Crystal structure

Abstract

The invention relates to crystals of the enzyme ketopantoate reductase, and in particular its crystal structure and the use of this structure in drug discovery.

Description

FIELD OF THE INVENTION

[0001] The present invention relates to the enzyme ketopantoate reductase, and in particular its crystal structure and the use of this structure in drug discovery.

BACKGROUND OF THE INVENTION

[0002] Pantothenic acid (vitamin B5) is found in coenzyme A (CoA) and the acyl carrier protein (ACP), both of which are involved in fatty acid metabolism.

[0003] Pantothenic acid can be synthesised by plants and microorganisms but animals are apparently unable to make the vitamin, and require it in their diet. However, all organisms are able to convert pantothenic acid to its metabolically active form, coenzyme A.

[0004] The pathway for the synthesis of pantothenic acid is shown in FIG. 1. It provides a potential target for the treatment of infectious disease, since inhibitors of the pathway should be damaging to bacteria and fungi but not to human or animal subjects infected by bacteria.

[0005] Of specific interest is the enzyme ketopantoate reductase. Ketopantoate reductase (EC 1.1.1.169, KPR, PanE) is the third enzyme on the biosynthetic pathway to pantothenate, vitamin B5, the precursor of the phosphopantetheine, the acyl carrier in coenzyme A and on acyl carrier proteins. In animals, pantothenate is supplied in the diet; in plants and microorganisms, it is synthesised de novo. In Escherichia coli pantothenate is synthesized from its precursors α-keto-isovalerate and aspartate by a four-step pathway (Jackowski et al., 1996). Three genes out of four involved in this biosynthesis, panB, panC and panD were identified and mapped on the E. coli chromosome at 4 min (Berlyn et al., 1996). The last gene in the pathway to be identified was panE. It comprises a 912 bp coding region which specifies a protein of 303 amino acid with deduced molecular mass of 33.8 kD (Elischewski et al., 1999).

[0006] The enzyme substrate, ketopantoic acid can exist either as the cyclic ketopantoyl lactone or as the ring opened hydroxyacid, ketopantoate. Both ketopantoate reductases and ketopantoyl lactone reductases have been reported (King and Wilken, 1972). Ketopantoyl lactone reductase has been purified from yeast (King et al., 1974), Norcardia asteroides (Kataoka et al., 1992) and spinach (Julliard, 1994). The spinach enzyme is reported to be soluble and monomeric with a molecular mass of 33-36 kDa. In contrast the Norcardia enzyme is membrane-bound with a subunit molecular mass of 42 kDa. The molecular weight of the native enzyme is reported to be over 600 kDa. The role of ketopantoyl lactone reductase in pantothenate biosynthesis is unclear as the cyclic product pantoyl lactone is not a direct substrate for pantothenate synthetase from plants (Genschel, 1997).

[0007] Ketopantoate reductase, the enzyme which reduces the ring open form of the substrate, was initially purified from yeast (King and Wilken, 1972) and subsequently from Pseudomonas maltophilia 845 (Shimizu et al., 1988). The subunit molecular mass of the Pseudomonas enzyme was approximately 30.5 kDa. Experiments to determine the molecular mass of the native protein were inconclusive and gave values between 87-160 KDa.

[0008] It has recently been demonstrated that the panE gene is allelic to apbA in Salmonella typhimurium and maps to minute 10 in the genome (Frodyma and Downs, 1998b ). The alternative pyrimidine biosynthesis pathway provides a second route for the generation of the pyrimidine part of thiamine, other than by de novo purine biosynthesis. It has been proposed that the apbA gene product is ketopantoate reductase (Frodmya and Downs, 1998a). The ApbA protein from S. typhimurium has been purified to homogeneity. It is a monomer with a molecular mass of 31.1 kDa. The enzyme has apparent KMs of 0.77 and 0.74 mM for NADPH and ketopantoate respectively. It has been reported that, under conditions where apbA mutants required thiamine, pantoate was sufficient to restore growth (Frodmya and Downs, 1998a). Nevertheless, the role of pantoate in thiamine biosynthesis remains unclear, and may be indirect. Using gene replacement and transposon mutagenesis (Tn5) an E. coli ilvc panE double mutant was isolated which was devoid of ketopantoate reductase activity Manch, J. N. (1981) Can J Microbiol 27, 1231-1233; Primerano, D., and Burns, R. O. (1993) J. Bacteriol. 153, 259-269). This mutant was used to isolate the panE gene by functional complementation. This mutant was rescued by functional complementation using either apbA or ilvC, providing further circumstantial support that apbA and panE are identical. The panE gene was expressed under the control of a tac promoter. A three fold increase in activity was observed. This in turn led to a 3.5 fold increase in the secretion of pantothenate, which could be enhanced further by the addition of ketopantoate (Elischewski et al., 1999). Inhibitors (whether competitive, non-competitive, uncompetitive or irreversible) of pantothenate synthetase would be of significant technical and commercial interest.

[0009] Knowledge of the structure of KPR would significantly assist the rational design of novel therapeutics based on modulators of KPR activity.

DESCRIPTION OF THE DRAWINGS

[0010] FIG. 1 illustrates the pantothenate synthesis pathway.

[0011] FIG. 2 shows (A) the binding of NADPH and (B) the binding of ketopantoate to KPR.

SUMMARY OF THE INVENTION

[0012] The present invention is at based on the novel determination of a high resolution X-ray crystal structure of KPR. The invention is based upon a KPR crystal which has a resolution better than (i.e. numerically lower than) 2 Å.

[0013] In one aspect, the invention provides a KPR crystal having a tetragonal space group P41212 with unit cell dimensions of a=103.7, b=103.7, c=55.7 Å, or more generally, a=103.7±0.2, b=103.7±0.2, c=55.7±0.2 Å. Such a structure includes the KPR crystal of Table 1. An advantageous feature of the structure is that it has a high resolution, of about 1.7 Å. Another feature of the structure is that it was obtained in a method which utilised selenomethionine substituted enzyme. These features, both singly and in combination all contribute to features of the invention which are advantageous.

[0014] The coordinates of Table 1 provide a measure of atomic location in Angstroms, to a third decimal place. The coordinates are a relative set of positions that define a shape in three dimensions, so it is possible that an entirely different set of coordinates having a different origin and/or axes could define a similar or identical shape. Furthermore, 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 in Table 1 for the residue backbone atoms, will generally result in a structure which is substantially the same as the structure of Table 1 in terms of both its structural characteristics and potency for structure-based design of KPR inhibitors. Likewise changing the number and/or positions of the water molecules and/or substrate molecules of Table 1 will not generally affect the potency of the structure for structure-based design of KPR inhibitors. Thus for the purposes described herein as being aspects of the present invention, it is within the scope of the invention if: the Table 1 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 Table 1 for the residue backbone atoms; and/or the number and/or positions of water molecules and/or substrate molecules is varied. Reference herein to the coordinate data of Table 1 thus includes the coordinate data in which one or more individual values of the Table are varied in this way. By “root mean square deviation” we mean the square root of the arithmetic mean of the squares of the deviations from the mean.

[0015] The provision of the high resolution structure of Table 1 provides those of skill in the art with a detailed insight into the mechanisms of action of KPR. This insight provides a means to design new antibacterial agents which have the potential to inhibit the process of pantothenate synthesis in bacteria and fungi, or to modulate the activity of the enzyme, for example such that the enzyme works more effectively on prodrugs which are converted by KPR into an antibacterial drug.

[0016] In a further aspect, the invention provides a method for crystallizing a selenium atom KPR derivative which comprises producing KPR by recombinant production in a bacterial host (e.g. E. coli) in the presence of selenomethionine, recovering a selenium atom KPR derivative from the host and growing crystals from the recovered selenium atom KPR derivative.

[0017] Thus, the selenium atom KPR derivative and KPR produced by crystallising native KPR (see the detailed description below) are provided as crystallised proteins suitable for X-ray diffraction analysis.

[0018] The crystals may be grown by any suitable method, e.g. the hanging drop method.

[0019] The provision of the crystal structure of KPR allows a novel approach for drug discovery for modulators of this enzyme. Accordingly, the invention provides a computer-based method of rational drug design which comprises:

[0020] providing the structure of the KPR as defined by the coordinates of Table 1;

[0021] providing the structure of a candidate modulator molecule; and

[0022] fitting the structure of candidate to the structure of the KPR of Table 1.

[0023] In an alternative aspect, the method of the invention may utilise the coordinates of atoms of interest of the KPR which are in the vicinity of a the putative substrate and/or co-factor binding regions in order to model the pocket in which the substrate or co-factor binds. These coordinates may be used to define a space which is then screened “in silico” against a candidate modulator molecule. Thus the invention provides a computer-based method of rational drug design which comprises:

[0024] providing the coordinates of at least two atoms of Table 1 of the KPR (“selected coordinates”);

[0025] providing the structure of a candidate modulator molecule; and

[0026] fitting the structure of candidate to the selected coordinates of the KPR.

[0027] In practice, it will be desirable to model a sufficient number of atoms of the KPR as defined by the coordinates of Table 1 which represent a binding pocket. Binding pockets and other features of the interaction of KPR with co-factor are described in the accompanying example. Thus, in this embodiment of the invention, there will preferably be provided the coordinates of at least 5, preferably at least 10, more preferably at least 50 and even more preferably at least 100 atoms of the KPR structure.

[0028] Our structure of KPR has allowed us to identify particular sites of interaction of NADPH and ketopantoate. The selected coordinates preferably include at least one of the coordinates identified in the accompanying examples. These include Leu6, Cys8, Gly9, Leu11, Leu30, Arg31, Leu71, Lys72, Gln75, Asn98, His120, Ala122, Arg124, Lys176, Ser244, and Glu256.

[0029] In another aspect, the method of the invention may utilise a sub-domain of interest of the KPR which is in the vicinity of a region which binds substrate or co-factor. Thus, the invention provides a computer-based method of rational drug design which comprises:

[0030] providing the coordinates of at least a sub-domain of the KPR;

[0031] providing the structure of a candidate modulator molecule; and

[0032] fitting the structure of the candidate to the coordinates of the KPR sub-domain provided.

DETAILED DESCRIPTION OF THE INVENTION

[0033] By “fitting”, it is meant determining by automatic, or semi-automatic means, interactions between at least one atom of the candidate and at least one atom of the KPR, and calculating the extent to which such an interaction is stable. Interactions include attraction and repulsion, brought about by charge, steric considerations and the like. Various computer-based methods for fitting are described further herein.

[0034] By “sub-domain” is meant at least one (e.g. one, two, three or four) complete element(s) of secondary structure, i.e. an alpha helix or a beta sheet, as described in the detailed description below.

[0035] Particular regions of the KPR include those identified as putative substrate or cofactor binding regions based on the data provided in Table 1.

[0036] As indicated above, modulators of KPR may be inhibitors of the enzyme or compounds which affect its specificity or activity in relation to ketopantoate in other ways. The invention is particularly suitable for the design, screening and development of KPR inhibitor components. It is thus a preferred aspect of the invention that modulators are inhibitors.

[0037] If more than one KPR active site is characterised and a plurality of respective compounds are designed or selected, the potential modulator may be formed by linking the respective compounds into a larger compound which maintains the relative positions and orientations of the respective compounds at the active sites. The larger compound may be formed as a real molecule or by computer modelling.

[0038] The step of providing the structure of a candidate modulator molecule may involve selecting the compound by computationally screening a database of compounds for interaction with the active site. For example, a 3-D descriptor for the potential modulator may be derived, the descriptor including geometric and functional constraints derived from the architecture and chemical nature of the active site. The descriptor may then be used to interrogate the compound database, a potential modulator being a compound that has a good match to the features of the descriptor. In effect, the descriptor is a type of virtual pharmacophore.

[0039] In any event, the determination of the three-dimensional structure of KPR provides a basis for the design of new and specific modulators for KPR. For example, knowing the three-dimensional structure of KPR, computer modelling programs may be used to design different molecules expected to interact with possible or confirmed active sites, such as binding sites or other structural or functional features of KPR.

[0040] More specifically, a potential modulator of KPR 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) to identify potential inhibitors of KPR. This procedure can include computer fitting of potential modulators to KPR to ascertain how well the shape and the chemical structure of the potential inhibitor will bind to the enzyme.

[0041] Also computer-assisted, manual examination of the active site structure of KPR 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 active site to predict partial structures of modulating compounds.

[0042] Computer programs can be employed to estimate the attraction, repulsion, and steric hindrance of the two binding partners (e.g. the KPR 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 candidate modulator, the more likely it is that it will not interact with other proteins as well. This will tend to minimise potential side-effects due to unwanted interactions with other proteins.

[0043] In another aspect, in place of in silico methods, high throughput screening of compounds to select compounds with binding activity may be undertaken, and those compounds which show binding activity may be selected as possible candidate modulators, and further crystallized with KPR (e.g. by co-crystallization or by soaking) for X-ray analysis. The resulting X-ray structure may be compared with that of Table 1 for a variety of purposes. For example, where the contacts made by such compounds overlap with those may by ketopantoate, novel molecules comprising residues which contain contacts of both ketopantoate and the other compound may be provided.

[0044] Having designed or selected possible binding candidate modulators by determining those which have favourable fitting properties (e.g. strong attraction between candidate and KPR), these can then be screened for activity. Consequently, the method preferably further comprises the further steps of:

[0045] obtaining or synthesising the candidate modulator; and

[0046] contacting the candidate modulator with KPR to determine the ability of the candidate inhibitor to interact with KPR.

[0047] More preferably, in latter step the candidate modulator is contacted with KPR under conditions to determine its function.

[0048] Instead of, or in addition to, performing such an assay, the method may comprise the further steps of:

[0049] obtaining or synthesising said candidate modulator;

[0050] forming a complex of KPR and said potential modulator; and

[0051] analysing said complex by X-ray crystallography to determine the ability of said candidate modulator to interact with KPR. Detailed structural information can then be obtained about the binding of the candidate modulator to KPR, and in the light of this information adjustments can be made to the structure or functionality of the potential modulator, e.g. to improve binding to the active site. The above steps may be repeated and re-repeated as necessary.

[0052] More preferably, in contacting step above the potential modulator is contacted with KPR in the presence of a substrate, and typically a buffer, to determine the ability of said potential modulator to alter the function of KPR. The substrate may be e.g. ketopantoate (or a salt thereof) and/or NADPH. So, for example, an assay mixture for KPR may be produced which comprises the potential modulator, substrate (e.g. NADPH) and buffer.

[0053] In another aspect, the invention relates to a method of determining three dimensional structures of KPR homologues of unknown structure by utilising the structural coordinates of Table 1.

[0054] For example, if X-ray crystallographic or NMR spectroscopic data is provided for a KPR homologue of unknown structure, the structure of KPR as defined by Table 1 may be used to interpret that data to provide a likely structure for the KPR homologue by techniques which are well known in the art, e.g. phase modelling in the case of X-ray crystallography.

[0055] One embodiment of the method comprises the steps of:

[0056] (a) aligning a representation of an amino acid sequence of a KPR homologue of unknown structure with the amino acid sequence of KPR to match homologous regions of the amino acid sequences;

[0057] (b) modelling the structure of the matched homologous regions of the KPR of unknown structure on the structure as defined by Table 1 of the corresponding regions of KPR; and

[0058] (c) determining a conformation (e.g. so that favourable interactions are formed within the KPR of unknown structure and/or so that a low energy conformation is formed) for the KPR of unknown structure which substantially preserves the structure of said matched homologous regions.

[0059] 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.

[0060] Preferably one or all of steps (a) to (c) are performed by computer modelling. Homology modelling is a technique that is well known to those skilled in the art (see e.g. Greer, Science, Vol. 228, (1985), 1055, and Blundell et al., Eur. J. Biochem, Vol. 172, (1988), 513).

[0061] 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.

[0062] Homology between amino acid sequences can be determined using commercially available algorithms. The programs BLAST, gapped BLAST, BLASTN and PSI-BLAST (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.

[0063] 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.

[0064] 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.

[0065] The aspects of the invention described herein which utilise the KPR structure in silico may be equally applied to homologue models of KPR obtained by the above aspect of the invention, and this application forms a further aspect of the present invention. Thus having determined a conformation of a KPR by the method described above, such a conformation may be used in a computer-based method of rational drug design as described herein.

[0066] In another aspect, the invention includes a compound which is identified as a modulator of a KPR by the methods of the invention described above.

[0067] In a further aspect, the invention provides a method for determining the structure of a modulator of KPR bound to KPR, said method comprising:

[0068] providing a crystal of KPR according to the invention;

[0069] soaking the crystal with said modulator; and

[0070] determining the structure of said KPR-modulator complex.

[0071] Alternatively, the KPR and modulator may be co-crystallized. In either case, ketopantoate and/or NADP or an analogue thereof may optionally be present.

[0072] Having obtained and characterized a modulator compound according to the invention, the invention further provides a method for modulating the activity of KPR which method comprises:

[0073] providing KPR under conditions where, in the absence of modulator, the KPR is able to synthesize pantoate from ketopantoate;

[0074] providing a modulator compound; and

[0075] determining the extent to which the activity of KPR is altered by the presence of said compound.

[0076] In another aspect, the present invention provides systems, particularly a computer systems, intended to generate structures and/or perform rational drug design for a KPR or a complex of KPR and potential modulator, the systems containing either (a) atomic coordinate data according to Table 1 or derived therefrom by homology modelling, said data defining the three-dimensional structure of a KPR or at least one sub-domain thereof, or (c) structure factor data for KPR, said structure factor data being derivable from the atomic coordinate data of Table 1.

[0077] In a further aspect, the present invention provides computer readable media with either (a) atomic coordinate data according to Table 1 or derived from Table 1 by homology modelling recorded thereon, said data defining the three-dimensional structure of KPR, at least one atom or at least one sub-domain thereof, or (b) structure factor data for KPR recorded thereon, the structure factor data being derivable from the atomic coordinate data of Table 1.

[0078] As used herein, “computer readable media” refers to any media which can be read and accessed directly by a computer. 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.

[0079] By providing such computer readable media, the atomic coordinate data can be routinely accessed to model KPR or a sub-domain 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.

[0080] 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.

[0081] As used herein, “a computer system” refers to the hardware means, software means and data storage means used to analyse the atomic coordinate data of the present invention. 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.

[0082] In another aspect, the invention provides a method of analysing a complex of KPR and a potential modulator comprising the step of employing (i) X-ray crystallographic diffraction data from the complex and (ii) a three-dimensional structure of KPR, or at least one sub-domain thereof, to generate a difference Fourier electron density map of the complex, the three-dimensional structure being defined by atomic coordinate data according to Table 1.

[0083] Therefore, such 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 KPR and the solved structure of uncomplexed KPR. These maps can then be used to determine whether and where a particular potential modulator binds to KPR and/or changes the conformation of KPR.

[0084] 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 Crystallograhy, A47, (1991), 110-119) can be used.

[0085] The structure is defined in Table 1 which gives atomic coordinate data for KPR and associated water molecules. Table 1 lists each atom by a unique number; the chemical element and (in the case of KPR) its position in each amino acid residue; the amino acid residue in which the element is located; the number of the residue; X, Y and Z coordinates which define, with respect to the crystallographic axes, the atomic position (in D) of the respective atom; the occupancy of the atom in the respective position; “B”, a temperature factor (in D2) which accounts for movement of the atom around its atomic centre; and atomic number.

[0086] Structure-Based Drug Design

[0087] Determination of the 3D structure of KPR provides important information about the likely active sites of KPR, particularly when comparisons are made with similar enzymes. This information may then be used for rational design of KPR inhibitors, e.g. by computational techniques which identify possible binding ligands for the active sites, by enabling linked-fragment approaches to drug design, and by enabling the identification and location of bound ligands using X-ray crystallographic analysis. These techniques are discussed in more detail below.

[0088] Greer et al. mentioned above describes an iterative approach to ligand design based on repeated sequences of computer modelling, protein-ligand complex formation and X-ray analysis. Thus novel thymidylate synthase inhibitor series were designed de novo by Greer et al., and KPR inhibitors may also be designed in the this way. More specifically, using e.g. GRID on the solved 3D structure of KPR, a potential modulator for KPR may be designed that complements the functionalities of the KPR active site(s). The potential modulator compound can then be synthesised, formed into a complex with KPR, and the complex then analysed by X-ray crystallography to identify the actual position of the bound compound.

[0089] Determination of the position of the potential modulator in the complex allows determination of the interactions of it with KPR. This will allow those of skill in the art to analyse the affinity and specificity of the compound for KPR, and to propose modifications to the compound to increase or decrease either or both of these properties. Thus the structure and/or functional groups of the compound 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 compound is obtained. Related approaches to structure-based drug design are also discussed in Bohacek et al., Medicinal Research Reviews, Vol.16, (1996), 3-50.

[0090] As a result of the determination of the KPR 3D structure, more purely computational techniques for rational drug design may also be used to design KPR modulators (for an overview of these techniques see e.g. Walters et al. mentioned above). 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 KPR modulators.

[0091] Linked-fragment approaches to drug design also require accurate information on the atomic coordinates of target receptors. Small compounds which have the potential to bind to regions of KPR which in themselves may not be modulator compounds may be assembled by chemical linkage to provide potential modulators. Thus the basic idea behind these approaches is to determine 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 ligands may be provided computationally and modelled in a computer system, or provided in an experimental setting, wherein crystals according to the invention are provided and a plurality of ligands soaked separately or in mixed pools into the crystal prior to X-ray analysis and determination of their location.

[0092] The binding site of two of more ligands are determined and may be connected to 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 KPR modulators is made possible by the determination of the KPR structure.

[0093] Many of the techniques and approaches to structure-based drug design described above require X-ray analysis to identify the binding position of a potential modulator in a complex with a protein. 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 potential modulator. However, in order to produce the map (as explained e.g. by Blundell et al. mentioned above) it is necessary to know beforehand the protein 3D structure (or at least the protein structure factors).

[0094] Therefore, determination of the KPR structure also allows difference Fourier electron density maps of complexes of KPR with a potential modulator to be produced, which can greatly assist the process of rational drug design.

[0095] The approaches to structure-based drug design described above all require initial identification of possible compounds for interaction with target bio-molecule (in this case KPR). Sometimes these compounds are known e.g. from the research literature. However, when they are not, 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 active 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 KPR structure allows the architecture and chemical nature of each KPR active 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.

[0096] Compounds which have a chemical structure selected using the methods of the invention described herein, wherein said compounds are KPR modulators, form a further aspect of the invention. Such compounds may be used in methods of medical treatments, such as in the treatment of bacterial infections in the human or animal body. The compounds may be used alone or in conjunction with other anti-bacterial compounds to enhance their effect.

[0097] 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.

[0098] The following example illustrates the invention.

[0099] Materials and Methods

[0100] Cloning of E. coli panE Gene.

[0101] The E. coli panE (apbA) gene sequence had been submitted to the EMBL database (Acc N° U34923) and this sequence is part of the plasmid pVJS78, which contains a 6 kb fragment of E. coli genomic DNA (obtained from Dr T Begley, Dept of Chemistry, Cornell University, New York). A PCR product, representing the full-length panE gene, was generated using the following primers EPANENdeF

[0102] (5′ ATACATATGAAAATTACCGTATTGGGATG 3′) and EPANEBamHIR

[0103] (5′ TATGGATCCTCACCAGGGGCGAGGCAAACC 3′), which had NdeI and

[0104] BamHI restriction sites respectively (underlined). This 915 bp PCR product was digested with NdeI/BamHI and ligated into NdeI/BamHI restricted pET24b vector (Novagen). The panE gene was sequenced and found to be identical to that in the database. Crude soluble protein extracts of the bacterial cells harboring pET24b-panE had measurable KPR activity

[0105] Protein Expression and Purification

[0106] E. coli BL21 Cell culture containing pET24-b-apbA was grown in LB media containing ampicillin (50 mg/mL) at 37° C. to an OD600 of 0.6-0.7, and expression of KPR was induced by addition of isopropylthio-β-D-galactoside (IPTG) to a final concentration of 0.5 mM. The cells were harvested after 4 h and resuspended in extraction buffer containing 100 mM KH2PO4 pH 7.5, 1 mM EDTA and 1 mM PMSF. Cells were lysed by sonication and centrifuged. Nucleic acids were precipitated by the addition of 5 mL protamine sulfate (2% w/v) and centrifugation. The supernatant was fractionated with solid ammonium sulfate and the precipitate occurring between 5%-40% saturation was collected by centrifugation. The protein was redissolved in 25 mM KH2PO4 pH 7.5 containing 1 mM EDTA, dialyzed against 2 L of the same buffer and purified by fast phase liquid chromatography (FPLC). The FPLC purification procedure consisted of passing the protein through two anion exchange and one gel filtration column. Protein, in less than 10 mL of buffer containing 25 mM potassium chloride, was applied to a Hiprep 16/10 Q XL anion exchange column and eluted with a linear 25 mM-500 mM potassium chloride gradient. Fractions containing KPR were concentrated and desalted. The protein solution, in less than 10 mL of buffer containing 25 mM potassium chloride, was then applied to a Source 15Q XV 16/10 anion exchange column and eluted with a linear 25 mM-500 mM potassium chloride gradient. Protein, in less than 5 ml of buffer, was then applied to a Hiload 16/60 Superdex 200 pg gel filtration column and fractions containing KPR were concentrated to greater than 5 mg/mL. Fractions were analyzed by SDS-PAGE, according to the method of Laemmli (Laemmli, 1970). Protein concentration was determined using the Bio-Rad protein assay kit, using bovine serum albumin as a standard and confirmed spectrophotometrically, using A280 (ε calculated) (Gill and von Hippel, 1989). Electrospray mass spectra were recorded on a VG BioQ quadrupole mass spectrometer. The mass of the protein calculated from the primary amino acid sequence (33, 870 Da) of the wild type compares well with the ESMS (33, 876 Da) of the recombinant protein. N-terminal sequencing for the first 9 residues as well as amino acid analysis was the same as the wild type.

[0107] Selenomethionine-substituted enzyme (SeMet KPR) was prepared by expression of the freshly transformed pET24-β-apbA. The E. coli BL21 cell culture was grown at 37° C. to an OD600 of 0.8 in M9 minimal media containing 4% glucose. The medium was then supplemented by 6 amino acids (Lys, Phe, Thr, Ile, Leu, Val) and selenomethionine at 50 mg/L, with 0.5% thiamine (Doublie, S., (1997) Methods Enzymol. 278, 523-530). Cells were induced using IPTG (25 mg/L) for two and a half hours and harvested. Purification of Se-Met KPR was performed as described above with addition of 5 mM DTT to prevent oxidation of the seleno-methionines.

[0108] Determination of KPR Activity.

[0109] KPR activity was determined at 37° C. in the forward direction by monitoring the decrease in NADPH over time (as absorbance at 340 nm) as described (7). The assay comprised 100 mM potassium phosphate buffer, pH 7.4, 150 μM NADPH, 30 nM KPR and was initiated with 500 μM potassium ketopantoate, in a final volume of 1 mL.

[0110] Crystallization

[0111] Regular prismatic KPR crystals were prepared by the hanging drop vapor-diffusion technique, using 25-27% PEG 4000, 0.1 M Tris pH 9.4 and 0.20-0.25 M NaOAc as the precipitant solution. Protein concentration was 11 mg/mL in 10 mM Hepes pH 8.0. The hanging drops, consisting of 1 μL of protein solution and 1 μL well solution. were equilibrated at 4° C. for several days. Crystals with dimensions 0.4×0.2×0.2 mm3 grew from clear drops. These belonged to the tetragonal space group P42212 with cell parameters a=b=104.2 Å and c=55.8 Å, accommodating one enzyme molecule per asymmetric unit, with a solvent content of 45%.

[0112] SeMet KPR crystals, prepared in a similar way to native KPR crystals, were obtained using two different protein concentrations, 8 mg/ml and 16 mg/ml. The Se-Met KPR stock solution contained 15 mM Tris, pH 8 and 2 mM DTT to protect the Se atoms from oxidation. Optimised crystallization conditions are 28-38% PEG 4000, 0.1 M Tris pH 9.4 Ånd 0.25 M NaOAc.

[0113] Data Collection and Processing

[0114] The structure of ketopantoate reductase (KPR) was solved by MAD method using a selenomethionine derivative. Data to 2.3 Å resolution were collected at 100 K, at 3 wavelengths on the BW7A beamline at the EMBL outstation in DESY, Hamburg. Flash-freezing of the crystal was proceeded by soaking for 30 s in a cryoprotectant solution consisting of 15% glycerol, 30% PEG 4000, 0.1 M Tris pH=9.4 and 0.25 M sodium-acetate. An X-ray fluorescence spectrum was recorded and used to select wavelengths for subsequent MAD data collection. Data were collected at the Se absorption edge λe=0.979272 Å (12 661.00 eV), the absorption peak λp=0.9790501 Å (12 663.77 eV) and at remote reference wavelength λr=0.885612 Å (14 000 eV). The diffraction data were indexed and integrated using the DENZO package (Otwinowski and Minor, 1997). The three data-sets were scaled to the remote data-set using SCALA (CCP4, 1994; Evans, 1997) and structure-factor amplitudes were calculated using TRUNCATE (CCP4, 1994). Statistics of the processed data are listed in Table 2. The native data set was collected to 1.7 Å resolution at the Daresbury SRS beamline 9.6. A cryo-protectant solution contained 30% PEG1500, 100 mM Tris buffer (pH 9.4), 300 mM sodium-acetate and 20% of glycerol.

TABLE 2
X-ray data collection statistics
	Se-Met derivative		Native
Dataset	Edge	Peak	Remote
Wavelength (Å)	0.979272	0.9790501	0.885612	0.87
Resolution (Å)	2.3	2.3	2.3	1.7
Unique reflections	13640	11259	13720	32249
Redundancy	3.77	4.5	3.95	5.4
Completeness (%)	95.2	96.3	97.5	94.9
Rano (%)	5.8	6.8	4.6	—
Rmerge (%)	9.9	10.8	9.4	4.3
f′, f″ (experimental)	−11.1873	−7.5644	−1.5	—
	4.1205	5.9692	—
f′, f″ (theoretical)	−11.0597	−7.46687	−1.3	—
	4.38418	6.29644	3.2
Phasing power	2.288	2.889	2.108	—
R				0.230
R (free)				0.289
No. reflexions:	working set			30610
	test set			1639
Ramachandran plot:	% residues favorable			91.9
	% residues			None
	unfavorable
R.m.s. deviation:	Bond lengths			0.016
	Bond angles			1.9
	Planarity			0.024

[0115] Structure Determination and Refinement

[0116] Six selenium sites were found with the program SHELXS96 (Sheldrick, 1996) using direct methods and anomalous difference data of λp Se-Met. Data were phased with SHARP (La Fortelle et al., 1997) using all three wavelength data sets, which also revealed two additional Se sites in the residual maps. Data collected at the remote wavelength were treated as the reference data set and resolution limits of 40 to 2.3 Å were imposed. Theoretical values of f′ and f″ were used and refined during analysis. The resulting values are very similar to the theoretical values and are given in Table 1. Experimental phases were improved by solvent flattening using SOLOMON(CCP4, 1994), via the SUSHI graphical user interface (La Fortelle et al., 1997) with a solvent content of 43%. The final electron-density map was easily interpretable and whole polypeptide chain was assigned based on the initial electron density map.

[0117] The polypeptide chain was fitted in MAD electron density map using program O (Jones et al., 1991). Rounds of maximum likelihood refinement with REFMAC (Murshudov et al., 1997) were alternated with visual inspection of electron density and manual rebuilding of side chains. Several rounds of simulated annealing with CNS (Brunger et al., 1998) were included to properly refine the position of the main-chain. The current model contains 291 residues and 272 water molecules.

[0118] Results and Discussion

[0119] KPR from E. coli was expressed and purified in order to determine its 3D structure using X-ray crystallography. The crystal structure was determined using selenomethionine-substituted KPR and MAD method.

[0120] Selenomethionine-substituted KPR was expressed in minimum medium containing a cocktail of six amino acids inhibiting methionine biosynthesis.

[0121] Structure Solution and Refinement

[0122] Initial phases were calculated by MAD technique using three data sets collected at wavelengths on and away from the selenium Kα absorption edge. After solvent flattening an easily interpretable electron-density map was obtained at 2.3 A resolution. Secondary structural elements were clearly defined in the electron density bones calculated with MAPMAN (Kleywegt & Jones, 1996).

[0123] The asymmetric unit consists of one monomeric KPR molecule. The main chain of the molecule was traced using secondary structure template building functionality in O. and the sequence was easily determined from the positions of selenium atoms from SHARP.

[0124] The model was improved by restrained isotropic maximum likelihood refinement with REFMAC. Crystallographic refinement was alternated with manual model rebuilding in O. Torsional simulated annealing (starting temperature 3000K) in CNS was used to improve difficult parts of the model. Ordered water molecules were modelled by automated cycles of water addition and removal by ARP (Perrakis et al., 1999) and refinement by REFMAC. A final model containing 291 residues and 272 water molecules was refined to an R factor of 0.230 and Rfree of 0.289. The last 12 residues at the c-terminus are not visible in electron density maps.

[0125] The quality of the model and its geometry were assessed by PROCHECK (Laskowski et al., 1993). There are no Ramachandran outliers, and 91.9% of residues lie in the most favoured regions of the plot.

[0126] Overall Structure

[0127] The secondary structure assignment of KPR, as analyzed using the DSSP programme (Kabsch and Sander, 1983), shows the molecule to be constructed from twelve α-helices, three 310-helices and eleven β-strands. The enzyme is monomeric and has two domains separated by a deep cleft. The N-terminal domain has an alpha-beta fold of Rossman type and comprises residues 1-169. It is formed of two β-sheets joined together by β-bridge and three α-helices. The central α-helix is surrounded by the seven-stranded β-sheet of mixed parallel and antiparallel character and also by a smaller four stranded β-sheet that contains two pairs of antiparallel strands. This central α-helix (α1) separates the first two β-strands and comprises a dinucleotide binding unit. The sequence between the end of β1-strand and the α1-helix contains a glycine-rich region. The GCGALG sequence represent the motif GXGXXG that is very often an indicator of the nucleotide binding site in dehydrogenases (Branden, C. Tooze, J. (1991) Introduction to protein structure, Garland Publishing, Inc. New York). The C-terminal domain is all alpha-helical composed of the eight α-helices including remaining residues to the C-terminus (170-291).

[0128] Nucleotide-Binding Site

[0129] The structural similarity between the N-terminal domains of KPR and human SCHAD enabled us to carry out molecular modelling to identify the cofactor binding site, since the structure of the binary complex of SCHAD with NAD+ has been determined (PDB code 2hdh). The SCHAD structure was fitted to the KPR structure and NAD+ cofactor extracted from SCHAD to KPR. Water molecules clashing with cofactor were removed and hydrogen atoms added to the model with SYBYL Biopolymer module (Tripos, 1998) for force field optimization purposes. The NAD+ molecule was edited to NADPH and optimized as a substructure using the Tripos force field. In the process the pyrophosphate group of NADPH changed conformation to fit into the inter-domain cleft (FIG. 2A). Only side-chains involved in interactions with cofactor moved during geometry optimization. In the resulting model NADPH is largely buried between two domains, with only the adenine moiety of NADPH partially exposed, as seen in many enzymes with the nucleotide binding fold. There is no evidence of direct hydrogen bonding between the adenine ring and the protein. The adenine pocket contains side chains of residues Leu6, Leu7l, Gln75, Leu30 and Arg31. The glycine-rich turn that lies between β-1 of the N-terminal domain and α1 is directly involved in the recognition of the adenine ribose through two main chain hydrogen bonds of hydroxyl groups with main chain nitrogen atoms of residues Cys8 and Gly9. The 2′-phosphate (which distinguishes NADPH from NADH) is involved in two salt bridges with the guanidine moieties of residues Arg31 and Arg124 that are located on the protein surface. The conserved residue Lys72 interacts with the pyrophosphate moiety through three hydrogen bonds, implying that this residue plays a major role in cofactor recognition. This observation is interesting, since it has previously been reported that a Lys72Ala mutant had wild-type enzyme activity in a crude cell free preparation, comparable to their Asp250Ala mutation, which is remote from the active site. A second residue, Leu11, recognises pyrophosphate through its main chain nitrogen, which interacts with nicotinamide ribose phosphate. The nicotinamide portion of the cofactor is anchored in place by hydrogen bonds to its ribose hydroxyl by the conserved residues Glu256 Oε2 atom and Asn98 main chain nitrogen atom (FIG. 2B). Additionally, the nicotinamide ring interacts with main chain nitrogen atom of His120 and Ala122.

[0130] Substrate Binding Site and Reaction Mechanism

[0131] Although the apoenzyme is in a more open conformation than would be expected for catalysis, it is still possible to identify key catalytic residues and those involved in binding ketopantoate. In particular Lys176 and Glu256, which have previously been identified as being important in catalysis by site directed mutagenesis, are located near the putative NADPH site, some distance apart, and could accommodate ketopantoate between them. From knowledge of the stereochemical course of the reaction, that the proS hydrogen of NADPH is delivered to the si face of ketopantoate, and considering the expected geometry for hydride transfer, it is possible to construct two models for the ternary complex. In one, the carbonyl group of ketopantoate points away from the nitrogen of the dihydronicotinamide ring. This places the carboxyl group towards Lys176 and the hydroxymethyl group towards Glu256. However it introduces unfavorable steric interactions between the gem dimethyl group on ketopantoate and the C-3 primary amide on the dehydronicotinamide ring. The alternative structure is generated from the first one, by rotating ketopantoate in the plane of the carbonyl group by 180 degrees, so that the latter points towards the nitrogen of the dehydronicotinamide ring. This places the carboxyl group of ketopantoate towards Glu256 and the hydroxymethyl group towards Lys176. FIG. 2B shows this structure and highlights other key conserved residues, Asn98 and Ser244, (after some slight adjustment of the side chains of these residues and a larger movement of Lys176). In this structure, there is good hydrogen bonding of Lys176 and Asn98 to the hydroxyl group of ketopantoate, and of Ser244 to the carboxyl. Furthermore Glu256 could act as the acid to protonate the developing negative charge on ketopantoate as hydride is delivered from NADPH, albeit relayed through the C-3 hydroxyl of the ribose.

[0132] Structural and Functional Comparison of KPR with Other Enzymes

[0133] Comparison of the fold against all structures in the Protein Data Bank using the DALI server (Holm et al., 1995; Holm & Sander, 1998) revealed that the KPR molecule is topographically similar to the N-(1-D-carboxylethyl)-L norvaline dehydrogenase (CENDH) (Britton et al., 1998) in both domains while N-terminal domain shows similarity to some dehydrogenases including human heart short chain L-3-hydroxyacyl-CoA dehydrogenase (SCHAD) (Barycki et al., 1999), 6-phosphogluconate dehydrogenase (6PGDH) (Phillips et al., 1998) and plant acetohydroxy acid isomeroreductase (Biou et al., 1997) as well. Despite the high degree of structural similarity of KPR with CENDH, CENDH is a homodimer (subunit molecular weight of ˜36000), with the α-helical C-terminal domain providing the dimerisation interface while KPR is monomer.

[0134] In conclusion, KPR plays a key step on the biosynthesis of pantothenate, and as such is a potential herbicide and antimicrobial target. From the structure of the apoenzyme provided herein it has been possible to construct models of the holoenzyme and the ternary complex, and provide a proposed catalytic mechanism. The model confirms the importance of Lys176 and Glu256 in binding ketopantoate and in the catalytic mechanism. Thus the structure of the present invention will be useful in the design of novel modulators of KPR activity.

REFERENCES

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[0136] Berlyn, M. K. B., Low, K. B., Rudd, K. E., 1996. In: Neidhardt, F. C., et al (Eds.), Escherichia coli and Salmonella, 2nd ed., ASM Press, Washington, D.C., pp. 1715-1902.

[0137] Biou, V., Dumas, R., Cohen-Addad. C., Douce, R., Job, D., Pebay-Peyroula, E. (1997) EMBO J. 16 (12), 3405-3415.

[0138] Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T. & Warren, C. L. (1998). Acta Crystallographica D54, 905-921.

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[0141] Dumas, R., Butikofer, M. -C., Job, D. and Douce, R. (1995) Biochemistry 34, 6026-6036.

[0142] Elischewski, F, Puller A., Kalinowski J. (1999) J. Biotech. 75, 135-146.

[0143] Evans, P. R. (1997). Scaling of MAD data. In Recent Advances in Phasing (ed. K. S. Wilson, G. Davies, A. W. Ashton and S. Bailey), pp. 97-102. Council for the Central Laboratory of the Research Councils Daresbury Laboratory, Daresbury, UK.

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[0146] Genschel, U. (1997). Molecular and biochemical analyses of pantothenic acid biosynthetic enzymes. Ph.D. Thesis, University of Cambridge.

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[0150] Jackowski, S., 1996. In: Neidhardt, F. C., et al (Eds.), Escherichia coli and Salmonella, 2nd ed., ASM Press, Washington, D.C., pp. 687-694.

[0151] Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. (1991). Acta Crystallographica A47, 110-119.

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[0159] La Fortelle, E. de & Bricogne, G. (1997) Methods in Enzymology 276, 472-494.

[0160] La Fortelle, E. d., Irwin, J. J. & Bricogne, G. (1997). Advances in MIR and MAD phasing: Maximum-likelihood refinement in a graphical environment, with SHARP. In CCP4 study week-end: Recent Advances in Phasing. (ed. K. S. Wilson, G. Davies, A. W. Ashton and S. Bailey), Daresbury Laboratory, UK

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TABLE 1
ORIGX1	1.000000	0.000000	0.000000	0.00000
ORIGX2	0.000000	1.000000	0.000000	0.00000
ORIGX3	0.000000	0.000000	1.000000	0.00000
CRYST1	103.732	103.732	55.737	90.000	90.000	90.000
SCALE1	0.00964	0.00000	0.00000	0.00000
SCALE2	0.00000	0.00964	0.00000	0.00000
SCALE3	0.00000	0.00000	0.01794	0.00000
ATOM	1	CB	MET A	1	53.656	8.328	−7.807	1.00	25.16	6	C
ATOM	2	CG	MET A	1	53.462	8.700	−6.359	1.00	27.38	6	C
ATOM	3	SD	MET A	1	52.363	10.015	−5.974	1.00	31.67	16	S
ATOM	4	CE	MET A	1	53.026	10.727	−4.486	1.00	32.03	6	C
ATOM	5	C	MET A	1	55.984	7.342	−7.629	1.00	20.87	6	C
ATOM	6	O	MET A	1	56.594	6.589	−6.865	1.00	23.34	8	O
ATOM	7	N	MET A	1	53.946	5.919	−7.256	1.00	24.61	7	N
ATOM	8	CA	MET A	1	54.518	7.082	−8.004	1.00	23.08	6	C
ATOM	9	N	LYS A	2	56.562	8.341	−8.294	1.00	19.63	7	N
ATOM	10	CA	LYS A	2	57.984	8.698	−8.121	1.00	22.21	6	C
ATOM	11	CB	LYS A	2	58.564	8.717	−9.549	1.00	25.49	6	C
ATOM	12	CG	LYS A	2	60.078	8.679	−9.528	1.00	29.33	6	C
ATOM	13	CD	LYS A	2	60.516	8.306	−10.953	1.00	29.37	6	C
ATOM	14	CE	LYS A	2	61.928	7.843	−11.073	1.00	31.30	6	C
ATOM	15	NZ	LYS A	2	62.252	7.690	−12.536	1.00	29.64	7	N
ATOM	16	C	LYS A	2	58.051	10.032	−7.426	1.00	17.19	6	C
ATOM	17	O	LYS A	2	57.404	11.028	−7.852	1.00	17.21	8	O
ATOM	18	N	ILE A	3	58.764	10.044	−6.241	1.00	14.92	7	N
ATOM	19	CA	ILE A	3	58.705	11.287	−5.475	1.00	15.39	6	C
ATOM	20	CB	ILE A	3	57.999	11.115	−4.097	1.00	17.61	6	C
ATOM	21	CG2	ILE A	3	57.944	12.447	−3.357	1.00	17.47	6	C
ATOM	22	CG1	ILE A	3	56.536	10.592	−4.199	1.00	20.47	6	C
ATOM	23	CD1	ILE A	3	56.475	9.067	−4.169	1.00	21.64	6	C
ATOM	24	C	ILE A	3	60.147	11.685	−5.129	1.00	13.79	6	C
ATOM	25	O	ILE A	3	60.955	10.803	−4.833	1.00	16.60	8	O
ATOM	26	N	THR A	4	60.456	12.954	−5.335	1.00	13.50	7	N
ATOM	27	CA	THR A	4	61.760	13.455	−4.818	1.00	12.56	6	C
ATOM	28	CB	THR A	4	62.444	14.378	−5.800	1.00	14.61	6	C
ATOM	29	OG1	THR A	4	62.917	13.532	−6.904	1.00	14.84	8	O
ATOM	30	CG2	THR A	4	63.682	15.024	−5.232	1.00	15.01	6	C
ATOM	31	C	THR A	4	61.481	14.247	−3.552	1.00	13.83	6	C
ATOM	32	O	THR A	4	60.592	15.091	−3.541	1.00	15.98	8	O
ATOM	33	N	VAL A	5	62.138	13.871	−2.449	1.00	15.82	7	N
ATOM	34	CA	VAL A	5	61.931	14.584	−1.162	1.00	16.34	6	C
ATOM	35	CB	VAL A	5	61.855	13.590	−0.006	1.00	16.01	6	C
ATOM	36	CG1	VAL A	5	61.594	14.392	1.273	1.00	15.34	6	C
ATOM	37	CG2	VAL A	5	60.588	12.738	−0.276	1.00	14.70	6	C
ATOM	38	C	VAL A	5	63.098	15.565	−0.956	1.00	13.32	6	C
ATOM	39	O	VAL A	5	64.229	15.061	−0.885	1.00	16.84	8	O
ATOM	40	N	LEU A	6	62.814	16.824	−0.845	1.00	15.55	7	N
ATOM	41	CA	LEU A	6	63.888	17.841	−0.764	1.00	14.62	6	C
ATOM	42	CB	LEU A	6	63.388	19.096	−1.459	1.00	17.58	6	C
ATOM	43	CG	LEU A	6	64.380	20.273	−1.534	1.00	22.04	6	C
ATOM	44	CD1	LEU A	6	65.793	19.938	−1.876	1.00	18.88	6	C
ATOM	45	CD2	LEU A	6	63.812	21.299	−2.524	1.00	19.30	6	C
ATOM	46	C	LEU A	6	64.190	18.068	0.708	1.00	18.31	6	C
ATOM	47	O	LEU A	6	63.351	18.593	1.448	1.00	20.51	8	O
ATOM	48	N	GLY A	7	65.360	17.604	1.139	1.00	23.20	7	N
ATOM	49	CA	GLY A	7	65.757	17.747	2.553	1.00	24.61	6	C
ATOM	50	C	GLY A	7	65.807	16.365	3.176	1.00	24.52	6	C
ATOM	51	O	GLY A	7	64.791	15.647	3.078	1.00	27.29	8	O
ATOM	52	N	CYS A	8	66.918	15.864	3.690	1.00	25.89	7	N
ATOM	53	CA	CYS A	8	67.001	14.560	4.315	1.00	28.80	6	C
ATOM	54	C	CYS A	8	67.175	14.739	5.833	1.00	25.20	6	C
ATOM	55	O	CYS A	8	67.938	13.961	6.413	1.00	25.70	8	O
ATOM	56	CB	CYS A	8	68.070	13.525	3.902	1.00	34.71	6	C
ATOM	57	SG	CYS A	8	67.189	12.009	3.419	1.00	46.36	16	S
ATOM	58	N	GLY A	9	66.475	15.712	6.411	1.00	24.26	7	N
ATOM	59	CA	GLY A	9	66.532	15.945	7.854	1.00	22.02	6	C
ATOM	60	C	GLY A	9	65.406	15.219	8.574	1.00	20.60	6	C
ATOM	61	O	GLY A	9	64.955	14.239	7.986	1.00	18.40	8	O
ATOM	62	N	ALA A	10	64.963	15.735	9.748	1.00	19.36	7	N
ATOM	63	CA	ALA A	10	63.921	14.868	10.426	1.00	21.05	6	C
ATOM	64	CB	ALA A	10	63.551	15.551	11.745	1.00	21.49	6	C
ATOM	65	C	ALA A	10	62.636	14.662	9.666	1.00	19.44	6	C
ATOM	66	O	ALA A	10	62.087	13.549	9.525	1.00	19.81	8	O
ATOM	67	N	LEU A	11	62.002	15.784	9.235	1.00	20.27	7	N
ATOM	68	CA	LEU A	11	60.728	15.686	8.536	1.00	18.28	6	C
ATOM	69	CB	LEU A	11	60.139	17.119	8.405	1.00	21.71	6	C
ATOM	70	CG	LEU A	11	58.889	17.163	7.555	1.00	22.72	6	C
ATOM	71	CD1	LEU A	11	57.771	16.356	8.192	1.00	24.38	6	C
ATOM	72	CD2	LEU A	11	58.516	18.637	7.299	1.00	23.72	6	C
ATOM	73	C	LEU A	11	60.889	15.004	7.181	1.00	17.57	6	C
ATOM	74	O	LEU A	11	60.011	14.158	6.766	1.00	17.25	8	O
ATOM	75	N	GLY A	12	62.012	15.263	6.511	1.00	15.67	7	N
ATOM	76	CA	GLY A	12	62.254	14.590	5.248	1.00	18.30	6	C
ATOM	77	C	GLY A	12	62.451	13.094	5.370	1.00	18.15	6	C
ATOM	78	O	GLY A	12	61.919	12.267	4.570	1.00	17.92	8	O
ATOM	79	N	GLN A	13	63.199	12.653	6.397	1.00	19.55	7	N
ATOM	80	CA	GLN A	13	63.335	11.210	6.624	1.00	18.33	6	C
ATOM	81	CB	GLN A	13	64.442	10.939	7.700	1.00	18.91	6	C
ATOM	82	CG	GLN A	13	65.818	11.293	7.063	1.00	20.08	6	C
ATOM	83	CD	GLN A	13	66.940	10.761	7.997	1.00	22.93	6	C
ATOM	84	OE1	GLN A	13	66.808	9.659	8.507	1.00	23.62	8	O
ATOM	85	NE2	GLN A	13	67.941	11.601	8.170	1.00	25.45	7	N
ATOM	86	C	GLN A	13	62.000	10.622	7.061	1.00	15.51	6	C
ATOM	87	O	GLN A	13	61.745	9.472	6.751	1.00	16.12	8	O
ATOM	88	N	LEU A	14	61.181	11.341	7.835	1.00	14.35	7	N
ATOM	89	CA	LEU A	14	59.860	10.711	8.172	1.00	17.19	6	C
ATOM	90	CB	LEU A	14	59.139	11.750	9.061	1.00	16.49	6	C
ATOM	91	CG	LEU A	14	57.686	11.325	9.410	1.00	18.59	6	C
ATOM	92	CD1	LEU A	14	57.638	10.077	10.285	1.00	21.00	6	C
ATOM	93	CD2	LEU A	14	56.942	12.463	10.096	1.00	19.96	6	C
ATOM	94	C	LEU A	14	59.048	10.470	6.906	1.00	17.91	6	C
ATOM	95	O	LEU A	14	58.436	9.391	6.811	1.00	15.26	8	O
ATOM	96	N	TRP A	15	59.039	11.449	5.978	1.00	16.91	7	N
ATOM	97	CA	TRP A	15	58.322	11.180	4.692	1.00	16.16	6	C
ATOM	98	CB	TRP A	15	58.076	12.517	3.938	1.00	17.68	6	C
ATOM	99	CG	TRP A	15	56.910	13.278	4.501	1.00	18.00	6	C
ATOM	100	CD2	TRP A	15	55.522	13.014	4.245	1.00	19.10	6	C
ATOM	101	CE2	TRP A	15	54.770	13.956	4.964	1.00	18.74	6	C
ATOM	102	CE3	TRP A	15	54.873	12.034	3.467	1.00	19.08	6	C
ATOM	103	CD1	TRP A	15	56.937	14.340	5.341	1.00	18.78	6	C
ATOM	104	NE1	TRP A	15	55.637	14.772	5.633	1.00	19.15	7	N
ATOM	105	CZ2	TRP A	15	53.375	13.984	4.927	1.00	20.45	6	C
ATOM	106	CZ3	TRP A	15	53.480	12.066	3.411	1.00	19.42	6	C
ATOM	107	CH2	TRP A	15	52.773	13.023	4.161	1.00	17.84	6	C
ATOM	108	C	TRP A	15	58.917	10.151	3.787	1.00	16.85	6	C
ATOM	109	O	TRP A	15	58.248	9.258	3.153	1.00	17.10	8	O
ATOM	110	N	LEU A	16	60.263	10.149	3.684	1.00	15.77	7	N
ATOM	111	CA	LEU A	16	60.975	9.137	2.892	1.00	20.28	6	C
ATOM	112	CB	LEU A	16	62.478	9.343	2.927	1.00	20.13	6	C
ATOM	113	CG	LEU A	16	62.958	10.487	2.008	1.00	20.00	6	C
ATOM	114	CD1	LEU A	16	64.361	10.910	2.379	1.00	21.07	6	C
ATOM	115	CD2	LEU A	16	62.876	10.141	0.529	1.00	21.60	6	C
ATOM	116	C	LEU A	16	60.615	7.728	3.436	1.00	20.33	6	C
ATOM	117	O	LEU A	16	60.383	6.818	2.634	1.00	19.53	8	O
ATOM	118	N	THR A	17	60.741	7.552	4.758	1.00	19.26	7	N
ATOM	119	CA	THR A	17	60.371	6.280	5.398	1.00	18.67	6	C
ATOM	120	CB	THR A	17	60.546	6.360	6.929	1.00	19.72	6	C
ATOM	121	OG1	THR A	17	61.930	6.610	7.205	1.00	18.94	8	O
ATOM	122	CG2	THR A	17	60.050	5.086	7.559	1.00	20.09	6	C
ATOM	123	C	THR A	17	58.938	5.874	5.062	1.00	18.71	6	C
ATOM	124	O	THR A	17	58.697	4.747	4.636	1.00	20.38	8	O
ATOM	125	N	ALA A	18	57.966	6.814	5.202	1.00	17.14	7	N
ATOM	126	CA	ALA A	18	56.591	6.411	4.941	1.00	16.53	6	C
ATOM	127	CB	ALA A	18	55.614	7.586	5.288	1.00	16.23	6	C
ATOM	128	C	ALA A	18	56.315	6.082	3.489	1.00	18.72	6	C
ATOM	129	O	ALA A	18	55.576	5.120	3.148	1.00	17.41	8	O
ATOM	130	N	LEU A	19	56.908	6.858	2.596	1.00	18.01	7	N
ATOM	131	CA	LEU A	19	56.757	6.614	1.159	1.00	18.56	6	C
ATOM	132	CB	LEU A	19	57.315	7.733	0.289	1.00	17.67	6	C
ATOM	133	CG	LEU A	19	56.585	9.039	0.338	1.00	18.41	6	C
ATOM	134	CD1	LEU A	19	57.427	10.221	−0.135	1.00	17.13	6	C
ATOM	135	CD2	LEU A	19	55.270	9.124	−0.474	1.00	19.35	6	C
ATOM	136	C	LEU A	19	57.410	5.294	0.745	1.00	19.60	6	C
ATOM	137	O	LEU A	19	56.838	4.593	−0.077	1.00	21.93	8	O
ATOM	138	N	CYS A	20	58.543	5.068	1.379	1.00	21.17	7	N
ATOM	139	CA	CYS A	20	59.314	3.889	1.205	1.00	26.06	6	C
ATOM	140	CB	CYS A	20	60.662	3.921	1.943	1.00	30.09	6	C
ATOM	141	SG	CYS A	20	61.845	4.632	0.747	1.00	38.10	16	S
ATOM	142	C	CYS A	20	58.579	2.672	1.706	1.00	28.22	6	C
ATOM	143	O	CYS A	20	59.071	1.924	0.908	1.00	36.01	8	O
ATOM	144	N	LYS A	21	57.768	2.656	2.704	1.00	24.14	7	N
ATOM	145	CA	LYS A	21	57.047	1.519	3.193	1.00	25.65	6	C
ATOM	146	CB	LYS A	21	56.646	1.747	4.660	1.00	27.10	6	C
ATOM	147	CG	LYS A	21	57.737	1.801	5.711	1.00	27.34	6	C
ATOM	148	CD	LYS A	21	57.106	1.829	7.074	1.00	30.27	6	C
ATOM	149	CE	LYS A	21	56.401	3.129	7.419	1.00	31.99	6	C
ATOM	150	NZ	LYS A	21	56.267	3.203	8.950	1.00	34.09	7	N
ATOM	151	C	LYS A	21	55.748	1.120	2.484	1.00	26.37	6	C
ATOM	152	O	LYS A	21	55.197	0.082	2.622	1.00	28.40	8	O
ATOM	153	N	GLN A	22	55.102	1.902	1.657	1.00	26.00	7	N
ATOM	154	CA	GLN A	22	54.106	1.895	0.699	1.00	25.65	6	C
ATOM	155	CB	GLN A	22	53.261	3.184	0.606	1.00	25.09	6	C
ATOM	156	CG	GLN A	22	52.420	3.247	1.925	1.00	28.14	6	C
ATOM	157	CD	GLN A	22	51.388	2.138	1.882	1.00	30.98	6	C
ATOM	158	OE1	GLN A	22	51.164	1.365	2.805	1.00	33.33	8	O
ATOM	159	NE2	GLN A	22	50.703	1.992	0.756	1.00	28.07	7	N
ATOM	160	C	GLN A	22	54.677	1.532	−0.670	1.00	25.24	6	C
ATOM	161	O	GLN A	22	53.814	1.430	−1.551	1.00	27.33	8	O
ATOM	162	N	GLY A	23	55.985	1.321	−0.859	1.00	22.64	7	N
ATOM	163	CA	GLY A	23	56.396	0.840	−2.172	1.00	25.64	6	C
ATOM	164	C	GLY A	23	56.560	1.832	−3.299	1.00	26.93	6	C
ATOM	165	O	GLY A	23	56.815	1.475	−4.461	1.00	26.62	8	O
ATOM	166	N	HIS A	24	56.570	3.131	−2.954	1.00	23.72	7	N
ATOM	167	CA	HIS A	24	56.787	4.167	−3.937	1.00	19.67	6	C
ATOM	168	CB	HIS A	24	56.287	5.539	−3.430	1.00	18.69	6	C
ATOM	169	CG	HIS A	24	54.813	5.561	−3.226	1.00	24.69	6	C
ATOM	170	CD2	HIS A	24	54.059	5.544	−2.097	1.00	21.39	6	C
ATOM	171	ND1	HIS A	24	53.926	5.636	−4.274	1.00	25.95	7	N
ATOM	172	CE1	HIS A	24	52.679	5.687	−3.786	1.00	25.47	6	C
ATOM	173	NE2	HIS A	24	52.744	5.620	−2.456	1.00	22.89	7	N
ATOM	174	C	HIS A	24	58.252	4.279	−4.270	1.00	19.83	6	C
ATOM	175	O	HIS A	24	59.089	3.816	−3.529	1.00	23.43	8	O
ATOM	176	N	GLU A	25	58.572	4.780	−5.452	1.00	17.34	7	N
ATOM	177	CA	GLU A	25	59.954	4.966	−5.910	1.00	20.52	6	C
ATOM	178	CB	GLU A	25	60.058	5.072	−7.419	1.00	20.84	6	C
ATOM	179	CG	GLU A	25	59.874	3.705	−8.085	1.00	29.19	6	C
ATOM	180	CD	GLU A	25	59.997	3.925	−9.594	1.00	32.13	6	C
ATOM	181	OE1	GLU A	25	61.038	4.393	−10.102	1.00	38.37	8	O
ATOM	182	OE2	GLU A	25	58.986	3.638	−10.237	1.00	37.08	8	O
ATOM	183	C	GLU A	25	60.311	6.318	−5.303	1.00	17.03	6	C
ATOM	184	O	GLU A	25	59.549	7.266	−5.523	1.00	18.66	8	O
ATOM	185	N	VAL A	26	61.394	6.418	−4.549	1.00	16.73	7	N
ATOM	186	CA	VAL A	26	61.711	7.667	−3.880	1.00	18.82	6	C
ATOM	187	CB	VAL A	26	61.228	7.674	−2.413	1.00	21.87	6	C
ATOM	188	CG1	VAL A	26	59.799	7.325	−2.163	1.00	23.24	6	C
ATOM	189	CG2	VAL A	26	62.084	6.731	−1.578	1.00	25.16	6	C
ATOM	190	C	VAL A	26	63.214	7.980	−3.894	1.00	19.86	6	C
ATOM	191	O	VAL A	26	64.117	7.097	−4.092	1.00	20.32	8	O
ATOM	192	N	GLN A	27	63.502	9.258	−3.856	1.00	16.71	7	N
ATOM	193	CA	GLN A	27	64.884	9.723	−3.700	1.00	18.79	6	C
ATOM	194	CB	GLN A	27	65.643	10.142	−4.955	1.00	19.11	6	C
ATOM	195	CG	GLN A	27	65.385	11.526	−5.489	1.00	18.83	6	C
ATOM	196	CD	GLN A	27	66.341	11.935	−6.630	1.00	19.19	6	C
ATOM	197	OE1	GLN A	27	67.464	11.424	−6.644	1.00	22.00	8	O
ATOM	198	NE2	GLN A	27	65.775	12.832	−7.417	1.00	18.74	7	N
ATOM	199	C	GLN A	27	64.803	10.912	−2.723	1.00	18.35	6	C
ATOM	200	O	GLN A	27	63.811	11.629	−2.617	1.00	17.81	8	O
ATOM	201	N	GLY A	28	65.981	11.156	−2.062	1.00	20.09	7	N
ATOM	202	CA	GLY A	28	66.059	12.440	−1.303	1.00	19.20	6	C
ATOM	203	C	GLY A	28	66.936	13.387	−2.146	1.00	19.03	6	C
ATOM	204	O	GLY A	28	67.406	13.096	−3.253	1.00	20.33	8	O
ATOM	205	N	TRP A	29	67.018	14.619	−1.675	1.00	20.95	7	N
ATOM	206	CA	TRP A	29	67.830	15.646	−2.337	1.00	19.59	6	C
ATOM	207	CB	TRP A	29	66.947	16.516	−3.232	1.00	20.98	6	C
ATOM	208	CG	TRP A	29	67.815	17.265	−4.195	1.00	23.63	6	C
ATOM	209	CD2	TRP A	29	68.091	16.950	−5.559	1.00	25.60	6	C
ATOM	210	CE2	TRP A	29	68.993	17.914	−6.029	1.00	24.26	6	C
ATOM	211	CE3	TRP A	29	67.648	15.919	−6.411	1.00	24.54	6	C
ATOM	212	CD1	TRP A	29	68.546	18.401	−3.902	1.00	22.61	6	C
ATOM	213	NE1	TRP A	29	69.263	18.803	−4.980	1.00	23.69	7	N
ATOM	214	CZ2	TRP A	29	69.454	17.872	−7.328	1.00	24.60	6	C
ATOM	215	CZ3	TRP A	29	68.087	15.903	−7.726	1.00	25.88	6	C
ATOM	216	CH2	TRP A	29	69.006	16.888	−8.138	1.00	27.86	6	C
ATOM	217	C	TRP A	29	68.516	16.467	−1.230	1.00	22.92	6	C
ATOM	218	O	TRP A	29	67.784	17.107	−0.463	1.00	22.38	8	O
ATOM	219	N	LEU A	30	69.846	16.551	−1.269	1.00	24.34	7	N
ATOM	220	CA	LEU A	30	70.650	17.199	−0.239	1.00	27.04	6	C
ATOM	221	CB	LEU A	30	71.818	16.374	0.282	1.00	28.94	6	C
ATOM	222	CG	LEU A	30	71.574	15.166	1.178	1.00	33.56	6	C
ATOM	223	CD1	LEU A	30	72.854	14.355	1.393	1.00	37.67	6	C
ATOM	224	CD2	LEU A	30	70.974	15.623	2.497	1.00	34.22	6	C
ATOM	225	C	LEU A	30	71.270	18.505	−0.754	1.00	29.02	6	C
ATOM	226	O	LEU A	30	71.553	18.620	−1.932	1.00	27.41	8	O
ATOM	227	N	ALA A	31	71.439	19.492	0.126	1.00	32.32	7	N
ATOM	228	CA	ALA A	31	72.085	20.745	−0.268	1.00	34.74	6	C
ATOM	229	CB	ALA A	31	71.906	21.785	0.827	1.00	35.48	6	C
ATOM	230	C	ALA A	31	73.544	20.476	−0.636	1.00	34.80	6	C
ATOM	231	O	ALA A	31	74.089	21.067	−1.574	1.00	36.63	8	O
ATOM	232	N	VAL A	32	74.193	19.536	0.020	1.00	37.59	7	N
ATOM	233	CA	VAL A	32	75.532	19.049	−0.235	1.00	39.02	6	C
ATOM	234	CB	VAL A	32	76.408	18.846	1.014	1.00	41.34	6	C
ATOM	235	CG1	VAL A	32	77.795	18.385	0.595	1.00	42.42	6	C
ATOM	236	CG2	VAL A	32	76.521	20.102	1.864	1.00	42.34	6	C
ATOM	237	C	VAL A	32	75.384	17.670	−0.909	1.00	37.58	6	C
ATOM	238	O	VAL A	32	75.199	16.639	−0.263	1.00	38.05	8	O
ATOM	239	N	PRO A	33	75.462	17.665	−2.226	1.00	37.22	7	N
ATOM	240	CD	PRO A	33	75.719	18.835	−3.101	1.00	37.43	6	C
ATOM	241	CA	PRO A	33	75.243	16.462	−3.013	1.00	35.52	6	C
ATOM	242	CB	PRO A	33	75.530	16.861	−4.452	1.00	36.13	6	C
ATOM	243	CG	PRO A	33	75.440	18.344	−4.487	1.00	37.75	6	C
ATOM	244	C	PRO A	33	76.011	15.249	−2.566	1.00	36.25	6	C
ATOM	245	O	PRO A	33	77.193	15.245	−2.257	1.00	36.26	8	O
ATOM	246	N	GLN A	34	75.284	14.135	−2.429	1.00	34.19	7	N
ATOM	247	CA	GLN A	34	75.785	12.828	−2.112	1.00	35.75	6	C
ATOM	248	CB	GLN A	34	75.750	12.408	−0.649	1.00	39.04	6	C
ATOM	249	CG	GLN A	34	76.549	13.260	0.311	1.00	43.93	6	C
ATOM	250	CD	GLN A	34	76.547	12.770	1.742	1.00	47.29	6	C
ATOM	251	OE1	GLN A	34	75.712	13.219	2.535	1.00	50.44	8	O
ATOM	252	NE2	GLN A	34	77.461	11.877	2.088	1.00	49.07	7	N
ATOM	253	C	GLN A	34	74.858	11.902	−2.917	1.00	33.61	6	C
ATOM	254	O	GLN A	34	73.722	12.272	−3.172	1.00	32.97	8	O
ATOM	255	N	PRO A	35	75.370	10.758	−3.305	1.00	30.29	7	N
ATOM	256	CD	PRO A	35	76.783	10.321	−3.124	1.00	31.14	6	C
ATOM	257	CA	PRO A	35	74.605	9.826	−4.109	1.00	28.27	6	C
ATOM	258	CB	PRO A	35	75.683	8.843	−4.606	1.00	28.55	6	C
ATOM	259	CG	PRO A	35	76.677	8.850	−3.483	1.00	29.06	6	C
ATOM	260	C	PRO A	35	73.521	9.134	−3.324	1.00	27.10	6	C
ATOM	261	O	PRO A	35	72.672	8.499	−3.961	1.00	24.38	8	O
ATOM	262	N	TYR A	36	73.518	9.108	−1.984	1.00	26.11	7	N
ATOM	263	CA	TYR A	36	72.515	8.467	−1.178	1.00	28.72	6	C
ATOM	264	CB	TYR A	36	72.976	7.107	−0.635	1.00	30.45	6	C
ATOM	265	CG	TYR A	36	73.447	6.127	−1.687	1.00	30.95	6	C
ATOM	266	CD1	TYR A	36	74.785	6.123	−2.064	1.00	31.40	6	C
ATOM	267	CE1	TYR A	36	75.231	5.271	−3.067	1.00	32.73	6	C
ATOM	268	CD2	TYR A	36	72.549	5.282	−2.324	1.00	32.13	6	C
ATOM	269	CE2	TYR A	36	72.997	4.412	−3.321	1.00	34.36	6	C
ATOM	270	CZ	TYR A	36	74.330	4.407	−3.657	1.00	35.08	6	C
ATOM	271	OH	TYR A	36	74.755	3.531	−4.629	1.00	36.75	8	O
ATOM	272	C	TYR A	36	72.161	9.277	0.082	1.00	30.06	6	C
ATOM	273	O	TYR A	36	72.957	10.091	0.532	1.00	27.93	8	O
ATOM	274	N	CYS A	37	70.972	9.078	0.631	1.00	31.17	7	N
ATOM	275	CA	CYS A	37	70.506	9.588	1.887	1.00	33.35	6	C
ATOM	276	C	CYS A	37	70.413	8.407	2.855	1.00	32.03	6	C
ATOM	277	O	CYS A	37	69.647	7.469	2.556	1.00	28.66	8	O
ATOM	278	CB	CYS A	37	69.055	10.099	1.758	1.00	38.20	6	C
ATOM	279	SG	CYS A	37	68.363	10.414	3.373	1.00	45.18	16	S
ATOM	280	N	SER A	38	71.164	8.366	3.945	1.00	29.83	7	N
ATOM	281	CA	SER A	38	71.086	7.207	4.838	1.00	30.30	6	C
ATOM	282	CB	SER A	38	72.375	7.035	5.676	1.00	32.01	6	C
ATOM	283	OG	SER A	38	73.444	6.795	4.738	1.00	37.81	8	O
ATOM	284	C	SER A	38	69.922	7.445	5.794	1.00	28.69	6	C
ATOM	285	O	SER A	38	70.078	8.267	6.684	1.00	31.39	8	O
ATOM	286	N	VAL A	39	68.804	6.737	5.655	1.00	26.81	7	N
ATOM	287	CA	VAL A	39	67.699	6.918	6.612	1.00	27.33	6	C
ATOM	288	CB	VAL A	39	66.395	6.658	5.811	1.00	29.60	6	C
ATOM	289	CG1	VAL A	39	65.183	6.775	6.746	1.00	27.91	6	C
ATOM	290	CG2	VAL A	39	66.294	7.642	4.650	1.00	28.67	6	C
ATOM	291	C	VAL A	39	67.767	5.996	7.806	1.00	30.13	6	C
ATOM	292	O	VAL A	39	68.033	4.782	7.787	1.00	27.57	8	O
ATOM	293	N	ASN A	40	67.553	6.571	8.993	1.00	28.95	7	N
ATOM	294	CA	ASN A	40	67.581	5.767	10.223	1.00	30.58	6	C
ATOM	295	CB	ASN A	40	68.953	5.725	10.906	1.00	35.11	6	C
ATOM	296	CG	ASN A	40	68.826	4.881	12.163	1.00	36.53	6	C
ATOM	297	OD1	ASN A	40	68.026	5.242	13.066	1.00	41.25	8	O
ATOM	298	ND2	ASN A	40	69.404	3.708	12.250	1.00	35.72	7	N
ATOM	299	C	ASN A	40	66.562	6.419	11.139	1.00	30.39	6	C
ATOM	300	O	ASN A	40	66.914	7.361	11.855	1.00	31.27	8	O
ATOM	301	N	LEU A	41	65.343	5.912	11.097	1.00	29.97	7	N
ATOM	302	CA	LEU A	41	64.313	6.501	11.907	1.00	28.42	6	C
ATOM	303	CB	LEU A	41	63.208	6.936	10.903	1.00	30.47	6	C
ATOM	304	CG	LEU A	41	62.022	7.631	11.568	1.00	32.81	6	C
ATOM	305	CD1	LEU A	41	61.543	8.748	10.656	1.00	35.09	6	C
ATOM	306	CD2	LEU A	41	60.942	6.582	11.755	1.00	32.60	6	C
ATOM	307	C	LEU A	41	63.697	5.528	12.906	1.00	28.47	6	C
ATOM	308	O	LEU A	41	63.562	4.342	12.616	1.00	25.42	8	O
ATOM	309	N	VAL A	42	63.438	6.021	14.104	1.00	22.39	7	N
ATOM	310	CA	VAL A	42	62.762	5.248	15.145	1.00	22.71	6	C
ATOM	311	CB	VAL A	42	63.320	5.650	16.500	1.00	22.47	6	C
ATOM	312	CG1	VAL A	42	62.670	4.901	17.690	1.00	20.48	6	C
ATOM	313	CG2	VAL A	42	64.847	5.383	16.540	1.00	20.32	6	C
ATOM	314	C	VAL A	42	61.261	5.511	15.092	1.00	24.25	6	C
ATOM	315	O	VAL A	42	60.843	6.670	15.314	1.00	22.31	8	O
ATOM	316	N	GLU A	43	60.445	4.479	14.893	1.00	25.16	7	N
ATOM	317	CA	GLU A	43	58.989	4.574	14.877	1.00	26.39	6	C
ATOM	318	CB	GLU A	43	58.439	3.214	14.353	1.00	28.10	6	C
ATOM	319	CG	GLU A	43	59.005	2.782	12.984	1.00	28.95	6	C
ATOM	320	CD	GLU A	43	58.148	3.305	11.839	1.00	33.52	6	C
ATOM	321	OE1	GLU A	43	57.372	4.287	12.009	1.00	32.49	8	O
ATOM	322	OE2	GLU A	43	58.157	2.730	10.718	1.00	31.85	8	O
ATOM	323	C	GLU A	43	58.377	4.882	16.221	1.00	27.61	6	C
ATOM	324	O	GLU A	43	59.039	4.736	17.258	1.00	28.26	8	O
ATOM	325	N	THR A	44	57.092	5.292	16.355	1.00	27.54	7	N
ATOM	326	CA	THR A	44	56.510	5.670	17.618	1.00	27.58	6	C
ATOM	327	CB	THR A	44	55.078	6.251	17.547	1.00	29.47	6	C
ATOM	328	OG1	THR A	44	54.224	5.342	16.837	1.00	29.12	8	O
ATOM	329	CG2	THR A	44	55.085	7.594	16.818	1.00	29.28	6	C
ATOM	330	C	THR A	44	56.487	4.496	18.620	1.00	30.49	6	C
ATOM	331	O	THR A	44	56.453	4.767	19.825	1.00	32.82	8	O
ATOM	332	N	ASP A	45	56.541	3.262	18.104	1.00	31.19	7	N
ATOM	333	CA	ASP A	45	56.562	2.152	19.104	1.00	33.22	6	C
ATOM	334	CB	ASP A	45	55.872	0.898	18.580	1.00	34.18	6	C
ATOM	335	CG	ASP A	45	56.565	0.236	17.422	1.00	34.94	6	C
ATOM	336	OD1	ASP A	45	57.414	0.823	16.723	1.00	32.61	8	O
ATOM	337	OD2	ASP A	45	56.284	−0.937	17.087	1.00	40.48	8	O
ATOM	338	C	ASP A	45	57.998	1.799	19.465	1.00	32.01	6	C
ATOM	339	O	ASP A	45	58.171	0.784	20.150	1.00	32.97	8	O
ATOM	340	N	GLY A	46	58.999	2.520	18.950	1.00	27.61	7	N
ATOM	341	CA	GLY A	46	60.382	2.153	19.286	1.00	26.30	6	C
ATOM	342	C	GLY A	46	61.032	1.283	18.231	1.00	25.92	6	C
ATOM	343	O	GLY A	46	62.231	0.945	18.310	1.00	28.47	8	O
ATOM	344	N	SER A	47	60.296	0.831	17.232	1.00	25.17	7	N
ATOM	345	CA	SER A	47	60.845	−0.009	16.181	1.00	26.65	6	C
ATOM	346	CB	SER A	47	59.795	−0.746	15.369	1.00	28.94	6	C
ATOM	347	OG	SER A	47	58.668	0.008	14.970	1.00	31.45	8	O
ATOM	348	C	SER A	47	61.771	0.827	15.302	1.00	27.69	6	C
ATOM	349	O	SER A	47	61.673	2.052	15.261	1.00	27.44	8	O
ATOM	350	N	ILE A	48	62.734	0.138	14.702	1.00	28.27	7	N
ATOM	351	CA	ILE A	48	63.641	0.937	13.818	1.00	26.68	6	C
ATOM	352	CB	ILE A	48	65.108	0.554	14.107	1.00	28.07	6	C
ATOM	353	CG2	ILE A	48	66.073	1.364	13.261	1.00	27.07	6	C
ATOM	354	CG1	ILE A	48	65.363	0.837	15.590	1.00	27.86	6	C
ATOM	355	CD1	ILE A	48	66.784	0.588	16.060	1.00	30.99	6	C
ATOM	356	C	ILE A	48	63.277	0.663	12.375	1.00	30.36	6	C
ATOM	357	O	ILE A	48	63.152	−0.541	12.448	1.00	31.57	8	O
ATOM	358	N	PHE A	49	63.555	1.550	11.474	1.00	26.28	7	N
ATOM	359	CA	PHE A	49	63.541	1.550	10.030	1.00	26.18	6	C
ATOM	360	CB	PHE A	49	62.460	2.397	9.352	1.00	26.59	6	C
ATOM	361	CG	PHE A	49	62.477	2.458	7.891	1.00	26.59	6	C
ATOM	362	CD1	PHE A	49	61.729	1.568	7.117	1.00	28.67	6	C
ATOM	363	CD2	PHE A	49	63.224	3.382	7.159	1.00	26.37	6	C
ATOM	364	CE1	PHE A	49	61.717	1.584	5.745	1.00	25.41	6	C
ATOM	365	CE2	PHE A	49	63.237	3.412	5.776	1.00	28.69	6	C
ATOM	366	CZ	PHE A	49	62.474	2.511	5.050	1.00	28.49	6	C
ATOM	367	C	PHE A	49	64.905	2.139	9.573	1.00	25.57	6	C
ATOM	368	O	PHE A	49	65.230	3.256	9.955	1.00	27.53	8	O
ATOM	369	N	ASN A	50	65.630	1.405	8.704	1.00	24.76	7	N
ATOM	370	CA	ASN A	50	66.967	1.843	8.287	1.00	27.69	6	C
ATOM	371	CB	ASN A	50	68.001	1.351	9.343	1.00	30.08	6	C
ATOM	372	CG	ASN A	50	69.412	1.805	9.002	1.00	31.06	6	C
ATOM	373	OD1	ASN A	50	69.926	2.596	9.818	1.00	34.00	8	O
ATOM	374	ND2	ASN A	50	70.064	1.351	7.961	1.00	30.73	7	N
ATOM	375	C	ASN A	50	67.303	1.324	6.944	1.00	30.93	6	C
ATOM	376	O	ASN A	50	67.404	0.144	6.639	1.00	29.95	8	O
ATOM	377	N	GLU A	51	67.326	2.255	5.984	1.00	29.10	7	N
ATOM	378	CA	GLU A	51	67.600	1.975	4.579	1.00	30.55	6	C
ATOM	379	CB	GLU A	51	66.297	1.865	3.773	1.00	31.87	6	C
ATOM	380	CC	GLU A	51	65.505	0.595	4.093	1.00	38.93	6	C
ATOM	381	CD	GLU A	51	66.396	−0.620	3.826	1.00	40.93	6	C
ATOM	382	OE1	GLU A	51	67.105	−0.596	2.785	1.00	43.62	8	O
ATOM	383	OE2	GLU A	51	66.411	−1.517	4.669	1.00	44.47	8	O
ATOM	384	C	GLU A	51	68.444	3.095	4.012	1.00	29.33	6	C
ATOM	385	O	GLU A	51	68.362	4.252	4.354	1.00	29.83	8	O
ATOM	386	N	SER A	52	69.120	2.776	2.902	1.00	28.60	7	N
ATOM	387	CA	SER A	52	69.899	3.708	2.102	1.00	27.45	6	C
ATOM	388	CB	SER A	52	71.237	3.115	1.651	1.00	28.30	6	C
ATOM	389	OG	SER A	52	72.241	3.248	2.626	1.00	30.94	8	O
ATOM	390	C	SER A	52	69.176	4.097	0.814	1.00	26.94	6	C
ATOM	391	O	SER A	52	69.065	3.297	−0.114	1.00	28.23	8	O
ATOM	392	N	LEU A	53	68.739	5.339	0.654	1.00	24.84	7	N
ATOM	393	CA	LEU A	53	68.007	5.713	−0.549	1.00	24.79	6	C
ATOM	394	CB	LEU A	53	66.697	6.455	−0.173	1.00	26.66	6	C
ATOM	395	CG	LEU A	53	65.820	5.727	0.848	1.00	28.60	6	C
ATOM	396	CD1	LEU A	53	64.633	6.633	1.213	1.00	30.62	6	C
ATOM	397	CD2	LEU A	53	65.338	4.406	0.269	1.00	30.17	6	C
ATOM	398	C	LEU A	53	68.805	6.548	−1.536	1.00	25.47	6	C
ATOM	399	O	LEU A	53	69.776	7.240	−1.202	1.00	26.52	8	O
ATOM	400	N	THR A	54	68.400	6.491	−2.811	1.00	23.31	7	N
ATOM	401	CA	THR A	54	68.991	7.285	−3.872	1.00	23.91	6	C
ATOM	402	CB	THR A	54	68.194	7.155	−5.216	1.00	25.87	6	C
ATOM	403	OG1	THR A	54	68.498	5.838	−5.702	1.00	27.15	8	O
ATOM	404	CG2	THR A	54	68.672	8.153	−6.252	1.00	25.02	6	C
ATOM	405	C	THR A	54	68.874	8.773	−3.519	1.00	23.03	6	C
ATOM	406	O	THR A	54	67.920	9.109	−2.851	1.00	22.88	8	O
ATOM	407	N	ALA A	55	69.864	9.600	−3.774	1.00	23.21	7	N
ATOM	408	CA	ALA A	55	69.750	11.042	−3.548	1.00	24.90	6	C
ATOM	409	CB	ALA A	55	70.407	11.503	−2.223	1.00	22.63	6	C
ATOM	410	C	ALA A	55	70.402	11.794	−4.693	1.00	23.12	6	C
ATOM	411	O	ALA A	55	71.332	11.290	−5.379	1.00	24.57	8	O
ATOM	412	N	ASN A	56	69.889	12.965	−5.025	1.00	21.77	7	N
ATOM	413	CA	ASN A	56	70.494	13.903	−5.950	1.00	22.43	6	C
ATOM	414	CB	ASN A	56	71.792	14.458	−5.353	1.00	25.10	6	C
ATOM	415	CG	ASN A	56	71.596	15.370	−4.145	1.00	25.06	6	C
ATOM	416	OD1	ASN A	56	71.184	14.930	−3.095	1.00	24.70	8	O
ATOM	417	ND2	ASN A	56	71.921	16.651	−4.357	1.00	26.52	7	N
ATOM	418	C	ASN A	56	70.729	13.405	−7.360	1.00	22.86	6	C
ATOM	419	O	ASN A	56	71.663	13.778	−8.064	1.00	24.56	8	O
ATOM	420	N	ASP A	57	69.859	12.549	−7.854	1.00	21.29	7	N
ATOM	421	CA	ASP A	57	69.841	12.006	−9.202	1.00	23.50	6	C
ATOM	422	CB	ASP A	57	69.245	10.598	−9.082	1.00	24.41	6	C
ATOM	423	CG	ASP A	57	69.320	9.885	−10.446	1.00	27.36	6	C
ATOM	424	OD1	ASP A	57	69.210	10.544	−11.491	1.00	27.51	8	O
ATOM	425	OD2	ASP A	57	69.421	8.641	−10.351	1.00	27.67	8	O
ATOM	426	C	ASP A	57	68.943	12.911	−10.044	1.00	25.21	6	C
ATOM	427	O	ASP A	57	67.725	12.979	−9.865	1.00	21.29	8	O
ATOM	428	N	PRO A	58	69.537	13.711	−10.964	1.00	24.99	7	N
ATOM	429	CD	PRO A	58	70.990	13.600	−11.279	1.00	26.79	6	C
ATOM	430	CA	PRO A	58	68.850	14.606	−11.841	1.00	24.66	6	C
ATOM	431	CB	PRO A	58	70.008	15.325	−12.578	1.00	28.21	6	C
ATOM	432	CG	PRO A	58	71.118	14.313	−12.596	1.00	28.45	6	C
ATOM	433	C	PRO A	58	67.872	13.933	−12.814	1.00	23.24	6	C
ATOM	434	O	PRO A	58	66.932	14.576	−13.183	1.00	19.94	8	O
ATOM	435	N	ASP A	59	68.161	12.713	−13.212	1.00	24.23	7	N
ATOM	436	CA	ASP A	59	67.245	11.994	−14.117	1.00	26.19	6	C
ATOM	437	CB	ASP A	59	67.961	10.851	−14.821	1.00	30.36	6	C
ATOM	438	CG	ASP A	59	69.077	11.362	−15.715	1.00	32.27	6	C
ATOM	439	OD1	ASP A	59	68.814	12.259	−16.532	1.00	32.01	8	O
ATOM	440	OD2	ASP A	59	70.207	10.832	−15.619	1.00	32.97	8	O
ATOM	441	C	ASP A	59	66.007	11.534	−13.362	1.00	22.45	6	C
ATOM	442	O	ASP A	59	64.934	11.545	−13.936	1.00	23.55	8	O
ATOM	443	N	PHE A	60	66.145	11.138	−12.109	1.00	24.18	7	N
ATOM	444	CA	PHE A	60	65.022	10.719	−11.266	1.00	20.30	6	C
ATOM	445	CB	PHE A	60	65.605	10.154	−9.945	1.00	20.19	6	C
ATOM	446	CG	PHE A	60	64.583	9.499	−9.052	1.00	19.97	6	C
ATOM	447	CD1	PHE A	60	64.581	8.136	−8.894	1.00	26.19	6	C
ATOM	448	CD2	PHE A	60	63.613	10.260	−8.375	1.00	20.25	6	C
ATOM	449	CE1	PHE A	60	63.622	7.510	−8.077	1.00	26.55	6	C
ATOM	450	CE2	PHE A	60	62.667	9.674	−7.556	1.00	21.54	6	C
ATOM	451	CZ	PHE A	60	62.692	8.304	−7.431	1.00	24.51	6	C
ATOM	452	C	PHE A	60	64.175	11.974	−10.932	1.00	19.89	6	C
ATOM	453	O	PHE A	60	62.948	12.041	−11.052	1.00	19.19	8	O
ATOM	454	N	LEU A	61	64.871	13.131	−10.698	1.00	18.98	7	N
ATOM	455	CA	LEU A	61	64.122	14.371	−10.522	1.00	18.49	6	C
ATOM	456	CB	LEU A	61	65.094	15.529	−10.179	1.00	19.12	6	C
ATOM	457	CG	LEU A	61	64.440	16.918	−10.060	1.00	19.99	6	C
ATOM	458	CD1	LEU A	61	63.482	16.970	−8.880	1.00	19.96	6	C
ATOM	459	CD2	LEU A	61	65.627	17.916	−9.948	1.00	20.79	6	C
ATOM	460	C	LEU A	61	63.315	14.765	−11.740	1.00	19.01	6	C
ATOM	461	O	LEU A	61	62.162	15.182	−11.660	1.00	16.82	8	O
ATOM	462	N	ALA A	62	63.920	14.597	−12.962	1.00	21.18	7	N
ATOM	463	CA	ALA A	62	63.249	14.967	−14.193	1.00	22.64	6	C
ATOM	464	CB	ALA A	62	64.258	14.800	−15.334	1.00	23.13	6	C
ATOM	465	C	ALA A	62	62.068	14.038	−14.516	1.00	23.74	6	C
ATOM	466	O	ALA A	62	61.287	14.417	−15.402	1.00	21.55	8	O
ATOM	467	N	THR A	63	61.889	12.913	−13.854	1.00	20.73	7	N
ATOM	468	CA	THR A	63	60.741	12.038	−14.064	1.00	21.42	6	C
ATOM	469	CB	THR A	63	61.187	10.641	−14.571	1.00	24.63	6	C
ATOM	470	OG1	THR A	63	62.298	10.243	−13.764	1.00	25.73	8	O
ATOM	471	CG2	THR A	63	61.583	10.705	−16.033	1.00	28.77	6	C
ATOM	472	C	THR A	63	59.877	11.818	−12.833	1.00	21.48	6	C
ATOM	473	O	THR A	63	59.056	10.886	−12.654	1.00	20.77	8	O
ATOM	474	N	SER A	64	60.012	12.694	−11.829	1.00	18.51	7	N
ATOM	475	CA	SER A	64	59.237	12.633	−10.614	1.00	18.29	6	C
ATOM	476	CB	SER A	64	59.970	13.489	−9.522	1.00	15.65	6	C
ATOM	477	OG	SER A	64	61.100	12.794	−9.045	1.00	16.92	8	O
ATOM	478	C	SER A	64	57.832	13.205	−10.766	1.00	17.95	6	C
ATOM	479	O	SER A	64	57.545	14.117	−11.508	1.00	20.47	8	O
ATOM	480	N	ASP A	65	56.884	12.593	−10.057	1.00	17.41	7	N
ATOM	481	CA	ASP A	65	55.487	12.904	−10.022	1.00	17.41	6	C
ATOM	482	CB	ASP A	65	54.648	11.577	−9.941	1.00	19.70	6	C
ATOM	483	CG	ASP A	65	54.993	10.654	−11.118	1.00	22.29	6	C
ATOM	484	OD1	ASP A	65	54.820	11.083	−12.274	1.00	23.75	8	O
ATOM	485	OD2	ASP A	65	55.491	9.566	−10.830	1.00	22.12	8	O
ATOM	486	C	ASP A	65	55.052	13.754	−8.849	1.00	16.95	6	C
ATOM	487	O	ASP A	65	53.963	14.325	−8.840	1.00	16.63	8	O
ATOM	488	N	LEU A	66	56.033	14.011	−7.963	1.00	17.15	7	N
ATOM	489	CA	LEU A	66	55.779	14.936	−6.826	1.00	16.87	6	C
ATOM	490	CB	LEU A	66	54.960	14.271	−5.709	1.00	17.02	6	C
ATOM	491	CG	LEU A	66	54.874	15.039	−4.364	1.00	14.65	6	C
ATOM	492	CD1	LEU A	66	53.871	16.247	−4.524	1.00	14.57	6	C
ATOM	493	CD2	LEU A	66	54.291	14.204	−3.233	1.00	14.66	6	C
ATOM	494	C	LEU A	66	57.135	15.380	−6.256	1.00	15.24	6	C
ATOM	495	O	LEU A	66	58.078	14.575	−6.303	1.00	16.38	8	O
ATOM	496	N	LEU A	67	57.268	16.653	−5.981	1.00	17.25	7	N
ATOM	497	CA	LEU A	67	58.461	17.226	−5.313	1.00	15.53	6	C
ATOM	498	CB	LEU A	67	59.094	18.430	−5.976	1.00	13.95	6	C
ATOM	499	CG	LEU A	67	60.232	19.155	−5.200	1.00	16.50	6	C
ATOM	500	CD1	LEU A	67	61.370	18.132	−5.018	1.00	16.64	6	C
ATOM	501	CD2	LEU A	67	60.750	20.346	−6.039	1.00	17.22	6	C
ATOM	502	C	LEU A	67	57.905	17.582	−3.916	1.00	14.98	6	C
ATOM	503	O	LEU A	67	57.023	18.458	−3.810	1.00	14.63	8	O
ATOM	504	N	LEU A	68	58.367	16.857	−2.868	1.00	14.52	7	N
ATOM	505	CA	LEU A	68	57.845	17.122	−1.522	1.00	15.85	6	C
ATOM	506	CB	LEU A	68	57.540	15.810	−0.796	1.00	17.84	6	C
ATOM	507	CG	LEU A	68	56.662	15.861	0.470	1.00	23.41	6	C
ATOM	508	CD1	LEU A	68	56.378	14.362	0.765	1.00	25.33	6	C
ATOM	509	CD2	LEU A	68	57.556	16.260	1.636	1.00	22.62	6	C
ATOM	510	C	LEU A	68	58.928	17.915	−0.729	1.00	14.52	6	C
ATOM	511	O	LEU A	68	59.964	17.291	−0.513	1.00	15.28	8	O
ATOM	512	N	VAL A	69	58.693	19.125	−0.291	1.00	13.09	7	N
ATOM	513	CA	VAL A	69	59.789	19.898	0.346	1.00	13.59	6	C
ATOM	514	CB	VAL A	69	59.705	21.331	−0.270	1.00	15.34	6	C
ATOM	515	CG1	VAL A	69	60.811	22.215	0.292	1.00	16.51	6	C
ATOM	516	CG2	VAL A	69	59.759	21.246	−1.798	1.00	16.33	6	C
ATOM	517	C	VAL A	69	59.620	20.034	1.853	1.00	16.08	6	C
ATOM	518	O	VAL A	69	58.531	20.359	2.346	1.00	17.15	8	O
ATOM	519	N	THR A	70	60.788	19.703	2.485	1.00	13.35	7	N
ATOM	520	CA	THR A	70	60.722	19.582	3.961	1.00	14.54	6	C
ATOM	521	CB	THR A	70	60.842	18.132	4.482	1.00	15.96	6	C
ATOM	522	OG1	THR A	70	62.065	17.512	4.066	1.00	19.36	8	O
ATOM	523	CG2	THR A	70	59.740	17.233	3.879	1.00	15.54	6	C
ATOM	524	C	THR A	70	61.868	20.353	4.554	1.00	17.39	6	C
ATOM	525	O	THR A	70	62.185	20.112	5.757	1.00	23.55	8	O
ATOM	526	N	LEU A	71	62.265	21.411	3.884	1.00	17.46	7	N
ATOM	527	CA	LEU A	71	63.316	22.278	4.473	1.00	19.45	6	C
ATOM	528	CB	LEU A	71	63.950	22.962	3.250	1.00	21.65	6	C
ATOM	529	CG	LEU A	71	64.694	22.077	2.273	1.00	20.39	6	C
ATOM	530	CD1	LEU A	71	65.196	22.884	1.088	1.00	25.73	6	C
ATOM	531	CD2	LEU A	71	65.860	21.340	2.955	1.00	26.91	6	C
ATOM	532	C	LEU A	71	62.787	23.307	5.416	1.00	20.85	6	C
ATOM	533	O	LEU A	71	61.591	23.568	5.479	1.00	18.79	8	O
ATOM	534	N	LYS A	72	63.679	23.993	6.213	1.00	20.21	7	N
ATOM	535	CA	LYS A	72	63.212	25.089	7.027	1.00	22.60	6	C
ATOM	536	CB	LYS A	72	64.357	25.614	7.909	1.00	25.53	6	C
ATOM	537	CG	LYS A	72	65.059	24.491	8.677	1.00	29.68	6	C
ATOM	538	CD	LYS A	72	64.106	24.080	9.787	1.00	33.74	6	C
ATOM	539	CE	LYS A	72	64.024	22.555	9.795	1.00	38.42	6	C
ATOM	540	NZ	LYS A	72	63.270	22.103	11.027	1.00	41.23	7	N
ATOM	541	C	LYS A	72	62.826	26.247	6.083	1.00	22.00	6	C
ATOM	542	O	LYS A	72	63.355	26.350	4.980	1.00	21.07	8	O
ATOM	543	N	ALA A	73	61.957	27.098	6.580	1.00	21.11	7	N
ATOM	544	CA	ALA A	73	61.360	28.118	5.727	1.00	19.00	6	C
ATOM	545	CB	ALA A	73	60.406	28.962	6.538	1.00	20.88	6	C
ATOM	546	C	ALA A	73	62.354	29.016	4.992	1.00	19.18	6	C
ATOM	547	O	ALA A	73	62.112	29.286	3.787	1.00	17.71	8	O
ATOM	548	N	TRP A	74	63.406	29.441	5.658	1.00	20.62	7	N
ATOM	549	CA	TRP A	74	64.359	30.366	4.992	1.00	20.81	6	C
ATOM	550	CB	TRP A	74	65.279	30.968	6.104	1.00	23.28	6	C
ATOM	551	CG	TRP A	74	66.030	29.984	6.928	1.00	22.49	6	C
ATOM	552	CD2	TRP A	74	67.316	29.409	6.699	1.00	26.07	6	C
ATOM	553	CE2	TRP A	74	67.596	28.552	7.779	1.00	27.46	6	C
ATOM	554	CE3	TPP A	74	68.288	29.608	5.705	1.00	27.76	6	C
ATOM	555	CD1	TRP A	74	65.611	29.443	8.113	1.00	24.70	6	C
ATOM	556	NE1	TRP A	74	66.506	28.548	8.609	1.00	27.52	7	N
ATOM	557	CZ2	TRP A	74	68.780	27.832	7.882	1.00	31.03	6	C
ATOM	558	CZ3	TRP A	74	69.476	28.888	5.816	1.00	31.29	6	C
ATOM	559	CH2	TRP A	74	69.699	28.016	6.889	1.00	30.15	6	C
ATOM	560	C	TRP A	74	65.182	29.745	3.899	1.00	22.12	6	C
ATOM	561	O	TRP A	74	65.915	30.384	3.090	1.00	21.36	8	O
ATOM	562	N	GLN A	75	65.153	28.417	3.745	1.00	20.22	7	N
ATOM	563	CA	GLN A	75	65.858	27.646	2.771	1.00	22.57	6	C
ATOM	564	CB	GLN A	75	66.286	26.282	3.342	1.00	25.07	6	C
ATOM	565	CG	GLN A	75	67.311	26.385	4.485	1.00	28.42	6	C
ATOM	566	CD	GLN A	75	67.484	25.102	5.258	1.00	33.15	6	C
ATOM	567	OE1	GLN A	75	66.670	24.161	5.307	1.00	34.09	8	O
ATOM	568	NE2	GLN A	75	68.588	24.993	6.019	1.00	34.82	7	N
ATOM	569	C	GLN A	75	64.949	27.366	1.556	1.00	22.13	6	C
ATOM	570	O	GLN A	75	65.583	26.773	0.631	1.00	23.16	8	O
ATOM	571	N	VAL A	76	63.673	27.283	1.746	1.00	20.65	7	N
ATOM	572	CA	VAL A	76	62.779	26.823	0.707	1.00	18.83	6	C
ATOM	573	CB	VAL A	76	61.339	26.862	1.262	1.00	19.12	6	C
ATOM	574	CG1	VAL A	76	60.278	26.693	0.178	1.00	19.10	6	C
ATOM	575	CG2	VAL A	76	61.172	25.912	2.456	1.00	20.33	6	C
ATOM	576	C	VAL A	76	62.867	27.486	−0.653	1.00	19.86	6	C
ATOM	577	O	VAL A	76	62.994	26.682	−1.622	1.00	22.31	8	O
ATOM	578	N	SER A	77	62.631	28.760	−0.748	1.00	20.94	7	N
ATOM	579	CA	SER A	77	62.424	29.328	−2.104	1.00	22.51	6	C
ATOM	580	CB	SER A	77	61.834	30.735	−1.945	1.00	22.72	6	C
ATOM	581	OG	SER A	77	62.875	31.614	−1.526	1.00	28.58	8	O
ATOM	582	C	SER A	77	63.626	29.194	−2.999	1.00	24.42	6	C
ATOM	583	O	SER A	77	63.503	28.771	−4.168	1.00	25.80	8	O
ATOM	584	N	ASP A	78	64.864	29.387	−2.487	1.00	26.64	7	N
ATOM	585	CA	ASP A	78	66.049	29.200	−3.323	1.00	27.37	6	C
ATOM	586	CB	ASP A	78	67.327	29.651	−2.624	1.00	30.35	6	C
ATOM	587	CG	ASP A	78	67.474	31.131	−2.350	1.00	34.66	6	C
ATOM	588	OD1	ASP A	78	67.050	32.001	−3.125	1.00	36.48	8	O
ATOM	589	OD2	ASP A	78	68.014	31.488	−1.273	1.00	35.74	8	O
ATOM	590	C	ASP A	78	66.228	27.756	−3.792	1.00	26.83	6	C
ATOM	591	O	ASP A	78	66.577	27.507	−4.979	1.00	26.62	8	O
ATOM	592	N	ALA A	79	66.031	26.778	−2.890	1.00	24.51	7	N
ATOM	593	CA	ALA A	79	66.223	25.391	−3.245	1.00	23.01	6	C
ATOM	594	CB	ALA A	79	66.218	24.440	−2.065	1.00	23.43	6	C
ATOM	595	C	ALA A	79	65.141	24.952	−4.279	1.00	21.89	6	C
ATOM	596	O	ALA A	79	65.539	24.282	−5.234	1.00	20.72	8	O
ATOM	597	N	VAL A	80	63.899	25.340	−4.100	1.00	18.80	7	N
ATOM	598	CA	VAL A	80	62.847	25.004	−5.069	1.00	20.18	6	C
ATOM	599	CB	VAL A	80	61.454	25.459	−4.601	1.00	20.16	6	C
ATOM	600	CG1	VAL A	80	60.329	25.289	−5.644	1.00	19.66	6	C
ATOM	601	CG2	VAL A	80	61.066	24.569	−3.390	1.00	20.18	6	C
ATOM	602	C	VAL A	80	63.186	25.640	−6.418	1.00	21.67	6	C
ATOM	603	O	VAL A	80	63.113	24.934	−7.456	1.00	22.95	8	O
ATOM	604	N	LYS A	81	63.593	26.908	−6.439	1.00	21.12	7	N
ATOM	605	CA	LYS A	81	63.887	27.547	−7.780	1.00	20.40	6	C
ATOM	606	CB	LYS A	81	64.131	29.027	−7.546	1.00	21.88	6	C
ATOM	607	CG	LYS A	81	62.954	29.895	−7.201	1.00	24.11	6	C
ATOM	608	CD	LYS A	81	63.388	31.305	−6.859	1.00	28.17	6	C
ATOM	609	CE	LYS A	81	62.253	32.257	−6.649	1.00	32.11	6	C
ATOM	610	NZ	LYS A	81	62.755	33.492	−5.946	1.00	32.28	7	N
ATOM	611	C	LYS A	81	65.013	26.801	−8.461	1.00	23.68	6	C
ATOM	612	O	LYS A	81	64.933	26.629	−9.714	1.00	22.41	8	O
ATOM	613	N	SER A	82	66.031	26.288	−7.756	1.00	24.42	7	N
ATOM	614	CA	SER A	82	67.129	25.555	−8.299	1.00	27.30	6	C
ATOM	615	CB	SER A	82	68.192	25.145	−7.282	1.00	31.44	6	C
ATOM	616	OG	SER A	82	67.931	24.117	−6.337	1.00	35.47	8	O
ATOM	617	C	SER A	82	66.677	24.270	−9.031	1.00	27.43	6	C
ATOM	618	O	SER A	82	67.431	23.789	−9.876	1.00	29.76	8	O
ATOM	619	N	LEU A	83	65.666	23.600	−8.509	1.00	25.35	7	N
ATOM	620	CA	LEU A	83	65.225	22.342	−9.105	1.00	25.04	6	C
ATOM	621	CB	LEU A	83	64.726	21.428	−7.958	1.00	23.04	6	C
ATOM	622	CG	LEU A	83	65.718	21.028	−6.887	1.00	25.94	6	C
ATOM	623	CD1	LEU A	83	65.141	19.787	−6.137	1.00	25.74	6	C
ATOM	624	CD2	LEU A	83	67.088	20.630	−7.381	1.00	24.66	6	C
ATOM	625	C	LEU A	83	64.083	22.483	−10.078	1.00	25.04	6	C
ATOM	626	O	LEU A	83	63.723	21.487	−10.703	1.00	24.30	8	O
ATOM	627	N	ALA A	84	63.383	23.603	−10.149	1.00	25.31	7	N
ATOM	628	CA	ALA A	84	62.197	23.734	−10.936	1.00	27.21	6	C
ATOM	629	CB	ALA A	84	61.364	24.938	−10.515	1.00	29.05	6	C
ATOM	630	C	ALA A	84	62.419	23.669	−12.450	1.00	27.24	6	C
ATOM	631	O	ALA A	84	61.469	23.277	−13.149	1.00	26.80	8	O
ATOM	632	N	SER A	85	63.617	24.022	−12.933	1.00	26.34	7	N
ATOM	633	CA	SER A	85	63.800	23.860	−14.389	1.00	27.31	6	C
ATOM	634	CB	SER A	85	64.988	24.741	−14.845	1.00	28.02	6	C
ATOM	635	OG	SER A	85	66.134	23.998	−14.398	1.00	34.04	8	O
ATOM	636	C	SER A	85	64.014	22.445	−14.823	1.00	27.16	6	C
ATOM	637	O	SER A	85	63.832	22.013	−15.974	1.00	27.41	8	O
ATOM	638	N	THR A	86	64.350	21.521	−13.904	1.00	25.79	7	N
ATOM	639	CA	THR A	86	64.597	20.123	−14.147	1.00	23.33	6	C
ATOM	640	CB	THR A	86	65.800	19.610	−13.339	1.00	25.22	6	C
ATOM	641	OG1	THR A	86	66.991	20.316	−13.756	1.00	26.39	8	O
ATOM	642	CG2	THR A	86	66.019	18.127	−13.577	1.00	24.19	6	C
ATOM	643	C	THR A	86	63.358	19.268	−13.854	1.00	22.48	6	C
ATOM	644	O	THR A	86	63.074	18.350	−14.630	1.00	22.47	8	O
ATOM	645	N	LEU A	87	62.663	19.608	−12.775	1.00	19.32	7	N
ATOM	646	CA	LEU A	87	61.422	18.821	−12.459	1.00	20.09	6	C
ATOM	647	CB	LEU A	87	60.910	19.490	−11.140	1.00	20.09	6	C
ATOM	648	CG	LEU A	87	59.658	18.896	−10.518	1.00	21.12	6	C
ATOM	649	CD1	LEU A	87	60.074	17.573	−9.827	1.00	18.86	6	C
ATOM	650	CD2	LEU A	87	58.949	19.786	−9.498	1.00	17.84	6	C
ATOM	651	C	LEU A	87	60.433	19.058	−13.589	1.00	19.47	6	C
ATOM	652	O	LEU A	87	60.404	20.261	−14.069	1.00	22.51	8	O
ATOM	653	N	PRO A	88	59.577	18.118	−13.961	1.00	18.84	7	N
ATOM	654	CD	PRO A	88	59.523	16.734	−13.439	1.00	17.45	6	C
ATOM	655	CA	PRO A	88	58.601	18.425	−14.993	1.00	20.15	6	C
ATOM	656	CB	PRO A	88	57.882	17.064	−15.092	1.00	19.07	6	C
ATOM	657	CG	PRO A	88	58.739	15.970	−14.502	1.00	17.86	6	C
ATOM	658	C	PRO A	88	57.703	19.545	−14.640	1.00	21.15	6	C
ATOM	659	O	PRO A	88	57.253	19.837	−13.538	1.00	19.76	8	O
ATOM	660	N	VAL A	89	57.392	20.445	−15.608	1.00	23.63	7	N
ATOM	661	CA	VAL A	89	56.536	21.599	−15.441	1.00	26.38	6	C
ATOM	662	CB	VAL A	89	56.595	22.487	−16.723	1.00	27.05	6	C
ATOM	663	CG1	VAL A	89	55.751	21.820	−17.789	1.00	29.86	6	C
ATOM	664	CG2	VAL A	89	56.133	23.874	−16.385	1.00	29.49	6	C
ATOM	665	C	VAL A	89	55.064	21.305	−15.186	1.00	29.77	6	C
ATOM	666	O	VAL A	89	54.159	22.137	−15.235	1.00	38.50	8	O
ATOM	667	N	THR A	90	54.756	20.030	−15.001	1.00	26.08	7	N
ATOM	668	CA	THR A	90	53.440	19.488	−14.787	1.00	24.78	6	C
ATOM	669	CB	THR A	90	53.325	18.396	−15.882	1.00	25.50	6	C
ATOM	670	OG1	THR A	90	54.555	17.681	−16.060	1.00	33.86	8	O
ATOM	671	CG2	THR A	90	52.838	19.015	−17.176	1.00	28.70	6	C
ATOM	672	C	THR A	90	53.396	18.876	−13.392	1.00	23.61	6	C
ATOM	673	O	THR A	90	52.360	18.483	−12.935	1.00	21.44	8	O
ATOM	674	N	THR A	91	54.573	18.689	−12.814	1.00	21.25	7	N
ATOM	675	CA	THR A	91	54.634	18.000	−11.536	1.00	21.12	6	C
ATOM	676	CB	THR A	91	56.015	17.352	−11.352	1.00	21.89	6	C
ATOM	677	OG1	THR A	91	56.191	16.244	−12.273	1.00	20.52	8	O
ATOM	678	CG2	THR A	91	56.276	16.827	−9.939	1.00	20.92	6	C
ATOM	679	C	THR A	91	54.375	18.922	−10.344	1.00	19.28	6	C
ATOM	680	O	THR A	91	55.088	19.931	−10.180	1.00	20.13	8	O
ATOM	681	N	PRO A	92	53.470	18.556	−9.435	1.00	17.51	7	N
ATOM	682	CD	PRO A	92	52.608	17.371	−9.580	1.00	18.10	6	C
ATOM	683	CA	PRO A	92	53.164	19.354	−8.252	1.00	16.18	6	C
ATOM	684	CB	PRO A	92	51.957	18.676	−7.577	1.00	18.76	6	C
ATOM	685	CG	PRO A	92	51.720	17.422	−8.384	1.00	22.31	6	C
ATOM	686	C	PRO A	92	54.281	19.400	−7.202	1.00	17.00	6	C
ATOM	687	O	PRO A	92	55.109	18.501	−7.079	1.00	16.44	8	O
ATOM	688	N	ILE A	93	54.450	20.593	−6.632	1.00	16.56	7	N
ATOM	689	CA	ILE A	93	55.419	20.845	−5.546	1.00	16.18	6	C
ATOM	690	CB	ILE A	93	56.278	22.079	−5.936	1.00	17.62	6	C
ATOM	691	CG2	ILE A	93	57.202	22.434	−4.759	1.00	19.90	6	C
ATOM	692	CG1	ILE A	93	57.120	21.833	−7.176	1.00	17.46	6	C
ATOM	693	CD1	ILE A	93	57.934	23.073	−7.671	1.00	16.56	6	C
ATOM	694	C	ILE A	93	54.653	21.106	−4.265	1.00	17.19	6	C
ATOM	695	O	ILE A	93	53.826	22.004	−4.204	1.00	17.52	8	O
ATOM	696	N	LEU A	94	54.900	20.285	−3.217	1.00	14.75	7	N
ATOM	697	CA	LEU A	94	54.238	20.522	−1.940	1.00	15.00	6	C
ATOM	698	CB	LEU A	94	53.592	19.181	−1.498	1.00	16.18	6	C
ATOM	699	CG	LEU A	94	53.105	19.166	−0.071	1.00	17.15	6	C
ATOM	700	CD1	LEU A	94	51.981	20.200	0.116	1.00	17.51	6	C
ATOM	701	CD2	LEU A	94	52.576	17.802	0.321	1.00	17.70	6	C
ATOM	702	C	LEU A	94	55.229	21.042	−0.909	1.00	16.00	6	C
ATOM	703	O	LEU A	94	56.191	20.303	−0.673	1.00	15.06	8	O
ATOM	704	N	LEU A	95	54.887	22.184	−0.300	1.00	15.63	7	N
ATOM	705	CA	LEU A	95	55.826	22.695	0.702	1.00	15.01	6	C
ATOM	706	CB	LEU A	95	55.822	24.239	0.534	1.00	16.98	6	C
ATOM	707	CG	LEU A	95	56.179	24.782	−0.855	1.00	17.83	6	C
ATOM	708	CD1	LEU A	95	56.083	26.305	−0.768	1.00	18.15	6	C
ATOM	709	CD2	LEU A	95	57.481	24.292	−1.475	1.00	14.31	6	C
ATOM	710	C	LEU A	95	55.317	22.370	2.102	1.00	16.42	6	C
ATOM	711	O	LEU A	95	54.135	22.675	2.349	1.00	17.96	8	O
ATOM	712	N	ILE A	96	56.116	21.685	2.946	1.00	13.74	7	N
ATOM	713	CA	ILE A	96	55.661	21.494	4.320	1.00	16.86	6	C
ATOM	714	CB	ILE A	96	55.474	20.011	4.704	1.00	16.96	6	C
ATOM	715	CG2	ILE A	96	54.927	19.855	6.122	1.00	17.31	6	C
ATOM	716	CG1	ILE A	96	54.476	19.270	3.747	1.00	18.40	6	C
ATOM	717	CD1	ILE A	96	54.504	17.736	4.031	1.00	17.83	6	C
ATOM	718	C	ILE A	96	56.654	22.200	5.287	1.00	16.68	6	C
ATOM	719	O	ILE A	96	57.801	21.779	5.404	1.00	16.25	8	O
ATOM	720	N	HIS A	97	56.173	23.233	5.955	1.00	16.14	7	N
ATOM	721	CA	HIS A	97	57.060	23.933	6.923	1.00	18.56	6	C
ATOM	722	CB	HIS A	97	58.150	24.723	6.156	1.00	16.61	6	C
ATOM	723	CG	HIS A	97	57.621	25.860	5.339	1.00	19.07	6	C
ATOM	724	CD2	HIS A	97	57.079	27.019	5.735	1.00	15.06	6	C
ATOM	725	ND1	HIS A	97	57.504	25.861	3.954	1.00	20.25	7	N
ATOM	726	CE1	HIS A	97	56.924	27.007	3.555	1.00	17.08	6	C
ATOM	727	NE2	HIS A	97	56.672	27.750	4.649	1.00	21.50	7	N
ATOM	728	C	HIS A	97	56.283	24.826	7.852	1.00	20.66	6	C
ATOM	729	O	HIS A	97	55.100	25.083	7.630	1.00	23.11	8	O
ATOM	730	N	ASN A	98	56.964	25.302	8.928	1.00	19.34	7	N
ATOM	731	CA	ASN A	98	56.241	26.216	9.818	1.00	23.32	6	C
ATOM	732	CB	ASN A	98	56.799	26.008	11.230	1.00	28.80	6	C
ATOM	733	CG	ASN A	98	56.175	24.787	11.864	1.00	32.56	6	C
ATOM	734	OD1	ASN A	98	54.924	24.624	11.706	1.00	37.71	8	O
ATOM	735	ND2	ASN A	98	56.870	23.936	12.580	1.00	34.54	7	N
ATOM	736	C	ASN A	98	56.484	27.639	9.313	1.00	22.28	6	C
ATOM	737	O	ASN A	98	57.395	27.813	8.503	1.00	22.49	8	O
ATOM	738	N	GLY A	99	55.668	28.603	9.687	1.00	23.56	7	N
ATOM	739	CA	GLY A	99	55.868	29.936	9.111	1.00	21.71	6	C
ATOM	740	C	GLY A	99	55.246	30.101	7.709	1.00	22.72	6	C
ATOM	741	O	GLY A	99	54.657	29.189	7.085	1.00	18.49	8	O
ATOM	742	N	MET A	100	55.218	31.387	7.351	1.00	20.67	7	N
ATOM	743	CA	MET A	100	54.584	31.824	6.088	1.00	20.09	6	C
ATOM	744	CB	MET A	100	53.231	32.418	6.360	1.00	18.47	6	C
ATOM	745	CG	MET A	100	52.191	31.467	7.008	1.00	21.61	6	C
ATOM	746	SD	MET A	100	50.691	32.333	7.598	1.00	22.79	16	S
ATOM	747	CE	MET A	100	49.925	32.298	5.967	1.00	22.69	6	C
ATOM	748	C	MET A	100	55.485	32.869	5.390	1.00	20.73	6	C
ATOM	749	O	MET A	100	56.407	33.482	5.946	1.00	22.44	8	O
ATOM	750	N	GLY A	101	55.268	32.954	4.060	1.00	20.68	7	N
ATOM	751	CA	GLY A	101	56.025	33.894	3.251	1.00	22.08	6	C
ATOM	752	C	GLY A	101	56.858	33.269	2.141	1.00	22.61	6	C
ATOM	753	O	GLY A	101	57.514	34.026	1.418	1.00	21.68	8	O
ATOM	754	N	THR A	102	56.771	31.965	1.947	1.00	18.22	7	N
ATOM	755	CA	THR A	102	57.582	31.276	0.915	1.00	19.19	6	C
ATOM	756	CB	THR A	102	58.022	29.841	1.245	1.00	19.68	6	C
ATOM	757	OG1	THR A	102	56.848	29.067	1.529	1.00	17.55	8	O
ATOM	758	CG2	THR A	102	59.033	29.812	2.396	1.00	21.14	6	C
ATOM	759	C	THR A	102	56.777	31.383	−0.389	1.00	18.24	6	C
ATOM	760	O	THR A	102	57.402	31.332	−1.451	1.00	18.19	8	O
ATOM	761	N	ILE A	103	55.439	31.399	−0.308	1.00	18.81	7	N
ATOM	762	CA	ILE A	103	54.629	31.460	−1.543	1.00	19.46	6	C
ATOM	763	CB	ILE A	103	53.137	31.296	−1.228	1.00	21.01	6	C
ATOM	764	CG2	ILE A	103	52.341	31.547	−2.544	1.00	23.49	6	C
ATOM	765	CG1	ILE A	103	52.891	29.856	−0.773	1.00	22.16	6	C
ATOM	766	CD1	ILE A	103	53.624	28.775	−1.645	1.00	24.52	6	C
ATOM	767	C	ILE A	103	54.872	32.768	−2.299	1.00	23.85	6	C
ATOM	768	O	ILE A	103	54.998	32.791	−3.532	1.00	21.71	8	O
ATOM	769	N	GLU A	104	55.021	33.861	−1.552	1.00	23.16	7	N
ATOM	770	CA	GLU A	104	55.341	35.146	−2.184	1.00	25.98	6	C
ATOM	771	CB	GLU A	104	55.309	36.202	−1.055	1.00	29.89	6	C
ATOM	772	CG	GLU A	104	53.885	36.435	−0.592	1.00	34.28	6	C
ATOM	773	CD	GLU A	104	53.257	35.373	0.250	1.00	36.85	6	C
ATOM	774	OE1	GLU A	104	52.096	35.576	0.690	1.00	36.90	8	O
ATOM	775	OE2	GLU A	104	53.877	34.306	0.450	1.00	37.42	8	O
ATOM	776	C	GLU A	104	56.663	35.114	−2.895	1.00	26.03	6	C
ATOM	777	O	GLU A	104	56.839	35.826	−3.919	1.00	27.72	8	O
ATOM	778	N	GLU A	105	57.642	34.347	−2.444	1.00	21.54	7	N
ATOM	779	CA	GLU A	105	58.934	34.165	−3.036	1.00	21.43	6	C
ATOM	780	CB	GLU A	105	60.000	33.614	−2.064	1.00	22.40	6	C
ATOM	781	CG	GLU A	105	60.179	34.582	−0.855	1.00	23.22	6	C
ATOM	782	CD	GLU A	105	61.000	33.973	0.287	1.00	25.80	6	C
ATOM	783	OE1	GLU A	105	60.968	32.769	0.476	1.00	26.56	8	O
ATOM	784	OE2	GLU A	105	61.543	34.840	1.005	1.00	27.46	8	O
ATOM	785	C	GLU A	105	58.888	33.215	−4.251	1.00	25.62	6	C
ATOM	786	O	GLU A	105	59.902	33.122	−4.943	1.00	26.81	8	O
ATOM	787	N	LEU A	106	57.806	32.479	−4.401	1.00	23.68	7	N
ATOM	788	CA	LEU A	106	57.663	31.484	−5.466	1.00	24.45	6	C
ATOM	789	CB	LEU A	106	57.511	30.088	−4.816	1.00	23.41	6	C
ATOM	790	CG	LEU A	106	58.730	29.520	−4.101	1.00	20.11	6	C
ATOM	791	CD1	LEU A	106	58.328	28.272	−3.300	1.00	22.13	6	C
ATOM	792	CD2	LEU A	106	59.906	29.150	−5.017	1.00	19.79	6	C
ATOM	793	C	LEU A	106	56.508	31.773	−6.413	1.00	25.80	6	C
ATOM	794	O	LEU A	106	55.960	30.883	−7.108	1.00	22.72	8	O
ATOM	795	N	GLN A	107	56.069	33.044	−6.559	1.00	27.10	7	N
ATOM	796	CA	GLN A	107	54.918	33.325	−7.372	1.00	32.34	6	C
ATOM	797	CB	GLN A	107	54.249	34.672	−7.123	1.00	35.01	6	C
ATOM	798	CG	GLN A	107	55.086	35.899	−7.292	1.00	41.84	6	C
ATOM	799	CD	GLN A	107	54.240	37.155	−7.067	1.00	45.49	6	C
ATOM	800	OE1	GLN A	107	53.762	37.446	−5.969	1.00	47.72	8	O
ATOM	801	NE2	GLN A	107	54.040	37.935	−8.129	1.00	47.24	7	N
ATOM	802	C	GLN A	107	55.077	33.105	−8.875	1.00	32.83	6	C
ATOM	803	O	GLN A	107	54.015	33.015	−9.522	1.00	36.23	8	O
ATOM	804	N	ASN A	108	56.296	33.011	−9.379	1.00	29.89	7	N
ATOM	805	CA	ASN A	108	56.411	32.771	−10.831	1.00	28.94	6	C
ATOM	806	CB	ASN A	108	57.584	33.617	−11.350	1.00	30.62	6	C
ATOM	807	CG	ASN A	108	57.118	35.076	−11.339	1.00	35.75	6	C
ATOM	808	OD1	ASN A	108	55.887	35.266	−11.319	1.00	37.19	8	O
ATOM	809	ND2	ASN A	108	57.940	36.092	−11.334	1.00	36.26	7	N
ATOM	810	C	ASN A	108	56.643	31.305	−11.157	1.00	25.33	6	C
ATOM	811	O	ASN A	108	56.854	30.981	−12.333	1.00	23.65	8	O
ATOM	812	N	ILE A	109	56.620	30.422	−10.154	1.00	22.74	7	N
ATOM	813	CA	ILE A	109	56.775	28.993	−10.390	1.00	22.01	6	C
ATOM	814	CB	ILE A	109	56.690	28.267	−9.013	1.00	21.76	6	C
ATOM	815	CG2	ILE A	109	56.267	26.811	−9.130	1.00	24.11	6	C
ATOM	816	CG1	ILE A	109	58.019	28.363	−8.275	1.00	22.06	6	C
ATOM	817	CD1	ILE A	109	59.195	27.564	−8.815	1.00	21.82	6	C
ATOM	818	C	ILE A	109	55.668	28.513	−11.325	1.00	20.34	6	C
ATOM	819	O	ILE A	109	54.502	28.793	−11.087	1.00	22.89	8	O
ATOM	820	N	GLN A	110	56.056	27.791	−12.371	1.00	23.85	7	N
ATOM	821	CA	GLN A	110	55.067	27.279	−13.315	1.00	22.34	6	C
ATOM	822	CB	GLN A	110	55.779	26.865	−14.609	1.00	27.91	6	C
ATOM	823	CG	GLN A	110	56.460	28.025	−15.364	1.00	34.45	6	C
ATOM	824	CD	GLN A	110	56.847	27.447	−16.723	1.00	39.75	6	C
ATOM	825	OE1	GLN A	110	56.055	27.530	−17.659	1.00	42.27	8	O
ATOM	826	NE2	GLN A	110	57.992	26.774	−16.821	1.00	41.49	7	N
ATOM	827	C	GLN A	110	54.319	26.052	−12.828	1.00	20.76	6	C
ATOM	828	O	GLN A	110	53.146	25.807	−13.158	1.00	22.00	8	O
ATOM	829	N	GLN A	111	55.038	25.201	−12.069	1.00	18.88	7	N
ATOM	830	CA	GLN A	111	54.355	23.990	−11.564	1.00	19.71	6	C
ATOM	831	CB	GLN A	111	55.377	23.170	−10.733	1.00	17.41	6	C
ATOM	832	CG	GLN A	111	56.511	22.429	−11.406	1.00	17.72	6	C
ATOM	833	CD	GLN A	111	57.708	23.254	−11.844	1.00	19.26	6	C
ATOM	834	OE1	GLN A	111	57.807	24.462	−11.501	1.00	21.21	8	O
ATOM	835	NE2	GLN A	111	58.668	22.569	−12.461	1.00	19.89	7	N
ATOM	836	C	GLN A	111	53.237	24.317	−10.603	1.00	18.64	6	C
ATOM	837	O	GLN A	111	53.096	25.360	−9.924	1.00	19.84	8	O
ATOM	838	N	PRO A	112	52.316	23.355	−10.350	1.00	19.32	7	N
ATOM	839	CD	PRO A	112	52.273	22.049	−11.085	1.00	19.54	6	C
ATOM	840	CA	PRO A	112	51.287	23.413	−9.350	1.00	17.67	6	C
ATOM	841	CB	PRO A	112	50.594	22.057	−9.388	1.00	19.86	6	C
ATOM	842	CG	PRO A	112	50.850	21.610	−10.813	1.00	18.51	6	C
ATOM	843	C	PRO A	112	52.025	23.497	−7.977	1.00	19.87	6	C
ATOM	844	O	PRO A	112	53.018	22.785	−7.860	1.00	19.45	8	O
ATOM	845	N	LEU A	113	51.580	24.401	−7.169	1.00	17.14	7	N
ATOM	846	CA	LEU A	113	52.202	24.624	−5.850	1.00	19.51	6	C
ATOM	847	CB	LEU A	113	52.870	26.002	−5.999	1.00	21.10	6	C
ATOM	848	CG	LEU A	113	53.662	26.552	−4.853	1.00	24.03	6	C
ATOM	849	CD1	LEU A	113	54.900	25.632	−4.677	1.00	19.16	6	C
ATOM	850	CD2	LEU A	113	54.083	27.998	−5.120	1.00	24.04	6	C
ATOM	851	C	LEU A	113	51.158	24.508	−4.801	1.00	17.03	6	C
ATOM	852	O	LEU A	113	50.116	25.162	−4.683	1.00	16.75	8	O
ATOM	853	N	LEU A	114	51.522	23.700	−3.740	1.00	18.49	7	N
ATOM	854	CA	LEU A	114	50.664	23.451	−2.634	1.00	17.95	6	C
ATOM	855	CB	LEU A	114	50.143	22.034	−2.424	1.00	19.85	6	C
ATOM	856	CG	LEU A	114	49.460	21.423	−3.695	1.00	23.60	6	C
ATOM	857	CD1	LEU A	114	48.843	20.154	−3.102	1.00	26.64	6	C
ATOM	858	CD2	LEU A	114	48.382	22.345	−4.172	1.00	21.17	6	C
ATOM	859	C	LEU A	114	51.419	23.777	−1.296	1.00	16.88	6	C
ATOM	860	O	LEU A	114	52.638	23.612	−1.303	1.00	19.10	8	O
ATOM	861	N	MET A	115	50.651	24.260	−0.366	1.00	16.64	7	N
ATOM	862	CA	MET A	115	51.342	24.700	0.865	1.00	22.56	6	C
ATOM	863	CB	MET A	115	51.003	26.206	0.696	1.00	28.53	6	C
ATOM	864	CG	MET A	115	49.907	26.765	1.596	1.00	34.11	6	C
ATOM	865	SD	MET A	115	49.652	28.550	1.466	1.00	37.01	16	S
ATOM	866	CE	MET A	115	51.135	29.351	1.982	1.00	39.07	6	C
ATOM	867	C	MET A	115	50.775	23.830	1.998	1.00	20.36	6	C
ATOM	868	O	MET A	115	49.633	23.417	1.899	1.00	21.26	8	O
ATOM	869	N	GLY A	116	51.565	23.625	3.073	1.00	19.46	7	N
ATOM	870	CA	GLY A	116	51.102	22.711	4.116	1.00	18.10	6	C
ATOM	871	C	GLY A	116	51.961	22.796	5.403	1.00	18.47	6	C
ATOM	872	O	GLY A	116	52.978	23.469	5.415	1.00	16.76	8	O
ATOM	873	N	THR A	117	51.360	22.195	6.420	1.00	17.51	7	N
ATOM	874	CA	THR A	117	52.076	22.228	7.730	1.00	19.25	6	C
ATOM	875	CB	THR A	117	51.737	23.548	8.444	1.00	21.89	6	C
ATOM	876	OG1	THR A	117	52.507	23.641	9.658	1.00	26.41	8	O
ATOM	877	CG2	THR A	117	50.272	23.539	8.776	1.00	25.02	6	C
ATOM	878	C	THR A	117	51.620	20.989	8.482	1.00	18.36	6	C
ATOM	879	O	THR A	117	50.579	20.398	8.140	1.00	21.62	8	O
ATOM	880	N	THR A	118	52.471	20.531	9.427	1.00	18.75	7	N
ATOM	881	CA	THR A	118	52.126	19.278	10.091	1.00	16.38	6	C
ATOM	882	CB	THR A	118	53.093	18.158	9.577	1.00	16.51	6	C
ATOM	883	OG1	THR A	118	52.519	16.881	9.952	1.00	18.48	8	O
ATOM	884	CG2	THR A	118	54.527	18.234	10.036	1.00	16.97	6	C
ATOM	885	C	THR A	118	52.213	19.422	11.608	1.00	19.31	6	C
ATOM	886	O	THR A	118	52.986	20.236	12.109	1.00	19.95	8	O
ATOM	887	N	THR A	119	51.516	18.530	12.289	1.00	17.85	7	N
ATOM	888	CA	THR A	119	51.603	18.471	13.738	1.00	20.62	6	C
ATOM	889	CB	THR A	119	50.306	18.508	14.510	1.00	21.64	6	C
ATOM	890	OG1	THR A	119	49.405	17.452	14.107	1.00	21.73	8	O
ATOM	891	CG2	THR A	119	49.552	19.832	14.282	1.00	24.91	6	C
ATOM	892	C	THR A	119	52.293	17.139	14.097	1.00	22.31	6	C
ATOM	893	O	THR A	119	52.425	16.856	15.310	1.00	24.98	8	O
ATOM	894	N	HIS A	120	52.768	16.441	13.073	1.00	21.78	7	N
ATOM	895	CA	HIS A	120	53.632	15.286	13.365	1.00	19.23	6	C
ATOM	896	CB	HIS A	120	54.077	14.504	12.138	1.00	18.17	6	C
ATOM	897	CG	HIS A	120	53.142	13.400	11.723	1.00	17.11	6	C
ATOM	898	CD2	HIS A	120	53.227	12.102	12.102	1.00	16.15	6	C
ATOM	899	ND1	HIS A	120	52.066	13.447	10.881	1.00	20.80	7	N
ATOM	900	CE1	HIS A	120	51.504	12.252	10.723	1.00	16.47	6	C
ATOM	901	NE2	HIS A	120	52.231	11.403	11.501	1.00	20.33	7	N
ATOM	902	C	HIS A	120	54.851	15.888	14.043	1.00	19.92	6	C
ATOM	903	O	HIS A	120	55.330	16.956	13.615	1.00	21.65	8	O
ATOM	904	N	ALA A	121	55.542	15.129	14.895	1.00	19.64	7	N
ATOM	905	CA	ALA A	121	56.722	15.603	15.596	1.00	20.97	6	C
ATOM	906	CB	ALA A	121	56.447	15.713	17.091	1.00	20.83	6	C
ATOM	907	C	ALA A	121	57.877	14.606	15.379	1.00	20.32	6	C
ATOM	908	O	ALA A	121	57.661	13.416	15.530	1.00	20.48	8	O
ATOM	909	N	ALA A	122	58.948	15.085	14.841	1.00	20.43	7	N
ATOM	910	CA	ALA A	122	60.133	14.319	14.482	1.00	18.93	6	C
ATOM	911	CB	ALA A	122	60.296	14.084	12.985	1.00	23.71	6	C
ATOM	912	C	ALA A	122	61.384	15.071	14.922	1.00	21.86	6	C
ATOM	913	O	ALA A	122	61.629	16.224	14.543	1.00	23.59	8	O
ATOM	914	N	ARG A	123	62.209	14.422	15.742	1.00	22.93	7	N
ATOM	915	CA	ARG A	123	63.429	15.000	16.302	1.00	23.09	6	C
ATOM	916	CB	ARG A	123	63.416	14.740	17.846	1.00	23.23	6	C
ATOM	917	CG	ARG A	123	64.439	15.643	18.523	1.00	29.39	6	C
ATOM	918	CD	ARG A	123	64.440	15.454	20.029	1.00	29.72	6	C
ATOM	919	NE	ARG A	123	64.915	14.095	20.372	1.00	31.81	7	N
ATOM	920	CZ	ARG A	123	64.191	13.171	20.969	1.00	31.03	6	C
ATOM	921	NH1	ARG A	123	62.957	13.363	21.353	1.00	32.54	7	N
ATOM	922	NH2	ARG A	123	64.757	11.982	21.176	1.00	31.02	7	N
ATOM	923	C	ARG A	123	64.696	14.378	15.744	1.00	21.31	6	C
ATOM	924	O	ARG A	123	64.755	13.186	15.473	1.00	21.06	8	O
ATOM	925	N	ARG A	124	65.738	15.202	15.492	1.00	21.81	7	N
ATOM	926	CA	ARG A	124	66.982	14.627	14.981	1.00	22.14	6	C
ATOM	927	CB	ARG A	124	67.537	15.375	13.766	1.00	26.55	6	C
ATOM	928	CG	ARG A	124	68.974	15.092	13.354	1.00	29.85	6	C
ATOM	929	CD	ARG A	124	69.297	15.837	12.065	1.00	36.14	6	C
ATOM	930	NE	ARG A	124	70.279	15.186	11.256	1.00	38.31	7	N
ATOM	931	CZ	ARG A	124	70.445	15.060	9.959	1.00	42.15	6	C
ATOM	932	NH1	ARG A	124	71.533	14.378	9.575	1.00	43.04	7	N
ATOM	933	NH2	ARG A	124	69.643	15.525	9.016	1.00	40.89	7	N
ATOM	934	C	ARG A	124	68.019	14.637	16.108	1.00	23.57	6	C
ATOM	935	O	ARG A	124	68.272	15.673	16.740	1.00	24.93	8	O
ATOM	936	N	ASP A	125	68.523	13.439	16.435	1.00	21.32	7	N
ATOM	937	CA	ASP A	125	69.604	13.276	17.399	1.00	22.50	6	C
ATOM	938	CB	ASP A	125	69.177	12.237	18.461	1.00	26.84	6	C
ATOM	939	CG	ASP A	125	69.872	12.410	19.794	1.00	33.28	6	C
ATOM	940	OD1	ASP A	125	71.081	12.757	19.821	1.00	36.62	8	O
ATOM	941	OD2	ASP A	125	69.269	12.241	20.883	1.00	36.16	8	O
ATOM	942	C	ASP A	125	70.833	12.756	16.681	1.00	22.87	6	C
ATOM	943	O	ASP A	125	70.986	11.610	16.378	1.00	21.22	8	O
ATOM	944	N	GLY A	126	71.701	13.672	16.168	1.00	22.62	7	N
ATOM	945	CA	GLY A	126	72.859	13.236	15.376	1.00	25.05	6	C
ATOM	946	C	GLY A	126	72.361	12.694	14.033	1.00	26.03	6	C
ATOM	947	O	GLY A	126	71.685	13.393	13.286	1.00	27.91	8	O
ATOM	948	N	ASN A	127	72.634	11.422	13.752	1.00	25.62	7	N
ATOM	949	CA	ASN A	127	72.215	10.753	12.538	1.00	28.77	6	C
ATOM	950	CB	ASN A	127	73.334	9.949	11.887	1.00	34.37	6	C
ATOM	951	CG	ASN A	127	74.520	10.856	11.544	1.00	38.21	6	C
ATOM	952	OD1	ASN A	127	74.254	11.920	10.968	1.00	41.87	8	O
ATOM	953	ND2	ASN A	127	75.728	10.471	11.907	1.00	41.91	7	N
ATOM	954	C	ASN A	127	70.991	9.865	12.808	1.00	26.63	6	C
ATOM	955	O	ASN A	127	70.666	9.018	11.983	1.00	27.36	8	O
ATOM	956	N	VAL A	128	70.452	10.046	14.010	1.00	22.18	7	N
ATOM	957	CA	VAL A	128	69.205	9.291	14.332	1.00	18.19	6	C
ATOM	958	CB	VAL A	128	69.205	8.608	15.726	1.00	18.38	6	C
ATOM	959	CG1	VAL A	128	67.897	7.843	15.987	1.00	19.12	6	C
ATOM	960	CG2	VAL A	128	70.310	7.548	15.766	1.00	20.01	6	C
ATOM	961	C	VAL A	128	67.986	10.191	14.274	1.00	18.73	6	C
ATOM	962	O	VAL A	128	68.025	11.216	14.929	1.00	19.21	8	O
ATOM	963	N	ILE A	129	66.885	9.791	13.620	1.00	19.98	7	N
ATOM	964	CA	ILE A	129	65.668	10.583	13.613	1.00	17.06	6	C
ATOM	965	CB	ILE A	129	65.085	10.783	12.210	1.00	16.56	6	C
ATOM	966	CG2	ILE A	129	63.764	11.544	12.262	1.00	17.69	6	C
ATOM	967	CG1	ILE A	129	66.083	11.492	11.324	1.00	17.86	6	C
ATOM	968	CD1	ILE A	129	66.738	12.760	11.797	1.00	18.89	6	C
ATOM	969	C	ILE A	129	64.648	9.847	14.465	1.00	18.59	6	C
ATOM	970	O	ILE A	129	64.437	8.643	14.258	1.00	21.80	8	O
ATOM	971	N	ILE A	130	63.969	10.532	15.338	1.00	17.75	7	N
ATOM	972	CA	ILE A	130	62.945	9.921	16.198	1.00	18.22	6	C
ATOM	973	CB	ILE A	130	63.234	10.203	17.675	1.00	18.34	6	C
ATOM	974	CG2	ILE A	130	62.171	9.527	18.566	1.00	23.73	6	C
ATOM	975	CG1	ILE A	130	64.638	9.672	18.046	1.00	19.70	6	C
ATOM	976	CD1	ILE A	130	65.800	10.582	17.806	1.00	23.85	6	C
ATOM	977	C	ILE A	130	61.572	10.470	15.833	1.00	18.69	6	C
ATOM	978	O	ILE A	130	61.332	11.697	15.844	1.00	21.39	8	O
ATOM	979	N	HIS A	131	60.682	9.538	15.458	1.00	17.63	7	N
ATOM	980	CA	HIS A	131	59.289	9.953	15.209	1.00	19.41	6	C
ATOM	981	CB	HIS A	131	58.556	8.966	14.288	1.00	19.44	6	C
ATOM	982	CG	HIS A	131	57.242	9.438	13.782	1.00	16.44	6	C
ATOM	983	CD2	HIS A	131	56.590	10.631	13.899	1.00	18.30	6	C
ATOM	984	ND1	HIS A	131	56.287	8.643	13.136	1.00	19.15	7	N
ATOM	985	CE1	HIS A	131	55.167	9.295	12.831	1.00	19.09	6	C
ATOM	986	NE2	HIS A	131	55.364	10.520	13.285	1.00	17.79	7	N
ATOM	987	C	HIS A	131	58.652	10.025	16.597	1.00	22.70	6	C
ATOM	988	O	HIS A	131	58.289	9.010	17.211	1.00	23.54	8	O
ATOM	989	N	VAL A	132	58.575	11.222	17.167	1.00	23.13	7	N
ATOM	990	CA	VAL A	132	58.088	11.444	18.514	1.00	24.97	6	C
ATOM	991	CB	VAL A	132	58.486	12.851	19.001	1.00	25.58	6	C
ATOM	992	CG1	VAL A	132	57.829	13.230	20.328	1.00	27.80	6	C
ATOM	993	CG2	VAL A	132	60.009	12.970	19.046	1.00	24.87	6	C
ATOM	994	C	VAL A	132	56.569	11.307	18.636	1.00	26.11	6	C
ATOM	995	O	VAL A	132	56.053	10.833	19.650	1.00	26.81	8	O
ATOM	996	N	ALA A	133	55.795	11.897	17.717	1.00	23.08	7	N
ATOM	997	CA	ALA A	133	54.369	11.749	17.758	1.00	21.40	6	C
ATOM	998	CB	ALA A	133	53.722	12.855	18.588	1.00	24.59	6	C
ATOM	999	C	ALA A	133	53.709	11.847	16.360	1.00	20.17	6	C
ATOM	1000	O	ALA A	133	54.233	12.463	15.494	1.00	20.54	8	O
ATOM	1001	N	ASN A	134	52.590	11.105	16.312	1.00	20.07	7	N
ATOM	1002	CA	ASN A	134	51.788	11.077	15.094	1.00	21.32	6	C
ATOM	1003	CB	ASN A	134	50.815	9.868	15.149	1.00	22.44	6	C
ATOM	1004	CG	ASN A	134	51.568	8.568	14.909	1.00	27.18	6	C
ATOM	1005	OD1	ASN A	134	52.184	8.360	13.889	1.00	31.36	8	O
ATOM	1006	ND2	ASN A	134	51.422	7.659	15.866	1.00	32.50	7	N
ATOM	1007	C	ASN A	134	50.959	12.338	15.079	1.00	20.24	6	C
ATOM	1008	O	ASN A	134	50.953	13.027	16.096	1.00	23.52	8	O
ATOM	1009	N	GLY A	135	50.354	12.710	13.965	1.00	20.08	7	N
ATOM	1010	CA	GLY A	135	49.564	13.959	13.948	1.00	20.50	6	C
ATOM	1011	C	GLY A	135	48.911	14.083	12.577	1.00	20.77	6	C
ATOM	1012	O	GLY A	135	48.600	13.088	11.917	1.00	19.40	8	O
ATOM	1013	N	ILE A	136	48.589	15.318	12.207	1.00	19.11	7	N
ATOM	1014	CA	ILE A	136	47.860	15.595	10.973	1.00	21.63	6	C
ATOM	1015	CB	ILE A	136	46.424	16.113	11.252	1.00	23.68	6	C
ATOM	1016	CG2	ILE A	136	46.492	17.392	12.068	1.00	26.67	6	C
ATOM	1017	CG1	ILE A	136	45.604	16.306	9.958	1.00	25.90	6	C
ATOM	1018	CD1	ILE A	136	44.088	16.306	10.319	1.00	31.29	6	C
ATOM	1019	C	ILE A	136	48.636	16.587	10.104	1.00	19.20	6	C
ATOM	1020	O	ILE A	136	49.258	17.522	10.601	1.00	20.74	8	O
ATOM	1021	N	THR A	137	48.583	16.374	8.813	1.00	19.40	7	N
ATOM	1022	CA	THR A	137	49.274	17.279	7.885	1.00	15.74	6	C
ATOM	1023	CB	THR A	137	50.191	16.495	6.929	1.00	18.54	6	C
ATOM	1024	OG1	THR A	137	51.216	15.809	7.698	1.00	16.49	8	O
ATOM	1025	CG2	THR A	137	50.861	17.443	5.925	1.00	16.61	6	C
ATOM	1026	C	THR A	137	48.150	17.983	7.065	1.00	16.50	6	C
ATOM	1027	O	THR A	137	47.336	17.245	6.496	1.00	16.25	8	O
ATOM	1028	N	HIS A	138	48.128	19.296	7.206	1.00	17.18	7	N
ATOM	1029	CA	HIS A	138	47.058	20.022	6.485	1.00	18.37	6	C
ATOM	1030	CB	HIS A	138	46.523	21.200	7.336	1.00	23.83	6	C
ATOM	1031	CG	HIS A	138	45.821	20.780	8.598	1.00	25.62	6	C
ATOM	1032	CD2	HIS A	138	44.634	20.213	8.773	1.00	25.94	6	C
ATOM	1033	ND1	HIS A	138	46.355	20.881	9.873	1.00	29.72	7	N
ATOM	1034	CE1	HIS A	138	45.479	20.408	10.747	1.00	28.06	6	C
ATOM	1035	NE2	HIS A	138	44.399	19.993	10.114	1.00	28.38	7	N
ATOM	1036	C	HIS A	138	47.649	20.597	5.212	1.00	19.00	6	C
ATOM	1037	O	HIS A	138	48.706	21.216	5.300	1.00	18.61	8	O
ATOM	1038	N	ILE A	139	47.060	20.376	4.036	1.00	18.69	7	N
ATOM	1039	CA	ILE A	139	47.665	20.954	2.823	1.00	16.45	6	C
ATOM	1040	CB	ILE A	139	48.345	19.873	1.975	1.00	19.05	6	C
ATOM	1041	CG2	ILE A	139	49.419	19.219	2.843	1.00	17.33	6	C
ATOM	1042	CG1	ILE A	139	47.343	18.786	1.489	1.00	19.82	6	C
ATOM	1043	CD1	ILE A	139	47.976	17.968	0.362	1.00	24.74	6	C
ATOM	1044	C	ILE A	139	46.582	21.657	2.016	1.00	16.59	6	C
ATOM	1045	O	ILE A	139	45.392	21.438	2.272	1.00	17.78	8	O
ATOM	1046	N	GLY A	140	46.942	22.455	1.030	1.00	17.82	7	N
ATOM	1047	CA	GLY A	140	45.962	23.146	0.204	1.00	17.52	6	C
ATOM	1048	C	GLY A	140	46.691	23.966	−0.851	1.00	17.87	6	C
ATOM	1049	O	GLY A	140	47.873	24.039	−0.949	1.00	16.45	8	O
ATOM	1050	N	PRO A	141	45.890	24.672	−1.697	1.00	16.51	7	N
ATOM	1051	CD	PRO A	141	44.406	24.623	−1.629	1.00	19.58	6	C
ATOM	1052	CA	PRO A	141	46.463	25.356	−2.815	1.00	18.64	6	C
ATOM	1053	CB	PRO A	141	45.212	25.506	−3.699	1.00	19.10	6	C
ATOM	1054	CG	PRO A	141	44.068	25.614	−2.764	1.00	20.80	6	C
ATOM	1055	C	PRO A	141	47.140	26.668	−2.466	1.00	17.22	6	C
ATOM	1056	O	PRO A	141	46.535	27.477	−1.743	1.00	23.01	8	O
ATOM	1057	N	ALA A	142	48.326	26.891	−2.991	1.00	17.82	7	N
ATOM	1058	CA	ALA A	142	49.064	28.137	−2.732	1.00	23.14	6	C
ATOM	1059	CB	ALA A	142	50.519	27.971	−3.124	1.00	25.44	6	C
ATOM	1060	C	ALA A	142	48.425	29.321	−3.426	1.00	27.19	6	C
ATOM	1061	O	ALA A	142	48.214	30.393	−2.836	1.00	30.17	8	O
ATOM	1062	N	ARG A	143	48.031	29.114	−4.688	1.00	27.39	7	N
ATOM	1063	CA	ARG A	143	47.435	30.206	−5.474	1.00	31.04	6	C
ATOM	1064	CB	ARG A	143	48.432	30.602	−6.585	1.00	30.87	6	C
ATOM	1065	CG	ARG A	143	49.836	30.972	−6.164	1.00	31.39	6	C
ATOM	1066	CD	ARG A	143	50.833	30.738	−7.285	1.00	31.39	6	C
ATOM	1067	NE	ARG A	143	50.873	29.353	−7.750	1.00	27.23	7	N
ATOM	1068	CZ	ARG A	143	51.779	28.869	−8.610	1.00	25.80	6	C
ATOM	1069	NH1	ARG A	143	52.760	29.628	−9.081	1.00	25.09	7	N
ATOM	1070	NH2	ARG A	143	51.745	27.595	−8.978	1.00	24.32	7	N
ATOM	1071	C	ARG A	143	46.107	29.759	−6.026	1.00	30.38	6	C
ATOM	1072	O	ARG A	143	45.716	28.600	−6.054	1.00	29.56	8	O
ATOM	1073	N	GLN A	144	45.388	30.683	−6.744	1.00	34.97	7	N
ATOM	1074	CA	GLN A	144	44.096	30.284	−7.307	1.00	37.01	6	C
ATOM	1075	CB	GLN A	144	43.444	31.577	−7.862	1.00	42.13	6	C
ATOM	1076	CG	GLN A	144	43.274	32.527	−6.683	1.00	46.82	6	C
ATOM	1077	CD	GLN A	144	42.412	33.744	−6.935	1.00	50.54	6	C
ATOM	1078	OE1	GLN A	144	42.502	34.392	−7.992	1.00	52.59	8	O
ATOM	1079	NE2	GLN A	144	41.572	34.087	−5.953	1.00	50.31	7	N
ATOM	1080	C	GLN A	144	44.186	29.186	−8.330	1.00	35.09	6	C
ATOM	1081	O	GLN A	144	43.439	28.231	−8.458	1.00	35.19	8	O
ATOM	1082	N	GLN A	145	45.277	29.212	−9.098	1.00	35.05	7	N
ATOM	1083	CA	GLN A	145	45.584	28.232	−10.114	1.00	31.72	6	C
ATOM	1084	CB	GLN A	145	46.605	28.813	−11.078	1.00	34.36	6	C
ATOM	1085	CG	GLN A	145	48.042	28.996	−10.680	1.00	33.82	6	C
ATOM	1086	CD	GLN A	145	48.463	30.393	−10.265	1.00	36.58	6	C
ATOM	1087	OE1	GLN A	145	47.779	31.296	−9.770	1.00	36.44	8	O
ATOM	1088	NE2	GLN A	145	49.755	30.685	−10.421	1.00	36.77	7	N
ATOM	1089	C	GLN A	145	46.039	26.855	−9.616	1.00	28.92	6	C
ATOM	1090	O	GLN A	145	46.190	25.988	−10.468	1.00	26.42	8	O
ATOM	1091	N	ASP A	146	46.177	26.628	−8.297	1.00	24.03	7	N
ATOM	1092	CA	ASP A	146	46.550	25.278	−7.822	1.00	22.12	6	C
ATOM	1093	CB	ASP A	146	47.570	25.571	−6.678	1.00	22.29	6	C
ATOM	1094	CG	ASP A	146	48.725	26.364	−7.251	1.00	19.59	6	C
ATOM	1095	OD1	ASP A	146	49.373	26.005	−8.273	1.00	23.09	8	O
ATOM	1096	OD2	ASP A	146	48.984	27.431	−6.658	1.00	21.75	8	O
ATOM	1097	C	ASP A	146	45.439	24.484	−7.205	1.00	22.09	6	C
ATOM	1098	O	ASP A	146	45.552	23.429	−6.524	1.00	21.95	8	O
ATOM	1099	N	GLY A	147	44.188	24.933	−7.307	1.00	20.41	7	N
ATOM	1100	CA	GLY A	147	43.078	24.336	−6.616	1.00	22.44	6	C
ATOM	1101	C	GLY A	147	42.648	22.966	−7.094	1.00	20.12	6	C
ATOM	1102	O	GLY A	147	41.821	22.407	−6.393	1.00	20.35	8	O
ATOM	1103	N	ASP A	148	43.150	22.417	−8.220	1.00	18.21	7	N
ATOM	1104	CA	ASP A	148	42.597	21.129	−8.666	1.00	19.50	6	C
ATOM	1105	CB	ASP A	148	42.619	21.018	−10.198	1.00	19.46	6	C
ATOM	1106	CG	ASP A	148	41.656	22.017	−10.872	1.00	19.59	6	C
ATOM	1107	OD1	ASP A	148	40.773	22.496	−10.126	1.00	23.55	8	O
ATOM	1108	OD2	ASP A	148	41.857	22.327	−12.054	1.00	22.94	8	O
ATOM	1109	C	ASP A	148	43.462	19.934	−8.202	1.00	20.82	6	C
ATOM	1110	O	ASP A	148	43.276	18.830	−8.704	1.00	19.57	8	O
ATOM	1111	N	TYR A	149	44.287	20.152	−7.171	1.00	17.71	7	N
ATOM	1112	CA	TYR A	149	45.253	19.083	−6.803	1.00	19.31	6	C
ATOM	1113	CB	TYR A	149	46.673	19.764	−6.813	1.00	19.25	6	C
ATOM	1114	CG	TYR A	149	47.105	19.891	−8.276	1.00	18.61	6	C
ATOM	1115	CD1	TYR A	149	46.719	20.962	−9.052	1.00	18.99	6	C
ATOM	1116	CE1	TYR A	149	47.061	21.054	−10.388	1.00	20.38	6	C
ATOM	1117	CD2	TYR A	149	47.918	18.921	−8.882	1.00	18.56	6	C
ATOM	1118	CE2	TYR A	149	48.266	18.974	−10.202	1.00	21.43	6	C
ATOM	1119	CZ	TYR A	149	47.839	20.061	−10.955	1.00	21.46	6	C
ATOM	1120	OH	TYR A	149	48.131	20.116	−12.304	1.00	24.87	8	O
ATOM	1121	C	TYR A	149	44.966	18.399	−5.496	1.00	19.78	6	C
ATOM	1122	O	TYR A	149	45.795	17.754	−4.838	1.00	19.59	8	O
ATOM	1123	N	SER A	150	43.685	18.336	−5.118	1.00	19.04	7	N
ATOM	1124	CA	SER A	150	43.201	17.703	−3.893	1.00	18.29	6	C
ATOM	1125	CB	SER A	150	41.778	18.114	−3.619	1.00	21.78	6	C
ATOM	1126	OG	SER A	150	40.839	17.596	−4.580	1.00	24.40	8	O
ATOM	1127	C	SER A	150	43.418	16.201	−3.879	1.00	19.10	6	C
ATOM	1128	O	SER A	150	43.538	15.581	−2.797	1.00	16.86	8	O
ATOM	1129	N	TYR A	151	43.630	15.584	−5.098	1.00	17.41	7	N
ATOM	1130	CA	TYR A	151	43.992	14.192	−5.117	1.00	18.39	6	C
ATOM	1131	CB	TYR A	151	44.143	13.607	−6.535	1.00	19.38	6	C
ATOM	1132	CG	TYR A	151	45.412	14.035	−7.229	1.00	19.51	6	C
ATOM	1133	CD1	TYR A	151	46.527	13.165	−7.130	1.00	18.99	6	C
ATOM	1134	CE1	TYR A	151	47.723	13.514	−7.732	1.00	20.45	6	C
ATOM	1135	CD2	TYR A	151	45.561	15.226	−7.900	1.00	19.91	6	C
ATOM	1136	CE2	TYR A	151	46.763	15.573	−8.520	1.00	17.70	6	C
ATOM	1137	CZ	TYR A	151	47.839	14.704	−8.408	1.00	20.22	6	C
ATOM	1138	OH	TYR A	151	49.008	15.082	−9.008	1.00	21.10	8	O
ATOM	1139	C	TYR A	151	45.260	13.871	−4.315	1.00	19.82	6	C
ATOM	1140	O	TYR A	151	45.371	12.734	−3.846	1.00	18.80	8	O
ATOM	1141	N	LEU A	152	46.251	14.778	−4.265	1.00	18.06	7	N
ATOM	1142	CA	LEU A	152	47.412	14.487	−3.435	1.00	17.83	6	C
ATOM	1143	CB	LEU A	152	48.389	15.681	−3.520	1.00	18.77	6	C
ATOM	1144	CG	LEU A	152	48.991	15.943	−4.885	1.00	20.30	6	C
ATOM	1145	CD1	LEU A	152	49.729	17.268	−4.940	1.00	22.80	6	C
ATOM	1146	CD2	LEU A	152	49.969	14.799	−5.168	1.00	22.59	6	C
ATOM	1147	C	LEU A	152	47.073	14.230	−1.984	1.00	17.28	6	C
ATOM	1148	O	LEU A	152	47.821	13.450	−1.336	1.00	17.59	8	O
ATOM	1149	N	ALA A	153	46.021	14.831	−1.393	1.00	15.70	7	N
ATOM	1150	CA	ALA A	153	45.725	14.550	0.011	1.00	16.83	6	C
ATOM	1151	CB	ALA A	153	44.783	15.594	0.556	1.00	16.96	6	C
ATOM	1152	C	ALA A	153	45.173	13.116	0.193	1.00	17.84	6	C
ATOM	1153	O	ALA A	153	45.460	12.457	1.201	1.00	19.86	8	O
ATOM	1154	N	ASP A	154	44.451	12.613	−0.837	1.00	17.86	7	N
ATOM	1155	CA	ASP A	154	44.077	11.213	−0.746	1.00	18.40	6	C
ATOM	1156	CB	ASP A	154	43.075	10.857	−1.890	1.00	23.21	6	C
ATOM	1157	CG	ASP A	154	41.826	11.731	−1.783	1.00	27.81	6	C
ATOM	1158	OD1	ASP A	154	41.377	11.886	−0.635	1.00	29.48	8	O
ATOM	1159	OD2	ASP A	154	41.322	12.207	−2.825	1.00	29.29	8	O
ATOM	1160	C	ASP A	154	45.281	10.286	−0.872	1.00	17.75	6	C
ATOM	1161	O	ASP A	154	45.276	9.260	−0.169	1.00	19.35	8	O
ATOM	1162	N	ILE A	155	46.233	10.545	−1.791	1.00	18.07	7	N
ATOM	1163	CA	ILE A	155	47.363	9.600	−1.891	1.00	18.81	6	C
ATOM	1164	CB	ILE A	155	48.268	10.046	−3.051	1.00	18.97	6	C
ATOM	1165	CG2	ILE A	155	49.584	9.278	−3.003	1.00	21.14	6	C
ATOM	1166	CG1	ILE A	155	47.573	9.892	−4.403	1.00	19.05	6	C
ATOM	1167	CD1	ILE A	155	48.320	10.463	−5.609	1.00	21.72	6	C
ATOM	1168	C	ILE A	155	48.155	9.631	−0.574	1.00	19.63	6	C
ATOM	1169	O	ILE A	155	48.599	8.626	−0.012	1.00	18.45	8	O
ATOM	1170	N	LEU A	156	48.514	10.877	−0.163	1.00	18.51	7	N
ATOM	1171	CA	LEU A	156	49.330	11.051	1.062	1.00	18.42	6	C
ATOM	1172	CB	LEU A	156	49.886	12.498	1.167	1.00	17.08	6	C
ATOM	1173	CG	LEU A	156	50.696	12.921	−0.066	1.00	18.25	6	C
ATOM	1174	CD1	LEU A	156	51.137	14.361	−0.133	1.00	18.42	6	C
ATOM	1175	CD2	LEU A	156	51.981	12.051	−0.126	1.00	17.93	6	C
ATOM	1176	C	LEU A	156	48.661	10.469	2.311	1.00	20.17	6	C
ATOM	1177	O	LEU A	156	49.388	10.083	3.271	1.00	17.32	8	O
ATOM	1178	N	GLN A	157	47.341	10.474	2.415	1.00	17.74	7	N
ATOM	1179	CA	GLN A	157	46.660	9.866	3.556	1.00	20.92	6	C
ATOM	1180	CB	GLN A	157	45.165	9.975	3.328	1.00	20.02	6	C
ATOM	1181	CG	GLN A	157	44.351	9.149	4.326	1.00	23.11	6	C
ATOM	1182	CD	GLN A	157	44.402	9.703	5.739	1.00	26.23	6	C
ATOM	1183	OE1	GLN A	157	44.563	10.899	6.002	1.00	26.75	8	O
ATOM	1184	NE2	GLN A	157	44.167	8.825	6.716	1.00	25.25	7	N
ATOM	1185	C	GLN A	157	47.115	8.399	3.682	1.00	20.20	6	C
ATOM	1186	O	GLN A	157	47.256	7.940	4.825	1.00	24.89	8	O
ATOM	1187	N	THR A	158	47.184	7.690	2.560	1.00	21.62	7	N
ATOM	1188	CA	THR A	158	47.620	6.298	2.561	1.00	23.71	6	C
ATOM	1189	CB	THR A	158	47.393	5.565	1.207	1.00	24.12	6	C
ATOM	1190	OG1	THR A	158	48.340	6.029	0.221	1.00	26.48	8	O
ATOM	1191	CG2	THR A	158	45.978	5.718	0.677	1.00	24.75	6	C
ATOM	1192	C	THR A	158	49.045	6.078	2.999	1.00	22.40	6	C
ATOM	1193	O	THR A	158	49.491	4.921	3.279	1.00	22.94	8	O
ATOM	1194	N	VAL A	159	49.915	7.105	2.970	1.00	18.84	7	N
ATOM	1195	CA	VAL A	159	51.313	7.010	3.279	1.00	17.40	6	C
ATOM	1196	CB	VAL A	159	52.025	8.038	2.343	1.00	20.38	6	C
ATOM	1197	CG1	VAL A	159	53.483	8.258	2.615	1.00	18.85	6	C
ATOM	1198	CG2	VAL A	159	51.795	7.503	0.946	1.00	20.55	6	C
ATOM	1199	C	VAL A	159	51.642	7.413	4.693	1.00	18.65	6	C
ATOM	1200	O	VAL A	159	52.420	6.732	5.370	1.00	17.88	8	O
ATOM	1201	N	LEU A	160	51.139	8.516	5.238	1.00	18.36	7	N
ATOM	1202	CA	LEU A	160	51.415	9.006	6.556	1.00	14.96	6	C
ATOM	1203	CB	LEU A	160	52.592	10.035	6.502	1.00	14.95	6	C
ATOM	1204	CG	LEU A	160	52.952	10.554	7.920	1.00	15.76	6	C
ATOM	1205	CD1	LEU A	160	53.677	9.452	8.679	1.00	18.53	6	C
ATOM	1206	CD2	LEU A	160	53.818	11.827	7.863	1.00	17.23	6	C
ATOM	1207	C	LEU A	160	50.162	9.655	7.122	1.00	19.50	6	C
ATOM	1208	O	LEU A	160	49.937	10.845	7.007	1.00	17.83	8	O
ATOM	1209	N	PRO A	161	49.242	8.791	7.623	1.00	20.05	7	N
ATOM	1210	CD	PRO A	161	49.447	7.346	7.746	1.00	22.88	6	C
ATOM	1211	CA	PRO A	161	47.987	9.317	8.188	1.00	22.07	6	C
ATOM	1212	CB	PRO A	161	47.427	8.034	8.827	1.00	23.37	6	C
ATOM	1213	CG	PRO A	161	48.104	6.871	8.206	1.00	25.78	6	C
ATOM	1214	C	PRO A	161	48.269	10.387	9.197	1.00	17.48	6	C
ATOM	1215	O	PRO A	161	49.206	10.280	10.005	1.00	18.09	8	O
ATOM	1216	N	ASP A	162	47.441	11.408	9.434	1.00	17.11	7	N
ATOM	1217	CA	ASP A	162	46.275	11.733	8.634	1.00	20.91	6	C
ATOM	1218	CB	ASP A	162	45.110	12.191	9.533	1.00	21.15	6	C
ATOM	1219	CG	ASP A	162	44.606	11.011	10.384	1.00	23.93	6	C
ATOM	1220	OD1	ASP A	162	44.427	11.224	11.597	1.00	26.09	8	O
ATOM	1221	OD2	ASP A	162	44.359	9.974	9.747	1.00	25.38	8	O
ATOM	1222	C	ASP A	162	46.635	12.948	7.754	1.00	20.14	6	C
ATOM	1223	O	ASP A	162	47.409	13.818	8.216	1.00	17.58	8	O
ATOM	1224	N	VAL A	163	45.983	13.117	6.591	1.00	18.77	7	N
ATOM	1225	CA	VAL A	163	46.256	14.288	5.761	1.00	20.26	6	C
ATOM	1226	CB	VAL A	163	46.955	13.882	4.449	1.00	19.23	6	C
ATOM	1227	CG1	VAL A	163	47.205	15.131	3.548	1.00	18.64	6	C
ATOM	1228	CG2	VAL A	163	48.279	13.185	4.773	1.00	17.67	6	C
ATOM	1229	C	VAL A	163	44.912	14.950	5.418	1.00	25.61	6	C
ATOM	1230	O	VAL A	163	43.982	14.148	5.193	1.00	26.99	8	O
ATOM	1231	N	ALA A	164	44.802	16.252	5.477	1.00	23.09	7	N
ATOM	1232	CA	ALA A	164	43.520	16.903	5.130	1.00	25.35	6	C
ATOM	1233	CB	ALA A	164	42.885	17.556	6.366	1.00	26.07	6	C
ATOM	1234	C	ALA A	164	43.742	18.004	4.101	1.00	25.43	6	C
ATOM	1235	O	ALA A	164	44.669	18.783	4.256	1.00	21.31	8	O
ATOM	1236	N	TRP A	165	42.884	18.080	3.094	1.00	25.90	7	N
ATOM	1237	CA	TRP A	165	42.910	19.161	2.119	1.00	24.31	6	C
ATOM	1238	CB	TRP A	165	42.277	18.601	0.828	1.00	24.64	6	C
ATOM	1239	CG	TRP A	165	42.165	19.645	−0.249	1.00	23.94	6	C
ATOM	1240	CD2	TRP A	165	43.210	20.066	−1.134	1.00	23.27	6	C
ATOM	1241	CE2	TRP A	165	42.664	21.063	−1.987	1.00	24.22	6	C
ATOM	1242	CE3	TRP A	165	44.562	19.693	−1.303	1.00	21.75	6	C
ATOM	1243	CD1	TRP A	165	41.047	20.380	−0.564	1.00	24.22	6	C
ATOM	1244	NE1	TRP A	165	41.358	21.237	−1.562	1.00	24.36	7	N
ATOM	1245	CZ2	TRP A	165	43.434	21.668	−2.951	1.00	24.21	6	C
ATOM	1246	CZ3	TRP A	165	45.293	20.315	−2.316	1.00	23.39	6	C
ATOM	1247	CH2	TRP A	165	44.731	21.317	−3.143	1.00	22.79	6	C
ATOM	1248	C	TRP A	165	42.023	20.330	2.597	1.00	23.95	6	C
ATOM	1249	O	TRP A	165	40.956	20.025	3.102	1.00	24.83	8	O
ATOM	1250	N	HIS A	166	42.533	21.523	2.498	1.00	21.92	7	N
ATOM	1251	CA	HIS A	166	41.763	22.731	2.813	1.00	26.16	6	C
ATOM	1252	CB	HIS A	166	42.503	23.520	3.923	1.00	28.94	6	C
ATOM	1253	CG	HIS A	166	42.416	23.009	5.311	1.00	31.73	6	C
ATOM	1254	CD2	HIS A	166	41.819	23.535	6.397	1.00	32.29	6	C
ATOM	1255	ND1	HIS A	166	43.012	21.846	5.744	1.00	35.64	7	N
ATOM	1256	CE1	HIS A	166	42.752	21.671	7.021	1.00	33.06	6	C
ATOM	1257	NE2	HIS A	166	42.009	22.662	7.460	1.00	35.48	7	N
ATOM	1258	C	HIS A	166	41.769	23.651	1.600	1.00	27.45	6	C
ATOM	1259	O	HIS A	166	42.867	24.027	1.162	1.00	24.48	8	O
ATOM	1260	N	ASN A	167	40.577	24.065	1.151	1.00	27.45	7	N
ATOM	1261	CA	ASN A	167	40.602	25.027	0.031	1.00	28.70	6	C
ATOM	1262	CB	ASN A	167	39.215	25.180	−0.565	1.00	32.95	6	C
ATOM	1263	CG	ASN A	167	38.685	23.910	−1.201	1.00	37.78	6	C
ATOM	1264	OD1	ASN A	167	37.750	23.235	−0.724	1.00	43.16	8	O
ATOM	1265	ND2	ASN A	167	39.249	23.490	−2.322	1.00	38.01	7	N
ATOM	1266	C	ASN A	167	41.224	26.367	0.396	1.00	29.07	6	C
ATOM	1267	O	ASN A	167	41.787	27.080	−0.446	1.00	29.87	8	O
ATOM	1268	N	ASN A	168	41.151	26.758	1.656	1.00	28.01	7	N
ATOM	1269	CA	ASN A	168	41.735	27.986	2.191	1.00	27.50	6	C
ATOM	1270	CB	ASN A	168	40.586	28.843	2.716	1.00	30.31	6	C
ATOM	1271	CG	ASN A	168	41.110	30.176	3.249	1.00	34.40	6	C
ATOM	1272	OD1	ASN A	168	40.418	30.801	4.029	1.00	35.33	8	O
ATOM	1273	ND2	ASN A	168	42.277	30.557	2.754	1.00	34.66	7	N
ATOM	1274	C	ASN A	168	42.675	27.612	3.337	1.00	25.27	6	C
ATOM	1275	O	ASN A	168	42.411	27.775	4.535	1.00	25.28	8	O
ATOM	1276	N	ILE A	169	43.817	27.070	2.946	1.00	23.01	7	N
ATOM	1277	CA	ILE A	169	44.824	26.571	3.869	1.00	22.62	6	C
ATOM	1278	CB	ILE A	169	45.870	25.743	3.111	1.00	22.81	6	C
ATOM	1279	CG2	ILE A	169	46.662	26.592	2.150	1.00	24.55	6	C
ATOM	1280	CG1	ILE A	169	46.825	25.062	4.140	1.00	22.70	6	C
ATOM	1281	CD1	ILE A	169	46.171	24.064	5.042	1.00	24.31	6	C
ATOM	1282	C	ILE A	169	45.447	27.697	4.705	1.00	21.77	6	C
ATOM	1283	O	ILE A	169	45.858	27.466	5.841	1.00	17.89	8	O
ATOM	1284	N	ARG A	170	45.464	28.937	4.194	1.00	24.71	7	N
ATOM	1285	CA	ARG A	170	46.002	30.060	4.980	1.00	26.16	6	C
ATOM	1286	CB	ARG A	170	45.977	31.408	4.246	1.00	25.22	6	C
ATOM	1287	CG	ARG A	170	47.035	31.472	3.136	1.00	26.01	6	C
ATOM	1288	CD	ARG A	170	46.739	32.618	2.183	1.00	28.66	6	C
ATOM	1289	NE	ARG A	170	47.777	32.796	1.170	1.00	28.74	7	N
ATOM	1290	CZ	ARG A	170	47.921	32.047	0.078	1.00	28.10	6	C
ATOM	1291	NH1	ARG A	170	47.112	31.054	−0.198	1.00	27.50	7	N
ATOM	1292	NH2	ARG A	170	48.916	32.299	−0.773	1.00	26.55	7	N
ATOM	1293	C	ARG A	170	45.278	30.230	6.316	1.00	23.86	6	C
ATOM	1294	O	ARG A	170	45.888	30.743	7.289	1.00	22.23	8	O
ATOM	1295	N	ALA A	171	44.008	29.907	6.462	1.00	25.00	7	N
ATOM	1296	CA	ALA A	171	43.328	29.992	7.754	1.00	25.32	6	C
ATOM	1297	CB	ALA A	171	41.885	29.555	7.584	1.00	26.49	6	C
ATOM	1298	C	ALA A	171	44.029	29.135	8.811	1.00	26.63	6	C
ATOM	1299	O	ALA A	171	44.307	29.602	9.939	1.00	25.59	8	O
ATOM	1300	N	GLU A	172	44.318	27.865	8.467	1.00	25.88	7	N
ATOM	1301	CA	GLU A	172	45.043	27.018	9.427	1.00	27.61	6	C
ATOM	1302	CB	GLU A	172	44.953	25.537	8.990	1.00	32.05	6	C
ATOM	1303	CG	GLU A	172	44.147	24.675	10.005	1.00	39.62	6	C
ATOM	1304	CD	GLU A	172	45.075	24.212	11.102	1.00	43.09	6	C
ATOM	1305	OE1	GLU A	172	46.310	24.301	10.824	1.00	46.76	8	O
ATOM	1306	OE2	GLU A	172	44.926	23.763	12.243	1.00	46.39	8	O
ATOM	1307	C	GLU A	172	46.496	27.484	9.632	1.00	23.72	6	C
ATOM	1308	O	GLU A	172	46.985	27.429	10.785	1.00	23.95	8	O
ATOM	1309	N	LEU A	173	47.171	27.918	8.556	1.00	21.07	7	N
ATOM	1310	CA	LEU A	173	48.528	28.435	8.732	1.00	22.25	6	C
ATOM	1311	CB	LEU A	173	49.153	28.820	7.406	1.00	21.01	6	C
ATOM	1312	CG	LEU A	173	49.162	27.731	6.323	1.00	20.24	6	C
ATOM	1313	CD1	LEU A	173	49.773	28.278	5.023	1.00	20.08	6	C
ATOM	1314	CD2	LEU A	173	49.855	26.479	6.849	1.00	22.60	6	C
ATOM	1315	C	LEU A	173	48.544	29.611	9.706	1.00	22.82	6	C
ATOM	1316	O	LEU A	173	49.421	29.704	10.555	1.00	21.34	8	O
ATOM	1317	N	TRP A	174	47.609	30.566	9.539	1.00	22.83	7	N
ATOM	1318	CA	TRP A	174	47.650	31.707	10.516	1.00	23.51	6	C
ATOM	1319	CB	TRP A	174	46.559	32.725	10.134	1.00	23.11	6	C
ATOM	1320	CG	TRP A	174	47.069	33.716	9.124	1.00	26.78	6	C
ATOM	1321	CD2	TRP A	174	47.989	34.778	9.399	1.00	28.58	6	C
ATOM	1322	CE2	TRP A	174	48.192	35.459	8.176	1.00	30.00	6	C
ATOM	1323	CE3	TRP A	174	48.652	35.210	10.553	1.00	28.70	6	C
ATOM	1324	CD1	TRP A	174	46.743	33.809	7.813	1.00	27.80	6	C
ATOM	1325	NE1	TRP A	174	47.419	34.852	7.221	1.00	29.52	7	N
ATOM	1326	CZ2	TRP A	174	49.034	36.571	8.081	1.00	31.38	6	C
ATOM	1327	CZ3	TRP A	174	49.507	36.332	10.443	1.00	29.43	6	C
ATOM	1328	CH2	TRP A	174	49.681	36.968	9.209	1.00	30.53	6	C
ATOM	1329	C	TRP A	174	47.375	31.312	11.950	1.00	25.29	6	C
ATOM	1330	O	TRP A	174	47.823	32.005	12.866	1.00	23.65	8	O
ATOM	1331	N	ARG A	175	46.584	30.275	12.205	1.00	24.50	7	N
ATOM	1332	CA	ARG A	175	46.257	29.876	13.568	1.00	26.52	6	C
ATOM	1333	CB	ARG A	175	45.290	28.700	13.664	1.00	28.84	6	C
ATOM	1334	CG	ARG A	175	44.985	28.364	15.144	1.00	33.06	6	C
ATOM	1335	CD	ARG A	175	44.082	27.143	15.260	1.00	37.50	6	C
ATOM	1336	NE	ARG A	175	44.737	25.928	14.797	1.00	41.71	7	N
ATOM	1337	CZ	ARG A	175	45.692	25.235	15.382	1.00	43.60	6	C
ATOM	1338	NH1	ARG A	175	46.220	25.593	16.553	1.00	44.31	7	N
ATOM	1339	NH2	ARG A	175	46.196	24.150	14.815	1.00	44.59	7	N
ATOM	1340	C	ARG A	175	47.567	29.468	14.251	1.00	25.51	6	C
ATOM	1341	O	ARG A	175	47.898	29.911	15.334	1.00	25.39	8	O
ATOM	1342	N	LYS A	176	48.355	28.625	13.559	1.00	23.60	7	N
ATOM	1343	CA	LYS A	176	49.640	28.258	14.145	1.00	23.20	6	C
ATOM	1344	CB	LYS A	176	50.234	27.029	13.428	1.00	26.07	6	C
ATOM	1345	CG	LYS A	176	49.285	25.821	13.676	1.00	34.60	6	C
ATOM	1346	CD	LYS A	176	50.194	24.602	13.582	1.00	40.07	6	C
ATOM	1347	CE	LYS A	176	50.524	24.233	12.142	1.00	43.53	6	C
ATOM	1348	NZ	LYS A	176	51.993	23.880	12.082	1.00	47.01	7	N
ATOM	1349	C	LYS A	176	50.646	29.381	14.188	1.00	21.35	6	C
ATOM	1350	O	LYS A	176	51.231	29.615	15.238	1.00	22.23	8	O
ATOM	1351	N	LEU A	177	50.764	30.193	13.122	1.00	18.60	7	N
ATOM	1352	CA	LEU A	177	51.716	31.332	13.150	1.00	18.23	6	C
ATOM	1353	CB	LEU A	177	51.715	32.043	11.793	1.00	22.54	6	C
ATOM	1354	CG	LEU A	177	52.784	33.167	11.675	1.00	24.69	6	C
ATOM	1355	CD1	LEU A	177	53.234	33.294	10.245	1.00	27.74	6	C
ATOM	1356	CD2	LEU A	177	52.041	34.461	12.047	1.00	30.03	6	C
ATOM	1357	C	LEU A	177	51.310	32.360	14.203	1.00	18.36	6	C
ATOM	1358	O	LEU A	177	52.190	32.931	14.870	1.00	20.29	8	O
ATOM	1359	N	ALA A	178	50.041	32.560	14.495	1.00	21.31	7	N
ATOM	1360	CA	ALA A	178	49.680	33.541	15.560	1.00	23.94	6	C
ATOM	1361	CB	ALA A	178	48.157	33.635	15.703	1.00	24.01	6	C
ATOM	1362	C	ALA A	178	50.308	33.185	16.907	1.00	23.64	6	C
ATOM	1363	O	ALA A	178	50.852	34.064	17.630	1.00	22.84	8	O
ATOM	1364	N	VAL A	179	50.168	31.929	17.282	1.00	21.39	7	N
ATOM	1365	CA	VAL A	179	50.732	31.438	18.549	1.00	22.43	6	C
ATOM	1366	CB	VAL A	179	50.343	29.981	18.861	1.00	22.10	6	C
ATOM	1367	CG1	VAL A	179	50.951	29.530	20.187	1.00	23.11	6	C
ATOM	1368	CG2	VAL A	179	48.820	29.834	18.937	1.00	23.47	6	C
ATOM	1369	C	VAL A	179	52.245	31.537	18.469	1.00	20.48	6	C
ATOM	1370	O	VAL A	179	52.908	31.945	19.413	1.00	19.73	8	O
ATOM	1371	N	ASN A	180	52.891	31.153	17.338	1.00	19.20	7	N
ATOM	1372	CA	ASN A	180	54.335	31.162	17.284	1.00	19.90	6	C
ATOM	1373	CB	ASN A	180	54.741	30.494	15.925	1.00	20.96	6	C
ATOM	1374	CG	ASN A	180	54.641	28.976	16.044	1.00	27.73	6	C
ATOM	1375	OD1	ASN A	180	54.775	28.408	17.135	1.00	30.37	8	O
ATOM	1376	ND2	ASN A	180	54.399	28.360	14.905	1.00	29.03	7	N
ATOM	1377	C	ASN A	180	54.935	32.565	17.346	1.00	18.72	6	C
ATOM	1378	O	ASN A	180	56.027	32.746	17.883	1.00	19.07	8	O
ATOM	1379	N	CYS A	181	54.171	33.577	16.899	1.00	18.21	7	N
ATOM	1380	CA	CYS A	181	54.684	34.954	17.001	1.00	19.81	6	C
ATOM	1381	CB	CYS A	181	53.695	35.935	16.354	1.00	19.04	6	C
ATOM	1382	SG	CYS A	181	53.758	35.997	14.522	1.00	20.27	16	S
ATOM	1383	C	CYS A	181	54.804	35.383	18.475	1.00	20.92	6	C
ATOM	1384	O	CYS A	181	55.605	36.297	18.689	1.00	20.72	8	O
ATOM	1385	N	VAL A	182	54.112	34.755	19.402	1.00	21.32	7	N
ATOM	1386	CA	VAL A	182	54.237	35.149	20.819	1.00	22.16	6	C
ATOM	1387	CB	VAL A	182	52.909	34.884	21.539	1.00	24.56	6	C
ATOM	1388	CG1	VAL A	182	53.106	35.037	23.070	1.00	24.16	6	C
ATOM	1389	CG2	VAL A	182	51.784	35.745	21.041	1.00	24.61	6	C
ATOM	1390	C	VAL A	182	55.290	34.282	21.489	1.00	22.03	6	C
ATOM	1391	O	VAL A	182	56.317	34.682	22.044	1.00	23.31	8	O
ATOM	1392	N	ILE A	183	55.035	32.961	21.459	1.00	21.31	7	N
ATOM	1393	CA	ILE A	183	55.914	32.016	22.141	1.00	23.41	6	C
ATOM	1394	CB	ILE A	183	55.275	30.592	22.170	1.00	25.25	6	C
ATOM	1395	CG2	ILE A	183	56.195	29.575	22.843	1.00	21.69	6	C
ATOM	1396	CG1	ILE A	183	53.937	30.690	22.897	1.00	22.10	6	C
ATOM	1397	CD1	ILE A	183	53.169	29.346	22.962	1.00	26.09	6	C
ATOM	1398	C	ILE A	183	57.348	31.988	21.670	1.00	24.52	6	C
ATOM	1399	O	ILE A	183	58.305	31.941	22.438	1.00	24.88	8	O
ATOM	1400	N	ASN A	184	57.668	31.937	20.363	1.00	19.27	7	N
ATOM	1401	CA	ASN A	184	58.998	31.742	19.876	1.00	23.27	6	C
ATOM	1402	CB	ASN A	184	59.013	31.461	18.363	1.00	25.05	6	C
ATOM	1403	CG	ASN A	184	58.715	30.015	18.026	1.00	29.29	6	C
ATOM	1404	OD1	ASN A	184	59.110	29.138	18.781	1.00	31.28	8	O
ATOM	1405	ND2	ASN A	184	58.066	29.666	16.912	1.00	31.45	7	N
ATOM	1406	C	ASN A	184	59.967	32.890	20.219	1.00	22.82	6	C
ATOM	1407	O	ASN A	184	60.979	32.560	20.809	1.00	23.61	8	O
ATOM	1408	N	PRO A	185	59.659	34.106	19.855	1.00	24.35	7	N
ATOM	1409	CD	PRO A	185	58.493	34.554	19.103	1.00	23.26	6	C
ATOM	1410	CA	PRO A	185	60.586	35.233	20.135	1.00	24.56	6	C
ATOM	1411	CB	PRO A	185	60.046	36.410	19.381	1.00	25.90	6	C
ATOM	1412	CG	PRO A	185	58.639	36.065	19.048	1.00	25.05	6	C
ATOM	1413	C	PRO A	185	60.671	35.542	21.642	1.00	25.36	6	C
ATOM	1414	O	PRO A	185	61.821	35.786	22.059	1.00	23.15	8	O
ATOM	1415	N	LEU A	186	59.590	35.511	22.388	1.00	23.66	7	N
ATOM	1416	CA	LEU A	186	59.723	35.775	23.848	1.00	25.26	6	C
ATOM	1417	CB	LEU A	186	58.381	35.851	24.519	1.00	26.65	6	C
ATOM	1418	CG	LEU A	186	57.497	37.047	24.176	1.00	26.42	6	C
ATOM	1419	CD1	LEU A	186	56.179	36.947	24.905	1.00	27.09	6	C
ATOM	1420	CD2	LEU A	186	58.210	38.384	24.491	1.00	27.26	6	C
ATOM	1421	C	LEU A	186	60.626	34.776	24.510	1.00	26.39	6	C
ATOM	1422	O	LEU A	186	61.553	35.200	25.272	1.00	26.22	8	O
ATOM	1423	N	THR A	187	60.424	33.463	24.363	1.00	24.66	7	N
ATOM	1424	CA	THR A	187	61.294	32.450	24.874	1.00	26.73	6	C
ATOM	1425	CB	THR A	187	60.902	30.977	24.565	1.00	25.80	6	C
ATOM	1426	OG1	THR A	187	60.767	30.740	23.150	1.00	26.21	8	O
ATOM	1427	CG2	THR A	187	59.607	30.774	25.365	1.00	25.53	6	C
ATOM	1428	C	THR A	187	62.747	32.613	24.398	1.00	28.97	6	C
ATOM	1429	O	THR A	187	63.725	32.170	25.010	1.00	28.90	8	O
ATOM	1430	N	ALA A	188	62.893	33.071	23.141	1.00	27.15	7	N
ATOM	1431	CA	ALA A	188	64.179	33.247	22.547	1.00	28.24	6	C
ATOM	1432	CB	ALA A	188	64.013	33.638	21.079	1.00	26.69	6	C
ATOM	1433	C	ALA A	188	64.929	34.392	23.276	1.00	26.56	6	C
ATOM	1434	O	ALA A	188	66.085	34.131	23.538	1.00	31.03	8	O
ATOM	1435	N	ILE A	189	64.247	35.480	23.520	1.00	28.59	7	N
ATOM	1436	CA	ILE A	189	64.847	36.681	24.089	1.00	31.95	6	C
ATOM	1437	CB	ILE A	189	63.944	37.886	23.862	1.00	34.61	6	C
ATOM	1438	CG2	ILE A	189	64.349	39.093	24.682	1.00	39.21	6	C
ATOM	1439	CG1	ILE A	189	63.972	38.315	22.366	1.00	35.95	6	C
ATOM	1440	CD1	ILE A	189	62.719	39.074	22.016	1.00	38.04	6	C
ATOM	1441	C	ILE A	189	65.027	36.539	25.602	1.00	33.11	6	C
ATOM	1442	O	ILE A	189	65.931	37.189	26.149	1.00	33.25	8	O
ATOM	1443	N	TRP A	190	64.171	35.748	26.225	1.00	29.51	7	N
ATOM	1444	CA	TRP A	190	64.323	35.624	27.681	1.00	31.44	6	C
ATOM	1445	CB	TRP A	190	63.025	35.600	28.489	1.00	28.21	6	C
ATOM	1446	CG	TRP A	190	62.310	36.907	28.440	1.00	27.33	6	C
ATOM	1447	CD2	TRP A	190	60.897	37.076	28.507	1.00	27.98	6	C
ATOM	1448	CE2	TRP A	190	60.647	38.462	28.418	1.00	27.50	6	C
ATOM	1449	CE3	TRP A	190	59.830	36.184	28.630	1.00	27.50	6	C
ATOM	1450	CD1	TRP A	190	62.867	38.144	28.327	1.00	26.66	6	C
ATOM	1451	NE1	TRP A	190	61.878	39.064	28.289	1.00	27.63	7	N
ATOM	1452	CZ2	TRP A	190	59.347	38.977	28.443	1.00	26.20	6	C
ATOM	1453	CZ3	TRP A	190	58.557	36.687	28.654	1.00	24.89	6	C
ATOM	1454	CH2	TRP A	190	58.305	38.088	28.574	1.00	27.33	6	C
ATOM	1455	C	TRP A	190	64.964	34.324	28.037	1.00	30.14	6	C
ATOM	1456	O	TRP A	190	64.989	34.026	29.228	1.00	35.07	8	O
ATOM	1457	N	ASN A	191	65.413	33.530	27.127	1.00	32.14	7	N
ATOM	1458	CA	ASN A	191	65.949	32.197	27.148	1.00	35.02	6	C
ATOM	1459	CB	ASN A	191	67.447	32.173	26.994	1.00	40.16	6	C
ATOM	1460	CG	ASN A	191	68.181	30.939	27.415	1.00	39.38	6	C
ATOM	1461	OD1	ASN A	191	68.376	29.912	26.770	1.00	39.89	8	O
ATOM	1462	ND2	ASN A	191	68.617	31.096	28.668	1.00	42.80	7	N
ATOM	1463	C	ASN A	191	65.394	31.348	28.296	1.00	36.01	6	C
ATOM	1464	O	ASN A	191	66.044	30.562	29.017	1.00	37.38	8	O
ATOM	1465	N	CYS A	192	64.077	31.238	28.285	1.00	33.47	7	N
ATOM	1466	CA	CYS A	192	63.273	30.556	29.261	1.00	33.13	6	C
ATOM	1467	CB	CYS A	192	62.363	31.601	29.929	1.00	32.53	6	C
ATOM	1468	SG	CYS A	192	61.228	32.491	28.808	1.00	25.76	16	S
ATOM	1469	C	CYS A	192	62.384	29.475	28.667	1.00	33.65	6	C
ATOM	1470	O	CYS A	192	61.907	29.549	27.538	1.00	34.06	8	O
ATOM	1471	N	PRO A	193	62.029	28.528	29.523	1.00	31.85	7	N
ATOM	1472	CD	PRO A	193	62.530	28.367	30.923	1.00	30.41	6	C
ATOM	1473	CA	PRO A	193	61.089	27.478	29.133	1.00	28.79	6	C
ATOM	1474	CB	PRO A	193	60.922	26.700	30.436	1.00	30.28	6	C
ATOM	1475	CG	PRO A	193	62.243	26.878	31.120	1.00	32.19	6	C
ATOM	1476	C	PRO A	193	59.772	28.075	28.758	1.00	24.94	6	C
ATOM	1477	O	PRO A	193	59.584	29.190	29.295	1.00	26.27	8	o
ATOM	1478	N	ASN A	194	58.818	27.503	28.041	1.00	24.49	7	N
ATOM	1479	CA	ASN A	194	57.543	28.193	27.783	1.00	22.29	6	C
ATOM	1480	CB	ASN A	194	56.639	27.220	26.981	1.00	23.65	6	C
ATOM	1481	CG	ASN A	194	57.209	26.860	25.645	1.00	25.45	6	C
ATOM	1482	OD1	ASN A	194	58.241	27.362	25.152	1.00	24.24	8	O
ATOM	1483	ND2	ASN A	194	56.595	25.963	24.866	1.00	25.09	7	N
ATOM	1484	C	ASN A	194	56.761	28.713	28.962	1.00	20.12	6	C
ATOM	1485	O	ASN A	194	56.085	29.766	28.913	1.00	22.50	8	O
ATOM	1486	N	GLY A	195	56.753	28.011	30.073	1.00	26.62	7	N
ATOM	1487	CA	GLY A	195	56.115	28.289	31.322	1.00	26.43	6	C
ATOM	1488	C	GLY A	195	56.409	29.630	31.936	1.00	27.31	6	C
ATOM	1489	O	GLY A	195	55.527	30.281	32.463	1.00	26.30	8	O
ATOM	1490	N	GLU A	196	57.616	30.224	31.676	1.00	28.17	7	N
ATOM	1491	CA	GLU A	196	57.902	31.569	32.142	1.00	27.07	6	C
ATOM	1492	CB	GLU A	196	59.360	31.933	31.762	1.00	28.03	6	C
ATOM	1493	CG	GLU A	196	59.778	33.384	31.953	1.00	28.94	6	C
ATOM	1494	CD	GLU A	196	59.723	33.969	33.355	1.00	31.47	6	C
ATOM	1495	OE1	GLU A	196	59.755	33.248	34.382	1.00	31.17	8	O
ATOM	1496	OE2	GLU A	196	59.549	35.189	33.512	1.00	29.20	8	O
ATOM	1497	C	GLU A	196	56.956	32.613	31.682	1.00	24.33	6	C
ATOM	1498	O	GLU A	196	56.440	33.536	32.295	1.00	23.08	8	O
ATOM	1499	N	LEU A	197	56.452	32.441	30.398	1.00	26.15	7	N
ATOM	1500	CA	LEU A	197	55.581	33.376	29.747	1.00	27.39	6	C
ATOM	1501	CB	LEU A	197	55.341	33.039	28.289	1.00	26.19	6	C
ATOM	1502	CG	LEU A	197	56.482	33.342	27.303	1.00	25.11	6	C
ATOM	1503	CD1	LEU A	197	57.837	32.764	27.722	1.00	21.88	6	C
ATOM	1504	CD2	LEU A	197	56.103	32.760	25.920	1.00	23.70	6	C
ATOM	1505	C	LEU A	197	54.305	33.604	30.558	1.00	30.74	6	C
ATOM	1506	O	LEU A	197	54.011	34.819	30.477	1.00	33.28	8	O
ATOM	1507	N	ARG A	198	53.866	32.621	31.328	1.00	33.73	7	N
ATOM	1508	CA	ARG A	198	52.703	32.702	32.172	1.00	38.60	6	C
ATOM	1509	CB	ARG A	198	52.508	31.396	32.969	1.00	41.00	6	C
ATOM	1510	CG	ARG A	198	53.453	31.254	34.140	1.00	46.30	6	C
ATOM	1511	CD	ARG A	198	53.449	29.998	34.986	1.00	48.19	6	C
ATOM	1512	NE	ARG A	198	53.367	28.801	34.144	1.00	49.91	7	N
ATOM	1513	CZ	ARG A	198	52.239	28.126	33.953	1.00	52.06	6	C
ATOM	1514	NH1	ARG A	198	51.165	28.574	34.606	1.00	52.69	7	N
ATOM	1515	NH2	ARG A	198	52.154	27.056	33.193	1.00	51.48	7	N
ATOM	1516	C	ARG A	198	52.817	33.918	33.076	1.00	40.25	6	C
ATOM	1517	O	ARG A	198	51.839	34.645	33.277	1.00	38.34	8	O
ATOM	1518	N	HIS A	199	54.021	34.249	33.533	1.00	41.34	7	N
ATOM	1519	CA	HIS A	199	54.308	35.402	34.359	1.00	43.94	6	C
ATOM	1520	CB	HIS A	199	55.692	35.267	35.029	1.00	43.20	6	C
ATOM	1521	CG	HIS A	199	55.815	34.020	35.831	1.00	43.20	6	C
ATOM	1522	CD2	HIS A	199	56.564	32.901	35.729	1.00	42.22	6	C
ATOM	1523	ND1	HIS A	199	55.057	33.870	36.986	1.00	43.41	7	N
ATOM	1524	CE1	HIS A	199	55.342	32.717	37.532	1.00	41.35	6	C
ATOM	1525	NE2	HIS A	199	56.240	32.097	36.805	1.00	41.60	7	N
ATOM	1526	C	HIS A	199	54.292	36.727	33.611	1.00	46.20	6	C
ATOM	1527	O	HIS A	199	54.665	37.738	34.229	1.00	45.70	8	O
ATOM	1528	N	HIS A	200	53.885	36.816	32.353	1.00	45.71	7	N
ATOM	1529	CA	HIS A	200	53.824	38.027	31.563	1.00	46.94	6	C
ATOM	1530	CB	HIS A	200	55.011	38.096	30.590	1.00	43.85	6	C
ATOM	1531	CG	HIS A	200	56.349	38.102	31.246	1.00	41.89	6	C
ATOM	1532	CD2	HIS A	200	57.101	39.133	31.714	1.00	39.90	6	C
ATOM	1533	ND1	HIS A	200	57.051	36.937	31.486	1.00	39.39	7	N
ATOM	1534	CE1	HIS A	200	58.192	37.261	32.053	1.00	38.66	6	C
ATOM	1535	NE2	HIS A	200	58.250	38.565	32.187	1.00	38.30	7	N
ATOM	1536	C	HIS A	200	52.557	38.177	30.723	1.00	49.59	6	C
ATOM	1537	O	HIS A	200	52.552	38.374	29.495	1.00	49.25	8	O
ATOM	1538	N	PRO A	201	51.409	38.252	31.382	1.00	51.21	7	N
ATOM	1539	CD	PRO A	201	51.220	38.097	32.843	1.00	51.88	6	C
ATOM	1540	CA	PRO A	201	50.131	38.391	30.715	1.00	51.97	6	C
ATOM	1541	CB	PRO A	201	49.093	38.248	31.833	1.00	52.67	6	C
ATOM	1542	CG	PRO A	201	49.850	38.692	33.042	1.00	52.12	6	C
ATOM	1543	C	PRO A	201	49.932	39.702	29.989	1.00	51.85	6	C
ATOM	1544	O	PRO A	201	49.500	39.678	28.836	1.00	52.23	8	O
ATOM	1545	N	GLN A	202	50.223	40.839	30.618	1.00	52.04	7	N
ATOM	1546	CA	GLN A	202	49.956	42.117	29.973	1.00	51.98	6	C
ATOM	1547	C	GLN A	202	50.650	42.302	28.629	1.00	49.40	6	C
ATOM	1548	O	GLN A	202	50.015	42.725	27.657	1.00	48.97	8	O
ATOM	1549	CB	GLN A	202	50.327	43.269	30.909	1.00	54.78	6	C
ATOM	1550	CG	GLN A	202	49.300	43.490	32.015	1.00	57.14	6	C
ATOM	1551	CD	GLN A	202	49.431	44.907	32.561	1.00	58.39	6	C
ATOM	1552	OE1	GLN A	202	50.506	45.509	32.561	1.00	59.46	8	O
ATOM	1553	NE2	GLN A	202	48.310	45.452	33.008	1.00	58.40	7	N
ATOM	1554	N	GLU A	203	51.930	41.983	28.568	1.00	46.29	7	N
ATOM	1555	CA	GLU A	203	52.768	42.017	27.394	1.00	45.75	6	C
ATOM	1556	CB	GLU A	203	54.174	41.552	27.780	1.00	48.61	6	C
ATOM	1557	CG	GLU A	203	55.309	42.104	26.940	1.00	55.35	6	C
ATOM	1558	CD	GLU A	203	56.559	41.243	27.111	1.00	58.68	6	C
ATOM	1559	OE1	GLU A	203	56.364	40.011	26.928	1.00	60.64	8	O
ATOM	1560	OE2	GLU A	203	57.654	41.760	27.413	1.00	60.48	8	O
ATOM	1561	C	GLU A	203	52.298	41.077	26.267	1.00	42.01	6	C
ATOM	1562	O	GLU A	203	52.351	41.439	25.102	1.00	36.83	8	O
ATOM	1563	N	ILE A	204	51.887	39.875	26.653	1.00	37.26	7	N
ATOM	1564	CA	ILE A	204	51.375	38.902	25.672	1.00	34.86	6	C
ATOM	1565	CB	ILE A	204	51.125	37.516	26.295	1.00	33.38	6	C
ATOM	1566	CG2	ILE A	204	50.235	36.647	25.414	1.00	32.50	6	C
ATOM	1567	CG1	ILE A	204	52.491	36.837	26.506	1.00	32.44	6	C
ATOM	1568	CD1	ILE A	204	52.526	35.510	27.199	1.00	33.69	6	C
ATOM	1569	C	ILE A	204	50.150	39.478	24.998	1.00	35.79	6	C
ATOM	1570	O	ILE A	204	49.942	39.318	23.783	1.00	33.96	8	O
ATOM	1571	N	MET A	205	49.292	40.164	25.762	1.00	36.04	7	N
ATOM	1572	CA	MET A	205	48.109	40.787	25.173	1.00	39.85	6	C
ATOM	1573	CB	MET A	205	47.299	41.516	26.258	1.00	42.17	6	C
ATOM	1574	CG	MET A	205	45.870	41.037	26.363	1.00	45.40	6	C
ATOM	1575	SD	MET A	205	44.877	41.345	24.930	1.00	49.73	16	S
ATOM	1576	CE	MET A	205	45.097	39.901	23.971	1.00	49.33	6	C
ATOM	1577	C	MET A	205	48.503	41.781	24.084	1.00	38.13	6	C
ATOM	1578	O	MET A	205	47.869	41.802	23.039	1.00	39.53	8	O
ATOM	1579	N	GLN A	206	49.485	42.626	24.339	1.00	39.17	7	N
ATOM	1580	CA	GLN A	206	49.938	43.628	23.385	1.00	38.73	6	C
ATOM	1581	CB	GLN A	206	51.053	44.495	23.943	1.00	43.09	6	C
ATOM	1582	CG	GLN A	206	50.545	45.751	24.654	1.00	47.58	6	C
ATOM	1583	CD	GLN A	206	51.648	46.364	25.504	1.00	50.94	6	C
ATOM	1584	OE1	GLN A	206	52.392	47.242	25.045	1.00	52.20	8	O
ATOM	1585	NE2	GLN A	206	51.705	45.838	26.727	1.00	51.79	7	N
ATOM	1586	C	GLN A	206	50.381	42.967	22.071	1.00	37.79	6	C
ATOM	1587	O	GLN A	206	50.020	43.460	20.994	1.00	34.91	8	O
ATOM	1588	N	ILE A	207	51.161	41.881	22.205	1.00	34.29	7	N
ATOM	1589	CA	ILE A	207	51.554	41.174	20.954	1.00	33.32	6	C
ATOM	1590	CB	ILE A	207	52.526	40.022	21.276	1.00	31.81	6	C
ATOM	1591	CG2	ILE A	207	52.959	39.225	20.063	1.00	30.02	6	C
ATOM	1592	CG1	ILE A	207	53.737	40.617	22.003	1.00	30.60	6	C
ATOM	1593	CD1	ILE A	207	54.741	39.688	22.591	1.00	30.71	6	C
ATOM	1594	C	ILE A	207	50.325	40.619	20.281	1.00	32.72	6	C
ATOM	1595	O	ILE A	207	50.164	40.781	19.061	1.00	30.79	8	O
ATOM	1596	N	CYS A	208	49.415	39.982	21.055	1.00	30.93	7	N
ATOM	1597	CA	CYS A	208	48.215	39.426	20.459	1.00	32.17	6	C
ATOM	1598	CB	CYS A	208	47.373	38.602	21.471	1.00	30.26	6	C
ATOM	1599	SG	CYS A	208	48.207	37.141	22.108	1.00	28.13	16	S
ATOM	1600	C	CYS A	208	47.320	40.478	19.819	1.00	32.96	6	C
ATOM	1601	O	CYS A	208	46.643	40.223	18.835	1.00	32.33	8	O
ATOM	1602	N	GLU A	209	47.354	41.704	20.343	1.00	37.50	7	N
ATOM	1603	CA	GLU A	209	46.513	42.755	19.746	1.00	39.18	6	C
ATOM	1604	CB	GLU A	209	46.468	43.983	20.661	1.00	44.01	6	C
ATOM	1605	CG	GLU A	209	45.045	44.528	20.829	1.00	48.18	6	C
ATOM	1606	CD	GLU A	209	44.773	44.945	22.260	1.00	50.80	6	C
ATOM	1607	OE1	GLU A	209	45.611	45.671	22.845	1.00	53.20	8	O
ATOM	1608	OE2	GLU A	209	43.739	44.572	22.853	1.00	52.38	8	O
ATOM	1609	C	GLU A	209	47.042	43.114	18.364	1.00	37.08	6	C
ATOM	1610	O	GLU A	209	46.283	43.325	17.432	1.00	36.61	8	O
ATOM	1611	N	GLU A	210	48.364	43.119	18.206	1.00	35.73	7	N
ATOM	1612	CA	GLU A	210	49.001	43.407	16.932	1.00	33.99	6	C
ATOM	1613	CB	GLU A	210	50.500	43.623	17.066	1.00	36.31	6	C
ATOM	1614	CG	GLU A	210	50.947	44.920	17.709	1.00	37.10	6	C
ATOM	1615	CD	GLU A	210	52.408	45.056	17.955	1.00	39.26	6	C
ATOM	1616	OE1	GLU A	210	53.241	44.246	17.452	1.00	38.74	8	O
ATOM	1617	OE2	GLU A	210	52.864	46.010	18.660	1.00	39.33	8	O
ATOM	1618	C	GLU A	210	48.755	42.266	15.938	1.00	33.60	6	C
ATOM	1619	O	GLU A	210	48.447	42.526	14.771	1.00	31.24	8	O
ATOM	1620	N	VAL A	211	48.916	41.033	16.452	1.00	32.10	7	N
ATOM	1621	CA	VAL A	211	48.694	39.871	15.581	1.00	31.23	6	C
ATOM	1622	CB	VAL A	211	49.012	38.549	16.330	1.00	28.69	6	C
ATOM	1623	CG1	VAL A	211	48.674	37.337	15.462	1.00	29.45	6	C
ATOM	1624	CG2	VAL A	211	50.462	38.551	16.759	1.00	29.65	6	C
ATOM	1625	C	VAL A	211	47.284	39.828	15.074	1.00	31.39	6	C
ATOM	1626	O	VAL A	211	46.954	39.624	13.900	1.00	32.71	8	O
ATOM	1627	N	ALA A	212	46.335	40.103	15.991	1.00	30.93	7	N
ATOM	1628	CA	ALA A	212	44.924	40.091	15.689	1.00	32.89	6	C
ATOM	1629	CB	ALA A	212	44.116	40.300	16.976	1.00	32.30	6	C
ATOM	1630	C	ALA A	212	44.571	41.155	14.659	1.00	33.48	6	C
ATOM	1631	O	ALA A	212	43.774	40.939	13.749	1.00	36.23	8	O
ATOM	1632	N	ALA A	213	45.219	42.315	14.742	1.00	35.20	7	N
ATOM	1633	CA	ALA A	213	44.954	43.392	13.785	1.00	36.38	6	C
ATOM	1634	CB	ALA A	213	45.618	44.688	14.226	1.00	37.67	6	C
ATOM	1635	C	ALA A	213	45.391	43.011	12.375	1.00	37.84	6	C
ATOM	1636	O	ALA A	213	44.650	43.316	11.430	1.00	37.96	8	O
ATOM	1637	N	VAL A	214	46.542	42.358	12.206	1.00	36.16	7	N
ATOM	1638	CA	VAL A	214	46.937	41.939	10.865	1.00	34.52	6	C
ATOM	1639	CB	VAL A	214	48.417	41.471	10.889	1.00	34.87	6	C
ATOM	1640	CG1	VAL A	214	48.877	40.966	9.532	1.00	33.28	6	C
ATOM	1641	CG2	VAL A	214	49.261	42.632	11.389	1.00	32.43	6	C
ATOM	1642	C	VAL A	214	46.084	40.831	10.294	1.00	35.47	6	C
ATOM	1643	O	VAL A	214	45.731	40.804	9.104	1.00	35.36	8	O
ATOM	1644	N	ILE A	215	45.687	39.842	11.095	1.00	35.92	7	N
ATOM	1645	CA	ILE A	215	44.914	38.693	10.645	1.00	38.92	6	C
ATOM	1646	CB	ILE A	215	44.795	37.632	11.767	1.00	40.37	6	C
ATOM	1647	CG2	ILE A	215	43.836	36.513	11.407	1.00	39.92	6	C
ATOM	1648	CG1	ILE A	215	46.226	37.114	12.086	1.00	40.26	6	C
ATOM	1649	CD1	ILE A	215	46.241	36.213	13.307	1.00	40.89	6	C
ATOM	1650	C	ILE A	215	43.513	39.061	10.191	1.00	41.16	6	C
ATOM	1651	O	ILE A	215	42.956	38.539	9.222	1.00	37.05	8	O
ATOM	1652	N	GLU A	216	42.912	39.991	10.932	1.00	45.02	7	N
ATOM	1653	CA	GLU A	216	41.560	40.454	10.614	1.00	50.87	6	C
ATOM	1654	CB	GLU A	216	41.066	41.428	11.678	1.00	54.57	6	C
ATOM	1655	CG	GLU A	216	39.570	41.689	11.610	1.00	58.44	6	C
ATOM	1656	CD	GLU A	216	38.733	40.449	11.858	1.00	61.16	6	C
ATOM	1657	OE1	GLU A	216	38.851	39.862	12.957	1.00	62.37	8	O
ATOM	1658	OE2	GLU A	216	37.953	40.055	10.964	1.00	62.50	8	O
ATOM	1659	C	GLU A	216	41.542	41.079	9.226	1.00	52.67	6	C
ATOM	1660	O	GLU A	216	40.689	40.791	8.382	1.00	51.01	8	O
ATOM	1661	N	ARG A	217	42.557	41.881	8.923	1.00	54.94	7	N
ATOM	1662	CA	ARG A	217	42.710	42.519	7.625	1.00	58.93	6	C
ATOM	1663	CB	ARG A	217	43.774	43.620	7.689	1.00	62.40	6	C
ATOM	1664	CG	ARG A	217	43.705	44.614	6.551	1.00	67.19	6	C
ATOM	1665	CD	ARG A	217	42.346	45.264	6.377	1.00	70.69	6	C
ATOM	1666	NE	ARG A	217	42.021	46.176	7.465	1.00	73.78	7	N
ATOM	1667	CZ	ARG A	217	42.651	47.308	7.746	1.00	75.90	6	C
ATOM	1668	NH1	ARG A	217	43.690	47.736	7.031	1.00	76.39	7	N
ATOM	1669	NH2	ARG A	217	42.234	48.047	8.774	1.00	77.03	7	N
ATOM	1670	C	ARG A	217	43.045	41.542	6.509	1.00	59.09	6	C
ATOM	1671	O	ARG A	217	42.801	41.773	5.325	1.00	56.80	8	O
ATOM	1672	N	GLU A	218	43.568	40.370	6.868	1.00	59.09	7	N
ATOM	1673	CA	GLU A	218	43.902	39.308	5.940	1.00	59.58	6	C
ATOM	1674	CB	GLU A	218	44.945	38.373	6.556	1.00	58.99	6	C
ATOM	1675	CG	GLU A	218	46.338	38.949	6.702	1.00	58.23	6	C
ATOM	1676	CD	GLU A	218	47.133	38.977	5.425	1.00	58.08	6	C
ATOM	1677	OE1	GLU A	218	47.693	37.952	4.994	1.00	58.06	8	O
ATOM	1678	OE2	GLU A	218	47.249	40.042	4.786	1.00	57.22	8	O
ATOM	1679	C	GLU A	218	42.676	38.498	5.527	1.00	60.35	6	C
ATOM	1680	O	GLU A	218	42.747	37.690	4.603	1.00	59.78	8	O
ATOM	1681	N	GLY A	219	41.548	38.679	6.200	1.00	60.81	7	N
ATOM	1682	CA	GLY A	219	40.319	38.004	5.870	1.00	62.25	6	C
ATOM	1683	C	GLY A	219	39.855	36.916	6.810	1.00	62.90	6	C
ATOM	1684	O	GLY A	219	38.933	36.173	6.465	1.00	63.53	8	O
ATOM	1685	N	HIS A	220	40.473	36.762	7.975	1.00	63.00	7	N
ATOM	1686	CA	HIS A	220	40.100	35.726	8.925	1.00	63.21	6	C
ATOM	1687	CB	HIS A	220	41.300	34.823	9.259	1.00	62.08	6	C
ATOM	1688	CG	HIS A	220	41.892	34.220	8.019	1.00	60.36	6	C
ATOM	1689	CD2	HIS A	220	41.472	33.226	7.208	1.00	59.68	6	C
ATOM	1690	ND1	HIS A	220	43.047	34.710	7.463	1.00	59.52	7	N
ATOM	1691	CE1	HIS A	220	43.339	34.032	6.370	1.00	59.32	6	C
ATOM	1692	NE2	HIS A	220	42.393	33.127	6.194	1.00	59.69	7	N
ATOM	1693	C	HIS A	220	39.514	36.288	10.215	1.00	63.87	6	C
ATOM	1694	O	HIS A	220	39.897	37.340	10.709	1.00	63.38	8	O
ATOM	1695	N	ALA A	221	38.564	35.535	10.761	1.00	65.10	7	N
ATOM	1696	CA	ALA A	221	37.863	35.905	11.973	1.00	65.68	6	C
ATOM	1697	CB	ALA A	221	36.442	35.347	11.963	1.00	65.64	6	C
ATOM	1698	C	ALA A	221	38.579	35.419	13.229	1.00	65.76	6	C
ATOM	1699	O	ALA A	221	38.544	34.231	13.546	1.00	66.16	8	O
ATOM	1700	N	THR A	222	39.159	36.370	13.948	1.00	65.60	7	N
ATOM	1701	CA	THR A	222	39.810	36.056	15.215	1.00	65.70	6	C
ATOM	1702	CB	THR A	222	41.271	35.616	15.087	1.00	66.10	6	C
ATOM	1703	OG1	THR A	222	41.582	34.879	16.283	1.00	66.76	8	O
ATOM	1704	CG2	THR A	222	42.226	36.786	14.959	1.00	66.34	6	C
ATOM	1705	C	THR A	222	39.707	37.277	16.127	1.00	64.58	6	C
ATOM	1706	O	THR A	222	39.414	38.381	15.662	1.00	65.05	8	O
ATOM	1707	N	SER A	223	39.953	37.082	17.405	1.00	62.62	7	N
ATOM	1708	CA	SER A	223	39.903	38.169	18.371	1.00	61.43	6	C
ATOM	1709	CB	SER A	223	38.750	37.955	19.352	1.00	61.09	6	C
ATOM	1710	OG	SER A	223	39.155	38.211	20.686	1.00	61.49	8	O
ATOM	1711	C	SER A	223	41.218	38.209	19.140	1.00	59.63	6	C
ATOM	1712	O	SER A	223	41.780	37.151	19.418	1.00	58.18	8	O
ATOM	1713	N	ALA A	224	41.634	39.397	19.566	1.00	58.25	7	N
ATOM	1714	CA	ALA A	224	42.870	39.497	20.337	1.00	57.60	6	C
ATOM	1715	CB	ALA A	224	43.258	40.929	20.651	1.00	57.58	6	C
ATOM	1716	C	ALA A	224	42.751	38.698	21.631	1.00	57.36	6	C
ATOM	1717	O	ALA A	224	43.704	38.040	22.054	1.00	55.22	8	O
ATOM	1718	N	GLU A	225	41.588	38.814	22.279	1.00	57.66	7	N
ATOM	1719	CA	GLU A	225	41.351	38.117	23.535	1.00	57.65	6	C
ATOM	1720	CB	GLU A	225	40.036	38.601	24.170	1.00	61.33	6	C
ATOM	1721	CG	GLU A	225	40.181	40.010	24.737	1.00	65.19	6	C
ATOM	1722	CD	GLU A	225	38.971	40.424	25.558	1.00	66.72	6	C
ATOM	1723	OE1	GLU A	225	38.685	39.763	26.572	1.00	67.70	8	O
ATOM	1724	OE2	GLU A	225	38.379	41.456	25.193	1.00	68.14	8	O
ATOM	1725	C	GLU A	225	41.334	36.610	23.361	1.00	54.22	6	C
ATOM	1726	O	GLU A	225	41.935	35.882	24.153	1.00	53.30	8	O
ATOM	1727	N	ASP A	226	40.657	36.144	22.315	1.00	50.88	7	N
ATOM	1728	CA	ASP A	226	40.547	34.718	22.030	1.00	46.63	6	C
ATOM	1729	CB	ASP A	226	39.654	34.428	20.835	1.00	48.51	6	C
ATOM	1730	CG	ASP A	226	38.182	34.727	21.070	1.00	50.00	6	C
ATOM	1731	OD1	ASP A	226	37.416	34.660	20.086	1.00	50.52	8	O
ATOM	1732	OD2	ASP A	226	37.820	35.044	22.210	1.00	50.96	8	O
ATOM	1733	C	ASP A	226	41.940	34.128	21.786	1.00	42.46	6	C
ATOM	1734	O	ASP A	226	42.332	33.087	22.324	1.00	39.02	8	O
ATOM	1735	N	LEU A	227	42.688	34.893	20.989	1.00	36.79	7	N
ATOM	1736	CA	LEU A	227	44.063	34.517	20.676	1.00	32.81	6	C
ATOM	1737	CB	LEU A	227	44.718	35.456	19.657	1.00	30.59	6	C
ATOM	1738	CG	LEU A	227	46.223	35.297	19.500	1.00	32.42	6	C
ATOM	1739	CD1	LEU A	227	46.555	33.852	19.107	1.00	31.07	6	C
ATOM	1740	CD2	LEU A	227	46.810	36.242	18.453	1.00	33.85	6	C
ATOM	1741	C	LEU A	227	44.910	34.486	21.937	1.00	29.60	6	C
ATOM	1742	O	LEU A	227	45.705	33.590	22.175	1.00	26.35	8	O
ATOM	1743	N	ARG A	228	44.694	35.466	22.846	1.00	30.78	7	N
ATOM	1744	CA	ARG A	228	45.458	35.523	24.084	1.00	31.06	6	C
ATOM	1745	CB	ARG A	228	45.124	36.799	24.862	1.00	33.22	6	C
ATOM	1746	CG	ARG A	228	45.941	37.033	26.124	1.00	34.67	6	C
ATOM	1747	CD	ARG A	228	45.273	36.387	27.333	1.00	38.78	6	C
ATOM	1748	NE	ARG A	228	43.824	36.507	27.313	1.00	40.70	7	N
ATOM	1749	CZ	ARG A	228	43.096	37.614	27.406	1.00	42.92	6	C
ATOM	1750	NH1	ARG A	228	43.596	38.832	27.521	1.00	44.40	7	N
ATOM	1751	NH2	ARG A	228	41.769	37.634	27.364	1.00	42.41	7	N
ATOM	1752	C	ARG A	228	45.157	34.315	24.971	1.00	30.66	6	C
ATOM	1753	O	ARG A	228	46.056	33.661	25.513	1.00	28.39	8	O
ATOM	1754	N	ASP A	229	43.881	34.006	25.096	1.00	31.66	7	N
ATOM	1755	CA	ASP A	229	43.449	32.873	25.930	1.00	31.43	6	C
ATOM	1756	CB	ASP A	229	41.932	32.799	25.970	1.00	35.87	6	C
ATOM	1757	CG	ASP A	229	41.328	33.930	26.796	1.00	38.05	6	C
ATOM	1758	OD1	ASP A	229	42.051	34.551	27.586	1.00	38.95	8	O
ATOM	1759	OD2	ASP A	229	40.118	34.107	26.571	1.00	40.48	8	O
ATOM	1760	C	ASP A	229	44.024	31.539	25.469	1.00	29.42	6	C
ATOM	1761	O	ASP A	229	44.449	30.702	26.273	1.00	26.73	8	O
ATOM	1762	N	TYR A	230	44.028	31.367	24.145	1.00	28.87	7	N
ATOM	1763	CA	TYR A	230	44.583	30.145	23.557	1.00	27.46	6	C
ATOM	1764	CB	TYR A	230	44.178	30.105	22.067	1.00	29.58	6	C
ATOM	1765	CG	TYR A	230	44.676	28.861	21.352	1.00	30.96	6	C
ATOM	1766	CD1	TYR A	230	44.383	27.603	21.830	1.00	33.87	6	C
ATOM	1767	CE1	TYR A	230	44.844	26.453	21.197	1.00	35.06	6	C
ATOM	1768	CD2	TYR A	230	45.437	28.928	20.182	1.00	34.27	6	C
ATOM	1769	CE2	TYR A	230	45.910	27.791	19.542	1.00	35.29	6	C
ATOM	1770	CZ	TYR A	230	45.598	26.551	20.054	1.00	36.17	6	C
ATOM	1771	OH	TYR A	230	46.018	25.375	19.458	1.00	36.87	8	O
ATOM	1772	C	TYR A	230	46.068	30.008	23.770	1.00	25.36	6	C
ATOM	1773	O	TYR A	230	46.579	28.972	24.171	1.00	24.45	8	O
ATOM	1774	N	VAL A	231	46.864	31.093	23.582	1.00	24.69	7	N
ATOM	1775	CA	VAL A	231	48.288	31.093	23.792	1.00	24.36	6	C
ATOM	1776	CB	VAL A	231	48.909	32.484	23.465	1.00	26.19	6	C
ATOM	1777	CG1	VAL A	231	50.342	32.558	23.970	1.00	27.75	6	C
ATOM	1778	CG2	VAL A	231	48.845	32.821	21.984	1.00	25.64	6	C
ATOM	1779	C	VAL A	231	48.617	30.727	25.227	1.00	23.15	6	C
ATOM	1780	O	VAL A	231	49.504	29.906	25.504	1.00	23.27	8	O
ATOM	1781	N	MET A	232	47.839	31.324	26.138	1.00	24.47	7	N
ATOM	1782	CA	MET A	232	48.097	30.982	27.566	1.00	28.80	6	C
ATOM	1783	CB	MET A	232	47.237	31.909	28.423	1.00	33.07	6	C
ATOM	1784	CG	MET A	232	47.804	33.350	28.394	1.00	36.34	6	C
ATOM	1785	SD	MET A	232	49.573	33.379	28.672	1.00	38.34	16	S
ATOM	1786	CE	MET A	232	49.643	33.480	30.463	1.00	38.38	6	C
ATOM	1787	C	MET A	232	47.830	29.504	27.869	1.00	26.80	6	C
ATOM	1788	O	MET A	232	48.488	28.805	28.646	1.00	26.62	8	O
ATOM	1789	N	GLN A	233	46.820	28.949	27.187	1.00	25.29	7	N
ATOM	1790	CA	GLN A	233	46.476	27.519	27.342	1.00	25.62	6	C
ATOM	1791	CB	GLN A	233	45.130	27.188	26.740	1.00	26.45	6	C
ATOM	1792	CG	GLN A	233	43.924	27.908	27.335	1.00	28.74	6	C
ATOM	1793	CD	GLN A	233	42.654	27.817	26.515	1.00	31.11	6	C
ATOM	1794	OE1	GLN A	233	42.626	27.978	25.296	1.00	32.14	8	O
ATOM	1795	NE2	GLN A	233	41.494	27.554	27.138	1.00	32.03	7	N
ATOM	1796	C	GLN A	233	47.594	26.641	26.764	1.00	24.07	6	C
ATOM	1797	O	GLN A	233	47.926	25.640	27.391	1.00	24.21	8	O
ATOM	1798	N	VAL A	234	48.177	27.079	25.639	1.00	22.55	7	N
ATOM	1799	CA	VAL A	234	49.307	26.352	25.079	1.00	22.93	6	C
ATOM	1800	CB	VAL A	234	49.674	26.935	23.688	1.00	22.37	6	C
ATOM	1801	CG1	VAL A	234	50.994	26.335	23.240	1.00	24.31	6	C
ATOM	1802	CG2	VAL A	234	48.533	26.584	22.738	1.00	26.04	6	C
ATOM	1803	C	VAL A	234	50.499	26.439	26.021	1.00	24.00	6	C
ATOM	1804	O	VAL A	234	51.164	25.418	26.279	1.00	26.18	8	O
ATOM	1805	N	ILE A	235	50.798	27.637	26.539	1.00	26.08	7	N
ATOM	1806	CA	ILE A	235	51.901	27.821	27.489	1.00	27.11	6	C
ATOM	1807	CB	ILE A	235	52.084	29.302	27.907	1.00	27.12	6	C
ATOM	1808	CG2	ILE A	235	53.080	29.686	28.995	1.00	29.21	6	C
ATOM	1809	CG1	ILE A	235	52.547	30.035	26.603	1.00	26.70	6	C
ATOM	1810	CD1	ILE A	235	52.251	31.528	26.798	1.00	28.09	6	C
ATOM	1811	C	ILE A	235	51.883	26.998	28.772	1.00	29.93	6	C
ATOM	1812	O	ILE A	235	53.011	26.717	29.254	1.00	35.76	8	O
ATOM	1813	N	ASP A	236	50.676	26.703	29.262	1.00	31.31	7	N
ATOM	1814	CA	ASP A	236	50.357	25.923	30.434	1.00	32.18	6	C
ATOM	1815	CB	ASP A	236	48.920	26.067	30.960	1.00	32.45	6	C
ATOM	1816	CG	ASP A	236	48.651	27.287	31.818	1.00	33.88	6	C
ATOM	1817	OD1	ASP A	236	49.637	27.867	32.359	1.00	33.21	8	O
ATOM	1818	OD2	ASP A	236	47.474	27.706	31.890	1.00	35.80	8	O
ATOM	1819	C	ASP A	236	50.610	24.456	30.124	1.00	31.32	6	C
ATOM	1820	O	ASP A	236	51.182	23.715	30.921	1.00	32.51	8	O
ATOM	1821	N	ALA A	237	50.158	24.043	28.941	1.00	30.15	7	N
ATOM	1822	CA	ALA A	237	50.267	22.650	28.525	1.00	29.73	6	C
ATOM	1823	CB	ALA A	237	49.270	22.352	27.405	1.00	27.85	6	C
ATOM	1824	C	ALA A	237	51.655	22.249	28.117	1.00	29.97	6	C
ATOM	1825	O	ALA A	237	52.154	21.135	28.157	1.00	31.07	8	O
ATOM	1826	N	THR A	238	52.471	23.228	27.710	1.00	28.81	7	N
ATOM	1827	CA	THR A	238	53.863	22.954	27.315	1.00	29.70	6	C
ATOM	1828	CB	THR A	238	54.171	23.445	25.879	1.00	28.72	6	C
ATOM	1829	OG1	THR A	238	53.944	24.856	25.824	1.00	28.32	8	O
ATOM	1830	CG2	THR A	238	53.366	22.701	24.827	1.00	30.64	6	C
ATOM	1831	C	THR A	238	54.873	23.646	28.228	1.00	32.30	6	C
ATOM	1832	O	THR A	238	55.970	23.995	27.791	1.00	29.50	8	O
ATOM	1833	N	ALA A	239	54.499	23.837	29.479	1.00	32.51	7	N
ATOM	1834	CA	ALA A	239	55.241	24.622	30.447	1.00	36.82	6	C
ATOM	1835	CB	ALA A	239	54.603	24.442	31.824	1.00	35.83	6	C
ATOM	1836	C	ALA A	239	56.745	24.359	30.552	1.00	37.39	6	C
ATOM	1837	O	ALA A	239	57.486	25.340	30.666	1.00	37.58	8	O
ATOM	1838	N	GLU A	240	57.113	23.105	30.560	1.00	39.92	7	N
ATOM	1839	CA	GLU A	240	58.514	22.712	30.684	1.00	43.43	6	C
ATOM	1840	CB	GLU A	240	58.590	21.376	31.436	1.00	47.51	6	C
ATOM	1841	CG	GLU A	240	58.526	21.597	32.935	1.00	52.60	6	C
ATOM	1842	CD	GLU A	240	57.130	21.783	33.484	1.00	56.58	6	C
ATOM	1843	OE1	GLU A	240	56.272	20.868	33.365	1.00	58.99	8	O
ATOM	1844	OE2	GLU A	240	56.871	22.851	34.085	1.00	58.37	8	O
ATOM	1845	C	GLU A	240	59.271	22.673	29.375	1.00	41.19	6	C
ATOM	1846	O	GLU A	240	60.492	22.782	29.438	1.00	43.22	8	O
ATOM	1847	N	ASN A	241	58.626	22.679	28.220	1.00	39.11	7	N
ATOM	1848	CA	ASN A	241	59.334	22.632	26.952	1.00	37.18	6	C
ATOM	1849	CB	ASN A	241	58.291	22.479	25.833	1.00	39.30	6	C
ATOM	1850	CG	ASN A	241	57.501	21.179	25.964	1.00	41.56	6	C
ATOM	1851	OD1	ASN A	241	56.664	21.010	25.067	1.00	41.45	8	O
ATOM	1852	ND2	ASN A	241	57.777	20.355	26.956	1.00	40.47	7	N
ATOM	1853	C	ASN A	241	60.174	23.872	26.598	1.00	33.45	6	C
ATOM	1854	O	ASN A	241	59.885	24.949	27.062	1.00	31.38	8	O
ATOM	1855	N	ILE A	242	61.135	23.598	25.737	1.00	32.31	7	N
ATOM	1856	CA	ILE A	242	61.985	24.618	25.119	1.00	32.09	6	C
ATOM	1857	CB	ILE A	242	63.458	24.173	25.081	1.00	31.78	6	C
ATOM	1858	CG2	ILE A	242	64.349	25.226	24.443	1.00	30.95	6	C
ATOM	1859	CG1	ILE A	242	63.910	23.874	26.540	1.00	31.96	6	C
ATOM	1860	CD1	ILE A	242	63.612	25.005	27.512	1.00	32.18	6	C
ATOM	1861	C	ILE A	242	61.427	24.796	23.717	1.00	30.11	6	C
ATOM	1862	O	ILE A	242	61.315	23.780	22.976	1.00	31.69	8	O
ATOM	1863	N	SER A	243	61.079	26.028	23.328	1.00	28.62	7	N
ATOM	1864	CA	SER A	243	60.516	26.217	21.990	1.00	29.16	6	C
ATOM	1865	CB	SER A	243	60.041	27.661	21.826	1.00	28.29	6	C
ATOM	1866	OG	SER A	243	61.160	28.560	21.760	1.00	26.85	8	O
ATOM	1867	C	SER A	243	61.448	25.858	20.854	1.00	28.52	6	C
ATOM	1868	O	SER A	243	62.680	25.795	20.958	1.00	28.35	8	O
ATOM	1869	N	SER A	244	60.873	25.762	19.629	1.00	26.17	7	N
ATOM	1870	CA	SER A	244	61.682	25.478	18.453	1.00	26.74	6	C
ATOM	1871	CB	SER A	244	60.878	25.251	17.163	1.00	27.44	6	C
ATOM	1872	OG	SER A	244	60.061	26.385	16.920	1.00	29.47	8	O
ATOM	1873	C	SER A	244	62.669	26.634	18.202	1.00	27.21	6	C
ATOM	1874	O	SER A	244	63.779	26.338	17.769	1.00	28.33	8	O
ATOM	1875	N	MET A	245	62.238	27.872	18.403	1.00	26.31	7	N
ATOM	1876	CA	MET A	245	63.106	29.042	18.197	1.00	22.50	6	C
ATOM	1877	CB	MET A	245	62.278	30.333	18.086	1.00	23.49	6	C
ATOM	1878	CG	MET A	245	63.175	31.469	17.467	1.00	20.17	6	C
ATOM	1879	SD	MET A	245	62.223	32.952	17.255	1.00	22.14	16	S
ATOM	1880	CE	MET A	245	61.471	32.506	15.645	1.00	20.01	6	C
ATOM	1881	C	MET A	245	64.208	29.146	19.245	1.00	29.11	6	C
ATOM	1882	O	MET A	245	65.384	29.350	18.868	1.00	29.77	8	O
ATOM	1883	N	LEU A	246	63.895	28.891	20.499	1.00	27.45	7	N
ATOM	1884	CA	LEU A	246	64.903	28.950	21.569	1.00	32.56	6	C
ATOM	1885	CB	LEU A	246	64.302	28.828	22.961	1.00	30.90	6	C
ATOM	1886	CG	LEU A	246	65.282	28.813	24.163	1.00	31.21	6	C
ATOM	1887	CD1	LEU A	246	66.323	29.931	23.993	1.00	29.92	6	C
ATOM	1888	CD2	LEU A	246	64.567	28.959	25.480	1.00	28.69	6	C
ATOM	1889	C	LEU A	246	65.919	27.846	21.313	1.00	34.75	6	C
ATOM	1890	O	LEU A	246	67.141	27.985	21.335	1.00	36.47	8	O
ATOM	1891	N	GLN A	247	65.420	26.696	20.863	1.00	35.19	7	N
ATOM	1892	CA	GLN A	247	66.256	25.568	20.503	1.00	39.33	6	C
ATOM	1893	CB	GLN A	247	65.370	24.447	19.957	1.00	43.06	6	C
ATOM	1894	CG	GLN A	247	65.911	23.064	20.267	1.00	47.74	6	C
ATOM	1895	CD	GLN A	247	64.868	22.020	19.898	1.00	49.30	6	C
ATOM	1896	OE1	GLN A	247	63.699	22.209	20.237	1.00	51.62	8	O
ATOM	1897	NE2	GLN A	247	65.271	20.975	19.205	1.00	50.76	7	N
ATOM	1898	C	GLN A	247	67.284	25.922	19.436	1.00	39.74	6	C
ATOM	1899	O	GLN A	247	68.450	25.488	19.457	1.00	40.51	8	O
ATOM	1900	N	ASP A	248	66.847	26.705	18.453	1.00	37.82	7	N
ATOM	1901	CA	ASP A	248	67.741	27.168	17.400	1.00	38.31	6	C
ATOM	1902	CB	ASP A	248	66.953	27.860	16.279	1.00	34.47	6	C
ATOM	1903	CG	ASP A	248	66.131	26.925	15.406	1.00	33.49	6	C
ATOM	1904	OD1	ASP A	248	66.521	25.763	15.172	1.00	32.56	8	O
ATOM	1905	OD2	ASP A	248	65.078	27.313	14.860	1.00	30.46	8	O
ATOM	1906	C	ASP A	248	68.770	28.112	18.041	1.00	39.62	6	C
ATOM	1907	O	ASP A	248	69.987	27.986	17.793	1.00	40.39	8	O
ATOM	1908	N	ILE A	249	68.282	29.059	18.836	1.00	39.67	7	N
ATOM	1909	CA	ILE A	249	69.146	30.030	19.502	1.00	42.53	6	C
ATOM	1910	CB	ILE A	249	68.350	30.925	20.466	1.00	42.48	6	C
ATOM	1911	CG2	ILE A	249	69.244	31.662	21.462	1.00	42.45	6	C
ATOM	1912	CG1	ILE A	249	67.435	31.896	19.718	1.00	42.13	6	C
ATOM	1913	CD1	ILE A	249	68.067	33.084	19.041	1.00	39.99	6	C
ATOM	1914	C	ILE A	249	70.241	29.311	20.289	1.00	45.30	6	C
ATOM	1915	O	ILE A	249	71.435	29.434	20.012	1.00	45.09	8	O
ATOM	1916	N	ARG A	250	69.846	28.459	21.224	1.00	46.11	7	N
ATOM	1917	CA	ARG A	250	70.777	27.714	22.059	1.00	49.58	6	C
ATOM	1918	CB	ARG A	250	70.047	26.803	23.053	1.00	48.49	6	C
ATOM	1919	CG	ARG A	250	69.221	27.551	24.082	1.00	48.25	6	C
ATOM	1920	CD	ARG A	250	68.639	26.596	25.111	1.00	48.29	6	C
ATOM	1921	NE	ARG A	250	68.097	27.322	26.264	1.00	47.22	7	N
ATOM	1922	CZ	ARG A	250	67.460	26.725	27.258	1.00	46.33	6	C
ATOM	1923	NH1	ARG A	250	66.984	27.465	28.256	1.00	46.74	7	N
ATOM	1924	NH2	ARG A	250	67.260	25.432	27.274	1.00	46.59	7	N
ATOM	1925	C	ARG A	250	71.793	26.932	21.246	1.00	51.10	6	C
ATOM	1926	O	ARG A	250	72.931	26.733	21.687	1.00	52.50	8	O
ATOM	1927	N	ALA A	251	71.468	26.476	20.043	1.00	52.45	7	N
ATOM	1928	CA	ALA A	251	72.409	25.782	19.184	1.00	52.80	6	C
ATOM	1929	CB	ALA A	251	71.678	24.660	18.460	1.00	52.47	6	C
ATOM	1930	C	ALA A	251	73.051	26.710	18.161	1.00	52.93	6	C
ATOM	1931	O	ALA A	251	73.767	26.271	17.256	1.00	52.77	8	O
ATOM	1932	N	LEU A	252	72.734	27.996	18.195	1.00	53.59	7	N
ATOM	1933	CA	LEU A	252	73.215	28.974	17.242	1.00	54.61	6	C
ATOM	1934	CB	LEU A	252	74.708	29.198	17.439	1.00	56.65	6	C
ATOM	1935	CG	LEU A	252	75.284	29.550	18.776	1.00	57.62	6	C
ATOM	1936	CD1	LEU A	252	76.693	29.114	18.901	1.00	58.39	6	C
ATOM	1937	CD2	LEU A	252	74.966	30.934	19.276	1.00	58.87	6	C
ATOM	1938	C	LEU A	252	72.931	28.556	15.792	1.00	53.74	6	C
ATOM	1939	O	LEU A	252	73.830	28.702	14.957	1.00	53.37	8	O
ATOM	1940	N	ARG A	253	71.741	28.030	15.512	1.00	51.31	7	N
ATOM	1941	CA	ARG A	253	71.390	27.688	14.137	1.00	49.13	6	C
ATOM	1942	CB	ARG A	253	70.570	26.428	13.946	1.00	51.31	6	C
ATOM	1943	CG	ARG A	253	70.845	25.223	14.806	1.00	54.01	6	C
ATOM	1944	CD	ARG A	253	69.827	24.101	14.635	1.00	56.03	6	C
ATOM	1945	NE	ARG A	253	69.626	23.295	15.827	1.00	57.53	7	N
ATOM	1946	CZ	ARG A	253	68.614	23.330	16.679	1.00	58.76	6	C
ATOM	1947	NH1	ARG A	253	67.556	24.113	16.564	1.00	59.59	7	N
ATOM	1948	NH2	ARG A	253	68.643	22.508	17.729	1.00	60.24	7	N
ATOM	1949	C	ARG A	253	70.589	28.913	13.684	1.00	45.03	6	C
ATOM	1950	O	ARG A	253	70.057	29.608	14.561	1.00	42.83	8	O
ATOM	1951	N	HIS A	254	70.542	29.180	12.388	1.00	42.19	7	N
ATOM	1952	CA	HIS A	254	69.707	30.301	11.940	1.00	38.35	6	C
ATOM	1953	CB	HIS A	254	69.702	30.407	10.426	1.00	41.95	6	C
ATOM	1954	CG	HIS A	254	70.940	30.976	9.829	1.00	46.54	6	C
ATOM	1955	CD2	HIS A	254	71.484	32.211	9.915	1.00	48.24	6	C
ATOM	1956	ND1	HIS A	254	71.789	30.249	9.023	1.00	48.43	7	N
ATOM	1957	CE1	HIS A	254	72.798	31.002	8.624	1.00	49.00	6	C
ATOM	1958	NE2	HIS A	254	72.638	32.201	9.160	1.00	49.34	7	N
ATOM	1959	C	HIS A	254	68.256	30.056	12.401	1.00	34.21	6	C
ATOM	1960	O	HIS A	254	67.912	28.876	12.490	1.00	32.74	8	O
ATOM	1961	N	THR A	255	67.459	31.088	12.650	1.00	30.00	7	N
ATOM	1962	CA	THR A	255	66.108	30.900	13.101	1.00	27.94	6	C
ATOM	1963	CB	THR A	255	65.585	31.868	14.182	1.00	24.63	6	C
ATOM	1964	OG1	THR A	255	65.252	33.118	13.631	1.00	25.36	8	O
ATOM	1965	CG2	THR A	255	66.589	31.981	15.335	1.00	25.51	6	C
ATOM	1966	C	THR A	255	65.103	31.022	11.939	1.00	27.14	6	C
ATOM	1967	O	THR A	255	65.506	31.473	10.867	1.00	26.33	8	O
ATOM	1968	N	GLU A	256	63.836	30.684	12.178	1.00	25.22	7	N
ATOM	1969	CA	GLU A	256	62.797	30.829	11.173	1.00	22.10	6	C
ATOM	1970	CB	GLU A	256	61.778	29.665	11.126	1.00	25.40	6	C
ATOM	1971	CG	GLU A	256	62.408	28.371	10.595	1.00	26.74	6	C
ATOM	1972	CD	GLU A	256	61.481	27.152	10.560	1.00	31.16	6	C
ATOM	1973	OE1	GLU A	256	61.114	26.755	9.408	1.00	28.77	8	O
ATOM	1974	OE2	GLU A	256	61.147	26.609	11.630	1.00	28.79	8	O
ATOM	1975	C	GLU A	256	62.059	32.140	11.440	1.00	22.57	6	C
ATOM	1976	O	GLU A	256	60.989	32.372	10.887	1.00	21.91	8	O
ATOM	1977	N	ILE A	257	62.642	33.052	12.215	1.00	23.68	7	N
ATOM	1978	CA	ILE A	257	61.970	34.320	12.539	1.00	22.55	6	C
ATOM	1979	CB	ILE A	257	63.077	35.100	13.327	1.00	28.11	6	C
ATOM	1980	CG2	ILE A	257	64.164	35.579	12.377	1.00	30.70	6	C
ATOM	1981	CG1	ILE A	257	62.458	36.327	13.971	1.00	32.19	6	C
ATOM	1982	CD1	ILE A	257	61.417	36.123	15.048	1.00	33.04	6	C
ATOM	1983	C	ILE A	257	61.581	35.145	11.335	1.00	19.40	6	C
ATOM	1984	O	ILE A	257	60.606	35.901	11.441	1.00	19.60	8	O
ATOM	1985	N	ASP A	258	62.279	35.076	10.179	1.00	20.73	7	N
ATOM	1986	CA	ASP A	258	61.912	35.873	9.032	1.00	20.84	6	C
ATOM	1987	CB	ASP A	258	63.044	35.747	7.984	1.00	24.46	6	C
ATOM	1988	CG	ASP A	258	64.263	36.542	8.446	1.00	26.53	6	C
ATOM	1989	OD1	ASP A	258	64.120	37.758	8.496	1.00	25.11	8	O
ATOM	1990	OD2	ASP A	258	65.256	35.868	8.711	1.00	30.20	8	O
ATOM	1991	C	ASP A	258	60.577	35.489	8.394	1.00	21.17	6	C
ATOM	1992	O	ASP A	258	59.935	36.190	7.623	1.00	22.70	8	O
ATOM	1993	N	TYR A	259	60.115	34.278	8.751	1.00	19.28	7	N
ATOM	1994	CA	TYR A	259	58.894	33.671	8.285	1.00	20.42	6	C
ATOM	1995	CB	TYR A	259	59.238	32.309	7.600	1.00	19.36	6	C
ATOM	1996	CG	TYR A	259	60.126	32.623	6.404	1.00	21.28	6	C
ATOM	1997	CD1	TYR A	259	61.493	32.659	6.538	1.00	22.25	6	C
ATOM	1998	CE1	TYR A	259	62.335	33.011	5.509	1.00	21.86	6	C
ATOM	1999	CD2	TYR A	259	59.544	32.874	5.145	1.00	21.59	6	C
ATOM	2000	CE2	TYR A	259	60.410	33.243	4.100	1.00	22.21	6	C
ATOM	2001	CZ	TYR A	259	61.756	33.315	4.286	1.00	24.74	6	C
ATOM	2002	OH	TYR A	259	62.563	33.695	3.246	1.00	23.85	8	O
ATOM	2003	C	TYR A	259	57.846	33.495	9.369	1.00	19.80	6	C
ATOM	2004	O	TYR A	259	56.850	32.765	9.251	1.00	19.43	8	O
ATOM	2005	N	ILE A	260	58.108	34.111	10.567	1.00	19.72	7	N
ATOM	2006	CA	ILE A	260	57.123	34.048	11.660	1.00	19.94	6	C
ATOM	2007	CB	ILE A	260	57.701	33.308	12.875	1.00	19.22	6	C
ATOM	2008	CG2	ILE A	260	56.679	33.215	14.015	1.00	21.48	6	C
ATOM	2009	CG1	ILE A	260	58.183	31.903	12.516	1.00	21.49	6	C
ATOM	2010	CD1	ILE A	260	58.844	31.107	13.610	1.00	22.06	6	C
ATOM	2011	C	ILE A	260	56.828	35.507	11.976	1.00	20.82	6	C
ATOM	2012	O	ILE A	260	55.928	36.023	11.294	1.00	20.92	8	O
ATOM	2013	N	ASN A	261	57.581	36.199	12.839	1.00	18.77	7	N
ATOM	2014	CA	ASN A	261	57.164	37.602	13.069	1.00	20.51	6	C
ATOM	2015	CB	ASN A	261	57.688	38.211	14.363	1.00	21.31	6	C
ATOM	2016	CG	ASN A	261	57.425	37.271	15.558	1.00	20.99	6	C
ATOM	2017	OD1	ASN A	261	58.010	36.188	15.684	1.00	19.55	8	O
ATOM	2018	ND2	ASN A	261	56.696	37.802	16.521	1.00	22.13	7	N
ATOM	2019	C	ASN A	261	57.659	38.459	11.900	1.00	19.63	6	C
ATOM	2020	O	ASN A	261	56.856	39.374	11.591	1.00	21.43	8	O
ATOM	2021	N	GLY A	262	58.651	38.027	11.168	1.00	22.52	7	N
ATOM	2022	CA	GLY A	262	59.041	38.747	9.970	1.00	21.76	6	C
ATOM	2023	C	GLY A	262	57.932	38.760	8.939	1.00	25.21	6	C
ATOM	2024	O	GLY A	262	57.704	39.789	8.268	1.00	26.10	8	O
ATOM	2025	N	PHE A	263	57.174	37.674	8.758	1.00	24.05	7	N
ATOM	2026	CA	PHE A	263	56.047	37.664	7.837	1.00	21.20	6	C
ATOM	2027	CB	PHE A	263	55.440	36.273	7.679	1.00	22.11	6	C
ATOM	2028	CG	PHE A	263	54.274	36.162	6.736	1.00	23.66	6	C
ATOM	2029	CD1	PHE A	263	54.480	36.263	5.363	1.00	25.61	6	C
ATOM	2030	CD2	PHE A	263	53.003	35.896	7.189	1.00	23.05	6	C
ATOM	2031	CE1	PHE A	263	53.407	36.105	4.494	1.00	24.77	6	C
ATOM	2032	CE2	PHE A	263	51.912	35.790	6.360	1.00	24.86	6	C
ATOM	2033	CZ	PHE A	263	52.136	35.901	4.988	1.00	24.61	6	C
ATOM	2034	C	PHE A	263	54.966	38.592	8.356	1.00	23.52	6	C
ATOM	2035	O	PHE A	263	54.272	39.266	7.597	1.00	21.50	8	O
ATOM	2036	N	LEU A	264	54.677	38.582	9.690	1.00	22.18	7	N
ATOM	2037	CA	LEU A	264	53.630	39.465	10.213	1.00	23.10	6	C
ATOM	2038	CB	LEU A	264	53.478	39.301	11.723	1.00	24.44	6	C
ATOM	2039	CG	LEU A	264	52.263	39.978	12.390	1.00	23.36	6	C
ATOM	2040	CD1	LEU A	264	50.992	39.178	12.198	1.00	24.30	6	C
ATOM	2041	CD2	LEU A	264	52.609	40.193	13.860	1.00	27.78	6	C
ATOM	2042	C	LEU A	264	53.999	40.938	9.931	1.00	24.62	6	C
ATOM	2043	O	LEU A	264	53.072	41.705	9.604	1.00	23.80	8	O
ATOM	2044	N	LEU A	265	55.266	41.253	10.094	1.00	24.78	7	N
ATOM	2045	CA	LEU A	265	55.725	42.624	9.836	1.00	27.41	6	C
ATOM	2046	CB	LEU A	265	57.222	42.731	10.060	1.00	27.68	6	C
ATOM	2047	CG	LEU A	265	57.784	42.517	11.467	1.00	29.43	6	C
ATOM	2048	CD1	LEU A	265	59.027	43.366	11.642	1.00	29.74	6	C
ATOM	2049	CD2	LEU A	265	56.809	42.878	12.582	1.00	29.36	6	C
ATOM	2050	C	LEU A	265	55.504	42.986	8.353	1.00	29.14	6	C
ATOM	2051	O	LEU A	265	55.016	44.056	8.034	1.00	29.48	8	O
ATOM	2052	N	ARG A	266	55.899	42.061	7.470	1.00	26.87	7	N
ATOM	2053	CA	ARG A	266	55.698	42.290	6.025	1.00	29.62	6	C
ATOM	2054	CB	ARG A	266	56.284	41.102	5.219	1.00	30.88	6	C
ATOM	2055	CG	ARG A	266	57.815	41.163	5.241	1.00	31.87	6	C
ATOM	2056	CD	ARG A	266	58.439	40.296	4.164	1.00	32.86	6	C
ATOM	2057	NE	ARG A	266	58.243	38.865	4.346	1.00	33.01	7	N
ATOM	2058	CZ	ARG A	266	58.864	38.032	5.200	1.00	32.19	6	C
ATOM	2059	NH1	ARG A	266	58.534	36.724	5.214	1.00	30.07	7	N
ATOM	2060	NH2	ARG A	266	59.765	38.542	6.018	1.00	30.88	7	N
ATOM	2061	C	ARG A	266	54.239	42.483	5.666	1.00	31.12	6	C
ATOM	2062	O	ARG A	266	53.880	43.441	4.971	1.00	33.66	8	O
ATOM	2063	N	ARG A	267	53.303	41.697	6.201	1.00	30.85	7	N
ATOM	2064	CA	ARG A	267	51.890	41.814	5.921	1.00	30.08	6	C
ATOM	2065	CB	ARG A	267	51.026	40.604	6.326	1.00	29.69	6	C
ATOM	2066	CG	ARG A	267	51.394	39.338	5.552	1.00	29.63	6	C
ATOM	2067	CD	ARG A	267	51.301	39.578	4.042	1.00	32.69	6	C
ATOM	2068	NE	ARG A	267	49.980	39.976	3.615	1.00	34.59	7	N
ATOM	2069	CZ	ARG A	267	49.677	40.679	2.517	1.00	36.23	6	C
ATOM	2070	NH1	ARG A	267	48.389	40.956	2.281	1.00	36.98	7	N
ATOM	2071	NH2	ARG A	267	50.549	41.110	1.613	1.00	39.16	7	N
ATOM	2072	C	ARG A	267	51.293	43.051	6.609	1.00	32.47	6	C
ATOM	2073	O	ARG A	267	50.404	43.730	6.091	1.00	31.18	8	O
ATOM	2074	N	ALA A	268	51.851	43.354	7.784	1.00	33.41	7	N
ATOM	2075	CA	ALA A	268	51.397	44.529	8.539	1.00	37.78	6	C
ATOM	2076	CB	ALA A	268	52.144	44.592	9.863	1.00	37.31	6	C
ATOM	2077	C	ALA A	268	51.691	45.801	7.731	1.00	41.15	6	C
ATOM	2078	O	ALA A	268	50.908	46.750	7.637	1.00	40.60	8	O
ATOM	2079	N	ARG A	269	52.878	45.755	7.145	1.00	43.21	7	N
ATOM	2080	CA	ARG A	269	53.408	46.776	6.286	1.00	48.62	6	C
ATOM	2081	CB	ARG A	269	54.815	46.403	5.779	1.00	51.90	6	C
ATOM	2082	CG	ARG A	269	55.391	47.625	5.043	1.00	57.13	6	C
ATOM	2083	CD	ARG A	269	55.450	48.735	6.088	1.00	60.85	6	C
ATOM	2084	NE	ARG A	269	56.189	49.909	5.724	1.00	64.02	7	N
ATOM	2085	CZ	ARG A	269	57.400	49.943	5.189	1.00	65.87	6	C
ATOM	2086	NH1	ARG A	269	58.123	48.869	4.900	1.00	66.08	7	N
ATOM	2087	NH2	ARG A	269	57.936	51.128	4.916	1.00	66.42	7	N
ATOM	2088	C	ARG A	269	52.540	46.982	5.053	1.00	49.03	6	C
ATOM	2089	O	ARG A	269	52.229	48.124	4.731	1.00	49.58	8	O
ATOM	2090	N	ALA A	270	52.101	45.906	4.426	1.00	48.94	7	N
ATOM	2091	CA	ALA A	270	51.252	45.978	3.247	1.00	50.47	6	C
ATOM	2092	CB	ALA A	270	51.201	44.606	2.586	1.00	49.60	6	C
ATOM	2093	C	ALA A	270	49.858	46.506	3.555	1.00	51.98	6	C
ATOM	2094	O	ALA A	270	49.212	47.103	2.685	1.00	50.99	8	O
ATOM	2095	N	HIS A	271	49.364	46.309	4.767	1.00	52.89	7	N
ATOM	2096	CA	HIS A	271	48.057	46.770	5.182	1.00	54.55	6	C
ATOM	2097	CB	HIS A	271	47.368	45.729	6.076	1.00	55.17	6	C
ATOM	2098	CG	HIS A	271	46.967	44.484	5.347	1.00	56.38	6	C
ATOM	2099	CD2	HIS A	271	47.371	43.198	5.448	1.00	55.91	6	C
ATOM	2100	ND1	HIS A	271	45.990	44.508	4.373	1.00	56.70	7	N
ATOM	2101	CE1	HIS A	271	45.814	43.293	3.892	1.00	57.04	6	C
ATOM	2102	NE2	HIS A	271	46.642	42.485	4.530	1.00	57.14	7	N
ATOM	2103	C	HIS A	271	48.144	48.080	5.961	1.00	55.21	6	C
ATOM	2104	O	HIS A	271	47.131	48.726	6.231	1.00	54.83	8	O
ATOM	2105	N	GLY A	272	49.351	48.449	6.355	1.00	54.60	7	N
ATOM	2106	CA	GLY A	272	49.582	49.649	7.149	1.00	55.42	6	C
ATOM	2107	C	GLY A	272	49.021	49.512	8.557	1.00	54.48	6	C
ATOM	2108	O	GLY A	272	48.128	50.261	8.954	1.00	56.08	8	O
ATOM	2109	N	ILE A	273	49.537	48.555	9.323	1.00	52.89	7	N
ATOM	2110	CA	ILE A	273	49.108	48.292	10.686	1.00	50.36	6	C
ATOM	2111	CB	ILE A	273	48.547	46.863	10.852	1.00	50.50	6	C
ATOM	2112	CG2	ILE A	273	48.292	46.533	12.315	1.00	49.35	6	C
ATOM	2113	CG1	ILE A	273	47.305	46.647	9.991	1.00	49.58	6	C
ATOM	2114	CD1	ILE A	273	46.175	47.615	10.248	1.00	49.55	6	C
ATOM	2115	C	ILE A	273	50.274	48.472	11.644	1.00	49.24	6	C
ATOM	2116	O	ILE A	273	51.372	47.968	11.372	1.00	49.40	8	O
ATOM	2117	N	ALA A	274	50.072	49.174	12.745	1.00	47.44	7	N
ATOM	2118	CA	ALA A	274	51.137	49.409	13.711	1.00	44.91	6	C
ATOM	2119	CB	ALA A	274	50.640	50.426	14.733	1.00	46.11	6	C
ATOM	2120	C	ALA A	274	51.558	48.127	14.409	1.00	44.18	6	C
ATOM	2121	O	ALA A	274	50.756	47.475	15.057	1.00	42.49	8	O
ATOM	2122	N	VAL A	275	52.845	47.773	14.328	1.00	42.23	7	N
ATOM	2123	CA	VAL A	275	53.330	46.575	15.019	1.00	41.70	6	C
ATOM	2124	CB	VAL A	275	53.374	45.397	14.027	1.00	41.14	6	C
ATOM	2125	CG1	VAL A	275	52.021	44.784	13.716	1.00	39.29	6	C
ATOM	2126	CG2	VAL A	275	54.052	45.839	12.731	1.00	41.40	6	C
ATOM	2127	C	VAL A	275	54.648	46.796	15.732	1.00	40.65	6	C
ATOM	2128	O	VAL A	275	55.694	46.177	15.518	1.00	39.82	8	O
ATOM	2129	N	PRO A	276	54.650	47.682	16.749	1.00	40.69	7	N
ATOM	2130	CD	PRO A	276	53.528	48.537	17.188	1.00	40.98	6	C
ATOM	2131	CA	PRO A	276	55.862	48.028	17.466	1.00	39.58	6	C
ATOM	2132	CB	PRO A	276	55.483	49.298	18.235	1.00	39.57	6	C
ATOM	2133	CG	PRO A	276	54.027	49.103	18.522	1.00	39.75	6	C
ATOM	2134	C	PRO A	276	56.427	46.930	18.335	1.00	38.04	6	C
ATOM	2135	O	PRO A	276	57.654	46.789	18.332	1.00	38.45	8	O
ATOM	2136	N	GLU A	277	55.584	46.177	19.033	1.00	35.64	7	N
ATOM	2137	CA	GLU A	277	56.088	45.083	19.873	1.00	34.74	6	C
ATOM	2138	CB	GLU A	277	54.980	44.499	20.733	1.00	35.92	6	C
ATOM	2139	CG	GLU A	277	54.156	45.470	21.552	1.00	40.50	6	C
ATOM	2140	CD	GLU A	277	55.030	46.419	22.349	1.00	42.93	6	C
ATOM	2141	OE1	GLU A	277	56.117	46.052	22.843	1.00	43.29	8	O
ATOM	2142	OE2	GLU A	277	54.597	47.586	22.488	1.00	45.14	8	O
ATOM	2143	C	GLU A	277	56.692	43.992	18.996	1.00	29.74	6	C
ATOM	2144	O	GLU A	277	57.754	43.483	19.329	1.00	29.09	8	O
ATOM	2145	N	ASN A	278	55.964	43.624	17.941	1.00	31.27	7	N
ATOM	2146	CA	ASN A	278	56.509	42.599	17.005	1.00	29.44	6	C
ATOM	2147	CB	ASN A	278	55.378	42.277	15.999	1.00	28.98	6	C
ATOM	2148	CG	ASN A	278	54.446	41.209	16.554	1.00	30.11	6	C
ATOM	2149	OD1	ASN A	278	54.835	40.018	16.559	1.00	29.75	8	O
ATOM	2150	ND2	ASN A	278	53.256	41.547	17.009	1.00	27.06	7	N
ATOM	2151	C	ASN A	278	57.784	43.018	16.304	1.00	29.12	6	C
ATOM	2152	O	ASN A	278	58.769	42.245	16.175	1.00	29.06	8	O
ATOM	2153	N	THR A	279	57.903	44.290	15.912	1.00	29.75	7	N
ATOM	2154	CA	THR A	279	59.150	44.803	15.340	1.00	32.13	6	C
ATOM	2155	CB	THR A	279	58.957	46.188	14.698	1.00	34.38	6	C
ATOM	2156	OG1	THR A	279	58.462	47.117	15.677	1.00	38.52	8	O
ATOM	2157	CG2	THR A	279	57.911	46.153	13.591	1.00	33.74	6	C
ATOM	2158	C	THR A	279	60.299	44.775	16.332	1.00	30.10	6	C
ATOM	2159	O	THR A	279	61.374	44.206	16.112	1.00	29.36	8	O
ATOM	2160	N	ARG A	280	60.079	45.255	17.577	1.00	31.39	7	N
ATOM	2161	CA	ARG A	280	61.139	45.156	18.581	1.00	32.07	6	C
ATOM	2162	CB	ARG A	280	60.647	45.698	19.939	1.00	34.98	6	C
ATOM	2163	CG	ARG A	280	61.710	45.630	21.024	1.00	39.35	6	C
ATOM	2164	CD	ARG A	280	61.318	46.478	22.238	1.00	43.50	6	C
ATOM	2165	NE	ARG A	280	60.534	45.725	23.187	1.00	47.87	7	N
ATOM	2166	CZ	ARG A	280	60.898	44.892	24.146	1.00	49.41	6	C
ATOM	2167	NH1	ARG A	280	59.960	44.288	24.882	1.00	50.02	7	N
ATOM	2168	NH2	ARG A	280	62.153	44.609	24.464	1.00	50.53	7	N
ATOM	2169	C	ARG A	280	61.646	43.736	18.758	1.00	28.75	6	C
ATOM	2170	O	ARG A	280	62.815	43.462	18.808	1.00	27.51	8	O
ATOM	2171	N	LEU A	281	60.733	42.757	18.957	1.00	29.52	7	N
ATOM	2172	CA	LEU A	281	61.115	41.378	19.148	1.00	29.08	6	C
ATOM	2173	CB	LEU A	281	59.878	40.482	19.401	1.00	30.92	6	C
ATOM	2174	CG	LEU A	281	59.000	40.892	20.605	1.00	33.95	6	C
ATOM	2175	CD1	LEU A	281	57.733	40.042	20.666	1.00	32.63	6	C
ATOM	2176	CD2	LEU A	281	59.817	40.766	21.876	1.00	33.55	6	C
ATOM	2177	C	LEU A	281	61.844	40.821	17.928	1.00	25.76	6	C
ATOM	2178	O	LEU A	281	62.818	40.076	18.070	1.00	21.64	8	O
ATOM	2179	N	PHE A	282	61.314	41.126	16.749	1.00	25.15	7	N
ATOM	2180	CA	PHE A	282	61.957	40.652	15.516	1.00	25.56	6	C
ATOM	2181	CB	PHE A	282	61.134	41.151	14.305	1.00	26.05	6	C
ATOM	2182	CG	PHE A	282	61.869	40.875	13.009	1.00	26.48	6	C
ATOM	2183	CD1	PHE A	282	61.860	39.598	12.485	1.00	28.15	6	C
ATOM	2184	CD2	PHE A	282	62.547	41.876	12.338	1.00	26.62	6	C
ATOM	2185	CE1	PHE A	282	62.497	39.306	11.302	1.00	27.83	6	C
ATOM	2186	CE2	PHE A	282	63.218	41.591	11.164	1.00	27.17	6	C
ATOM	2187	CZ	PHE A	282	63.201	40.302	10.662	1.00	29.01	6	C
ATOM	2188	C	PHE A	282	63.400	41.152	15.427	1.00	25.50	6	C
ATOM	2189	O	PHE A	282	64.317	40.363	15.278	1.00	24.99	8	O
ATOM	2190	N	GLU A	283	63.593	42.456	15.654	1.00	28.59	7	N
ATOM	2191	CA	GLU A	283	64.933	43.037	15.574	1.00	31.75	6	C
ATOM	2192	CB	GLU A	283	64.906	44.571	15.676	1.00	35.85	6	C
ATOM	2193	CG	GLU A	283	64.141	45.212	14.523	1.00	41.71	6	C
ATOM	2194	CD	GLU A	283	63.948	46.697	14.743	1.00	46.13	6	C
ATOM	2195	OE1	GLU A	283	64.906	47.453	15.019	1.00	46.68	8	O
ATOM	2196	OE2	GLU A	283	62.796	47.181	14.663	1.00	50.06	8	O
ATOM	2197	C	GLU A	283	65.865	42.483	16.641	1.00	29.73	6	C
ATOM	2198	O	GLU A	283	67.012	42.217	16.301	1.00	30.42	8	O
ATOM	2199	N	MET A	284	65.361	42.288	17.857	1.00	28.92	7	N
ATOM	2200	CA	MET A	284	66.143	41.676	18.907	1.00	28.74	6	C
ATOM	2201	CB	MET A	284	65.328	41.555	20.217	1.00	29.44	6	C
ATOM	2202	CG	MET A	284	64.839	42.819	20.892	1.00	31.83	6	C
ATOM	2203	SD	MET A	284	64.349	42.591	22.632	1.00	35.57	16	S
ATOM	2204	CE	MET A	284	65.824	41.621	23.060	1.00	26.72	6	C
ATOM	2205	C	MET A	284	66.665	40.306	18.567	1.00	25.37	6	C
ATOM	2206	O	MET A	284	67.827	39.970	18.774	1.00	27.80	8	O
ATOM	2207	N	VAL A	285	65.822	39.360	18.112	1.00	24.69	7	N
ATOM	2208	CA	VAL A	285	66.194	38.035	17.722	1.00	22.10	6	C
ATOM	2209	CB	VAL A	285	64.938	37.209	17.237	1.00	22.25	6	C
ATOM	2210	CG1	VAL A	285	65.445	35.907	16.678	1.00	21.99	6	C
ATOM	2211	CG2	VAL A	285	64.146	36.970	18.526	1.00	22.56	6	C
ATOM	2212	C	VAL A	285	67.239	38.084	16.574	1.00	22.61	6	C
ATOM	2213	O	VAL A	285	68.205	37.337	16.576	1.00	25.80	8	O
ATOM	2214	N	LYS A	286	67.045	38.916	15.598	1.00	26.81	7	N
ATOM	2215	CA	LYS A	286	67.995	39.104	14.490	1.00	30.63	6	C
ATOM	2216	CB	LYS A	286	67.449	40.148	13.520	1.00	32.69	6	C
ATOM	2217	CG	LYS A	286	66.202	39.697	12.760	1.00	33.80	6	C
ATOM	2218	CD	LYS A	286	66.463	38.370	12.067	1.00	35.04	6	C
ATOM	2219	CE	LYS A	286	67.293	38.445	10.807	1.00	34.54	6	C
ATOM	2220	NZ	LYS A	286	67.550	37.072	10.261	1.00	35.90	7	N
ATOM	2221	C	LYS A	286	69.376	39.526	15.006	1.00	30.82	6	C
ATOM	2222	O	LYS A	286	70.396	39.036	14.508	1.00	32.76	8	O
ATOM	2223	N	ARG A	287	69.431	40.400	16.013	1.00	31.10	7	N
ATOM	2224	CA	ARG A	287	70.714	40.816	16.604	1.00	30.96	6	C
ATOM	2225	CB	ARG A	287	70.583	42.005	17.529	1.00	30.38	6	C
ATOM	2226	CG	ARG A	287	70.116	43.375	17.152	1.00	32.68	6	C
ATOM	2227	CD	ARG A	287	69.484	44.170	18.348	1.00	33.81	6	C
ATOM	2228	NE	ARG A	287	68.533	45.133	17.764	1.00	36.54	7	N
ATOM	2229	CZ	ARG A	287	67.488	45.691	18.267	1.00	34.85	6	C
ATOM	2230	NH1	ARG A	287	67.137	45.373	19.538	1.00	35.39	7	N
ATOM	2231	NH2	ARG A	287	66.748	46.556	17.570	1.00	36.57	7	N
ATOM	2232	C	ARG A	287	71.356	39.638	17.308	1.00	32.30	6	C
ATOM	2233	O	ARG A	287	72.542	39.411	17.109	1.00	33.47	8	O
ATOM	2234	N	LYS A	288	70.600	38.785	18.034	1.00	32.62	7	N
ATOM	2235	CA	LYS A	288	71.145	37.597	18.640	1.00	33.94	6	C
ATOM	2236	CB	LYS A	288	70.111	36.854	19.507	1.00	35.23	6	C
ATOM	2237	CG	LYS A	288	69.608	37.710	20.659	1.00	35.37	6	C
ATOM	2238	CD	LYS A	288	68.867	36.870	21.687	1.00	37.31	6	C
ATOM	2239	CE	LYS A	288	68.151	37.797	22.658	1.00	37.75	6	C
ATOM	2240	NZ	LYS A	288	68.902	37.955	23.939	1.00	38.18	7	N
ATOM	2241	C	LYS A	288	71.713	36.605	17.641	1.00	37.09	6	C
ATOM	2242	O	LYS A	288	72.668	35.903	17.972	1.00	36.11	8	O
ATOM	2243	N	GLU A	289	71.075	36.440	16.481	1.00	41.18	7	N
ATOM	2244	CA	GLU A	289	71.519	35.514	15.452	1.00	44.56	6	C
ATOM	2245	CB	GLU A	289	70.568	35.544	14.260	1.00	46.83	6	C
ATOM	2246	CG	GLU A	289	69.201	34.909	14.469	1.00	49.19	6	C
ATOM	2247	CD	GLU A	289	68.529	34.899	13.100	1.00	50.64	6	C
ATOM	2248	OE1	GLU A	289	68.442	36.038	12.597	1.00	52.06	8	O
ATOM	2249	OE2	GLU A	289	68.146	33.861	12.537	1.00	51.29	8	O
ATOM	2250	C	GLU A	289	72.890	35.910	14.891	1.00	45.68	6	C
ATOM	2251	O	GLU A	289	73.818	35.137	14.677	1.00	44.19	8	O
ATOM	2252	N	SER A	290	73.013	37.221	14.674	1.00	48.65	7	N
ATOM	2253	CA	SER A	290	74.306	37.727	14.231	1.00	52.68	6	C
ATOM	2254	CB	SER A	290	74.278	39.186	13.806	1.00	52.54	6	C
ATOM	2255	OG	SER A	290	75.677	39.491	13.632	1.00	53.21	8	O
ATOM	2256	C	SER A	290	75.323	37.552	15.371	1.00	55.65	6	C
ATOM	2257	O	SER A	290	76.478	37.189	15.146	1.00	55.72	8	O
ATOM	2258	N	GLU A	291	74.872	37.757	16.592	1.00	58.14	7	N
ATOM	2259	CA	GLU A	291	75.584	37.641	17.833	1.00	61.11	6	C
ATOM	2260	CB	GLU A	291	76.917	36.906	17.785	1.00	62.15	6	C
ATOM	2261	CG	GLU A	291	76.937	35.556	18.465	1.00	64.10	6	C
ATOM	2262	CD	GLU A	291	76.620	34.394	17.555	1.00	65.44	6	C
ATOM	2263	OE1	GLU A	291	76.734	33.228	17.991	1.00	66.46	8	O
ATOM	2264	OE2	GLU A	291	76.263	34.563	16.379	1.00	66.51	8	O
ATOM	2265	C	GLU A	291	75.826	39.022	18.451	1.00	61.44	6	C
ATOM	2266	O	GLU A	291	75.122	39.336	19.425	1.00	62.15	8	O
ATOM	2267	OT	GLU A	291	76.698	39.760	17.949	1.00	62.85	8	O
ATOM	2268	OW0	WAT W	1	50.217	13.385	8.209	1.00	18.85	8	O
ATOM	2269	OW0	WAT W	2	51.099	13.263	−8.741	1.00	23.12	8	O
ATOM	2270	OW0	WAT W	3	59.588	23.064	3.410	1.00	20.25	8	O
ATOM	2271	OW0	WAT W	4	44.433	27.839	−0.089	1.00	21.90	8	O
ATOM	2272	OW0	WAT W	5	62.584	30.723	1.451	1.00	21.49	8	O
ATOM	2273	OW0	WAT W	6	53.660	4.312	5.088	1.00	23.56	8	O
ATOM	2274	OW0	WAT W	7	42.461	16.502	−7.442	1.00	19.28	8	O
ATOM	2275	OW0	WAT W	8	50.471	4.408	−0.984	1.00	28.60	8	O
ATOM	2276	OW0	WAT W	9	49.743	18.658	−13.374	1.00	32.32	8	O
ATOM	2277	OW0	WAT W	10	44.689	29.884	1.451	1.00	28.29	8	O
ATOM	2278	OW0	WAT W	11	49.899	34.479	2.565	1.00	38.46	8	O
ATOM	2279	OW0	WAT W	12	41.559	11.016	−5.279	1.00	27.37	8	O
ATOM	2280	OW0	WAT W	13	46.109	24.308	29.035	1.00	30.91	8	O
ATOM	2281	OW0	WAT W	14	53.259	27.112	7.872	1.00	28.13	8	O
ATOM	2282	OW0	WAT W	15	65.303	30.595	0.296	1.00	26.04	8	O
ATOM	2283	OW0	WAT W	16	58.733	26.677	−12.881	1.00	28.60	8	O
ATOM	2284	OW0	WAT W	17	61.058	27.725	25.573	1.00	28.38	8	O
ATOM	2285	OW0	WAT W	18	56.024	5.831	13.865	1.00	26.82	8	O
ATOM	2286	OW0	WAT W	19	57.892	36.531	2.311	1.00	32.51	8	O
ATOM	2287	OW0	WAT W	20	64.032	17.458	6.356	1.00	25.67	8	O
ATOM	2288	OW0	WAT W	21	53.531	26.503	2.690	1.00	24.96	8	O
ATOM	2289	OW0	WAT W	22	48.109	10.443	12.991	1.00	33.12	8	O
ATOM	2290	OW0	WAT W	23	63.052	29.353	14.789	1.00	27.25	8	O
ATOM	2291	OW0	WAT W	24	58.658	19.577	−18.215	1.00	31.14	8	O
ATOM	2292	OW0	WAT W	25	69.574	45.629	15.048	1.00	23.96	8	O
ATOM	2293	OW0	WAT W	26	64.033	32.895	−3.472	1.00	30.38	8	O
ATOM	2294	OW0	WAT W	27	45.265	26.382	30.985	1.00	37.20	8	O
ATOM	2296	OW0	WAT W	29	64.316	33.139	9.120	1.00	28.20	8	O
ATOM	2297	OW0	WAT W	30	69.017	43.023	14.050	1.00	36.84	8	O
ATOM	2298	OW0	WAT W	31	56.424	6.042	9.451	1.00	45.62	8	O
ATOM	2299	OW0	WAT W	32	65.473	25.882	−12.349	1.00	31.77	8	O
ATOM	2300	OW0	WAT W	33	54.047	28.809	12.233	1.00	32.98	8	O
ATOM	2301	OW0	WAT W	34	71.715	11.099	21.805	1.00	28.72	8	O
ATOM	2302	OW0	WAT W	35	44.866	23.772	−10.264	1.00	31.01	8	O
ATOM	2303	OW0	WAT W	36	42.891	8.225	0.183	1.00	45.65	8	O
ATOM	2304	OW0	WAT W	37	70.091	9.899	9.438	1.00	42.64	8	O
ATOM	2305	OW0	WAT W	38	55.173	20.751	30.386	1.00	47.17	8	O
ATOM	2306	OW0	WAT W	39	64.556	−1.132	7.808	1.00	41.30	8	O
ATOM	2307	OW0	WAT W	40	43.741	44.189	17.880	1.00	46.34	8	O
ATOM	2308	OW0	WAT W	41	65.303	17.923	15.681	1.00	36.89	8	O
ATOM	2309	OW0	WAT W	42	65.926	5.299	−3.431	1.00	35.15	8	O
ATOM	2310	OW0	WAT W	43	48.814	25.326	−10.907	1.00	36.32	8	O
ATOM	2311	OW0	WAT W	44	71.256	20.768	−5.622	1.00	45.70	8	O
ATOM	2312	OW0	WAT W	45	43.487	7.489	10.572	1.00	41.45	8	O
ATOM	2313	OW0	WAT W	46	53.848	5.218	8.719	1.00	47.18	8	O
ATOM	2314	OW0	WAT W	47	65.635	33.112	2.964	1.00	34.64	8	O
ATOM	2315	OW0	WAT W	48	40.726	28.714	23.437	1.00	38.77	8	O
ATOM	2316	OW0	WAT W	49	43.440	32.012	14.188	1.00	44.70	8	O
ATOM	2317	OW0	WAT W	50	76.019	8.562	0.201	1.00	32.02	8	O
ATOM	2318	OW0	WAT W	51	61.127	48.537	25.049	1.00	56.13	8	O
ATOM	2319	OW0	WAT W	52	65.781	33.797	−0.396	1.00	45.54	8	O
ATOM	2320	OW0	WAT W	53	42.177	13.006	3.059	1.00	41.61	8	O
ATOM	2321	OW0	WAT W	54	66.903	22.848	−12.476	1.00	29.57	8	O
ATOM	2322	OW0	WAT W	55	42.048	30.487	−1.394	1.00	56.64	8	O
ATOM	2323	OW0	WAT W	56	60.361	22.604	−15.611	1.00	32.16	8	O
ATOM	2324	OW0	WAT W	57	52.219	28.431	10.189	1.00	27.74	8	O
ATOM	2325	OW0	WAT W	58	49.598	30.240	30.888	1.00	37.18	8	O
ATOM	2326	OW0	WAT W	59	64.471	34.651	−7.853	1.00	40.08	8	O
ATOM	2327	OW0	WAT W	60	37.370	33.351	9.660	1.00	41.05	8	O
ATOM	2328	OW0	WAT W	61	59.810	24.408	9.179	1.00	24.99	8	O
ATOM	2329	OW0	WAT W	62	54.904	22.048	9.493	1.00	26.52	8	O
ATOM	2330	OW0	WAT W	63	59.801	22.030	7.519	1.00	31.69	8	O
ATOM	2331	OW0	WAT W	64	61.589	20.737	9.336	1.00	37.29	8	O
ATOM	2332	OW0	WAT W	65	54.273	30.364	2.612	1.00	31.63	8	O
ATOM	2333	OW0	WAT W	66	51.721	9.464	18.710	1.00	41.21	8	O
ATOM	2334	OW0	WAT W	67	39.698	15.341	−4.655	1.00	41.50	8	O
ATOM	2335	OW0	WAT W	68	65.849	18.347	10.526	1.00	36.90	8	O
ATOM	2336	OW0	WAT W	69	63.148	4.922	−12.137	1.00	44.78	8	O
ATOM	2337	OW0	WAT W	70	59.514	48.884	18.189	1.00	41.71	8	O
ATOM	2338	OW0	WAT W	71	67.904	3.430	15.950	1.00	29.67	8	O
ATOM	2339	OW0	WAT W	72	60.457	28.514	−12.39O	1.00	41.62	8	O
ATOM	2340	OW0	WAT W	73	64.593	19.854	7.512	1.00	38.96	8	O
ATOM	2341	OW0	WAT W	74	62.953	18.712	9.638	1.00	31.50	8	O
ATOM	2342	OW0	WAT W	75	58.999	18.160	14.139	1.00	36.51	8	O
ATOM	2343	OW0	WAT W	76	60.140	11.877	22.642	1.00	50.94	8	O
ATOM	2344	OW0	WAT W	77	45.591	40.024	2.139	1.00	79.57	8	O
ATOM	2345	OW0	WAT W	78	69.205	23.538	21.104	1.00	37.43	8	O
ATOM	2346	OW0	WAT W	79	41.543	31.614	11.031	1.00	59.04	8	O
ATOM	2347	OW0	WAT W	80	68.389	27.416	1.198	1.00	62.23	8	O
ATOM	2348	OW0	WAT W	81	44.130	10.194	−5.136	1.00	36.84	8	O
ATOM	2349	OW0	WAT W	82	66.868	21.240	9.977	1.00	37.21	8	O
ATOM	2350	OW0	WAT W	83	58.659	17.118	−18.714	1.00	35.94	8	O
ATOM	2351	OW0	WAT W	84	48.207	28.942	−15.536	1.00	80.94	8	O
ATOM	2352	OW0	WAT W	85	59.985	35.614	−7.715	1.00	63.41	8	O
ATOM	2353	OW0	WAT W	86	68.848	7.807	−12.897	1.00	54.20	8	O
ATOM	2354	OW0	WAT W	87	50.732	8.107	10.734	1.00	29.14	8	O
ATOM	2355	OW0	WAT W	88	57.598	31.502	−15.596	1.00	67.97	8	O
ATOM	2356	OW0	WAT W	89	45.523	35.059	4.411	1.00	43.42	8	O
ATOM	2357	OW0	WAT W	90	43.953	31.511	16.602	1.00	58.48	8	O
ATOM	2358	OW0	WAT W	91	62.804	19.278	16.014	1.00	48.73	8	O
ATOM	2359	OW0	WAT W	92	55.227	19.291	15.486	1.00	41.12	8	O
ATOM	2360	OW0	WAT W	93	74.125	5.232	2.711	1.00	37.31	8	O
ATOM	2361	OW0	WAT W	94	47.921	47.666	16.091	1.00	46.05	8	O
ATOM	2362	OW0	WAT W	95	44.648	30.547	−2.533	1.00	56.72	8	O
ATOM	2363	OW0	WAT W	96	43.159	13.302	12.753	1.00	31.02	8	O
ATOM	2364	OW0	WAT W	97	76.289	13.068	−6.287	1.00	60.16	8	O
ATOM	2365	OW0	WAT W	98	40.454	31.194	22.897	1.00	47.18	8	O
ATOM	2366	OW0	WAT W	99	56.619	24.955	22.006	1.00	34.02	8	O
ATOM	2367	OW0	WAT W	100	57.214	26.810	17.742	1.00	42.53	8	O
ATOM	2368	OW0	WAT W	101	72.485	31.810	15.402	1.00	48.53	8	O
ATOM	2369	OW0	WAT W	102	58.554	25.994	33.289	1.00	42.04	8	O
ATOM	2370	OW0	WAT W	103	58.901	33.000	−8.347	1.00	35.50	8	O
ATOM	2371	OW0	WAT W	104	48.684	42.585	−0.562	1.00	53.83	8	O
ATOM	2372	OW0	WAT W	105	72.840	7.443	−6.312	1.00	34.41	8	O
ATOM	2373	OW0	WAT W	106	60.649	41.443	6.936	1.00	46.14	8	O
ATOM	2374	OW0	WAT W	107	55.930	20.902	12.923	1.00	42.34	8	O
ATOM	2375	OW0	WAT W	108	56.276	10.614	22.445	1.00	83.32	8	O
ATOM	2376	OW0	WAT W	109	59.177	−2.036	11.105	1.00	87.00	8	O
ATOM	2377	OW0	WAT W	110	68.330	19.216	11.389	1.00	70.09	8	O
ATOM	2378	OW0	WAT W	111	62.535	3.830	−3.900	1.00	39.80	8	O
ATOM	2379	OW0	WAT W	112	41.144	15.596	2.174	1.00	40.32	8	O
ATOM	2380	OW0	WAT W	113	69.370	17.211	4.420	1.00	48.23	8	O
ATOM	2381	OW0	WAT W	114	68.319	23.527	25.851	1.00	57.14	8	O
ATOM	2382	OW0	WAT W	115	64.404	45.735	19.468	1.00	41.92	8	O
ATOM	2383	OW0	WAT W	116	45.942	2.698	−1.562	1.00	76.01	8	O
ATOM	2384	OW0	WAT W	117	57.931	44.072	22.182	1.00	40.11	8	O
ATOM	2386	OW0	WAT W	119	56.524	7.343	−12.363	1.00	48.25	8	O
ATOM	2387	OW0	WAT W	120	40.832	27.869	−4.695	1.00	68.68	8	O
ATOM	2388	OW0	WAT W	121	50.854	48.038	19.585	1.00	48.13	8	O
ATOM	2389	OW0	WAT W	122	51.900	26.821	−17.165	1.00	87.36	8	O
ATOM	2390	OW0	WAT W	123	59.155	22.302	22.180	1.00	39.59	8	O
ATOM	2391	OW0	WAT W	124	61.429	20.643	−17.207	1.00	56.75	8	O
ATOM	2392	OW0	WAT W	125	60.712	37.193	1.919	1.00	55.44	8	O
ATOM	2393	OW0	WAT W	126	73.565	18.085	2.425	1.00	68.15	8	O
ATOM	2394	OW0	WAT W	127	59.651	30.426	35.039	1.00	33.15	8	O
ATOM	2395	OW0	WAT W	128	62.379	37.582	4.161	1.00	61.18	8	O
ATOM	2396	OW0	WAT W	129	70.181	31.887	16.650	1.00	36.26	8	O
ATOM	2397	OW0	WAT W	130	37.334	19.934	−1.505	1.00	58.69	8	O
ATOM	2398	OW0	WAT W	131	61.399	20.771	25.090	1.00	50.02	8	O
ATOM	2399	OW0	WAT W	132	68.076	35.145	25.475	1.00	37.05	8	O
ATOM	2400	OW0	WAT W	133	60.505	7.047	−14.800	1.00	37.95	8	O
ATOM	2401	OW0	WAT W	134	54.115	16.074	7.368	1.00	38.68	8	O
ATOM	2402	OW0	WAT W	135	70.773	38.203	11.598	1.00	65.07	8	O
ATOM	2403	OW0	WAT W	136	70.458	19.171	2.818	1.00	47.13	8	O
ATOM	2404	OW0	WAT W	137	50.264	27.459	−12.167	1.00	94.45	8	O
ATOM	2405	OW0	WAT W	138	72.688	2.033	4.919	1.00	55.96	8	O
ATOM	2406	OW0	WAT W	139	66.483	0.919	−1.206	1.00	68.63	8	O
ATOM	2407	OW0	WAT W	140	44.865	5.901	6.299	1.00	49.31	8	O
ATOM	2408	OW0	WAT W	141	52.797	4.031	18.728	1.00	51.39	8	O
ATOM	2410	OW0	WAT W	143	45.567	39.187	29.528	1.00	55.02	8	O
ATOM	2411	OW0	WAT W	144	75.438	16.139	2.640	1.00	50.00	8	O
ATOM	2412	OW0	WAT W	145	69.844	33.346	6.328	1.00	59.27	8	O
ATOM	2413	OW0	WAT W	146	39.466	30.238	−0.842	1.00	56.38	8	O
ATOM	2414	OW0	WAT W	147	44.062	5.699	8.806	1.00	52.80	8	O
ATOM	2415	OW0	WAT W	148	59.516	1.238	−5.799	1.00	41.14	8	O
ATOM	2416	OW0	WAT W	149	47.532	2.806	3.371	1.00	51.28	8	O
ATOM	2418	OW0	WAT W	151	43.200	31.185	29.288	1.00	44.17	8	O
ATOM	2419	OW0	WAT W	152	53.785	43.131	−0.198	1.00	81.11	8	O
ATOM	2420	OW0	WAT W	153	64.038	−2.169	5.299	1.00	46.34	8	O
ATOM	2421	OW0	WAT W	154	38.979	21.681	−8.628	1.00	36.79	8	O
ATOM	2422	OW0	WAT W	155	58.390	19.129	16.402	1.00	55.19	8	O
ATOM	2423	OW0	WAT W	156	68.504	22.779	8.616	1.00	40.79	8	O
ATOM	2424	OW0	WAT W	157	55.387	40.436	34.674	1.00	49.21	8	O
ATOM	2425	OW0	WAT W	158	53.019	39.301	−1.129	1.00	96.43	8	O
ATOM	2426	OW0	WAT W	159	41.477	15.278	−1.137	1.00	32.11	8	O
ATOM	2427	OW0	WAT W	160	38.535	9.180	−2.033	1.00	46.62	8	O
ATOM	2428	OW0	WAT W	161	60.419	23.551	11.903	1.00	57.65	8	O
ATOM	2429	OW0	WAT W	162	47.468	44.822	27.591	1.00	55.55	8	O
ATOM	2430	OW0	WAT W	163	56.215	−1.570	0.715	1.00	75.61	8	O
ATOM	2431	OW0	WAT W	164	62.001	48.322	17.294	1.00	60.03	8	O
ATOM	2432	OW0	WAT W	165	44.207	22.903	−12.975	1.00	33.12	8	O
ATOM	2433	OW0	WAT W	166	65.534	18.704	13.254	1.00	58.88	8	O
ATOM	2434	OW0	WAT W	167	36.524	38.366	27.592	1.00	96.00	8	O
ATOM	2435	OW0	WAT W	168	52.063	6.514	19.512	1.00	58.91	8	O
ATOM	2436	OW0	WAT W	169	72.416	10.815	4.633	1.00	37.38	8	O
ATOM	2437	OW0	WAT W	170	36.786	39.018	22.128	1.00	47.31	8	O
ATOM	2438	OW0	WAT W	171	55.889	4.109	−8.888	1.00	45.08	8	O
ATOM	2439	OW0	WAT W	172	70.959	4.313	6.468	1.00	39.12	8	O
ATOM	2440	OW0	WAT W	173	60.991	15.486	21.392	1.00	46.15	8	O
ATOM	2441	OW0	WAT W	174	65.401	7.600	−12.565	1.00	43.95	8	O
ATOM	2442	OW0	WAT W	175	53.786	48.388	9.725	1.00	41.68	8	O
ATOM	2443	OW0	WAT W	176	53.110	5.798	13.932	1.00	33.46	8	O
ATOM	2444	OW0	WAT W	177	58.883	4.598	−12.625	1.00	44.97	8	O
ATOM	2445	OW0	WAT W	178	62.227	39.315	7.259	1.00	42.67	8	O
ATOM	2446	OW0	WAT W	179	73.940	41.878	19.168	1.00	51.61	8	O
ATOM	2447	OW0	WAT W	180	68.342	19.961	1.138	1.00	50.35	8	O
ATOM	2448	OW0	WAT W	181	55.358	44.850	2.862	1.00	49.87	8	O
ATOM	2449	OW0	WAT W	182	79.585	32.525	13.716	1.00	66.67	8	O
ATOM	2451	OW0	WAT W	184	64.518	23.932	15.951	1.00	44.99	8	O
ATOM	2453	OW0	WAT W	186	51.154	31.181	36.820	1.00	61.70	8	O
ATOM	2454	OW0	WAT W	187	51.013	15.442	17.418	1.00	45.79	8	O
ATOM	2455	OW0	WAT W	188	39.771	41.527	18.524	1.00	49.74	8	O
ATOM	2456	OW0	WAT W	189	72.438	9.840	−7.353	1.00	40.07	8	O
ATOM	2457	OW0	WAT W	190	46.902	14.835	15.177	1.00	46.39	8	O
ATOM	2458	OW0	WAT W	191	57.675	20.757	10.803	1.00	50.78	8	O
ATOM	2459	OW0	WAT W	192	69.479	12.450	0.686	1.00	31.78	8	O
ATOM	2460	OW0	WAT W	193	61.498	42.666	4.391	1.00	49.75	8	O
ATOM	2461	OW0	WAT W	194	40.573	23.622	−4.508	1.00	49.50	8	O
ATOM	2462	OW0	WAT W	195	63.239	22.036	17.365	1.00	60.76	8	O
ATOM	2463	OW0	WAT W	196	50.230	38.893	−1.160	1.00	78.76	8	O
ATOM	2464	OW0	WAT W	197	71.530	40.221	22.322	1.00	55.72	8	O
ATOM	2465	OW0	WAT W	198	75.489	8.467	5.178	1.00	65.56	8	O
ATOM	2466	OW0	WAT W	199	45.696	45.482	25.583	1.00	49.39	8	O
ATOM	2467	OW0	WAT W	200	37.019	43.489	24.116	1.00	57.82	8	O
ATOM	2468	OW0	WAT W	201	40.688	15.783	8.184	1.00	48.78	8	O
ATOM	2470	OW0	WAT W	203	62.458	2.230	1.187	1.00	40.73	8	O
ATOM	2471	OW0	WAT W	204	52.440	32.379	2.873	1.00	34.91	8	O
ATOM	2472	OW0	WAT W	205	57.846	25.412	19.786	1.00	38.28	8	O
ATOM	2473	OW0	WAT W	206	67.361	33.501	10.026	1.00	49.47	8	O
ATOM	2474	OW0	WAT W	207	67.350	13.501	1.221	1.00	45.88	8	O
ATOM	2475	OW0	WAT W	208	53.533	40.792	1.526	1.00	46.36	8	O
ATOM	2476	OW0	WAT W	209	41.314	31.067	18.590	1.00	50.24	8	O
ATOM	2477	OW0	WAT W	210	54.131	15.501	−14.694	1.00	42.77	8	O
ATOM	2478	OW0	WAT W	211	60.554	17.337	17.933	1.00	53.34	8	O
ATOM	2479	OW0	WAT W	212	67.523	14.077	19.660	1.00	50.05	8	O
ATOM	2480	OW0	WAT W	213	40.813	42.013	26.973	1.00	54.37	8	O
ATOM	2481	OW0	WAT W	214	66.196	27.079	11.041	1.00	46.02	8	O
ATOM	2482	OW0	WAT W	215	55.181	36.388	−13.734	1.00	53.91	8	O
ATOM	2483	OW0	WAT W	216	48.057	35.571	4.408	1.00	42.80	8	O
ATOM	2484	OW0	WAT W	217	52.470	1.706	5.097	1.00	45.08	8	O
ATOM	2485	OW0	WAT W	218	38.558	17.450	−0.591	1.00	52.74	8	O
ATOM	2486	OW0	WAT W	219	48.977	22.868	15.771	1.00	53.86	8	O
ATOM	2487	OW0	WAT W	220	59.800	7.098	18.579	1.00	45.62	8	O
ATOM	2488	OW0	WAT W	221	58.023	35.899	−6.089	1.00	48.40	8	O
ATOM	2489	OW0	WAT W	222	61.021	27.781	14.513	1.00	46.58	8	O
ATOM	2490	OW0	WAT W	223	47.444	22.887	12.782	1.00	56.07	8	O
ATOM	2491	OW0	WAT W	224	50.705	37.582	1.322	1.00	48.64	8	O
ATOM	2492	OW0	WAT W	225	66.183	26.023	30.771	1.00	48.27	8	O
ATOM	2493	OW0	WAT W	226	48.692	34.988	33.176	1.00	52.17	8	O
ATOM	2494	OW0	WAT W	227	42.523	6.385	−1.745	1.00	51.24	8	O
ATOM	2495	OW0	WAT W	228	68.475	30.124	0.782	1.00	55.52	8	O
ATOM	2496	OW0	WAT W	229	46.706	18.388	15.459	1.00	57.98	8	O
ATOM	2497	OW0	WAT W	230	35.641	36.427	9.282	1.00	55.60	8	O
ATOM	2498	OW0	WAT W	231	72.587	4.072	9.251	1.00	54.93	8	O
ATOM	2499	OW0	WAT W	232	41.618	10.474	1.751	1.00	54.38	8	O
ATOM	2500	OW0	WAT W	233	57.543	50.282	15.470	1.00	58.67	8	O
ATOM	2501	OW0	WAT W	234	44.867	42.335	0.710	1.00	57.80	8	O
ATOM	2502	OW0	WAT W	235	57.128	25.399	15.459	1.00	58.90	8	O
ATOM	2503	OW0	WAT W	236	68.901	21.881	−0.580	1.00	53.19	8	O
ATOM	2504	OW0	WAT W	237	53.588	2.879	−6.515	1.00	59.80	8	O
ATOM	2505	OW0	WAT W	238	44.473	7.462	−3.404	1.00	53.96	8	O
ATOM	2506	OW0	WAT W	239	74.820	10.403	6.976	1.00	54.01	8	O
ATOM	2507	OW0	WAT W	240	56.842	9.771	−13.835	1.00	55.94	8	O
ATOM	2508	OW0	WAT W	241	38.570	22.438	2.343	1.00	57.94	8	O
ATOM	2509	OW0	WAT W	242	65.608	−0.573	10.932	1.00	56.24	8	O
ATOM	2510	OW0	WAT W	243	67.275	33.989	6.398	1.00	59.57	8	O
ATOM	2511	OW0	WAT W	244	38.494	27.454	26.177	1.00	56.65	8	O
ATOM	2512	OW0	WAT W	245	79.415	38.544	19.049	1.00	55.94	8	O
ATOM	2513	OW0	WAT W	246	41.428	43.667	23.851	1.00	48.67	8	O
ATOM	2514	OW0	WAT W	247	45.669	8.862	−7.019	1.00	54.07	8	O
ATOM	2515	OW0	WAT W	248	57.584	17.844	11.964	1.00	57.11	8	O
ATOM	2516	OW0	WAT W	249	63.334	28.290	−11.159	1.00	52.99	8	O
ATOM	2517	OW0	WAT W	250	50.101	5.187	11.030	1.00	58.96	8	O
ATOM	2518	OW0	WAT W	251	55.531	46.308	9.306	1.00	49.04	8	O
ATOM	2519	OW0	WAT W	252	73.201	1.607	−5.272	1.00	58.26	8	O
ATOM	2520	OW0	WAT W	253	71.038	8.861	−13.814	1.00	56.92	8	O
ATOM	2521	OW0	WAT W	254	65.195	4.663	−5.993	1.00	57.84	8	O
ATOM	2522	OW0	WAT W	255	69.290	21.864	3.630	1.00	60.04	8	O
ATOM	2523	OW0	WAT W	256	60.282	28.198	33.064	1.00	52.37	8	O
ATOM	2524	OW0	WAT W	257	54.999	26.806	34.737	1.00	59.86	8	O
ATOM	2525	OW0	WAT W	258	69.644	21.889	−3.484	1.00	55.95	8	O
ATOM	2526	OW0	WAT W	259	41.512	12.680	8.317	1.00	57.27	8	O
ATOM	2527	OW0	WAT W	260	38.620	20.840	−3.595	1.00	60.58	8	O
ATOM	2528	OW0	WAT W	261	42.796	29.152	−3.495	1.00	57.83	8	O
ATOM	2529	OW0	WAT W	262	43.194	45.599	12.173	1.00	60.81	8	O
ATOM	2530	OW0	WAT W	263	43.689	32.979	−2.364	1.00	61.53	8	O
ATOM	2531	OW0	WAT W	264	55.096	12.692	−14.255	1.00	56.51	8	O
ATOM	2532	OW0	WAT W	265	66.719	21.323	27.411	1.00	60.18	8	O
ATOM	2533	OW0	WAT W	266	48.925	24.154	−13.326	1.00	59.99	8	O
ATOM	2534	OW0	WAT W	267	50.424	34.508	−0.963	1.00	58.47	8	O
ATOM	2535	OW0	WAT W	268	69.496	0.033	1.507	1.00	60.26	8	O
ATOM	2536	OW0	WAT W	269	57.574	46.046	3.695	1.00	59.77	8	O
ATOM	2537	OW0	WAT W	270	57.679	42.153	24.392	1.00	59.49	8	O
ATOM	2538	OW0	WAT W	271	46.096	35.339	31.158	1.00	60.76	8	O
ATOM	2539	OW0	WAT W	272	38.455	35.588	24.574	1.00	60.34	8	O

Claims

1. A crystal of ketopantoate reductase having a tetragonal space group P41212 with unit cell dimensions of a=103.7±0.2, b=103.7±0.2, c=55.7±0.2 Å.

2. A crystal of ketopantoate reductase having a resolution better than 2 Å.

3. A crystal of ketopantoate reductase having the structure defined by the co-ordinates of Table 1.

4. A method for crystallizing a selenium atom KPR derivative which comprises producing KPR by recombinant production in a bacterial host in the presence of selenomethionine, recovering a selenium atom KPR derivative from the host and growing crystals from the recovered selenium atom KPR derivative.

5. A computer-based method of rational drug design which comprises: providing the structure of the KPR as defined by the coordinates of Table 1; providing the structure of a candidate modulator molecule; and fitting the structure of candidate to the structure of the KPR of Table 1.

6. A computer-based method of rational drug design which comprises: providing the coordinates of at least two atoms of Table 1 of the KPR (“selected coordinates”; providing the structure of a candidate modulator molecule; and fitting the structure of candidate to the selected coordinates of the KPR.

7. A computer-based method of rational drug design which comprises: providing the coordinates of at least a sub-domain of the KPR; providing the structure of a candidate modulator molecule; and fitting the structure of the candidate to the coordinates of the KPR sub-domain provided.

8. The method of claim 5, 6 or 7 which further comprises the steps of: obtaining or synthesising the candidate modulator; and contacting the candidate modulator with KPR to determine the ability of the candidate modulator to interact with KPR.

9. The method of claim 5, 6 or 7 which further comprises the steps of: obtaining or synthesising said candidate modulator; forming a complex of KPR and said potential modulator; and analysing said complex by X-ray crystallography to determine the ability of said candidate modulator to interact with KPR.

10. A compound having a chemical structure selected using the method of claim 5, 6 or 7, said compound being an inhibitor of KPR.

11. A computer system, intended to generate structures and/or perform rational drug design for KPR or complexes of KPR with a potential modulator, the systems containing either (a) atomic coordinate data according to Table 1, said data defining the three-dimensional structure of KPR or at least one sub-domain thereof, or (b) structure factor data for KPR, said structure factor data being derivable from the atomic coordinate data of Table 1.

12. A computer readable media with either (a) atomic coordinate data according to Table 1 recorded thereon, said data defining the three-dimensional structure of KPR, at least one atom or at least one sub-domain thereof, or (b) structure factor data for KPR recorded thereon, the structure factor data being derivable from the atomic coordinate data of Table 1.