567
−80.842
1.00
87.94

ATOM
1478
OD1
ASP

354
−2.119
94.708
−80.151
1.00
90.28

ATOM
1479
OD2
ASP

354
−0.504
95.302
−81.528
1.00
87.84

ATOM
1480
C
ASP

354
−4.459
96.681
−80.233
1.00
83.94

ATOM
1481
O
ASP

354
−5.641
96.437
−80.498
1.00
84.30

ATOM
1482
N
HIS

355
−3.964
96.586
−79.000
1.00
82.80

ATOM
1483
CA
HIS

355
−4.799
96.195
−77.879
1.00
81.64

ATOM
1484
CB
HIS

355
−5.490
94.878
−78.157
1.00
83.58

ATOM
1485
CG
HIS

355
−6.368
94.442
−77.037
1.00
86.16

ATOM
1486
CD2
HIS

355
−6.152
93.571
−76.023
1.00
87.75

ATOM
1487
ND1
HIS

355
−7.600
95.012
−76.801
1.00
87.65

ATOM
1488
CE1
HIS

355
−8.105
94.512
−75.687
1.00
89.10

ATOM
1489
NE2
HIS

355
−7.246
93.637
−75.194
1.00
89.32

ATOM
1490
C
HIS

355
−4.057
96.050
−76.560
1.00
80.62

ATOM
1491
O
HIS

355
−4.595
96.378
−75.504
1.00
79.87

ATOM
1492
N
GLU

356
−2.841
95.520
−76.618
1.00
79.66

ATOM
1493
CA
GLU

356
−2.026
95.338
−75.419
1.00
78.61

ATOM
1494
CB
GLU

356
−0.847
94.420
−75.722
1.00
80.80

ATOM
1495
CG
GLU

356
−1.193
93.207
−76.563
1.00
83.90

ATOM
1496
CD
GLU

356
0.001
92.724
−77.378
1.00
86.67

ATOM
1497
OE1
GLU

356
0.459
93.483
−78.265
1.00
87.68

ATOM
1498
OE2
GLU

356
0.489
91.597
−77.132
1.00
87.85

ATOM
1499
C
GLU

356
−1.505
96.714
−75.015
1.00
76.92

ATOM
1500
O
GLU

356
−0.868
96.877
−73.969
1.00
75.86

ATOM
1501
N
ARG

357
−1.793
97.694
−75.873
1.00
74.27

ATOM
1502
CA
ARG

357
−1.397
99.078
−75.675
1.00
72.32

ATOM
1503
CB
ARG

357
−1.191
99.739
−77.037
1.00
74.34

ATOM
1504
CG
ARG

357
0.195
99.502
−77.581
1.00
79.91

ATOM
1505
CD
ARG

357
0.263
99.418
−79.105
1.00
82.36

ATOM
1506
NE
ARG

357
1.516
98.766
−79.495
1.00
85.32

ATOM
1507
CZ
ARG

357
1.806
98.354
−80.724
1.00
86.63

ATOM
1508
NH1
ARG

357
0.932
98.530
−81.707
1.00
87.74

ATOM
1509
NH2
ARG

357
2.963
97.747
−80.966
1.00
86.74

ATOM
1510
C
ARG

357
−2.360
99.925
−74.836
1.00
69.50

ATOM
1511
O
ARG

357
−2.093
101.108
−74.603
1.00
70.06

ATOM
1512
N
LEU

358
−3.462
99.338
−74.369
1.00
64.22

ATOM
1513
CA
LEU

358
−4.426
100.101
−73.573
1.00
60.12

ATOM
1514
CB
LEU

358
−5.656
99.260
−73.228
1.00
58.17

ATOM
1515
CG
LEU

358
−6.603
99.058
−74.406
1.00
55.93

ATOM
1516
CD1
LEU

358
−7.651
98.053
−74.043
1.00
54.94

ATOM
1517
CD2
LEU

358
−7.227
100.391
−74.799
1.00
56.22

ATOM
1518
C
LEU

358
−3.847
100.675
−72.302
1.00
58.03

ATOM
1519
O
LEU

358
−4.130
101.821
−71.971
1.00
57.79

ATOM
1520
N
PHE

359
−3.034
99.898
−71.588
1.00
55.72

ATOM
1521
CA
PHE

359
−2.448
100.396
−70.347
1.00
52.62

ATOM
1522
CB
PHE

359
−1.434
99.407
−69.769
1.00
47.27

ATOM
1523
CG
PHE

359
−0.904
99.808
−68.422
1.00
42.38

ATOM
1524
CD1
PHE

359
−1.547
99.405
−67.257
1.00
38.30

ATOM
1525
CD2
PHE

359
0.207
100.633
−68.319
1.00
39.93

ATOM
1526
CE1
PHE

359
−1.099
99.815
−66.011
1.00
39.00

ATOM
1527
CE2
PHE

359
0.670
101.055
−67.069
1.00
40.03

ATOM
1528
CZ
PHE

359
0.018
100.650
−65.912
1.00
38.98

ATOM
1529
C
PHE

359
−1.749
101.729
−70.619
1.00
54.41

ATOM
1530
O
PHE

359
−2.036
102.741
−69.961
1.00
54.88

ATOM
1531
N
GLU

360
−0.836
101.731
−71.587
1.00
54.09

ATOM
1532
CA
GLU

360
−0.116
102.952
−71.931
1.00
54.89

ATOM
1533
CB
GLU

360
1.008
102.670
−72.943
1.00
56.26

ATOM
1534
CG
GLU

360
1.838
101.412
−72.700
1.00
59.95

ATOM
1535
CD
GLU

360
1.293
100.190
−73.435
1.00
61.50

ATOM
1536
OE1
GLU

360
0.748
99.292
−72.760
1.00
64.26

ATOM
1537
OE2
GLU

360
1.401
100.125
−74.683
1.00
60.63

ATOM
1538
C
GLU

360
−1.079
103.993
−72.541
1.00
53.30

ATOM
1539
O
GLU

360
−0.979
105.186
−72.265
1.00
53.36

ATOM
1540
N
LEU

361
−2.004
103.533
−73.371
1.00
50.46

ATOM
1541
CA
LEU

361
−2.941
104.430
−74.024
1.00
49.32

ATOM
1542
CB
LEU

361
−3.773
103.655
−75.044
1.00
49.29

ATOM
1543
CG
LEU

361
−3.043
103.239
−76.317
1.00
49.37

ATOM
1544
CD1
LEU

361
−4.047
102.750
−77.322
1.00
49.11

ATOM
1545
CD2
LEU

361
−2.290
104.440
−76.891
1.00
51.54

ATOM
1546
C
LEU

361
−3.874
105.190
−73.079
1.00
48.48

ATOM
1547
O
LEU

361
−3.886
106.423
−73.059
1.00
46.65

ATOM
1548
N
ILE

362
−4.657
104.443
−72.310
1.00
46.31

ATOM
1549
CA
ILE

362
−5.590
105.027
−71.368
1.00
45.23

ATOM
1550
CB
ILE

362
−6.303
103.938
−70.556
1.00
43.00

ATOM
1551
CG2
ILE

362
−7.225
104.568
−69.518
1.00
41.69

ATOM
1552
CG1
ILE

362
−7.096
103.049
−71.500
1.00
42.41

ATOM
1553
CD1
ILE

362
−7.636
101.818
−70.838
1.00
42.87

ATOM
1554
C
ILE

362
−4.899
105.970
−70.406
1.00
45.61

ATOM
1555
O
ILE

362
−5.489
106.937
−69.945
1.00
46.19

ATOM
1556
N
LEU

363
−3.644
105.701
−70.108
1.00
47.28

ATOM
1557
CA
LEU

363
−2.926
106.538
−69.174
1.00
50.66

ATOM
1558
CB
LEU

363
−1.884
105.721
−68.432
1.00
50.05

ATOM
1559
CG
LEU

363
−2.428
104.872
−67.298
1.00
51.81

ATOM
1560
CD1
LEU

363
−1.435
103.757
−66.994
1.00
49.66

ATOM
1561
CD2
LEU

363
−2.671
105.750
−66.077
1.00
50.15

ATOM
1562
C
LEU

363
−2.241
107.743
−69.757
1.00
52.43

ATOM
1563
O
LEU

363
−2.322
108.813
−69.177
1.00
53.85

ATOM
1564
N
MET

364
−1.581
107.580
−70.899
1.00
53.89

ATOM
1565
CA
MET

364
−0.815
108.671
−71.494
1.00
56.15

ATOM
1566
CB
MET

364
0.668
108.311
−71.453
1.00
56.17

ATOM
1567
CG
MET

364
1.154
107.902
−70.088
1.00
58.72

ATOM
1568
SD
MET

364
2.845
107.242
−70.080
1.00
61.25

ATOM
1569
CE
MET

364
2.525
105.577
−70.470
1.00
59.93

ATOM
1570
C
MET

364
−1.159
109.093
−72.910
1.00
56.72

ATOM
1571
O
MET

364
−0.388
109.797
−73.542
1.00
58.49

ATOM
1572
N
GLU

365
−2.299
108.682
−73.421
1.00
57.45

ATOM
1573
CA
GLU

365
−2.654
109.048
−74.783
1.00
58.82

ATOM
1574
CB
GLU

365
−2.927
107.767
−75.574
1.00
60.59

ATOM
1575
CG
GLU

365
−3.351
107.998
−76.995
1.00
62.48

ATOM
1576
CD
GLU

365
−2.242
108.579
−77.814
1.00
64.91

ATOM
1577
OE1
GLU

365
−1.669
109.608
−77.386
1.00
65.42

ATOM
1578
OE2
GLU

365
−1.940
108.003
−78.882
1.00
66.95

ATOM
1579
C
GLU

365
−3.877
109.980
−74.866
1.00
59.32

ATOM
1580
O
GLU

365
−4.943
109.652
−74.336
1.00
58.16

ATOM
1581
N
GLU

366
−3.740
111.128
−75.531
1.00
60.08

ATOM
1582
CA
GLU

366
−4.885
112.034
−75.655
1.00
61.95

ATOM
1583
CB
GLU

366
−4.514
113.327
−76.389
1.00
65.27

ATOM
1584
CG
GLU

366
−4.218
113.143
−77.890
1.00
70.51

ATOM
1585
CD
GLU

366
−4.067
114.469
−78.658
1.00
72.07

ATOM
1586
OE1
GLU

366
−5.100
115.096
−78.995
1.00
72.95

ATOM
1587
OE2
GLU

366
−2.912
114.880
−78.918
1.00
72.96

ATOM
1588
C
GLU

366
−5.965
111.308
−76.444
1.00
60.79

ATOM
1589
O
GLU

366
−5.682
110.679
−77.466
1.00
61.20

ATOM
1590
N
ILE

367
−7.193
111.382
−75.949
1.00
58.81

ATOM
1591
CA
ILE

367
−8.326
110.740
−76.594
1.00
59.29

ATOM
1592
CB
ILE

367
−9.436
110.401
−75.557
1.00
58.55

ATOM
1593
CG2
ILE

367
−10.740
110.094
−76.259
1.00
57.35

ATOM
1594
CG1
ILE

367
−8.989
109.216
−74.691
1.00
58.42

ATOM
1595
CD1
ILE

367
−10.002
108.764
−73.650
1.00
56.35

ATOM
1596
C
ILE

367
−8.866
111.695
−77.656
1.00
60.85

ATOM
1597
O
ILE

367
−9.357
112.786
−77.346
1.00
61.82

ATOM
1598
N
ARG

368
−8.768
111.268
−78.910
1.00
61.14

ATOM
1599
CA
ARG

368
−9.204
112.053
−80.060
1.00
60.62

ATOM
1600
CB
ARG

368
−8.402
111.582
−81.290
1.00
62.52

ATOM
1601
CG
ARG

368
−8.695
112.294
−82.587
1.00
68.23

ATOM
1602
CD
ARG

368
−7.459
112.359
−83.502
1.00
72.52

ATOM
1603
NE
ARG

368
−6.505
113.424
−83.147
1.00
75.13

ATOM
1604
CZ
ARG

368
−6.734
114.740
−83.254
1.00
76.98

ATOM
1605
NH1
ARG

368
−7.901
115.210
−83.709
1.00
75.68

ATOM
1606
NH2
ARG

368
−5.779
115.598
−82.912
1.00
77.83

ATOM
1607
C
ARG

368
−10.716
111.927
−80.280
1.00
59.50

ATOM
1608
O
ARG

368
−11.290
110.876
−80.011
1.00
57.56

ATOM
1609
N
PHE

369
−11.349
113.006
−80.761
1.00
59.17

ATOM
1610
CA
PHE

369
−12.804
113.052
−81.010
1.00
57.48

ATOM
1611
CB
PHE

369
−13.452
114.164
−80.175
1.00
55.03

ATOM
1612
CG
PHE

369
−13.170
114.067
−78.723
1.00
50.65

ATOM
1613
CD1
PHE

369
−13.747
113.070
−77.958
1.00
49.85

ATOM
1614
CD2
PHE

369
−12.291
114.950
−78.125
1.00
51.15

ATOM
1615
CE1
PHE

369
−13.444
112.951
−76.620
1.00
50.03

ATOM
1616
CE2
PHE

369
−11.980
114.839
−76.782
1.00
51.20

ATOM
1617
CZ
PHE

369
−12.558
113.840
−76.028
1.00
50.48

ATOM
1618
C
PHE

369
−13.191
113.310
−82.466
1.00
57.86

ATOM
1619
O
PHE

369
−12.643
114.207
−83.109
1.00
58.06

ATOM
1620
N
PRO

370
−14.161
112.549
−82.997
1.00
57.46

ATOM
1621
CD
PRO

370
−14.923
111.456
−82.380
1.00
57.08

ATOM
1622
CA
PRO

370
−14.578
112.758
−84.381
1.00
58.74

ATOM
1623
CB
PRO

370
−15.851
111.930
−84.479
1.00
56.87

ATOM
1624
CG
PRO

370
−15.597
110.815
−83.562
1.00
56.30

ATOM
1625
C
PRO

370
−14.837
114.252
−84.600
1.00
61.42

ATOM
1626
O
PRO

370
−15.027
114.996
−83.633
1.00
60.59

ATOM
1627
N
ARG

371
−14.829
114.694
−85.860
1.00
63.84

ATOM
1628
CA
ARG

371
−15.067
116.103
−86.166
1.00
65.67

ATOM
1629
CB
ARG

371
−14.529
116.464
−87.567
1.00
68.73

ATOM
1630
CG
ARG

371
−13.042
116.127
−87.862
1.00
70.85

ATOM
1631
CD
ARG

371
−12.645
116.430
−89.354
1.00
73.12

ATOM
1632
NE
ARG

371
−13.489
115.727
−90.341
1.00
75.75

ATOM
1633
CZ
ARG

371
−13.244
114.522
−90.870
1.00
76.26

ATOM
1634
NH1
ARG

371
−12.153
113.835
−90.543
1.00
77.37

ATOM
1635
NH2
ARG

371
−14.120
113.978
−91.708
1.00
75.59

ATOM
1636
C
ARG

371
−16.585
116.329
−86.113
1.00
65.13

ATOM
1637
O
ARG

371
−17.051
117.381
−85.713
1.00
64.96

ATOM
1638
N
THR

372
−17.340
115.314
−86.505
1.00
64.83

ATOM
1639
CA
THR

372
−18.796
115.362
−86.517
1.00
66.68

ATOM
1640
CB
THR

372
−19.317
114.141
−87.307
1.00
66.65

ATOM
1641
OG1
THR

372
−20.589
113.722
−86.800
1.00
66.63

ATOM
1642
CG2
THR

372
−18.316
112.984
−87.205
1.00
68.01

ATOM
1643
C
THR

372
−19.458
115.402
−85.115
1.00
68.74

ATOM
1644
O
THR

372
−20.558
114.862
−84.912
1.00
69.22

ATOM
1645
N
LEU

373
−18.812
116.058
−84.151
1.00
68.80

ATOM
1646
CA
LEU

373
−19.349
116.103
−82.786
1.00
67.20

ATOM
1647
CB
LEU

373
−18.308
115.549
−81.805
1.00
67.75

ATOM
1648
CG
LEU

373
−18.834
114.570
−80.754
1.00
67.05

ATOM
1649
CD1
LEU

373
−19.565
113.431
−81.463
1.00
66.30

ATOM
1650
CD2
LEU

373
−17.700
114.043
−79.905
1.00
66.07

ATOM
1651
C
LEU

373
−19.754
117.491
−82.339
1.00
66.05

ATOM
1652
O
LEU

373
−18.989
118.434
−82.505
1.00
64.33

ATOM
1653
N
SER

374
−20.948
117.609
−81.760
1.00
65.94

ATOM
1654
CA
SER

374
−21.437
118.903
−81.281
1.00
66.63

ATOM
1655
CB
SER

374
−22.794
118.740
−80.612
1.00
66.82

ATOM
1656
OG
SER

374
−22.640
118.150
−79.329
1.00
68.04

ATOM
1657
C
SER

374
−20.435
119.443
−80.259
1.00
66.46

ATOM
1658
O
SER

374
−20.113
118.771
−79.291
1.00
67.55

ATOM
1659
N
PRO

375
−19.964
120.681
−80.439
1.00
66.35

ATOM
1660
CD
PRO

375
−20.566
121.710
−81.304
1.00
65.88

ATOM
1661
CA
PRO

375
−18.985
121.271
−79.509
1.00
65.76

ATOM
1662
CB
PRO

375
−19.020
122.761
−79.863
1.00
65.81

ATOM
1663
CG
PRO

375
−20.407
122.944
−80.470
1.00
66.57

ATOM
1664
C
PRO

375
−19.214
120.995
−78.020
1.00
65.51

ATOM
1665
O
PRO

375
−18.270
121.022
−77.221
1.00
64.18

ATOM
1666
N
GLU

376
−20.465
120.730
−77.655
1.00
65.60

ATOM
1667
CA
GLU

376
−20.807
120.427
−76.268
1.00
65.58

ATOM
1668
CB
GLU

376
−22.299
120.682
−75.995
1.00
64.87

ATOM
1669
CG
GLU

376
−23.240
120.197
−77.079
1.00
67.54

ATOM
1670
CD
GLU

376
−23.425
121.213
−78.208
1.00
69.22

ATOM
1671
OE1
GLU

376
−22.465
121.962
−78.522
1.00
69.87

ATOM
1672
OE2
GLU

376
−24.530
121.249
−78.794
1.00
67.83

ATOM
1673
C
GLU

376
−20.451
118.964
−75.950
1.00
64.54

ATOM
1674
O
GLU

376
−19.781
118.695
−74.932
1.00
64.14

ATOM
1675
N
ALA

377
−20.880
118.035
−76.817
1.00
61.55

ATOM
1676
CA
ALA

377
−20.578
116.611
−76.629
1.00
59.15

ATOM
1677
CB
ALA

377
−21.120
115.793
−77.786
1.00
58.55

ATOM
1678
C
ALA

377
−19.067
116.435
−76.512
1.00
56.95

ATOM
1679
O
ALA

377
−18.576
115.721
−75.646
1.00
56.48

ATOM
1680
N
LYS

378
−18.332
117.119
−77.374
1.00
56.10

ATOM
1681
CA
LYS

378
−16.882
117.063
−77.347
1.00
57.07

ATOM
1682
CB
LYS

378
−16.307
117.800
−78.567
1.00
59.37

ATOM
1683
CG
LYS

378
−14.766
117.884
−78.630
1.00
62.85

ATOM
1684
CD
LYS

378
−14.298
118.366
−80.020
1.00
64.41

ATOM
1685
CE
LYS

378
−12.782
118.471
−80.126
1.00
66.49

ATOM
1686
NZ
LYS

378
−12.305
118.762
−81.519
1.00
66.73

ATOM
1687
C
LYS

378
−16.347
117.663
−76.051
1.00
55.38

ATOM
1688
O
LYS

378
−15.250
117.308
−75.592
1.00
55.74

ATOM
1689
N
SER

379
−17.125
118.566
−75.457
1.00
54.04

ATOM
1690
CA
SER

379
−16.728
119.212
−74.198
1.00
51.41

ATOM
1691
CB
SER

379
−17.551
120.496
−73.934
1.00
52.13

ATOM
1692
OG
SER

379
−16.845
121.401
−73.069
1.00
50.56

ATOM
1693
C
SER

379
−16.964
118.221
−73.067
1.00
49.05

ATOM
1694
O
SER

379
−16.132
118.073
−72.169
1.00
47.48

ATOM
1695
N
LEU

380
−18.111
117.551
−73.143
1.00
45.28

ATOM
1696
CA
LEU

380
−18.497
116.564
−72.167
1.00
43.11

ATOM
1697
CB
LEU

380
−19.878
116.017
−72.526
1.00
38.76

ATOM
1698
CG
LEU

380
−20.533
115.044
−71.528
1.00
39.57

ATOM
1699
CD1
LEU

380
−20.838
115.719
−70.185
1.00
37.26

ATOM
1700
CD2
LEU

380
−21.806
114.513
−72.114
1.00
34.86

ATOM
1701
C
LEU

380
−17.436
115.429
−72.144
1.00
44.07

ATOM
1702
O
LEU

380
−16.745
115.192
−71.128
1.00
40.04

ATOM
1703
N
LEU

381
−17.309
114.736
−73.266
1.00
44.99

ATOM
1704
CA
LEU

381
−16.356
113.647
−73.349
1.00
46.41

ATOM
1705
CB
LEU

381
−16.247
113.161
−74.779
1.00
48.06

ATOM
1706
CG
LEU

381
−17.641
112.708
−75.191
1.00
49.42

ATOM
1707
CD1
LEU

381
−17.711
112.436
−76.691
1.00
48.99

ATOM
1708
CD2
LEU

381
−17.980
111.495
−74.381
1.00
48.20

ATOM
1709
C
LEU

381
−15.011
114.079
−72.834
1.00
45.89

ATOM
1710
O
LEU

381
−14.420
113.404
−72.008
1.00
47.29

ATOM
1711
N
ALA

382
−14.519
115.217
−73.285
1.00
45.76

ATOM
1712
CA
ALA

382
−13.220
115.632
−72.793
1.00
46.22

ATOM
1713
CB
ALA

382
−12.815
116.967
−73.425
1.00
45.57

ATOM
1714
C
ALA

382
−13.241
115.731
−71.263
1.00
46.30

ATOM
1715
O
ALA

382
−12.266
115.396
−70.594
1.00
46.70

ATOM
1716
N
GLY

383
−14.363
116.183
−70.710
1.00
47.25

ATOM
1717
CA
GLY

383
−14.465
116.312
−69.263
1.00
46.46

ATOM
1718
C
GLY

383
−14.568
114.980
−68.527
1.00
45.14

ATOM
1719
O
GLY

383
−13.926
114.776
−67.501
1.00
43.56

ATOM
1720
N
LEU

384
−15.384
114.075
−69.050
1.00
43.14

ATOM
1721
CA
LEU

384
−15.541
112.788
−68.432
1.00
44.46

ATOM
1722
CB
LEU

384
−16.736
112.078
−69.038
1.00
41.26

ATOM
1723
CG
LEU

384
−18.061
112.778
−68.723
1.00
40.91

ATOM
1724
CD1
LEU

384
−19.241
111.945
−69.258
1.00
36.77

ATOM
1725
CD2
LEU

384
−18.168
112.974
−67.188
1.00
39.38

ATOM
1726
C
LEU

384
−14.294
111.928
−68.593
1.00
47.06

ATOM
1727
O
LEU

384
−14.144
110.902
−67.924
1.00
50.25

ATOM
1728
N
LEU

385
−13.381
112.351
−69.459
1.00
46.08

ATOM
1729
CA
LEU

385
−12.193
111.565
−69.708
1.00
43.78

ATOM
1730
CB
LEU

385
−12.124
111.220
−71.171
1.00
40.79

ATOM
1731
CG
LEU

385
−13.379
110.487
−71.586
1.00
41.49

ATOM
1732
CD1
LEU

385
−13.433
110.335
−73.108
1.00
42.27

ATOM
1733
CD2
LEU

385
−13.395
109.163
−70.886
1.00
42.15

ATOM
1734
C
LEU

385
−10.885
112.173
−69.281
1.00
45.19

ATOM
1735
O
LEU

385
−9.840
111.689
−69.699
1.00
44.34

ATOM
1736
N
LYS

386
−10.914
113.224
−68.468
1.00
44.93

ATOM
1737
CA
LYS

386
−9.661
113.789
−68.005
1.00
48.68

ATOM
1738
CB
LYS

386
−9.910
114.978
−67.070
1.00
50.26

ATOM
1739
CG
LYS

386
−10.478
116.202
−67.757
1.00
54.40

ATOM
1740
CD
LYS

386
−9.449
116.873
−68.663
1.00
55.80

ATOM
1741
CE
LYS

386
−8.889
118.178
−68.061
1.00
59.30

ATOM
1742
NZ
LYS

386
−8.176
118.012
−66.747
1.00
59.24

ATOM
1743
C
LYS

386
−8.954
112.644
−67.258
1.00
50.22

ATOM
1744
O
LYS

386
−9.555
111.985
−66.418
1.00
49.08

ATOM
1745
N
LYS

387
−7.686
112.405
−67.575
1.00
51.70

ATOM
1746
CA
LYS

387
−6.939
111.329
−66.940
1.00
54.32

ATOM
1747
CB
LYS

387
−5.638
111.096
−67.715
1.00
53.52

ATOM
1748
CG
LYS

387
−5.908
110.577
−69.121
1.00
53.08

ATOM
1749
CD
LYS

387
−4.667
110.602
−69.989
1.00
52.12

ATOM
1750
CE
LYS

387
−4.637
109.426
−70.975
1.00
51.71

ATOM
1751
NZ
LYS

387
−5.836
109.281
−71.860
1.00
47.59

ATOM
1752
C
LYS

387
−6.670
111.596
−65.461
1.00
55.74

ATOM
1753
O
LYS

387
−6.152
110.748
−64.742
1.00
55.94

ATOM
1754
N
ASP

388
−7.041
112.783
−65.006
1.00
57.24

ATOM
1755
CA
ASP

388
−6.857
113.155
−63.608
1.00
59.65

ATOM
1756
CB
ASP

388
−6.310
114.576
−63.523
1.00
59.36

ATOM
1757
CG
ASP

388
−5.664
114.873
−62.198
1.00
60.90

ATOM
1758
OD1
ASP

388
−6.186
114.405
−61.164
1.00
62.09

ATOM
1759
OD2
ASP

388
−4.634
115.588
−62.189
1.00
61.76

ATOM
1760
C
ASP

388
−8.238
113.098
−62.946
1.00
61.18

ATOM
1761
O
ASP

388
−9.153
113.822
−63.353
1.00
61.70

ATOM
1762
N
PRO

389
−8.426
112.229
−61.932
1.00
61.74

ATOM
1763
CD
PRO

389
−7.562
111.229
−61.278
1.00
61.36

ATOM
1764
CA
PRO

389
−9.776
112.235
−61.348
1.00
61.60

ATOM
1765
CB
PRO

389
−9.720
111.105
−60.314
1.00
61.15

ATOM
1766
CG
PRO

389
−8.258
111.024
−59.954
1.00
60.71

ATOM
1767
C
PRO

389
−10.104
113.602
−60.746
1.00
61.45

ATOM
1768
O
PRO

389
−11.205
114.116
−60.914
1.00
61.30

ATOM
1769
N
LYS

390
−9.122
114.201
−60.083
1.00
61.86

ATOM
1770
CA
LYS

390
−9.290
115.501
−59.462
1.00
61.85

ATOM
1771
CB
LYS

390
−7.967
115.944
−58.824
1.00
62.78

ATOM
1772
CG
LYS

390
−7.835
115.572
−57.343
1.00
65.33

ATOM
1773
CD
LYS

390
−6.398
115.721
−56.844
1.00
69.08

ATOM
1774
CE
LYS

390
−6.316
116.072
−55.348
1.00
73.04

ATOM
1775
NZ
LYS

390
−6.920
115.057
−54.412
1.00
75.04

ATOM
1776
C
LYS

390
−9.783
116.547
−60.453
1.00
61.37

ATOM
1777
O
LYS

390
−10.512
117.472
−60.082
1.00
61.57

ATOM
1778
N
GLN

391
−9.404
116.400
−61.715
1.00
60.55

ATOM
1779
CA
GLN

391
−9.830
117.358
−62.729
1.00
59.17

ATOM
1780
CB
GLN

391
−8.670
117.734
−63.641
1.00
61.43

ATOM
1781
CG
GLN

391
−7.491
118.394
−62.966
1.00
66.61

ATOM
1782
CD
GLN

391
−6.344
118.587
−63.946
1.00
71.01

ATOM
1783
OE1
GLN

391
−6.492
119.260
−64.980
1.00
72.45

ATOM
1784
NE2
GLN

391
−5.193
117.982
−63.639
1.00
73.41

ATOM
1785
C
GLN

391
−10.961
116.851
−63.600
1.00
57.21

ATOM
1786
O
GLN

391
−11.419
117.562
−64.484
1.00
59.18

ATOM
1787
N
ARG

392
−11.426
115.633
−63.367
1.00
54.41

ATOM
1788
CA
ARG

392
−12.491
115.096
−64.203
1.00
52.12

ATOM
1789
CB
ARG

392
−12.660
113.599
−63.937
1.00
51.91

ATOM
1790
CG
ARG

392
−13.469
112.810
−64.973
1.00
50.23

ATOM
1791
CD
ARG

392
−13.170
111.289
−64.814
1.00
52.15

ATOM
1792
NE
ARG

392
−11.727
111.045
−64.788
1.00
51.60

ATOM
1793
CZ
ARG

392
−11.127
110.060
−64.127
1.00
51.35

ATOM
1794
NH1
ARG

392
−11.850
109.194
−63.431
1.00
51.78

ATOM
1795
NH2
ARG

392
−9.794
109.980
−64.121
1.00
49.46

ATOM
1796
C
ARG

392
−13.823
115.798
−64.008
1.00
51.09

ATOM
1797
O
ARG

392
−14.121
116.328
−62.947
1.00
50.99

ATOM
1798
N
LEU

393
−14.614
115.811
−65.060
1.00
49.90

ATOM
1799
CA
LEU

393
−15.924
116.386
−64.989
1.00
50.20

ATOM
1800
CB
LEU

393
−16.583
116.304
−66.362
1.00
47.21

ATOM
1801
CG
LEU

393
−17.757
117.184
−66.789
1.00
46.02

ATOM
1802
CD1
LEU

393
−18.598
116.420
−67.792
1.00
45.59

ATOM
1803
CD2
LEU

393
−18.593
117.562
−65.617
1.00
48.67

ATOM
1804
C
LEU

393
−16.630
115.436
−64.012
1.00
52.76

ATOM
1805
O
LEU

393
−16.912
114.285
−64.354
1.00
53.97

ATOM
1806
N
GLY

394
−16.903
115.902
−62.796
1.00
53.46

ATOM
1807
CA
GLY

394
−17.576
115.055
−61.826
1.00
52.91

ATOM
1808
C
GLY

394
−16.643
114.595
−60.728
1.00
52.32

ATOM
1809
O
GLY

394
−17.047
113.925
−59.780
1.00
50.61

ATOM
1810
N
GLY

395
−15.381
114.969
−60.872
1.00
53.78

ATOM
1811
CA
GLY

395
−14.374
114.592
−59.906
1.00
55.17

ATOM
1812
C
GLY

395
−14.268
115.729
−58.935
1.00
56.78

ATOM
1813
O
GLY

395
−13.474
115.705
−57.987
1.00
57.28

ATOM
1814
N
GLY

396
−15.085
116.741
−59.188
1.00
56.35

ATOM
1815
CA
GLY

396
−15.101
117.898
−58.320
1.00
56.73

ATOM
1816
C
GLY

396
−15.861
117.602
−57.042
1.00
56.84

ATOM
1817
O
GLY

396
−16.788
116.787
−57.038
1.00
53.97

ATOM
1818
N
PRO

397
−15.495
118.272
−55.940
1.00
57.58

ATOM
1819
CD
PRO

397
−14.603
119.442
−55.934
1.00
57.97

ATOM
1820
CA
PRO

397
−16.123
118.103
−54.628
1.00
58.12

ATOM
1821
CB
PRO

397
−15.501
119.228
−53.801
1.00
59.18

ATOM
1822
CG
PRO

397
−15.187
120.261
−54.817
1.00
59.66

ATOM
1823
C
PRO

397
−17.641
118.166
−54.655
1.00
57.97

ATOM
1824
O
PRO

397
−18.292
117.753
−53.703
1.00
58.47

ATOM
1825
N
SER

398
−18.188
118.677
−55.755
1.00
58.12

ATOM
1826
CA
SER

398
−19.627
118.805
−55.955
1.00
57.49

ATOM
1827
CB
SER

398
−19.910
120.019
−56.841
1.00
59.12

ATOM
1828
OG
SER

398
−21.222
119.962
−57.381
1.00
60.35

ATOM
1829
C
SER

398
−20.202
117.557
−56.613
1.00
57.12

ATOM
1830
O
SER

398
−21.421
117.424
−56.756
1.00
57.38

ATOM
1831
N
ASP

399
−19.304
116.666
−57.031
1.00
55.79

ATOM
1832
CA
ASP

399
−19.642
115.409
−57.688
1.00
53.64

ATOM
1833
CB
ASP

399
−20.239
114.408
−56.681
1.00
53.34

ATOM
1834
CG
ASP

399
−20.167
112.961
−57.175
1.00
54.18

ATOM
1835
OD1
ASP

399
−21.224
112.359
−57.451
1.00
53.28

ATOM
1836
OD2
ASP

399
−19.041
112.421
−57.295
1.00
54.72

ATOM
1837
C
ASP

399
−20.590
115.605
−58.868
1.00
52.33

ATOM
1838
O
ASP

399
−20.341
116.429
−59.720
1.00
52.52

ATOM
1839
N
ALA

400
−21.681
114.852
−58.906
1.00
50.77

ATOM
1840
CA
ALA

400
−22.631
114.931
−60.001
1.00
50.76

ATOM
1841
CB
ALA

400
−23.868
114.070
−59.687
1.00
45.81

ATOM
1842
C
ALA

400
−23.067
116.335
−60.443
1.00
52.56

ATOM
1843
O
ALA

400
−23.289
116.553
−61.625
1.00
53.16

ATOM
1844
N
LYS

401
−23.206
117.290
−59.532
1.00
54.96

ATOM
1845
CA
LYS

401
−23.634
118.619
−59.974
1.00
57.33

ATOM
1846
CB
LYS

401
−23.497
119.636
−58.838
1.00
58.45

ATOM
1847
CG
LYS

401
−24.688
119.577
−57.889
1.00
60.29

ATOM
1848
CD
LYS

401
−24.318
119.955
−56.464
1.00
62.86

ATOM
1849
CE
LYS

401
−25.286
119.355
−55.445
1.00
60.93

ATOM
1850
NZ
LYS

401
−24.950
119.774
−54.058
1.00
61.71

ATOM
1851
C
LYS

401
−22.851
119.057
−61.211
1.00
57.18

ATOM
1852
O
LYS

401
−23.438
119.391
−62.233
1.00
58.02

ATOM
1853
N
GLU

402
−21.531
119.018
−61.125
1.00
56.57

ATOM
1854
CA
GLU

402
−20.693
119.375
−62.250
1.00
57.62

ATOM
1855
CB
GLU

402
−19.246
118.959
−61.968
1.00
59.68

ATOM
1856
CG
GLU

402
−18.392
120.067
−61.410
1.00
61.99

ATOM
1857
CD
GLU

402
−17.300
119.560
−60.502
1.00
65.15

ATOM
1858
OE1
GLU

402
−16.447
118.777
−60.971
1.00
66.65

ATOM
1859
OE2
GLU

402
−17.297
119.951
−59.312
1.00
69.23

ATOM
1860
C
GLU

402
−21.155
118.733
−63.556
1.00
57.40

ATOM
1861
O
GLU

402
−21.109
119.363
−64.603
1.00
59.82

ATOM
1862
N
VAL

403
−21.594
117.482
−63.499
1.00
56.49

ATOM
1863
CA
VAL

403
−22.032
116.770
−64.700
1.00
56.82

ATOM
1864
CB
VAL

403
−21.892
115.217
−64.530
1.00
54.96

ATOM
1865
CG1
VAL

403
−22.520
114.482
−65.703
1.00
50.91

ATOM
1866
CG2
VAL

403
−20.420
114.858
−64.398
1.00
52.81

ATOM
1867
C
VAL

403
−23.455
117.115
−65.063
1.00
57.58

ATOM
1868
O
VAL

403
−23.810
117.172
−66.232
1.00
59.33

ATOM
1869
N
MET

404
−24.283
117.336
−64.061
1.00
58.50

ATOM
1870
CA
MET

404
−25.662
117.710
−64.322
1.00
59.50

ATOM
1871
CB
MET

404
−26.456
117.677
−63.028
1.00
59.06

ATOM
1872
CG
MET

404
−27.071
116.338
−62.746
1.00
60.52

ATOM
1873
SD
MET

404
−27.833
116.352
−61.173
1.00
62.79

ATOM
1874
CE
MET

404
−26.339
116.511
−60.161
1.00
60.54

ATOM
1875
C
MET

404
−25.696
119.117
−64.921
1.00
60.09

ATOM
1876
O
MET

404
−26.549
119.436
−65.745
1.00
58.33

ATOM
1877
N
GLU

405
−24.730
119.935
−64.518
1.00
61.13

ATOM
1878
CA
GLU

405
−24.634
121.308
−64.977
1.00
63.25

ATOM
1879
CB
GLU

405
−24.262
122.205
−63.807
1.00
64.98

ATOM
1880
CG
GLU

405
−25.212
122.114
−62.663
1.00
68.67

ATOM
1881
CD
GLU

405
−24.829
123.062
−61.576
1.00
71.27

ATOM
1882
OE1
GLU

405
−23.642
123.033
−61.169
1.00
72.33

ATOM
1883
OE2
GLU

405
−25.708
123.836
−61.134
1.00
73.78

ATOM
1884
C
GLU

405
−23.659
121.578
−66.126
1.00
63.54

ATOM
1885
O
GLU

405
−23.259
122.734
−66.339
1.00
64.29

ATOM
1886
N
HIS

406
−23.262
120.537
−66.858
1.00
61.74

ATOM
1887
CA
HIS

406
−22.364
120.746
−67.988
1.00
58.19

ATOM
1888
CB
HIS

406
−21.586
119.475
−68.369
1.00
53.04

ATOM
1889
CG
HIS

406
−20.810
119.609
−69.645
1.00
47.77

ATOM
1890
CD2
HIS

406
−19.573
120.110
−69.886
1.00
45.07

ATOM
1891
ND1
HIS

406
−21.345
119.294
−70.879
1.00
44.27

ATOM
1892
CE1
HIS

406
−20.472
119.601
−71.824
1.00
44.31

ATOM
1893
NE2
HIS

406
−19.390
120.099
−71.250
1.00
43.15

ATOM
1894
C
HIS

406
−23.187
121.185
−69.181
1.00
58.97

ATOM
1895
O
HIS

406
−24.339
120.764
−69.355
1.00
57.85

ATOM
1896
N
ARG

407
−22.564
122.028
−69.998
1.00
59.59

ATOM
1897
CA
ARG

407
−23.167
122.565
−71.205
1.00
60.40

ATOM
1898
CB
ARG

407
−22.063
123.126
−72.112
1.00
62.98

ATOM
1899
CG
ARG

407
−22.553
123.584
−73.474
1.00
67.27

ATOM
1900
CD
ARG

407
−21.392
124.001
−74.366
1.00
72.05

ATOM
1901
NE
ARG

407
−21.840
124.293
−75.730
1.00
77.01

ATOM
1902
CZ
ARG

407
−21.165
125.042
−76.602
1.00
79.85

ATOM
1903
NH1
ARG

407
−19.997
125.589
−76.257
1.00
80.74

ATOM
1904
NH2
ARG

407
−21.661
125.245
−77.822
1.00
80.37

ATOM
1905
C
ARG

407
−24.010
121.542
−71.976
1.00
58.41

ATOM
1906
O
ARG

407
−25.114
121.874
−72.432
1.00
58.61

ATOM
1907
N
PHE

408
−23.492
120.315
−72.116
1.00
54.72

ATOM
1908
CA
PHE

408
−24.175
119.246
−72.852
1.00
51.67

ATOM
1909
CB
PHE

408
−23.315
117.953
−72.912
1.00
50.96

ATOM
1910
CG
PHE

408
−24.011
116.792
−73.614
1.00
45.30

ATOM
1911
CD1
PHE

408
−24.103
116.753
−74.996
1.00
44.86

ATOM
1912
CD2
PHE

408
−24.700
115.834
−72.880
1.00
41.97

ATOM
1913
CE1
PHE

408
−24.881
115.780
−75.643
1.00
44.63

ATOM
1914
CE2
PHE

408
−25.483
114.860
−73.509
1.00
40.86

ATOM
1915
CZ
PHE

408
−25.574
114.834
−74.896
1.00
42.82

ATOM
1916
C
PHE

408
−25.531
118.877
−72.290
1.00
52.59

ATOM
1917
O
PHE

408
−26.377
118.361
−73.012
1.00
50.75

ATOM
1918
N
PHE

409
−25.736
119.142
−71.002
1.00
53.94

ATOM
1919
CA
PHE

409
−26.978
118.776
−70.338
1.00
56.44

ATOM
1920
CB
PHE

409
−26.654
118.021
−69.038
1.00
56.94

ATOM
1921
CG
PHE

409
−26.034
116.651
−69.239
1.00
55.15

ATOM
1922
CD1
PHE

409
−26.776
115.598
−69.778
1.00
53.68

ATOM
1923
CD2
PHE

409
−24.736
116.398
−68.810
1.00
54.15

ATOM
1924
CE1
PHE

409
−26.237
114.318
−69.873
1.00
51.49

ATOM
1925
CE2
PHE

409
−24.195
115.116
−68.905
1.00
53.05

ATOM
1926
CZ
PHE

409
−24.955
114.081
−69.437
1.00
49.81

ATOM
1927
C
PHE

409
−27.939
119.926
−70.009
1.00
58.91

ATOM
1928
O
PHE

409
−28.336
120.095
−68.846
1.00
58.32

ATOM
1929
N
LEU

410
−28.327
120.705
−71.018
1.00
60.17

ATOM
1930
CA
LEU

410
−29.252
121.819
−70.797
1.00
61.03

ATOM
1931
CB
LEU

410
−29.066
122.887
−71.868
1.00
62.18

ATOM
1932
CG
LEU

410
−30.276
123.781
−72.119
1.00
62.82

ATOM
1933
CD1
LEU

410
−29.781
125.191
−72.337
1.00
63.59

ATOM
1934
CD2
LEU

410
−31.095
123.263
−73.314
1.00
61.19

ATOM
1935
C
LEU

410
−30.710
121.381
−70.788
1.00
60.51

ATOM
1936
O
LEU

410
−31.413
121.574
−69.799
1.00
61.04

ATOM
1937
N
SER

411
−31.149
120.802
−71.898
1.00
59.14

ATOM
1938
CA
SER

411
−32.512
120.323
−72.058
1.00
59.17

ATOM
1939
CB
SER

411
−32.659
119.679
−73.426
1.00
61.25

ATOM
1940
OG
SER

411
−31.790
118.557
−73.550
1.00
62.98

ATOM
1941
C
SER

411
−32.864
119.277
−71.020
1.00
59.35

ATOM
1942
O
SER

411
−33.792
118.484
−71.213
1.00
59.64

ATOM
1943
N
ILE

412
−32.137
119.275
−69.914
1.00
58.52

ATOM
1944
CA
ILE

412
−32.347
118.256
−68.909
1.00
57.09

ATOM
1945
CB
ILE

412
−30.965
117.681
−68.469
1.00
55.80

ATOM
1946
CG2
ILE

412
−31.129
116.665
−67.341
1.00
54.27

ATOM
1947
CG1
ILE

412
−30.279
117.039
−69.687
1.00
53.36

ATOM
1948
CD1
ILE

412
−31.207
116.117
−70.531
1.00
47.19

ATOM
1949
C
ILE

412
−33.180
118.611
−67.697
1.00
56.60

ATOM
1950
O
ILE

412
−32.866
119.527
−66.946
1.00
56.94

ATOM
1951
N
ASN

413
−34.256
117.859
−67.516
1.00
56.83

ATOM
1952
CA
ASN

413
−35.139
118.054
−66.374
1.00
56.44

ATOM
1953
CB
ASN

413
−36.609
118.029
−66.807
1.00
56.52

ATOM
1954
CG
ASN

413
−37.497
118.734
−65.807
1.00
57.09

ATOM
1955
OD1
ASN

413
−38.330
118.116
−65.126
1.00
54.58

ATOM
1956
ND2
ASN

413
−37.297
120.044
−65.687
1.00
58.16

ATOM
1957
C
ASN

413
−34.870
116.926
−65.375
1.00
54.26

ATOM
1958
O
ASN

413
−35.589
115.909
−65.336
1.00
50.66

ATOM
1959
N
TRP

414
−33.838
117.132
−64.564
1.00
54.29

ATOM
1960
CA
TRP

414
−33.406
116.132
−63.596
1.00
56.88

ATOM
1961
CB
TRP

414
−32.261
116.699
−62.759
1.00
59.59

ATOM
1962
CG
TRP

414
−31.001
116.991
−63.578
1.00
65.04

ATOM
1963
CD2
TRP

414
−30.231
116.061
−64.370
1.00
66.58

ATOM
1964
CE2
TRP

414
−29.129
116.778
−64.904
1.00
67.20

ATOM
1965
CE3
TRP

414
−30.363
114.705
−64.677
1.00
67.03

ATOM
1966
CD1
TRP

414
−30.348
118.190
−63.671
1.00
67.27

ATOM
1967
NE1
TRP

414
−29.226
118.067
−64.465
1.00
68.59

ATOM
1968
CZ2
TRP

414
−28.161
116.172
−65.725
1.00
65.83

ATOM
1969
CZ3
TRP

414
−29.391
114.105
−65.502
1.00
67.18

ATOM
1970
CH2
TRP

414
−28.309
114.844
−66.011
1.00
65.33

ATOM
1971
C
TRP

414
−34.481
115.516
−62.699
1.00
56.82

ATOM
1972
O
TRP

414
−34.258
114.480
−62.116
1.00
58.02

ATOM
1973
N
GLN

415
−35.653
116.136
−62.605
1.00
57.42

ATOM
1974
CA
GLN

415
−36.733
115.608
−61.782
1.00
54.54

ATOM
1975
CB
GLN

415
−37.658
116.724
−61.304
1.00
54.51

ATOM
1976
CG
GLN

415
−37.491
117.064
−59.868
1.00
53.45

ATOM
1977
CD
GLN

415
−38.620
117.895
−59.319
1.00
52.95

ATOM
1978
OE1
GLN

415
−39.775
117.483
−59.319
1.00
55.09

ATOM
1979
NE2
GLN

415
−38.286
119.064
−58.821
1.00
52.40

ATOM
1980
C
GLN

415
−37.532
114.650
−62.619
1.00
55.66

ATOM
1981
O
GLN

415
−38.101
113.698
−62.108
1.00
54.58

ATOM
1982
N
ASP

416
−37.585
114.917
−63.916
1.00
56.96

ATOM
1983
CA
ASP

416
−38.328
114.061
−64.827
1.00
59.08

ATOM
1984
CB
ASP

416
−38.469
114.714
−66.189
1.00
63.17

ATOM
1985
CG
ASP

416
−39.587
115.700
−66.232
1.00
65.07

ATOM
1986
OD1
ASP

416
−40.718
115.322
−65.832
1.00
66.66

ATOM
1987
OD2
ASP

416
−39.326
116.841
−66.673
1.00
65.92

ATOM
1988
C
ASP

416
−37.632
112.747
−65.012
1.00
58.15

ATOM
1989
O
ASP

416
−38.271
111.713
−65.194
1.00
57.45

ATOM
1990
N
VAL

417
−36.308
112.807
−64.992
1.00
58.07

ATOM
1991
CA
VAL

417
−35.494
111.611
−65.141
1.00
57.45

ATOM
1992
CB
VAL

417
−34.027
111.919
−65.001
1.00
56.19

ATOM
1993
CG1
VAL

417
−33.252
110.664
−65.241
1.00
57.02

ATOM
1994
CG2
VAL

417
−33.627
113.023
−65.970
1.00
54.44

ATOM
1995
C
VAL

417
−35.845
110.580
−64.084
1.00
57.37

ATOM
1996
O
VAL

417
−36.406
109.539
−64.411
1.00
57.05

ATOM
1997
N
VAL

418
−35.535
110.876
−62.820
1.00
57.88

ATOM
1998
CA
VAL

418
−35.821
109.929
−61.739
1.00
60.11

ATOM
1999
CB
VAL

418
−35.553
110.522
−60.343
1.00
58.28

ATOM
2000
CG1
VAL

418
−34.146
110.989
−60.244
1.00
58.15

ATOM
2001
CG2
VAL

418
−36.505
111.658
−60.077
1.00
59.19

ATOM
2002
C
VAL

418
−37.276
109.530
−61.780
1.00
61.81

ATOM
2003
O
VAL

418
−37.676
108.486
−61.247
1.00
63.52

ATOM
2004
N
GLN

419
−38.068
110.368
−62.425
1.00
61.85

ATOM
2005
CA
GLN

419
−39.484
110.117
−62.501
1.00
65.20

ATOM
2006
CB
GLN

419
−40.211
111.459
−62.562
1.00
66.41

ATOM
2007
CG
GLN

419
−40.141
112.262
−61.265
1.00
67.19

ATOM
2008
CD
GLN

419
−40.918
111.616
−60.145
1.00
69.64

ATOM
2009
OE1
GLN

419
−42.108
111.329
−60.284
1.00
72.38

ATOM
2010
NE2
GLN

419
−40.254
111.386
−59.021
1.00
70.84

ATOM
2011
C
GLN

419
−39.925
109.210
−63.651
1.00
66.54

ATOM
2012
O
GLN

419
−41.101
108.862
−63.743
1.00
67.18

ATOM
2013
N
LYS

420
−38.986
108.798
−64.502
1.00
68.03

ATOM
2014
CA
LYS

420
−39.314
107.959
−65.651
1.00
67.91

ATOM
2015
CB
LYS

420
−39.885
106.610
−65.199
1.00
67.82

ATOM
2016
CG
LYS

420
−38.854
105.707
−64.557
1.00
67.76

ATOM
2017
CD
LYS

420
−39.145
104.232
−64.797
1.00
66.82

ATOM
2018
CE
LYS

420
−37.855
103.439
−64.661
1.00
67.85

ATOM
2019
NZ
LYS

420
−38.036
101.982
−64.890
1.00
66.83

ATOM
2020
C
LYS

420
−40.347
108.738
−66.454
1.00
68.30

ATOM
2021
O
LYS

420
−41.243
108.172
−67.099
1.00
67.93

ATOM
2022
N
LYS

421
−40.200
110.055
−66.382
1.00
68.73

ATOM
2023
CA
LYS

421
−41.084
110.993
−67.052
1.00
70.80

ATOM
2024
CB
LYS

421
−41.093
112.333
−66.302
1.00
72.18

ATOM
2025
CG
LYS

421
−42.469
112.725
−65.754
1.00
75.21

ATOM
2026
CD
LYS

421
−43.105
111.599
−64.918
1.00
77.43

ATOM
2027
CE
LYS

421
−44.591
111.858
−64.618
1.00
78.67

ATOM
2028
NZ
LYS

421
−44.864
113.113
−63.853
1.00
79.81

ATOM
2029
C
LYS

421
−40.679
111.199
−68.505
1.00
70.49

ATOM
2030
O
LYS

421
−41.530
111.117
−69.395
1.00
70.30

ATOM
2031
N
LEU

422
−39.394
111.465
−68.750
1.00
69.36

ATOM
2032
CA
LEU

422
−38.923
111.652
−70.122
1.00
67.65

ATOM
2033
CB
LEU

422
−37.397
111.583
−70.210
1.00
66.12

ATOM
2034
CG
LEU

422
−36.538
112.611
−69.467
1.00
66.13

ATOM
2035
CD1
LEU

422
−35.097
112.377
−69.864
1.00
65.76

ATOM
2036
CD2
LEU

422
−36.942
114.039
−69.801
1.00
65.12

ATOM
2037
C
LEU

422
−39.505
110.525
−70.959
1.00
66.67

ATOM
2038
O
LEU

422
−39.916
109.488
−70.428
1.00
65.65

ATOM
2039
N
LEU

423
−39.579
110.733
−72.263
1.00
66.27

ATOM
2040
CA
LEU

423
−40.096
109.688
−73.121
1.00
66.60

ATOM
2041
CB
LEU

423
−40.965
110.266
−74.254
1.00
65.11

ATOM
2042
CG
LEU

423
−41.521
109.187
−75.209
1.00
65.13

ATOM
2043
CD1
LEU

423
−42.684
108.433
−74.548
1.00
62.44

ATOM
2044
CD2
LEU

423
−41.961
109.815
−76.513
1.00
64.03

ATOM
2045
C
LEU

423
−38.883
108.956
−73.698
1.00
66.75

ATOM
2046
O
LEU

423
−37.938
109.577
−74.183
1.00
67.08

ATOM
2047
N
PRO

424
−38.879
107.626
−73.627
1.00
67.08

ATOM
2048
CD
PRO

424
−39.933
106.682
−73.206
1.00
67.32

ATOM
2049
CA
PRO

424
−37.723
106.922
−74.181
1.00
67.83

ATOM
2050
CB
PRO

424
−38.013
105.464
−73.824
1.00
67.11

ATOM
2051
CG
PRO

424
−39.525
105.402
−73.908
1.00
67.45

ATOM
2052
C
PRO

424
−37.682
107.168
−75.694
1.00
68.28

ATOM
2053
O
PRO

424
−38.681
106.942
−76.391
1.00
68.67

ATOM
2054
N
PRO

425
−36.543
107.668
−76.212
1.00
67.74

ATOM
2055
CD
PRO

425
−35.442
108.255
−75.431
1.00
67.36

ATOM
2056
CA
PRO

425
−36.367
107.948
−77.643
1.00
67.05

ATOM
2057
CB
PRO

425
−34.996
108.641
−77.706
1.00
66.39

ATOM
2058
CG
PRO

425
−34.327
108.260
−76.431
1.00
66.57

ATOM
2059
C
PRO

425
−36.461
106.728
−78.556
1.00
66.83

ATOM
2060
O
PRO

425
−36.675
106.851
−79.760
1.00
67.38

ATOM
2061
N
PHE

426
−36.294
105.549
−77.984
1.00
66.92

ATOM
2062
CA
PHE

426
−36.392
104.322
−78.752
1.00
67.44

ATOM
2063
CB
PHE

426
−35.000
103.789
−79.085
1.00
68.71

ATOM
2064
CG
PHE

426
−34.976
102.330
−79.402
1.00
68.61

ATOM
2065
CD1
PHE

426
−35.783
101.811
−80.402
1.00
68.75

ATOM
2066
CD2
PHE

426
−34.213
101.462
−78.641
1.00
68.76

ATOM
2067
CE1
PHE

426
−35.840
100.443
−80.632
1.00
69.27

ATOM
2068
CE2
PHE

426
−34.263
100.096
−78.862
1.00
69.47

ATOM
2069
CZ
PHE

426
−35.081
99.583
−79.860
1.00
69.98

ATOM
2070
C
PHE

426
−37.143
103.355
−77.864
1.00
68.25

ATOM
2071
O
PHE

426
−36.813
103.201
−76.692
1.00
69.44

ATOM
2072
N
LYS

427
−38.158
102.706
−78.403
1.00
68.40

ATOM
2073
CA
LYS

427
−38.933
101.802
−77.588
1.00
70.12

ATOM
2074
CB
LYS

427
−40.401
102.215
−77.609
1.00
71.43

ATOM
2075
CG
LYS

427
−41.350
101.193
−77.006
1.00
74.17

ATOM
2076
CD
LYS

427
−42.120
101.795
−75.838
1.00
76.63

ATOM
2077
CE
LYS

427
−43.040
100.776
−75.170
1.00
76.97

ATOM
2078
NZ
LYS

427
−43.801
101.410
−74.046
1.00
77.57

ATOM
2079
C
LYS

427
−38.824
100.355
−77.997
1.00
71.38

ATOM
2080
O
LYS

427
−39.300
99.971
−79.064
1.00
71.46

ATOM
2081
N
PRO

428
−38.187
99.526
−77.148
1.00
72.96

ATOM
2082
CD
PRO

428
−37.468
99.936
−75.928
1.00
72.02

ATOM
2083
CA
PRO

428
−38.008
98.091
−77.395
1.00
73.63

ATOM
2084
CB
PRO

428
−37.523
97.583
−76.053
1.00
73.04

ATOM
2085
CG
PRO

428
−36.640
98.716
−75.610
1.00
72.25

ATOM
2086
C
PRO

428
−39.351
97.507
−77.798
1.00
75.14

ATOM
2087
O
PRO

428
−40.396
98.005
−77.383
1.00
75.21

ATOM
2088
N
GLN

429
−39.322
96.449
−78.593
1.00
76.75

ATOM
2089
CA
GLN

429
−40.551
95.865
−79.100
1.00
79.71

ATOM
2090
CB
GLN

429
−40.317
95.497
−80.571
1.00
80.94

ATOM
2091
CG
GLN

429
−39.747
96.692
−81.355
1.00
82.23

ATOM
2092
CD
GLN

429
−38.917
96.322
−82.589
1.00
84.38

ATOM
2093
OE1
GLN

429
−38.118
95.374
−82.572
1.00
84.60

ATOM
2094
NE2
GLN

429
−39.084
97.098
−83.662
1.00
84.18

ATOM
2095
C
GLN

429
−41.156
94.703
−78.317
1.00
81.21

ATOM
2096
O
GLN

429
−41.342
93.611
−78.850
1.00
81.60

ATOM
2097
N
VAL

430
−41.498
94.955
−77.055
1.00
83.92

ATOM
2098
CA
VAL

430
−42.097
93.922
−76.206
1.00
87.13

ATOM
2099
CB
VAL

430
−41.211
93.626
−74.961
1.00
86.96

ATOM
2100
CG1
VAL

430
−39.913
92.962
−75.395
1.00
87.00

ATOM
2101
CG2
VAL

430
−40.923
94.908
−74.201
1.00
86.29

ATOM
2102
C
VAL

430
−43.519
94.251
−75.722
1.00
89.08

ATOM
2103
O
VAL

430
−43.827
95.411
−75.408
1.00
89.39

ATOM
2104
N
THR

431
−44.372
93.221
−75.671
1.00
90.54

ATOM
2105
CA
THR

431
−45.769
93.353
−75.223
1.00
91.77

ATOM
2106
CB
THR

431
−46.566
92.037
−75.446
1.00
91.58

ATOM
2107
OG1
THR

431
−46.459
91.626
−76.814
1.00
90.98

ATOM
2108
CG2
THR

431
−48.038
92.237
−75.094
1.00
92.07

ATOM
2109
C
THR

431
−45.789
93.658
−73.726
1.00
92.67

ATOM
2110
O
THR

431
−46.132
94.764
−73.295
1.00
91.94

ATOM
2111
N
SER

432
−45.419
92.645
−72.946
1.00
94.41

ATOM
2112
CA
SER

432
−45.351
92.739
−71.491
1.00
95.94

ATOM
2113
CB
SER

432
−46.421
91.850
−70.844
1.00
95.92

ATOM
2114
OG
SER

432
−46.179
90.474
−71.095
1.00
96.12

ATOM
2115
C
SER

432
−43.965
92.270
−71.055
1.00
96.83

ATOM
2116
O
SER

432
−43.225
91.683
−71.851
1.00
97.29

ATOM
2117
N
GLU

433
−43.615
92.524
−69.797
1.00
97.40

ATOM
2118
CA
GLU

433
−42.314
92.119
−69.278
1.00
98.03

ATOM
2119
CB
GLU

433
−42.152
92.608
−67.836
1.00
98.40

ATOM
2120
CG
GLU

433
−43.433
92.581
−67.033
1.00
100.35

ATOM
2121
CD
GLU

433
−43.393
93.526
−65.847
1.00
101.56

ATOM
2122
OE1
GLU

433
−42.595
93.289
−64.910
1.00
102.03

ATOM
2123
OE2
GLU

433
−44.164
94.513
−65.859
1.00
102.14

ATOM
2124
C
GLU

433
−42.084
90.610
−69.369
1.00
98.07

ATOM
2125
O
GLU

433
−40.996
90.119
−69.064
1.00
97.73

ATOM
2126
N
VAL

434
−43.108
89.882
−69.805
1.00
98.00

ATOM
2127
CA
VAL

434
−43.014
88.436
−69.958
1.00
98.10

ATOM
2128
CB
VAL

434
−44.341
87.748
−69.603
1.00
98.68

ATOM
2129
CG1
VAL

434
−44.198
86.239
−69.712
1.00
98.59

ATOM
2130
CG2
VAL

434
−44.761
88.148
−68.203
1.00
99.00

ATOM
2131
C
VAL

434
−42.673
88.111
−71.405
1.00
97.97

ATOM
2132
O
VAL

434
−42.399
86.960
−71.742
1.00
98.01

ATOM
2133
N
ASP

435
−42.703
89.132
−72.258
0.00
98.37

ATOM
2134
CA
ASP

435
−42.385
88.963
−73.671
1.00
98.70

ATOM
2135
CB
ASP

435
−42.677
90.264
−74.434
1.00
99.53

ATOM
2136
CG
ASP

435
−42.591
90.090
−75.940
1.00
100.16

ATOM
2137
OD1
ASP

435
−43.270
89.187
−76.471
1.00
100.60

ATOM
2138
OD2
ASP

435
−41.849
90.858
−76.594
1.00
100.18

ATOM
2139
C
ASP

435
−40.901
88.600
−73.749
1.00
98.21

ATOM
2140
O
ASP

435
−40.027
89.463
−73.678
1.00
96.94

ATOM
2141
N
THR

436
−40.628
87.310
−73.898
1.00
98.29

ATOM
2142
CA
THR

436
−39.259
86.817
−73.935
1.00
98.83

ATOM
2143
CB
THR

436
−39.177
85.398
−73.327
1.00
98.41

ATOM
2144
OG1
THR

436
−39.806
84.458
−74.208
1.00
98.06

ATOM
2145
CG2
THR

436
−39.869
85.360
−71.979
1.00
97.72

ATOM
2146
C
THR

436
−38.584
86.764
−75.299
1.00
99.29

ATOM
2147
O
THR

436
−37.995
85.739
−75.650
1.00
99.89

ATOM
2148
N
ARG

437
−38.637
87.844
−76.072
1.00
99.63

ATOM
2149
CA
ARG

437
−37.990
87.788
−77.376
1.00
100.28

ATOM
2150
CB
ARG

437
−38.763
88.587
−78.429
1.00
101.13

ATOM
2151
CG
ARG

437
−38.677
90.098
−78.355
1.00
101.69

ATOM
2152
CD
ARG

437
−39.574
90.642
−79.444
1.00
102.76

ATOM
2153
NE
ARG

437
−40.849
89.921
−79.422
1.00
104.17

ATOM
2154
CZ
ARG

437
−41.742
89.912
−80.409
1.00
104.28

ATOM
2155
NH1
ARG

437
−41.514
90.593
−81.525
1.00
104.34

ATOM
2156
NH2
ARG

437
−42.861
89.207
−80.283
1.00
103.71

ATOM
2157
C
ARG

437
−36.546
88.239
−77.343
1.00
100.10

ATOM
2158
O
ARG

437
−35.704
87.652
−78.019
1.00
100.44

ATOM
2159
N
TYR

438
−36.246
89.265
−76.557
1.00
99.91

ATOM
2160
CA
TYR

438
−34.871
89.738
−76.477
1.00
100.03

ATOM
2161
CB
TYR

438
−34.802
91.122
−75.831
1.00
99.89

ATOM
2162
CG
TYR

438
−35.278
92.236
−76.727
1.00
99.94

ATOM
2163
CD1
TYR

438
−36.610
92.645
−76.719
1.00
99.48

ATOM
2164
CE1
TYR

438
−37.055
93.650
−77.567
1.00
99.75

ATOM
2165
CD2
TYR

438
−34.398
92.865
−77.611
1.00
100.01

ATOM
2166
CE2
TYR

438
−34.831
93.869
−78.466
1.00
99.53

ATOM
2167
CZ
TYR

438
−36.160
94.255
−78.440
1.00
99.78

ATOM
2168
OH
TYR

438
−36.599
95.234
−79.300
1.00
101.08

ATOM
2169
C
TYR

438
−33.987
88.776
−75.695
1.00
100.06

ATOM
2170
O
TYR

438
−32.919
89.164
−75.221
1.00
100.26

ATOM
2171
N
PHE

439
−34.426
87.524
−75.569
1.00
99.97

ATOM
2172
CA
PHE

439
−33.662
86.522
−74.830
1.00
100.18

ATOM
2173
CB
PHE

439
−34.596
85.725
−73.910
1.00
99.09

ATOM
2174
CG
PHE

439
−35.216
86.547
−72.796
1.00
98.42

ATOM
2175
CD1
PHE

439
−36.189
85.994
−71.967
1.00
98.25

ATOM
2176
CD2
PHE

439
−34.833
87.868
−72.577
1.00
98.50

ATOM
2177
CE1
PHE

439
−36.773
86.739
−70.943
1.00
97.85

ATOM
2178
CE2
PHE

439
−35.411
88.620
−71.557
1.00
97.63

ATOM
2179
CZ
PHE

439
−36.382
88.052
−70.739
1.00
97.96

ATOM
2180
C
PHE

439
−32.857
85.571
−75.717
1.00
100.83

ATOM
2181
O
PHE

439
−32.461
84.495
−75.279
1.00
100.96

ATOM
2182
N
ASP

440
−32.615
85.975
−76.961
1.00
102.02

ATOM
2183
CA
ASP

440
−31.832
85.177
−77.902
1.00
103.27

ATOM
2184
CB
ASP

440
−32.709
84.713
−79.066
1.00
103.42

ATOM
2185
CG
ASP

440
−33.772
83.719
−78.633
1.00
103.54

ATOM
2186
OD1
ASP

440
−34.618
84.083
−77.791
1.00
103.91

ATOM
2187
OD2
ASP

440
−33.761
82.574
−79.133
1.00
103.74

ATOM
2188
C
ASP

440
−30.650
86.010
−78.415
1.00
104.64

ATOM
2189
O
ASP

440
−29.738
86.315
−77.644
1.00
105.47

ATOM
2190
N
ASP

441
−30.654
86.381
−79.698
1.00
105.56

ATOM
2191
CA
ASP

441
−29.563
87.193
−80.259
1.00
106.36

ATOM
2192
CB
ASP

441
−28.606
86.330
−81.085
1.00
107.59

ATOM
2193
CG
ASP

441
−27.486
85.745
−80.257
1.00
108.98

ATOM
2194
OD1
ASP

441
−27.749
84.815
−79.459
1.00
109.39

ATOM
2195
OD2
ASP

441
−26.339
86.227
−80.405
1.00
109.38

ATOM
2196
C
ASP

441
−30.034
88.355
−81.129
1.00
106.32

ATOM
2197
O
ASP

441
−29.458
88.538
−82.226
1.00
105.62

ATOM
2198
OXT
ASP

441
−30.956
89.080
−80.694
1.00
106.44

ATOM
2199
OH2
TIP
S
1
−27.623
117.071
−74.436
1.00
50.08
S

ATOM
2200
OH2
TIP
S
2
−6.363
114.551
−69.692
1.00
52.44
S

ATOM
2201
OH2
TIP
S
3
−30.995
107.519
−76.234
1.00
49.63
S

ATOM
2202
OH2
TIP
S
4
−14.629
98.513
−69.834
1.00
49.61
S

ATOM
2203
OH2
TIP
S
5
−20.407
90.237
−73.881
1.00
46.15
S

ATOM
2204
OH2
TIP
S
6
−42.857
114.573
−63.472
1.00
98.81
S

ATOM
2205
OH2
TIP
S
7
−32.915
115.097
−69.111
1.00
49.65
S

ATOM
2206
OH2
TIP
S
8
−24.764
110.454
−73.650
1.00
61.01
S

ATOM
2207
OH2
TIP
S
9
−23.310
107.488
−74.515
1.00
109.59
S

ATOM
2208
OH2
TIP
S
10
−10.718
83.937
−50.781
1.00
57.03
S

ATOM
2209
OH2
TIP
S
11
−20.355
123.203
−69.628
1.00
57.71
S

ATOM
2210
OH2
TIP
S
12
−29.683
79.225
−62.379
1.00
60.08
S

ATOM
2211
OH2
TIP
S
13
−15.022
108.281
−72.715
1.00
101.82
S

ATOM
2212
OH2
TIP
S
14
−30.449
120.422
−66.954
1.00
51.43
S

ATOM
2213
OH2
TIP
S
15
−20.564
93.070
−63.487
1.00
56.25
S

ATOM
2214
OH2
TIP
S
16
−15.157
102.558
−64.601
1.00
29.10
S

ATOM
2215
OH2
TIP
S
17
−17.616
103.074
−63.099
1.00
38.17
S

ATOM
2216
OH2
TIP
S
18
−2.634
106.999
−59.689
1.00
45.82
S

ATOM
2217
OH2
TIP
S
19
−39.218
100.823
−60.421
1.00
67.49
S

ATOM
2218
OH2
TIP
S
20
−23.554
97.041
−63.102
1.00
56.11
S

ATOM
2219
OH2
TIP
S
21
−24.036
113.009
−71.653
1.00
115.47
S

ATOM
2220
OH2
TIP
S
22
−17.643
98.286
−74.324
1.00
46.61
S

ATOM
2221
OH2
TIP
S
23
−4.263
95.763
−72.959
1.00
63.95
S

ATOM
2222
OH2
TIP
S
24
−25.175
95.708
−73.068
1.00
52.58
S

ATOM
2223
OH2
TIP
S
25
−31.683
109.565
−81.647
1.00
71.71
S

ATOM
2224
OH2
TIP
S
26
−31.483
113.973
−74.194
1.00
38.69
S

ATOM
2225
OH2
TIP
S
27
−17.619
102.102
−52.493
1.00
44.50
S

ATOM
2226
OH2
TIP
S
28
−25.520
91.421
−58.993
1.00
84.60
S

ATOM
2227
OH2
TIP
S
29
−25.401
74.677
−52.567
1.00
99.27
S

ATOM
2228
OH2
TIP
S
30
−19.973
111.319
−52.542
1.00
49.17
S

ATOM
2229
OH2
TIP
S
31
−29.000
120.084
−73.348
1.00
55.97
S

ATOM
2230
OH2
TIP
S
32
−17.714
100.955
−71.187
1.00
62.36
S

ATOM
2231
OH2
TIP
S
33
−3.482
98.885
−78.668
1.00
109.07
S

ATOM
2232
OH2
TIP
S
34
−50.390
95.737
−54.746
1.00
55.63
S

ATOM
2233
OH2
TIP
S
35
−22.101
73.825
−55.182
1.00
108.71
S

ATOM
2234
OH2
TIP
S
36
−18.664
123.812
−72.193
1.00
49.19
S

ATOM
2235
OH2
TIP
S
37
−28.743
117.565
−72.160
1.00
136.28
S

ATOM
2236
OH2
TIP
S
38
−22.769
112.806
−73.840
1.00
62.32
S

ATOM
2237
OH2
TIP
S
39
−36.606
111.229
−74.968
1.00
64.70
S

ATOM
2238
OH2
TIP
S
40
−31.320
98.646
−45.930
1.00
103.40
S

ATOM
2239
OH2
TIP
S
41
−13.865
127.291
−55.664
1.00
68.04
S

ATOM
2240
OH2
TIP
S
42
−25.892
121.805
−67.521
1.00
63.93
S

ATOM
2241
OH2
TIP
S
43
−27.862
122.177
−61.186
1.00
53.75
S

ATOM
2242
OH2
TIP
S
44
−21.137
80.560
−57.614
1.00
97.15
S

ATOM
2243
OH2
TIP
S
45
−28.633
118.831
−66.826
1.00
127.75
S

ATOM
2244
OH2
TIP
S
46
−15.616
96.600
−54.071
1.00
71.96
S

ATOM
2245
OH2
TIP
S
47
−15.464
112.410
−79.938
1.00
103.12
S

ATOM
2246
OH2
TIP
S
48
−27.144
117.541
−79.370
1.00
38.56
S

ATOM
2247
OH2
TIP
S
49
−18.430
94.208
−65.102
1.00
94.29
S

ATOM
2248
OH2
TIP
S
50
−41.024
98.946
−60.461
1.00
56.05
S

ATOM
2249
OH2
TIP
S
51
−22.575
92.336
−82.496
1.00
62.33
S

ATOM
2250
OH2
TIP
S
52
−27.415
89.929
−85.543
1.00
54.98
S

ATOM
2251
OH2
TIP
S
53
−18.120
123.217
−57.412
1.00
70.50
S

ATOM
2252
OH2
TIP
S
54
−18.647
93.038
−70.008
1.00
62.14
S

ATOM
2253
OH2
TIP
S
55
−34.891
116.991
−69.553
1.00
71.14
S

ATOM
2254
OH2
TIP
S
56
−24.452
109.908
−62.339
1.00
82.11
S

ATOM
2255
OH2
TIP
S
57
−9.140
95.619
−78.673
1.00
59.11
S

ATOM
2256
OH2
TIP
S
58
−22.630
77.355
−64.914
1.00
54.06
S

ATOM
2257
OH2
TIP
S
59
−21.707
107.688
−76.681
1.00
80.24
S

ATOM
2258
OH2
TIP
S
60
−25.218
92.131
−45.479
1.00
65.39
S

ATOM
2259
OH2
TIP
S
61
−33.478
91.675
−72.540
1.00
45.17
S

ATOM
2260
OH2
TIP
S
62
−6.638
100.525
−89.582
1.00
57.51
S

ATOM
2261
OH2
TIP
S
63
−12.751
101.404
−63.852
1.00
57.39
S

ATOM
2262
OH2
TIP
S
64
−16.620
90.320
−50.785
1.00
65.96
S

ATOM
2263
OH2
TIP
S
65
−25.697
92.664
−68.885
1.00
68.28
S

ATOM
2264
OH2
TIP
S
66
−15.025
118.312
−89.771
1.00
58.18
S

ATOM
2265
OH2
TIP
S
67
−26.931
126.107
−71.665
1.00
63.11
S

ATOM
2266
OH2
TIP
S
68
−34.795
103.669
−75.122
1.00
72.18
S

ATOM
2267
OH2
TIP
S
69
−6.831
109.056
−79.337
1.00
56.79
S

ATOM
2268
OH2
TIP
S
70
−40.479
91.734
−58.440
1.00
70.62
S

ATOM
2269
OH2
TIP
S
71
−20.314
83.170
−45.556
1.00
56.27
S

ATOM
2270
OH2
TIP
S
72
−26.070
77.761
−66.849
1.00
72.74
S

ATOM
2271
OH2
TIP
S
73
−0.282
120.436
−52.404
1.00
59.59
S

ATOM
2272
OH2
TIP
S
74
−32.286
112.812
−61.349
1.00
43.83
S

ATOM
2273
OH2
TIP
S
75
−21.294
97.870
−79.101
1.00
58.86
S

ATOM
2274
OH2
TIP
S
76
−27.673
75.363
−70.379
1.00
76.66
S

ATOM
2275
OH2
TIP
S
77
−39.412
105.973
−60.762
1.00
56.79
S

ATOM
2276
OH2
TIP
S
78
−20.303
89.918
−51.002
1.00
64.33
S

ATOM
2277
OH2
TIP
S
79
−17.189
106.753
−51.920
1.00
46.41
S

ATOM
2278
OH2
TIP
S
80
−47.843
80.379
−64.135
1.00
60.37
S

ATOM
2279
OH2
TIP
S
81
−17.573
113.712
−84.502
1.00
110.19
S

ATOM
2280
OH2
TIP
S
82
−37.065
102.989
−56.757
1.00
54.22
S

ATOM
2281
OH2
TIP
S
83
−14.498
111.272
−91.417
1.00
101.41
S

ATOM
2282
OH2
TIP
S
84
−30.372
106.961
−82.277
1.00
70.02
S

ATOM
2283
OH2
TIP
S
85
−9.664
113.440
−56.086
1.00
59.88
S

ATOM
2284
OH2
TIP
S
86
−24.964
98.917
−55.078
1.00
55.96
S

ATOM
2285
OH2
TIP
S
87
−37.843
98.707
−65.463
1.00
78.73
S

ATOM
2286
OH2
TIP
S
88
−31.274
103.379
−51.826
1.00
127.66
S

ATOM
2287
OH2
TIP
S
89
−10.475
113.309
−84.373
1.00
75.64
S

ATOM
2288
OH2
TIP
S
90
−27.341
123.774
−70.092
1.00
71.65
S

ATOM
2289
OH2
TIP
S
91
−18.711
90.537
−62.683
1.00
55.83
S

ATOM
2290
OH2
TIP
S
92
−33.403
106.130
−77.985
1.00
78.72
S

ATOM
2291
OH2
TIP
S
93
−24.005
90.870
−56.466
1.00
65.52
S

ATOM
2292
OH2
TIP
S
94
−27.617
104.616
−54.961
1.00
111.64
S

ATOM
2293
OH2
TIP
S
95
−13.742
93.007
−62.576
1.00
55.12
S

ATOM
2294
OH2
TIP
S
96
−26.852
118.188
−57.257
1.00
50.05
S

ATOM
2295
OH2
TIP
S
97
−22.007
123.757
−63.602
1.00
81.09
S

ATOM
2296
OH2
TIP
S
98
−23.230
88.728
−66.431
1.00
110.10
S

ATOM
2297
OH2
TIP
S
99
−13.360
112.796
−87.736
1.00
51.81
S

ATOM
2298
OH2
TIP
S
100
−16.221
123.986
−53.826
1.00
64.19
S

ATOM
2299
OH2
TIP
S
101
−21.410
129.947
−61.869
1.00
51.98
S

ATOM
2300
OH2
TIP
S
102
−10.815
115.537
−81.525
1.00
79.49
S

ATOM
2301
OH2
TIP
S
103
−10.813
93.308
−60.006
1.00
73.70
S

ATOM
2302
OH2
TIP
S
104
−40.267
90.357
−71.550
1.00
102.57
S

ATOM
2303
OH2
TIP
S
105
−33.508
104.329
−71.475
1.00
130.44
S

ATOM
2304
OH2
TIP
S
106
−18.744
92.097
−73.138
1.00
57.33
S

ATOM
2305
OH2
TIP
S
107
−36.651
100.017
−59.561
1.00
80.34
S

ATOM
2306
OH2
TIP
S
108
−35.655
83.715
−66.690
1.00
92.34
S

ATOM
2307
OH2
TIP
S
109
−15.004
123.171
−72.873
1.00
64.24
S

ATOM
2308
OH2
TIP
S
110
−19.809
86.420
−75.382
1.00
60.00
S

ATOM
2309
OH2
TIP
S
111
−22.061
106.390
−65.510
1.00
141.40
S

ATOM
2310
OH2
TIP
S
112
−30.065
119.754
−61.428
1.00
54.41
S

ATOM
2311
OH2
TIP
S
113
−21.117
101.845
−76.666
1.00
133.00
S

ATOM
2312
OH2
TIP
S
114
−36.169
94.852
−53.914
1.00
52.74
S

ATOM
2313
OH2
TIP
S
115
−20.513
90.392
−76.531
1.00
62.03
S

ATOM
2314
OH2
TIP
S
116
−7.874
116.642
−87.594
1.00
65.17
S

ATOM
2315
OH2
TIP
S
117
−12.611
91.681
−79.605
1.00
54.76
S

ATOM
2316
OH2
TIP
S
118
−39.602
93.998
−67.457
1.00
74.47
S

ATOM
2317
OH2
TIP
S
119
−31.966
115.257
−81.634
1.00
96.68
S

ATOM
2318
OH2
TIP
S
120
−20.353
112.035
−73.437
1.00
110.82
S

ATOM
2319
OH2
TIP
S
121
−8.471
110.279
−71.660
1.00
75.05
S

ATOM
2320
OH2
TIP
S
122
−19.609
72.745
−59.575
1.00
57.01
S

ATOM
2321
OH2
TIP
S
123
−3.225
126.719
−50.300
1.00
46.98
S

ATOM
2322
OH2
TIP
S
124
−13.531
110.225
−57.101
1.00
47.35
S

ATOM
2323
OH2
TIP
S
125
−15.950
117.562
−82.262
1.00
82.90
S

ATOM
2324
OH2
TIP
S
126
−9.300
127.283
−56.135
1.00
64.58
S

ATOM
2325
OH2
TIP
S
127
−40.326
100.805
−86.362
1.00
67.40
S

ATOM
2326
OH2
TIP
S
128
−26.743
109.839
−47.135
1.00
56.64
S

ATOM
2327
OH2
TIP
S
129
−21.152
78.015
−44.545
1.00
63.33
S

ATOM
2328
OH2
TIP
S
130
−15.502
111.092
−65.948
1.00
93.70
S

ATOM
2329
OH2
TIP
S
131
−61.010
80.720
−82.560
1.00
59.97
S

ATOM
2330
OH2
TIP
S
132
−5.754
114.545
−88.180
1.00
46.35
S

ATOM
2331
OH2
TIP
S
133
−17.343
102.484
−73.188
1.00
80.48
S

ATOM
2332
OH2
TIP
S
134
−22.668
100.024
−66.101
1.00
160.50
S

ATOM
2333
OH2
TIP
S
135
−13.492
97.626
−62.513
1.00
74.96
S

ATOM
2334
OH2
TIP
S
136
−34.975
118.383
−60.826
1.00
54.24
S

ATOM
2335
OH2
TIP
S
137
−39.901
98.826
−74.968
1.00
107.12
S

ATOM
2336
OH2
TIP
S
138
−13.081
90.301
−74.716
1.00
80.68
S

ATOM
2337
OH2
TIP
S
139
−6.679
129.585
−62.277
1.00
58.26
S

ATOM
2338
OH2
TIP
S
140
−24.229
112.256
−55.630
1.00
42.51
S

ATOM
2339
OH2
TIP
S
141
−29.294
92.995
−46.924
1.00
62.81
S

ATOM
2340
OH2
TIP
S
142
−33.181
120.270
−61.770
1.00
58.91
S

ATOM
2341
OH2
TIP
S
143
−15.987
93.183
−52.324
1.00
56.26
S

ATOM
2342
OH2
TIP
S
144
−33.793
120.291
−64.846
1.00
128.61
S

ATOM
2343
OH2
TIP
S
145
−7.502
112.874
−86.551
1.00
89.97
S

ATOM
2344
OH2
TIP
S
146
−28.737
113.816
−70.544
1.00
90.60
S

ATOM
2345
OH2
TIP
S
147
−25.751
91.368
−78.478
1.00
56.02
S

ATOM
2346
OH2
TIP
S
148
−5.538
108.115
−57.303
1.00
61.91
S

ATOM
2347
OH2
TIP
S
149
−6.750
117.327
−84.625
1.00
55.56
S

ATOM
2348
OH2
TIP
S
150
−6.064
113.190
−80.641
1.00
84.73
S

ATOM
2349
OH2
TIP
S
151
−14.898
122.897
−70.515
1.00
72.28
S

ATOM
2350
OH2
TIP
S
152
−17.385
119.055
−80.821
1.00
117.81
S

ATOM
2351
OH2
TIP
S
153
−17.722
92.098
−76.941
1.00
77.30
S

ATOM
2352
OH2
TIP
S
154
−41.186
101.886
−63.398
1.00
70.46
S

ATOM
2353
OH2
TIP
S
155
−36.523
109.555
−67.648
1.00
63.22
S

ATOM
2354
OH2
TIP
S
156
−46.348
79.889
−42.332
1.00
70.93
S

ATOM
2355
OH2
TIP
S
157
−31.159
112.205
−64.750
1.00
96.21
S

ATOM
2356
OH2
TIP
S
158
−16.496
98.729
−51.917
1.00
68.11
S

ATOM
2357
OH2
TIP
S
159
−27.445
92.326
−55.432
1.00
105.80
S

ATOM
2358
OH2
TIP
S
160
−12.883
122.829
−51.350
1.00
52.37
S

ATOM
2359
OH2
TIP
S
161
−37.558
90.883
−73.852
1.00
56.64
S

ATOM
2360
OH2
TIP
S
162
−32.439
111.015
−77.093
1.00
95.14
S

ATOM
2361
OH2
TIP
S
163
−29.848
91.790
−64.074
1.00
53.48
S

ATOM
2362
OH2
TIP
S
164
−47.202
94.576
−65.895
1.00
62.74
S

ATOM
2363
OH2
TIP
S
165
−10.553
86.337
−79.886
1.00
62.46
S

ATOM
2364
OH2
TIP
S
166
−28.158
117.033
−76.907
1.00
50.72
S

ATOM
2365
OH2
TIP
S
167
−20.768
90.813
−71.552
1.00
63.30
S

ATOM
2366
OH2
TIP
S
168
−42.018
80.510
−57.537
1.00
72.58
S

ATOM
2367
OH2
TIP
S
169
−30.391
84.848
−82.737
1.00
69.68
S

ATOM
2368
OH2
TIP
S
170
−4.077
114.307
−69.426
1.00
63.76
S

ATOM
2369
OH2
TIP
S
171
−16.148
98.312
−71.887
1.00
84.16
S

ATOM
2370
OH2
TIP
S
172
−19.294
101.248
−73.895
1.00
115.91
S

ATOM
2371
OH2
TIP
S
173
−29.677
116.091
−74.250
1.00
112.47
S

ATOM
2372
OH2
TIP
S
174
−16.280
101.239
−66.115
1.00
51.98
S

ATOM
2373
OH2
TIP
S
175
−31.445
90.794
−73.675
1.00
76.22
S

ATOM
2374
OH2
TIP
S
176
−37.325
101.693
−52.478
1.00
115.74
S

ATOM
2375
OH2
TIP
S
177
−33.007
116.295
−72.875
1.00
132.16
S

ATOM
2376
OH2
TIP
S
178
−33.602
108.930
−56.008
1.00
78.57
S

ATOM
2377
OH2
TIP
S
179
−27.755
103.470
−66.606
1.00
111.83
S

ATOM
2378
OH2
TIP
S
180
−23.711
110.440
−82.309
1.00
52.25
S

ATOM
2379
OH2
TIP
S
181
−19.445
77.703
−62.696
1.00
94.18
S

ATOM
2380
OH2
TIP
S
182
−40.075
101.931
−67.249
1.00
53.34
S

ATOM
2381
OH2
TIP
S
183
−9.169
88.933
−70.344
1.00
48.03
S

ATOM
2382
OH2
TIP
S
184
−7.205
111.603
−56.621
1.00
53.47
S

ATOM
2383
OH2
TIP
S
185
−26.172
121.826
−70.446
1.00
101.08
S

ATOM
2384
OH2
TIP
S
186
−17.802
111.367
−89.651
1.00
66.17
S

ATOM
2385
OH2
TIP
S
187
−4.045
107.148
−89.001
1.00
58.76
S

ATOM
2386
OH2
TIP
S
188
−28.598
115.945
−80.483
1.00
91.65
S

ATOM
2387
OH2
TIP
S
189
−19.368
110.747
−54.934
1.00
128.20
S

ATOM
2388
OH2
TIP
S
190
−20.905
75.083
−60.333
1.00
91.67
S

ATOM
2389
OH2
TIP
S
191
−25.133
114.645
−61.905
1.00
118.77
S

ATOM
2390
OH2
TIP
S
192
−10.847
108.163
−58.161
1.00
55.70
S

ATOM
2391
OH2
TIP
S
193
−31.040
90.727
−62.161
1.00
127.17
S

ATOM
2392
OH2
TIP
S
194
−24.361
88.949
−61.408
1.00
96.03
S

ATOM
2393
OH2
TIP
S
195
−25.845
118.902
−77.997
1.00
101.37
S

ATOM
2394
OH2
TIP
S
196
−45.257
100.264
−64.437
1.00
67.73
S

ATOM
2395
OH2
TIP
S
197
−19.534
122.816
−60.513
1.00
57.10
S

ATOM
2396
OH2
TIP
S
198
−17.729
89.087
−73.164
1.00
62.32
S

ATOM
2397
OH2
TIP
S
199
−25.598
115.479
−56.345
1.00
58.00
S

ATOM
2398
OH2
TIP
S
200
−11.966
110.289
−86.531
1.00
58.38
S

ATOM
2399
OH2
TIP
S
201
−11.862
111.179
−90.005
1.00
62.26
S

ATOM
2400
OH2
TIP
S
202
−23.146
103.334
−74.388
1.00
86.36
S

ATOM
2401
OH2
TIP
S
203
−25.348
100.591
−88.904
1.00
83.58
S

ATOM
2402
OH2
TIP
S
204
−33.579
99.455
−57.461
1.00
123.22
S

ATOM
2403
OH2
TIP
S
205
−19.262
110.559
−81.294
1.00
94.92
S

ATOM
2404
OH2
TIP
S
206
−3.814
105.699
−53.606
1.00
59.43
S

ATOM
2405
OH2
TIP
S
207
−42.986
86.709
−66.627
1.00
101.31
S

ATOM
2406
OH2
TIP
S
208
−1.519
111.809
−84.036
1.00
50.96
S

ATOM
2407
OH2
TIP
S
209
−17.903
106.223
−57.233
1.00
112.85
S

ATOM
2408
OH2
TIP
S
210
−39.670
95.363
−88.124
1.00
59.37
S

ATOM
2409
OH2
TIP
S
211
−17.795
75.194
−56.614
1.00
104.92
S

ATOM
2410
OH2
TIP
S
212
−20.005
112.200
−78.821
1.00
110.72
S

ATOM
2411
OH2
TIP
S
213
−0.589
117.171
−54.358
1.00
56.45
S

ATOM
2412
OH2
TIP
S
214
−30.338
92.585
−76.714
1.00
110.56
S

ATOM
2413
OH2
TIP
S
215
−0.557
94.041
−72.839
1.00
72.72
S

ATOM
2414
OH2
TIP
S
216
−44.272
80.569
−64.137
1.00
88.29
S

ATOM
2415
OH2
TIP
S
217
−8.330
108.845
−85.172
1.00
61.74
S

ATOM
2416
OH2
TIP
S
218
−38.922
101.691
−58.270
1.00
100.23
S

ATOM
2417
OH2
TIP
S
219
−14.469
88.506
−51.433
1.00
69.37
S

ATOM
2418
OH2
TIP
S
220
−15.575
95.883
−51.472
1.00
92.96
S

ATOM
2419
OH2
TIP
S
221
−23.554
92.371
−47.328
1.00
103.71
S

ATOM
2420
OH2
TIP
S
222
−3.867
118.046
−85.348
1.00
77.94
S

ATOM
2421
OH2
TIP
S
223
−35.589
120.474
−63.099
1.00
87.19
S

ATOM
2422
OH2
TIP
S
224
−44.239
110.368
−58.934
1.00
77.76
S

ATOM
2423
OH2
TIP
S
225
−32.794
111.024
−68.824
1.00
108.60
S

ATOM
2424
OH2
TIP
S
226
−22.720
80.213
−59.846
1.00
130.32
S

ATOM
2425
OH2
TIP
S
227
−42.005
107.878
−70.190
1.00
96.92
S

ATOM
2426
OH2
TIP
S
228
−15.709
78.715
−43.542
1.00
58.73
S

ATOM
2427
OH2
TIP
S
229
−39.901
97.291
−52.193
1.00
60.44
S

ATOM
2428
OH2
TIP
S
230
−33.181
83.277
−46.966
1.00
74.04
S

ATOM
2429
OH2
TIP
S
231
−36.075
105.384
−71.283
1.00
111.20
S

ATOM
2430
OH2
TIP
S
232
−23.807
124.303
−80.685
1.00
57.30
S

ATOM
2431
OH2
TIP
S
233
−32.691
113.570
−83.528
1.00
93.84
S

ATOM
2432
OH2
TIP
S
234
−35.384
101.526
−65.535
1.00
74.54
S

ATOM
2433
OH2
TIP
S
235
−52.003
97.430
−68.647
1.00
73.21
S

ATOM
2434
OH2
TIP
S
236
−53.636
92.100
−47.728
1.00
83.96
S

ATOM
2435
OH2
TIP
S
237
−32.998
79.952
−48.805
1.00
77.92
S

ATOM
2436
OH2
TIP
S
238
−19.609
88.765
−71.863
1.00
63.44
S

ATOM
2437
OH2
TIP
S
239
−37.978
101.579
−62.221
1.00
114.24
S

ATOM
2438
OH2
TIP
S
240
−40.568
92.296
−86.674
1.00
65.76
S

ATOM
2439
OH2
TIP
S
241
−23.296
93.673
−73.044
1.00
87.42
S

ATOM
2440
OH2
TIP
S
242
−18.241
102.306
−50.261
1.00
99.29
S

ATOM
2441
OH2
TIP
S
243
−45.686
89.248
−74.060
1.00
80.50
S

ATOM
2442
OH2
TIP
S
244
−48.990
77.329
−65.285
1.00
62.79
S

ATOM
2443
OH2
TIP
S
245
−39.670
103.275
−60.596
1.00
78.31
S

ATOM
2444
OH2
TIP
S
246
−49.281
84.180
−38.445
1.00
62.88
S

ATOM
2445
OH2
TIP
S
247
−35.923
76.665
−73.082
1.00
90.47
S

ATOM
2446
OH2
TIP
S
248
−22.650
98.270
−55.329
1.00
66.55
S

ATOM
2447
OH2
TIP
S
249
−1.136
105.962
−80.208
1.00
95.63
S

ATOM
2448
OH2
TIP
S
250
−30.948
81.763
−46.481
1.00
64.39
S

ATOM
2449
OH2
TIP
S
251
−31.424
106.525
−70.271
1.00
146.73
S

ATOM
2450
OH2
TIP
S
252
−47.586
98.613
−55.205
1.00
71.91
S

ATOM
2451
OH2
TIP
S
253
−2.582
111.252
−61.347
1.00
64.80
S

ATOM
2452
OH2
TIP
S
254
−32.001
99.414
−81.548
1.00
75.73
S

ATOM
2453
OH2
TIP
S
255
−14.287
99.143
−64.847
1.00
86.21
S

ATOM
2454
OH2
TIP
S
256
−54.384
78.808
−65.841
1.00
53.97
S

ATOM
2455
OH2
TIP
S
257
−26.112
120.574
−60.165
1.00
104.99
S

ATOM
2456
OH2
TIP
S
258
−45.064
97.484
−65.973
1.00
70.27
S

ATOM
2457
OH2
TIP
S
259
−27.816
89.385
−78.676
1.00
86.86
S

ATOM
2458
OH2
TIP
S
260
−46.644
107.061
−62.630
1.00
70.71
S

ATOM
2459
OH2
TIP
S
261
−18.353
98.010
−49.930
1.00
105.72
S

ATOM
2460
OH2
TIP
S
262
−8.406
116.226
−81.494
1.00
104.02
S

ATOM
2461
OH2
TIP
S
263
−33.763
81.288
−44.581
1.00
67.25
S

ATOM
2462
OH2
TIP
S
264
−14.153
87.119
−63.758
1.00
70.68
S

ATOM
2463
OH2
TIP
S
265
−16.810
120.032
−69.896
1.00
88.49
S

ATOM
2464
OH2
TIP
S
266
0.697
78.048
−53.011
1.00
79.10
S

ATOM
2465
OH2
TIP
S
267
−13.291
117.712
−84.014
1.00
86.90
S

ATOM
2466
OH2
TIP
S
268
−41.914
95.291
−85.766
1.00
66.46
S

END

Number	Date	Country	Kind
0119860.5	Aug 2001	GB
0209985.1	May 2002	GB

Kinase crystal structures and materials and methods for kinase activation

Information

Publication Number

Date Filed

Date Published

Inventors

Original Assignees

CPC

US Classifications

International Classifications

Abstract

Description

Claims

Priority Claims (2)