Patent Publication Number: US-2007099232-A1

Title: Ecdysone receptor ligand-binding domain structure

Description:
FIELD OF THE INVENTION  
      The present invention relates to structural studies of the functional insect ecdysone receptor. More particularly, the invention relates to the crystal structure of the whitefly ecdysone receptor ligand-binding domain, specifically that of  Bemisia tabaci , and uses of the crystal and related structural information to select and screen for compounds that interact with the receptor. Moreover, the crystal structure of the present invention can be used to predict the structure of the ligand-binding pocket of functional ecdysone receptors from related species and to guide site-directed mutagenesis of amino acid residues influencing discrimination between different ligands.  
     BACKGROUND OF THE INVENTION  
      Carroll Williams in the 1960s pointed out that over 99% of insect species are either innocuous or beneficial from the human point of view. Some are even indispensable, e.g. bees via their role in pollination. Approximately 0.1% of insects are actually pests. Williams suggested that a new generation of safer insecticides exhibiting specificity for particular pests might be developed based on the chemistry of the insect&#39;s own hormones (Williams, 1967; Williams, 1967). The levels of the non-peptide hormones controlling growth and development, 20-hydroxyecdysone and juvenile hormone, are precisely controlled. Inappropriate levels of compounds with ecdysteroid or juvenoid activity lead to major perturbation of insect development and subsequent lethality.  
      A problem with this approach, not initially appreciated, stems from the efficient mechanisms insects possess for clearing these hormones by metabolic degradation during normal development. This problem might be overcome by the discovery of compounds exhibiting high receptor affinities but with different chemistry to the native hormones and thus not subject to the host&#39;s catabolic pathways.  
      The two non-peptide hormones known to play key roles in regulating insect growth and development are the steroid moulting hormone, 20-hydroxyecdysone, hereafter referred to as ecdysone, and the sesquiterpenoid juvenile hormone, hereafter referred to as JH. JH is responsible for maintaining larval or nymphal states in moulting insects in addition to a role in adults in the regulation of reproductive processes. The titre of ecdysone may rise and fall as many as six or more times during the life cycle of insects, regulating, for example, the moulting process between larval instars, the synthesis of new cuticle, the onset of metamorphosis (after a decline in JH titre) and aspects of vitellogenesis in the adult ovary. The giant polytene chromosomes seen in the dipteran  Drosophila melanogaster , have given insights into the complexity of the response to a rise in ecdysone titre at the level of changes in gene expression. It was postulated by Ashburner and co-workers (Ashburner et al., 1974) that ecdysone exerts its action in regulating gene expression via a protein receptor. A few early responding genes produce further gene transcription regulatory proteins that transmit the response to a whole bank of late responding genes; these regulatory proteins can be detected in action at the late-responding chromosomal loci (Hill et al., 1993).  
      Over the past decade much progress has been made in understanding the molecular mechanisms underlying the key role of ecdysone in controlling insect development. This research has been led by studies involving the combined power of genetics and molecular biology employing the fly  D. melanogaster . Of particular importance to the present application has been the elucidation of the nature of the ecdysone receptor. It has been shown to be a heterodimer made up of the products of two genes called ecr and usp (Yao et al., 1993). The protein products of these genes, EcR and USP, are members of the nuclear receptor superfamily. This family is characterised by an overall structural plan in which a series of domains impart, in order from the N-terminus: transcriptional activation (A/B), DNA binding (C), nuclear localisation (so-called “linker”, D) and ligand binding (E/F). The ligand-binding domain also imparts transactivation in response to the binding of agonist ligands.  
      Both the EcR and USP subunits of ecdysone receptors have been cloned from a number of insects—see for example (Koelle et al., 1991; Hannan &amp; Hill, 1997; Hannan &amp; Hill, 2001; Oro et al., 1990, WO 99/36520, WO 01/02436).  
      Despite the considerable interest in JH since the 1960&#39;s, the nature of its receptor has proven more elusive. Research reported late in 1997 and subsequent publications suggests that this long-sought-after receptor may also involve USP (Jones &amp; Sharp, 1997; Sasorith et al., 2002) but this remains controversial. Even in the absence of precise knowledge of its receptor, JH has served as a model for intensive programs of chemical synthesis over three decades leading to a host of diverse molecules that mimic the activity of the hormone. Some of these have been registered as insecticides. Recently, three-dimensional structures have been solved for monomeric ligand-binding domains of USPs from the lepidopteran  Heliothis virescens  (Billas et al., 2001) and the dipteran  D. melanogaster  (Clayton et al., 2001).  
      Until the 1980&#39;s, chemical approaches to the development of ecdysone mimics were hampered by the structural complexity and synthetic inaccessibility of the steroids for commercial-scale field applications. However in 1988, Rohm and Haas Company scientists (Wing et al., 1988; Wing, 1988) reported that a class of bisacylhydrazine insecticides, which the company had discovered serendipitously, were acting primarily via interaction with ecdysone receptors. Members of this class display remarkable selectivity at the level of orders within the Insecta, for example RH-5992 is some two to three orders of magnitude more effective against  Lepidotera  than it is against  Diptera . This difference correlates with different dissociation constants for interaction of the compound with ecdysone receptors from the two insect orders (Dhadialla et al., 1998). Although subsequent studies (Sundaram et al., 1998) have demonstrated a contribution in some cases by active transport clearance, there is little doubt that variation in the structure of the ecdysone receptors per se between different orders plays a very significant role in underlying the selectivity of extant insecticides in this class.  
      The selectivity of the bisacylhydrazines for the  Lepidoptera  and some  Coleoptera  has both positive and negative connotations. On the positive side, we see a harbinger of safer, more environmentally-friendly insecticides targeting a receptor not only absent from vertebrates but also exhibiting sufficient variation across the Insecta to allow discrimination between pests and friendly or innocuous species. On the negative side, the present relatively narrow spectrum of activity limits sales and also leaves a significant number of insect orders that cannot be controlled by safe ecdysone receptor targeting chemistries. Industry has been trying to extend the spectrum of activity of agents with this mode of action but with relatively little success.  
      Since much of the selectivity of current agents stems from variations in the structure of the ecdysone receptor, there is a need in the art for knowledge of the three-dimensional structures of the ligand-binding domain of ecdysone receptors, not only to guide the design of new ligand chemistries, but also to introduce into this design process an understanding of receptor atomic features underlying selectivity of action.  
      Homology modelling based on the known three-dimensional structures of other nuclear receptor ligand-binding domains, including those of retinoic acid receptor and vitamin D receptor (Wurtz et al., 2000) and those of human thyroid hormone receptor β, human estrogen receptor a and human progesterone receptor (Kasuya et al., 2003), has been employed to predict the structure of the corresponding domains of ecdysone receptors for ligand docking studies. Such approaches do not distinguish between alternative potential three-dimensional protein structures and alternative orientations for ligand docking.  
      Furthermore, ecdysone receptors and their functional domains are employed as components of ecdysone switches for the control of therapeutic genes in mammalian cells and for control of transgenes more generally in agriculturally important species, both animal and plant. Knowledge of the three-dimensional structure of the ligand-binding domain of ecdysone receptors should aid in the design of safer more effective ligands to act as effectors for such switches and to guide site-directed mutagenesis to change ligand preferences of the receptors.  
      Accordingly, knowledge of the three-dimensional structure co-ordinates of the ecdysone receptor, and in particular the ligand-binding pocket of the receptor, would be useful in facilitating the design of potential selective agonists/antagonists which, in turn, are expected to have insecticidal activity and to include potential safe effectors for ecdysone switches.  
     SUMMARY OF THE INVENTION  
      The present inventors have now obtained three-dimensional structural information concerning the functional ligand-binding domain of the ecdysone receptor of  Bemisia tabaci  (silverleaf whitefly). The functional  B. tabaci  ecdysone receptor is a heterodimeric receptor comprising ecdysone receptor subunit protein (BtEcR) and ultraspiracle subunit protein (BtUSP). The BtUSP partner protein associates with the BtEcR receptor protein to confer greatly enhanced affinity for insect steroids or analogues thereof. Compounds that typically modulate the activity of the ecdysone receptor include 20-hydroxyecdysone (henceforth referred to as “ecdysone”), ponasterone A, muristerone A, analogues of an ecdysteroid or certain non-steroidal ecdysone receptor agonists or antagonists, including for example those having dibenzoyl hydrazine chemistries.  
      The information presented in this application can be used to predict the structure of related members of the ecdysone receptor family from other species as well as to select and/or design compounds which interact with the  B. tabaci  ecdysone receptor and other ecdysone receptors for use as insecticidally-active agents.  
      In the remainder of this application the term “ecdysone receptor” is used to denote the functional EcR/USP heterodimer receptor and the subunits are referred to as EcR and USP. Specifically the subunits from  B. tabaci  are referred to as BtEcR and BtUSP. The term ligand-binding domain will be abbreviated to LBD.  
      Accordingly, in a first aspect the present invention consists in a crystalline composition comprising BtEcR/BtUSP heterodimer LBD or portion thereof, or a crystalline composition comprising BtEcR/BtUSP heterodimer LBD or portion thereof co-crystallized with a ligand.  
      In a second aspect the present invention provides a method of selecting or designing a compound that interacts with an ecdysone receptor and modulates an activity mediated by the receptor, the method comprising the step of assessing the stereochemical complementarity between the compound and a topographic region of the BtEcR/BtUSP heterodimer LBD, wherein the heterodimer LBD is characterised by 
      (a) amino acids 179-415 of the BtEcR monomer and amino adds 300-492 of the BtUSP monomer positioned at atomic coordinates as shown in Appendix I, or structural coordinates wherein the backbone atoms of each monomer has a root mean square deviation from the backbone atoms of their corresponding partners in either amino adds 179-415 of the BtEcR monomer or amino adds 300-492 of the BtUSP monomer of not more than 1.5 Å; or     (b) one or more subsets of said amino adds related to the coordinates of the monomers shown in Appendix I by whole body translations and/or rotations.    

      By “stereochemical complementarity” we mean that the compound or a portion thereof makes a sufficient number of energetically favourable contacts with the receptor, or topographic region thereof, as to have a net reduction of free energy on binding to the receptor, or topographic region thereof.  
      Stereochemical complementarity or how well a given chemical compound structure binds or fits to a specified site or cavity in the protein structure can be measured by using one or more of the scoring functions available for this purpose. (See for example P. Ferrara, H. Gohlke, D. J. Price, G. Klebe, and C. L. Brooks III, Assessing scoring functions for protein-ligand interactions, J. Med. Chem., vol. 47, 3032-3047(2004).) A specific example of such a scoring function is X-SCORE (R. Wang, L. Lai, S. Wang, Further development and validation of empirical scoring functions for structure-based binding affinity prediction, J. Comput.-Aided Mol. Des., vol. 16, 11-26(2002)), which is a scoring function that calculates the dissociation constant of a given protein-ligand complex, and was constructed by calibrating to experimental data on a set of 200 protein-ligand complexes.  
      By “topographic region” is meant a subset of the molecular surface (Connolly, 1983) of the BtEcR LBD alone, the BtUSP LBD alone or the BtEcR/BtUSP heterodimer LBD. This subset may consist of either a single region or multiple disjoint regions. In this context the surface of enclosed cavities within the BtEcR/BtUSP heterodimer LBD or its constituent partners is also treated as part of the molecular surface.  
      In a third aspect the present invention provides a computer-assisted method for identifying potential compounds able to interact with an ecdysone receptor and thereby modulate an activity mediated by the receptor, using a programmed computer comprising a processor, an input device, and an output device, comprising the steps of: 
      (a) inputting into the programmed computer, through the input device, data comprising the atomic coordinates of amino adds 179-415 of the BtEcR monomer and amino adds 300-492 of the BtUSP monomer and ponasterone A positioned at atomic coordinates as shown in Appendix I, or structural coordinates wherein the backbone atoms of each monomer has a root mean square deviation from the backbone atoms of their corresponding partners in either amino acids 179-415 of the BtEcR monomer or amino acids 300-492 of the BtUSP monomer of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations;     (b) generating, using computer methods, a set of atomic coordinates of a structure that possesses stereochemical complementarity to the atomic coordinates of amino acids 179-415 of the BtEcR monomer and/or amino acids 300-492 of the BtUSP monomer positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of their corresponding partners in either amino acids 179-415 of the BtEcR monomer or amino acids 300-492 of the BtUSP monomer of not more than 1.5 Å, or one or more subsets of said amino adds, or one or more subsets of said amino adds related to the coordinates shown in Appendix I by whole body translations and/or rotations, thereby generating a criteria data set;     (c) comparing, using the processor, the criteria data set to a computer database of chemical structures;     (d) selecting from the database, using computer methods, chemical structures which are similar to a portion of said criteria data set; and     (e) outputting, to the output device, the selected chemical structures which are complementary to or similar to a portion of the criteria data set.    

      In a fourth aspect the present invention provides a computer for producing a three-dimensional representation of a molecule or molecular complex, wherein the computer comprises: 
      (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the machine readable data comprises the atomic coordinates of amino acids 179-415 of the BtEcR monomer and amino acids 300-492 of the BtUSP monomer and ponasterone A as shown in Appendix I, or structural coordinates wherein the backbone atoms of each monomer has a root mean square deviation from the backbone atoms of their corresponding partners in either amino acids 179-415 of the BtEcR monomer or amino acids 300-492 of the BtUSP monomer of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations;     (b) a working memory for storing instructions for processing the machine-readable data;     (c) a central-processing unit coupled to the working memory and to the machine-readable data storage medium, for processing the machine-readable data into the three dimensional representation; and     (d) an output hardware coupled to the central processing unit, for receiving the three-dimensional representation.    

      In a fifth aspect the present invention provides a compound able to modulate an activity mediated by an ecdysone receptor, the compound being obtained by a method according to the present invention.  
      In a sixth aspect the present invention provides a compound which possesses stereochemical complementarity to a topographic region of the BtEcR/BtUSP heterodimer LBD and which modulates an activity mediated by the receptor, wherein the heterodimer is characterised by 
      (a) amino acids 179-415 of the BtEcR monomer and amino acids 300-492 of the BtUSP monomer positioned at atomic coordinates as shown in Appendix I, or structural coordinates wherein the backbone atoms of each monomer has a root mean square deviation from the backbone atoms of their corresponding partners in either amino acids 179-415 of the BtEcR monomer or amino acids 300-415 of the BtUSP monomer of not more than 1.5 Å; or     (b) one or more subsets of said amino acids related to the coordinates of the monomers shown in Appendix I by whole body translations and/or rotations; 
 
 with the proviso that the compound is not a naturally occurring ligand of a molecule of the  B. tabaci  ecdysone receptor. 
   

      In a seventh aspect, the present invention provides an insecticidal composition for control of insects which comprises a compound according to the fifth or sixth aspects of the present invention and a pharmaceutically acceptable carrier or diluent.  
      In yet another aspect, the present invention provides a method for evaluating the ability of a chemical entity to interact with an ecdysone receptor LBD, said method comprising the steps of: 
      (a) creating a computer model of at least one region of the BtEcR/BtUSP heterodimer LBD using structure coordinates wherein the root mean square deviation between the backbone atoms of the (i) the BtEcR component of the model and the corresponding structure coordinates of amino acids 179-415 of the BtEcR monomer or (ii) the BtUSP component of the model and the corresponding structure coordinates of amino acids 300-492 of the BtUSP monomer as set forth in Appendix I, are not more than 1.5 Å;     (b) employing computational means to perform a fitting operation between the chemical entity and said computer model of at least one region of the monomers of the BtEcR/BtUSP heterodimer LBD; and     (c) analysing the results of said fitting operation to quantify the association between the chemical entity and at least one region of the BtEcR/BtUSP heterodimer LBD model.    

      In another aspect the present invention consists in a method of assessing the interaction between a compound and the BtEcR/BtUSP heterodimer LBD, the method comprising exposing a crystalline composition comprising BtEcR/BtUSP heterodimer LBD or portion thereof or variant of these to the compound and measuring the level of binding of the compound to the crystal.  
      As will be readily understood by persons skilled in this field, the methods of the present invention provide a rational method for designing and selecting compounds which interact with an ecdysone receptor and specifically that of  B. tabaci . In the majority of cases these compounds will require further development in order to increase activity. Such further development is routine in this field and will be assisted by the structural information provided in this application and screens employing EcR and optionally USP nucleotide and/or polypeptide sequences. In vitro competitive binding screens compete unlabelled test compounds against a labelled ligand (tracer) to observe if they inhibit the binding of the latter to functional receptor LBDs. In vitro competition binding screens may utilise LBD sequences or D (linker) domain sequences linked to LBD sequences. In vivo cell-based screens employ full-length EcR and optionally full-length USP nucleotide sequences functionally linked to suitable promoters for expression in mammalian, insect or yeast cells containing a suitable reporter gene construct. Alternatively, in vivo cell-based screens may employ the EF or DEF domain encoding regions of EcR and optionally of USP nucleotide sequences functionally linked to nucleotide sequences encoding domains from other transcription factors. In particular, the BtEcR nucleotide sequence (SEQ ID NO 1) and/or polypeptide sequence (SEQ ID NO 2) and optionally BtUSP nucleotide sequence and/or polypeptide sequence or the corresponding EF or DEF domains may be utilised in screens to develop improved compounds derived by rational design employing the  B. tabaci  EcR/USP crystal structure. It is intended that in particular embodiments the methods of the present invention includes such further developmental steps.  
      In yet a further aspect, the invention provides a method of utilizing molecular replacement to obtain structural information about a molecule or a molecular complex of unknown structure, comprising the steps of: 
      (a) crystallising said molecule or molecular complex;     (b) collecting an X-ray diffraction data set from said crystallized molecule or molecular complex;     (c) applying at least a portion of the structure coordinates set forth in Appendix I to the X-ray diffraction data set to generate a three-dimensional electron density map of at least a portion of the molecule or molecular complex whose structure is unknown. The term “molecular replacement” refers to a method that involves generating a preliminary model of an ecdysone receptor crystal whose structure coordinates are unknown, by orienting and positioning a molecule whose structure coordinates are known (e.g., BtEcR/BtUSP heterodimer LBD coordinates from Appendix I) within the unit cell of the unknown crystal so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. This, in turn, can be subject to any of the several forms of refinement to provide a final, accurate structure of the unknown crystal (Lattman, 1985; Rossmann, 1990).    

      As will be clear from the following discussion the present inventors have also isolated a nucleic add molecule encoding the BtEcR.  
      Accordingly, in a further aspect the present invention provides an isolated nucleic acid molecule comprising a nucleotide sequence which encodes at least the LBD of BtEcR, wherein the nucleotide sequence is selected from the group consisting of: 
      (i) a nucleotide sequence comprising a sequence having at least 90% identity to the sequence from nucleotide 535 to nucleotide 1248 of SEQ ID NO: 1 or the complementary nucleotide sequence;     (ii) a nucleotide sequence comprising a sequence that hybridises under high stringency conditions to the sequence from nucleotide 535 to nucleotide 1248 of SEQ ID NO: 1 or the complementary nucleotide sequence; and     (iii) a nucleotide sequence which encodes a polypeptide comprising the sequence from amino acid P179 to amino acid S416 of SEQ ID NO: 2.   

    
    
     BRIEF DESCRIPTION OF THE FIGURES  
       FIG. 1  Schematic diagram of the structure of the BtEcR/BtUSP heterodimer LBD with bound ponasterone A shown in the binding pocket. The BtEcR LBD is shown in grey, whilst the BtUSP LBD is in black. Individual helices are shown as cylinders and individual β-strands as arrows. The N- and C-terminii of each molecule are labelled. Ponasterone A is shown in black with its oxygen atoms in white. Helix 3 of the BtEcR LBD is rendered transparent in order to enable viewing of the ponasterone A moeity. The surface of the binding pocket itself is shown in transparent grey.  
       FIG. 2  View of the extended ecdysteroid binding pocket, showing the surface of the pocket, bound ponasterone A and all residues that form the walls of the pocket. The pocket is separated into two parts for clarity—the entire pocket can be re-generated by rotating the lower image about a vertical axis running in the plane of the paper and placing it on top of the upper image. Ponasterone A is shown in black as a “thick” stick representation in both images with its oxygen atoms represented by black balls. Surrounding residues that form the cavity are labelled and are shown as “thin” grey sticks if they are totally conserved across all species, else they are shown as “thin” black sticks. Individual atoms within residues are rendered as follows—nitrogen: small balls, oxygen: medium balls and sulphur: large balls. Again for clarity, side chain or alternatively backbone atoms are omitted for individual residues if these groups of atoms do not form any part of the cavity wall. Hydrogen bonds between individual protein residues and ponasterone A are shown as black dotted lines. The molecular surface of the binding pocket is shown in transparent grey.  
       FIG. 3  Stick/CPK diagram of the BtEcR LBD co-activator/co-repressor binding groove (without H12) with individual residues labelled. All atoms from residues 231 to 265 are rendered as transparent CPK and a Cα trace to delineate the groove. Individual residues with putatively capable of interaction with co-activator/co-repressor proteins are rendered in black stick format, with nitrogen atoms as small grey balls and oxygen atoms as large grey balls.  
       FIG. 4  An analysis of freshly-prepared recombinant BtEcR LBD samples by 12% SDS-PAGE, with staining by Coomassie Blue. Samples were boiled in the presence of 5% (v/v) 2-mercaptoethanol before loading. M: marker proteins, with molecular masses shown in kilodaltons (kDa). Lane 1: Immobilised metal-ion affinity chromatography (IMAC) eluate, showing recombinant BtEcR and BtUSP LBDs (major doublet) and many additional bands (contaminating proteins). Lane 2: Concentrated gel filtration eluate, showing BtEcR and BtUSP LBD&#39;s (main doublet) with relatively few contaminating proteins.  
       FIG. 5  Residues defining the terminal end of the major pocket. The Van der Waals surface for the binding pocket in this region is shown as a smooth grey surface to the right. Space-filling representation of ponasterone A in the X-ray structure of the ligand-receptor complex. The smooth grey surface to the right represents the Van der Waals surface of the binding pocket in the region near the alkyl chain of the ecdysteroid.  
       FIG. 6  Highly-ranked FlexX docking of ponasterone A superimposed on the X-ray structure of ponasterone A bound into the EcR. The dark grey structure represents the x-ray orientation of ponasterone A and the light grey structure represents one of the FlexX poses for ponasterone A. The ability of FlexX to dock a ligand into the receptor can be assessed by the high similarity of the ponasterone A orientation from docking to that in the X-ray model.  
       FIG. 7  Highly-ranked FlexX docking pose for compound III. The thiophene ring extends into the lipophilic end of the receptor pocket, in the region where the C25 end of ponasterone A binds. The cyclic ester is able to make hydrogen bonds with Asn390 and the ring nitrogen form a hydrogen bond with Thr231. The phenyl ring lies in the same position as that of the C/D rings of ponasterone A.  
       FIG. 8  Overlay of the hemipteran  B. tabaci  and lepidopteran  H virescens  ecdysone receptor LBD ponasterone A bound pockets and superposition of ligands. The HvEcR 1R1K (ponasterone A containing) and HvEcR 1R20 (synthetic agonist BYI06830 containing) LBDs were aligned to the BtEcR (ponasterone A containing) LBD by least squares alignment of the protein Cα backbone atoms. The ligand agonists are shown in ball and stick format with the BTECR ponasterone A in “thick” black sticks, the HvEcR 1R1K ponasterone A in “thick” grey sticks and, the HvEcR 1R20 BYI06830 in “thin” grey sticks. The carbon atoms are rendered in black, the oxygen atoms in grey and the nitrogen atoms in white. The BtEcR ponasterone A bound pocket is shown as a transparent pale grey surface and the HvEcR 1R1K ponasterone A bound pocket surface shown in transparent dark grey. (For clarity, the surface of the BY106830 bound pocket is not depicted in the figure.) A pronounced bulge, absent from the BtEcR ponasterone A bound pocket, is apparent in the HvEcR ponasterone A bound pocket at top left. 
    
    
     DETAILED DESCRIPTION  
      The present inventors have doned BtEcR and BtUSP and expressed, crystallised and determined the three-dimensional structure of the BtEcR/BtUSP heterodimer LBD of the ecdysone receptor from  Bemisia tabaci.    
      The fold of BtEcR LBD is that of a canonical nuclear hormone receptor. The secondary structure elements of BtUSP/BtEcR LBD discerned in this structure are located within the BTECR sequence as follows: helix H1—residues 182 to 198, helix H2—residues 202 to 211, helix H3—residues 220 to 244, helix H4—residues 252 to 264, helix H5—residues 267 to 275, strand s0—residues 275 to 277, strand s1—residues 282 to 285, strand s2—residues 288 to 291, helix H6—residues 292 to 300, helix H7—residues 304 to 319, helix H8—residues 321 to 334, helix H9—residues 342 to 364, helix H10—residues 368 to 400 and helix H12—residues 405 to 413. Thus, the structure of BtEcR LBD comprises α-helices H1 to H10 and H12, and β-strands s1 and s2 located between helices H5 and H6, as shown in  FIG. 1 . An additional short β-strand (labelled here as s0) lies between helix H5 and strand s1. Helix H12 in BtEcR is observed in the so-called agonist conformation (Renaud &amp; Moras, 2000).  
      The structure of the BtEcR LBD was compared with those available for other nuclear receptors. The closest structural neighbour was the LBD of retinoic acid receptor (RAR). The root-mean-square deviation of 206 (out of 237) corresponding backbone C α  atoms between the BtEcR structure and that of RAR-γ2 (RCSB id: 1EXA) is 1.29 Å. The major difference between these structures lies in the conformation of the loop between helices H1 and H3. In RAR this loop has a random coil conformation and lies across the outer surface of the s1-s2 β-sheet loop. In EcR the segment contains an intact helix H2 which packs anti-parallel on the N-terminal portion of helix H3 and interacts with the opposite surface of the s1-s2 β-sheet loop.  
      The ligand ponasterone A was observed to lie in a totally-enclosed pocket formed by residues F194, Q195, N196, Y198, E199, H200, P201, H226, I227, T228, I230, T231, L233, T234, L237, I238, F241, S242, V267, M268, M269, F270, R271, M272, R274, R275, I283, L284, F285, A286, Y296, M301, T304, L308, Y325, A326, T329, 1333, M389, N390, T393, C394, L397, V404, P405, L408 and W412 ( FIG. 2 ). The pocket has a “J-shaped” architecture, with the major part (the leg of the “J”) accommodating the ligand, plus an ancillary part (the curved tail of the “J”) existing as an extension of the major part via a narrow channel. The inner wall of the channel linking the major and ancillary parts of the pocket is formed by the side chain of residue R271. The accessible volume of the entire cavity is approximately 766 Å 3 , whilst the volume of the ponasterone A itself is 434 Å 3 , both figures calculated using VOIDOO (Kleywegt &amp; Jones, 1994). The ancillary cavity appears unoccupied in the structure presented here. The narrowness of channel connecting the major and ancillary parts of the pocket suggests that it in some dynamic states of the protein these two parts may become disjoint rather than forming a single topological entity.  
      Potential hydrogen bonds between individual protein atoms and ligand are as follows: A286 N to the ponasterone A hydroxyl at C-6, T234 O γ1  to the ponasterone A hydroxyl at C-14, T231 O γ1  to the ponasterone A hydroxyl at C-14, R271 NH1 to the ponasterone A hydroxyl at C-2, E199 O to the ponasterone A hydroxyl at C-2, E199 O to the ponasterone A hydroxyl at C-3, Y296 OH to the ponasterone A hydroxyl at C-20 ( FIG. 2 ). The remainder of the contacts between ligands and protein are overwhelmingly hydrophobic in nature and formed by contacts between the side chains of residues P201, I227, T228, I230, M268, M269, R271, M272, R275, 1283, F285, A286, M301, L308, M389, L397, P405, L408 and W412 and the ligand.  
      Helix H12 was observed to lie in the so-called agonistic conformation (Renaud &amp; Moras, 2000) possibly locking the ligand into the site via the side chain of W412 which hangs into the ligand-binding site. A salt bridge between BtEcR residues D413 and K261 appears to stabilize the C-terminus of H12. In this conformation a co-activator can bind to a site that includes H12 and the surface of the hydrophobic cleft between helices H3 and H4. The molecular detail of this cleft is presented in  FIG. 3 . Side chains forming the cleft and its immediate surrounds include those of residues I232, V235, Q236, V239, E240, K243, F248, R253, E254, Q256, I257, L260, K261, S264, and residues S406, F407, L408, E410, I411 and D413 of H12. Excluding H12, this groove is totally conserved across all ecdysone receptor sequences except for R253. This residue lies at the distal end of the binding groove (with respect to the position of H12 shown in this structure) and it is unclear at this stage whether or not its side chain interacts directly with the co-repressor or co-activator upon binding of these elements.  
      The structure of the BtUSP protein resembles that of other published USP structures (Billas et al., 2001; Clayton et al., 2001), but with the following major difference. No electron density was visible for residues prior to V300, i.e. helix H1, and part of the loop connecting H1 to H3 are totally unobserved. Part of the volume occupied by these structural elements in other USP structures is now occupied by the H10-H12 loop. H12 lies in the so-called antagonistic conformation (Renaud &amp; Moras, 2000) whilst the helix H11 appears not to be formed. No ligand was observed in the site corresponding to that occupied by phospholipid in the two above published structures, and indeed part of that binding site is now occluded by a repositioning of the H10-H12 loop, and by a repositioning of helix H6 and residues immediately adjacent to this element (residues 371 to 384). The repositioning of the H10-H12 loop likely arises from the absence of residues prior to H3 in our structure, allowing this element to collapse into the region normally occupied by the H1-H3 loop in the intact USP ligand-binding domains. Part of the movement of the H10-H12 loop may be caused by the involvement of that loop in a crystal contact with a neighbouring molecule in our structure. Alternatively the observed conformation of the H10-H12 loop may be adopted in solution as well in view of the absence of H1. The secondary structure elements of BtUSP/BtEcR LBD discerned in this structure are located within the BtUSP sequence as follows: helix H3—residues 301 to 321, helix H4—residues 328 to 339, helix H5—residues 340 to 353, strand s1 residues 359 to 361, strand s2—residues 365 to 367, helix H6—residues 371 to 376, helix H7—residues 380 to 396, helix H8—residues 399 to 411, helix H9—residues 420 to 443, helix H10—residues 448 to 466 and helix H12—residues 481 to 491.  
      The dimeric association between BtEcR and BtUSP ligand-binding domains resembles that of the corresponding RAR-RXR complex. These two heterodimeric structures can be overlaid with an root-mean-square deviation of 1.37 Å for 339 matched C α  atoms. The interface is formed by EcR residues contained in H9, H10 and the loop between H8 and H9 on one hand and USP residues contained in H7, H9, H10 and the loop between H6 and H7 on the other (see Table 5). Residues involved in the interface include BtEcR residues H314, M315, I331, S335, E336, R337, P338, E347, Q350, E351, I354, E355, K358, T370, T371, F373, A374, K375, L377, S378, L380, T381, E382, R384, T385 and N388 on one hand and BtUSP residues E342, R383, T386, E387, K391, E414, E425, E429, Y432, A433, E436, S447, G448, F450, A451, K452, L454, L455, R456, L457, P458, A459, R461, S462 and L465 on the other. The interface was estimated by computing all residues with any atom&#39;s van der Waals surface within 1.4 Å of that of any atom of the opposite chain followed by visual inspection.  
      Potential inter-chain salt bridges include those from USP E429 to EcR K375, USP K391 to EcR E336, USP K391 to EcR E347, USP K452 to EcR E351 and USP E425 to EcR K375. Out of these, only the salt bridge between EcR E347 and USP K391 is conserved across all species (although the Dipteran,  Chironomus tentans  EcR has Asp at the position corresponding to E347 in BtEcR), and compounds which bind to the interface and disrupt a particular salt bridge could be the basis of specific antagonists.  
      Hydrogen bonds occur between the side chains of USP S447 and the side chain of EcR E355A, between the backbone carbonyl of USP S447 and the side chain of EcR K358 and between the side chains of EcR R384 and USP S462. The remainder of the contacts are hydrophobic in nature. A single phosphate ion is included in the interface, coordinated by the side chains of the EcR residue R384, the carbonyl oxygen of EcR residue E336 and the side chains of USP residues R383, B387 and R456.  
      PASS (Brady &amp; Stouten, 2000) shows the existence of a pocket on the BtEcR surface on the edge of the heterodimeric interface bounded by residues including A262, S265, E266, R337, R384, G387, N388 and S391 of BtEcR. PASS also shows the existence of a pocket on the BtUSP surface on the edge of the heterodimeric interface bounded by residues including K337, S338, N341, E342, K416, G464, L465, C467 and H470 of BtUSP.  
      Clearly the information provided in this application will enable rational design/selection of compounds which will interact with the ecdysone receptor.  
      Accordingly, in a first aspect the present invention consists in a crystalline composition comprising BtEcR/BtUSP heterodirner LBD or portion thereof, or a crystalline composition comprising BtEcR/BtUSP heterodimer LBD or portion thereof co-crystallized with a ligand.  
      In a second aspect the present invention provides a method of selecting or designing a compound that interacts with an ecdysone receptor and modulates an activity mediated by the receptor, the method comprising the step of assessing the stereochemical complementarity between the compound and a topographic region of the BtEcR/BtUSP heterodimer LBD, wherein the heterodimer is characterised by 
      (a) amino acids 179-415 of the BtEcR monomer and amino adds 300-492 of the BtUSP monomer positioned at atomic coordinates as shown in Appendix I, or structural coordinates wherein the backbone atoms of each monomer has a root mean square deviation from the backbone atoms of their corresponding partners in either amino acids 179-415 of the BtEcR monomer or amino adds 300-492 of the BtUSP monomer of not more than 1.5 Å; or     (b) one or more subsets of said amino adds related to the coordinates of the monomers shown in Appendix I by whole body translations and/or rotations.    

      In a preferred embodiment of this aspect of the invention the structural coordinates have a root mean square deviation from the backbone atoms of said amino acids of not more than 1.0 Å, and more preferably not more than 0.7 Å.  
      As discussed above the ligand ponasterone A was observed to lie in a totally-enclosed pocket formed by residues F194, Q195, N196, Y198, E199, H200, P201, H226, I227, T228, I230, T231, L233, T234, L237, I238, F241, S242, V267, M268, M269, F270, R271, M272, R274, R275, I283, L284, F285, A286, Y296, M301, T304, L308, Y325, A326, T329, I333, M389, N390, T393, C394, L397, V404, P405, L408 and W412. Accordingly, in one embodiment of the second aspect, the topographic region of the ecdysone receptor to which the compound, or a portion thereof has stereochemical complementarity is the ligand-binding pocket of the BtEcR subunit defined by amino acids F194, Q195, N196, Y198, E199, H200, P201, H226, I227, T228, I230, T231, L233, T234, L237, I238, F241, S242, V267, M268, M269, F270, R271, M272, R274, R275, I283, L284, F285, A286, Y296, M301, T304, L308, Y325, A326, T329, I333, M389, N390, T393, C394, L397, V404, P405, L408 and W412.  
      In another embodiment of the second aspect, the topographic region of the ecdysone receptor to which the compound, or a portion thereof has stereochemical complementarity is the interface between the BtEcR and BtUSP subunits defined by BtEcR residues H314, M315, I331, S335, E336, R337, P338, E347, Q350, E351, I354, E355, K358, T370, T371, P373, A374, K375, L377, S378, L380, T381, E382, R384, T385 and N388 on one hand and BtUSP residues E342, R383, T386, E387, K391, E414, E425, E429, Y432, A433, E436, S447, G448, F450, A451, K452, L454, L455, R456, L457, P458, A459, R461, S462 and L465 on the other. in a still further embodiment of the second aspect, the topographic region of the ecdysone receptor to which the compound, or a portion thereof has stereochemical complementarity is the co-activator/ co-repressor binding groove formed by helices H3 and H4 on the surface of BtEcR defined by residues I232, V235, Q236, V239, E240, K243, F248, R253, E254, Q256, I257, L260, K261, S264, S265, M268, S406, P407, L408, E410, I411 and D413. By “stereochemical complementarity” we mean that the compound or a portion thereof makes a sufficient number of energetically favourable contacts with the receptor, or topographic region thereof, as to have a net reduction of free energy on binding to the receptor, or topographic region thereof.  
      In the preferred embodiment of the second aspect of the present invention, the method comprises selecting a compound which has portions that match residues positioned in the topographic region of the receptor defined by the specified amino add residues.  
      By “match” we mean that the identified portions interact with the surface residues, for example, via hydrogen bonding or by enthalpy-reducing Van der Waals interactions which promote desolvation of the biologically active compound with the receptor, in such a way that retention of the compound by the receptor is favoured energetically.  
      Preferably, the method comprises selecting a compound which forms hydrogen bonds with at least one amino acid residue selected from the group consisting of E199, I227, T231, T234, R271, A286, Y296, T304, N390 and C394 of the ligand-binding pocket of the BtEcR LBD, wherein the compound is not a naturally-occurring ecdysteroid ligand of the ligand-binding pocket of the receptor.  
      Still more preferably, the method comprises selecting a compound which further forms hydrophobic contacts with the side chains of at least one amino acid residue selected from the group consisting of P201, I227, T228, I230, M268, M269, R271, M272, R275, I283, F285, A286, M301, L308, M389, L397, P405, L408 and W412 of the ligand-binding pocket of the BtEcR subunit, wherein the compound is not the natural ligand of the ligand-binding pocket of the receptor.  
      In another embodiment crystals of the unliganded EcR/USP heterodimer are exposed to libraries of compounds according to the method of (Nienaber et al., 2000). The most potent ligand will bind preferentially to the crystal and can be identified by difference electron density maps.  
      In a still further embodiment of the second aspect, the method comprises selecting a compound which is an antagonist of the  B. tabaci  ecdysone receptor.  
      Alternatively, the method comprises selecting a compound which is an agonist of the  B. tabaci  ecdysone receptor.  
      It is anticipated that modulation of the activity of the  B. tabaci  ecdysone receptor may be achieved by a number of different means.  
      The compound may bind to the receptor so as to interfere sterically or allosterically with natural steroid ligand binding. For example. 
      (a) The compound may bind to the BtEcR ligand-binding pocket of the receptor such as to decrease the size of the ligand-binding pocket thereby preventing access of the ligand to one or more of the specified residues critical for receptor activity.     (b) The compound may bind at or near the interface between the BtEcR and BtUSP association interface to thereby perturb the subunit association for the signalling competent ligand-receptor complex.     (c) The compound may bind at a site remote from the BtEcR ligand-binding pocket but disturb the receptor structure so as to modulate the affinity of ligand-binding.    

      The compound may interfere with association of the BtEcR and BtUSP subunits of the ecdysone receptor in a number of ways. For example, the compound may bind to the  B. tabaci  ecdysone receptor at or near one or more of the specified residues of the association interface and by steric overlap and/or electrostatic repulsion prevent association. Alternatively, the compound may bind so as to interfere allosterically with association of the subunits. In addition, the compound may bind to the BtUSP subunit so as to alter the association of the subunits and thereby modulate the affinity of the BtEcR subunit for the natural ligand.  
      In the preferred form, the compound is selected or designed to interact with the  B. tabaci  ecdysone receptor in a manner such as to interfere with the association of the BtEcR and BtUSP subunits by inhibiting the association of BtEcR residues H314, M315, I331, S335, E336, R337, P338, E347, Q350, E351, I354, E355, K358, T370, T371, F373, A374, K375, L377, S378, V379, L380, T381, E382, R384, T385 and N388 on one hand and BtUSP residues E342, R383, T386, E387, K391, I408, V409, E414, E425, R428, E429, Y432, A433, E436, S447, G448, F450, A451, K452, L454, L455, R456, L457, A459, R461, S462 and L465 on the other.  
      In another preferred form the compound may bind to the receptor so as to interfere with signalling of the receptor. For example, the compound may be selected or modified from a known compound (such as the natural ligand), or identified from a data base. It would be expected that such a variant would compete with binding of the natural ligand to the receptor.  
      In another preferred embodiment the compound is selected or designed based on the natural ligand, the compound being designed or selected such that it interacts with at least one amino add selected from the group consisting of F194, Q195, N196, Y198, E199, H200, P201, H226, I227, T228, I230, T231, L233, T234, L237, I238, F241, S242, V267, M268, M269, F270, R271, M272, R274, R275, I283, L284, F285, A286, Y296, M301, T304, L308, Y325, A326, T329, I333, M389, N390, T393, C394, L397, V404, P405, L408 and W412. In a preferred embodiment, the compound is selected or designed such that the interaction between the compound and the  B. tabaci  ecdysone receptor is preferred over the interaction of the natural ligand with the  B. tabaci  ecdysone receptor. Such compounds may be agonists or antagonists of receptor activity.  
      In a preferred embodiment of the second aspect the method further comprises the step of obtaining a compound which possesses stereochemical complementarity to a topographic region of the BtEcR/BtUSP heterodimer LBD and testing the compound for insecticidal activity.  
      In a third aspect the present invention provides a computer-assisted method for identifying potential compounds able to interact with an ecdysone receptor and thereby modulate an activity mediated by the receptor, using a programmed computer comprising a processor, an input device, and an output device, comprising the steps of: 
      (a) inputting into the programmed computer, through the input device, data comprising the atomic coordinates of amino acids 179-415 of the BtEcR monomer and amino acids 300-492 of the BtUSP monomer and ponasterone A positioned at atomic coordinates as shown in Appendix I, or structural coordinates wherein the backbone atoms of each monomer has a root mean square deviation from the backbone atoms of their corresponding partners in either amino adds 179-415 of the BtEcR monomer or amino acids 300-492 of the BtUSP monomer of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations;     (b) generating, using computer methods, a set of atomic coordinates of a structure that possesses stereochemical complementarity to the atomic coordinates of amino acids 179-415 of the BtEcR monomer and/or amino acids 300-492 of the BtUSP monomer positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of their corresponding partners in either amino adds 179-415 of the BtEcR monomer or amino adds 300-492 of the BtUSP monomer of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations, thereby generating a criteria data set;     (c) comparing, using the processor, the criteria data set to a computer database of chemical structures;     (d) selecting from the database, using computer methods, chemical structures which are similar to a portion of said criteria data set; and     (e) outputting, to the output device, the selected chemical structures which are complementary to or similar to a portion of the criteria data set.    

      In a preferred embodiment of this aspect of the invention the structural coordinates have a root mean square deviation from the backbone atoms of said amino adds of not more than 1.0 Å, and more preferably not more than 0.7 Å.  
      Preferably, the method is used to identify potential compounds which are insecticidally active agents or safe effectors for ecdysone switches.  
      In a further preferred embodiment of the third aspect the method further comprises the step of obtaining a compound with a chemical structure selected in steps (d) and (e), and testing the compound for insecticidal activity.  
      In a preferred embodiment the subset of amino acids is that defining the ligand-binding pocket of the BtEcR subunit, namely P194, Q195, N196, Y198, E199, H200, P201, H226, I227, T228, I230, T231, L233, T234, L237, I238, F241, S242, V267, M268, M269, F270, R271, M272, R274, R275, I283, L284, F285, A286, Y296, M301, T304, L308, Y325, A326, T329, I333, M389, N390, T393, C394, L397, V404, P405, L408 and W412.  
      In another embodiment the subset of amino acids is that defining the interface between the BtEcR and BtUSP subunits defined by BtEcR residues H314, M315, I331, S335, E336, R337, P338, E347, Q350, E351, I354, E355, K358, T370, T371, F373, A374, K375, L377, S378, L380, T381, E382, R384, T385 and N388 on one hand and BtUSP residues E342, R383, T386, E387, K391, E414, E425, E429, Y432, A433, E436, S447, G448, F450, A451, K452, L454, L455, R456, L457, P458, A459, R461, S462 and L465 on the other.  
      In a still further embodiment the subset of amino acids is that defining the co-activator/co-repressor binding groove formed by helices H3 and H4 on the surface of BtEcR defined by residues I232, V235, Q236, V239, E240, K243, F248, R253, E254, Q256, I257, L260, K261, S264, S265, M268, S406, F407, L408, E410, I411 and D413.  
      The present invention also provides a method of screening of a putative compound having the ability to modulate the activity of the  B. tabaci  ecdysone receptor (BtEcR/BtUSP) or a heterodimer comprising BtEcR (SEQ ID NO 1) paired with another functional partner protein such as RXR, comprising the steps of identifying a putative compound according to the second or third aspects, and testing the compound for activity. In one embodiment, testing is carried out in vitro. Preferably, the in vitro test is a high throughput assay. In another embodiment, the test is carried out in vivo employing cell-based or whole organism-based screens.  
      In a fourth aspect the present invention provides a computer for producing a three-dimensional representation of a molecule or molecular complex, wherein the computer comprises: 
      (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the machine readable data comprises the atomic coordinates of amino acids 179-415 of the BtEcR monomer and amino adds 300-492 of the BtUSP monomer and ponasterone A as shown in Appendix I, or structural coordinates wherein the backbone atoms of each monomer has a root mean square deviation from the backbone atoms of their corresponding partners in either amino acids 179-415 of the BtEcR monomer or amino acids 300-492 of the BtUSP monomer of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations;     (b) a working memory for storing instructions for processing the machine-readable data;     (c) a central-processing unit coupled to the working memory and to the machine-readable data storage medium, for processing the machine-readable data into the three dimensional representation; and     (d) an output hardware coupled to the central processing unit, for receiving the three-dimensional representation.    

      In a preferred embodiment of this aspect of the invention the structural coordinates have a root mean square deviation from the backbone atoms of said amino acids of not more than 1.0 Å, and more preferably not more than 0.7 Å.  
      In a preferred embodiment the subset of amino adds is that defining the ligand-binding pocket of the BtEcR subunit, namely F194, Q195, N196, Y198, E199, H200, P201, H226, I227, T228, I230, T231, L233, T234, L237, I238, F241, S242, V267, M268, M269, F270, R271, M272, R274, R275, I283, L284, F285, A286, Y296, M301, T304, L308, Y325, A326, T329, I333, M389, N390, T393, C394, L397, V404, P405, L408 and W412.  
      In another embodiment the subset of amino adds is that defining the interface between the BtEcR and BtUSP subunits defined by BtEcR residues H314, M315, I331, S335, E336, R337, P338, E347, Q350, E351, I354, E355, K358, T370, T371, F373, A374, K375, L377, S378, L380, T381, E382, R384, T385 and N388 on one hand and BtUSP residues E342, R383, T386, E387, K391, E414, E425, E429, Y432, A433, E436, S447, G448, F450, A451, K452, L454, L455, R456, L457, P458, A459, R461, S462 and L465 on the other.  
      In a still further embodiment the subset of amino acids is that defining the co-activator/co-repressor binding groove formed by helices H3 and H4 on the surface of BtEcR defined by residues I232, V235, Q236, V239, E240, K243, F248, R253, E254, Q256, I257, L260, K261, S264, S265, M268, S406, F407, L408, E410, I411 and D413.  
      In a fifth aspect the present invention provides a compound able to modulate an activity mediated by an ecdysone receptor, the compound being obtained by a method according to the present invention.  
      In a sixth aspect the present invention provides a compound which possesses stereochemical complementarity to a topographic region of the BtEcR/BtUSP heterodimer LBD and which modulates an activity mediated by the receptor, wherein the heterodimer LBD is characterised by (
      a) amino acids 179-415 of the BtEcR monomer and amino acids 300-492 of the BtUSP monomer positioned at atomic coordinates as shown in Appendix I, or structural coordinates wherein the backbone atoms of each monomer has a root mean square deviation from the backbone atoms of their corresponding partners in either amino adds 179-415 of the BtEcR monomer or amino acids 300-492 of the BtUSP monomer of not more than 1.5 Å; or     (b) one or more subsets of said amino acids related to the coordinates of the monomers shown in Appendix I by whole body translations and/or rotations; 
 
 with the proviso that the compound is not a naturally occurring ligand of a molecule of the receptor. 
   

      In a preferred embodiment of this aspect of the invention the structural coordinates have a root mean square deviation from the backbone atoms of said amino acids of not more than 1.0 Å, and more preferably not more than 0.7 Å.  
      In one embodiment the sixth aspect, the topographic region of the ecdysone receptor to which the compound, or a portion thereof has stereochemical complementarity is the ligand-binding pocket of the BtEcR subunit defined by amino adds F194, Q195, N196, Y198, E199, H200, P201, H226, I227, T228, I230, T231, L233, T234, L237, I238, F241, S242, V267, M268, M269, F270, R271, M272, R274, R275, I283, L284, F285, A286, Y296, M301, T304, L308, Y325, A326, T329, I333, M389, N390, T393, C394, L397, V404, P405, L408 and W412.  
      In another embodiment of the sixth aspect, the topographic region of the ecdysone receptor to which the compound, or a portion thereof has stereochemical complementarity is the interface between the BtEcR and BtUSP subunits, defined by BtEcR residues H314, M315, I331, S335, E336, R337, P338, E347, Q350, E351, I354, E355, K358, T370, T371, F373, A374, K375, L377, S378, L380, T381, E382, R384, T385 and N388 on one hand and BtUSP residues E342, R383, T386, E387, K391, E414, E425, E429, Y432, A433, E436, S447, G448, F450, A451, K452, L454, L455, R456, L457, P458, A459, R461, S462 and L465 on the other.  
      In still a further embodiment of the sixth aspect the topographic region of the ecdysone receptor to which the compound, or a portion thereof has stereochemical complementarity is the co-activator/co-repressor binding groove formed by helices H3 and H4 on the surface of BtEcR defined by residues I232, V235, Q236, V239, E240, K243, F248, R253, E254, Q256, I257, L260, K261, S264, S265, M268, S406, F407, L408, E410, I411 and D413.  
      In a seventh aspect, the present invention provides an insecticidal composition for control of insects which comprises a compound according to the fifth or sixth aspects of the present invention and a pharmaceutically acceptable carrier or diluent.  
      In yet another aspect, the present invention provides a method for evaluating the ability of a chemical entity to interact with the BtEcR/BtUSP heterodimer LBD, said method comprising the steps of: 
      (a) creating a computer model of at least one region of the BtEcR/BtUSP heterodimer LBD using structure coordinates wherein the root mean square deviation between the backbone atoms of (i) the BtEcR component of the model and the corresponding structure coordinates of amino acids 179-415 of the BtEcR monomer or (ii) the BtUSP component of the model and the corresponding structure coordinates of amino adds 300-492 of the BtUSP monomer, as set forth in Appendix I is not more than 1.5 Å;     (b) employing computational means to perform a fitting operation between the chemical entity and said computer model of at least one region of the monomers of the BtEcR/BtUSP heterodimer LBD; and     (c) analysing the results of said fitting operation to quantify the association between the chemical entity and at least one region of the BtEcR/BtUSP heterodimer LBD model.    

      In a preferred embodiment of this aspect of the invention the structural coordinates have a root mean square deviation from the backbone atoms of said amino acids of not more than 1.0 Å, and more preferably not more than 0.7 Å.  
      In a preferred embodiment the region is the ligand-binding pocket of the BtEcR subunit defined by amino adds F194, Q195, N196, Y198, E199, H200, P201, H226, I227, T228, I230, T231, L233, T234, L237, I238, F241, S242, V267, M268, M269, F270, R271, M272, R274, R275, I283, L284, F285, A286, Y296, M301, T304, L308, Y325, A326, T329, I333, M389, N390, T393, C394, L397, V404, P405, L408 and W412.  
      In another embodiment the region is the interface between the BtEcR and BtUSP subunits defined by BtEcR residues H314, M315, I331, S335, E336, R337, P338, E347, Q350, E351, I354, E355, K358, T370, T371, F373, A374, K375, L377, S378, L380, T381, E382, R384, T385 and N388 on one hand and BtUSP residues E342, R383, T386, E387, K391, E414, E425, E429, Y432, A433, E436, S447, G448, F450, A451, K452, L454, L455, R456, L457, P458, A459, R461, S462 and L465 on the other.  
      In a still further embodiment the region is the co-activator/co-repressor binding groove formed by helices H3 and H4 on the surface of BtEcR defined by residues I232, V235, Q236, V239, E240, K243, F248, R253, E254, Q256, I257, L260, K261, S264, S265, M268, S406, F407, L408, E410, I411 and D413.  
      As will be readily understood by persons skilled in this field the methods of the present invention provide a rational method for designing and selecting compounds which interact with the ecdysone receptor. In the majority of cases these compounds will require further development in order to increase activity. Such further development is routine in this field and will be assisted by the structural information provided in this application. It is intended that in particular embodiments the methods of the present invention includes such further developmental steps.  
      In another aspect the present invention consists in a method of assessing the interaction between a compound and the BtEcR/BtUSP heterodimer LBD, the method comprising exposing a crystalline composition comprising BtEcR/BtUSP heterodimer LBD or portion thereof or variant of these to the compound and measuring the level of binding of the compound to the crystal.  
      Accordingly, in another aspect the present invention consists in a method of designing or selecting a compound which modulates ecdysone receptor signalling, the method comprising subjecting a compound obtained by a method according to any one of the previous aspects of the present invention to biological screens and assessing the ability of the compound to modulate ecdysone receptor signalling. These screens employ cloned EcR sequences. In particular they may employ BtEcR nucleic acid sequence (SEQ ID No 1).  
      Another aspect of the present invention provides a method to guide site-directed mutagenesis of the ecdysone receptor ligand-binding domain to change residues in the ligand-binding domain and at the dimerisation interface in order to change ligand preferences.  
      For other nuclear receptor LBD&#39;s, 3D structural information has been used to identify residues involved in specific contacts with ligands. This information has been employed to guide site-directed mutagenesis of residues leading to directed changes in ligand specificity. For example, on this basis, a single E353Q replacement was made in the human estrogen receptor-α and found to causes a 9-fold reduction in transactivation potency of estradiol and a concomitant 10-140-fold increase in potency of androgens (Ekena et al., 1998).  
      Homology modelling has been previously employed to predict the structure of ecdysone receptor LBDs complexed with ecdysteroids and dibenzoyl hydrazines. The resultant models have been used to guide site-directed mutagenesis or interpret its outcomes (Kumar et al., 2002; Grebe &amp; Spindler-Barth, 2002). However, the X-ray structure for the  B. tabaci  ecdysone receptor LBD bound to ponasterone A described in the present invention reveals the previous models to inaccurately reflect important aspects of the LBD protein structures and contacts with ligands. For example, while one single point mutation, A110P, was observed to decrease responsiveness of  Choristoneura fumiferana  EcR to ecdysteroids without affecting response to non-steroidal ligands RG-102240 and RG-102317 (Kumar et al., 2002), the molecular interpretation for the underlying protein-ligand interactions postulated was incorrect. For example, their model places the alkyl chain of the bound ecdysteroid ligand close to this key residue, whereas our X-ray structure shows that it is the A/B rings of the steroid core that are located close to the corresponding residue in BtEcR (A286). The  B. tabaci  crystal structure shows that this A286 lies in the deepest (i.e. the s1-s2 β-sheet loop) part of the ligand binding pocket. The line of reasoning advanced by (Kumar et al., 2002) to interpret the insensitivity of the binding of dibenzoyl hydrazines to replacement of this Ala residue with larger residues thus actually suggests that dibenzoyl hydrazine ligands bind  
      more centrally in the cavity of the ligand binding pocket or closer to its H12 end, rather than occupying the bottom part of the pocket as suggested by these workers.  
      An understanding of the effects involved based on the X-ray structure of the ecdysone receptor (for  B. tabaci ) and homology models derived therefrom (for ecdysone receptors from other species) will facilitate future site-directed mutagenesis to achieve desirable changes in ligand selectivity. The actual residues contacting steroid in the binding site and those involved in the dimerisation interface in the X-ray structure are set out in the Results Section below under the sub-heading “Structure description”.  
      In yet a further aspect, the invention provides a method of utilizing molecular replacement to obtain structural information about a molecule or a molecular complex of unknown structure, comprising the steps of: 
      (i) crystallising said molecule or molecular complex;     (ii) collecting an X-ray diffraction data set from said crystallized molecule or molecular complex;     (iii) applying at least a portion of the structure coordinates set forth in Appendix I to the X-ray diffraction data set to generate a three-dimensional electron density map of at least a portion of the molecule or molecular complex whose structure is unknown.    

      The term “molecular replacement” refers to a method that involves generating a preliminary model of an ecdysone receptor crystal whose structure coordinates are unknown, by orienting and positioning a molecule whose structure coordinates are known (e.g. BtEcR/BtUSP LBD heterodimer coordinates from Appendix I) within the unit cell of the unknown crystal so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. This, in turn, can be subject to any of the several forms of refinement to provide a final, accurate structure of the unknown crystal (Lattman, 1985; Rossmann, 1990).  
      The present inventors have now obtained three dimensional structural information about the ligand-binding domain of the ecdysone receptor which enables a more accurate understanding of how the binding of ligand leads to signal transduction. Such information provides a rational basis for the development of ligands for specific applications, something that heretofore could not have been predicted de novo from available sequence data.  
      The precise mechanisms underlying the binding of agonists and antagonists to the ecdysone receptor are not fully clarified. However, the binding of good ligands to the receptor site, for example those with a dissociation constant in the order of 10 −8 M or lower, is understood to arise from enhanced stereochemical complementarity relative to naturally occurring ecdysone receptor ligands.  
      Such stereochemical complementarity, pursuant to the present invention, is characteristic of a molecule that matches surface residues the ligand binding pocket of EcR as enumerated by the coordinates set out in Appendix I. By “match” we mean that the identified portions interact with the surface residues, for example, via hydrogen bonding or by non-covalent Van der Waals and Coulomb interactions which promote desolvation of the biologically active compound within the site, in such a way that retention of the biologically active compound within the ligand binding pocket is favoured energetically.  
      Substances which are complementary to the shape and electrostatics or chemistry of the ligand binding site characterised by amino acids positioned at atomic coordinates set out in Appendix I will be able to bind to the receptor, and when the binding is sufficiently strong, substantially prohibit binding of the naturally occurring ligands to the site. The substance bound to the receptor may also, of its own accord and in the absence of any natural ligand, promote either the agonist or antagonist conformation of the receptor, and thereby determine the biological outcomes effected by the receptor.  
      It will be appreciated that it is not necessary that the complementarity between ligands and the receptor site extend over all residues lining the pocket in order to modulate binding of the natural ligand.  
      In general, the design of a molecule possessing stereochemical complementarity can be accomplished by means of techniques that optimise, chemically and/or geometrically, the “fit” between a molecule and a target receptor. Known techniques of this sort are reviewed by (Goodford, 1984; Beddell, 1984; Hol, 1986; Sheridan &amp; Venkataraghavan, 1987; Walters et al., 1998; Verlinde &amp; Hol, 1994; Gane &amp; Dean, 2000; Good, 2001; Langer &amp; Hoffnann, 2001); the respective contents of which are hereby incorporated by reference. See also (Blundell et al., 1987) (drug development based on information regarding receptor structure) and (Loughney et al., 1999) (database mining application on the growth hormone receptor).  
      There are two preferred approaches to designing a molecule, according to the present invention, that complements the stereochemistry of the ecdysone receptor. The first approach is to dock directly in silico molecules from a three-dimensional structural database to the receptor site, using mostly, but not exclusively, geometric criteria to assess the goodness-of-fit of a particular molecule to the site. In this approach, the number of internal degrees of freedom (and the corresponding local minima in the molecular conformation space) is reduced by considering only the geometric (hard-sphere) interactions of two rigid bodies, where one body (the active site) contains “pockets” or “grooves” that form binding sites for the second body (the complementing molecule, as ligand).  
      This approach is illustrated by (Kuntz et al., 1982), and (Ewing et al., 2001), the contents of which are hereby incorporated by reference, whose algorithm for ligand design is implemented in a commercial software package, DOCK version 4.0, distributed by the Regents of the University of California and further described in a document, provided by the distributor, which is entitled “Overview of the DOCK program suite” the contents of which are hereby incorporated by reference. Pursuant to the Kuntz algorithm, the shape of the cavity represented by the ecdysone receptor site is defined as a series of overlapping spheres of different radii. One or more extant databases of crystallographic data, such as the Cambridge Structural Database System maintained by Cambridge University (University Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, UK.), the Protein Data Bank maintained by the Research Collaboratory for Structural Bioinformatics (Rutgers University, N.J., U.S.A.), LeadQuest (Tripos Associates, Inc., St. Louis, Mo.), Available Chemicals Directory (Molecular Design Ltd., San Leandro, Calif.), and the NCI database (National Cancer Institute, U.S.A.) is then searched for molecules which approximate the shape thus defined.  
      Molecules identified in this way, on the basis of geometric parameters, can then be modified to satisfy criteria associated with chemical complementarity, such as hydrogen bonding, ionic interactions and Van der Waals interactions. Different scoring functions can be employed to rank and select the best molecule from a database. See for example (Bohm &amp; Stahl, 1999). The software package FlexX, marketed by Tripos Associates, Inc. (St. Louis, Mo.) is another program that can be used in this direct docking approach (Rarey et al., 1996).  
      The second preferred approach entails an assessment of the interaction of respective chemical groups (“probes”) with the active site at sample positions within and around the site, resulting in an array of energy values from which three-dimensional contour surfaces at selected energy levels can be generated. The chemical-probe approach to ligand design is described, for example, by (Goodford, 1984), the contents of which are hereby incorporated by reference, and is implemented in several commercial software packages, such as GRID (product of Molecular Discovery Ltd., West Way House, Elms Parade, Oxford OX2 9LL, U.K.). Pursuant to this approach, the chemical prerequisites for a site-complementing molecule are identified at the outset, by probing the active site with different chemical probes, e.g. water, a methyl group, an amine nitrogen, a carboxyl oxygen, and a hydroxyl. Favoured sites for interaction between the active site and each probe are thus determined, and from the resulting three-dimensional pattern of such sites a putative complementary molecule can be generated. This may be done either by programs that can search three-dimensional databases to identify molecules incorporating desired pharmacophore patterns or by programs which using the favoured sites and probes as input perform de novo design.  
      Programs suitable for searching three-dimensional databases to identify molecules bearing a desired pharmacophore include MACCS-3D and ISIS/3D (Molecular Design Ltd., San Leandro, Calif.) and Sybyl/3DB Unity (Tripos Associates, Inc., St. Louis, Mo.).  
      Programs suitable for pharmacophore selection and design include DISCO (Abbott Laboratories, Abbott Park, Ill.) and Catalyst (Accelrys, San Diego, Calif.).  
      Databases of chemical structures are available from a number of sources including Cambridge Crystallographic Data Centre (Cambridge, U.K.), Molecular Design, Ltd., (San Leandro, Calif.), Tripos Associates, Inc. (St. Louis, Mo.) and Chemical Abstracts Service (Columbus, Ohio).  
      De novo design programs include Ludi (Biosym Technologies Inc., San Diego, Calif.), LeapFrog (Tripos Associates, Inc.), Aladdin (Daylight Chemical Information Systems, Irvine, Calif.) and LigBuilder (Peking University, China).  
      Those skilled in the art will recognize that the design of a mimetic may require slight structural alteration or adjustment of a chemical structure designed or identified using the methods of the invention.  
      The invention may be implemented in hardware or software, or a combination of both. However, preferably, the invention is implemented in computer programs executing on programmable computers each comprising a processor, a data storage system (including volatile and non-volatile memory and/or storage elements), at least one input device, and at least one output device. Program code is applied to input data to perform the functions described above and generate output information. The output information is applied to one or more output devices, in known fashion. The computer may be, for example, a personal computer, microcomputer or workstation of conventional design.  
      Each program is preferably implemented in a high level procedural or object-oriented programming language to communicate with a computer system. However, the programs can be implemented in assembly or machine language, if desired. In any case, the language may be compiled or interpreted language.  
      Each such computer program is preferably stored on a storage medium or device (e.g. ROM or magnetic diskette) readable by a general or special purpose programmable computer, for configuring and operating the computer when the storage media or device is read by the computer to perform the procedures described herein. The inventive system may also be considered to be implemented as a computer-readable storage medium, configured with a computer program, where the storage medium so configured causes a computer to operate in a specific and predefined manner to perform the functions described herein.  
      Biological assays to measure the activity of ecdysone receptor agonists and antagonists are well known in the field. Traditional screens for ecdysone receptor agonists examine candidate compounds for an ability to induce the moulting or pupation of whole insect larvae (Becker, 1941; Cymborowski, 1989), the evagination of imaginal discs (Fristrom J. W. &amp; Yund, 1976) or morphological transformation of the Drosophila BII cell line (Clément et al., 1993). More recent assays use mammalian or other eukaryotic cells that have been co-transfected with a recombinant ecdysone receptor and a reporter gene linked to an appropriate response element Both types of screen can also be reformatted to detect non-agonist ligands (antagonists), which can be recognised by their ability to inhibit the activation the receptor by an agonist provided as a standard component of the assay (Yang et al., 1986; Oberdorster et al., 2001)(Oberdorster et al, 2001). In addition, there are in vitro binding assays in which intact insect cells, cell extracts or purified recombinant ecdysone receptors are incubated with a radioactive ecdysone receptor ligand such as  3 H-ponasterone A. These assays detect both agonists and antagonists indiscriminately because both types of ligand compete with the radioactive tracer for binding to the ecdysone receptor (Yund et al., 1978; Cherbas et al., 1988). In addition, potential agonists and antagonists may be screened for their ability to inhibit the binding of europium-labelled ecdysone receptor ligands to soluble, recombinant ecdysone receptor in a microplate-based format Europium is a lanthanide fluorophore, the presence of which can be measured using time-resolved fluorometry. The sensitivity of this assay matches that achieved by radioisotopes, measurement is rapid and is performed in a microplate format to allow high-sample throughput, and the approach is gaining wide acceptance as the method of choice in the development of screens for receptor agonists/antagonists (Appell et al., 1998; Inglese et al., 1998). Binding affinity and inhibitor potency may also be measured for candidate inhibitors using biosensor technology.  
      The three-dimensional structure ligand-binding pocket of the  B. tabadecdysone  receptor provided in the present application makes it possible to predict, by homology modelling methods, the three-dimensional structure of the ligand-binding pockets of ecdysone receptors from other organisms. For example, the program Modeler (Sali &amp; Blundell, 1993) builds homology models from the satisfaction of spatial restraints derived from the alignment of the target (i.e. an EcR LBD from other species) with the template (which would be three-dimensional structure of the BtEcR LBD this case). Differences in the ligand-binding pockets of different species can thus be modelled.  
      In a further aspect the present invention provides an isolated nucleic acid molecule comprising a nucleotide sequence which encodes at least the ligand binding domain of BtEcR, wherein the nucleotide sequence is selected from the group consisting of: 
      (i) a nucleotide sequence comprising a sequence having at least 90% identity to the sequence from nucleotide 535 to nucleotide 1248 of SEQ ID NO: 1 or the complementary nucleotide sequence;     (ii) a nucleotide sequence comprising a sequence that hybridises under high stringency conditions to the sequence from nucleotide 535 to nucleotide 1248 of SEQ ID NO: 1 or the complementary nucleotide sequence; and     (iii) a nucleotide sequence which encodes a polypeptide comprising the sequence from amino acid P179 to amino acid S416 of SEQ ID NO: 2.    

      In a preferred embodiment the nucleic acid molecule further comprises a nucleotide sequence selected from the group consisting of: 
      (i) a nucleotide sequence comprising a sequence having at least 90% identity to the sequence from nucleotide 355 to nucleotide 1248 of SEQ ID NO: 1 or the complementary nucleotide sequence;     (ii) a nucleotide sequence comprising a sequence that hybridises under high stringency conditions to the sequence from nucleotide 355 to nucleotide 1248 of SEQ ID NO: 1 or the complementary nucleotide sequence; and     (iii) a nucleotide sequence which encodes a polypeptide comprising the sequence from amino acid R119 to amino acid S416 of SEQ ID NO: 2.    

      In a further preferred embodiment the nucleic acid molecule comprises a nucleotide sequence selected from the group consisting of: 
      (i) a nucleotide sequence comprising a sequence having at least 90% identity to SEQ ID NO: 1 or the complementary nucleotide sequence;     (ii) a nucleotide sequence comprising a sequence that hybridises under high stringency conditions to SEQ ID NO: 1 or the complementary nucleotide sequence; and     (iii) a nucleotide sequence which encodes the polypeptide of SEQ ID NO: 2.    

      In a further preferred embodiment the level of identity is at least 95%, more preferably at least 97% and most preferably at least 99%.  
      In a further preferred embodiment the nucleic acid molecule comprises the sequence set out in SEQ ID NO. 1 or comprises a nucleotide sequence which encodes the polypeptide of SEQ ID NO. 2.  
      In determining whether or not two nucleotide sequences fall within these percentage limits, those skilled in the art will be aware that it is necessary to conduct a side-by-side comparison or multiple alignment of sequences. In such comparisons or alignments, differences may arise in the positioning of non-identical residues, depending upon the algorithm used to perform the alignment. In the present context, reference to a percentage identity between two or more nucleotide sequences shall be taken to refer to the number of identical residues between said sequences as determined using any standard algorithm known to those skilled in the art. For example, nucleotide sequences may be aligned and their identity calculated using the BESTFIT programme or other appropriate programme of the Genetics Computer Group, Inc., University Research Park, Madison, Wis., United States of America (Devereux et al., 1984)  
      The concept of hybridisation under high stringency conditions is a concept well understood in the art. For the purposes of defining the level of stringency as used herein “high stringency” comprises a hybridisation and/or a wash carried out in 0.1×SSC−0.2×SSC buffer, 0.1% (w/v) SDS at a temperature of at least 55° C. Conditions for hybridisations and washes are well understood by one normally skilled in the art. For the purposes of further clarification only, reference to the parameters affecting hybridisation between nucleic acid molecules is found in (Ausubel, 1992), which is herein incorporated by reference.  
      Throughout this specification, the word “comprise”, or variations such as “comprises” or “comprising” will be understood to imply the inclusion of a stated element, integer or step, or groups of elements, integers or steps, but not the exclusion of any other element, integer or step, or groups of elements, integers or steps.  
      Any discussion of documents, acts, materials, devices, articles or the like which has been included in the present specification is solely for the purpose of providing a context for the present invention. It is not to be taken as an admission that any or all of these matters form part of the prior art base or were common general knowledge in the field relevant to the present invention as it existed in Australia before the priority date of each claim of the application.  
      In order that the nature of the present invention may be more dearly understood, preferred forms thereof will now be described with reference to the following non-limiting examples.  
     Experimental  
     Methods  
      Cloning and Characterizing the EcR and USP Subunits of the  B. tabaci  Ecdysone Receptor  
      Experimental Animals and RNA Isolation  
      Animals were reared and maintained by the CSIRO Division of Entomology, Canberra. Fourth instar nymphs, collected in our laboratory in Sydney from the under-side of hibiscus leaves, were rapidly subjected to total RNA isolation using the guanidine isothiocynate-CsTFA method (Okayama et al., 1987). mRNA was subsequently purified using the PolyATract mRNA isolation kit (Promega) and quantitated in aqueous ethidium bromide under UV light.  
      Screening Probe Preparations by PCR  
      Animals were collected as described above and  B. tabaci  genomic DNA was isolated according to methods described in (Sambrook et al., 1989). To amplify a homologous  B. tabaci  EcR screening probe from the genomic DNA, two degenerate primers were employed to obtain a 165 bp product encompassing sequence encoding most of the DNA binding domain (DBD), as described by (Hannan &amp; Hill, 1997). A product of the correct size was obtained, cloned into Bluescript SK + (Stratagene), cycle sequenced (ABI Prism, Perkin-Elmer with gel separation by Australian Genome Research Facility) in both directions and subjected to database analyses by BlastA via the Australian National Genomic Information Service. The information obtained indicated that product encoded the DBD of a steroid nuclear receptor, with highest identity to  L. migratoria  EcR (Genbank accession number AF049136). Similar efforts, using degenerate primers (Tzertzinis et al., 1994), were unsuccessful in doning a USP screening probe from the  B. tabaci  genomic DNA. However, the use of library cDNA as a template yielded a product of the correct size (147 bp), and BlastA analysis of the TOPO TA (Invitrogen) cloned product revealed that this fragment had highest identity to the USP/RXR family.  
      cDNA Library Construction and Screening  
      A  B. tabaci  cDNA library was constructed from cDNA that had been oligo-dT primed (Hannan &amp; Hill, 1997) from 5 μg of high quality mRNA and cloned into a Lambda ZapII vector employing a (Stratagene) kit. This primary library, consisting of 1.9×10 6  plaque forming units (pfu), was amplified once to give a titre of 1.5×10 9  pfu/ml. Screening for EcR required the plating of 2.5×10 6  pfu on an  E. coli  XL1 Blue (Stratagene) lawn and screening for USP required 1.5×10 6  pfu. Plaques were lifted onto Hybond N (Amersham) membranes, denatured and fixed according to the manufacturer&#39;s instructions. Probes were labelled and hybridised as described (Hannan &amp; Hill, 1997). Lambda plaques were converted to pBK-CMV phagemid vector by the excision method (Stratagene) and ORF&#39;s were cycle sequenced in both directions using multiple primers and compilation employing the GCG Wisconsin package.  
      Library screening with the EcR DBD probe identified four pBK-CMV clones, three of which (pBK-CMV4, 6 and 8) were truncated in the LBD at position 1078 bp (methionine is +1). The fourth clone (pBK-CMV7) was identical at the nucleotide level to the first three but had a complete LBD (an extra 173 bp) and a 3′ UTR with polyA tail. In total, pBK-CMV7 contained a 2291 bp cDNA insert with an ORF of 1251 bp encoding a 416 aa protein. BlastN and BlastP analysis of the ORF/putative peptide revealed similarity to ecdysone receptor analogues. Specifically, highest identity was to  Locusta migratoria  EcR, which was 73% identical at the DNA level and 79% identical at the peptide level. Alignment of the encoded peptide (BtEcR) along with that of other arthropods (data not shown), reveals conservation of the nuclear receptor domains. Specifically, BtEcR exhibits the characteristic five-domain structure (A/B, C, D, E, F) with highest conservation (88% and 48% amino acid sequence identity) observed in the DBD and LBD regions, respectively. Additionally, we observe the conservation of the P and D-boxes, the regions thought to mediate hormone response element (HRE) binding (Zilliacus et al., 1995). We also observed conservation of the AF-2 ligand dependent activation region (Durand et al., 1994) with the invariant Glu410 (numbers are from BtEcR) located in the last helix of the E domain. This Glu along with Lys261 have been suggested to be implicated in salt bridge formation on the basis of homology modelling (Wurtz et al., 2000). The  B. tabaci  crystal structure does indicate a salt bridge in this vicinity but it actually involves Lys261 and Asp413 (which is also highly conserved).  
      The library was also screened with the USP DBD probe for the USP cDNA. In this screen, three positive dones were identified and after preliminary data base analysis (BlastN and BlastP) one clone, pBK-CMV21(a), revealed high sequence identity to the USP/RXR receptor family members (WO 01/02436). Of the remaining two clones, one showed no significant identity to lodged sequences and the other corresponded to the  Drosophilia  Thr3 gene. Thr3 is an orphan nuclear receptor. pBK-CMV21(a) contains a 4.2 kb cDNA insert, cloned in the reverse orientation, with a 1491 bp ORF encoding a 496 aa protein. BlastN and BlastP analysis revealed the ORF and encoded protein had highest similarity to  Locusta migratoria  RXR, the two species being 62% and 72% identical at the DNA and protein level, respectively. Interestingly, the region corresponding to the USP screening probe does not exactly match done pBK-CMV21(a), the two only being 72% identical at the DNA level (data not shown). Amino acid alignment of the putative peptide (BtUSP) along with USP/RXR from related species (data not shown) revealed the canonical domain structure (A/B, C, D, E/F) and sequence conservation strongest in the DNA binding region. We note that for this region BtUSP retains a perfect P-box and imperfect D-box, the regions implicated in DNA sequence specificity (Danielsen et al., 1989; Umesono &amp; Evans, 1989) and a perfect T-box, a region also thought to direct DNA binding (Chung et al, 1998). Additionally, the ninth heptad repeat of the LBD, a region thought to direct heterodimer formation and the selection of HRE&#39;s (Perlmann et al., 1996), is well conserved. Also present is a putative AF-2 site, a region involved in coactivator binding and transactivation (Le Douarin et al., 1995). As with EcR, the highest sequence conservation is observed in the C domain but in contrast to EcR the E/F domain was less conserved.  
      In-vitro Translation and Gel Retardation Assays  
      Gene integrity was confirmed by coupled reticulocyte lysate transcription and translation (TNT, Promega). For EcR, transcription/translation was performed with 1.0 μg of done pBK-CMV 7 utilizing the T3 promoter of the vector and  35 S methionine incorporation. For USP, however, a 1.7 kb SspI fragment encompassing the ORF was cloned into pBluescript SK (Stratagene) and then transcribed from this vector&#39;s T3 promoter. This re-cloning of BtUSP was performed to remove the lengthy (1.3 kb) 5′UTR from the pBK-CMV 21(a) insert. After these reactions, 2 μl of the mix was electrophoresed in an SDS-polyacrylamide gel according to the manufacturer&#39;s (Promega) instructions and product was detected by the Molecular Dynamics Phosphorimaging system. As anticipated, the BtEcR recombinant plasmid produced a 50 kDa protein (expected size, 47.5 kDa) and BtUSPplasmid produced a 62 kDa protein (expected size, 55.6 kDa).  
      DNA binding function was assessed by electrophoretic mobility shift assay (EMSA). For these experiments, EcR and USP proteins were translated as above but using unlabelled methionine. The EcRE probe (hsp27 response element) was prepared by α- 32 P labelling 5 pmol of annealed oligo (5′AGCTTCAAGGGTTCAATGCACTTGTCCATCG3′ and 5′AGCTCGATGGACAAGTGCATTGAACCCTTGA3′) with Klenow (GIGAPRIME Labelling Kit, Geneworks). This mix was then phenol/chloroform extracted, ethanol precipitated and resuspended in 100 μl of TE. Binding and electrophoresis were performed as described by (Molloy, 2000). For a 20 μl reaction mix, 2.5 μl of each translated extract was incubated with 8.0 μl of BufferA (20 mM HEPES pH 7.9, 100 mM KCI, 2 mM dithiothreitol (DTT), 1 mM EDTA, 20% (v/v) glycerol), 2 μl of 2% (v/v) NP-40, 1 μl BSA (10 mg/ml), 0.5 μl 2 mg/ml poly (dI-dC).poly(dI-dC), 6 μg single stranded DNA plus or minus 1 μl of 100 mM MgCl 2 . After 20 minutes at room temperature, 0.05 pmoles of labelled probe was added and the mix was incubated again for 20 minutes. One sample also had the addition of excess (1.25 pmoles) unlabelled EcRE DNA. 10 μl of the mix was analysed by electrophoresis at 4° C., 80 V in a 0.25×TBE, 5% polyacrylamide gel. After fixing and drying, radioactive species were visualized by the Molecular Dynamics Phosphorimaging system. Once DNA binding conditions had been established, the reactions were repeated (in the presence of 5mM MgCl 2 ) +/−ponasterone A. As before, probe was added after 20 minutes and electrophoresis was at 40 minutes. In one case, the order of probe and ponasterone A additions were reversed, i.e. probe was included from the beginning and ponasterone A was added after 20 minutes.  
      The results indicated that BtEcR and BtUSP bind EcRE DNA only as a heterdodimer and not as homodimers. We observed binding to be greatly enhanced in the presence of Mg 2+ . Binding specificity also was confirmed by the by successful competition with unlabelled competitor DNA. The presence of hormone (ponasterone A) clearly enhanced binding of the receptor heterodimer to EcRE when compared to binding without hormone. Again, the binding was specific and the amount of receptor-EcRE complex was reduced by the inclusion of unlabelled EcRE DNA. Adding EcRE 20 minutes before the addition of hormone did not increase the binding of receptor to EcRE.  
      The nucleotide and amino acid sequence of BtEcR are set out in SEQ ID NO. 1 and SEQ ID NO. 2, respectively.  
      The conceptually-translated amino add sequence of BtEcR is 416 residues long and displays the five domains typical of a nuclear receptor. The BtUSP protein is 496 residues in length and also displays all domains typical of a nuclear receptor. In functional assays, we demonstrated specific and co-operative binding of the BtEcR and BtUSP subunits to an ecdysone response element and showed that this phenomenon was enhanced by the addition of an ecdysteroid ligand, ponasterone A.  
      Construction of a Baculovirus for Co-expression of the Ligand-binding Domains of BtEcR and BtUSP  
      Step 1: Cloning pFastBacDual metHis 6 EcR  
      pBK-CMV7 was digested with HaeIII and PstI to excise a 1.3 kb DNA fragment (Fragment A) which encodes the BtEcR D and E domains.  
      Two oligonucleotides were synthesised (1) ncoI metHis 6  upper (CATGGGTATGAGAGGATCGCATCACCATCACCATCACAGG) and (2) ncoI metHis 6  lower (CCTGTGATGGTGATGGTGATGCGATCCTCTCATACC) treated with kinase and annealed to construct a DNA duplex (Linker A) which encodes a hexahistidine tag at the amino terminus of the BtEcR D domain.  
      pFastbac Dual (Invitrogen) was digested with NcoI and NsiI and treated with phosphatase by standard methods (Sambrook et al., 1989).  
      Fragment A and Linker A were ligated into the NcoI and NsiA treated pFastBacDual to construct pFastbac metHis 6  EcR.  
      Step 2: Cloning pFastBacDual His 6 EcR FLAG USP  
      pBK-CMV21(a) was used as template in a PCR (TdIDNA polymerase, Promega) with primers (1) avaIIusp5 (TGTCTCGCTATGGGACCGAAAAGAGAAGCC) and (2) pstusp3 (GATAATGCTGCAGATGGTGATAATT) to produce a 1370 bp DNA fragment (Fragment B) encoding the BtUSP D and E domains. A PsfI site exists in the 3′UTR of BtUSP but a 5′ AvaII site is introduced by primer avaIIusp5.  
      Two oligonucleotides were synthesised (1) BssHuspFLAGupper (CGCGCTTAACTATGGACTACAAGGACGACGATGACAAGG) and (2) avauspFLAGlower (GGTCCCTTGTCATCGTCGTCCTTGTAGTCCATAGTTAAG) treated with kinase and annealed to construct a DNA duplex (Linker B) which encodes a FLAG tag at the amino terminus of the BtUSP D domain.  
      pFastbac metHis 6 EcR was digested with BssHI(PauI) and PstI. Fragment B and Linker B were ligated into the BssHI(PauI) and PstI treated pFastBacDual to construct pFastbac His 6 EcR FLAG USP.  
      Step 3. Transposition From pFastbac His 6 EcR FLAG USP Into a Bacmid and Baculovirus Construction.  
      The mini-Tn7 expression cassette in the donor plasmid pFastbac His 6 EcR FLAG USP was transposed into a baculovirus genome by transformation into DH10Bac competent cells and selection of white colonies. White colonies were colony purified and grown up in liquid culture. Mini-preparations of Bacmid DNA were made using a alkaline lysis procedure in which attention was payed to minimisation of shear forces. The resultant DNA was monitored for the presence of high molecular weight bacmid DNA by electophoresis through a 0.5% agarose gel.  
      Mid-log phase Sf9 insect cells were transfected with bacmid DNA using Cellfectin (Invitrogen) and standard procedures and grown for 72 hours at 27° C. Virus was harvested from the culture supernatant and titrated by plaque assay.  
      Expression and Purification of Recombinant Heterodimeric EcR-USP Ligand-binding Domain  
      Pilot-scale expression of recombinant heterodimeric BtEcR-BtUSP LBD was achieved by infection of suspension cultures of Sf9, Sf21 and or Hi-5 insect cells in spinner flasks or Schott bottles on a shaker platform maintained at 27° C. Insect cells infected with the virus engineered to express BtEcR/BtUSP ligand-binding domain were shown by gel electrophoresis to contain the expressed polypeptides corresponding to the two tagged domains. The recombinant cell lysates had a greatly enhanced ability to bind the radiolabelled ecdysteroid, [ 3 H]-ponasterone A, compared to control cell lysates. These results indicated that the recombinant virus was expressing functional LBDs that were able to heterodimerise and form a recombinant  B. tabaci  receptor LBD that bound ecdysteroids with high affinity. Equilibrium binding studies with [ 3 H]-ponasterone A as ligand gave (by direct curve fitting) a K d  value of 1.21±0.17 nM.  
      Large-scale recombinant protein production was carried out in a Celligen (New Brunswick Scientific) stirred bioreactor under controlled conditions (27° C., 35 r.p.m.). Successful 5-6 L cultures yielded 70-100 g wet cells, which typically contained about 0.2 mg recombinant LBD protein per gram cells. Heterodimer could be affinity-purified from cell extracts by using a nickel chelate resin to capture the His 6 -tag of the recombinant EcR ligand-binding domain. Further purification could be achieved by subjecting the affinity-purified material to ion exchange chromatography (Pharmacia Mono-Q) or gel filtration (Pharmacia Superdex-200). All three chromatography steps were efficient (&gt;60% yield) and inexpensive. Yields were estimated from measurements of protein concentration and from binding of [ 3 H]-ponasterone A. Identity, integrity and purity were monitored by SDS-polyacrylamide gel electrophoresis (PAGE; Coomassie-stained or immunoblotted), non-denaturing PAGE, non-denaturing isoelectric focussing gels, and mass spectrometry.  
      To purify the recombinant heterodimeric LBD (with bound ecdysteroid ligand) for crystallization trials, 60-70 g recombinant cells were lysed by sonication in the presence of excess ligand (ponasterone A) and the receptor LBD-ligand complex was purified from the clarified lysate using affinity purification followed by at least one other chromatography step (see above). In the absence of reducing conditions, such as prevails in conventional crystallisation trials, disulphide bonds rapidly form within and/or between some of the recombinant LBD molecules. Fortunately, the undesirable disulphide-mediated oligomerisation could be suppressed by using thiol-specific reagents (iodoacetic acid or iodoacetamide) to modify the surface-accessible cysteine residues. The chemical modification was preferably done between the first and second chromatography steps. However, mass spectrometry suggested that such modification was introducing chemical microheterogeneity into the recombinant proteins. A way was therefore found to conduct crystallisation trials under reducing conditions in a nitrogen atmosphere (see below), which obviated the need for chemical modification. Amplified recombinant baculovirus engineered to express the heterodimeric  B. tabaci  ligand-binding domain, prepared as described above, was used to infect a 5-litre culture of Hi-5 insect cells in the a Celligen Bioreactor with a multiplicity of infection of approximately 1. Harvested at 49 h post-infection, this culture yielded 65 g wet weight of recombinant insect cells, which were snap-frozen in liquid nitrogen and stored at −70° C. The entire batch of cells was later thawed and suspended in 130 ml HEPES buffer containing sufficient ponasterone A to saturate the anticipated number of ligand-binding sites (100 mM HEPES, 40 mM KCI, 10% glycerol, 1 M EDTA, 3 mM sodium azide, 52 μM ponasterone A, 8.9 μM leupeptin, 2.7 μM pepstatin, 1.3 mM phenylmethanesulphonyl fluoride, 26 mM Na 2 S 2 O 5 , 13 mM 2-mercaptoethanol, pH 7.0, 4° C.) and sonicated to break open the cells (4 batches of equal volume, each treated with 13×5 sec pulses, with 25 sec cooling in salted ice between each pulse, on a MSE Type 11 74.MK2 sonicator fitted with a 19 mm diameter probe). The sonicates were recombined (210 ml total volume) and the ionic strength was then raised by addition of 20.8 ml 4M KCI. This sample was ultracentrifuged to pellet cellular debris (Beckman 60Ti rotor in Beckman L8-80M Ultracentrifuge: 100 000 g, 2 h, 4° C.). The supernatant was dialysed (Spectrum Spectra/Por 1 tubing, 40 cm long×5 cm diameter) for 3 h at 4° C. against 1100 ml HEPES buffer (25 mM HEPES, 40 mM KCI, 10% glycerol, 1 mM EDTA, 3 mM sodium azide, 10 mM 2-mercaptoethanol, 0.1 μM ponasterone A, pH 7.0) to lower the ionic strength. The dialysate (which had become cloudy) was clarified by centrifugation (Beckman JA14 rotor in Beckman J2-21 centrifuge, 12 000 rpm, 30 min, 4° C.). The pH was found to have dropped below pH 7, so 20 ml 0.5M HEPES pH 7.0 was added dropwise with stirring (on ice) to elevate it before snap-freezing the sample in liquid nitrogen and storing it at −70° C. To resume the purification, the sample was thawed rapidly (by shaking in a 37° C. water bath) and dialysed (Spectrum Spectra/Por 1 tubing, 40 cm long×5 cm diameter) twice for 3 h at 4° C. against 1100 ml phosphate buffer (50 mM sodium phosphate, 10% glycerol, 0.3M NaCl, 10 mM mercaptoethanol, 0.1 μM ponasterone A, 3 mM sodium azide, pH 7.4). The dialysate (200 ml total) was then snap-frozen in liquid nitrogen and stored at −70° C.  
      In the immobilized metal-ion affinity chromatography (IMAC) step, Ni-NTA-agarose was used to capture the recombinant heterodimer by way of the His 6 -tag on the BtEcR LBD. Capture, wash and elution were performed in the presence of 2-mercaptoethanol and ponasterone A, as follows. The frozen dialysate was thawed rapidly (by shaking in a 37° C. water bath) and re-clarified (Beckman JA14 rotor in Beckman J2-21 centrifuge, 12 000 rpm, 20 min, 4° C.). To the clarified protein sample was added 2 ml 2M imidazole, pH 7.4, containing 3 mM sodium azide. A 12 ml portion of a 50% slurry of Ni-NTA agarose beads (Qiagen, Cat. 30210) was washed twice with 20 ml phosphate buffer (50 mM sodium phosphate, 10% glycerol, 0.3M NaCl, 10 nM 2-mercaptoethanol, 3 mM sodium azide, pH 7.4). The washed beads were combined with the protein sample and the suspension was rotated slowly (RotoTorque: 10 rpm, 3 h, 4° C.). The beads were then pelleted by centrifugation (Beckman JA14 rotor in Beckman J2-21 centrifuge, 10 000 rpm, 20 min, 4° C.). The supernatant was removed carefully, after which the beads were transferred to a mini-column (a 20 ml syringe body clamped upright, with a disc of Whatman filter-paper serving as a frit at the base) at 4° C. Unbound proteins were removed by washing the column of beads with 120 ml phosphate buffer (50 mM sodium phosphate, 10% glycerol, 0.3M NaCl, 10 mM 2-mercaptoethanol, 20 mM imidazole, 0.5 μM ponasterone A, 3 mM sodium azide, pH 7.4) at 4° C. Specifically-bound proteins were eluted with a buffer containing a high imidazole concentration (50 mM sodium phosphate, 10% glycerol, 0.3M NaCl, 10 mM 2-mercaptoethanol, 250 mM imidazole, 3 μM ponasterone A, 3 mM sodium azide, pH 7.4). To maximise recovery, the elution buffer was applied to the column as 2×4.5 ml aliquots with a 20 min interval between each application. The eluates were combined and a portion was assayed for protein content (Pierce Coomassie Plus assay, calibrated using bovine serum albumin). The IMAC step yielded a total of 41 mg of purified receptor. This procedure typically yields a preparation in which the recombinant EcR and USP LBDs are present in approximately equal amounts. An analysis of the IMAC eluate by reducing SDS-PAGE is shown ( FIG. 4 , lane 1). The MAC eluate was snap-frozen in liquid nitrogen and stored at −70° C.  
      To resume the purification, the IMAC eluate was thawed rapidly by shaking in a 37° C. water bath. Since we had evidence that the non-denaturing detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulphonate (CHAPS) could maximise the extent of high-affinity receptor-ecdysteroid binding, the IMAC eluate was dialysed (Spectrum Spectra/Por 1 tubing, 150 mm long×15 mm diam.) twice for 3 h at 4° C. against 500 ml CHAPS-containing Tris buffer (50 mM Tris, 230 mM NaCl, 10% glycerol, 10 mM 2-mercaptoethanol, 0.5 μM ponasterone A, 2 mM CHAPS, 3 mM sodium azide, pH 7.5). Following this, any additional ligand-binding capacity was satisfied by incubating the sample overnight at 4° C. in the presence of CHAPS and a large excess of ponasterone A; this was done by transferring the dialysis bag to a 100 ml graduated cylinder containing 100 ml 50 mM Tris, 230 mM NaCl, 10% glycerol, 10 mM 2-mercaptoethanol, 61 μM ponasterone A, 2 mM CHAPS, 3 mM sodium azide, pH 7.5, and dialysing overnight at 4° C. However, since it was also feared that CHAPS might interfere with crystallisation, this additive was removed by a subsequent dialysis step into a CHAPS-free Tris buffer, and CHAPS was omitted from later stages of the purification. (It was expected that any improvements in ligand-binding stoichiometry would persist after the removal of the CHAPS so long as free ponasterone A was maintained at saturating concentrations). Thus, CHAPS was removed from the sample by dialysing it (Spectrum Spectra/Por 1 tubing, 150 mm long×15 mm diam) twice for 3 h at 4° C. against 1000 ml 50 mM Tris, 230 mM NaCl, 10% glycerol, 2 mM dithiothreitol, 0.5μM ponasterone A, 3 mM sodium azide, pH 7.5. The dialysate was supplemented to a final concentration of 3 μM ponasterone A, snap-frozen in liquid nitrogen, and stored at −70° C. To resume the purification, the sample was thawed rapidly by shaking in a 37° C. water bath. The heterodimer sample was then concentrated by ultrafiltration (Pall MicroSep-10, spun in Beckman JA-20 rotor in Beckman J2-21 centrifuge, 7500 rpm, 4° C.) until the volume of retentate was about 0.7 ml. The retentate was then supplemented with 0.1 ml fresh 16 mM dithiothreitol solution and incubated on ice, 2 h, to ensure the reduction of any disulphide bonds that might have formed during the concentration step. The sample (38 mg protein) was then split into two aliquots (so as not to overload the column) and each aliquot was purified identically by high-performance gel filtration chromatography (Pharmacia Superdex-200 HR 10/30 column, equilibrated at room temperature in 50 mM Tris, 230 mM NaCl, 10% glycerol, 2 mM dithiothreitol, 1 μM ponasterone A, 3 mM sodium azide, pH 7.5, flow rate 0.5 ml/min). The UV absorbance of the column eluate (monitored at 280 nm) indicated that a significant amount of material with molecular masses above that expected for the recombinant heterodimer complex was resolved by the column in each case. In each case, the absorbance peak for the recombinant heterodimer itself was sharp and symmetrical, and the eluate fractions (from both column runs) that corresponded to this dominant peak were pooled to provide a single sample of purified heterodimer for further processing. The pooled eluate was concentrated by ultrafiltration (Pall NanoSep-10, spun in Sigma 1K15 minifuge, 14 000 g, 4° C.). The retentate was retrieved, combined with washings of the ultrafiltration membrane, and supplemented to a final concentration of 3 μM ponasterone A. The concentrated sample was sterilized by spin-filtration (Costar Spin-X 0.22 μm cellulose acetate filter) and stored at 4° C. under nitrogen. At this stage, the recombinant heterodimer sample contained 13.2 mg protein in 0.33 ml buffer (50 mM Tris, 230 mM NaCl, 10% glycerol, 2 mM dithiothreitol, 3 μM ponasterone A, 3 mM sodium azide, pH 7.5). Analysis by SDS-PAGE confirmed the presence of the purified recombinant BtEcR and BtUSP LBDs, ( FIG. 4 , lane 2). Their gene-predicted molecular masses are 35.8 and 30 kDa, respectively, but we find that recombinant LBDs from the ecdysone receptors of many insects typically run more slowly than expected on SDS-PAGE.  
      Samples of the purified receptor complex were tested in crystallisation trials, as described below.  
      Crystallisation  
      Crystals of the BtEcR/BtUSP heterodimer ligand-binding domain were grown using the hanging drop vapour diffusion method (McPherson, 1982). The well solution contained 0.1M sodium HEPES (pH 7.5), 1.0 M ammonium dihydrogen phosphate, 4.5% trehalose and 10 mM dithiothreitol, while the drop solution contained 1 μl of protein (40 mg/ml) in 50 mM Tris HCI (pH 7.5), 0.23 M sodium chloride, 10% glycerol, 10 mM dithiothreitol, 3 mM sodium azide, and 3 μM ponasterone A, mixed with 1 μl of well solution. Crystals were also found to grow in an alternate well solution containing 0.1M Citrate (pH 5.2), 7-8.5% PEG 3350, 67 mM KH 2 PO 4  and 10 nM TCEP HCI (Tris(2-carboxyethyl)phosphine hydrochloride). The drops were set up under a nitrogen atmosphere and the plates stored at room temperature (20° C.) in a nitrogen incubator. Crystals appeared after 3 months and had a maximum dimension of 0.5 mm.  
      Data Collection  
      Crystals were transferred to a solution containing 0.1M sodium HEPES (pH 7.5), 1.0 M ammonium dihydrogen phosphate, 4.5% trehalose, 10 mM dithiothreitol and 30% glycerol, mounted in a cryoloop (Teng, 1990) and frozen in a stream of nitrogen gas at −160° C. X-ray diffraction data from the crystal were then collected on a MacSdence X-ray generator equipped with focusing mirrors, a helium path and a Rigaku R-Axis IV detector. Data processing was conducted using the HKL suite of software (Otwinowski &amp; Minor, 1997). Data statistics are presented in Table 1. The crystal had unit cell dimensions 143.01 Å×143.01 Å×84.01 Å and belonged either to space group P4 1 2 1 2 or P4 3 2 1 2.  
      Homology Modelling  
      A homology model of the BtEcR/BtUSP ligand-binding domains heterodimer was constructed using as the template, the crystal structure of the heterodimeric complex between the ligand-binding domains of human RAR-α and mouse RXR-α (RCSB id: 1DKF). The A-chain of the structure (mRXR-α) was the structural template for USP while the B-chain (hRAR-α) was the template for EcR. The fold recognition module of the program ProCeryon (ProCeryon Biosciences GmbH, Salzburg, Austria) was used to thread the respective sequences on to the structural templates, and these alignments, after some manual adjustments, were used as the input to the program Modeller (Sali &amp; Blundell, 1993) as implemented within InsightII v. 98.0 (Accelrys, Inc., San Diego, USA) to generate several three-dimensional models of the target protein complex. The model with the lowest objective function value was chosen as the best model, and its quality was checked with the programs Profiles-3D (Lüthy et al., 1992), ProsaII (Sippl, 1993) and ProCheck (Laskowski et al., 1993). It should be noted that in this model helix H12 of both EcR and of USP was in the antagonist conformation, i.e. lying in the groove between helices H3 and H4 of the respective LBD&#39;s (Renaud &amp; Moras, 2000).  
      Structure Determination  
      Structure solution proceeded via molecular replacement using the program MOLREP (Vagin &amp; Teplyakov, 1997) within the CCP4 software suite (Collaborative Computing Project No. 4, 1994). Molecular replacement employed all data to a resolution of 4.0 Å within the above homology model as the search structure. The correct solution exhibited a correlation coefficient of 0.319, convincingly above the next highest value of 0.278. The space group was verified to be P43212 and the solution demonstrated viable crystal packing of the heterodimer model. Crystallographic refinement then proceeded via simulated annealing within X-PLOR (Brünger, 1992) which reduced the crystallographic R-factor to 0.331 (Rfree=0.441), confirming that the molecular replacement solution was substantially correct. Iterative rounds of model building using O (Jones et al., 1991) and crystallographic refinement using CNS (Brünger et al., 1998) yielded a model encompassing residues P179 to V415 of BtEcR and V300 to S492 of BtUSP (employing the single-letter amino acid code for naming residues here and throughout). Electron density that could readily be interpreted as the ligand ponasterone A, was visible in the anticipated site within the BtEcR LBD (Renaud &amp; Moras, 2000). The non-planarity of the four-ring moiety allowed unambiguous assignment of ligand orientation and position. Details of the final refinement statistics are presented in Table 2. Stereochemical analysis of the structure showed that only BtEcR residue I180 and BtUSP residue T363 lay in the disallowed regions of the Ramachandran plot. Electron density associated with these residues was poor and their backbone conformation could not be modelled accurately. However, neither of these residues lay in the vicinity of the ponasterone A binding site and the accuracy of their conformation was thus highly unlikely to be of any consequence to the structural details and implications of the ponasterone A binding site. Also included in the model are three phosphate ions, presumably arising from the solution used for crystallization of the heterodimer.  
      The crystallographic R-factors in Table 2 suggested that the structure was essentially correct to the resolution determined (viz. 3.07 Å). The observed absence of residues N-terminal of BtEcR P179 and N-terminal of BtUSP V300 could be due to their being totally disordered in the crystal or due to their prior removal via contaminating proteases, or both. Analysis of SDS PAGE gels of crystals (run under reducing conditions) indicated the presence of bands at 31 kDa, 26 kDa, 23 kDa and 22 kDa, all of these being smaller than the apparent molecular weights of the freshly purified LBDs ( FIG. 4 , lane 2) and also smaller than the gene-predicted molecular masses of the intact ligand-binding domains (35.8 and 30 kDa). We thus conclude that partial proteolysis may have contributed in whole or in part to the absence of these residues.  
     RESULTS  
      Structure Description  
      The fold of the BtEcR LBD is that of a canonical nuclear hormone receptor ( FIG. 1 ). The secondary structure elements of BtUSP/BtEcR LBD discerned in this structure are located within the BTECR sequence as follows: helix H1—residues 182 to 198, helix H2—residues 202 to 211, helix H3—residues 220 to 244, helix H4—residues 252 to 264, helix H5—residues 267 to 275, strand s0—residues 275 to 277, strand s1—residues 282 to 285, strand s2—residues 288 to 291, helix H6—residues 292 to 300, helix H7—residues 304 to 319, helix H8—residues 321 to 334, helix H9—residues 342 to 364, helix H10—residues 368 to 400 and helix H12—residues 405 to 413. Thus it comprises α-helices H1 to H10 and H12, and β-strands s1 and s2 located between helices H5 and H6. An additional short β-strand (labelled here as s0) lies between helix H5 and strand s1.  
      Helix H12 in BtEcR is observed in the so-called agonist conformation (Renaud &amp; Moras, 2000). The structure of BtEcR was compared with those available for other nuclear receptors. The closest structural neighbour was the retinoic add receptor (RAR). The root-mean-square deviation of 206 (out of 237) corresponding backbone C α  atoms between the BtEcR structure and that of RAR-γ2 (RCSB id: 1EXA, in the agonist conformation) is 1.29 Å. The major difference between these structures lies in the conformation of the loop between helices H1 and H3. In RAR this loop has a random coil conformation and lies across the outer surface of the s1-s2 β-sheet loop. In EcR the segment contains an intact helix H2 which packs anti-parallel on the N-terminal portion of helix H3 and interacts with the opposite surface of the s1-s2 β-sheet loop.  
      The ligand ponasterone A was observed to lie in a totally-enclosed pocket formed by residues F194, Q195, N196, Y198, E199, H200, P201, H226, I227, T228, I230, T231, L233, T234, L237, I238, F241, S242, V267, M268, M269, F270, R271, M272, R274, R275, I283, L284, F285, A286, Y296, M301, T304, L308, Y325, A326, T329, I333, M389, N390, T393, C394, L397, V404, P405, L408 and W412 ( FIG. 2 ). The pocket has a “J-shaped” architecture, with the major part (the leg of the “J”) accommodating the ligand, plus an ancillary part (the curved tail of the “J”) existing as an extension of the major part via a narrow channel. The inner wall of the channel linking the major and ancillary parts of the pocket is formed by the side chain of residue R271. The accessible volume of the entire cavity is approximately 766 Å 3 , whilst the volume of the ponasterone A itself is 434 Å 3 , both figures calculated using VOIDOO (Kleywegt &amp; Jones, 1994). The ancillary cavity appears unoccupied in the structure presented here. The narrowness of channel connecting the major and ancillary parts of the pocket suggests that it in some dynamic states of the protein these two parts may become disjoint rather than forming a single topological entity.  
      Potential hydrogen bonds between individual protein atoms and ligand are as follows: A286 N to the ponasterone A hydroxyl at C-6, T234 O γ1  to the ponasterone A hydroxyl at C-14, T231 O γ1  to the ponasterone A hydroxyl at C-14, R271 NH1 to the ponasterone A hydroxyl at C-2, E199 O to the ponasterone A hydroxyl at C-2, E199 O to the ponasterone A hydroxyl at C-3, Y296 OH to the ponasterone A hydroxyl at C-20 ( FIG. 2 ). The remainder of the contacts between ligands and protein are overwhelmingly hydrophobic in nature and formed by contacts between the side chains of residues P201, I227, T228, I230, M268, R271, M272, R275, I283, F285, A286, M301 and W412 and the ligand. The hydrogen bond between the side-chain of Y296 and the C-20 hydroxyl of ponasterone A probably explains the importance for high-affinity binding of having a C-20 hydroxyl group in the ecdysteroid. The Tyr at position 296 (of BtEcR) is completely conserved across insect orders, suggesting that this hydrogen bond may be a general feature of high-affinity ecdysteroid binding by EcR. The significance of this interaction was not apparent from earlier homology models of EcR (Wurtz et al., 2000; Kasuya et al., 2003).  
      Helix H12 was observed to lie in the so-called agonistic conformation (Renaud &amp; Moras, 2000) possibly locking the ligand into the site via the side chain of W412 which hangs into the ligand-binding site. A salt bridge between BtEcR residues D413 and K261 appears to stabilize the C-terminus of H12. In this conformation a co-activator can bind to a site that includes H12 and the surface of the hydrophobic cleft between helices H3 and H4. The molecular detail of this cleft is presented in  FIG. 3 . Side chains forming the deft and its immediate surrounds include those of residues V235, Q236, V239, E240, K243, F248, R253, Q256, I257, L260, K261, S264, S265 and M268. This groove is totally conserved across all ecdysone receptor sequences displayed in Table 5, apart from the residue R253. This residue lies at the distal end of the binding groove (with respect to the position of H12 shown in this structure) and it is unclear at this stage whether or not its side chain interacts with the co-repressor or co-activator upon binding of these elements.  
      The structure of the BtUSP protein closely resembles that of other published USP structures (Billas et al., 2001; Clayton et al., 2001) but with the following major difference. The secondary structure elements of BtUSP/BtEcR LBD discerned in this structure are located within the BtUSP sequence as follows: helix H3—residues 301 to 321, helix H4—residues 328 to 339, helix H5—residues 340 to 353, strand s1 residues 359 to 361, strand s2—residues 365 to 367, helix H6—residues 371 to 376, helix H7—residues 380 to 396, helix H8—residues 399 to 411, helix H9—residues 420 to 443, helix H10—residues 448 to 466 and helix H12—residues 481 to 491. No electron density was visible for residues prior to V300, i.e. helix H1, and part of the loop connecting H1 to H3 are totally unobserved. Part of the volume occupied by these structural elements in other USP structures is now occupied by the H10-H12 loop. H12 lies in the so-called antagonistic conformation (Renaud &amp; Moras, 2000). The helix H11 appears not to be formed. No ligand was observed in the site corresponding to that occupied by phospholipid in the two above published structures, and indeed part of that binding site is now occluded by a repositioning of the H10-H12 loop, and by a repositioning of helix H6 and residues immediately adjacent to this element (residues 371 to 384). The repositioning of the H10-H12 loop likely arises from the absence of residues prior to H3 in our structure, allowing this element to collapse into the region normally occupied by the H1-H3 loop in the intact USP ligand-binding domains. Part of the movement of the H10-H12 loop may be caused by the involvement of that loop in a crystal contact with a neighbouring molecule in our structure.  
      The dimeric association between BtEcR and BtUSP ligand-binding domains resembles that of the corresponding RAR-RXR complex. These two heterodimeric structures can be overlaid with an root-mean-square deviation of 1.37 Å for 339 matched Cα atoms. The interface is formed by EcR residues contained in H9, H10 and the loop between H8 and H9 on one hand and USP residues contained in H7, H9, H10 and the loop between H6 and H7 on the other (see Table 5). Residues involved in the interface include BtEcR residues H314, M315, I331, S335, E336, R337, P338, E347, Q350, E351, I354, E355, K358, T370, T371, F373, A374, K375, L377, S378, L380, T381, E382, R384, T385 and N388 on one hand and BtUSP residues E342, R383, T386, E387, K391, E414, E425, E429, Y432, A433, E436, S447, G448, F450, A451, K452, L454, L455, R456, L457, P458, A459, R461, S462 and L465 on the other. The interface was estimated by computing all residues with any atom&#39;s van der Waals surface within 1.4 Å of that of any atom of the opposite chain followed by visual inspection.  
      Potential inter-chain salt bridges include those from USP E429 to EcR K375, USP K391 to EcR E336, USP K391 to EcR E347, USP K452 to EcR E351 and USP E425 to EcR K375. Out of these, only the salt bridge between EcR E347 and USP K391 is conserved across all species (although the Dipteran  Chiromus tentans  EcR has Asp instead of Glu at the position corresponding to residue 347 in BtEcR), and compounds which bind to the interface and disrupt a particular salt bridge could be the basis of specific antagonists.  
      Hydrogen bonds occur between the side chains of USP S447 and the side chain of EcR E355A, between the backbone carbonyl of USP S447 and the side chain of EcR K358 and between the side chains of EcR R384 and USP S462. The remainder of the contacts are hydrophobic in nature. A single phosphate ion is included in the interface, coordinated by the side chains of the EcR residue R384, the carbonyl oxygen of EcR residue E336 and the side chains of USP residues R383, E387 and R456.  
      PASS (Brady &amp; Stouten, 2000) shows the existence of a pocket on the BtEcR surface on the edge of the heterodimeric interface bounded by residues including A262, S265, E266, R337, R384, G387, N388 and S391 of BtEcR. PASS also shows the existence of a pocket on the BtUSP surface on the edge of the heterodimeric interface bounded by residues including K337, S338, N341, E342, K416, G464, L465, C467 and H470 of BtUSP.  
      Designing Species-specific Agonists in the EcR Pocket  
      Table 3 presents the inter-order variation apparent across a variety of Insecta EcR LBDs for those residues that line the ecdysteroid binding pocket observed in the  B. tabaci  structure. Analysis of Table 3 indicates that there are differences in the residues in the ligand binding pocket of EcRs between insect species. For example, in the hemipteran  B. tabaci  (resistant to the bisacylhydrazine compounds) residue 272 is methionine, whereas in lepidopteran species (susceptible to bisacylhydrazines) the residue at this position is a smaller valine. Attention has also been drawn to the potential importance of the residue at this position in relation to the control spectrum of bisacylhydrazine insecticides in the communication by Billas et al. (2003) reporting the crystal structure of the lepidopteran  Heliothis virescens  EcR/USP heterodimeric LBD. It is apparent from Table 3 of the present application that the methionine at position 272 is present in the  Hemiptera, Diptera, Orthoptera  and  Coleoptera  while the residue in this position of the  Lepidoptera  is valine. The  Lepidoptera, Diptera  and  Coleoptera  have been shown to be susceptible to bisacylhydrazines in varying degrees generally correlating with the binding affinities of their ecdysone receptors for the agonists (Dhadialla et al, 1998). Furthermore our laboratory has carried out in vitro binding studies employing purified recombinant LBDs to demonstrate significant affinity of a dipteran ( Lucilia cuprina ) receptor and only very low affinity of the whitefly ( B. tabaci ) receptor for RH5992 (unpublished results). Clearly the response to bisacylhydrazines is not simply dependent on the residue at the position corresponding to 272 in  B. tabaci.    
      We propose that the methionine residue at position 272 in  B. tabaci  does not act as a single determinant but that it has a synergistic effect with leucine 308 and methionine 389, and that the collective length, bulk and charge state of these side chains may lead to changes in the shape and affinity of the binding pocket for various agonists/antagonists. A methionine at position 389 is only found in the Hemiptera and Arachnida. Using this triplet of residues as an example, and assuming the binding pocket remains essentially the same in gross topography, the overall reduction in side-chain bulk at residues 272, 308 and 389 in the lepidopteran EcR creates an additional bulge in the lepidopteran pocket helping to accommodate the bisacylhydrazines.  
      A comparison of the ecdysteroid binding pockets of the hemipteran BtEcR and lepidopteran HvEcR shows that the triptych of residues discussed in the previous paragraph is largely responsible for differences in the pocket shape near the unoccupied region adjacent to C22-OH of ponasterone A in BtEcR. In HvEcR this unoccupied region is extended into a pronounced bulge in the ecdysteroid bound pocket (see distinct bulge in the HvEcR pocket at top left of  FIG. 8 ). Least squares alignments of the protein backbone C-alpha atoms of the EcR domains of all three structures, BtEcR (ponasterone A bound) HvEcR 1R1K (ponasterone A bound) and HvEcR 1R20 (synthetic agonist BYI06830 bound) places the A and B rings of the agonist BYI06830 in the vicinity of, but not enclosed by, this extra bulge in the HvEcR 1R1K ecdysteroid bound pocket. In the lepidopteran HvEcR 1R20 structure this bulge is further extended, probably by induced fit, to accommodate the synthetic agonist. We propose that in the hemipteran BtEcR structure, the absence of the bulge in this region of the potential binding pocket conformation would prevent initial binding of many of the bisacylhydrazines and subsequent expansion of the bulge by an induced-fit mechanism.  
      Clearly other changes in binding site residues which occur between orders, as detailed in Table 3, would alter the topography of the binding site, allowing for taxon-specific design of steroids or small molecule mimetics, which exploit these differences. Such design would be implemented using tools available to those skilled in the art as described above. M389 is found towards the C-terminus of H10/11 and the pocket opening that is closed by H12 on agonist binding. M389 makes minimal contact with the ponasterone A ligand; however, mutation of this residue to a smaller side chain such as valine, found in the  Lepidoptera , or glycine as found in the  Arachnida , could weaken the interaction between H11 and H7. This weakening appears to open up the binding site towards the C-terminus of H10/11 revealing the conserved L308 and highly conserved L386 as forming a hydrophobic indentation, potentially capable of accommodating ligand antagonist/agonists with bulky substituents such as a t-butyl group or even a benzene ring as found in some of the bisacylhydrazines.  
      The X-ray structure provides a precise description of the relative positions in three-dimensional space of the residues lining the binding pocket of BtEcR. The ecdysteroid ligand, ponasterone A, fits snugly into the major part of the binding pocket, with almost all receptor-free volume over the rigid steroid framework being occupied ( FIG. 2 ).  
      However, certain sites of extension are available as follows. There is a small pocket near the C20/C21 region of the ecdysteroid which is not fully occupied (as described two paragraphs above), and a larger volume beyond the terminus of the steroid alkyl chain which is also unfilled. There is significant receptor pocket volume not occupied by the ligand below and at the terminus of the alkyl chain. This larger, partially filled region is bounded by L408, V404, N390, C394, L408, I227, T228, T231, T393 and P405 as  FIG. 5  shows. The region denoted as the ancillary part of the binding pocket (the curved part of the ‘J’) may also be available for occupation by ligands, depending on the accessibility of this pocket  
      Clearly the BtEcR LBD X-ray structure could be used, together with molecular modelling methods well known to those skilled in the art, to design modifications of the steroid which better fill the receptor volume.  
      Alternatively, synthetic organic molecules could be designed by taking account of the properties of the residues lining the binding site, and using methods such as GRID (Goodford, 1984) to locate regions favourable for binding of particular substituents. Such substituents could be linked together by a scaffold or other molecular framework to present the ligand binding groups in optimum three-dimensional orientation to interact with complementary binding groups in the binding site. This can be done manually by a person skilled in the art, or in an automated fashion using programs such as LeapFrog (Tripos Associates, Inc., St. Louis, Mo.).  
      Another alternative would be that the three-dimensional orientation of complementary binding groups in the protein (derived from knowledge of the X-ray structure of the receptor) could be used as a pharmacophore query for database searching. This would identify molecules with correctly oriented functional groups which would be putative ligands for the receptor.  
      Another alternative would be using the shape and properties of the binding site obtained from the X-ray structure of the receptor as a database query directly. Programs such as DOCK (Ewing et al., 2001; Kuntz et al., 1982) and FlexX (Rarey et al., 1996) can use this type of information to search through databases of real or hypothetical molecules to find ones with the correct properties to bind to the receptor.  
      An example of how this can be done uses the program FlexX to dock known and putative ligands into the binding site of the EcR. The receptor structure was pre-processed to add all hydrogen atoms to the amino acids, and charges were applied using standard rules. A region within 6.5 Å of the ponasterone A ligand bound into the site was used for the FlexX calculations. To assess that the program was able to use the X-ray data to correctly dock ligands, the ponasterone A ligand was extracted from the X-ray structure, energy minimized and re-docked into the binding site. The FlexX program docked the ponasterone A ligand into a binding pose essentially identical to that in the X-ray structure (RMS 0.79 Å) with a very favourable docking score (−23.92). The quality of the docking results can be seen in  FIG. 6 .  
      In another docking experiment with FlexX, the score for the ponasterone A ligand was −28.4. In the same experiment a number of other potent EcR steroidal ligands gave the following scores:- muristerone A −27.6, 20-hydroxyecdysone −29.0, inokosterone −31.7. The highest ranked poses bound to the EcR in a similar mode to that of ponasterone A, and they exhibited similar binding scores to that computed for ponasterone A.  
      As a further example, several small synthetic molecules were docked into the EcR X-ray structure using FlexX. These were: bisacylhydrazines I and RH5992 (which show negligible binding in BtEcR competitive binding assay with [ 3 H]-ponasterone A as tracer); an oxadiazole derivative II (also negligible binding); an oxazolidinone derivative III (weak-moderate binding in assay); thiotetrahydroimidazole derivative IV (weak-moderate binding in assay).  
                 
 
      FlexX docking calculations were unable to find any binding poses in the BtEcR pocket which scored well with relatively low internal energy for the bisacylhydrazines (I and RH5992) and the oxadiazole derivative (II). However the two weak-moderate binding ligands, III and IV, were successfully docked into the EcR X-ray structure with relatively low internal strain and favourable docking scores (−14.9 and −15.8 respectively). Both of these compounds had FlexX binding poses which oriented their structures over the C/D rings of ponasterone A X-ray structure, and the alkyl chain of the steroid. An example of a successful docking pose for one of these small, synthetic ligands, the oxazolidinone derivative III, is given in  FIG. 7 .  
      Designing Compounds that Target the BtEcR/BtUSP Interface and Alter the Quaternary Association of these Molecules.  
      In a further aspect of this invention compounds (non-peptidic, peptidic or peptidomimetic) can be designed that mimic the USP component of the heterodimer interface. Details of residues forming this interface and their variation across orders are given in Table 4. Such compounds may bind to the EcR monomer and prevent the formation of a functional EcR USP heterodimer. Such design would utilize the conformational detail of the EcR/USP interface revealed in this application. Such design would also utilize the detail of the ligand binding interactions to identify ligand derivatization sites that could be used to disrupt the conformations and hence the interactions of the EcR helices involved in dimerization. Similarly compounds can be designed that mimic the EcR component of the heterodimer interface and so bind to the USP component, again preventing formation of the functional EcR/USP heterodimer.  
      Design of such compounds is feasible for the estrogen receptor, see for example (Yudt &amp; Koide, 2001). Rational interface peptide design has been demonstrated in a variety of other protein-protein interactions (Singh et al., 2001; Berezov et al., 2002).In addition, compounds can be designed/selected so as to bind into either of the two ‘pockets’ associated with the interface and form the basis of platforms to create steric hindrance to the process of heterodimerization and thus inhibit the function of the ecdysone receptor.  
      Designing Compounds that Target the BtEcR Co-activator/co-repressor Binding Cleft  
      In a further aspect of this invention compounds can be designed based on the BtEcR structure to target the co-activator/co-repressor binding cleft, and thereby be capable of acting as agents that modulate transactivation (Tran et al., 2001; Westin et al., 1998). This site is formed by two antiparallel helices, H3 and H4 and presents a groove into which the co-activator or co-repressor would bind. Co-activators have a conserved LXXLL motif (the “NR” box) which has been shown in studies of other nuclear receptors to form part of an amphipathic helix which interacts with the H3/H4 cleft via the leucines. Also involved in this interaction are the highly conserved glutamate in H12 and lysine in H3. On this basis it becomes possible to those skilled in the art to design peptides or peptidominmetics that mimic the binding of the co-activator NR box to the deft, utilizing the conformational detail of the EcR H3/H4 cleft presented here. Such compounds would have the potential to modulate the transactivational state of the receptor. This groove is substantially conserved across all known EcR sequences (Table 5).  
      It will be appreciated by persons skilled in the art that numerous variations and/or modifications may be made to the invention as shown in the specific embodiments without departing from the spirit or scope of the invention as broadly described. The present embodiments are, therefore, to be considered in all respects as illustrative and not restrictive.  
     TABLES  
     
       
         
           
               
             
               
                 TABLE 1 
               
               
                   
               
               
                   
               
               
                 X-ray data collection statistics 
               
               
                   
               
             
            
               
                   
               
            
           
           
               
               
               
            
               
                   
                 No. frames 
                 302 
               
               
                   
                 Oscillation angle (°) 
                 0.5 
               
               
                   
                 No. measurements 
                 191046 
               
               
                   
                 No. reflections 
                 16725 
               
               
                   
                 Multiplicity 
                 11.8 (10.5) 1   
               
               
                   
                 Resolution range (Å) 
                 30.0-3.07 
               
               
                   
                 Completeness (%) 
                 99.9 (100.0) 
               
               
                   
                 &lt;I/σ(I)&gt; 
                 19.3 (5.6)  
               
               
                   
                   
               
               
                   
                     1 Numbers in parenthesis refer to the statistic in the highest resolution shell.    
               
            
           
         
       
     
     
       
         
           
               
             
               
                 TABLE 2 
               
               
                   
               
               
                   
               
               
                 Crystallographic refinement statistics 
               
               
                   
               
             
            
               
                   
               
            
           
           
               
               
               
            
               
                   
                 Resolution range (Å) 
                 100-3.07 
               
               
                   
                 Total no. of reflections used 
                 16756 
               
               
                   
                 Crystallographic R-factor 
                 0.203 
               
               
                   
                 Free R-factor (5% of total reflections) 
                 0.275 
               
               
                   
                 No. of protein atoms 
                 3475 
               
               
                   
                 No. of ligand + solvent atoms 
                 53 
               
               
                   
                 Root-mean-square deviation of bond 
                 0.012 
               
               
                   
                 lengths from ideality (Å) 
               
               
                   
                 Root-mean-square deviation of bond 
                 1.56 
               
               
                   
                 angles from ideality (°) 
               
               
                   
                   
               
            
           
         
       
     
     
       
         
           
               
             
               
                 TABLE 3 
               
             
            
               
                   
               
               
                   
               
               
                 Residues lining the ponasterone A binding pocket in BtEcR and their 
               
               
                 inter-order variation across the sequences 
               
            
           
           
               
               
               
               
               
               
               
               
               
            
               
                   
                 lining atoms 
                 Hemiptera 
                 Diptera 
                 Lepidoptera 
                 Orthoptera 
                 Coleoptera 
                 Arachnida 
                 Crustacea 
               
               
                   
                   
               
            
           
           
               
               
               
               
               
               
               
               
               
            
               
                 F194 
                 2M 
                 F 
                 Y 
                 Y 
                 F 
                 F 
                 Y 
                 Y 
               
               
                 Q195* 
                 4M, 5S 
                 Q 
                 Q 
                 Q 
                 Q 
                 Q 
                 Q 
                 Q 
               
               
                 N196 
                 1M 
                 N, D 
                 D 
                 D, E 
                 N 
                 N 
                 Q 
                 E 
               
               
                 Y198 
                 4M, 1S 
                 Y 
                 Y 
                 Y 
                 Y 
                 Y 
                 F 
                 F 
               
               
                 
                   E199 
                 
                 4M, 5S 
                 E 
                 E 
                 E, D 
                 E 
                 E 
                 E 
                 E 
               
               
                 
                   H200 
                 
                 3M, 4S 
                 H, A 
                 Q 
                 Q 
                 S 
                 H 
                 S 
                 Q 
               
               
                 
                   P201* 
                 
                 2M, 3S 
                 P 
                 P 
                 P 
                 P 
                 P 
                 P 
                 P 
               
               
                 
                   H226 
                 
                 2M 
                 H, I 
                 H, Y 
                 Q 
                 H 
                 H 
                 H 
                 H 
               
               
                 
                   I227* 
                 
                 4M, 4S 
                 I 
                 I 
                 I 
                 I 
                 I 
                 I 
                 I 
               
               
                 
                   T228* 
                 
                 4M, 3S 
                 T 
                 T 
                 T 
                 T 
                 T 
                 T 
                 T 
               
               
                 
                   I230 
                 
                 4M, 4S 
                 I, M 
                 I, V 
                 M 
                 I 
                 I 
                 M 
                 I 
               
               
                 
                   T231* 
                 
                 2M, 3S 
                 T 
                 T 
                 T 
                 T 
                 T 
                 T 
                 T 
               
               
                 
                   L233* 
                 
                 3M, 3S 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
               
               
                 
                   T234* 
                 
                 3M, 3S 
                 T 
                 T 
                 T 
                 T 
                 T 
                 T 
                 T 
               
               
                 L237* 
                 2M, 3S 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
               
               
                 I238* 
                 4M, 4S 
                 I 
                 I 
                 I 
                 I 
                 I 
                 I 
                 I 
               
               
                 F241* 
                 2M, 7S 
                 F 
                 F 
                 F 
                 F 
                 F 
                 F 
                 F 
               
               
                 S242 
                 2M, 2S 
                 S, A 
                 A 
                 A 
                 A 
                 A 
                 S 
                 S 
               
               
                 V267 
                 3M, 3S 
                 V, A 
                 V 
                 V 
                 V 
                 V 
                 V 
                 V 
               
               
                 
                   M268* 
                 
                 3M, 3S 
                 M 
                 M 
                 M 
                 M 
                 M 
                 M 
                 M 
               
               
                 
                   M269* 
                 
                 2M, 4S 
                 M 
                 M 
                 M 
                 M 
                 M 
                 M 
                 M 
               
               
                 F270 
                 3M, 3S 
                 F 
                 L 
                 L 
                 F 
                 F 
                 L 
                 L 
               
               
                 
                   R271* 
                 
                 4M, 7S 
                 R 
                 R 
                 R 
                 R 
                 R 
                 R 
                 R 
               
               
                 
                   M272 
                 
                 4M, 4S 
                 M, V 
                 M 
                 V 
                 M 
                 M 
                 G 
                 A 
               
               
                 
                   R274* 
                 
                 2M, 6S 
                 R 
                 R 
                 R 
                 R 
                 R 
                 R 
                 R 
               
               
                 
                   R275 
                 
                 1M, 6S 
                 R, K 
                 R 
                 R 
                 R 
                 R 
                 K 
                 R 
               
               
                 I283 
                 1M, 4S 
                 I 
                 I 
                 V 
                 I 
                 I 
                 I 
                 I 
               
               
                 
                   L284 
                 
                 4M 
                 L, V 
                 F 
                 L, M 
                 L 
                 L 
                 V 
                 V 
               
               
                 
                   F285* 
                 
                 4M, 7S 
                 F 
                 F 
                 F 
                 F 
                 F 
                 F 
                 F 
               
               
                 
                   A286 
                 
                 2M, 1S 
                 A 
                 A 
                 A 
                 A 
                 V 
                 A 
                 G 
               
               
                 
                   Y296* 
                 
                 5S 
                 Y 
                 Y 
                 Y 
                 Y 
                 Y 
                 Y 
                 Y 
               
               
                 
                   M301 
                 
                 4S 
                 M, L 
                 M, V 
                 M, F 
                 M 
                 M 
                 V 
                 L 
               
               
                 
                   T304 
                 
                 1M, 3S 
                 T, A 
                 N, T 
                 V 
                 T 
                 T 
                 S 
                 S 
               
               
                 
                   L308 
                 
                 4S 
                 L, Q 
                 L 
                 L 
                 M 
                 L 
                 L 
                 L 
               
               
                 Y325 
                 1M, 4S 
                 Y 
                 Y 
                 Y, F 
                 Y 
                 Y 
                 Y 
                 Y 
               
               
                 A326* 
                 1M, 1S 
                 A 
                 A 
                 A 
                 A 
                 A 
                 A 
                 A 
               
               
                 T329 
                 3S 
                 T 
                 T 
                 T 
                 T 
                 T 
                 T 
                 A 
               
               
                 I333* 
                 2S 
                 I 
                 I 
                 I 
                 I 
                 I 
                 I 
                 I 
               
               
                 
                   M389 
                 
                 2M, 4S 
                 M, E 
                 Q K 
                 Q 
                 Q 
                 Q 
                 M 
                 I 
               
               
                 
                   N390* 
                 
                 4M 4S 
                 N 
                 N 
                 N 
                 N 
                 N 
                 N 
                 N 
               
               
                 
                   T393 
                 
                 3M, 3S 
                 T, L 
                 M 
                 M 
                 M 
                 M 
                 M 
                 M 
               
               
                 
                   C394* 
                 
                 2M, 2S 
                 C 
                 C 
                 C 
                 C 
                 C 
                 C 
                 C 
               
               
                 
                   L397* 
                 
                 2S 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
               
               
                 
                   V404 
                 
                 1M, 3S 
                 V 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
               
               
                 
                   P405* 
                 
                 1M, 2S 
                 P 
                 P 
                 P 
                 P 
                 P 
                 P 
                 P 
               
               
                 
                   L408* 
                 
                 3S 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
               
               
                 
                   W412* 
                 
                 4S 
                 W 
                 W 
                 W 
                 W 
                 W 
                 W 
                 W 
               
               
                   
               
               
                   “*” indicates total conservation across all sequences considered.    
               
               
                   The column headed “lining atoms” indicates the number of side chain atoms (S) and the number of main chain atoms (M) involved in forming the cavity wall.    
               
               
                   Underlined residues are those judged to form the major part of the ponasterone A binding cavity, the remainder forming the walls of the ancillary part of the ponasterone A binding cavity.    
               
            
           
         
       
     
     
       
         
           
               
             
               
                 TABLE 4 
               
               
                   
               
               
                   
               
               
                 Residues forming the BtEcR/BtUSP LBD interface and their 
               
               
                 inter-order variation across the sequences 
               
               
                   
               
             
            
               
                 (a) BtEcR residues 
               
            
           
           
               
               
               
               
               
               
               
               
            
               
                   
                 Hemiptera 
                 Diptera 
                 Lepidoptera 
                 Orthoptera 
                 Coleoptera 
                 Arachnida 
                 Crustacea 
               
               
                   
               
               
                 H314 
                 H, F 
                 Q 
                 C 
                 Q 
                 T 
                 K 
                 S 
               
               
                 M315 
                 M 
                 M 
                 M 
                 M 
                 M 
                 M 
                 L 
               
               
                 I331 
                 I 
                 I 
                 I, V 
                 I 
                 I 
                 I 
                 I 
               
               
                 S335 
                 S 
                 S 
                 S 
                 S 
                 S 
                 S 
                 S 
               
               
                 E336 
                 E, S 
                 D 
                 D 
                 E 
                 E 
                 E 
                 E 
               
               
                 R337 
                 R 
                 R 
                 R 
                 R 
                 R 
                 R 
                 R 
               
               
                 P338 
                 P 
                 P 
                 P 
                 P 
                 P 
                 P 
                 P 
               
               
                 E347 
                 E 
                 E 
                 E 
                 E 
                 E 
                 E 
                 E 
               
               
                 Q350 
                 Q 
                 Q 
                 Q 
                 Q 
                 Q 
                 Q 
                 Q 
               
               
                 E351 
                 E 
                 S 
                 R 
                 E 
                 E 
                 E 
                 E 
               
               
                 I354 
                 I, L 
                 T, I 
                 L 
                 L 
                 L 
                 I 
                 L 
               
               
                 E355 
                 E 
                 D 
                 N 
                 E 
                 E 
                 E 
                 E 
               
               
                 K358 
                 K 
                 K, R 
                 R 
                 K 
                 R 
                 R 
                 K 
               
               
                 T370 
                 T 
                 S, L 
                 S, A, P 
                 G 
                 G 
                 K 
                 N 
               
               
                 T371 
                 T, V 
                 V 
                 V 
                 T 
                 T 
                 N 
                 M 
               
               
                 F373 
                 F, Y 
                 F, Y 
                 F, Y 
                 F 
                 F 
                 F 
                 F 
               
               
                 A374 
                 A 
                 A 
                 G, A 
                 A 
                 A 
                 A 
                 A 
               
               
                 K375 
                 K, R 
                 K 
                 K, R 
                 K 
                 K 
                 R 
                 K 
               
               
                 L377 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
               
               
                 S378 
                 S 
                 G, S 
                 G, S 
                 S 
                 S 
                 S 
                 N 
               
               
                 L380 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
               
               
                 T381 
                 T 
                 T 
                 S, T 
                 T 
                 T 
                 T 
                 T 
               
               
                 E382 
                 E 
                 E 
                 E 
                 E 
                 E 
                 E 
                 E 
               
               
                 R384 
                 R 
                 R 
                 R 
                 R 
                 R 
                 R 
                 R 
               
               
                 T385 
                 T 
                 T 
                 T, S 
                 T 
                 T 
                 T 
                 T 
               
               
                 N388 
                 N 
                 N 
                 M, T 
                 N 
                 N 
                 N 
                 N 
               
               
                   
               
            
           
           
               
            
               
                 (b) BtUSP residues 
               
            
           
           
               
               
               
               
               
               
               
            
               
                   
                 Hemiptera 
                 Diptera 
                 Lepidoptera 
                 Orthoptera 
                 Hymenoptera 
                 Coleoptera 
               
               
                   
               
               
                 E342 
                 E 
                 E 
                 E 
                 E 
                 E 
                 E 
               
               
                 R383 
                 R 
                 R 
                 R 
                 R 
                 R 
                 R 
               
               
                 T386 
                 T 
                 S, C 
                 S 
                 T 
                 S 
                 S 
               
               
                 E387 
                 E 
                 E 
                 E 
                 E 
                 E 
                 E 
               
               
                 K391 
                 K 
                 K 
                 K 
                 K 
                 K 
                 K 
               
               
                 E414 
                 E, G 
                 D 
                 D 
                 E 
                 E 
                 T 
               
               
                 E425 
                 E, Q 
                 E, D 
                 D, E, V 
                 E 
                 T 
                 E 
               
               
                 E429 
                 E, D 
                 E, S 
                 E 
                 E 
                 E 
                 E 
               
               
                 Y432 
                 Y 
                 Y 
                 Y, F 
                 Y 
                 Y 
                 Y 
               
               
                 A433 
                 A, V 
                 A 
                 L, S 
                 A 
                 G 
                 G 
               
               
                 E436 
                 E 
                 D 
                 D 
                 E 
                 E 
                 E 
               
               
                 S447 
                 S, P 
                 D 
                 E 
                 P 
                 A 
                 P 
               
               
                 G448 
                 G 
                 G 
                 G 
                 G 
                 G 
                 G 
               
               
                 F450 
                 F 
                 F 
                 F 
                 F 
                 F 
                 F 
               
               
                 A451 
                 A 
                 A 
                 A 
                 A 
                 A 
                 A 
               
               
                 K452 
                 K 
                 Q 
                 A, S 
                 K 
                 K 
                 K 
               
               
                 L454 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
               
               
                 L455 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
               
               
                 R456 
                 R 
                 R 
                 R 
                 R 
                 R 
                 R 
               
               
                 L457 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
               
               
                 P458 
                 P 
                 P 
                 P 
                 P 
                 P 
                 P 
               
               
                 A459 
                 A, S 
                 S 
                 S 
                 A, S 
                 S 
                 S 
               
               
                 R461 
                 R 
                 R 
                 R 
                 R 
                 R 
                 R 
               
               
                 S462 
                 S 
                 S 
                 S 
                 S 
                 S 
                 S 
               
               
                 L465 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
               
               
                   
               
            
           
         
       
     
     
       
         
           
               
             
               
                 TABLE 5 
               
             
            
               
                   
               
               
                   
               
               
                 Residues forming the BtEcR LBD co-activator/co-repressor binding groove and their 
               
               
                 inter-order variation across the sequences. 
               
            
           
           
               
               
               
               
               
               
               
               
            
               
                   
                 Hemiptera 
                 Diptera 
                 Lepidoptera 
                 Orthoptera 
                 Coleoptera 
                 Arachnida 
                 Crustacea 
               
               
                   
                   
               
            
           
           
               
               
               
               
               
               
               
               
            
               
                 I232 
                 I 
                 I 
                 I 
                 I 
                 I 
                 I 
                 I 
               
               
                 V235 
                 V 
                 V 
                 V 
                 V 
                 V 
                 V 
                 V 
               
               
                 Q236 
                 Q 
                 Q 
                 Q 
                 Q 
                 Q 
                 Q 
                 Q 
               
               
                 V239 
                 V 
                 V 
                 V 
                 V 
                 V 
                 V 
                 V 
               
               
                 E240 
                 E 
                 E 
                 E 
                 E 
                 E 
                 E 
                 E 
               
               
                 K243 
                 K 
                 K 
                 K 
                 K 
                 K 
                 K 
                 K 
               
               
                 F248 
                 F 
                 F 
                 F 
                 F 
                 F 
                 F 
                 F 
               
               
                 R253 
                 R 
                 Q 
                 Q 
                 R 
                 Q 
                 R 
                 R 
               
               
                 E254 
                 E 
                 E 
                 P, S 
                 E 
                 E 
                 E 
                 E 
               
               
                 Q256 
                 Q 
                 Q 
                 Q 
                 Q 
                 Q 
                 Q 
                 Q 
               
               
                 I257 
                 I 
                 I 
                 I 
                 I 
                 I 
                 I 
                 I 
               
               
                 L260 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
               
               
                 K261 
                 K 
                 K 
                 K 
                 K 
                 K 
                 K 
                 K 
               
               
                 S264 
                 S 
                 S 
                 S 
                 S 
                 S 
                 S 
                 S 
               
               
                 S265 
                 S 
                 S 
                 S 
                 S 
                 S 
                 S 
                 S 
               
               
                 M268 
                 M 
                 M 
                 M 
                 M 
                 M 
                 M 
                 M 
               
               
                 S406* 
                 S, P 
                 R, K 
                 P 
                 P 
                 P 
                 P 
                 P 
               
               
                 F407* 
                 F 
                 F 
                 F 
                 F 
                 F 
                 F 
                 F 
               
               
                 L408* 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
                 L 
               
               
                 E410* 
                 E 
                 E 
                 E 
                 E 
                 E 
                 E 
                 E 
               
               
                 I411* 
                 I 
                 V, I 
                 I 
                 I 
                 I 
                 I 
                 I 
               
               
                 D413* 
                 D 
                 D 
                 D 
                 D 
                 D 
                 D 
                 D 
               
               
                   
               
               
                   The * identifies residues in H12 that would be expected to interact with co-activators but their involvement in co-repressor interactions is unknown.    
               
            
           
         
       
     
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               APPENDIX I                       The three-dimensional coordinates of the BtEcr/BtUSP LBD heterodimer       in Protein Databank format (Bernstein et al., 1977).                                                                                ATOM   1   CB   VAL   U   300   12.479   120.374   11.780   1.00   96.45   U       ATOM   2   CG1   VAL   U   300   13.280   120.902   12.976   1.00   94.22   U       ATOM   3   CG2   VAL   U   300   12.769   118.881   11.524   1.00   92.13   U       ATOM   4   C   VAL   U   300   10.448   119.789   13.212   1.00   91.04   U       ATOM   5   O   VAL   U   300   10.653   120.175   14.370   1.00   88.24   U       ATOM   6   N   VAL   U   300   10.637   122.069   12.175   1.00   91.77   U       ATOM   7   CA   VAL   U   300   10.938   120.609   12.006   1.00   93.66   U       ATOM   8   N   SER   U   301   9.797   118.659   12.928   1.00   87.56   U       ATOM   9   CA   SER   U   301   9.261   117.778   13.969   1.00   83.83   U       ATOM   10   CB   SER   U   301   8.702   116.493   13.349   1.00   82.36   U       ATOM   11   OG   SER   U   301   8.349   115.553   14.352   1.00   74.68   U       ATOM   12   C   SER   U   301   10.290   117.407   15.028   1.00   84.26   U       ATOM   13   O   SER   U   301   11.489   117.600   14.847   1.00   87.37   U       ATOM   14   N   ASP   U   302   9.812   116.854   16.134   1.00   80.44   U       ATOM   15   CA   ASP   U   302   10.692   116.461   17.223   1.00   75.43   U       ATOM   16   CB   ASP   U   302   9.860   116.236   18.489   1.00   76.98   U       ATOM   17   CG   ASP   U   302   10.571   116.702   19.741   1.00   78.13   U       ATOM   18   OD1   ASP   U   302   11.038   117.865   19.764   1.00   77.43   U       ATOM   19   OD2   ASP   U   302   10.656   115.912   20.705   1.00   77.91   U       ATOM   20   C   ASP   U   302   11.445   115.185   16.839   1.00   71.80   U       ATOM   21   O   ASP   U   302   12.676   115.121   16.897   1.00   68.49   U       ATOM   22   N   ILE   U   303   10.688   114.170   16.439   1.00   67.67   U       ATOM   23   CA   ILE   U   303   11.266   112.904   16.035   1.00   61.72   U       ATOM   24   CB   ILE   U   303   10.193   111.814   15.922   1.00   56.36   U       ATOM   25   CG2   ILE   U   303   9.165   112.226   14.886   1.00   50.29   U       ATOM   26   CG1   ILE   U   303   10.818   110.494   15.476   1.00   53.55   U       ATOM   27   CD1   ILE   U   303   12.092   110.141   16.184   1.00   49.74   U       ATOM   28   C   ILE   U   303   11.935   113.064   14.679   1.00   64.96   U       ATOM   29   O   ILE   U   303   12.902   112.376   14.373   1.00   68.02   U       ATOM   30   N   CYS   U   304   11.422   113.973   13.860   1.00   66.56   U       ATOM   31   CA   CYS   U   304   12.003   114.175   12.548   1.00   68.23   U       ATOM   32   CB   CYS   U   304   11.138   115.090   11.694   1.00   62.87   U       ATOM   33   SG   CYS   U   304   10.279   114.150   10.444   1.00   73.57   U       ATOM   34   C   CYS   U   304   13.410   114.717   12.600   1.00   71.44   U       ATOM   35   O   CYS   U   304   14.295   114.194   11.920   1.00   75.51   U       ATOM   36   N   GLN   U   305   13.635   115.756   13.399   1.00   71.15   U       ATOM   37   CA   GLN   U   305   14.978   116.312   13.464   1.00   66.48   U       ATOM   38   CB   GLN   U   305   14.992   117.701   14.120   1.00   74.21   U       ATOM   39   CG   GLN   U   305   14.420   117.759   15.524   1.00   83.63   U       ATOM   40   CD   GLN   U   305   14.512   119.150   16.138   1.00   85.41   U       ATOM   41   OE1   GLN   U   305   13.922   120.114   15.628   1.00   84.23   U       ATOM   42   NE2   GLN   U   305   15.250   119.259   17.245   1.00   83.08   U       ATOM   43   C   GLN   U   305   15.886   115.353   14.199   1.00   57.19   U       ATOM   44   O   GLN   U   305   17.106   115.417   14.037   1.00   56.19   U       ATOM   45   N   ALA   U   306   15.298   114.457   14.997   1.00   48.54   U       ATOM   46   CA   ALA   U   306   16.101   113.458   15.708   1.00   45.61   U       ATOM   47   CB   ALA   U   306   15.261   112.698   16.717   1.00   28.22   U       ATOM   48   C   ALA   U   306   16.651   112.502   14.647   1.00   47.44   U       ATOM   49   O   ALA   U   306   17.826   112.159   14.660   1.00   55.69   U       ATOM   50   N   ALA   U   307   15.791   112.100   13.716   1.00   42.85   U       ATOM   51   CA   ALA   U   307   16.157   111.210   12.632   1.00   41.52   U       ATOM   52   CB   ALA   U   307   14.924   110.873   11.825   1.00   43.36   U       ATOM   53   C   ALA   U   307   17.188   111.885   11.740   1.00   42.82   U       ATOM   54   O   ALA   U   307   18.173   111.277   11.325   1.00   42.93   U       ATOM   55   N   ASP   U   308   16.947   113.151   11.448   1.00   43.61   U       ATOM   56   CA   ASP   U   308   17.849   113.911   10.605   1.00   50.98   U       ATOM   57   CB   ASP   U   308   17.300   115.332   10.383   1.00   59.56   U       ATOM   58   CG   ASP   U   308   16.155   115.378   9.349   1.00   77.63   U       ATOM   59   OD1   ASP   U   308   16.431   115.189   8.136   1.00   77.42   U       ATOM   60   OD2   ASP   U   308   14.980   115.602   9.745   1.00   83.75   U       ATOM   61   C   ASP   U   308   19.253   113.961   11.193   1.00   50.06   U       ATOM   62   O   ASP   U   308   20.232   113.759   10.470   1.00   48.52   U       ATOM   63   N   ARG   U   309   19.343   114.215   12.501   1.00   50.01   U       ATOM   64   CA   ARG   U   309   20.626   114.306   13.212   1.00   46.81   U       ATOM   65   CB   ARG   U   309   20.416   114.928   14.611   1.00   52.16   U       ATOM   66   CG   ARG   U   309   21.719   115.269   15.356   1.00   64.05   U       ATOM   67   CD   ARG   U   309   21.480   115.849   16.754   1.00   72.60   U       ATOM   68   NE   ARG   U   309   22.329   115.193   17.760   1.00   85.46   U       ATOM   69   CZ   ARG   U   309   22.274   115.409   19.078   1.00   83.67   U       ATOM   70   NH1   ARG   U   309   21.406   116.281   19.585   1.00   76.09   U       ATOM   71   NH2   ARG   U   309   23.078   114.731   19.895   1.00   78.11   U       ATOM   72   C   ARG   U   309   21.261   112.918   13.339   1.00   43.26   U       ATOM   73   O   ARG   U   309   22.461   112.740   13.156   1.00   38.45   U       ATOM   74   N   GLN   U   310   20.429   111.933   13.626   1.00   40.97   U       ATOM   75   CA   GLN   U   310   20.876   110.561   13.793   1.00   41.56   U       ATOM   76   CB   GLN   U   310   19.677   109.664   14.090   1.00   41.72   U       ATOM   77   CG   GLN   U   310   20.043   108.269   14.527   1.00   42.82   U       ATOM   78   CD   GLN   U   310   19.845   108.037   16.008   1.00   43.14   U       ATOM   79   OE1   GLN   U   310   20.101   106.941   16.498   1.00   51.10   U       ATOM   80   NE2   GLN   U   310   19.390   109.058   16.730   1.00   41.54   U       ATOM   81   C   GLN   U   310   21.632   110.016   12.589   1.00   41.73   U       ATOM   82   O   GLN   U   310   22.583   109.243   12.747   1.00   41.77   U       ATOM   83   N   LEU   U   311   21.197   110.398   11.391   1.00   39.72   U       ATOM   84   CA   LEU   U   311   21.866   109.940   10.182   1.00   42.01   U       ATOM   85   CB   LEU   U   311   20.929   110.010   8.990   1.00   33.72   U       ATOM   86   CG   LEU   U   311   19.901   108.911   9.253   1.00   37.21   U       ATOM   87   CD1   LEU   U   311   18.722   109.006   8.305   1.00   42.07   U       ATOM   88   CD2   LEU   U   311   20.620   107.581   9.118   1.00   28.89   U       ATOM   89   C   LEU   U   311   23.073   110.792   9.958   1.00   42.61   U       ATOM   90   O   LEU   U   311   24.155   110.282   9.701   1.00   47.17   U       ATOM   91   N   TYR   U   312   22.893   112.099   10.075   1.00   44.31   U       ATOM   92   CA   TYR   U   312   24.008   113.006   9.915   1.00   43.52   U       ATOM   93   CB   TYR   U   312   23.604   114.426   10.302   1.00   42.27   U       ATOM   94   CG   TYR   U   312   24.792   115.357   10.330   1.00   51.55   U       ATOM   95   CD1   TYR   U   312   25.523   115.604   9.166   1.00   54.42   U       ATOM   96   CE1   TYR   U   312   26.673   116.375   9.190   1.00   58.59   U       ATOM   97   CD2   TYR   U   312   25.244   115.920   11.532   1.00   51.32   U       ATOM   98   CE2   TYR   U   312   26.399   116.696   11.572   1.00   52.75   U       ATOM   99   CZ   TYR   U   312   27.110   116.923   10.393   1.00   60.94   U       ATOM   100   OH   TYR   U   312   28.250   117.704   10.392   1.00   62.51   U       ATOM   101   C   TYR   U   312   25.162   112.540   10.818   1.00   47.20   U       ATOM   102   O   TYR   U   312   26.327   112.512   10.401   1.00   48.75   U       ATOM   103   N   GLN   U   313   24.847   112.178   12.060   1.00   45.21   U       ATOM   104   CA   GLN   U   313   25.890   111.721   12.967   1.00   44.40   U       ATOM   105   CB   GLN   U   313   25.327   111.573   14.384   1.00   43.42   U       ATOM   106   CG   GLN   U   313   25.057   112.909   15.071   1.00   53.09   U       ATOM   107   CD   GLN   U   313   24.580   112.759   16.512   1.00   62.29   U       ATOM   108   OE1   GLN   U   313   23.510   112.193   16.786   1.00   71.08   U       ATOM   109   NE2   GLN   U   313   25.371   113.273   17.442   1.00   58.49   U       ATOM   110   C   GLN   U   313   26.522   110.403   12.483   1.00   46.69   U       ATOM   111   O   GLN   U   313   27.740   110.199   12.583   1.00   42.76   U       ATOM   112   N   LEU   U   314   25.700   109.515   11.935   1.00   44.18   U       ATOM   113   CA   LEU   U   314   26.205   108.241   11.455   1.00   40.49   U       ATOM   114   CB   LEU   U   314   25.078   107.378   10.894   1.00   37.07   U       ATOM   115   CG   LEU   U   314   25.487   106.015   10.333   1.00   26.82   U       ATOM   116   CD1   LEU   U   314   25.942   105.112   11.450   1.00   20.92   U       ATOM   117   CD2   LEU   U   314   24.305   105.419   9.604   1.00   27.59   U       ATOM   118   C   LEU   U   314   27.211   108.457   10.359   1.00   41.48   U       ATOM   119   O   LEU   U   314   28.371   108.067   10.471   1.00   48.20   U       ATOM   120   N   ILE   U   315   26.752   109.075   9.283   1.00   40.04   U       ATOM   121   CA   ILE   U   315   27.601   109.321   8.141   1.00   36.91   U       ATOM   122   CB   ILE   U   315   26.784   110.052   7.060   1.00   30.15   U       ATOM   123   CG2   ILE   U   315   27.582   110.195   5.774   1.00   30.46   U       ATOM   124   CG1   ILE   U   315   25.569   109.182   6.721   1.00   34.16   U       ATOM   125   CD1   ILE   U   315   24.361   109.924   6.166   1.00   33.94   U       ATOM   126   C   ILE   U   315   28.866   110.078   8.566   1.00   43.49   U       ATOM   127   O   ILE   U   315   29.968   109.764   8.120   1.00   37.56   U       ATOM   128   N   GLU   U   316   28.731   111.041   9.470   1.00   47.27   U       ATOM   129   CA   GLU   U   316   29.905   111.782   9.902   1.00   43.86   U       ATOM   130   CB   GLU   U   316   29.477   113.020   10.704   1.00   50.83   U       ATOM   131   CG   GLU   U   316   30.378   114.251   10.478   1.00   60.61   U       ATOM   132   CD   GLU   U   316   30.496   114.645   8.997   1.00   70.18   U       ATOM   133   OE1   GLU   U   316   29.452   114.676   8.297   1.00   69.12   U       ATOM   134   OE2   GLU   U   316   31.633   114.931   8.536   1.00   72.57   U       ATOM   135   C   GLU   U   316   30.824   110.863   10.723   1.00   43.27   U       ATOM   136   O   GLU   U   316   32.046   110.987   10.673   1.00   47.56   U       ATOM   137   N   TRP   U   317   30.240   109.932   11.470   1.00   37.75   U       ATOM   138   CA   TRP   U   317   31.026   108.998   12.267   1.00   34.00   U       ATOM   139   CB   TRP   U   317   30.098   108.038   13.010   1.00   31.02   U       ATOM   140   CG   TRP   U   317   30.770   106.786   13.514   1.00   30.93   U       ATOM   141   CD2   TRP   U   317   30.677   105.464   12.939   1.00   36.63   U       ATOM   142   CE2   TRP   U   317   31.489   104.612   13.723   1.00   31.60   U       ATOM   143   CE3   TRP   U   317   29.984   104.921   11.837   1.00   34.52   U       ATOM   144   CD1   TRP   U   317   31.603   106.682   14.575   1.00   27.55   U       ATOM   145   NE1   TRP   U   317   32.042   105.381   14.712   1.00   32.28   U       ATOM   146   CZ2   TRP   U   317   31.641   103.245   13.442   1.00   34.19   U       ATOM   147   CZ3   TRP   U   317   30.134   103.563   11.556   1.00   37.31   U       ATOM   148   CH2   TRP   U   317   30.958   102.741   12.363   1.00   38.29   U       ATOM   149   C   TRP   U   317   31.947   108.198   11.362   1.00   39.77   U       ATOM   150   O   TRP   U   317   33.158   108.126   11.601   1.00   41.36   U       ATOM   151   N   ALA   U   318   31.353   107.595   10.328   1.00   37.36   U       ATOM   152   CA   ALA   U   318   32.080   106.776   9.367   1.00   37.84   U       ATOM   153   CB   ALA   U   318   31.113   106.097   8.414   1.00   32.85   U       ATOM   154   C   ALA   U   318   33.100   107.568   8.578   1.00   37.92   U       ATOM   155   O   ALA   U   318   34.186   107.062   8.285   1.00   35.70   U       ATOM   156   N   LYS   U   319   32.750   108.803   8.223   1.00   38.77   U       ATOM   157   CA   LYS   U   319   33.664   109.648   7.463   1.00   38.43   U       ATOM   158   CB   LYS   U   319   33.133   111.080   7.305   1.00   45.25   U       ATOM   159   CG   LYS   U   319   32.079   111.337   6.210   1.00   37.31   U       ATOM   160   CD   LYS   U   319   31.811   112.825   6.122   1.00   35.09   U       ATOM   161   CE   LYS   U   319   30.710   113.157   5.148   1.00   50.28   U       ATOM   162   NZ   LYS   U   319   30.362   114.621   5.151   1.00   53.41   U       ATOM   163   C   LYS   U   319   34.961   109.683   8.230   1.00   39.01   U       ATOM   164   O   LYS   U   319   36.032   109.652   7.622   1.00   43.09   U       ATOM   165   N   HIS   U   320   34.863   109.700   9.562   1.00   34.70   U       ATOM   166   CA   HIS   U   320   36.051   109.746   10.416   1.00   33.00   U       ATOM   167   CB   HIS   U   320   35.813   110.644   11.619   1.00   29.91   U       ATOM   168   CG   HIS   U   320   35.554   112.066   11.252   1.00   44.90   U       ATOM   169   CD2   HIS   U   320   36.398   113.109   11.075   1.00   51.89   U       ATOM   170   ND1   HIS   U   320   34.296   112.533   10.940   1.00   51.08   U       ATOM   171   CE1   HIS   U   320   34.379   113.803   10.583   1.00   56.48   U       ATOM   172   NE2   HIS   U   320   35.644   114.177   10.655   1.00   56.71   U       ATOM   173   C   HIS   U   320   36.674   108.450   10.918   1.00   32.75   U       ATOM   174   O   HIS   U   320   37.456   108.498   11.863   1.00   36.77   U       ATOM   175   N   ILE   U   321   36.344   107.309   10.311   1.00   32.76   U       ATOM   176   CA   ILE   U   321   36.939   106.030   10.720   1.00   30.81   U       ATOM   177   CB   ILE   U   321   36.039   104.819   10.404   1.00   32.67   U       ATOM   178   CG2   ILE   U   321   36.873   103.557   10.448   1.00   26.36   U       ATOM   179   CG1   ILE   U   321   34.802   104.788   11.313   1.00   25.98   U       ATOM   180   CD1   ILE   U   321   35.120   104.784   12.742   1.00   38.19   U       ATOM   181   C   ILE   U   321   38.172   105.883   9.852   1.00   30.90   U       ATOM   182   O   ILE   U   321   38.075   105.950   8.629   1.00   40.52   U       ATOM   183   N   PRO   U   322   39.342   105.684   10.461   1.00   28.11   U       ATOM   184   CD   PRO   U   322   39.609   105.683   11.907   1.00   29.42   U       ATOM   185   CA   PRO   U   322   40.588   105.540   9.710   1.00   28.24   U       ATOM   186   CB   PRO   U   322   41.553   105.017   10.759   1.00   27.46   U       ATOM   187   CG   PRO   U   322   41.128   105.777   11.954   1.00   32.35   U       ATOM   188   C   PRO   U   322   40.531   104.655   8.484   1.00   28.10   U       ATOM   189   O   PRO   U   322   40.343   103.452   8.604   1.00   40.32   U       ATOM   190   N   HIS   U   323   40.715   105.275   7.316   1.00   26.78   U       ATOM   191   CA   HIS   U   323   40.725   104.621   6.004   1.00   26.63   U       ATOM   192   CB   HIS   U   323   41.352   103.242   6.102   1.00   25.78   U       ATOM   193   CG   HIS   U   323   42.711   103.264   6.703   1.00   39.81   U       ATOM   194   CD2   HIS   U   323   43.216   102.640   7.790   1.00   48.36   U       ATOM   195   ND1   HIS   U   323   43.721   104.060   6.209   1.00   41.57   U       ATOM   196   CE1   HIS   U   323   44.791   103.926   6.971   1.00   48.87   U       ATOM   197   NE2   HIS   U   323   44.513   103.072   7.938   1.00   53.44   U       ATOM   198   C   HIS   U   323   39.404   104.494   5.273   1.00   30.76   U       ATOM   199   O   HIS   U   323   39.392   104.202   4.083   1.00   31.32   U       ATOM   200   N   PHE   U   324   38.295   104.709   5.970   1.00   35.37   U       ATOM   201   CA   PHE   U   324   36.990   104.584   5.340   1.00   36.68   U       ATOM   202   CB   PHE   U   324   35.886   105.074   6.275   1.00   30.95   U       ATOM   203   CG   PHE   U   324   34.511   104.881   5.707   1.00   38.02   U       ATOM   204   CD1   PHE   U   324   33.991   103.587   5.532   1.00   32.62   U       ATOM   205   CD2   PHE   U   324   33.763   105.979   5.261   1.00   34.48   U       ATOM   206   CE1   PHE   U   324   32.750   103.397   4.911   1.00   29.22   U       ATOM   207   CE2   PHE   U   324   32.511   105.800   4.636   1.00   31.30   U       ATOM   208   CZ   PHE   U   324   32.006   104.514   4.460   1.00   25.37   U       ATOM   209   C   PHE   U   324   36.886   105.351   4.015   1.00   41.75   U       ATOM   210   O   PHE   U   324   36.539   104.785   2.970   1.00   38.18   U       ATOM   211   N   THR   U   325   37.185   106.648   4.072   1.00   42.47   U       ATOM   212   CA   THR   U   325   37.104   107.509   2.903   1.00   37.33   U       ATOM   213   CB   THR   U   325   37.091   108.974   3.289   1.00   32.20   U       ATOM   214   OG1   THR   U   325   38.139   109.224   4.227   1.00   37.87   U       ATOM   215   CG2   THR   U   325   35.746   109.344   3.895   1.00   29.55   U       ATOM   216   C   THR   U   325   38.204   107.295   1.900   1.00   38.08   U       ATOM   217   O   THR   U   325   38.262   108.000   0.900   1.00   45.26   U       ATOM   218   N   GLU   U   326   39.086   106.339   2.156   1.00   35.21   U       ATOM   219   CA   GLU   U   326   40.130   106.050   1.197   1.00   35.59   U       ATOM   220   CB   GLU   U   326   41.426   105.642   1.898   1.00   43.50   U       ATOM   221   CG   GLU   U   326   41.942   106.651   2.935   1.00   52.68   U       ATOM   222   CD   GLU   U   326   43.381   106.359   3.366   1.00   56.78   U       ATOM   223   OE1   GLU   U   326   43.728   105.172   3.600   1.00   52.62   U       ATOM   224   OE2   GLU   U   326   44.166   107.324   3.477   1.00   55.12   U       ATOM   225   C   GLU   U   326   39.602   104.923   0.303   1.00   34.41   U       ATOM   226   O   GLU   U   326   40.253   104.499   −0.638   1.00   39.17   U       ATOM   227   N   LEU   U   327   38.414   104.424   0.604   1.00   35.62   U       ATOM   228   CA   LEU   U   327   37.811   103.391   −0.233   1.00   34.31   U       ATOM   229   CB   LEU   U   327   36.799   102.573   0.556   1.00   29.93   U       ATOM   230   CG   LEU   U   327   37.272   101.577   1.587   1.00   28.51   U       ATOM   231   CD1   LEU   U   327   36.200   101.454   2.633   1.00   31.32   U       ATOM   232   CD2   LEU   U   327   37.546   100.223   0.935   1.00   31.78   U       ATOM   233   C   LEU   U   327   37.077   104.099   −1.380   1.00   34.86   U       ATOM   234   O   LEU   U   327   36.764   105.291   −1.298   1.00   32.50   U       ATOM   235   N   PRO   U   328   36.783   103.368   −2.461   1.00   34.61   U       ATOM   236   CD   PRO   U   328   37.056   101.942   −2.704   1.00   36.41   U       ATOM   237   CA   PRO   U   328   36.081   103.965   −3.601   1.00   36.93   U       ATOM   238   CB   PRO   U   328   35.954   102.792   −4.566   1.00   42.49   U       ATOM   239   CG   PRO   U   328   37.112   101.898   −4.186   1.00   35.91   U       ATOM   240   C   PRO   U   328   34.722   104.507   −3.154   1.00   35.70   U       ATOM   241   O   PRO   U   328   33.939   103.798   −2.539   1.00   40.26   U       ATOM   242   N   VAL   U   329   34.423   105.752   −3.467   1.00   33.92   U       ATOM   243   CA   VAL   U   329   33.162   106.304   −3.012   1.00   40.39   U       ATOM   244   CB   VAL   U   329   32.844   107.587   −3.719   1.00   37.74   U       ATOM   245   CG1   VAL   U   329   31.899   108.388   −2.864   1.00   32.09   U       ATOM   246   CG2   VAL   U   329   34.131   108.345   −4.006   1.00   46.30   U       ATOM   247   C   VAL   U   329   31.940   105.397   −3.140   1.00   45.16   U       ATOM   248   O   VAL   U   329   31.085   105.387   −2.254   1.00   48.70   U       ATOM   249   N   GLU   U   330   31.853   104.648   −4.235   1.00   47.59   U       ATOM   250   CA   GLU   U   330   30.727   103.748   −4.479   1.00   49.23   U       ATOM   251   CB   GLU   U   330   30.852   103.100   −5.862   1.00   57.88   U       ATOM   252   CG   GLU   U   330   31.492   104.010   −6.919   1.00   75.31   U       ATOM   253   CD   GLU   U   330   33.028   104.105   −6.791   1.00   85.37   U       ATOM   254   OE1   GLU   U   330   33.717   103.102   −7.112   1.00   88.41   U       ATOM   255   OE2   GLU   U   330   33.545   105.175   −6.370   1.00   81.90   U       ATOM   256   C   GLU   U   330   30.691   102.671   −3.406   1.00   47.32   U       ATOM   257   O   GLU   U   330   29.619   102.265   −2.959   1.00   47.52   U       ATOM   258   N   ASP   U   331   31.868   102.202   −3.004   1.00   46.97   U       ATOM   259   CA   ASP   U   331   31.990   101.196   −1.951   1.00   48.96   U       ATOM   260   CB   ASP   U   331   33.414   100.659   −1.932   1.00   49.87   U       ATOM   261   CG   ASP   U   331   33.605   99.555   −2.924   1.00   53.38   U       ATOM   262   OD1   ASP   U   331   32.709   99.411   −3.783   1.00   56.13   U       ATOM   263   OD2   ASP   U   331   34.625   98.839   −2.843   1.00   47.10   U       ATOM   264   C   ASP   U   331   31.610   101.797   −0.588   1.00   49.54   U       ATOM   265   O   ASP   U   331   31.048   101.121   0.289   1.00   48.49   U       ATOM   266   N   GLN   U   332   31.930   103.074   −0.421   1.00   44.30   U       ATOM   267   CA   GLN   U   332   31.575   103.789   0.783   1.00   43.21   U       ATOM   268   CB   GLN   U   332   32.120   105.208   0.724   1.00   43.36   U       ATOM   269   CG   GLN   U   332   33.592   105.290   0.982   1.00   47.06   U       ATOM   270   CD   GLN   U   332   34.061   106.702   1.038   1.00   50.14   U       ATOM   271   OE1   GLN   U   332   33.377   107.574   1.575   1.00   50.22   U       ATOM   272   NE2   GLN   U   332   35.235   106.948   0.493   1.00   53.82   U       ATOM   273   C   GLN   U   332   30.050   103.827   0.896   1.00   44.72   U       ATOM   274   O   GLN   U   332   39.500   103.632   1.972   1.00   49.65   U       ATOM   275   N   VAL   U   333   29.362   104.079   −0.214   1.00   42.41   U       ATOM   276   CA   VAL   U   333   27.905   104.118   −0.187   1.00   40.09   U       ATOM   277   CB   VAL   U   333   27.352   104.654   −1.510   1.00   33.88   U       ATOM   278   CG1   VAL   U   333   25.838   104.693   −1.470   1.00   30.31   U       ATOM   279   CG2   VAL   U   333   27.882   106.070   −1.729   1.00   33.72   U       ATOM   280   C   VAL   U   333   27.364   102.723   0.107   1.00   40.39   U       ATOM   281   O   VAL   U   333   26.491   102.535   0.959   1.00   40.57   U       ATOM   282   N   ILE   U   334   27.907   101.742   −0.588   1.00   36.75   U       ATOM   283   CA   ILE   U   334   27.525   100.361   −0.367   1.00   39.58   U       ATOM   284   CB   ILE   U   334   28.405   99.427   −1.207   1.00   42.58   U       ATOM   285   CG2   ILE   U   334   28.248   97.979   −0.742   1.00   45.90   U       ATOM   286   CG1   ILE   U   334   28.075   99.618   −2.685   1.00   39.08   U       ATOM   287   CD1   ILE   U   334   28.839   98.687   −3.563   1.00   41.96   U       ATOM   288   C   ILE   U   334   27.676   99.956   1.105   1.00   41.97   U       ATOM   289   O   ILE   U   334   26.748   99.416   1.721   1.00   41.77   U       ATOM   290   N   LEU   U   335   28.855   100.203   1.662   1.00   38.84   U       ATOM   291   CA   LEU   U   335   39.093   99.825   3.037   1.00   38.04   U       ATOM   292   CB   LEU   U   335   30.542   100.127   3.430   1.00   38.86   U       ATOM   293   CG   LEU   U   335   31.569   99.106   2.923   1.00   41.31   U       ATOM   294   CD1   LEU   U   335   32.952   99.609   3.226   1.00   48.69   U       ATOM   295   CD2   LEU   U   335   31.358   97.753   3.575   1.00   36.63   U       ATOM   296   C   LEU   U   335   28.125   100.474   4.014   1.00   34.75   U       ATOM   297   O   LEU   U   335   27.690   99.840   4.974   1.00   35.11   U       ATOM   298   N   LEU   U   336   27.780   101.728   3.765   1.00   30.31   U       ATOM   299   CA   LEU   U   336   26.864   102.451   4.635   1.00   32.58   U       ATOM   300   CB   LEU   U   336   27.018   103.970   4.452   1.00   34.63   U       ATOM   301   CG   LEU   U   336   28.050   104.689   5.334   1.00   35.17   U       ATOM   302   CD1   LEU   U   336   28.378   106.062   4.769   1.00   29.95   U       ATOM   303   CD2   LEU   U   336   27.496   104.800   6.744   1.00   31.44   U       ATOM   304   C   LEU   U   336   25.430   102.069   4.353   1.00   35.51   U       ATOM   305   O   LEU   U   336   24.641   101.884   5.281   1.00   35.28   U       ATOM   306   N   LYS   U   337   25.084   101.951   3.071   1.00   36.77   U       ATOM   307   CA   LYS   U   337   23.713   101.615   2.720   1.00   34.23   U       ATOM   308   CB   LYS   U   337   23.507   101.623   1.206   1.00   41.87   U       ATOM   309   CG   LYS   U   337   22.052   101.329   0.782   1.00   47.78   U       ATOM   310   CD   LYS   U   337   21.822   101.410   −0.726   1.00   43.48   U       ATOM   311   CE   LYS   U   337   20.514   100.743   −1.064   1.00   42.29   U       ATOM   312   NZ   LYS   U   337   20.043   101.077   −2.425   1.00   54.28   U       ATOM   313   C   LYS   U   337   23.357   100.263   3.289   1.00   33.22   U       ATOM   314   O   LYS   U   337   22.211   100.016   3.656   1.00   37.11   U       ATOM   315   N   SER   U   338   24.354   99.393   3.370   1.00   25.79   U       ATOM   316   CA   SER   U   338   24.168   98.057   3.901   1.00   24.15   U       ATOM   317   CB   SER   U   338   25.161   97.124   3.203   1.00   21.99   U       ATOM   318   OG   SER   U   338   25.287   95.885   3.876   1.00   17.90   U       ATOM   319   C   SER   U   338   24.297   97.982   5.449   1.00   30.41   U       ATOM   320   O   SER   U   338   23.490   97.340   6.114   1.00   31.99   U       ATOM   321   N   GLY   U   339   25.301   98.637   6.030   1.00   32.94   U       ATOM   322   CA   GLY   U   339   25.457   98.604   7.476   1.00   28.86   U       ATOM   323   C   GLY   U   339   24.445   99.480   8.201   1.00   28.75   U       ATOM   324   O   GLY   U   339   24.231   99.328   9.402   1.00   26.26   U       ATOM   325   N   TRP   U   340   23.819   100.386   7.448   1.00   25.56   U       ATOM   326   CA   TRP   U   340   22.820   101.334   7.938   1.00   27.93   U       ATOM   327   CB   TRP   U   340   21.893   101.726   6.765   1.00   28.33   U       ATOM   328   CG   TRP   U   340   20.852   102.785   7.075   1.00   32.51   U       ATOM   329   CD2   TRP   U   340   20.701   104.069   6.446   1.00   36.24   U       ATOM   330   CE2   TRP   U   340   19.578   104.698   7.043   1.00   32.10   U       ATOM   331   CE3   TRP   U   340   21.400   104.752   5.438   1.00   33.50   U       ATOM   332   CD1   TRP   U   340   19.846   102.700   7.995   1.00   35.61   U       ATOM   333   NE1   TRP   U   340   19.079   103.838   7.981   1.00   33.30   U       ATOM   334   CZ2   TRP   U   340   19.146   105.978   6.673   1.00   22.67   U       ATOM   335   CZ3   TRP   U   340   20.959   106.041   5.069   1.00   22.73   U       ATOM   336   CH2   TRP   U   340   19.846   106.630   5.688   1.00   27.61   U       ATOM   337   C   TRP   U   340   22.007   100.896   9.179   1.00   30.07   U       ATOM   338   O   TRP   U   340   22.245   101.385   10.276   1.00   34.83   U       ATOM   339   N   ASN   U   341   21.067   99.973   9.040   1.00   30.01   U       ATOM   340   CA   ASN   U   341   20.276   99.597   10.204   1.00   29.52   U       ATOM   341   CB   ASN   U   341   19.227   98.570   9.804   1.00   32.18   U       ATOM   342   CG   ASN   U   341   18.089   99.182   9.016   1.00   31.81   U       ATOM   343   OD1   ASN   U   341   17.206   98.477   8.518   1.00   32.06   U       ATOM   344   ND2   ASN   U   341   18.099   100.497   8.900   1.00   28.83   U       ATOM   345   C   ASN   U   341   21.063   99.087   11.411   1.00   31.89   U       ATOM   346   O   ASN   U   341   20.911   99.592   12.526   1.00   34.91   U       ATOM   347   N   GLU   U   342   21.897   98.078   11.208   1.00   31.11   U       ATOM   348   CA   GLU   U   342   22.651   97.553   12.331   1.00   29.94   U       ATOM   349   CB   GLU   U   342   23.547   96.401   11.908   1.00   26.29   U       ATOM   350   CG   GLU   U   342   22.814   95.202   11.417   1.00   26.29   U       ATOM   351   CD   GLU   U   342   23.752   94.084   11.035   1.00   36.46   U       ATOM   352   OE1   GLU   U   342   23.997   93.876   9.828   1.00   30.05   U       ATOM   353   OE2   GLU   U   342   24.266   93.407   11.953   1.00   53.55   U       ATOM   354   C   GLU   U   342   23.505   98.632   12.965   1.00   33.66   U       ATOM   355   O   GLU   U   342   23.729   98.596   14.166   1.00   39.16   U       ATOM   356   N   LEU   U   343   23.984   99.592   12.178   1.00   29.29   U       ATOM   357   CA   LEU   U   343   24.817   100.634   12.747   1.00   30.23   U       ATOM   358   CB   LEU   U   343   25.555   101.417   11.653   1.00   27.80   U       ATOM   359   CG   LEU   U   343   26.745   100.750   10.930   1.00   32.16   U       ATOM   360   CD1   LEU   U   343   27.165   101.600   9.723   1.00   23.65   U       ATOM   361   CD2   LEU   U   343   27.904   100.562   11.880   1.00   16.27   U       ATOM   362   C   LEU   U   343   24.003   101.578   13.619   1.00   35.57   U       ATOM   363   O   LEU   U   343   24.399   101.870   14.758   1.00   33.58   U       ATOM   364   N   LEU   U   344   22.865   102.044   13.108   1.00   32.56   U       ATOM   365   CA   LEU   U   344   22.025   102.960   13.881   1.00   37.27   U       ATOM   366   CB   LEU   U   344   20.807   103.428   13.091   1.00   24.92   U       ATOM   367   CG   LEU   U   344   21.049   104.222   11.826   1.00   23.17   U       ATOM   368   CD1   LEU   U   344   19.729   104.429   11.171   1.00   24.49   U       ATOM   369   CD2   LEU   U   344   21.715   105.548   12.127   1.00   16.44   U       ATOM   370   C   LEU   U   344   21.517   102.291   15.137   1.00   41.23   U       ATOM   371   O   LEU   U   344   21.448   102.922   16.194   1.00   46.21   U       ATOM   372   N   ILE   U   345   21.148   101.018   15.004   1.00   39.57   U       ATOM   373   CA   ILE   U   345   20.607   100.245   16.112   1.00   37.50   U       ATOM   374   CB   ILE   U   345   20.150   98.857   15.627   1.00   36.70   U       ATOM   375   CG2   ILE   U   345   19.928   97.911   16.816   1.00   33.77   U       ATOM   376   CG1   ILE   U   345   18.882   99.009   14.792   1.00   31.92   U       ATOM   377   CD1   ILE   U   345   18.361   97.689   14.247   1.00   36.61   U       ATOM   378   C   ILE   U   345   21.602   100.087   17.244   1.00   34.63   U       ATOM   379   O   ILE   U   345   21.305   100.393   18.385   1.00   33.90   U       ATOM   380   N   ALA   U   346   22.787   99.603   16.922   1.00   34.92   U       ATOM   381   CA   ALA   U   346   23.827   99.402   17.919   1.00   33.34   U       ATOM   382   CB   ALA   U   346   25.079   98.872   17.233   1.00   20.38   U       ATOM   383   C   ALA   U   346   24.125   100.720   18.640   1.00   35.49   U       ATOM   384   O   ALA   U   346   24.349   100.759   19.853   1.00   32.79   U       ATOM   385   N   GLY   U   347   24.120   101.800   17.864   1.00   39.18   U       ATOM   386   CA   GLY   U   347   24.386   103.121   18.399   1.00   37.65   U       ATOM   387   C   GLY   U   347   23.359   103.573   19.413   1.00   39.12   U       ATOM   388   O   GLY   U   347   23.711   103.796   20.563   1.00   37.43   U       ATOM   389   N   PHE   U   348   22.095   103.710   19.011   1.00   39.25   U       ATOM   390   CA   PHE   U   348   21.101   104.140   19.975   1.00   34.80   U       ATOM   391   CB   PHE   U   348   19.778   104.588   19.305   1.00   33.33   U       ATOM   392   CG   PHE   U   348   19.037   103.532   18.536   1.00   32.08   U       ATOM   393   CD1   PHE   U   348   18.522   102.402   19.165   1.00   30.46   U       ATOM   394   CD2   PHE   U   348   18.760   103.726   17.176   1.00   32.54   U       ATOM   395   CE1   PHE   U   348   17.735   101.482   18.450   1.00   30.24   U       ATOM   396   CE2   PHE   U   348   17.976   102.812   16.452   1.00   26.04   U       ATOM   397   CZ   PHE   U   348   17.465   101.694   17.085   1.00   27.51   U       ATOM   398   C   PHE   U   348   20.851   103.128   21.073   1.00   33.35   U       ATOM   399   O   PHE   U   348   20.269   103.477   22.096   1.00   32.57   U       ATOM   400   N   SER   U   349   21.324   101.894   20.877   1.00   33.74   U       ATOM   401   CA   SER   U   349   21.174   100.815   21.865   1.00   35.08   U       ATOM   402   CB   SER   U   349   21.520   99.457   21.254   1.00   35.19   U       ATOM   403   OG   SER   U   349   20.413   98.887   20.592   1.00   43.14   U       ATOM   404   C   SER   U   349   22.093   101.056   23.051   1.00   34.96   U       ATOM   405   O   SER   U   349   21.679   101.001   24.210   1.00   35.52   U       ATOM   406   N   HIS   U   350   23.354   101.314   22.738   1.00   33.89   U       ATOM   407   CA   HIS   U   350   24.354   101.575   23.750   1.00   38.26   U       ATOM   408   CB   HIS   U   350   25.738   101.609   23.115   1.00   37.36   U       ATOM   409   CG   HIS   U   350   26.837   101.892   24.088   1.00   35.12   U       ATOM   410   CD2   HIS   U   350   27.588   101.058   24.851   1.00   32.12   U       ATOM   411   ND1   HIS   U   350   27.293   103.166   24.351   1.00   27.40   U       ATOM   412   CE1   HIS   U   350   28.284   103.103   25.224   1.00   31.15   U       ATOM   413   NE2   HIS   U   350   28.480   101.834   25.541   1.00   24.80   U       ATOM   414   C   HIS   U   350   24.080   102.891   24.454   1.00   41.29   U       ATOM   415   O   HIS   U   350   24.221   102.971   25.665   1.00   43.64   U       ATOM   416   N   ARG   U   351   23.698   103.917   23.687   1.00   46.27   U       ATOM   417   CA   ARG   U   351   23.390   105.244   24.223   1.00   41.47   U       ATOM   418   CB   ARG   U   351   23.084   106.247   23.107   1.00   40.73   U       ATOM   419   CG   ARG   U   351   22.823   107.679   23.626   1.00   52.88   U       ATOM   420   CD   ARG   U   351   22.703   108.675   22.482   1.00   65.75   U       ATOM   421   NE   ARG   U   351   22.716   110.064   22.939   1.00   78.56   U       ATOM   422   CZ   ARG   U   351   22.786   111.133   22.134   1.00   85.00   U       ATOM   423   NH1   ARG   U   351   22.852   110.999   20.807   1.00   82.69   U       ATOM   424   NH2   ARG   U   351   22.800   112.354   22.661   1.00   89.42   U       ATOM   425   C   ARG   U   351   22.200   105.224   25.169   1.00   43.65   U       ATOM   426   O   ARG   U   351   22.019   106.139   25.971   1.00   46.07   U       ATOM   427   N   SER   U   352   21.380   104.193   25.095   1.00   37.12   U       ATOM   428   CA   SER   U   352   20.244   104.182   25.976   1.00   41.58   U       ATOM   429   CB   SER   U   352   18.961   103.999   25.155   1.00   41.72   U       ATOM   430   OG   SER   U   352   19.142   103.057   24.142   1.00   40.19   U       ATOM   431   C   SER   U   352   20.355   103.155   27.083   1.00   42.37   U       ATOM   432   O   SER   U   352   19.352   102.574   27.494   1.00   44.94   U       ATOM   433   N   MET   U   353   21.572   102.958   27.589   1.00   43.30   U       ATOM   434   CA   MET   U   353   21.803   101.974   28.653   1.00   41.91   U       ATOM   435   CB   MET   U   353   23.288   101.657   28.827   1.00   37.50   U       ATOM   436   CG   MET   U   353   23.872   100.675   27.854   1.00   38.15   U       ATOM   437   SD   MET   U   353   25.607   100.366   28.215   1.00   42.35   U       ATOM   438   CE   MET   U   353   26.326   101.885   27.776   1.00   36.09   U       ATOM   439   C   MET   U   353   21.287   102.486   29.965   1.00   40.18   U       ATOM   440   O   MET   U   353   20.763   101.729   30.784   1.00   38.44   U       ATOM   441   N   SER   U   354   21.453   103.785   30.157   1.00   41.70   U       ATOM   442   CA   SER   U   354   21.023   104.434   31.381   1.00   52.28   U       ATOM   443   CB   SER   U   354   21.788   105.741   31.561   1.00   50.59   U       ATOM   444   OG   SER   U   354   21.749   106.498   30.357   1.00   62.08   U       ATOM   445   C   SER   U   354   19.516   104.689   31.371   1.00   57.36   U       ATOM   446   O   SER   U   354   18.869   104.579   32.411   1.00   66.59   U       ATOM   447   N   VAL   U   355   18.960   105.021   30.207   1.00   53.96   U       ATOM   448   CA   VAL   U   355   17.528   105.263   30.098   1.00   49.81   U       ATOM   449   CB   VAL   U   355   17.129   105.517   28.631   1.00   48.65   U       ATOM   450   CG1   VAL   U   355   15.632   105.396   28.471   1.00   38.73   U       ATOM   451   CG2   VAL   U   355   17.606   106.901   28.190   1.00   42.68   U       ATOM   452   C   VAL   U   355   16.761   104.046   30.623   1.00   53.60   U       ATOM   453   O   VAL   U   355   17.146   102.901   30.365   1.00   54.54   U       ATOM   454   N   LYS   U   356   15.690   104.293   31.374   1.00   55.40   U       ATOM   455   CA   LYS   U   356   14.887   103.196   31.906   1.00   60.98   U       ATOM   456   CB   LYS   U   356   14.344   103.539   33.294   1.00   67.99   U       ATOM   457   CG   LYS   U   356   13.463   102.430   33.900   1.00   75.32   U       ATOM   458   CD   LYS   U   356   12.748   102.863   35.190   1.00   77.01   U       ATOM   459   CE   LYS   U   356   13.725   103.184   36.330   1.00   79.62   U       ATOM   460   NZ   LYS   U   356   13.051   103.384   37.659   1.00   75.59   U       ATOM   461   C   LYS   U   356   13.723   102.942   30.957   1.00   62.54   U       ATOM   462   O   LYS   U   356   13.055   103.885   30.519   1.00   60.53   U       ATOM   463   N   ASP   U   357   13.487   101.670   30.642   1.00   63.08   U       ATOM   464   CA   ASP   U   357   12.412   101.269   29.734   1.00   67.30   U       ATOM   465   CB   ASP   U   357   11.083   101.222   30.478   1.00   74.78   U       ATOM   466   CG   ASP   U   357   10.959   99.998   31.355   1.00   88.42   U       ATOM   467   OD1   ASP   U   357   10.966   98.880   30.794   1.00   93.99   U       ATOM   468   OD2   ASP   U   357   10.859   100.150   32.599   1.00   97.29   U       ATOM   469   C   ASP   U   357   12.260   102.132   28.483   1.00   67.53   U       ATOM   470   O   ASP   U   357   11.183   102.671   28.208   1.00   66.44   U       ATOM   471   N   GLY   U   358   13.340   102.247   27.715   1.00   66.29   U       ATOM   472   CA   GLY   U   358   13.281   103.031   26.504   1.00   57.58   U       ATOM   473   C   GLY   U   358   14.569   103.066   25.712   1.00   57.81   U       ATOM   474   O   GLY   U   358   15.602   102.523   26.118   1.00   59.38   U       ATOM   475   N   ILE   U   359   14.465   103.736   24.568   1.00   53.70   U       ATOM   476   CA   ILE   U   359   15.532   103.943   23.601   1.00   47.56   U       ATOM   477   CB   ILE   U   359   15.116   103.351   22.218   1.00   39.27   U       ATOM   478   CG2   ILE   U   359   16.111   103.758   21.133   1.00   33.07   U       ATOM   479   CG1   ILE   U   359   14.988   101.830   22.326   1.00   41.53   U       ATOM   480   CD1   ILE   U   359   14.632   101.143   21.032   1.00   47.71   U       ATOM   481   C   ILE   U   359   15.725   105.453   23.435   1.00   50.08   U       ATOM   482   O   ILE   U   359   14.781   106.162   23.126   1.00   50.57   U       ATOM   483   N   MET   U   360   16.931   105.962   23.644   1.00   51.66   U       ATOM   484   CA   MET   U   360   17.153   107.392   23.447   1.00   54.19   U       ATOM   485   CB   MET   U   360   18.253   107.874   24.368   1.00   55.34   U       ATOM   486   CG   MET   U   360   18.559   109.320   24.191   1.00   63.76   U       ATOM   487   SD   MET   U   360   19.630   109.862   25.488   1.00   68.21   U       ATOM   488   CE   MET   U   360   18.423   110.302   26.681   1.00   63.93   U       ATOM   489   C   MET   U   360   17.550   107.636   21.986   1.00   57.24   U       ATOM   490   O   MET   U   360   18.051   106.731   21.331   1.00   62.64   U       ATOM   491   N   LEU   U   361   17.336   108.841   21.466   1.00   56.32   U       ATOM   492   CA   LEU   U   361   17.680   109.124   20.070   1.00   56.54   U       ATOM   493   CB   LEU   U   361   16.463   108.895   19.171   1.00   52.54   U       ATOM   494   CG   LEU   U   361   15.778   107.526   19.099   1.00   53.61   U       ATOM   495   CD1   LEU   U   361   14.474   107.633   18.310   1.00   46.05   U       ATOM   496   CD2   LEU   U   361   16.707   106.520   18.440   1.00   57.61   U       ATOM   497   C   LEU   U   361   18.157   110.556   19.870   1.00   62.43   U       ATOM   498   O   LEU   U   361   17.399   111.493   20.088   1.00   69.23   U       ATOM   499   N   ALA   U   362   19.397   110.732   19.430   1.00   72.75   U       ATOM   500   CA   ALA   U   362   19.945   112.077   19.207   1.00   81.97   U       ATOM   501   CB   ALA   U   362   19.448   112.637   17.875   1.00   82.62   U       ATOM   502   C   ALA   U   362   19.582   113.039   20.352   1.00   88.14   U       ATOM   503   O   ALA   U   362   18.788   113.989   20.170   1.00   86.81   U       ATOM   504   N   THR   U   363   20.186   112.762   21.516   1.00   90.21   U       ATOM   505   CA   THR   U   363   20.024   113.509   22.775   1.00   84.69   U       ATOM   506   CB   THR   U   363   20.732   114.906   22.742   1.00   84.81   U       ATOM   507   OG1   THR   U   363   21.948   114.849   23.508   1.00   74.38   U       ATOM   508   CG2   THR   U   363   19.823   115.996   23.318   1.00   78.85   U       ATOM   509   C   THR   U   363   18.579   113.700   23.162   1.00   80.56   U       ATOM   510   O   THR   U   363   17.762   114.165   22.365   1.00   76.72   U       ATOM   511   N   GLY   U   364   18.271   113.358   24.405   1.00   80.95   U       ATOM   512   CA   GLY   U   364   16.907   113.490   24.853   1.00   79.03   U       ATOM   513   C   GLY   U   364   16.090   112.686   23.863   1.00   78.51   U       ATOM   514   O   GLY   U   364   16.638   111.933   23.049   1.00   79.46   U       ATOM   515   N   LEU   U   365   14.780   112.876   23.903   1.00   72.04   U       ATOM   516   CA   LEU   U   365   13.866   112.142   23.049   1.00   64.93   U       ATOM   517   CB   LEU   U   365   14.132   112.386   21.557   1.00   54.02   U       ATOM   518   CG   LEU   U   365   12.824   112.119   20.785   1.00   50.92   U       ATOM   519   CD1   LEU   U   365   11.779   113.069   21.304   1.00   38.89   U       ATOM   520   CD2   LEU   U   365   12.974   112.315   19.302   1.00   51.79   U       ATOM   521   C   LEU   U   365   13.990   110.657   23.367   1.00   64.92   U       ATOM   522   O   LEU   U   365   14.497   109.863   22.574   1.00   69.33   U       ATOM   523   N   VAL   U   366   13.542   110.297   24.560   1.00   56.23   U       ATOM   524   CA   VAL   U   366   13.563   108.923   24.978   1.00   53.91   U       ATOM   525   CB   VAL   U   366   13.728   108.814   26.476   1.00   51.37   U       ATOM   526   CG1   VAL   U   366   13.522   107.380   26.913   1.00   48.12   U       ATOM   527   CG2   VAL   U   366   15.102   109.303   26.861   1.00   53.75   U       ATOM   528   C   VAL   U   366   12.246   108.291   24.580   1.00   57.47   U       ATOM   529   O   VAL   U   366   11.224   108.464   25.240   1.00   68.08   U       ATOM   530   N   VAL   U   367   12.273   107.578   23.470   1.00   55.00   U       ATOM   531   CA   VAL   U   367   11.100   106.891   22.965   1.00   49.29   U       ATOM   532   CB   VAL   U   367   11.436   106.249   21.619   1.00   35.95   U       ATOM   533   CG1   VAL   U   367   10.261   105.484   21.083   1.00   39.11   U       ATOM   534   CG2   VAL   U   367   11.881   107.314   20.660   1.00   36.47   U       ATOM   535   C   VAL   U   367   10.679   105.789   23.945   1.00   53.36   U       ATOM   536   O   VAL   U   367   11.525   105.036   24.435   1.00   56.64   U       ATOM   537   N   HIS   U   368   9.388   105.706   24.258   1.00   54.80   U       ATOM   538   CA   HIS   U   368   8.915   104.634   25.133   1.00   53.25   U       ATOM   539   CB   HIS   U   368   8.081   105.170   26.287   1.00   54.77   U       ATOM   540   CG   HIS   U   368   8.879   105.941   27.285   1.00   58.76   U       ATOM   541   CD2   HIS   U   368   8.956   107.269   27.534   1.00   58.35   U       ATOM   542   ND1   HIS   U   368   9.789   105.340   28.126   1.00   63.03   U       ATOM   543   CE1   HIS   U   368   10.395   106.266   28.850   1.00   62.51   U       ATOM   544   NE2   HIS   U   368   9.908   107.445   28.509   1.00   60.14   U       ATOM   545   C   HIS   U   368   8.093   103.700   24.280   1.00   50.90   U       ATOM   546   O   HIS   U   368   7.641   104.062   23.196   1.00   48.41   U       ATOM   547   N   ARG   U   369   7.898   102.489   24.766   1.00   52.36   U       ATOM   548   CA   ARG   U   369   7.153   101.515   23.996   1.00   52.38   U       ATOM   549   CB   ARG   U   369   6.907   100.271   24.830   1.00   48.03   U       ATOM   550   CG   ARG   U   369   6.370   99.130   24.021   1.00   46.98   U       ATOM   551   CD   ARG   U   369   5.934   98.029   24.947   1.00   54.79   U       ATOM   552   NE   ARG   U   369   4.898   97.229   24.317   1.00   55.68   U       ATOM   553   CZ   ARG   U   369   5.144   96.193   23.533   1.00   55.09   U       ATOM   554   NH1   ARG   U   369   6.398   95.842   23.302   1.00   56.98   U       ATOM   555   NH2   ARG   U   369   4.142   95.517   22.977   1.00   51.49   U       ATOM   556   C   ARG   U   369   5.833   102.060   23.486   1.00   54.06   U       ATOM   557   O   ARG   U   369   5.401   101.731   22.383   1.00   50.17   U       ATOM   558   N   ASN   U   370   5.210   102.922   24.282   1.00   57.80   U       ATOM   559   CA   ASN   U   370   3.914   103.493   23.923   1.00   61.00   U       ATOM   560   CB   ASN   U   370   3.341   104.296   25.092   1.00   63.08   U       ATOM   561   CG   ASN   U   370   3.963   105.667   25.214   1.00   68.85   U       ATOM   562   OD1   ASN   U   370   5.139   105.805   25.561   1.00   71.99   U       ATOM   563   ND2   ASN   U   370   3.175   106.697   24.924   1.00   71.17   U       ATOM   564   C   ASN   U   370   3.906   104.360   22.669   1.00   57.09   U       ATOM   565   O   ASN   U   370   2.895   104.962   22.343   1.00   58.09   U       ATOM   566   N   CYS   U   371   5.024   104.431   21.963   1.00   56.66   U       ATOM   567   CA   CYS   U   371   5.080   105.218   20.736   1.00   54.61   U       ATOM   568   CB   CYS   U   371   4.938   106.716   21.036   1.00   52.84   U       ATOM   569   SG   CYS   U   371   6.114   107.406   22.206   1.00   56.83   U       ATOM   570   C   CYS   U   371   6.378   104.914   20.003   1.00   53.71   U       ATOM   571   O   CYS   U   371   7.039   105.791   19.434   1.00   46.06   U       ATOM   572   N   ALA   U   372   6.742   103.638   20.048   1.00   50.90   U       ATOM   573   CA   ALA   U   372   7.916   103.168   19.358   1.00   49.08   U       ATOM   574   CB   ALA   U   372   8.202   101.735   19.748   1.00   46.77   U       ATOM   575   C   ALA   U   372   7.529   103.266   17.882   1.00   49.54   U       ATOM   576   O   ALA   U   372   8.364   103.574   17.032   1.00   44.53   U       ATOM   577   N   HIS   U   373   6.247   103.016   17.595   1.00   52.25   U       ATOM   578   CA   HIS   U   373   5.729   103.093   16.233   1.00   52.88   U       ATOM   579   CB   HIS   U   373   4.258   102.706   16.171   1.00   49.41   U       ATOM   580   CG   HIS   U   373   3.764   102.502   14.772   1.00   60.05   U       ATOM   581   CD2   HIS   U   373   3.170   103.351   13.903   1.00   57.01   U       ATOM   582   ND1   HIS   U   373   3.948   101.317   14.084   1.00   70.47   U       ATOM   583   CE1   HIS   U   373   3.489   101.451   12.851   1.00   64.76   U       ATOM   584   NE2   HIS   U   373   3.012   102.674   12.712   1.00   57.34   U       ATOM   585   C   HIS   U   373   5.898   104.508   15.674   1.00   55.40   U       ATOM   586   O   HIS   U   373   6.297   104.675   14.521   1.00   53.94   U       ATOM   587   N   GLN   U   374   5.575   105.528   16.472   1.00   58.34   U       ATOM   588   CA   GLN   U   374   5.765   106.904   16.016   1.00   60.92   U       ATOM   589   CB   GLN   U   374   5.473   107.935   17.121   1.00   72.96   U       ATOM   590   CG   GLN   U   374   4.001   108.340   17.317   1.00   90.65   U       ATOM   591   CD   GLN   U   374   3.824   109.665   18.108   1.00   96.81   U       ATOM   592   OE1   GLN   U   374   4.387   109.853   19.198   1.00   95.94   U       ATOM   593   NE2   GLN   U   374   3.022   110.576   17.553   1.00   99.87   U       ATOM   594   C   GLN   U   374   7.233   107.049   15.634   1.00   56.05   U       ATOM   595   O   GLN   U   374   7.556   107.320   14.480   1.00   54.14   U       ATOM   596   N   ALA   U   375   8.105   106.858   16.627   1.00   50.29   U       ATOM   597   CA   ALA   U   375   9.562   106.968   16.481   1.00   45.90   U       ATOM   598   CB   ALA   U   375   10.237   106.440   17.733   1.00   36.92   U       ATOM   599   C   ALA   U   375   10.164   106.285   15.244   1.00   46.33   U       ATOM   600   O   ALA   U   375   11.085   106.810   14.620   1.00   41.94   U       ATOM   601   N   GLY   U   376   9.664   105.106   14.902   1.00   45.56   U       ATOM   602   CA   GLY   U   376   10.186   104.425   13.740   1.00   42.75   U       ATOM   603   C   GLY   U   376   11.000   103.226   14.126   1.00   43.80   U       ATOM   604   O   GLY   U   376   11.761   102.687   13.311   1.00   48.74   U       ATOM   605   N   VAL   U   377   10.845   102.826   15.381   1.00   39.82   U       ATOM   606   CA   VAL   U   377   11.552   101.679   15.915   1.00   42.16   U       ATOM   607   CB   VAL   U   377   12.483   102.067   17.072   1.00   38.64   U       ATOM   608   CG1   VAL   U   377   13.687   102.855   16.538   1.00   41.57   U       ATOM   609   CG2   VAL   U   377   11.712   102.851   18.108   1.00   24.01   U       ATOM   610   C   VAL   U   377   10.509   100.714   16.431   1.00   47.28   U       ATOM   611   O   VAL   U   377   10.682   100.074   17.479   1.00   50.04   U       ATOM   612   N   GLY   U   378   9.421   100.611   15.679   1.00   47.61   U       ATOM   613   CA   GLY   U   378   8.338   99.744   16.087   1.00   42.89   U       ATOM   614   C   GLY   U   378   8.637   98.279   15.932   1.00   41.14   U       ATOM   615   O   GLY   U   378   8.259   97.478   16.761   1.00   48.83   U       ATOM   616   N   ALA   U   379   9.336   97.917   14.876   1.00   45.44   U       ATOM   617   CA   ALA   U   379   9.627   96.511   14.631   1.00   50.56   U       ATOM   618   CB   ALA   U   379   10.009   96.318   13.159   1.00   54.17   U       ATOM   619   C   ALA   U   379   10.712   95.919   15.507   1.00   52.59   U       ATOM   620   O   ALA   U   379   10.821   94.703   15.606   1.00   54.95   U       ATOM   621   N   ILE   U   380   11.497   96.771   16.158   1.00   52.15   U       ATOM   622   CA   ILE   U   380   12.619   96.302   16.957   1.00   43.86   U       ATOM   623   CB   ILE   U   380   13.917   96.838   16.346   1.00   42.13   U       ATOM   624   CG2   ILE   U   380   14.102   96.283   14.945   1.00   38.36   U       ATOM   625   CG1   ILE   U   380   13.844   98.366   16.296   1.00   29.73   U       ATOM   626   CD1   ILE   U   380   15.114   99.023   15.880   1.00   32.82   U       ATOM   627   C   ILE   U   380   12.638   96.647   18.442   1.00   45.23   U       ATOM   628   O   ILE   U   380   13.364   96.019   19.206   1.00   45.34   U       ATOM   629   N   PHE   U   381   11.856   97.639   18.852   1.00   41.47   U       ATOM   630   CA   PHE   U   381   11.834   98.077   20.250   1.00   39.86   U       ATOM   631   CB   PHE   U   381   10.536   98.812   20.520   1.00   40.79   U       ATOM   632   CG   PHE   U   381   10.577   99.631   21.751   1.00   38.51   U       ATOM   633   CD1   PHE   U   381   11.041   100.945   21.702   1.00   43.23   U       ATOM   634   CD2   PHE   U   381   10.225   99.076   22.976   1.00   31.79   U       ATOM   635   CE1   PHE   U   381   11.160   101.712   22.875   1.00   50.56   U       ATOM   636   CE2   PHE   U   381   10.338   99.820   24.153   1.00   40.15   U       ATOM   637   CZ   PHE   U   381   10.809   101.145   24.107   1.00   46.64   U       ATOM   638   C   PHE   U   381   12.081   97.057   21.393   1.00   38.24   U       ATOM   639   O   PHE   U   381   13.041   97.195   22.153   1.00   35.88   U       ATOM   640   N   ASP   U   382   11.214   96.057   21.530   1.00   36.81   U       ATOM   641   CA   ASP   U   382   11.370   95.040   22.584   1.00   41.40   U       ATOM   642   CB   ASP   U   382   10.287   93.949   22.481   1.00   48.31   U       ATOM   643   CG   ASP   U   382   8.897   94.435   22.894   1.00   53.81   U       ATOM   644   OD1   ASP   U   382   8.780   95.150   23.924   1.00   54.60   U       ATOM   645   OD2   ASP   U   382   7.919   94.071   22.189   1.00   51.69   U       ATOM   646   C   ASP   U   382   12.731   94.345   22.594   1.00   39.65   U       ATOM   647   O   ASP   U   382   13.439   94.371   23.592   1.00   41.97   U       ATOM   648   N   ARG   U   383   13.077   93.697   21.487   1.00   43.16   U       ATOM   649   CA   ARG   U   383   14.355   93.000   21.361   1.00   39.23   U       ATOM   650   CB   ARG   U   383   14.447   92.333   19.984   1.00   33.41   U       ATOM   651   CG   ARG   U   383   14.855   90.844   19.953   1.00   43.37   U       ATOM   652   CD   ARG   U   383   15.016   90.366   18.484   1.00   50.80   U       ATOM   653   NE   ARG   U   383   15.557   89.018   18.332   1.00   57.23   U       ATOM   654   CZ   AEG   U   383   16.858   88.718   18.348   1.00   74.35   U       ATOM   655   NH1   ARG   U   383   17.795   89.675   18.511   1.00   59.21   U       ATOM   656   NH2   ARG   U   383   17.221   87.441   18.196   1.00   76.48   U       ATOM   657   C   ARG   U   383   15.542   93.970   21.575   1.00   38.25   U       ATOM   658   O   ARG   U   383   16.539   93.600   22.189   1.00   38.14   U       ATOM   659   N   VAL   U   384   15.454   95.204   21.083   1.00   31.99   U       ATOM   660   CA   VAL   U   384   16.556   96.127   21.303   1.00   30.96   U       ATOM   661   CB   VAL   U   384   16.273   97.531   20.729   1.00   29.82   U       ATOM   662   CG1   VAL   U   384   17.224   98.561   21.338   1.00   21.88   U       ATOM   663   CG2   VAL   U   384   16.485   97.518   19.241   1.00   25.51   U       ATOM   664   C   VAL   U   384   16.838   96.232   22.800   1.00   34.32   U       ATOM   665   O   VAL   U   384   17.976   96.051   23.233   1.00   41.88   U       ATOM   666   N   LEU   U   385   15.817   96.493   23.602   1.00   30.94   U       ATOM   667   CA   LEU   U   385   16.029   96.608   25.036   1.00   30.42   U       ATOM   668   CB   LEU   U   385   14.720   96.993   25.724   1.00   28.36   U       ATOM   669   CG   LEU   U   385   14.070   98.331   25.373   1.00   37.72   U       ATOM   670   CD1   LEU   U   385   12.820   98.477   26.174   1.00   31.55   U       ATOM   671   CD2   LEU   U   385   14.994   99.495   25.684   1.00   38.29   U       ATOM   672   C   LEU   U   385   16.595   95.351   25.713   1.00   31.91   U       ATOM   673   O   LEU   U   385   17.476   95.439   26.569   1.00   33.34   U       ATOM   674   N   THR   U   386   16.109   94.179   25.321   1.00   26.65   U       ATOM   675   CA   THR   U   386   16.535   92.940   25.971   1.00   31.55   U       ATOM   676   CB   THR   U   386   15.385   91.910   26.010   1.00   34.28   U       ATOM   677   OG1   THR   U   386   15.014   91.541   24.677   1.00   44.67   U       ATOM   678   CG2   THR   U   386   14.171   92.497   26.708   1.00   31.26   U       ATOM   679   C   THR   U   386   17.764   92.215   25.458   1.00   36.23   U       ATOM   680   O   THR   U   386   18.501   91.638   26.254   1.00   40.01   U       ATOM   681   N   GLU   U   387   17.966   92.219   24.138   1.00   40.86   U       ATOM   682   CA   GLU   U   387   19.108   91.561   23.510   1.00   36.51   U       ATOM   683   CB   GLU   U   387   18.713   91.013   22.137   1.00   38.33   U       ATOM   684   CG   GLU   U   387   17.485   90.160   22.161   1.00   42.62   U       ATOM   685   CD   GLU   U   387   17.482   89.162   23.304   1.00   47.11   U       ATOM   686   OE1   GLU   U   387   18.256   88.166   23.254   1.00   44.10   U       ATOM   687   OE2   GLU   U   387   16.696   89.387   24.256   1.00   42.20   U       ATOM   688   C   GLU   U   387   20.337   92.468   23.350   1.00   36.93   U       ATOM   689   O   GLU   U   387   21.450   91.966   23.160   1.00   37.80   U       ATOM   690   N   LEU   U   388   20.141   93.787   23.401   1.00   28.40   U       ATOM   691   CA   LEU   U   388   21.253   94.710   23.267   1.00   30.94   U       ATOM   692   CB   LEU   U   388   21.128   95.542   21.990   1.00   28.29   U       ATOM   693   CG   LEU   U   388   21.185   94.698   20.704   1.00   30.69   U       ATOM   694   CD1   LEU   U   388   20.963   95.564   19.485   1.00   27.49   U       ATOM   695   CD2   LEU   U   388   22.517   93.980   20.626   1.00   22.93   U       ATOM   696   C   LEU   U   388   21.365   95.623   24.467   1.00   35.06   U       ATOM   697   O   LEU   U   388   22.353   95.562   25.203   1.00   36.04   U       ATOM   698   N   VAL   U   389   20.358   96.450   24.701   1.00   32.72   U       ATOM   699   CA   VAL   U   389   20.456   97.352   25.834   1.00   31.84   U       ATOM   700   CB   VAL   U   389   19.187   98.198   26.050   1.00   33.37   U       ATOM   701   CG1   VAL   U   389   19.404   99.110   27.259   1.00   27.98   U       ATOM   702   CG2   VAL   U   389   18.888   99.043   24.821   1.00   24.09   U       ATOM   703   C   VAL   U   389   20.769   96.626   27.132   1.00   30.80   U       ATOM   704   O   VAL   U   389   21.739   96.963   27.801   1.00   38.49   U       ATOM   705   N   ALA   U   390   19.962   95.636   27.494   1.00   32.86   U       ATOM   706   CA   ALA   U   390   20.193   94.893   28.736   1.00   33.12   U       ATOM   707   CB   ALA   U   390   19.120   93.861   28.927   1.00   30.29   U       ATOM   708   C   ALA   U   390   21.561   94.218   28.756   1.00   33.32   U       ATOM   709   O   ALA   U   390   22.336   94.396   29.680   1.00   32.84   U       ATOM   710   N   LYS   U   391   21.867   93.440   27.733   1.00   37.03   U       ATOM   711   CA   LYS   U   391   23.150   92.763   27.681   1.00   38.70   U       ATOM   712   CB   LYS   U   391   23.208   91.883   26.430   1.00   40.17   U       ATOM   713   CG   LYS   U   391   22.157   90.771   26.412   1.00   35.70   U       ATOM   714   CD   LYS   U   391   22.468   89.712   27.453   1.00   40.05   U       ATOM   715   CE   LYS   U   391   21.234   88.915   27.878   1.00   45.83   U       ATOM   716   NZ   LYS   U   391   21.521   88.077   29.099   1.00   49.07   U       ATOM   717   C   LYS   U   391   24.328   93.747   27.710   1.00   40.62   U       ATOM   718   O   LYS   U   391   25.410   93.424   28.234   1.00   33.01   U       ATOM   719   N   MET   U   392   24.115   94.942   27.153   1.00   40.44   U       ATOM   720   CA   MET   U   392   25.163   95.974   27.106   1.00   40.66   U       ATOM   721   CB   MET   U   392   24.731   97.145   26.229   1.00   35.96   U       ATOM   722   CG   MET   U   392   25.072   96.961   24.791   1.00   33.56   U       ATOM   723   SD   MET   U   392   24.440   98.258   23.783   1.00   40.35   U       ATOM   724   CE   MET   U   392   24.913   97.647   22.178   1.00   27.49   U       ATOM   725   C   MET   U   392   25.473   96.497   28.484   1.00   38.99   U       ATOM   726   O   MET   U   392   26.630   96.648   28.881   1.00   39.17   U       ATOM   727   N   ARG   U   393   24.398   96.790   29.191   1.00   37.45   U       ATOM   728   CA   ARG   U   393   24.453   97.291   30.541   1.00   32.99   U       ATOM   729   CB   ARG   U   393   23.045   97.654   30.969   1.00   34.44   U       ATOM   730   CG   ARG   U   393   22.929   98.436   32.223   1.00   41.19   U       ATOM   731   CD   ARG   U   393   21.610   99.172   32.177   1.00   47.37   U       ATOM   732   NE   ARG   U   393   20.517   98.254   31.880   1.00   55.20   U       ATOM   733   CZ   ARG   U   393   19.379   98.621   31.302   1.00   60.08   U       ATOM   734   NH1   ARG   U   393   19.185   99.893   30.958   1.00   50.39   U       ATOM   735   NH2   ARG   U   393   18.442   97.709   31.056   1.00   66.60   U       ATOM   736   C   ARG   U   393   25.025   96.191   31.419   1.00   28.95   U       ATOM   737   O   ARG   U   393   25.947   96.435   32.187   1.00   27.65   U       ATOM   738   N   GLU   U   394   24.505   94.973   31.287   1.00   26.38   U       ATOM   739   CA   GLU   U   394   25.006   93.862   32.089   1.00   32.40   U       ATOM   740   CB   GLU   U   394   24.355   92.548   31.658   1.00   34.10   U       ATOM   741   CG   GLU   U   394   22.857   92.493   31.857   1.00   47.11   U       ATOM   742   CD   GLU   U   394   22.255   91.185   31.350   1.00   57.63   U       ATOM   743   OE1   GLU   U   394   23.042   90.269   30.997   1.00   60.19   U       ATOM   744   OE2   GLU   U   394   21.005   91.071   31.308   1.00   57.06   U       ATOM   745   C   GLU   U   394   26.538   93.707   32.056   1.00   33.86   U       ATOM   746   O   GLU   U   394   27.146   93.459   33.082   1.00   33.65   U       ATOM   747   N   MET   U   395   27.161   93.854   30.888   1.00   37.99   U       ATOM   748   CA   MET   U   395   28.613   93.706   30.779   1.00   32.98   U       ATOM   749   CB   MET   U   395   29.005   93.009   29.468   1.00   36.56   U       ATOM   750   CG   MET   U   395   28.678   93.778   28.183   1.00   33.30   U       ATOM   751   SD   MET   U   395   29.054   92.793   26.707   1.00   37.42   U       ATOM   752   CE   MET   U   395   30.636   92.184   27.124   1.00   33.07   U       ATOM   753   C   MET   U   395   29.320   95.041   30.854   1.00   35.39   U       ATOM   754   O   MET   U   395   30.538   95.094   30.788   1.00   35.28   U       ATOM   755   N   LYS   U   396   28.567   96.125   30.980   1.00   27.78   U       ATOM   756   CA   LYS   U   396   29.203   97.411   31.059   1.00   29.20   U       ATOM   757   CB   LYS   U   396   30.001   97.486   32.358   1.00   32.38   U       ATOM   758   CG   LYS   U   396   29.118   97.516   33.605   1.00   43.32   U       ATOM   759   CD   LYS   U   396   29.916   97.831   34.872   1.00   54.00   U       ATOM   760   CE   LYS   U   396   29.011   97.989   36.092   1.00   57.36   U       ATOM   761   NZ   LYS   U   396   29.788   98.387   37.300   1.00   62.62   U       ATOM   762   C   LYS   U   396   30.108   97.621   29.847   1.00   30.91   U       ATOM   763   O   LYS   U   396   31.296   97.917   29.978   1.00   36.92   U       ATOM   764   N   MET   U   397   29.535   97.448   28.661   1.00   31.95   U       ATOM   765   CA   MET   U   397   30.265   97.620   27.407   1.00   35.62   U       ATOM   766   CB   MET   U   397   29.401   97.107   26.240   1.00   35.63   U       ATOM   767   CG   MET   U   397   29.977   97.373   24.858   1.00   34.00   U       ATOM   768   SD   MET   U   397   28.756   97.263   23.531   1.00   30.97   U       ATOM   769   CE   MET   U   397   28.855   95.574   23.156   1.00   31.90   U       ATOM   770   C   MET   U   397   30.575   99.109   27.224   1.00   33.23   U       ATOM   771   O   MET   U   397   29.668   99.926   27.139   1.00   36.18   U       ATOM   772   N   ASP   U   398   31.848   99.468   27.152   1.00   32.65   U       ATOM   773   CA   ASP   U   398   32.200   100.879   26.997   1.00   34.42   U       ATOM   774   CB   ASP   U   398   33.582   101.169   27.614   1.00   35.85   U       ATOM   775   CG   ASP   U   398   34.728   100.423   26.925   1.00   35.68   U       ATOM   776   OD1   ASP   U   398   34.792   100.441   25.677   1.00   38.98   U       ATOM   777   OD2   ASP   U   398   35.580   99.837   27.633   1.00   29.28   U       ATOM   778   C   ASP   U   398   32.167   101.405   25.559   1.00   39.08   U       ATOM   779   O   ASP   U   398   31.967   100.636   24.598   1.00   35.26   U       ATOM   780   N   LYS   U   399   32.366   102.724   25.441   1.00   37.68   U       ATOM   781   CA   LYS   U   399   32.378   103.450   24.165   1.00   36.84   U       ATOM   782   CB   LYS   U   399   32.656   104.953   24.387   1.00   42.08   U       ATOM   783   CG   LYS   U   399   31.637   105.771   25.183   1.00   48.45   U       ATOM   784   CD   LYS   U   399   32.218   107.182   25.482   1.00   53.38   U       ATOM   785   CE   LYS   U   399   31.441   107.945   26.589   1.00   53.01   U       ATOM   786   NZ   LYS   U   399   32.125   109.197   27.093   1.00   46.97   U       ATOM   787   C   LYS   U   399   33.442   102.926   23.172   1.00   35.69   U       ATOM   788   O   LYS   U   399   33.209   102.897   21.962   1.00   34.85   U       ATOM   789   N   THR   U   400   34.610   102.536   23.673   1.00   26.07   U       ATOM   790   CA   THR   U   400   35.684   102.061   22.814   1.00   29.08   U       ATOM   791   CB   THR   U   400   36.964   101.761   23.627   1.00   32.30   U       ATOM   792   OG1   THR   U   400   37.430   102.962   24.238   1.00   27.35   U       ATOM   793   CG2   THR   U   400   38.052   101.229   22.752   1.00   22.92   U       ATOM   794   C   THR   U   400   35.229   100.794   22.133   1.00   35.87   U       ATOM   795   O   THR   U   400   35.336   100.640   20.905   1.00   38.99   U       ATOM   796   N   GLU   U   401   34.715   99.887   22.953   1.00   36.25   U       ATOM   797   CA   GLU   U   401   34.226   98.604   22.484   1.00   34.75   U       ATOM   798   CB   GLU   U   401   33.757   97.799   23.691   1.00   30.59   U       ATOM   799   CG   GLU   U   401   34.890   97.654   24.684   1.00   35.88   U       ATOM   800   CD   GLU   U   401   34.537   96.872   25.915   1.00   36.12   U       ATOM   801   OE1   GLU   U   401   33.547   97.229   26.595   1.00   29.09   U       ATOM   802   OE2   GLU   U   401   35.271   95.903   26.205   1.00   36.39   U       ATOM   803   C   GLU   U   401   33.110   98.811   21.463   1.00   33.50   U       ATOM   804   O   GLU   U   401   33.123   98.217   20.376   1.00   32.04   U       ATOM   805   N   LEU   U   402   32.162   99.682   21.806   1.00   27.64   U       ATOM   806   CA   LEU   U   402   31.056   99.962   20.924   1.00   21.36   U       ATOM   807   CB   LEU   U   402   30.185   101.088   21.444   1.00   24.42   U       ATOM   808   CG   LEU   U   402   28.932   101.101   20.566   1.00   24.82   U       ATOM   809   CD1   LEU   U   402   28.024   99.963   21.003   1.00   35.56   U       ATOM   810   CD2   LEU   U   402   28.204   102.372   20.704   1.00   21.56   U       ATOM   811   C   LEU   U   402   31.580   100.373   19.586   1.00   24.94   U       ATOM   812   O   LEU   U   402   31.253   99.746   18.586   1.00   32.83   U       ATOM   813   N   GLY   U   403   32.375   101.442   19.561   1.00   24.62   U       ATOM   814   CA   GLY   U   403   32.945   101.925   18.311   1.00   22.95   U       ATOM   815   C   GLY   U   403   33.596   100.807   17.518   1.00   27.61   U       ATOM   816   O   GLY   U   403   33.468   100.738   16.303   1.00   26.58   U       ATOM   817   N   CYS   U   404   34.300   99.924   18.219   1.00   31.04   U       ATOM   818   CA   CYS   U   404   34.964   98.784   17.600   1.00   29.61   U       ATOM   819   CB   CYS   U   404   35.710   97.977   18.651   1.00   33.74   U       ATOM   820   SG   CYS   U   404   37.344   98.576   19.006   1.00   30.16   U       ATOM   821   C   CYS   U   404   33.988   97.861   16.897   1.00   35.64   U       ATOM   822   O   CYS   U   404   34.179   97.501   15.726   1.00   37.95   U       ATOM   823   N   LEU   U   405   32.952   97.450   17.617   1.00   29.69   U       ATOM   824   CA   LEU   U   405   31.977   96.564   17.020   1.00   31.19   U       ATOM   825   CB   LEU   U   405   30.935   96.136   18.052   1.00   23.77   U       ATOM   826   CG   LEU   U   405   31.439   95.309   19.227   1.00   23.97   U       ATOM   827   CD1   LEU   U   405   30.371   95.289   20.274   1.00   20.63   U       ATOM   828   CD2   LEU   U   405   31.838   93.905   18.782   1.00   13.06   U       ATOM   829   C   LEU   U   405   31.305   97.259   15.844   1.00   27.59   U       ATOM   830   O   LEU   U   405   31.135   96.668   14.782   1.00   31.16   U       ATOM   831   N   ARG   U   406   30.929   98.517   16.029   1.00   23.58   U       ATOM   832   CA   ARG   U   406   30.272   99.263   14.968   1.00   27.91   U       ATOM   833   CB   ARG   U   406   30.021   100.691   15.418   1.00   20.43   U       ATOM   834   CG   ARG   U   406   28.578   101.027   15.672   1.00   24.55   U       ATOM   835   CD   ARG   U   406   28.504   102.506   15.940   1.00   34.29   U       ATOM   836   NE   ARG   U   406   27.260   103.138   15.517   1.00   34.43   U       ATOM   837   CZ   ARG   U   406   27.092   104.457   15.521   1.00   39.30   U       ATOM   838   NH1   ARG   U   406   28.087   105.231   15.926   1.00   35.42   U       ATOM   839   NH2   ARG   U   406   25.953   105.011   15.114   1.00   41.12   U       ATOM   840   C   ARG   U   406   31.106   99.266   13.693   1.00   31.32   U       ATOM   841   O   ARG   U   406   30.575   99.237   12.584   1.00   32.23   U       ATOM   842   N   SER   U   407   32.419   99.298   13.866   1.00   29.69   U       ATOM   843   CA   SER   U   407   33.349   99.305   12.755   1.00   26.40   U       ATOM   844   CB   SER   U   407   34.711   99.770   13.230   1.00   23.92   U       ATOM   845   OG   SER   U   407   34.570   101.107   13.640   1.00   18.62   U       ATOM   846   C   SER   U   407   33.461   97.959   12.101   1.00   28.35   U       ATOM   847   O   SER   U   407   33.672   97.870   10.893   1.00   28.39   U       ATOM   848   N   ILE   U   408   33.357   96.908   12.907   1.00   33.99   U       ATOM   849   CA   ILE   U   408   33.386   95.554   12.372   1.00   30.44   U       ATOM   850   CB   ILE   U   408   33.331   94.526   13.492   1.00   23.83   U       ATOM   851   CG2   ILE   U   408   33.150   93.161   12.896   1.00   11.06   U       ATOM   852   CG1   ILE   U   408   34.582   94.660   14.365   1.00   20.58   U       ATOM   853   CD1   ILE   U   408   34.814   93.494   15.302   1.00   24.44   U       ATOM   854   C   ILE   U   408   32.132   95.431   11.489   1.00   32.15   U       ATOM   855   O   ILE   U   408   32.138   94.755   10.464   1.00   35.94   U       ATOM   856   N   VAL   U   409   31.065   96.119   11.894   1.00   31.92   U       ATOM   857   CA   VAL   U   409   29.816   96.134   11.146   1.00   32.54   U       ATOM   858   CB   VAL   U   409   28.635   96.731   11.992   1.00   34.95   U       ATOM   859   CG1   VAL   U   409   27.335   96.777   11.170   1.00   26.70   U       ATOM   860   CG2   VAL   U   409   28.431   95.893   13.251   1.00   24.09   U       ATOM   861   C   VAL   U   409   29.988   96.955   9.878   1.00   31.14   U       ATOM   862   O   VAL   U   409   29.588   96.523   8.816   1.00   38.10   U       ATOM   863   N   LEU   U   410   30.584   98.138   9.978   1.00   34.55   U       ATOM   864   CA   LEU   U   410   30.784   98.989   8.797   1.00   32.93   U       ATOM   865   CB   LEU   U   410   31.380   100.337   9.202   1.00   25.79   U       ATOM   866   CG   LEU   U   410   31.701   101.291   8.053   1.00   26.02   U       ATOM   867   CD1   LEU   U   410   30.479   102.056   7.707   1.00   29.87   U       ATOM   868   CD2   LEU   U   410   32.825   102.247   8.436   1.00   27.59   U       ATOM   869   C   LEU   U   410   31.705   98.340   7.751   1.00   36.39   U       ATOM   870   O   LEU   U   410   31.441   98.413   6.538   1.00   37.38   U       ATOM   871   N   PHE   U   411   32.782   97.711   8.226   1.00   36.01   U       ATOM   872   CA   PHE   U   411   33.752   97.074   7.345   1.00   36.64   U       ATOM   873   CB   PHE   U   411   35.177   97.147   7.920   1.00   40.37   U       ATOM   874   CG   PHE   U   411   35.781   98.533   7.883   1.00   42.32   U       ATOM   875   CD1   PHE   U   411   35.823   99.257   6.696   1.00   40.55   U       ATOM   876   CD2   PHE   U   411   36.264   99.127   9.036   1.00   39.00   U       ATOM   877   CE1   PHE   U   411   36.328   100.548   6.662   1.00   37.25   U       ATOM   878   CE2   PHE   U   411   36.768   100.414   9.001   1.00   42.65   U       ATOM   879   CZ   PHE   U   411   36.798   101.124   7.810   1.00   42.34   U       ATOM   880   C   PHE   U   411   33.394   95.640   7.106   1.00   38.55   U       ATOM   881   O   PHE   U   411   34.123   94.741   7.523   1.00   32.24   U       ATOM   882   N   ASN   U   412   32.270   95.456   6.412   1.00   40.99   U       ATOM   883   CA   ASN   U   412   31.729   94.155   6.048   1.00   39.36   U       ATOM   884   CB   ASN   U   412   30.235   94.148   6.360   1.00   38.79   U       ATOM   885   CG   ASN   U   412   29.476   93.047   5.644   1.00   40.78   U       ATOM   886   OD1   ASN   U   412   29.958   91.915   5.492   1.00   24.43   U       ATOM   887   ND2   ASN   U   412   28.255   93.374   5.217   1.00   36.88   U       ATOM   888   C   ASN   U   412   31.998   93.825   4.578   1.00   41.92   U       ATOM   889   O   ASN   U   412   31.423   94.426   3.661   1.00   40.06   U       ATOM   890   N   PRO   U   413   32.902   92.862   4.338   1.00   45.60   U       ATOM   891   CD   PRO   U   413   33.680   92.144   5.365   1.00   41.57   U       ATOM   892   CA   PRO   U   413   33.285   92.424   2.991   1.00   44.83   U       ATOM   893   CB   PRO   U   413   34.516   91.566   3.250   1.00   39.25   U       ATOM   894   CG   PRO   U   413   34.223   90.974   4.588   1.00   39.15   U       ATOM   895   C   PRO   U   413   32.201   91.676   2.234   1.00   45.73   U       ATOM   896   O   PRO   U   413   32.222   91.626   1.002   1.00   52.42   U       ATOM   897   N   GLU   U   414   31.251   91.091   2.956   1.00   43.05   U       ATOM   898   CA   GLU   U   414   30.183   90.374   2.291   1.00   39.64   U       ATOM   899   CB   GLU   U   414   29.562   89.320   3.197   1.00   42.37   U       ATOM   900   CG   GLU   U   414   30.499   88.603   4.149   1.00   60.36   U       ATOM   901   CD   GLU   U   414   31.506   87.697   3.463   1.00   71.15   U       ATOM   902   OE1   GLU   U   414   32.022   86.778   4.147   1.00   71.72   U       ATOM   903   OE2   GLU   U   414   31.786   87.910   2.256   1.00   74.25   U       ATOM   904   C   GLU   U   414   29.111   91.386   1.911   1.00   42.28   U       ATOM   905   O   GLU   U   414   28.000   91.010   1.542   1.00   41.06   U       ATOM   906   N   ALA   U   415   29.414   92.678   2.033   1.00   44.92   U       ATOM   907   CA   ALA   U   415   28.420   93.676   1.646   1.00   46.88   U       ATOM   908   CB   ALA   U   415   28.942   95.101   1.877   1.00   39.65   U       ATOM   909   C   ALA   U   415   28.148   93.420   0.158   1.00   47.70   U       ATOM   910   O   ALA   U   415   29.050   93.055   −0.615   1.00   40.83   U       ATOM   911   N   LYS   U   416   26.890   93.587   −0.216   1.00   50.22   U       ATOM   912   CA   LYS   U   416   26.416   93.351   −1.577   1.00   54.17   U       ATOM   913   CB   LYS   U   416   24.889   93.491   −1.608   1.00   61.27   U       ATOM   914   CG   LYS   U   416   24.209   93.154   −0.266   1.00   67.54   U       ATOM   915   CD   LYS   U   416   24.543   94.157   0.855   1.00   57.37   U       ATOM   916   CE   LYS   U   416   24.303   93.533   2.211   1.00   50.72   U       ATOM   917   NZ   LYS   U   416   22.901   93.042   2.362   1.00   56.29   U       ATOM   918   C   LYS   U   416   27.014   94.280   −2.623   1.00   50.92   U       ATOM   919   O   LYS   U   416   26.849   95.493   −2.551   1.00   51.14   U       ATOM   920   N   GLY   U   417   27.705   93.712   −3.599   1.00   48.01   U       ATOM   921   CA   GLY   U   417   28.281   94.530   −4.654   1.00   49.51   U       ATOM   922   C   GLY   U   417   29.534   95.307   −4.303   1.00   49.64   U       ATOM   923   O   GLY   U   417   30.071   96.041   −5.129   1.00   44.68   U       ATOM   924   N   LEU   U   418   29.991   95.165   −3.066   1.00   54.51   U       ATOM   925   CA   LEU   U   418   31.205   95.837   −2.622   1.00   48.92   U       ATOM   926   CB   LEU   U   418   31.587   95.340   −1.225   1.00   41.73   U       ATOM   927   CG   LEU   U   418   32.899   95.860   −0.671   1.00   35.06   U       ATOM   928   CD1   LEU   U   418   32.768   97.354   −0.506   1.00   40.21   U       ATOM   929   CD2   LEU   U   418   33.224   95.171   0.639   1.00   28.86   U       ATOM   930   C   LEU   U   418   32.291   95.459   −3.633   1.00   45.94   U       ATOM   931   O   LEU   U   418   32.422   94.297   −4.026   1.00   36.89   U       ATOM   932   N   LYS   U   419   33.069   96.433   −4.060   1.00   45.84   U       ATOM   933   CA   LYS   U   419   34.106   96.134   −5.024   1.00   49.15   U       ATOM   934   CB   LYS   U   419   34.329   97.351   −5.928   1.00   52.16   U       ATOM   935   CG   LYS   U   419   35.194   97.128   −7.152   1.00   56.76   U       ATOM   936   CD   LYS   U   419   35.818   98.459   −7.609   1.00   70.83   U       ATOM   937   CE   LYS   U   419   34.778   99.608   −7.755   1.00   77.52   U       ATOM   938   NZ   LYS   U   419   35.404   100.967   −8.007   1.00   72.38   U       ATOM   939   C   LYS   U   419   35.395   95.751   −4.307   1.00   48.58   U       ATOM   940   O   LYS   U   419   35.939   94.670   −4.542   1.00   51.80   U       ATOM   941   N   SER   U   420   35.863   96.619   −3.412   1.00   42.58   U       ATOM   942   CA   SER   U   420   37.110   96.376   −2.695   1.00   44.19   U       ATOM   943   CB   SER   U   420   37.672   97.697   −2.194   1.00   45.46   U       ATOM   944   OG   SER   U   420   36.928   98.781   −2.726   1.00   46.57   U       ATOM   945   C   SER   U   420   36.933   95.435   −1.525   1.00   47.56   U       ATOM   946   O   SER   U   420   37.248   95.784   −0.391   1.00   52.59   U       ATOM   947   N   THR   U   421   36.443   94.233   −1.792   1.00   44.38   U       ATOM   948   CA   THR   U   421   36.224   93.283   −0.720   1.00   42.89   U       ATOM   949   CB   THR   U   421   35.577   91.984   −1.239   1.00   38.16   U       ATOM   950   OG1   THR   U   421   36.442   91.353   −2.182   1.00   39.40   U       ATOM   951   CG2   THR   U   421   34.240   92.292   −1.907   1.00   45.42   U       ATOM   952   C   THR   U   421   37.495   92.945   0.044   1.00   43.04   U       ATOM   953   O   THR   U   421   37.505   92.954   1.272   1.00   46.52   U       ATOM   954   N   GLN   U   422   38.575   92.666   −0.670   1.00   44.07   U       ATOM   955   CA   GLN   U   422   39.810   92.331   0.009   1.00   44.59   U       ATOM   956   CB   GLN   U   422   40.896   91.968   −1.003   1.00   50.43   U       ATOM   957   CG   GLN   U   422   42.105   91.358   −0.319   1.00   56.93   U       ATOM   958   CD   GLN   U   422   41.709   90.282   0.702   1.00   66.07   U       ATOM   959   OE1   GLN   U   422   41.338   89.162   0.331   1.00   71.38   U       ATOM   960   NE2   GLN   U   422   41.776   90.626   1.993   1.00   64.40   U       ATOM   961   C   GLN   U   422   40.289   93.466   0.919   1.00   43.80   U       ATOM   962   O   GLN   U   422   40.727   93.234   2.042   1.00   36.35   U       ATOM   963   N   GLN   U   423   40.206   94.700   0.440   1.00   45.96   U       ATOM   964   CA   GLN   U   423   40.638   95.823   1.256   1.00   43.51   U       ATOM   965   CB   GLN   U   423   40.496   97.120   0.447   1.00   44.53   U       ATOM   966   CG   GLN   U   423   40.954   98.390   1.169   1.00   49.41   U       ATOM   967   CD   GLN   U   423   42.060   98.155   2.198   1.00   51.38   U       ATOM   968   OE1   GLN   U   423   43.087   97.541   1.909   1.00   55.81   U       ATOM   969   NE2   GLN   U   423   41.848   98.655   3.408   1.00   50.67   U       ATOM   970   C   GLN   U   423   39.819   95.862   2.555   1.00   43.42   U       ATOM   971   O   GLN   U   423   40.362   95.696   3.658   1.00   39.70   U       ATOM   972   N   VAL   U   424   38.511   96.066   2.398   1.00   39.62   U       ATOM   973   CA   VAL   U   424   37.543   96.121   3.495   1.00   33.70   U       ATOM   974   CB   VAL   U   424   36.119   96.067   2.908   1.00   32.61   U       ATOM   975   CG1   VAL   U   424   35.101   95.797   3.983   1.00   24.92   U       ATOM   976   CG2   VAL   U   424   35.818   97.385   2.187   1.00   36.03   U       ATOM   977   C   VAL   U   424   37.740   94.988   4.526   1.00   37.29   U       ATOM   978   O   VAL   U   424   37.546   95.162   5.730   1.00   39.08   U       ATOM   979   N   GLU   U   425   38.130   93.819   4.053   1.00   32.96   U       ATOM   980   CA   GLU   U   425   38.366   92.713   4.943   1.00   27.56   U       ATOM   981   CB   GLU   U   425   38.551   91.455   4.117   1.00   24.43   U       ATOM   982   CG   GLU   U   425   39.041   90.274   4.883   1.00   31.65   U       ATOM   983   CD   GLU   U   425   38.097   89.845   5.974   1.00   38.65   U       ATOM   984   OE1   GLU   U   425   36.902   90.192   5.878   1.00   46.22   U       ATOM   985   OE2   GLU   U   425   38.551   89.154   6.916   1.00   35.34   U       ATOM   986   C   GLU   U   425   39.593   92.989   5.818   1.00   32.07   U       ATOM   987   O   GLU   U   425   39.536   92.800   7.030   1.00   25.52   U       ATOM   988   N   ASN   U   426   40.694   93.450   5.219   1.00   35.40   U       ATOM   989   CA   ASN   U   426   41.911   93.733   5.993   1.00   39.46   U       ATOM   990   CB   ASN   U   426   43.056   94.262   5.121   1.00   44.98   U       ATOM   991   CG   ASN   U   426   43.538   93.242   4.099   1.00   56.28   U       ATOM   992   OD1   ASN   U   426   43.488   92.026   4.332   1.00   60.50   U       ATOM   993   ND2   ASN   U   426   44.021   93.732   2.964   1.00   53.75   U       ATOM   994   C   ASN   U   426   41.613   94.755   7.058   1.00   39.97   U       ATOM   995   O   ASN   U   426   42.164   94.690   8.166   1.00   40.06   U       ATOM   996   N   LEU   U   427   40.747   95.705   6.719   1.00   36.37   U       ATOM   997   CA   LEU   U   427   40.353   96.735   7.669   1.00   34.77   U       ATOM   998   CB   LEU   U   427   39.507   97.801   6.973   1.00   33.42   U       ATOM   999   CG   LEU   U   427   40.177   98.753   5.989   1.00   34.01   U       ATOM   1000   CD1   LEU   U   427   39.120   99.513   5.193   1.00   28.60   U       ATOM   1001   CD2   LEU   U   427   41.060   99.710   6.754   1.00   26.72   U       ATOM   1002   C   LEU   U   427   39.563   96.117   8.832   1.00   37.46   U       ATOM   1003   O   LEU   U   427   39.790   96.444   9.996   1.00   36.46   U       ATOM   1004   N   ARG   U   428   38.631   95.226   8.518   1.00   36.70   U       ATOM   1005   CA   ARG   U   428   37.836   94.581   9.564   1.00   39.47   U       ATOM   1006   CB   ARG   U   428   36.839   93.580   8.953   1.00   40.08   U       ATOM   1007   CG   ARG   U   428   35.825   92.988   9.921   1.00   23.37   U       ATOM   1008   CD   ARG   U   428   35.405   91.634   9.431   1.00   40.22   U       ATOM   1009   NE   ARG   U   428   34.019   91.230   9.725   1.00   43.20   U       ATOM   1010   CZ   ARG   U   428   32.941   91.863   9.283   1.00   27.82   U       ATOM   1011   NH1   ARG   U   428   33.071   92.943   8.544   1.00   40.71   U       ATOM   1012   NH2   ARG   U   428   31.742   91.386   9.523   1.00   27.69   U       ATOM   1013   C   ARG   U   428   38.746   93.825   10.515   1.00   37.61   U       ATOM   1014   O   ARG   U   428   38.546   93.840   11.730   1.00   35.39   U       ATOM   1015   N   GLU   U   429   39.742   93.163   9.938   1.00   37.57   U       ATOM   1016   CA   GLU   U   429   40.678   92.366   10.699   1.00   39.44   U       ATOM   1017   CB   GLU   U   429   41.512   91.530   9.751   1.00   43.58   U       ATOM   1018   CG   GLU   U   429   40.680   90.717   8.782   1.00   51.00   U       ATOM   1019   CD   GLU   U   429   41.442   89.532   8.227   1.00   54.03   U       ATOM   1020   OE1   GLU   U   429   42.136   88.874   9.025   1.00   59.29   U       ATOM   1021   OE2   GLU   U   429   41.341   89.239   7.015   1.00   53.59   U       ATOM   1022   C   GLU   U   429   41.567   93.166   11.641   1.00   42.36   U       ATOM   1023   O   GLU   U   429   42.022   92.619   12.649   1.00   45.72   U       ATOM   1024   N   LYS   U   430   41.821   94.442   11.323   1.00   40.65   U       ATOM   1025   CA   LYS   U   430   42.610   95.317   12.204   1.00   36.40   U       ATOM   1026   CB   LYS   U   430   42.848   96.691   11.573   1.00   38.62   U       ATOM   1027   CG   LYS   U   430   43.540   96.660   10.241   1.00   47.84   U       ATOM   1028   CD   LYS   U   430   44.948   96.101   10.323   1.00   54.43   U       ATOM   1029   CE   LYS   U   430   45.672   96.253   8.984   1.00   55.55   U       ATOM   1030   NZ   LYS   U   430   47.129   95.979   9.116   1.00   58.55   U       ATOM   1031   C   LYS   U   430   41.773   95.511   13.469   1.00   29.86   U       ATOM   1032   O   LYS   U   430   42.252   95.277   14.582   1.00   32.21   U       ATOM   1033   N   VAL   U   431   40.525   95.943   13.281   1.00   20.84   U       ATOM   1034   CA   VAL   U   431   39.594   96.137   14.384   1.00   25.88   U       ATOM   1035   CB   VAL   U   431   38.143   96.411   13.873   1.00   23.91   U       ATOM   1036   CG1   VAL   U   431   37.212   96.606   15.064   1.00   27.22   U       ATOM   1037   CG2   VAL   U   432   38.091   97.652   12.988   1.00   13.93   U       ATOM   1038   C   VAL   U   431   39.561   94.901   15.319   1.00   32.07   U       ATOM   1039   O   VAL   U   431   39.465   95.028   16.545   1.00   34.56   U       ATOM   1040   N   TYR   U   432   39.634   93.702   14.750   1.00   29.60   U       ATOM   1041   CA   TYR   U   432   39.610   92.504   15.574   1.00   28.79   U       ATOM   1042   CB   TYR   U   432   39.681   91.250   14.707   1.00   26.26   U       ATOM   1043   CG   TYR   U   432   38.407   90.812   14.019   1.00   28.57   U       ATOM   1044   CD1   TYR   U   432   38.467   89.932   12.942   1.00   31.46   U       ATOM   1045   CE1   TYR   U   432   37.338   89.530   12.271   1.00   30.13   U       ATOM   1046   CD2   TYR   U   432   37.154   91.279   14.413   1.00   35.44   U       ATOM   1047   CE2   TYR   U   432   36.000   90.877   13.731   1.00   33.27   U       ATOM   1048   CZ   TYR   U   432   36.108   89.998   12.661   1.00   32.17   U       ATOM   1049   OH   TYR   U   432   34.996   89.551   11.979   1.00   35.83   U       ATOM   1050   C   TYR   U   432   40.812   92.512   16.505   1.00   30.84   U       ATOM   1051   O   TYR   U   432   40.716   92.191   17.692   1.00   34.48   U       ATOM   1052   N   ALA   U   433   41.955   92.869   15.934   1.00   31.75   U       ATOM   1053   CA   ALA   U   433   43.211   92.907   16.657   1.00   28.58   U       ATOM   1054   CB   ALA   U   433   44.318   93.194   15.725   1.00   18.16   U       ATOM   1055   C   ALA   U   433   43.172   93.961   17.709   1.00   29.75   U       ATOM   1056   O   ALA   U   433   43.452   93.689   18.880   1.00   31.28   U       ATOM   1057   N   ILE   U   434   42.838   95.172   17.282   1.00   26.79   U       ATOM   1058   CA   ILE   U   434   42.760   96.313   18.187   1.00   28.71   U       ATOM   1059   CB   ILE   U   434   42.248   97.533   17.435   1.00   28.12   U       ATOM   1060   CG2   ILE   U   434   41.861   98.618   18.399   1.00   20.04   U       ATOM   1061   CG1   ILE   U   434   43.308   97.986   16.431   1.00   32.44   U       ATOM   1062   CD1   ILE   U   434   42.846   99.059   15.470   1.00   37.48   U       ATOM   1063   C   ILE   U   434   41.844   96.008   19.369   1.00   32.28   U       ATOM   1064   O   ILE   U   434   42.242   96.126   20.521   1.00   31.88   U       ATOM   1065   N   LEU   U   435   40.622   95.590   19.061   1.00   34.58   U       ATOM   1066   CA   LEU   U   435   39.626   95.255   20.064   1.00   30.55   U       ATOM   1067   CB   LEU   U   435   38.332   94.848   19.383   1.00   24.76   U       ATOM   1068   CG   LEU   U   435   37.245   94.435   20.358   1.00   22.75   U       ATOM   1069   CD1   LEU   U   435   36.888   95.597   21.287   1.00   14.85   U       ATOM   1070   CD2   LEU   U   435   36.055   93.992   19.572   1.00   20.23   U       ATOM   1071   C   LEU   U   435   40.061   94.137   21.000   1.00   33.58   U       ATOM   1072   O   LEU   U   435   39.782   94.189   22.193   1.00   36.34   U       ATOM   1073   N   GLU   U   436   40.728   93.115   20.470   1.00   35.92   U       ATOM   1074   CA   GLU   U   436   41.175   92.010   21.307   1.00   36.91   U       ATOM   1075   CB   GLU   U   436   41.803   90.914   20.448   1.00   39.15   U       ATOM   1076   CG   GLU   U   436   42.215   89.619   21.195   1.00   47.97   U       ATOM   1077   CD   GLU   U   436   43.422   89.797   22.130   1.00   57.74   U       ATOM   1078   OE1   GLU   U   436   44.370   90.522   21.752   1.00   57.59   U       ATOM   1079   OE2   GLU   U   436   43.431   89.197   23.237   1.00   59.28   U       ATOM   1080   C   GLU   U   436   42.192   92.546   22.308   1.00   39.00   U       ATOM   1081   O   GLU   U   436   42.077   92.330   23.516   1.00   43.08   U       ATOM   1082   N   GLU   U   437   43.179   93.272   21.806   1.00   33.63   U       ATOM   1083   CA   GLU   U   437   44.205   93.830   22.666   1.00   33.97   U       ATOM   1084   CB   GLU   U   437   45.288   94.465   21.788   1.00   35.76   U       ATOM   1085   CG   GLU   U   437   45.654   95.892   22.072   1.00   42.35   U       ATOM   1086   CD   GLU   U   437   46.806   95.998   23.013   1.00   46.27   U       ATOM   1087   OE1   GLU   U   437   47.829   95.318   22.791   1.00   52.89   U       ATOM   1088   OE2   GLU   U   437   46.690   96.773   23.977   1.00   54.39   U       ATOM   1089   C   GLU   U   437   43.620   94.828   23.666   1.00   37.00   U       ATOM   1090   O   GLU   U   437   44.014   94.850   24.831   1.00   35.19   U       ATOM   1091   N   TYR   U   438   42.655   95.633   23.229   1.00   38.30   U       ATOM   1092   CA   TYR   U   438   42.041   96.622   24.111   1.00   31.99   U       ATOM   1093   CB   TYR   U   438   41.003   97.431   23.367   1.00   21.67   U       ATOM   1094   CG   TYR   U   438   40.195   98.266   24.315   1.00   31.24   U       ATOM   1095   CD1   TYR   U   438   40.634   99.513   24.705   1.00   27.07   U       ATOM   1096   CE1   TYR   U   438   39.894   100.282   25.577   1.00   22.39   U       ATOM   1097   CD2   TYR   U   438   38.983   97.801   24.837   1.00   35.07   U       ATOM   1098   CE2   TYR   U   438   38.237   98.573   25.713   1.00   30.79   U       ATOM   1099   CZ   TYR   U   438   38.704   99.817   26.074   1.00   25.62   U       ATOM   1100   OH   TYR   U   438   37.974   100.624   26.909   1.00   33.17   U       ATOM   1101   C   TYR   U   438   41.372   96.015   25.330   1.00   31.47   U       ATOM   1102   O   TYR   U   438   41.455   96.573   26.424   1.00   25.85   U       ATOM   1103   N   CYS   U   439   40.673   94.897   25.123   1.00   31.38   U       ATOM   1104   CA   CYS   U   439   39.992   94.203   26.211   1.00   36.18   U       ATOM   1105   CB   CYS   U   439   39.130   93.070   25.688   1.00   31.50   U       ATOM   1106   SG   CYS   U   439   37.746   93.633   24.744   1.00   47.00   U       ATOM   1107   C   CYS   U   439   41.020   93.623   27.136   1.00   37.71   U       ATOM   1108   O   CYS   U   439   40.955   93.808   28.342   1.00   43.56   U       ATOM   1109   N   ARG   U   440   41.974   92.914   26.550   1.00   35.22   U       ATOM   1110   CA   ARG   U   440   43.046   92.292   27.302   1.00   33.73   U       ATOM   1111   CB   ARG   U   440   44.042   91.688   26.319   1.00   33.72   U       ATOM   1112   CG   ARG   U   440   44.799   90.454   26.800   1.00   33.46   U       ATOM   1113   CD   ARG   U   440   45.700   89.954   25.690   1.00   36.28   U       ATOM   1114   NE   ARG   U   440   46.605   91.014   25.248   1.00   49.83   U       ATOM   1115   CZ   ARG   U   440   46.961   91.203   23.982   1.00   58.58   U       ATOM   1116   NH1   ARG   U   440   46.485   90.394   23.038   1.00   65.49   U       ATOM   1117   NH2   ARG   U   440   47.780   92.201   23.657   1.00   54.79   U       ATOM   1118   C   ARG   U   440   43.737   93.314   28.209   1.00   37.07   U       ATOM   1119   O   ARG   U   440   43.996   93.045   29.383   1.00   36.27   U       ATOM   1120   N   GLN   U   441   44.032   94.491   27.664   1.00   38.15   U       ATOM   1121   CA   GLN   U   441   44.685   95.551   28.440   1.00   37.13   U       ATOM   1122   CB   GLN   U   441   45.169   96.684   27.541   1.00   41.00   U       ATOM   1123   CG   GLN   U   441   46.452   96.417   26.807   1.00   36.46   U       ATOM   1124   CD   GLN   U   441   47.543   96.001   27.729   1.00   38.92   U       ATOM   1125   OE1   GLN   U   441   47.541   96.353   28.918   1.00   36.95   U       ATOM   1126   NE2   GLN   U   441   48.505   95.252   27.196   1.00   37.41   U       ATOM   1127   C   GLN   U   441   43.790   96.183   29.476   1.00   35.04   U       ATOM   1128   O   GLN   U   441   44.202   96.334   30.614   1.00   36.54   U       ATOM   1129   N   THR   U   442   42.580   96.569   29.060   1.00   32.77   U       ATOM   1130   CA   THR   U   442   41.606   97.232   29.929   1.00   33.05   U       ATOM   1131   CB   THR   U   442   40.476   97.923   29.102   1.00   35.63   U       ATOM   1132   OG1   THR   U   442   41.051   98.748   28.084   1.00   37.35   U       ATOM   1133   CG2   THR   U   442   39.603   98.811   30.001   1.00   28.11   U       ATOM   1134   C   THR   U   442   40.947   96.338   30.972   1.00   32.93   U       ATOM   1135   O   THR   U   442   40.877   96.715   32.136   1.00   33.34   U       ATOM   1136   N   TYR   U   443   40.454   95.173   30.559   1.00   31.00   U       ATOM   1137   CA   TYR   U   443   39.788   94.234   31.475   1.00   32.69   U       ATOM   1138   CB   TYR   U   443   38.331   94.011   31.067   1.00   26.91   U       ATOM   1139   CG   TYR   U   443   37.568   95.283   30.832   1.00   31.76   U       ATOM   1140   CD1   TYR   U   443   37.137   96.074   31.908   1.00   23.68   U       ATOM   1141   CE1   TYR   U   443   36.466   97.271   31.689   1.00   27.05   U       ATOM   1142   CD2   TYR   U   443   37.306   95.726   29.522   1.00   30.21   U       ATOM   1143   CE2   TYR   U   443   36.640   96.925   29.291   1.00   28.42   U       ATOM   1144   CZ   TYR   U   443   36.221   97.692   30.379   1.00   34.16   U       ATOM   1145   OH   TYR   U   443   35.542   98.863   30.143   1.00   37.08   U       ATOM   1146   C   TYR   U   443   40.533   92.916   31.405   1.00   36.13   U       ATOM   1147   O   TYR   U   443   40.115   91.969   30.731   1.00   35.11   U       ATOM   1148   N   PRO   U   444   41.661   92.840   32.107   1.00   41.53   U       ATOM   1149   CD   PRO   U   444   42.276   93.918   32.892   1.00   37.80   U       ATOM   1150   CA   PRO   U   444   42.501   91.643   32.132   1.00   40.98   U       ATOM   1151   CB   PRO   U   444   43.748   92.120   32.855   1.00   29.62   U       ATOM   1152   CG   PRO   U   444   43.715   93.610   32.698   1.00   37.30   U       ATOM   1153   C   PRO   U   444   41.872   90.442   32.829   1.00   44.98   U       ATOM   1154   O   PRO   U   444   42.137   89.302   32.461   1.00   41.03   U       ATOM   1155   N   ASP   U   445   41.037   90.695   33.831   1.00   50.06   U       ATOM   1156   CA   ASP   U   445   40.432   89.600   34.570   1.00   52.26   U       ATOM   1157   CB   ASP   U   445   40.207   90.007   36.036   1.00   57.60   U       ATOM   1158   CG   ASP   U   445   41.510   90.407   36.744   1.00   69.88   U       ATOM   1159   OD1   ASP   U   445   42.602   89.947   36.326   1.00   72.62   U       ATOM   1160   OD2   ASP   U   445   41.441   91.177   37.731   1.00   79.62   U       ATOM   1161   C   ASP   U   445   39.145   89.094   33.942   1.00   51.13   U       ATOM   1162   O   ASP   U   445   38.335   88.447   34.598   1.00   55.43   U       ATOM   1163   N   GLN   U   446   38.956   89.377   32.663   1.00   43.93   U       ATOM   1164   CA   GLN   U   446   37.769   88.914   31.974   1.00   40.93   U       ATOM   1165   CB   GLN   U   446   36.891   90.091   31.610   1.00   36.72   U       ATOM   1166   CG   GLN   U   446   36.322   90.767   32.812   1.00   28.56   U       ATOM   1167   CD   GLN   U   446   35.470   91.937   32.460   1.00   32.74   U       ATOM   1168   OE1   GLN   U   446   34.587   91.855   31.595   1.00   38.58   U       ATOM   1169   NE2   GLN   U   446   35.709   93.044   33.135   1.00   29.24   U       ATOM   1170   C   GLN   U   446   38.199   88.199   30.724   1.00   44.06   U       ATOM   1171   O   GLN   U   446   38.212   88.798   29.648   1.00   49.92   U       ATOM   1172   N   SER   U   447   38.533   86.918   30.858   1.00   44.27   U       ATOM   1173   CA   SER   U   447   39.019   86.137   29.724   1.00   49.37   U       ATOM   1174   CB   SER   U   447   39.460   84.743   30.173   1.00   50.92   U       ATOM   1175   OG   SER   U   447   38.340   83.931   30.471   1.00   56.10   U       ATOM   1176   C   SER   U   447   38.043   85.983   28.571   1.00   49.09   U       ATOM   1177   O   SER   U   447   38.468   85.757   27.432   1.00   54.13   U       ATOM   1178   N   GLY   U   448   36.749   86.111   28.845   1.00   41.71   U       ATOM   1179   CA   GLY   U   448   35.791   85.935   27.774   1.00   40.85   U       ATOM   1180   C   GLY   U   448   35.196   87.190   27.186   1.00   38.14   U       ATOM   1181   O   GLY   U   448   34.415   87.123   26.239   1.00   40.33   U       ATOM   1182   N   ARG   U   449   35.562   88.340   27.730   1.00   34.32   U       ATOM   1183   CA   ARG   U   449   35.002   89.582   27.249   1.00   31.28   U       ATOM   1184   CB   ARG   U   449   35.658   90.760   27.959   1.00   31.25   U       ATOM   1185   CG   ARG   U   449   35.204   92.103   27.409   1.00   30.81   U       ATOM   1186   CD   ARG   U   449   35.491   93.203   28.385   1.00   28.49   U       ATOM   1187   NE   ARG   U   449   34.317   93.406   29.207   1.00   25.55   U       ATOM   1188   CZ   ARG   U   449   33.560   94.491   29.155   1.00   35.25   U       ATOM   1189   NH1   ARG   U   449   33.861   95.481   28.326   1.00   29.71   U       ATOM   1190   NH2   ARG   U   449   32.483   94.569   29.910   1.00   35.38   U       ATOM   1191   C   ARG   U   449   35.053   89.771   25.734   1.00   32.37   U       ATOM   1192   O   ARG   U   449   34.026   90.069   25.115   1.00   24.02   U       ATOM   1193   N   PHE   U   450   36.226   89.590   25.130   1.00   32.68   U       ATOM   1194   CA   PHE   U   450   36.344   89.770   23.685   1.00   33.86   U       ATOM   1195   CB   PHE   U   450   37.740   89.346   23.208   1.00   32.48   U       ATOM   1196   CG   PHE   U   450   37.964   89.516   21.724   1.00   27.55   U       ATOM   1197   CD1   PHE   U   450   38.552   88.505   20.986   1.00   18.94   U       ATOM   1198   CD2   PHE   U   450   37.604   90.694   21.079   1.00   32.79   U       ATOM   1199   CE1   PHE   U   450   38.783   88.656   19.635   1.00   26.39   U       ATOM   1200   CE2   PHE   U   450   37.829   90.862   19.720   1.00   31.98   U       ATOM   1201   CZ   PHE   U   450   38.420   89.844   18.996   1.00   28.81   U       ATOM   1202   C   PHE   U   450   35.255   88.994   22.926   1.00   35.97   U       ATOM   1203   O   PHE   U   450   34.476   89.576   22.141   1.00   29.59   U       ATOM   1204   N   ALA   U   451   35.193   87.685   23.147   1.00   34.16   U       ATOM   1205   CA   ALA   U   451   34.165   86.919   22.465   1.00   40.68   U       ATOM   1206   CB   ALA   U   451   34.369   85.403   22.679   1.00   37.32   U       ATOM   1207   C   ALA   U   451   32.763   87.358   22.937   1.00   37.16   U       ATOM   1208   O   ALA   U   451   31.811   87.373   22.149   1.00   30.92   U       ATOM   1209   N   LYS   U   452   32.632   87.742   24.206   1.00   33.43   U       ATOM   1210   CA   LYS   U   452   31.328   88.149   24.694   1.00   35.13   U       ATOM   1211   CB   LYS   U   452   31.388   88.491   26.194   1.00   33.79   U       ATOM   1212   CG   LYS   U   452   30.100   89.149   26.709   1.00   30.21   U       ATOM   1213   CD   LYS   U   452   29.938   89.171   28.205   1.00   25.99   U       ATOM   1214   CE   LYS   U   452   29.242   87.904   28.704   1.00   33.85   U       ATOM   1215   NZ   LYS   U   452   30.147   86.688   28.723   1.00   45.04   U       ATOM   1216   C   LYS   U   452   30.796   89.325   23.870   1.00   38.79   U       ATOM   1217   O   LYS   U   452   29.623   89.323   23.450   1.00   41.46   U       ATOM   1218   N   LEU   U   453   31.669   90.307   23.632   1.00   36.24   U       ATOM   1219   CA   LEU   U   453   31.346   91.504   22.853   1.00   35.60   U       ATOM   1220   CB   LEU   U   453   32.529   92.491   22.859   1.00   37.67   U       ATOM   1221   CG   LEU   U   453   32.925   93.408   24.017   1.00   37.01   U       ATOM   1222   CD1   LEU   U   453   34.319   93.957   23.772   1.00   26.98   U       ATOM   1223   CD2   LEU   U   453   31.929   94.536   24.126   1.00   28.37   U       ATOM   1224   C   LEU   U   453   31.089   91.120   21.399   1.00   36.84   U       ATOM   1225   O   LEU   U   453   30.185   91.625   20.754   1.00   39.36   U       ATOM   1226   N   LEU   U   454   31.923   90.236   20.875   1.00   30.51   U       ATOM   1227   CA   LEU   U   454   31.796   89.814   19.502   1.00   27.98   U       ATOM   1228   CB   LEU   U   454   32.978   88.931   19.162   1.00   19.45   U       ATOM   1229   CG   LEU   U   454   34.193   89.742   18.766   1.00   17.60   U       ATOM   1230   CD1   LEU   U   454   35.314   88.828   18.323   1.00   10.12   U       ATOM   1231   CD2   LEU   U   454   33.776   90.682   17.625   1.00   16.90   U       ATOM   1232   C   LEU   U   454   30.491   89.081   19.225   1.00   36.94   U       ATOM   1233   O   LEU   U   454   29.952   89.135   18.103   1.00   40.85   U       ATOM   1234   N   LEU   U   455   29.976   88.400   20.249   1.00   33.97   U       ATOM   1235   CA   LEU   U   455   28.748   87.645   20.107   1.00   29.01   U       ATOM   1236   CB   LEU   U   455   28.768   86.451   21.045   1.00   20.81   U       ATOM   1237   CG   LEU   U   455   29.785   85.367   20.661   1.00   31.44   U       ATOM   1238   CD1   LEU   U   455   29.688   84.190   21.655   1.00   28.59   U       ATOM   1239   CD2   LEU   U   455   29.546   84.885   19.212   1.00   24.17   U       ATOM   1240   C   LEU   U   455   27.434   88.418   20.241   1.00   34.24   U       ATOM   1241   O   LEU   U   455   26.362   87.828   20.338   1.00   40.87   U       ATOM   1242   N   ARG   U   456   27.494   89.739   20.246   1.00   34.86   U       ATOM   1243   CA   ARG   U   456   26.258   90.507   20.261   1.00   30.18   U       ATOM   1244   CB   ARG   U   456   26.347   91.717   21.177   1.00   19.46   U       ATOM   1245   CG   ARG   U   456   26.244   91.353   22.611   1.00   26.45   U       ATOM   1246   CD   ARG   U   456   24.835   91.561   23.174   1.00   36.76   U       ATOM   1247   NE   ARG   U   456   23.845   90.491   22.947   1.00   37.17   U       ATOM   1248   CZ   ARG   U   456   24.110   89.187   22.931   1.00   35.22   U       ATOM   1249   NH1   ARG   U   456   25.366   88.747   23.109   1.00   31.08   U       ATOM   1250   NH2   ARG   U   456   23.098   88.328   22.788   1.00   26.55   U       ATOM   1251   C   ARG   U   456   26.073   90.957   18.824   1.00   28.29   U       ATOM   1252   O   ARG   U   456   25.095   91.612   18.482   1.00   28.43   U       ATOM   1253   N   LEU   U   457   27.023   90.577   17.976   1.00   29.12   U       ATOM   1254   CA   LEU   U   457   26.969   90.955   16.574   1.00   35.79   U       ATOM   1255   CB   LEU   U   457   28.343   90.751   15.924   1.00   32.44   U       ATOM   1256   CG   LEU   U   457   29.240   91.945   16.283   1.00   29.42   U       ATOM   1257   CD1   LEU   U   457   30.596   91.843   15.600   1.00   20.16   U       ATOM   1258   CD2   LEU   U   457   28.507   93.239   15.902   1.00   7.52   U       ATOM   1259   C   LEU   U   457   25.864   90.210   15.846   1.00   35.57   U       ATOM   1260   O   LEU   U   457   25.176   90.781   14.994   1.00   37.45   U       ATOM   1261   N   PRO   U   458   25.697   88.917   16.154   1.00   39.69   U       ATOM   1262   CD   PRO   U   458   26.651   88.043   16.861   1.00   42.46   U       ATOM   1263   CA   PRO   U   458   24.639   88.129   15.520   1.00   40.64   U       ATOM   1264   CB   PRO   U   458   24.874   86.732   16.072   1.00   39.74   U       ATOM   1265   CG   PRO   U   458   26.341   86.690   16.281   1.00   39.34   U       ATOM   1266   C   PRO   U   458   23.328   88.732   16.043   1.00   39.56   U       ATOM   1267   O   PRO   U   458   22.474   89.151   15.285   1.00   37.25   U       ATOM   1268   N   ALA   U   459   23.194   88.803   17.360   1.00   42.78   U       ATOM   1269   CA   ALA   U   459   21.995   89.371   17.966   1.00   45.25   U       ATOM   1270   CB   ALA   U   459   22.237   89.654   19.453   1.00   50.98   U       ATOM   1271   C   ALA   U   459   21.536   90.644   17.272   1.00   42.47   U       ATOM   1272   O   ALA   U   459   20.336   90.835   17.045   1.00   45.28   U       ATOM   1273   N   LEU   U   460   22.504   91.505   16.964   1.00   36.60   U       ATOM   1274   CA   LEU   U   460   22.288   92.793   16.304   1.00   33.20   U       ATOM   1275   CB   LEU   U   460   23.596   93.582   16.274   1.00   27.00   U       ATOM   1276   CG   LEU   U   460   23.699   94.850   15.426   1.00   22.57   U       ATOM   1277   CD1   LEU   U   460   22.852   95.941   15.999   1.00   16.07   U       ATOM   1278   CD2   LEU   U   460   25.142   95.282   15.383   1.00   15.66   U       ATOM   1279   C   LEU   U   460   21.827   92.574   14.885   1.00   32.62   U       ATOM   1280   O   LEU   U   460   21.011   93.318   14.352   1.00   36.27   U       ATOM   1281   N   ARG   U   461   22.388   91.549   14.265   1.00   30.57   U       ATOM   1282   CA   ARG   U   461   22.033   91.214   12.907   1.00   28.42   U       ATOM   1283   CB   ARG   U   461   22.848   90.023   12.421   1.00   23.68   U       ATOM   1284   CG   ARG   U   461   22.351   89.510   11.121   1.00   21.90   U       ATOM   1285   CD   ARG   U   461   22.355   90.634   10.094   1.00   21.59   U       ATOM   1286   NE   ARG   U   461   23.722   90.984   9.723   1.00   25.86   U       ATOM   1287   CZ   ARG   U   461   24.559   90.155   9.108   1.00   24.69   U       ATOM   1288   NH1   ARG   U   461   24.173   88.932   8.775   1.00   31.52   U       ATOM   1289   NH2   ARG   U   461   25.796   90.525   8.867   1.00   13.72   U       ATOM   1290   C   ARG   U   461   20.560   90.872   12.882   1.00   28.82   U       ATOM   1291   O   ARG   U   461   19.788   91.477   12.151   1.00   34.06   U       ATOM   1292   N   SER   U   462   20.170   89.904   13.701   1.00   23.31   U       ATOM   1293   CA   SER   U   462   18.785   89.476   13.778   1.00   20.62   U       ATOM   1294   CB   SER   U   462   18.634   88.487   14.916   1.00   10.85   U       ATOM   1295   OG   SER   U   462   19.088   87.222   14.478   1.00   24.21   U       ATOM   1296   C   SER   U   462   17.789   90.626   13.932   1.00   25.13   U       ATOM   1297   O   SER   U   462   16.749   90.651   13.258   1.00   27.26   U       ATOM   1298   N   ILE   U   463   18.101   91.570   14.819   1.00   25.00   U       ATOM   1299   CA   ILE   U   463   17.235   92.719   15.035   1.00   22.59   U       ATOM   1300   CB   ILE   U   463   17.723   93.606   16.213   1.00   21.95   U       ATOM   1301   CG2   ILE   U   463   16.767   94.803   16.417   1.00   9.54   U       ATOM   1302   CG1   ILE   U   463   17.754   92.784   17.495   1.00   29.80   U       ATOM   1303   CD1   ILE   U   463   18.007   93.613   18.746   1.00   36.94   U       ATOM   1304   C   ILE   U   463   17.242   93.543   13.757   1.00   23.31   U       ATOM   1305   O   ILE   U   463   16.273   94.209   13.414   1.00   23.92   U       ATOM   1306   N   GLY   U   464   18.352   93.503   13.044   1.00   24.89   U       ATOM   1307   CA   GLY   U   464   18.426   94.260   11.809   1.00   33.03   U       ATOM   1308   C   GLY   U   464   17.482   93.699   10.764   1.00   31.59   U       ATOM   1309   O   GLY   U   464   16.797   94.458   10.077   1.00   31.92   U       ATOM   1310   N   LEU   U   465   17.437   92.370   10.648   1.00   30.09   U       ATOM   1311   CA   LEU   U   465   16.574   91.721   9.665   1.00   29.21   U       ATOM   1312   CB   LEU   U   465   16.778   90.196   9.651   1.00   28.45   U       ATOM   1313   CG   LEU   U   465   18.025   89.446   9.155   1.00   32.34   U       ATOM   1314   CD1   LEU   U   465   18.509   89.967   7.832   1.00   16.72   U       ATOM   1315   CD2   LEU   U   465   19.099   89.569   10.168   1.00   36.94   U       ATOM   1316   C   LEU   U   465   15.096   92.018   9.899   1.00   31.95   U       ATOM   1317   O   LEU   U   465   14.296   91.852   8.999   1.00   33.33   U       ATOM   1318   N   LYS   U   466   14.722   92.449   11.100   1.00   33.32   U       ATOM   1319   CA   LYS   U   466   13.323   92.747   11.375   1.00   35.15   U       ATOM   1320   CB   LYS   U   466   13.063   92.648   12.877   1.00   33.26   U       ATOM   1321   CG   LYS   U   466   13.287   91.263   13.412   1.00   41.55   U       ATOM   1322   CD   LYS   U   466   12.814   91.084   14.855   1.00   53.25   U       ATOM   1323   CE   LYS   U   466   12.802   89.586   15.233   1.00   58.29   U       ATOM   1324   NZ   LYS   U   466   12.566   89.308   16.689   1.00   55.16   U       ATOM   1325   C   LYS   U   466   12.858   94.113   10.826   1.00   40.67   U       ATOM   1326   O   LYS   U   466   11.662   94.425   10.834   1.00   43.41   U       ATOM   1327   N   CYS   U   467   13.805   94.918   10.342   1.00   42.42   U       ATOM   1328   CA   CYS   U   467   13.501   96.232   9.780   1.00   45.65   U       ATOM   1329   CB   CYS   U   467   14.704   97.150   9.903   1.00   41.08   U       ATOM   1330   SG   CYS   U   467   15.338   97.319   11.533   1.00   44.12   U       ATOM   1331   C   CYS   U   467   13.198   96.093   8.301   1.00   51.69   U       ATOM   1332   O   CYS   U   467   14.115   95.838   7.515   1.00   54.82   U       ATOM   1333   N   LEU   U   468   11.942   96.277   7.905   1.00   52.02   U       ATOM   1334   CA   LEU   U   468   11.587   96.159   6.486   1.00   55.73   U       ATOM   1335   CB   LEU   U   468   10.107   95.800   6.334   1.00   56.80   U       ATOM   1336   CG   LEU   U   468   9.600   94.477   6.915   1.00   51.27   U       ATOM   1337   CD1   LEU   U   468   8.101   94.283   6.550   1.00   43.06   U       ATOM   1338   CD2   LEU   U   468   10.452   93.341   6.373   1.00   34.14   U       ATOM   1339   C   LEU   U   468   11.856   97.455   5.724   1.00   56.78   U       ATOM   1340   O   LEU   U   468   11.130   97.789   4.785   1.00   59.23   U       ATOM   1341   N   GLU   U   469   12.913   98.163   6.120   1.00   55.46   U       ATOM   1342   CA   GLU   U   469   13.264   99.455   5.528   1.00   51.29   U       ATOM   1343   CB   GLU   U   469   12.166   100.452   5.858   1.00   53.54   U       ATOM   1344   CG   GLU   U   469   11.871   100.484   7.366   1.00   50.33   U       ATOM   1345   CD   GLU   U   469   11.356   101.823   7.837   1.00   58.50   U       ATOM   1346   OE1   GLU   U   469   10.734   102.528   7.004   1.00   53.57   U       ATOM   1347   OE2   GLU   U   469   11.564   102.154   9.037   1.00   60.67   U       ATOM   1348   C   GLU   U   469   14.542   99.958   6.185   1.00   49.04   U       ATOM   1349   O   GLU   U   469   15.025   99.352   7.145   1.00   45.50   U       ATOM   1350   N   HIS   U   470   15.089   101.066   5.686   1.00   41.63   U       ATOM   1351   CA   HIS   U   470   16.276   101.617   6.317   1.00   35.57   U       ATOM   1352   CB   HIS   U   470   17.156   102.333   5.304   1.00   42.93   U       ATOM   1353   CG   HIS   U   470   17.949   101.411   4.433   1.00   50.13   U       ATOM   1354   CD2   HIS   U   470   19.285   101.191   4.348   1.00   54.17   U       ATOM   1355   ND1   HIS   U   470   17.366   100.565   3.520   1.00   54.29   U       ATOM   1356   CE1   HIS   U   470   18.306   99.861   2.909   1.00   53.53   U       ATOM   1357   NE2   HIS   U   470   19.478   100.225   3.395   1.00   46.80   U       ATOM   1358   C   HIS   U   470   15.778   102.598   7.368   1.00   35.43   U       ATOM   1359   O   HIS   U   470   15.225   103.642   7.034   1.00   33.29   U       ATOM   1360   N   LEU   U   471   15.953   102.257   8.640   1.00   30.44   U       ATOM   1361   CA   LEU   U   471   15.483   103.105   9.731   1.00   33.39   U       ATOM   1362   CB   LEU   U   471   16.213   102.720   11.025   1.00   35.77   U       ATOM   1363   CG   LEU   U   471   15.997   101.303   11.567   1.00   33.74   U       ATOM   1364   CD1   LEU   U   471   16.933   101.053   12.723   1.00   32.19   U       ATOM   1365   CD2   LEU   U   471   14.558   101.135   11.994   1.00   29.88   U       ATOM   1366   C   LEU   U   471   15.577   104.634   9.502   1.00   31.56   U       ATOM   1367   O   LEU   U   471   16.566   105.134   8.992   1.00   32.92   U       ATOM   1368   N   PHE   U   472   14.518   105.343   9.903   1.00   31.99   U       ATOM   1369   CA   PHE   U   472   14.348   106.803   9.819   1.00   29.89   U       ATOM   1370   CB   PHE   U   472   15.328   107.516   10.754   1.00   29.21   U       ATOM   1371   CG   PHE   U   472   15.469   106.869   12.084   1.00   27.18   U       ATOM   1372   CD1   PHE   U   472   16.681   106.337   12.478   1.00   32.98   U       ATOM   1373   CD2   PHE   U   472   14.390   106.751   12.932   1.00   33.76   U       ATOM   1374   CE1   PHE   U   472   16.811   105.690   13.683   1.00   29.18   U       ATOM   1375   CE2   PHE   U   472   14.516   106.091   14.161   1.00   30.06   U       ATOM   1376   CZ   PHE   U   472   15.725   105.568   14.527   1.00   36.30   U       ATOM   1377   C   PHE   U   472   14.441   107.442   8.430   1.00   33.97   U       ATOM   1378   O   PHE   U   472   14.275   108.661   8.290   1.00   31.69   U       ATOM   1379   N   PHE   U   473   14.676   106.634   7.401   1.00   32.14   U       ATOM   1380   CA   PHE   U   473   14.808   107.182   6.059   1.00   33.71   U       ATOM   1381   CB   PHE   U   473   15.157   106.097   5.049   1.00   17.58   U       ATOM   1382   CG   PHE   U   473   15.498   106.647   3.705   1.00   31.82   U       ATOM   1383   CD1   PHE   U   473   16.670   107.393   3.522   1.00   30.74   U       ATOM   1384   CD2   PHE   U   473   14.640   106.459   2.616   1.00   36.15   U       ATOM   1385   CE1   PHE   U   473   16.983   107.940   2.275   1.00   34.57   U       ATOM   1386   CE2   PHE   U   473   14.940   107.000   1.361   1.00   32.37   U       ATOM   1387   CZ   PHE   U   473   16.118   107.742   1.192   1.00   33.69   U       ATOM   1388   C   PHE   U   473   13.626   107.983   5.510   1.00   33.99   U       ATOM   1389   O   PHE   U   473   13.816   109.005   4.868   1.00   39.78   U       ATOM   1390   N   PHE   U   474   12.404   107.545   5.734   1.00   36.94   U       ATOM   1391   CA   PHE   U   474   11.314   108.313   5.172   1.00   43.73   U       ATOM   1392   CB   PHE   U   474   10.131   107.387   4.853   1.00   39.72   U       ATOM   1393   CG   PHE   U   474   10.459   106.315   3.836   1.00   34.24   U       ATOM   1394   CD1   PHE   U   474   10.470   104.966   4.195   1.00   36.54   U       ATOM   1395   CD2   PHE   U   474   10.758   106.653   2.523   1.00   28.23   U       ATOM   1396   CE1   PHE   U   474   10.768   103.973   3.267   1.00   32.02   U       ATOM   1397   CE2   PHE   U   474   11.057   105.672   1.585   1.00   29.66   U       ATOM   1398   CZ   PHE   U   474   11.062   104.326   1.961   1.00   36.99   U       ATOM   1399   C   PHE   U   474   10.907   109.506   6.044   1.00   45.36   U       ATOM   1400   O   PHE   U   474   9.974   110.240   5.712   1.00   47.56   U       ATOM   1401   N   LYS   U   475   11.616   109.699   7.153   1.00   47.58   U       ATOM   1402   CA   LYS   U   475   11.347   110.832   8.036   1.00   49.62   U       ATOM   1403   CB   LYS   U   475   11.546   110.475   9.512   1.00   38.43   U       ATOM   1404   CG   LYS   U   475   10.376   109.777   10.134   1.00   37.81   U       ATOM   1405   CD   LYS   U   475   10.394   109.905   11.648   1.00   34.22   U       ATOM   1406   CE   LYS   U   415   9.368   108.993   12.279   1.00   24.58   U       ATOM   1407   NZ   LYS   U   475   9.543   107.623   11.704   1.00   31.52   U       ATOM   1408   C   LYS   U   475   12.334   111.922   7.668   1.00   53.12   U       ATOM   1409   O   LYS   U   475   12.257   113.050   8.176   1.00   50.05   U       ATOM   1410   N   LEU   U   476   13.271   111.565   6.788   1.00   54.37   U       ATOM   1411   CA   LEU   U   476   14.298   112.498   6.349   1.00   55.80   U       ATOM   1412   CB   LEU   U   476   15.409   111.780   5.586   1.00   46.03   U       ATOM   1413   CG   LEU   U   476   16.380   110.968   6.448   1.00   51.17   U       ATOM   1414   CD1   LEU   U   476   17.554   110.476   5.596   1.00   51.60   U       ATOM   1415   CD2   LEU   U   476   16.879   111.828   7.603   1.00   48.81   U       ATOM   1416   C   LEU   U   476   13.680   113.563   5.482   1.00   61.13   U       ATOM   1417   O   LEU   U   476   12.765   113.289   4.704   1.00   61.06   U       ATOM   1418   N   VAL   U   477   14.188   114.781   5.628   1.00   69.05   U       ATOM   1419   CA   VAL   U   477   13.677   115.924   4.889   1.00   75.86   U       ATOM   1420   CB   VAL   U   477   14.451   117.218   5.297   1.00   75.38   U       ATOM   1421   CG1   VAL   U   477   15.932   116.920   5.452   1.00   71.51   U       ATOM   1422   CG2   VAL   U   477   14.219   118.317   4.278   1.00   74.25   U       ATOM   1423   C   VAL   U   477   13.692   115.722   3.376   1.00   78.42   U       ATOM   1424   O   VAL   U   477   12.658   115.853   2.723   1.00   80.89   U       ATOM   1425   N   GLY   U   478   14.847   115.384   2.819   1.00   77.79   U       ATOM   1426   CA   GLY   U   478   14.920   115.183   1.383   1.00   82.22   U       ATOM   1427   C   GLY   U   478   14.152   113.968   0.900   1.00   84.69   U       ATOM   1428   O   GLY   U   478   13.911   113.030   1.673   1.00   85.31   U       ATOM   1429   N   ASN   U   479   13.773   113.977   −0.380   1.00   83.70   U       ATOM   1430   CA   ASN   U   479   13.031   112.863   −0.975   1.00   83.67   U       ATOM   1431   CB   ASN   U   479   11.621   113.323   −1.353   1.00   85.15   U       ATOM   1432   CG   ASN   U   479   10.543   112.379   −0.846   1.00   90.54   U       ATOM   1433   OD1   ASN   U   479   9.355   112.695   −0.914   1.00   97.66   U       ATOM   1434   ND2   ASN   U   479   10.951   111.210   −0.340   1.00   87.84   U       ATOM   1435   C   ASN   U   479   13.753   112.285   −2.202   1.00   79.08   U       ATOM   1436   O   ASN   U   479   13.276   112.379   −3.335   1.00   78.53   U       ATOM   1437   N   THR   U   480   14.907   111.676   −1.954   1.00   73.32   U       ATOM   1438   CA   THR   U   480   15.722   111.093   −3.011   1.00   68.11   U       ATOM   1439   CB   THR   U   480   17.147   111.650   −2.957   1.00   68.33   U       ATOM   1440   OG1   THR   U   480   17.732   111.290   −1.705   1.00   77.35   U       ATOM   1441   CG2   THR   U   480   17.144   113.162   −3.054   1.00   62.29   U       ATOM   1442   C   THR   U   480   15.789   109.582   −2.816   1.00   63.60   U       ATOM   1443   O   THR   U   480   14.882   108.995   −2.225   1.00   64.45   U       ATOM   1444   N   SER   U   481   16.856   108.960   −3.316   1.00   54.01   U       ATOM   1445   CA   SER   U   481   17.030   107.521   −3.172   1.00   58.62   U       ATOM   1446   CB   SER   U   481   17.533   106.898   −4.467   1.00   62.02   U       ATOM   1447   OG   SER   U   481   18.908   107.173   −4.665   1.00   59.14   U       ATOM   1448   C   SER   U   481   18.092   107.351   −2.105   1.00   61.40   U       ATOM   1449   O   SER   U   481   18.921   108.234   −1.949   1.00   60.96   U       ATOM   1450   N   ILE   U   482   18.081   106.230   −1.382   1.00   62.19   U       ATOM   1451   CA   ILE   U   482   19.061   106.012   −0.324   1.00   59.95   U       ATOM   1452   CB   ILE   U   482   19.132   104.525   0.152   1.00   63.75   U       ATOM   1453   CG2   ILE   U   482   19.994   104.415   1.428   1.00   56.37   U       ATOM   1454   CG1   ILE   U   482   17.737   103.992   0.472   1.00   66.43   U       ATOM   1455   CD1   ILE   U   482   17.207   104.421   1.805   1.00   68.96   U       ATOM   1456   C   ILE   U   482   20.436   106.392   −0.852   1.00   63.08   U       ATOM   1457   O   ILE   U   482   21.151   107.172   −0.216   1.00   66.14   U       ATOM   1458   N   ASP   U   483   20.790   105.864   −2.027   1.00   61.42   U       ATOM   1459   CA   ASP   U   483   22.109   106.112   −2.628   1.00   55.14   U       ATOM   1460   CB   ASP   U   483   22.286   105.279   −3.895   1.00   46.69   U       ATOM   1461   CG   ASP   U   483   21.833   103.868   −3.701   1.00   54.41   U       ATOM   1462   OD1   ASP   U   483   22.701   102.974   −3.646   1.00   44.31   U       ATOM   1463   OD2   ASP   U   483   20.594   103.669   −3.575   1.00   59.52   U       ATOM   1464   C   ASP   U   483   22.387   107.564   −2.934   1.00   51.45   U       ATOM   1465   O   ASP   U   483   23.481   108.051   −2.687   1.00   53.59   U       ATOM   1466   N   SER   U   484   21.410   108.269   −3.476   1.00   48.55   U       ATOM   1467   CA   SER   U   484   21.636   109.665   −3.767   1.00   50.31   U       ATOM   1468   CB   SER   U   484   20.457   110.233   −4.519   1.00   50.14   U       ATOM   1469   OG   SER   U   484   20.387   111.624   −4.289   1.00   63.43   U       ATOM   1470   C   SER   U   484   21.857   110.463   −2.476   1.00   52.59   U       ATOM   1471   O   SER   U   484   22.683   111.387   −2.432   1.00   53.49   U       ATOM   1472   N   PHE   U   485   21.109   110.099   −1.434   1.00   50.76   U       ATOM   1473   CA   PHE   U   485   21.199   110.746   −0.124   1.00   48.74   U       ATOM   1474   CB   PHE   U   485   20.119   110.208   0.821   1.00   42.60   U       ATOM   1475   CG   PHE   U   485   20.400   110.483   2.274   1.00   50.41   U       ATOM   1476   CD1   PHE   U   485   20.501   111.790   2.746   1.00   47.90   U       ATOM   1477   CD2   PHE   U   485   20.623   109.437   3.163   1.00   52.06   U       ATOM   1478   CE1   PHE   U   485   20.821   112.053   4.068   1.00   37.72   U       ATOM   1479   CE2   PHE   U   485   20.947   109.694   4.499   1.00   49.14   U       ATOM   1480   CZ   PHE   U   485   21.047   111.007   4.947   1.00   48.32   U       ATOM   1481   C   PHE   U   485   22.569   110.497   0.498   1.00   51.52   U       ATOM   1482   O   PHE   U   485   23.220   111.417   0.995   1.00   51.80   U       ATOM   1483   N   LEU   U   486   22.986   109.235   0.486   1.00   48.33   U       ATOM   1484   CA   LEU   U   486   24.275   108.838   1.030   1.00   42.40   U       ATOM   1485   CB   LEU   U   486   24.452   107.328   0.894   1.00   35.79   U       ATOM   1486   CG   LEU   U   486   23.728   106.462   1.915   1.00   33.49   U       ATOM   1487   CD1   LEU   U   486   23.949   105.002   1.579   1.00   26.67   U       ATOM   1488   CD2   LEU   U   486   24.243   106.790   3.305   1.00   22.57   U       ATOM   1489   C   LEU   U   486   25.409   109.529   0.298   1.00   46.74   U       ATOM   1490   O   LEU   U   486   26.260   110.184   0.888   1.00   46.00   U       ATOM   1491   N   LEU   U   487   25.417   109.362   −1.010   1.00   52.71   U       ATOM   1492   CA   LEU   U   487   26.447   109.946   −1.844   1.00   51.57   U       ATOM   1493   CB   LEU   U   487   26.095   109.686   −3.299   1.00   51.34   U       ATOM   1494   CG   LEU   U   487   26.974   110.286   −4.374   1.00   50.14   U       ATOM   1495   CD1   LEU   U   487   28.435   110.205   −4.001   1.00   49.39   U       ATOM   1496   CD2   LEU   U   487   26.676   109.529   −5.652   1.00   53.61   U       ATOM   1497   C   LEU   U   487   26.641   111.438   −1.589   1.00   48.88   U       ATOM   1498   O   LEU   U   487   27.750   111.892   −1.338   1.00   48.29   U       ATOM   1499   N   SER   U   488   25.561   112.201   −1.626   1.00   49.63   U       ATOM   1500   CA   SER   U   488   25.674   113.637   −1.408   1.00   52.15   U       ATOM   1501   CB   SER   U   488   24.370   114.327   −1.829   1.00   48.26   U       ATOM   1502   OG   SER   U   488   23.425   114.316   −0.786   1.00   45.39   U       ATOM   1503   C   SER   U   488   26.022   113.996   0.042   1.00   52.35   U       ATOM   1504   O   SER   U   488   26.669   115.007   0.323   1.00   54.71   U       ATOM   1505   N   MET   U   489   25.585   113.165   0.968   1.00   52.82   U       ATOM   1506   CA   MET   U   489   25.857   113.414   2.364   1.00   51.60   U       ATOM   1507   CB   MET   U   489   24.988   112.506   3.214   1.00   46.06   U       ATOM   1508   CG   MET   U   489   24.962   112.877   4.656   1.00   53.48   U       ATOM   1509   SD   MET   U   489   23.612   113.978   5.008   1.00   57.03   U       ATOM   1510   CE   MET   U   489   23.857   115.229   3.663   1.00   59.12   U       ATOM   1511   C   MET   U   489   27.334   113.124   2.616   1.00   57.18   U       ATOM   1512   O   MET   U   489   27.960   113.744   3.480   1.00   59.72   U       ATOM   1513   N   LEU   U   490   27.888   112.186   1.847   1.00   56.23   U       ATOM   1514   CA   LEU   U   490   29.289   111.810   1.990   1.00   55.97   U       ATOM   1515   CB   LEU   U   490   29.612   110.548   1.181   1.00   42.91   U       ATOM   1516   CG   LEU   U   490   29.308   109.231   1.904   1.00   45.20   U       ATOM   1517   CD1   LEU   U   490   29.785   108.064   1.089   1.00   44.97   U       ATOM   1518   CD2   LEU   U   490   29.998   109.206   3.256   1.00   41.97   U       ATOM   1519   C   LEU   U   490   30.203   112.945   1.576   1.00   63.45   U       ATOM   1520   O   LEU   U   490   31.196   113.206   2.251   1.00   69.94   U       ATOM   1521   N   GLU   U   491   29.859   113.614   0.472   1.00   69.84   U       ATOM   1522   CA   GLU   U   491   30.619   114.751   −0.064   1.00   68.81   U       ATOM   1523   CB   GLU   U   491   30.415   114.811   −1.578   1.00   66.97   U       ATOM   1524   CG   GLU   U   491   30.716   113.482   −2.293   1.00   72.32   U       ATOM   1525   CD   GLU   U   491   30.162   113.407   −3.726   1.00   78.93   U       ATOM   1526   OE1   GLU   U   491   30.549   112.473   −4.474   1.00   73.54   U       ATOM   1527   OE2   GLU   U   491   29.334   114.273   −4.102   1.00   77.88   U       ATOM   1528   C   GLU   U   491   30.078   116.023   0.609   1.00   70.94   U       ATOM   1529   O   GLU   U   491   29.054   116.563   0.200   1.00   70.28   U       ATOM   1530   N   SER   U   492   30.754   116.493   1.653   1.00   74.07   U       ATOM   1531   CA   SER   U   492   30.277   117.668   2.376   1.00   79.39   U       ATOM   1532   CB   SER   U   492   29.068   117.266   3.216   1.00   72.71   U       ATOM   1533   OG   SER   U   492   28.556   118.371   3.927   1.00   78.28   U       ATOM   1534   C   SER   U   492   31.344   118.316   3.275   1.00   87.95   U       ATOM   1535   O   SER   U   492   32.444   117.726   3.408   1.00   93.73   U       ATOM   1536   OXT   SER   U   492   31.074   119.409   3.839   1.00   90.10   U       ATOM   1537   CB   PRO   E   179   49.063   79.237   25.302   1.00   63.97   E       ATOM   1538   CG   PRO   E   179   49.523   80.699   25.165   1.00   57.54   E       ATOM   1539   C   PRO   E   179   47.730   78.002   27.104   1.00   62.42   E       ATOM   1540   O   PRO   E   179   47.490   77.949   28.307   1.00   55.36   E       ATOM   1541   N   PRO   E   179   48.555   80.420   27.318   1.00   59.63   E       ATOM   1542   CD   PRO   E   179   49.650   81.155   26.643   1.00   64.55   E       ATOM   1543   CA   PRO   E   179   48.032   79.363   26.427   1.00   62.65   E       ATOM   1544   N   ILE   E   180   47.712   76.941   26.281   1.00   63.43   E       ATOM   1545   CA   ILE   E   180   47.477   75.504   26.600   1.00   60.71   E       ATOM   1546   CB   ILE   E   180   48.481   74.973   27.657   1.00   56.02   E       ATOM   1547   CG2   ILE   E   180   49.882   75.406   27.284   1.00   49.91   E       ATOM   1548   CG1   ILE   E   180   48.084   75.440   29.052   1.00   56.69   E       ATOM   1549   CD1   ILE   E   180   48.587   74.527   30.150   1.00   64.15   E       ATOM   1550   C   ILE   E   180   46.080   74.938   26.962   1.00   59.69   E       ATOM   1551   O   ILE   E   180   45.474   75.331   27.961   1.00   61.02   E       ATOM   1552   N   THR   E   181   45.605   73.986   26.146   1.00   53.78   E       ATOM   1553   CA   THR   E   181   44.295   73.329   26.312   1.00   48.33   E       ATOM   1554   CB   THR   E   181   43.927   72.425   25.050   1.00   44.47   E       ATOM   1555   OG1   THR   E   181   43.969   73.171   23.825   1.00   32.66   E       ATOM   1556   CG2   THR   E   181   42.536   71.818   25.215   1.00   43.04   E       ATOM   1557   C   THR   E   181   44.297   72.377   27.526   1.00   49.61   E       ATOM   1558   O   THR   E   181   45.224   71.592   27.667   1.00   54.75   E       ATOM   1559   N   PRO   E   182   43.278   72.436   28.417   1.00   52.24   E       ATOM   1560   CD   PRO   E   182   42.438   73.617   28.652   1.00   59.60   E       ATOM   1561   CA   PRO   E   182   43.213   71.536   29.586   1.00   51.59   E       ATOM   1562   CB   PRO   E   182   42.509   72.364   30.668   1.00   45.60   E       ATOM   1563   CG   PRO   E   182   42.477   73.733   30.159   1.00   53.53   E       ATOM   1564   C   PRO   E   182   42.367   70.303   29.265   1.00   55.33   E       ATOM   1565   O   PRO   E   182   42.700   69.492   28.398   1.00   54.95   E       ATOM   1566   N   GLU   E   183   41.242   70.208   29.983   1.00   64.63   E       ATOM   1567   CA   GLU   E   183   40.258   69.114   29.890   1.00   59.48   E       ATOM   1568   CB   GLU   E   183   39.918   68.677   31.303   1.00   63.94   E       ATOM   1569   CG   GLU   E   183   41.252   68.361   32.006   1.00   67.86   E       ATOM   1570   CD   GLU   E   183   42.391   68.176   30.967   1.00   61.39   E       ATOM   1571   OE1   GLU   E   183   42.141   67.503   29.928   1.00   56.70   E       ATOM   1572   OE2   GLU   E   183   43.501   68.717   31.171   1.00   48.71   E       ATOM   1573   C   GLU   E   183   39.062   69.539   29.083   1.00   56.09   E       ATOM   1574   O   GLU   E   183   37.914   69.212   29.332   1.00   44.53   E       ATOM   1575   N   GLN   E   184   39.428   70.318   28.087   1.00   58.78   E       ATOM   1576   CA   GLN   E   184   38.567   70.860   27.086   1.00   54.12   E       ATOM   1577   CB   GLN   E   184   39.066   72.249   26.756   1.00   48.24   E       ATOM   1578   CG   GLN   E   184   39.271   73.052   28.012   1.00   45.50   E       ATOM   1579   CD   GLN   E   184   39.414   74.527   27.747   1.00   50.65   E       ATOM   1580   OE1   GLN   E   184   40.503   74.995   27.406   1.00   40.87   E       ATOM   1581   NE2   GLN   E   184   38.302   75.282   27.898   1.00   49.00   E       ATOM   1582   C   GLN   E   184   38.949   69.870   26.015   1.00   55.11   E       ATOM   1583   O   GLN   E   184   38.202   69.589   25.094   1.00   59.90   E       ATOM   1584   N   GLU   E   185   40.151   69.335   26.177   1.00   53.21   E       ATOM   1585   CA   GLU   E   185   40.668   68.340   25.279   1.00   49.10   E       ATOM   1586   CB   GLU   E   185   42.028   67.858   25.755   1.00   51.38   E       ATOM   1587   CG   GLU   E   185   42.739   67.063   24.692   1.00   61.09   E       ATOM   1588   CD   GLU   E   185   42.925   67.889   23.431   1.00   62.65   E       ATOM   1589   OE1   GLU   E   185   43.446   69.018   23.577   1.00   58.60   E       ATOM   1590   OE2   GLU   E   185   42.560   67.424   22.318   1.00   60.26   E       ATOM   1591   C   GLU   E   185   39.692   67.173   25.272   1.00   46.01   E       ATOM   1592   O   GLU   E   185   39.426   66.590   24.222   1.00   44.96   E       ATOM   1593   N   GLU   E   186   39.159   66.826   26.443   1.00   42.99   E       ATOM   1594   CA   GLU   E   186   38.200   65.732   26.507   1.00   43.92   E       ATOM   1595   CB   GLU   E   186   37.841   65.329   27.927   1.00   50.55   E       ATOM   1596   CG   GLU   E   186   36.916   64.111   27.932   1.00   54.03   E       ATOM   1597   CD   GLU   E   186   36.276   63.838   29.276   1.00   55.18   E       ATOM   1598   OE1   GLU   E   186   36.992   63.857   30.301   1.00   55.83   E       ATOM   1599   OE2   GLU   E   186   35.051   63.588   29.304   1.00   56.58   E       ATOM   1600   C   GLU   E   186   36.929   66.198   25.863   1.00   44.75   E       ATOM   1601   O   GLU   E   186   36.283   65.443   25.131   1.00   46.38   E       ATOM   1602   N   LEU   E   187   36.552   67.439   26.171   1.00   41.28   E       ATOM   1603   CA   LEU   E   187   35.344   68.019   25.597   1.00   34.84   E       ATOM   1604   CB   LEU   E   187   35.166   69.442   26.107   1.00   27.70   E       ATOM   1605   CG   LEU   E   187   33.949   70.135   25.489   1.00   28.29   E       ATOM   1606   CD1   LEU   E   187   32.628   69.518   25.994   1.00   25.76   E       ATOM   1607   CD2   LEU   E   187   34.049   71.604   25.807   1.00   32.95   E       ATOM   1608   C   LEU   E   187   35.363   68.024   24.051   1.00   34.96   E       ATOM   1609   O   LEU   E   187   34.356   67.724   23.384   1.00   35.08   E       ATOM   1610   N   ILE   E   188   36.516   68.376   23.495   1.00   29.71   E       ATOM   1611   CA   ILE   E   188   36.687   68.432   22.060   1.00   30.00   E       ATOM   1612   CB   ILE   E   188   38.018   69.131   21.687   1.00   24.30   E       ATOM   1613   CG2   ILE   E   188   38.142   69.293   20.166   1.00   11.17   E       ATOM   1614   CG1   ILE   E   188   38.046   70.520   22.323   1.00   22.82   E       ATOM   1615   CD1   ILE   E   188   39.347   71.238   22.144   1.00   20.00   E       ATOM   1616   C   ILE   E   188   36.625   67.033   21.454   1.00   37.51   E       ATOM   1617   O   ILE   E   188   35.999   66.845   20.401   1.00   41.11   E       ATOM   1618   N   HIS   E   189   37.247   66.044   22.091   1.00   34.59   E       ATOM   1619   CA   HIS   E   189   37.173   64.709   21.509   1.00   42.58   E       ATOM   1620   CB   HIS   E   189   37.961   63.699   22.350   1.00   52.40   E       ATOM   1621   CG   HIS   E   189   39.441   63.862   22.236   1.00   66.69   E       ATOM   1622   CD2   HIS   E   189   40.188   64.667   21.441   1.00   69.80   E       ATOM   1623   ND1   HIS   E   189   40.331   63.155   23.015   1.00   71.12   E       ATOM   1624   CE1   HIS   E   189   41.565   63.522   22.706   1.00   76.28   E       ATOM   1625   NE2   HIS   E   189   41.506   64.437   21.755   1.00   69.65   E       ATOM   1626   C   HIS   E   189   35.705   64.284   21.384   1.00   41.69   E       ATOM   1627   O   HIS   E   189   35.271   63.746   20.354   1.00   43.43   E       ATOM   1628   N   ARG   E   190   34.942   64.559   22.432   1.00   34.44   E       ATOM   1629   CA   ARG   E   190   33.540   64.212   22.451   1.00   38.70   E       ATOM   1630   CB   ARG   E   190   32.924   64.607   23.792   1.00   38.89   E       ATOM   1631   CG   ARG   E   190   31.427   64.807   23.737   1.00   36.05   E       ATOM   1632   CD   ARG   E   190   30.892   65.121   25.095   1.00   40.10   E       ATOM   1633   NE   ARG   E   190   31.170   64.036   26.022   1.00   40.47   E       ATOM   1634   CZ   ARG   E   190   32.040   64.137   27.013   1.00   47.56   E       ATOM   1635   NH1   ARG   E   190   32.705   65.278   27.199   1.00   46.35   E       ATOM   1636   NH2   ARG   E   190   32.249   63.099   27.806   1.00   44.64   E       ATOM   1637   C   ARG   E   190   32.746   64.859   21.314   1.00   38.24   E       ATOM   1638   O   ARG   E   190   32.020   64.166   20.593   1.00   36.82   E       ATOM   1639   N   LEU   E   191   32.858   66.175   21.158   1.00   30.98   E       ATOM   1640   CA   LEU   E   191   32.103   66.814   20.105   1.00   34.04   E       ATOM   1641   CB   LEU   E   191   32.219   68.324   20.178   1.00   30.97   E       ATOM   1642   CG   LEU   E   191   31.843   69.007   21.477   1.00   32.34   E       ATOM   1643   CD1   LEU   E   191   32.052   70.484   21.254   1.00   32.17   E       ATOM   1644   CD2   LEU   E   191   30.417   68.719   21.879   1.00   22.30   E       ATOM   1645   C   LEU   E   191   32.583   66.353   18.752   1.00   37.58   E       ATOM   1646   O   LEU   E   191   31.777   66.091   17.866   1.00   41.61   E       ATOM   1647   N   VAL   E   192   33.894   66.247   18.577   1.00   35.14   E       ATOM   1648   CA   VAL   E   192   34.409   65.822   17.286   1.00   34.28   E       ATOM   1649   CB   VAL   E   192   35.950   65.935   17.233   1.00   30.40   E       ATOM   1650   CG1   VAL   E   192   36.466   65.458   15.902   1.00   18.28   E       ATOM   1651   CG2   VAL   E   192   36.349   67.376   17.397   1.00   27.26   E       ATOM   1652   C   VAL   E   192   33.945   64.406   16.967   1.00   34.14   E       ATOM   1653   O   VAL   E   192   33.745   64.065   15.798   1.00   32.27   E       ATOM   1654   N   TYR   E   193   33.743   63.606   18.015   1.00   34.68   E       ATOM   1655   CA   TYR   E   193   33.280   62.211   17.895   1.00   38.61   E       ATOM   1656   CB   TYR   E   193   33.429   61.502   19.253   1.00   41.45   E       ATOM   1657   CG   TYR   E   193   33.063   60.027   19.294   1.00   37.93   E       ATOM   1658   CD1   TYR   E   193   34.011   59.040   19.042   1.00   39.12   E       ATOM   1659   CE1   TYR   E   193   33.692   57.682   19.117   1.00   44.28   E       ATOM   1660   CD2   TYR   E   193   31.778   59.625   19.623   1.00   44.95   E       ATOM   1661   CE2   TYR   E   193   31.441   58.278   19.702   1.00   50.21   E       ATOM   1662   CZ   TYR   E   193   32.399   57.305   19.451   1.00   53.79   E       ATOM   1663   OH   TYR   E   193   32.045   55.967   19.540   1.00   61.14   E       ATOM   1664   C   TYR   E   193   31.816   62.175   17.454   1.00   37.90   E       ATOM   1665   O   TYR   E   193   31.477   61.575   16.444   1.00   40.94   E       ATOM   1666   N   PHE   E   194   30.958   62.829   18.230   1.00   40.65   E       ATOM   1667   CA   PHE   E   194   29.525   62.900   17.957   1.00   39.80   E       ATOM   1668   CB   PHE   E   194   28.819   63.590   19.115   1.00   38.32   E       ATOM   1669   CG   PHE   E   194   28.760   62.751   20.345   1.00   52.35   E       ATOM   1670   CD1   PHE   E   194   29.002   63.306   21.596   1.00   53.88   E       ATOM   1671   CD2   PHE   E   194   28.480   61.386   20.249   1.00   50.61   E       ATOM   1672   CE1   PHE   E   194   28.970   62.515   22.733   1.00   59.51   E       ATOM   1673   CE2   PHE   E   194   28.445   60.585   21.374   1.00   41.95   E       ATOM   1674   CZ   PHE   E   194   28.690   61.143   22.620   1.00   54.73   E       ATOM   1675   C   PHE   E   194   29.197   63.613   16.670   1.00   37.86   E       ATOM   1676   O   PHE   E   194   28.162   63.360   16.066   1.00   38.35   E       ATOM   1677   N   GLN   E   195   30.064   64.529   16.264   1.00   34.83   E       ATOM   1678   CA   GLN   E   195   29.854   65.244   15.017   1.00   38.45   E       ATOM   1679   CB   GLN   E   195   30.969   66.277   14.824   1.00   38.16   E       ATOM   1680   CG   GLN   E   195   31.237   66.701   13.391   1.00   32.13   E       ATOM   1681   CD   GLN   E   195   31.768   68.113   13.297   1.00   34.61   E       ATOM   1682   OE1   GLN   E   195   31.005   69.095   13.290   1.00   33.03   E       ATOM   1683   NE2   GLN   E   195   33.084   68.228   13.242   1.00   43.63   E       ATOM   1684   C   GLN   E   195   29.912   64.173   13.937   1.00   39.42   E       ATOM   1685   O   GLN   E   195   28.977   63.974   13.150   1.00   36.82   E       ATOM   1686   N   ASN   E   196   31.037   63.477   13.941   1.00   41.99   E       ATOM   1687   CA   ASN   E   196   31.318   62.403   13.023   1.00   41.31   E       ATOM   1688   CB   ASN   E   196   32.646   61.775   13.450   1.00   45.98   E       ATOM   1689   CG   ASN   E   196   32.971   60.506   12.706   1.00   55.28   E       ATOM   1690   OD1   ASN   E   196   32.127   59.621   12.541   1.00   59.91   E       ATOM   1691   ND2   ASN   E   196   34.217   60.393   12.273   1.00   62.85   E       ATOM   1692   C   ASN   E   196   30.161   61.399   13.095   1.00   40.61   E       ATOM   1693   O   ASN   E   196   29.547   61.069   12.082   1.00   43.29   E       ATOM   1694   N   GLU   E   197   29.843   60.934   14.296   1.00   33.92   E       ATOM   1695   CA   GLU   E   197   28.774   59.963   14.451   1.00   35.85   E       ATOM   1696   CB   GLU   E   197   28.578   59.602   15.907   1.00   35.07   E       ATOM   1697   CG   GLU   E   197   27.342   58.754   16.113   1.00   39.99   E       ATOM   1698   CD   GLU   E   197   27.250   58.206   17.519   1.00   50.67   E       ATOM   1699   OE1   GLU   E   197   28.078   58.612   18.363   1.00   63.46   E       ATOM   1700   OE2   GLU   E   197   26.348   57.382   17.787   1.00   46.48   E       ATOM   1701   C   GLU   E   197   27.421   60.346   13.870   1.00   39.95   E       ATOM   1702   O   GLU   E   197   26.810   59.548   13.167   1.00   45.46   E       ATOM   1703   N   TYR   E   198   26.940   61.551   14.156   1.00   40.87   E       ATOM   1704   CA   TYR   E   198   25.643   61.971   13.628   1.00   41.62   E       ATOM   1705   CB   TYR   E   198   24.890   62.790   14.673   1.00   44.79   E       ATOM   1706   CG   TYR   E   198   24.575   62.013   15.919   1.00   43.32   E       ATOM   1707   CD1   TYR   E   198   25.219   62.305   17.123   1.00   46.37   E       ATOM   1708   CE1   TYR   E   198   24.942   61.588   18.274   1.00   44.89   E       ATOM   1709   CD2   TYR   E   198   23.645   60.984   15.895   1.00   33.72   E       ATOM   1710   CE2   TYR   E   198   23.362   60.262   17.033   1.00   41.24   E       ATOM   1711   CZ   TYR   E   198   24.008   60.569   18.221   1.00   46.02   E       ATOM   1712   OH   TYR   E   198   23.702   59.875   19.363   1.00   43.60   E       ATOM   1713   C   TYR   E   198   25.665   62.739   12.309   1.00   40.33   E       ATOM   1714   O   TYR   E   198   24.735   63.478   12.001   1.00   37.35   E       ATOM   1715   N   GLU   E   199   26.705   62.544   11.510   1.00   42.59   E       ATOM   1716   CA   GLU   E   199   26.798   63.254   10.246   1.00   44.32   E       ATOM   1717   CB   GLU   E   199   28.234   63.271   9.753   1.00   45.64   E       ATOM   1718   CG   GLU   E   199   28.358   63.729   8.323   1.00   60.30   E       ATOM   1719   CD   GLU   E   199   29.612   64.535   8.097   1.00   80.08   E       ATOM   1720   OE1   GLU   E   199   29.902   64.857   6.918   1.00   88.69   E       ATOM   1721   OE2   GLU   E   199   30.299   64.855   9.104   1.00   85.89   E       ATOM   1722   C   GLU   E   199   25.920   62.766   9.116   1.00   42.47   E       ATOM   1723   O   GLU   E   199   25.411   63.571   8.355   1.00   42.38   E       ATOM   1724   N   HIS   E   200   25.752   61.452   8.999   1.00   48.21   E       ATOM   1725   CA   HIS   E   200   24.969   60.879   7.904   1.00   50.56   E       ATOM   1726   CB   HIS   E   200   25.862   59.945   7.067   1.00   51.56   E       ATOM   1727   CG   HIS   E   200   27.160   60.579   6.659   1.00   66.93   E       ATOM   1728   CD2   HIS   E   200   27.416   61.710   5.949   1.00   70.41   E       ATOM   1729   ND1   HIS   E   200   28.388   60.115   7.083   1.00   71.63   E       ATOM   1730   CE1   HIS   E   200   29.343   60.929   6.662   1.00   68.48   E       ATOM   1731   NE2   HIS   E   200   28.776   61.906   5.973   1.00   73.24   E       ATOM   1732   C   HIS   E   200   23.746   60.137   8.385   1.00   48.07   E       ATOM   1733   O   HIS   E   200   23.768   59.497   9.435   1.00   47.76   E       ATOM   1734   N   PRO   E   201   22.640   60.258   7.646   1.00   45.24   E       ATOM   1735   CD   PRO   E   201   22.407   61.202   6.545   1.00   41.22   E       ATOM   1736   CA   PRO   E   201   21.408   59.565   8.029   1.00   48.15   E       ATOM   1737   CB   PRO   E   201   20.338   60.262   7.188   1.00   43.73   E       ATOM   1738   CG   PRO   E   201   21.101   60.721   5.992   1.00   46.22   E       ATOM   1739   C   PRO   E   201   21.576   58.082   7.693   1.00   51.43   E       ATOM   1740   O   PRO   E   201   22.348   57.726   6.795   1.00   52.90   E       ATOM   1741   N   SER   E   202   20.868   57.219   8.416   1.00   54.88   E       ATOM   1742   CA   SER   E   202   20.977   55.772   8.202   1.00   54.89   E       ATOM   1743   CB   SER   E   202   20.054   55.012   9.142   1.00   51.86   E       ATOM   1744   OG   SER   E   202   18.719   55.146   8.697   1.00   53.06   E       ATOM   1745   C   SER   E   202   20.621   55.388   6.784   1.00   55.91   E       ATOM   1746   O   SER   E   202   19.596   55.808   6.255   1.00   60.73   E       ATOM   1747   N   PRO   E   203   21.446   54.551   6.154   1.00   56.97   E       ATOM   1748   CD   PRO   E   203   22.606   53.808   6.670   1.00   47.11   E       ATOM   1749   CA   PRO   E   203   21.130   54.163   4.776   1.00   56.59   E       ATOM   1750   CB   PRO   E   203   22.259   53.203   4.433   1.00   52.66   E       ATOM   1751   CG   PRO   E   203   22.602   52.614   5.795   1.00   45.14   E       ATOM   1752   C   PRO   E   203   19.725   53.565   4.573   1.00   54.90   E       ATOM   1753   O   PRO   E   203   19.269   53.448   3.437   1.00   54.58   E       ATOM   1754   N   GLU   E   204   19.039   53.195   5.653   1.00   52.27   E       ATOM   1755   CA   GLU   E   204   17.691   52.640   5.524   1.00   60.56   E       ATOM   1756   CB   GLU   E   204   17.271   51.958   6.805   1.00   65.25   E       ATOM   1757   CG   GLU   E   204   18.292   51.010   7.350   1.00   87.18   E       ATOM   1758   CD   GLU   E   204   18.017   50.695   8.809   1.00   102.16   E       ATOM   1759   OE1   GLU   E   204   18.179   51.609   9.654   1.00   104.48   E       ATOM   1760   OE2   GLU   E   204   17.621   49.541   9.111   1.00   109.20   E       ATOM   1761   C   GLU   E   204   16.703   53.763   5.249   1.00   63.74   E       ATOM   1762   O   GLU   E   204   15.758   53.607   4.465   1.00   59.93   E       ATOM   1763   N   ASP   E   205   16.928   54.891   5.927   1.00   67.57   E       ATOM   1764   CA   ASP   E   205   16.097   56.088   5.800   1.00   62.39   E       ATOM   1765   CB   ASP   E   205   16.433   57.085   6.901   1.00   60.01   E       ATOM   1766   CG   ASP   E   205   15.984   56.617   8.259   1.00   60.01   E       ATOM   1767   OD1   ASP   E   205   15.093   55.744   8.312   1.00   54.54   E       ATOM   1768   OD2   ASP   E   205   16.505   57.138   9.270   1.00   66.85   E       ATOM   1769   C   ASP   E   205   16.278   56.758   4.453   1.00   60.40   E       ATOM   1770   O   ASP   E   205   15.343   57.341   3.918   1.00   61.44   E       ATOM   1771   N   ILE   E   206   17.497   56.693   3.931   1.00   58.45   E       ATOM   1772   CA   ILE   E   206   17.825   57.250   2.625   1.00   57.04   E       ATOM   1773   CB   ILE   E   206   19.361   57.355   2.443   1.00   54.15   E       ATOM   1774   CG2   ILE   E   206   19.709   57.780   1.021   1.00   41.45   E       ATOM   1775   CG1   ILE   E   206   19.930   58.357   3.443   1.00   51.02   E       ATOM   1776   CD1   ILE   E   206   21.440   58.304   3.548   1.00   65.11   E       ATOM   1777   C   ILE   E   206   17.222   56.299   1.586   1.00   60.40   E       ATOM   1778   O   ILE   E   206   16.886   56.710   0.472   1.00   60.60   E       ATOM   1779   N   LYS   E   207   17.091   55.024   1.966   1.00   65.28   E       ATOM   1780   CA   LYS   E   207   16.484   54.006   1.104   1.00   66.30   E       ATOM   1781   CB   LYS   E   207   16.533   52.609   1.753   1.00   74.28   E       ATOM   1782   CG   LYS   E   207   15.997   51.466   0.852   1.00   78.22   E       ATOM   1783   CD   LYS   E   207   15.241   50.353   1.618   1.00   79.75   E       ATOM   1784   CE   LYS   E   207   16.129   49.605   2.611   1.00   81.47   E       ATOM   1785   NZ   LYS   E   207   15.502   48.353   3.141   1.00   77.97   E       ATOM   1786   C   LYS   E   207   15.025   54.432   0.958   1.00   62.85   E       ATOM   1787   O   LYS   E   207   14.591   54.757   −0.143   1.00   63.37   E       ATOM   1788   N   ARG   E   208   14.284   54.448   2.072   1.00   55.10   E       ATOM   1789   CA   ARG   E   208   12.883   54.860   2.053   1.00   53.30   E       ATOM   1790   CB   ARG   E   208   12.403   55.269   3.434   1.00   51.20   E       ATOM   1791   CG   ARG   E   208   12.086   54.150   4.345   1.00   55.85   E       ATOM   1792   CD   ARG   E   208   11.595   54.684   5.675   1.00   66.14   E       ATOM   1793   NE   ARG   E   208   11.687   53.662   6.717   1.00   77.33   E       ATOM   1794   CZ   ARG   E   208   12.812   53.323   7.347   1.00   79.98   E       ATOM   1795   NH1   ARG   E   208   13.956   53.933   7.052   1.00   76.94   E       ATOM   1796   NH2   ARG   E   208   12.797   52.360   8.264   1.00   82.91   E       ATOM   1797   C   ARG   E   208   12.629   56.037   1.136   1.00   55.84   E       ATOM   1798   O   ARG   E   208   11.614   56.079   0.449   1.00   60.42   E       ATOM   1799   N   ILE   E   209   13.538   57.007   1.136   1.00   58.02   E       ATOM   1800   CA   ILE   E   209   13.361   58.179   0.297   1.00   58.86   E       ATOM   1801   CB   ILE   E   209   14.403   59.276   0.606   1.00   53.27   E       ATOM   1802   CG2   ILE   E   209   14.405   60.337   −0.493   1.00   52.48   E       ATOM   1803   CG1   ILE   E   209   14.059   59.938   1.936   1.00   41.03   E       ATOM   1804   CD1   ILE   E   209   14.868   61.134   2.232   1.00   45.96   E       ATOM   1805   C   ILE   E   209   13.399   57.859   −1.182   1.00   61.16   E       ATOM   1806   O   ILE   E   209   12.535   58.315   −1.928   1.00   68.46   E       ATOM   1807   N   VAL   E   210   14.380   57.074   −1.615   1.00   61.10   E       ATOM   1808   CA   VAL   E   210   14.464   56.743   −3.035   1.00   66.44   E       ATOM   1809   CB   VAL   E   210   15.785   56.059   −3.376   1.00   60.54   E       ATOM   1810   CG1   VAL   E   210   16.015   56.173   −4.872   1.00   49.11   E       ATOM   1811   CG2   VAL   E   210   16.924   56.678   −2.577   1.00   49.95   E       ATOM   1812   C   VAL   E   210   13.315   55.845   −3.519   1.00   70.77   E       ATOM   1813   O   VAL   E   210   12.790   56.032   −4.618   1.00   74.50   E       ATOM   1814   N   ASN   E   211   12.935   54.869   −2.701   1.00   70.69   E       ATOM   1815   CA   ASN   E   211   11.846   53.965   −3.043   1.00   70.57   E       ATOM   1816   CB   ASN   E   211   11.959   52.632   −2.301   1.00   74.41   E       ATOM   1817   CG   ASN   E   211   13.300   51.954   −2.503   1.00   78.30   E       ATOM   1818   OD1   ASN   E   211   14.015   52.225   −3.476   1.00   76.46   E       ATOM   1819   ND2   ASN   E   211   13.646   51.050   −1.583   1.00   80.75   E       ATOM   1820   C   ASN   E   211   10.582   54.627   −2.587   1.00   71.71   E       ATOM   1821   O   ASN   E   211   9.880   54.091   −1.734   1.00   73.49   E       ATOM   1822   N   ALA   E   212   10.308   55.804   −3.128   1.00   73.73   E       ATOM   1823   CA   ALA   E   212   9.107   56.543   −2.770   1.00   76.95   E       ATOM   1824   CB   ALA   E   212   9.397   57.541   −1.640   1.00   72.06   E       ATOM   1825   C   ALA   E   212   8.639   57.274   −4.011   1.00   79.72   E       ATOM   1826   O   ALA   E   212   7.513   57.782   −4.053   1.00   80.85   E       ATOM   1827   N   ALA   E   213   9.507   57.313   −5.024   1.00   79.03   E       ATOM   1828   CA   ALA   E   213   9.187   57.987   −6.280   1.00   85.44   E       ATOM   1829   CB   ALA   E   213   10.189   57.592   −7.361   1.00   74.35   E       ATOM   1830   C   ALA   E   213   7.766   57.643   −6.728   1.00   92.69   E       ATOM   1831   O   ALA   E   213   7.411   56.471   −6.832   1.00   97.04   E       ATOM   1832   N   PRO   E   214   6.922   58.662   −6.969   1.00   96.04   E       ATOM   1833   CD   PRO   E   214   7.085   60.071   −6.580   1.00   97.64   E       ATOM   1834   CA   PRO   E   214   5.547   58.414   −7.406   1.00   97.66   E       ATOM   1835   CB   PRO   E   214   4.898   59.793   −7.305   1.00   97.44   E       ATOM   1836   CG   PRO   E   214   5.672   60.454   −6.238   1.00   98.77   E       ATOM   1837   C   PRO   E   214   5.509   57.886   −8.839   1.00   100.95   E       ATOM   1838   O   PRO   E   214   6.551   57.609   −9.448   1.00   99.62   E       ATOM   1839   N   GLU   E   215   4.297   57.759   −9.369   1.00   103.11   E       ATOM   1840   CA   GLU   E   215   4.088   57.287   −10.731   1.00   103.57   E       ATOM   1841   CB   GLU   E   215   2.587   57.206   −11.013   1.00   105.61   E       ATOM   1842   CG   GLU   E   215   1.748   56.844   −9.792   1.00   110.38   E       ATOM   1843   CD   GLU   E   215   0.278   57.221   −9.949   1.00   115.86   E       ATOM   1844   OE1   GLU   E   215   −0.015   58.406   −10.237   1.00   115.76   E       ATOM   1845   OE2   GLU   E   215   −0.587   56.334   −9.774   1.00   119.71   E       ATOM   1846   C   GLU   E   215   4.749   58.302   −11.671   1.00   103.96   E       ATOM   1847   O   GLU   E   215   4.225   59.406   −11.872   1.00   102.63   E       ATOM   1848   N   GLU   E   216   5.901   57.932   −12.231   1.00   103.93   E       ATOM   1849   CA   GLU   E   216   6.641   58.819   −13.133   1.00   102.83   E       ATOM   1850   CB   GLU   E   216   5.908   58.949   −14.465   1.00   103.19   E       ATOM   1851   CG   GLU   E   216   5.919   57.666   −15.277   1.00   106.65   E       ATOM   1852   CD   GLU   E   216   5.094   57.763   −16.544   1.00   107.70   E       ATOM   1853   OE1   GLU   E   216   5.312   58.715   −17.323   1.00   111.42   E       ATOM   1854   OE2   GLU   E   216   4.234   56.884   −16.767   1.00   107.18   E       ATOM   1855   C   GLU   E   216   6.810   60.193   −12.495   1.00   101.72   E       ATOM   1856   O   GLU   E   216   6.120   61.153   −12.857   1.00   98.48   E       ATOM   1857   N   GLU   E   217   7.741   60.267   −11.545   1.00   101.00   E       ATOM   1858   CA   GLU   E   217   8.006   61.492   −10.810   1.00   96.68   E       ATOM   1859   CB   GLU   E   217   9.136   61.271   −9.803   1.00   95.92   E       ATOM   1860   CG   GLU   E   217   9.075   62.255   −8.647   1.00   92.06   E       ATOM   1861   CD   GLU   E   217   9.841   61.786   −7.433   1.00   87.31   E       ATOM   1862   OE1   GLU   E   217   9.603   62.357   −6.344   1.00   78.36   E       ATOM   1863   OE2   GLU   E   217   10.672   60.856   −7.577   1.00   82.01   E       ATOM   1864   C   GLU   E   217   8.327   62.675   −11.712   1.00   95.99   E       ATOM   1865   O   GLU   E   217   9.045   62.546   −12.709   1.00   91.78   E       ATOM   1866   N   ASN   E   218   7.780   63.828   −11.328   1.00   94.78   E       ATOM   1867   CA   ASN   E   218   7.915   65.094   −12.048   1.00   90.55   E       ATOM   1868   CB   ASN   E   218   7.362   66.227   −11.172   1.00   84.77   E       ATOM   1869   CG   ASN   E   218   5.951   65.933   −10.674   1.00   80.53   E       ATOM   1870   OD1   ASN   E   218   5.067   65.588   −11.460   1.00   84.63   E       ATOM   1871   ND2   ASN   E   218   5.734   66.067   −9.373   1.00   67.42   E       ATOM   1872   C   ASN   E   218   9.310   65.452   −12.577   1.00   89.43   E       ATOM   1873   O   ASN   E   218   9.467   66.499   −13.221   1.00   84.83   E       ATOM   1874   N   VAL   E   219   10.297   64.585   −12.302   1.00   85.75   E       ATOM   1875   CA   VAL   E   219   11.692   64.734   −12.751   1.00   83.21   E       ATOM   1876   CB   VAL   E   219   11.754   64.884   −14.302   1.00   86.51   E       ATOM   1877   CG1   VAL   E   219   11.816   66.377   −14.704   1.00   86.68   E       ATOM   1878   CG2   VAL   E   219   12.940   64.101   −14.855   1.00   84.48   E       ATOM   1879   C   VAL   E   219   12.431   65.909   −12.099   1.00   82.44   E       ATOM   1880   O   VAL   E   219   13.665   65.933   −12.023   1.00   71.78   E       ATOM   1881   N   ALA   E   220   11.649   66.894   −11.665   1.00   83.97   E       ATOM   1882   CA   ALA   E   220   12.147   68.082   −10.994   1.00   80.39   E       ATOM   1883   CB   ALA   E   220   11.562   69.330   −11.621   1.00   75.61   E       ATOM   1884   C   ALA   E   220   11.622   67.912   −9.590   1.00   82.06   E       ATOM   1885   O   ALA   E   220   11.923   68.690   −8.694   1.00   86.36   E       ATOM   1886   N   GLU   E   221   10.810   66.879   −9.417   1.00   81.39   E       ATOM   1887   CA   GLU   E   221   10.246   66.580   −8.125   1.00   86.99   E       ATOM   1888   CB   GLU   E   221   8.853   66.022   −8.297   1.00   92.66   E       ATOM   1889   CG   GLU   E   221   7.796   67.052   −8.041   1.00   102.40   E       ATOM   1890   CD   GLU   E   221   7.877   67.609   −6.633   1.00   109.23   E       ATOM   1891   OE1   GLU   E   221   8.134   66.810   −5.697   1.00   109.14   E       ATOM   1892   OE2   GLU   E   221   7.673   68.837   −6.465   1.00   109.67   E       ATOM   1893   C   GLU   E   221   11.132   65.590   −7.397   1.00   90.81   E       ATOM   1894   O   GLU   E   221   11.192   65.578   −6.165   1.00   89.18   E       ATOM   1895   N   GLU   E   222   11.828   64.760   −8.167   1.00   94.11   E       ATOM   1896   CA   GLU   E   222   12.733   63.781   −7.583   1.00   94.68   E       ATOM   1897   CB   GLU   E   222   13.042   62.658   −8.584   1.00   98.88   E       ATOM   1898   CG   GLU   E   222   13.844   61.481   −8.021   1.00   101.14   E       ATOM   1899   CD   GLU   E   222   15.339   61.589   −8.301   1.00   104.36   E       ATOM   1900   OE1   GLU   E   222   15.727   61.583   −9.494   1.00   102.91   E       ATOM   1901   OE2   GLU   E   222   16.125   61.679   −7.330   1.00   104.65   E       ATOM   1902   C   GLU   E   222   13.997   64.539   −7.205   1.00   92.44   E       ATOM   1903   O   GLU   E   222   15.042   63.948   −6.946   1.00   99.56   E       ATOM   1904   N   ARG   E   223   13.895   65.863   −7.204   1.00   83.62   E       ATOM   1905   CA   ARG   E   223   15.001   66.724   −6.816   1.00   73.36   E       ATOM   1906   CB   ARG   E   223   15.361   67.710   −7.927   1.00   68.97   E       ATOM   1907   CG   ARG   E   223   16.254   67.139   −9.003   1.00   74.59   E       ATOM   1908   CD   ARG   E   223   17.702   67.074   −8.553   1.00   80.35   E       ATOM   1909   NE   ARG   E   223   18.530   66.283   −9.463   1.00   87.11   E       ATOM   1910   CZ   ARG   E   223   18.519   64.951   −9.523   1.00   89.83   E       ATOM   1911   NH1   ARG   E   223   17.725   64.249   −8.720   1.00   89.06   E       ATOM   1912   NH2   ARG   E   223   19.296   64.317   −10.390   1.00   89.00   E       ATOM   1913   C   ARG   E   223   14.479   67.474   −5.616   1.00   66.94   E       ATOM   1914   O   ARG   E   223   15.141   67.575   −4.595   1.00   72.27   E       ATOM   1915   N   PHE   E   224   13.264   67.984   −5.739   1.00   56.45   E       ATOM   1916   CA   PHE   E   224   12.652   68.729   −4.657   1.00   51.72   E       ATOM   1917   CB   PHE   E   224   11.396   69.426   −5.162   1.00   45.84   E       ATOM   1918   CG   PHE   E   224   10.612   70.114   −4.081   1.00   44.08   E       ATOM   1919   CD1   PHE   E   224   10.903   71.427   −3.716   1.00   43.29   E       ATOM   1920   CD2   PHE   E   224   9.575   69.450   −3.427   1.00   33.81   E       ATOM   1921   CE1   PHE   E   224   10.164   72.063   −2.716   1.00   40.50   E       ATOM   1922   CE2   PHE   E   224   8.836   70.082   −2.435   1.00   32.02   E       ATOM   1923   CZ   PHE   E   224   9.131   71.389   −2.081   1.00   34.88   E       ATOM   1924   C   PHE   E   224   12.297   67.844   −3.465   1.00   54.07   E       ATOM   1925   O   PHE   E   224   12.523   68.212   −2.313   1.00   52.27   E       ATOM   1926   N   ARG   E   225   11.730   66.674   −3.746   1.00   59.88   E       ATOM   1927   CA   ARG   E   225   11.338   65.746   −2.689   1.00   55.01   E       ATOM   1928   CB   ARG   E   225   10.632   64.517   −3.275   1.00   57.72   E       ATOM   1929   CG   ARG   E   225   9.791   63.743   −2.259   1.00   58.92   E       ATOM   1930   CD   ARG   E   225   9.419   62.354   −2.766   1.00   58.97   E       ATOM   1931   NE   ARG   E   225   10.605   61.514   −2.893   1.00   65.72   E       ATOM   1932   CZ   ARG   E   225   10.790   60.660   −3.887   1.00   60.47   E       ATOM   1933   NH1   ARG   E   225   9.857   60.551   −4.812   1.00   66.80   E       ATOM   1934   NH2   ARG   E   225   11.905   59.946   −3.978   1.00   58.05   E       ATOM   1935   C   ARG   E   225   12.575   65.307   −1.923   1.00   49.76   E       ATOM   1936   O   ARG   E   225   12.523   65.132   −0.721   1.00   44.61   E       ATOM   1937   N   HIS   E   226   13.688   65.122   −2.623   1.00   49.52   E       ATOM   1938   CA   HIS   E   226   14.916   64.721   −1.956   1.00   50.69   E       ATOM   1939   CB   HIS   E   226   16.000   64.401   −2.988   1.00   56.47   E       ATOM   1940   CG   HIS   E   226   15.992   62.973   −3.446   1.00   61.46   E       ATOM   1941   CD2   HIS   E   226   16.988   62.181   −3.912   1.00   62.54   E       ATOM   1942   ND1   HIS   E   226   14.846   62.202   −3.467   1.00   56.15   E       ATOM   1943   CE1   HIS   E   226   15.136   60.997   −3.925   1.00   56.70   E       ATOM   1944   NE2   HIS   E   226   16.429   60.958   −4.203   1.00   65.13   E       ATOM   1945   C   HIS   E   226   15.370   65.824   −1.010   1.00   49.73   E       ATOM   1946   O   HIS   E   226   15.709   65.569   0.149   1.00   54.63   E       ATOM   1947   N   ILE   E   227   15.347   67.056   −1.501   1.00   45.93   E       ATOM   1948   CA   ILE   E   227   15.729   68.212   −0.710   1.00   39.16   E       ATOM   1949   CB   ILE   E   227   15.551   69.481   −1.532   1.00   33.64   E       ATOM   1950   CG2   ILE   E   227   15.619   70.697   −0.654   1.00   38.70   E       ATOM   1951   CG1   ILE   E   227   16.637   69.529   −2.596   1.00   39.45   E       ATOM   1952   CD1   ILE   E   227   16.600   70.746   −3.474   1.00   42.76   E       ATOM   1953   C   ILE   E   227   14.922   68.328   0.584   1.00   38.85   E       ATOM   1954   O   ILE   E   227   15.479   68.506   1.662   1.00   41.38   E       ATOM   1955   N   THR   E   228   13.608   68.206   0.493   1.00   36.96   E       ATOM   1956   CA   THR   E   228   12.797   68.336   1.692   1.00   39.83   E       ATOM   1957   CB   THR   E   228   11.390   68.903   1.339   1.00   32.96   E       ATOM   1958   OG1   THR   E   228   10.535   67.865   0.866   1.00   29.56   E       ATOM   1959   CG2   THR   E   228   11.515   69.940   0.256   1.00   28.02   E       ATOM   1960   C   THR   E   228   12.668   67.072   2.561   1.00   41.84   E       ATOM   1961   O   THR   E   228   12.536   67.162   3.785   1.00   45.14   E       ATOM   1962   N   GLU   E   229   12.723   65.902   1.941   1.00   41.17   E       ATOM   1963   CA   GLU   E   229   12.604   64.656   2.680   1.00   42.21   E       ATOM   1964   CB   GLU   E   229   12.345   63.516   1.713   1.00   52.27   E       ATOM   1965   CG   GLU   E   229   11.033   63.628   0.958   1.00   61.58   E       ATOM   1966   CD   GLU   E   229   9.879   62.936   1.663   1.00   67.04   E       ATOM   1967   OE1   GLU   E   229   9.615   63.279   2.847   1.00   64.96   E       ATOM   1968   OE2   GLU   E   229   9.244   62.056   1.015   1.00   68.59   E       ATOM   1969   C   GLU   E   229   13.883   64.388   3.458   1.00   43.81   E       ATOM   1970   O   GLU   E   229   13.854   64.107   4.668   1.00   41.33   E       ATOM   1971   N   ILE   E   230   15.013   64.471   2.761   1.00   38.60   E       ATOM   1972   CA   ILE   E   230   16.295   64.242   3.412   1.00   38.64   E       ATOM   1973   CB   ILE   E   230   17.452   64.356   2.401   1.00   33.51   E       ATOM   1974   CG2   ILE   E   230   18.771   64.116   3.091   1.00   34.50   E       ATOM   1975   CG1   ILE   E   230   17.275   63.334   1.288   1.00   30.46   E       ATOM   1976   CD1   ILE   E   230   18.326   63.439   0.187   1.00   34.35   E       ATOM   1977   C   ILE   E   230   16.529   65.254   4.552   1.00   41.49   E       ATOM   1978   O   ILE   E   230   17.167   64.928   5.549   1.00   42.12   E       ATOM   1979   N   THR   E   231   16.009   66.474   4.398   1.00   38.22   E       ATOM   1980   CA   THR   E   231   16.188   67.526   5.389   1.00   37.71   E       ATOM   1981   CB   THR   E   231   15.690   68.880   4.846   1.00   38.83   E       ATOM   1982   OG1   THR   E   231   16.599   69.343   3.845   1.00   36.93   E       ATOM   1983   CG2   THR   E   231   15.596   69.926   5.958   1.00   37.65   E       ATOM   1984   C   THR   E   231   15.488   67.202   6.699   1.00   40.58   E       ATOM   1985   O   THR   E   231   15.800   67.779   7.746   1.00   39.82   E       ATOM   1986   N   ILE   E   232   14.528   66.288   6.642   1.00   38.47   E       ATOM   1987   CA   ILE   E   232   13.842   65.884   7.856   1.00   37.93   E       ATOM   1988   CB   ILE   E   232   12.709   64.919   7.576   1.00   35.83   E       ATOM   1989   CG2   ILE   E   232   12.192   64.373   8.864   1.00   37.58   E       ATOM   1990   CG1   ILE   E   232   11.588   65.633   6.840   1.00   34.90   E       ATOM   1991   CD1   ILE   E   232   11.049   64.810   5.706   1.00   39.78   E       ATOM   1992   C   ILE   E   232   14.898   65.145   8.651   1.00   37.38   E       ATOM   1993   O   ILE   E   232   15.044   65.347   9.852   1.00   39.17   E       ATOM   1994   N   LEU   E   233   15.628   64.285   7.949   1.00   34.45   E       ATOM   1995   CA   LEU   E   233   16.723   63.503   8.517   1.00   35.30   E       ATOM   1996   CB   LEU   E   233   17.354   62.611   7.430   1.00   33.51   E       ATOM   1997   CG   LEU   E   233   16.711   61.228   7.214   1.00   30.84   E       ATOM   1998   CD1   LEU   E   233   15.355   61.186   7.974   1.00   4.40   E       ATOM   1999   CD2   LEU   E   233   16.583   60.926   5.695   1.00   23.27   E       ATOM   2000   C   LEU   E   233   17.804   64.391   9.113   1.00   35.91   E       ATOM   2001   O   LEU   E   233   18.360   64.069   10.166   1.00   29.18   E       ATOM   2002   N   THR   E   234   18.094   65.500   8.423   1.00   36.21   E       ATOM   2003   CA   THR   E   234   19.119   66.450   8.848   1.00   36.54   E       ATOM   2004   CB   THR   E   234   19.327   67.593   7.814   1.00   39.35   E       ATOM   2005   OG1   THR   E   234   19.557   67.043   6.508   1.00   41.29   E       ATOM   2006   CG2   THR   E   234   20.528   68.470   8.227   1.00   29.41   E       ATOM   2007   C   THR   E   234   18.741   67.081   10.181   1.00   37.17   E       ATOM   2008   O   THR   E   234   19.550   67.149   11.094   1.00   39.38   E       ATOM   2009   N   VAL   E   235   17.507   67.548   10.299   1.00   35.56   E       ATOM   2010   CA   VAL   E   235   17.086   68.169   11.540   1.00   33.16   E       ATOM   2011   CB   VAL   E   235   15.693   68.793   11.409   1.00   32.20   E       ATOM   2012   CG1   VAL   E   235   15.227   69.325   12.759   1.00   22.81   E       ATOM   2013   CG2   VAL   E   235   15.751   69.908   10.388   1.00   25.24   E       ATOM   2014   C   VAL   E   235   17.097   67.164   12.674   1.00   32.90   E       ATOM   2015   O   VAL   E   235   17.409   67.509   13.817   1.00   30.52   E       ATOM   2016   N   GLN   E   236   16.777   65.919   12.355   1.00   29.64   E       ATOM   2017   CA   GLN   E   236   16.772   64.883   13.361   1.00   35.12   E       ATOM   2018   CB   GLN   E   236   16.188   63.620   12.778   1.00   40.23   E       ATOM   2019   CG   GLN   E   236   14.822   63.861   12.211   1.00   53.81   E       ATOM   2020   CD   GLN   E   236   14.041   62.588   12.009   1.00   53.35   E       ATOM   2021   OE1   GLN   E   236   14.462   61.695   11.265   1.00   49.34   E       ATOM   2022   NE2   GLN   E   236   12.889   62.497   12.672   1.00   53.19   E       ATOM   2023   C   GLN   E   236   18.182   64.633   13.880   1.00   38.28   E       ATOM   2024   O   GLN   E   236   18.407   64.595   15.098   1.00   46.79   E       ATOM   2025   N   LEU   E   237   19.122   64.465   12.951   1.00   33.28   E       ATOM   2026   CA   LEU   E   237   20.525   64.260   13.276   1.00   28.95   E       ATOM   2027   CB   LEU   E   237   21.331   64.180   11.991   1.00   20.94   E       ATOM   2028   CG   LEU   E   237   21.164   62.888   11.220   1.00   24.35   E       ATOM   2029   CD1   LEU   E   237   21.703   63.031   9.811   1.00   31.88   E       ATOM   2030   CD2   LEU   E   237   21.877   61.798   11.981   1.00   12.59   E       ATOM   2031   C   LEU   E   237   21.023   65.445   14.124   1.00   32.97   E       ATOM   2032   O   LEU   E   237   21.847   65.279   15.031   1.00   34.52   E       ATOM   2033   N   ILE   E   238   20.529   66.644   13.823   1.00   27.69   E       ATOM   2034   CA   ILE   E   238   20.914   67.816   14.582   1.00   26.59   E       ATOM   2035   CB   ILE   E   238   20.332   69.082   13.973   1.00   21.55   E       ATOM   2036   CG2   ILE   E   238   20.483   70.227   14.948   1.00   19.01   E       ATOM   2037   CG1   ILE   E   238   21.036   69.366   12.639   1.00   26.28   E       ATOM   2038   CD1   ILE   E   238   20.473   70.523   11.831   1.00   19.16   E       ATOM   2039   C   ILE   E   238   20.408   67.669   16.010   1.00   32.55   E       ATOM   2040   O   ILE   E   238   21.132   67.980   16.964   1.00   30.08   E       ATOM   2041   N   VAL   E   239   19.173   67.190   16.168   1.00   30.61   E       ATOM   2042   CA   VAL   E   239   18.644   67.023   17.507   1.00   33.98   E       ATOM   2043   CB   VAL   E   239   17.162   66.625   17.518   1.00   29.85   E       ATOM   2044   CG1   VAL   E   239   16.647   66.660   18.940   1.00   37.96   E       ATOM   2045   CG2   VAL   E   239   16.355   67.575   16.706   1.00   35.97   E       ATOM   2046   C   VAL   E   239   19.428   65.930   18.219   1.00   37.91   E       ATOM   2047   O   VAL   E   239   19.685   66.032   19.423   1.00   39.77   E       ATOM   2048   N   GLU   E   240   19.806   64.894   17.470   1.00   30.46   E       ATOM   2049   CA   GLU   E   240   20.551   63.767   18.020   1.00   34.21   E       ATOM   2050   CB   GLU   E   240   20.834   62.716   16.938   1.00   49.56   E       ATOM   2051   CG   GLU   E   240   19.662   61.785   16.653   1.00   65.08   E       ATOM   2052   CD   GLU   E   240   18.953   61.378   17.939   1.00   79.27   E       ATOM   2053   OE1   GLU   E   240   17.993   62.086   18.344   1.00   83.63   E       ATOM   2054   OE2   GLU   E   240   19.376   60.369   18.561   1.00   84.61   E       ATOM   2055   C   GLU   E   240   21.851   64.203   18.648   1.00   33.16   E       ATOM   2056   O   GLU   E   240   22.186   63.805   19.760   1.00   37.83   E       ATOM   2057   N   PHE   E   241   22.580   65.027   17.919   1.00   35.09   E       ATOM   2058   CA   PHE   E   241   23.854   65.559   18.375   1.00   33.75   E       ATOM   2059   CB   PHE   E   241   24.552   66.222   17.174   1.00   34.01   E       ATOM   2060   CG   PHE   E   241   25.842   66.924   17.498   1.00   27.48   E       ATOM   2061   CD1   PHE   E   241   27.056   66.306   17.266   1.00   27.18   E       ATOM   2062   CD2   PHE   E   241   25.838   68.228   18.004   1.00   32.42   E       ATOM   2063   CE1   PHE   E   241   28.250   66.972   17.529   1.00   33.13   E       ATOM   2064   CE2   PHE   E   241   27.032   68.911   18.272   1.00   27.18   E       ATOM   2065   CZ   PHE   E   241   28.238   68.281   18.035   1.00   30.10   E       ATOM   2066   C   PHE   E   241   23.639   66.562   19.524   1.00   32.50   E       ATOM   2067   O   PHE   E   241   24.338   66.527   20.522   1.00   30.55   E       ATOM   2068   N   SER   E   242   22.660   67.448   19.397   1.00   34.08   E       ATOM   2069   CA   SER   E   242   22.420   68.435   20.447   1.00   38.69   E       ATOM   2070   CB   SER   E   242   21.212   69.303   20.100   1.00   40.24   E       ATOM   2071   OG   SER   E   242   21.477   70.073   18.944   1.00   37.08   E       ATOM   2072   C   SER   E   242   22.220   67.837   21.833   1.00   39.84   E       ATOM   2073   O   SER   E   242   22.591   68.434   22.835   1.00   40.74   E       ATOM   2074   N   LYS   E   243   21.654   66.645   21.896   1.00   42.89   E       ATOM   2075   CA   LYS   E   243   21.397   66.023   23.180   1.00   41.67   E       ATOM   2076   CB   LYS   E   243   20.298   64.981   23.011   1.00   38.11   E       ATOM   2077   CG   LYS   E   243   18.939   65.557   22.638   1.00   41.39   E       ATOM   2078   CD   LYS   E   243   17.925   64.436   22.447   1.00   43.69   E       ATOM   2079   CE   LYS   E   243   16.573   64.963   22.086   1.00   50.92   E       ATOM   2080   NZ   LYS   E   243   15.715   63.865   21.585   1.00   55.82   E       ATOM   2081   C   LYS   E   243   22.615   65.401   23.856   1.00   38.18   E       ATOM   2082   O   LYS   E   243   22.668   65.274   25.082   1.00   43.36   E       ATOM   2083   N   ARG   E   244   23.600   65.008   23.070   1.00   36.51   E       ATOM   2084   CA   ARG   E   244   24.787   64.386   23.651   1.00   41.55   E       ATOM   2085   CB   ARG   E   244   25.474   63.478   22.616   1.00   37.53   E       ATOM   2086   CG   ARG   E   244   24.497   62.607   21.818   1.00   46.34   E       ATOM   2087   CD   ARG   E   244   24.227   61.262   22.459   1.00   48.64   E       ATOM   2088   NE   ARG   E   244   25.425   60.432   22.424   1.00   54.52   E       ATOM   2089   CZ   ARG   E   244   25.468   59.163   22.803   1.00   58.12   E       ATOM   2090   NH1   ARG   E   244   24.366   58.566   23.245   1.00   67.20   E       ATOM   2091   NH2   ARG   E   244   26.619   58.498   22.765   1.00   59.41   E       ATOM   2092   C   ARG   E   244   25.759   65.464   24.128   1.00   41.59   E       ATOM   2093   O   ARG   E   244   26.862   65.143   24.594   1.00   39.08   E       ATOM   2094   N   LEU   E   245   25.337   66.730   24.010   1.00   33.30   E       ATOM   2095   CA   LEU   E   245   26.164   67.870   24.412   1.00   33.61   E       ATOM   2096   CB   LEU   E   245   25.776   69.153   23.656   1.00   35.79   E       ATOM   2097   CG   LEU   E   245   25.948   69.308   22.141   1.00   37.15   E       ATOM   2098   CD1   LEU   E   245   25.622   70.743   21.750   1.00   30.82   E       ATOM   2099   CD2   LEU   E   245   27.353   68.971   21.727   1.00   26.22   E       ATOM   2100   C   LEU   E   245   26.071   68.168   25.897   1.00   35.48   E       ATOM   2101   O   LEU   E   245   24.978   68.418   26.433   1.00   38.59   E       ATOM   2102   N   PRO   E   246   27.227   68.149   26.588   1.00   34.31   E       ATOM   2103   CD   PRO   E   246   28.510   67.738   25.993   1.00   29.84   E       ATOM   2104   CA   PRO   E   246   27.380   68.418   28.025   1.00   31.73   E       ATOM   2105   CB   PRO   E   246   28.883   68.555   28.175   1.00   26.92   E       ATOM   2106   CG   PRO   E   246   29.395   67.539   27.200   1.00   23.72   E       ATOM   2107   C   PRO   E   246   26.652   69.705   28.425   1.00   34.47   E       ATOM   2108   O   PRO   E   246   26.919   70.764   27.891   1.00   26.51   E       ATOM   2109   N   GLY   E   247   25.719   69.614   29.355   1.00   42.98   E       ATOM   2110   CA   GLY   E   247   25.011   70.808   29.760   1.00   44.36   E       ATOM   2111   C   GLY   E   247   23.590   70.854   29.251   1.00   46.41   E       ATOM   2112   O   GLY   E   247   22.739   71.505   29.848   1.00   52.00   E       ATOM   2113   N   PHE   E   248   23.317   70.165   28.152   1.00   45.04   E       ATOM   2114   CA   PHE   E   248   21.964   70.173   27.598   1.00   43.31   E       ATOM   2115   CB   PHE   E   248   21.927   69.389   26.287   1.00   32.36   E       ATOM   2116   CG   PHE   E   248   20.738   69.697   25.438   1.00   33.24   E       ATOM   2117   CD1   PHE   E   248   20.616   70.934   24.816   1.00   29.68   E       ATOM   2118   CD2   PHE   E   248   19.732   68.758   25.259   1.00   40.57   E       ATOM   2119   CE1   PHE   E   248   19.516   71.233   24.030   1.00   32.10   E       ATOM   2120   CE2   PHE   E   248   18.621   69.051   24.471   1.00   40.63   E       ATOM   2121   CZ   PHE   E   248   18.516   70.291   23.857   1.00   34.65   E       ATOM   2122   C   PHE   E   248   20.949   69.583   28.586   1.00   41.89   E       ATOM   2123   O   PHE   E   248   19.786   69.973   28.623   1.00   38.90   E       ATOM   2124   N   ASP   E   249   21.409   68.637   29.390   1.00   42.84   E       ATOM   2125   CA   ASP   E   249   20.565   67.990   30.373   1.00   46.68   E       ATOM   2126   CB   ASP   E   249   21.216   66.686   30.794   1.00   49.98   E       ATOM   2127   CG   ASP   E   249   22.575   66.903   31.437   1.00   62.57   E       ATOM   2128   OD1   ASP   E   249   23.126   65.933   32.000   1.00   70.44   E       ATOM   2129   OD2   ASP   E   249   23.099   68.045   31.382   1.00   67.68   E       ATOM   2130   C   ASP   E   249   20.363   68.889   31.603   1.00   47.20   E       ATOM   2131   O   ASP   E   249   19.433   68.716   32.373   1.00   49.50   E       ATOM   2132   N   LYS   E   250   21.237   69.854   31.802   1.00   45.53   E       ATOM   2133   CA   LYS   E   250   21.080   70.730   32.938   1.00   45.70   E       ATOM   2134   CB   LYS   E   250   22.406   71.450   33.188   1.00   49.35   E       ATOM   2135   CG   LYS   E   250   23.622   70.517   33.347   1.00   56.63   E       ATOM   2136   CD   LYS   E   250   23.506   69.582   34.555   1.00   63.25   E       ATOM   2137   CE   LYS   E   250   24.826   68.887   34.883   1.00   67.60   E       ATOM   2138   NZ   LYS   E   250   25.438   68.134   33.723   1.00   81.91   E       ATOM   2139   C   LYS   E   250   19.935   71.744   32.697   1.00   48.33   E       ATOM   2140   O   LYS   E   250   19.618   72.560   33.567   1.00   55.90   E       ATOM   2141   N   LEU   E   251   19.309   71.678   31.522   1.00   44.08   E       ATOM   2142   CA   LEU   E   251   18.220   72.591   31.138   1.00   36.71   E       ATOM   2143   CB   LEU   E   251   18.399   73.054   29.685   1.00   31.98   E       ATOM   2144   CG   LEU   E   251   19.714   73.688   29.267   1.00   30.27   E       ATOM   2145   CD1   LEU   E   251   19.603   74.195   27.846   1.00   26.21   E       ATOM   2146   CD2   LEU   E   251   20.033   74.827   30.209   1.00   31.20   E       ATOM   2147   C   LEU   E   251   16.838   71.964   31.252   1.00   34.43   E       ATOM   2148   O   LEU   E   251   16.680   70.748   31.166   1.00   31.57   E       ATOM   2149   N   ILE   E   252   15.827   72.805   31.403   1.00   33.03   E       ATOM   2150   CA   ILE   E   252   14.459   72.310   31.509   1.00   37.31   E       ATOM   2151   CB   ILE   E   252   13.592   73.372   32.252   1.00   37.73   E       ATOM   2152   CG2   ILE   E   252   14.493   74.225   33.126   1.00   36.05   E       ATOM   2153   CG1   ILE   E   252   12.925   74.333   31.275   1.00   39.95   E       ATOM   2154   CD1   ILE   E   252   12.218   75.477   31.937   1.00   27.77   E       ATOM   2155   C   ILE   E   252   13.889   71.941   30.108   1.00   40.70   E       ATOM   2156   O   ILE   E   252   14.277   72.542   29.101   1.00   36.30   E       ATOM   2157   N   ARG   E   253   12.990   70.952   30.040   1.00   41.30   E       ATOM   2158   CA   ARG   E   253   12.430   70.534   28.751   1.00   47.33   E       ATOM   2159   CB   ARG   E   253   11.251   69.575   28.927   1.00   51.86   E       ATOM   2160   CG   ARG   E   253   11.633   68.166   29.394   1.00   69.36   E       ATOM   2161   CD   ARG   E   253   10.418   67.208   29.302   1.00   81.36   E       ATOM   2162   NE   ARG   E   253   10.298   66.272   30.436   1.00   89.24   E       ATOM   2163   CZ   ARG   E   253   10.117   66.618   31.720   1.00   87.21   E       ATOM   2164   NH1   ARG   E   253   10.031   67.898   32.079   1.00   84.79   E       ATOM   2165   NH2   ARG   E   253   10.022   65.676   32.658   1.00   81.99   E       ATOM   2166   C   ARG   E   253   11.985   71.713   27.901   1.00   48.18   E       ATOM   2167   O   ARG   E   253   12.176   71.731   26.684   1.00   49.82   E       ATOM   2168   N   GLU   E   254   11.386   72.698   28.553   1.00   52.53   E       ATOM   2169   CA   GLU   E   254   10.903   73.902   27.889   1.00   50.59   E       ATOM   2170   CB   GLU   E   254   10.367   74.897   28.927   1.00   57.10   E       ATOM   2171   CG   GLU   E   254   9.074   74.487   29.649   1.00   66.58   E       ATOM   2172   CD   GLU   E   254   9.212   73.292   30.608   1.00   74.77   E       ATOM   2173   OE1   GLU   E   254   10.146   73.265   31.451   1.00   71.89   E       ATOM   2174   OE2   GLU   E   254   8.355   72.381   30.529   1.00   80.85   E       ATOM   2175   C   GLU   E   254   12.037   74.551   27.106   1.00   49.05   E       ATOM   2176   O   GLU   E   254   11.901   74.816   25.905   1.00   43.89   E       ATOM   2177   N   ASP   E   255   13.151   74.796   27.801   1.00   46.39   E       ATOM   2178   CA   ASP   E   255   14.327   75.423   27.207   1.00   47.30   E       ATOM   2179   CB   ASP   E   255   15.284   75.923   28.300   1.00   44.84   E       ATOM   2180   CG   ASP   E   255   14.756   77.171   29.041   1.00   50.25   E       ATOM   2181   OD1   ASP   E   255   13.728   77.751   28.611   1.00   47.08   E       ATOM   2182   OD2   ASP   E   255   15.383   77.575   30.053   1.00   38.00   E       ATOM   2183   C   ASP   E   255   15.064   74.495   26.245   1.00   46.83   E       ATOM   2184   O   ASP   E   255   15.597   74.944   25.239   1.00   45.90   E       ATOM   2185   N   GLN   E   256   15.099   73.202   26.545   1.00   47.36   E       ATOM   2186   CA   GLN   E   256   15.764   72.265   25.653   1.00   44.16   E       ATOM   2187   CB   GLN   E   256   15.623   70.840   26.155   1.00   39.83   E       ATOM   2188   CG   GLN   E   256   16.328   70.566   27.454   1.00   50.75   E       ATOM   2189   CD   GLN   E   256   16.201   69.116   27.891   1.00   51.86   E       ATOM   2190   OE1   GLN   E   256   17.093   68.580   28.551   1.00   51.56   E       ATOM   2191   NE2   GLN   E   256   15.092   68.477   27.535   1.00   51.80   E       ATOM   2192   C   GLN   E   256   15.082   72.371   24.306   1.00   47.75   E       ATOM   2193   O   GLN   E   256   15.729   72.557   23.282   1.00   52.70   E       ATOM   2194   N   ILE   E   257   13.760   72.266   24.315   1.00   45.22   E       ATOM   2195   CA   ILE   E   257   12.976   72.329   23.088   1.00   39.99   E       ATOM   2196   CB   ILE   E   257   11.483   72.029   23.401   1.00   34.69   E       ATOM   2197   CG2   ILE   E   257   10.621   72.336   22.202   1.00   39.38   E       ATOM   2198   CG1   ILE   E   257   11.326   70.557   23.790   1.00   33.50   E       ATOM   2199   CD1   ILE   E   257   9.907   70.125   24.072   1.00   38.84   E       ATOM   2200   C   ILE   E   257   13.120   73.659   22.327   1.00   38.00   E       ATOM   2201   O   ILE   E   257   13.139   73.697   21.102   1.00   39.30   E       ATOM   2202   N   ALA   E   258   13.243   74.752   23.056   1.00   34.43   E       ATOM   2203   CA   ALA   E   258   13.383   76.048   22.425   1.00   31.32   E       ATOM   2204   CB   ALA   E   258   13.292   77.129   23.474   1.00   26.11   E       ATOM   2205   C   ALA   E   258   14.710   76.149   21.683   1.00   36.70   E       ATOM   2206   O   ALA   E   258   14.735   76.537   20.511   1.00   34.47   E       ATOM   2207   N   LEU   E   259   15.800   75.807   22.386   1.00   36.87   E       ATOM   2208   CA   LEU   E   259   17.165   75.842   21.856   1.00   35.79   E       ATOM   2209   CB   LEU   E   259   18.164   75.243   22.848   1.00   33.20   E       ATOM   2210   CG   LEU   E   259   18.509   76.009   24.116   1.00   34.52   E       ATOM   2211   CD1   LEU   E   259   19.679   75.312   24.793   1.00   31.47   E       ATOM   2212   CD2   LEU   E   259   18.849   77.447   23.784   1.00   30.22   E       ATOM   2213   C   LEU   E   259   17.288   75.065   20.572   1.00   36.97   E       ATOM   2214   O   LEU   E   259   17.930   75.522   19.617   1.00   33.83   E       ATOM   2215   N   LEU   E   260   16.684   73.876   20.593   1.00   34.00   E       ATOM   2216   CA   LEU   E   260   16.663   72.933   19.480   1.00   30.57   E       ATOM   2217   CB   LEU   E   260   15.896   71.677   19.886   1.00   31.05   E       ATOM   2218   CG   LEU   E   260   16.639   70.378   20.192   1.00   36.94   E       ATOM   2219   CD1   LEU   E   260   17.999   70.651   20.816   1.00   42.80   E       ATOM   2220   CD2   LEU   E   260   15.778   69.534   21.121   1.00   41.52   E       ATOM   2221   C   LEU   E   260   16.015   73.545   18.262   1.00   31.96   E       ATOM   2222   O   LEU   E   260   16.593   73.552   17.182   1.00   41.76   E       ATOM   2223   N   LYS   E   261   14.804   74.056   18.424   1.00   25.94   E       ATOM   2224   CA   LYS   E   261   14.112   74.662   17.309   1.00   28.1.9   E       ATOM   2225   CB   LYS   E   261   12.730   75.126   17.756   1.00   26.86   E       ATOM   2226   CG   LYS   E   261   11.690   74.070   17.942   1.00   24.39   E       ATOM   2227   CD   LYS   E   261   10.661   74.588   18.933   1.00   30.08   E       ATOM   2228   CE   LYS   E   261   9.261   74.465   18.427   1.00   29.30   E       ATOM   2229   NZ   LYS   E   261   9.188   75.240   17.165   1.00   41.92   E       ATOM   2230   C   LYS   E   261   14.902   75.864   16.759   1.00   32.55   E       ATOM   2231   O   LYS   E   261   15.088   76.003   15.543   1.00   38.75   E       ATOM   2232   N   ALA   E   262   15.368   76.728   17.657   1.00   31.41   E       ATOM   2233   CA   ALA   E   262   16.102   77.922   17.264   1.00   34.42   E       ATOM   2234   CB   ALA   E   262   16.422   78.744   18.487   1.00   35.30   E       ATOM   2235   C   ALA   E   262   17.376   77.655   16.474   1.00   38.56   E       ATOM   2236   O   ALA   E   262   17.635   78.311   15.473   1.00   44.36   E       ATOM   2237   N   CYS   E   263   18.175   76.693   16.917   1.00   37.93   E       ATOM   2238   CA   CYS   E   263   19.418   76.392   16.236   1.00   34.78   E       ATOM   2239   CB   CYS   E   263   20.393   75.681   17.195   1.00   40.98   E       ATOM   2240   SG   CYS   E   263   20.184   73.848   17.433   1.00   41.61   E       ATOM   2241   C   CYS   E   263   19.275   75.556   14.978   1.00   34.16   E       ATOM   2242   O   CYS   E   263   20.121   75.649   14.112   1.00   41.65   E       ATOM   2243   N   SER   E   264   18.218   74.751   14.857   1.00   33.30   E       ATOM   2244   CA   SER   E   264   18.059   73.861   13.694   1.00   31.64   E       ATOM   2245   CB   SER   E   264   16.630   73.301   13.619   1.00   25.54   E       ATOM   2246   OG   SER   E   264   15.703   74.290   13.231   1.00   44.41   E       ATOM   2247   C   SER   E   264   18.486   74.436   12.331   1.00   29.78   E       ATOM   2248   O   SER   E   264   19.457   73.954   11.772   1.00   27.24   E       ATOM   2249   N   SER   E   265   17.791   75.453   11.810   1.00   32.04   E       ATOM   2250   CA   SER   E   265   18.136   76.071   10.521   1.00   31.46   E       ATOM   2251   CB   SER   E   265   17.128   77.154   10.157   1.00   28.33   E       ATOM   2252   OG   SER   E   265   16.739   77.850   11.326   1.00   45.47   E       ATOM   2253   C   SER   E   265   19.529   76.686   10.458   1.00   32.67   E       ATOM   2254   O   SER   E   265   20.104   76.768   9.381   1.00   40.29   E       ATOM   2255   N   GLU   E   266   20.070   77.149   11.584   1.00   28.39   E       ATOM   2256   CA   GLU   E   266   21.410   77.725   11.566   1.00   25.88   E       ATOM   2257   CB   GLU   E   266   21.654   78.598   12.796   1.00   22.84   E       ATOM   2258   CG   GLU   E   266   20.888   79.877   12.778   1.00   25.52   E       ATOM   2259   CD   GLU   E   266   21.005   80.647   14.070   1.00   38.74   E       ATOM   2260   OE1   GLU   E   266   21.291   80.020   15.109   1.00   41.08   E       ATOM   2261   OE2   GLU   E   266   20.787   81.876   14.062   1.00   49.52   E       ATOM   2262   C   GLU   E   266   22.445   76.610   11.495   1.00   28.30   E       ATOM   2263   O   GLU   E   266   23.337   76.650   10.659   1.00   35.01   E       ATOM   2264   N   VAL   E   267   22.321   75.617   12.372   1.00   29.09   E       ATOM   2265   CA   VAL   E   267   23.225   74.468   12.393   1.00   31.93   E       ATOM   2266   CB   VAL   E   267   22.868   73.542   13.554   1.00   27.95   E       ATOM   2267   CG1   VAL   E   267   23.643   72.276   13.464   1.00   32.35   E       ATOM   2268   CG2   VAL   E   267   23.193   74.211   14.829   1.00   32.98   E       ATOM   2269   C   VAL   E   267   23.174   73.682   11.064   1.00   33.52   E       ATOM   2270   O   VAL   E   267   24.168   73.120   10.614   1.00   37.32   E       ATOM   2271   N   MET   E   268   22.007   73.659   10.443   1.00   30.10   E       ATOM   2272   CA   MET   E   268   21.810   72.991   9.175   1.00   31.44   E       ATOM   2273   CB   MET   E   268   20.400   73.307   8.677   1.00   33.01   E       ATOM   2274   CG   MET   E   268   19.993   72.670   7.385   1.00   40.68   E       ATOM   2275   SD   MET   E   268   18.434   73.392   6.866   1.00   50.26   E       ATOM   2276   CE   MET   E   268   17.453   72.084   7.257   1.00   59.46   E       ATOM   2277   C   MET   E   268   22.860   73.455   8.158   1.00   36.00   E       ATOM   2278   O   MET   E   268   23.431   72.634   7.435   1.00   36.45   E       ATOM   2279   N   MET   E   269   23.118   74.766   8.116   1.00   38.01   E       ATOM   2280   CA   MET   E   269   24.095   75.365   7.192   1.00   33.54   E       ATOM   2281   CB   MET   E   269   24.065   76.891   7.318   1.00   29.18   E       ATOM   2282   CG   MET   E   269   22.688   77.525   7.232   1.00   29.83   E       ATOM   2283   SD   MET   E   269   21.893   77.406   5.629   1.00   36.33   E       ATOM   2284   CE   MET   E   269   20.192   77.383   6.059   1.00   35.76   E       ATOM   2285   C   MET   E   269   25.540   74.848   7.385   1.00   32.59   E       ATOM   2286   O   MET   E   269   26.301   74.760   6.421   1.00   32.25   E       ATOM   2287   N   PHE   E   270   25.923   74.528   8.623   1.00   24.35   E       ATOM   2288   CA   PHE   E   270   27.253   73.974   8.888   1.00   28.18   E       ATOM   2289   CB   PHE   E   270   27.519   73.884   10.394   1.00   30.27   E       ATOM   2290   CG   PHE   E   270   27.954   75.173   11.033   1.00   37.91   E       ATOM   2291   CD1   PHE   E   270   28.000   75.282   12.424   1.00   34.23   E       ATOM   2292   CD2   PHE   E   270   28.322   76.275   10.264   1.00   41.91   E       ATOM   2293   CE1   PHE   E   270   28.403   76.470   13.041   1.00   38.32   E       ATOM   2294   CE2   PHE   E   270   28.727   77.473   10.871   1.00   41.49   E       ATOM   2295   CZ   PHE   E   270   28.767   77.569   12.260   1.00   41.60   E       ATOM   2296   C   PHE   E   270   27.300   72.546   8.300   1.00   31.49   E       ATOM   2297   O   PHE   E   270   28.315   72.099   7.746   1.00   25.21   E       ATOM   2298   N   ARG   E   271   26.192   71.824   8.439   1.00   29.59   E       ATOM   2299   CA   ARG   E   271   26.113   70.474   7.921   1.00   33.01   E       ATOM   2300   CB   ARG   E   271   24.797   69.844   8.329   1.00   29.47   E       ATOM   2301   CG   ARG   E   271   24.907   69.091   9.623   1.00   30.97   E       ATOM   2302   CD   ARG   E   271   23.553   66.707   10.130   1.00   28.88   E       ATOM   2303   NE   ARG   E   271   23.637   67.946   11.371   1.00   29.81   E       ATOM   2304   CZ   ARG   E   271   23.959   66.656   11.446   1.00   35.74   E       ATOM   2305   NH1   ARG   E   271   24.241   65.954   10.353   1.00   32.07   E       ATOM   2306   NH2   ARG   E   271   23.959   66.055   12.625   1.00   38.84   E       ATOM   2307   C   ARG   E   271   26.258   70.472   6.413   1.00   36.29   E       ATOM   2308   O   ARG   E   271   27.030   69.692   5.860   1.00   35.05   E       ATOM   2309   N   MET   E   272   25.503   71.351   5.762   1.00   35.74   E       ATOM   2310   CA   MET   E   272   25.549   71.495   4.321   1.00   27.95   E       ATOM   2311   CB   MET   E   272   24.566   72.554   3.856   1.00   28.37   E       ATOM   2312   CG   MET   E   272   24.877   73.091   2.477   1.00   28.17   E       ATOM   2313   SD   MET   E   272   24.337   74.810   2.240   1.00   42.72   E       ATOM   2314   CE   MET   E   272   22.938   74.576   1.238   1.00   32.88   E       ATOM   2315   C   MET   E   272   26.940   71.936   3.928   1.00   26.79   E       ATOM   2316   O   MET   E   272   27.552   71.365   3.045   1.00   23.84   E       ATOM   2317   N   ALA   E   273   27.452   72.965   4.578   1.00   23.50   E       ATOM   2318   CA   ALA   E   273   28.781   73.425   4.212   1.00   29.19   E       ATOM   2319   CB   ALA   E   273   29.236   74.533   5.153   1.00   27.08   E       ATOM   2320   C   ALA   E   273   29.807   72.287   4.185   1.00   30.27   E       ATOM   2321   O   ALA   E   273   30.670   72.264   3.321   1.00   28.90   E       ATOM   2322   N   ARG   E   274   29.694   71.326   5.102   1.00   35.93   E       ATOM   2323   CA   ARG   E   274   30.662   70.230   5.177   1.00   33.33   E       ATOM   2324   CB   ARG   E   274   30.580   69.531   6.528   1.00   33.92   E       ATOM   2325   CG   ARG   E   274   30.624   70.457   7.705   1.00   36.71   E       ATOM   2326   CD   ARG   E   274   30.645   69.665   8.982   1.00   39.66   E       ATOM   2327   NE   ARG   E   274   32.000   69.288   9.347   1.00   33.19   E       ATOM   2328   CZ   ARG   E   274   32.359   68.076   9.750   1.00   34.09   E       ATOM   2329   NH1   ARG   E   274   31.473   67.080   9.841   1.00   22.87   E       ATOM   2330   NH2   ARG   E   274   33.616   67.867   10.090   1.00   30.93   E       ATOM   2331   C   ARG   E   274   30.529   69.187   4.098   1.00   36.69   E       ATOM   2332   O   ARG   E   274   31.309   68.255   4.045   1.00   44.32   E       ATOM   2333   N   ARG   E   275   29.531   69.320   3.248   1.00   39.84   E       ATOM   2334   CA   ARG   E   275   29.343   68.368   2.169   1.00   42.70   E       ATOM   2335   CB   ARG   E   275   27.948   67.776   2.250   1.00   36.63   E       ATOM   2336   CG   ARG   E   275   27.762   67.124   3.545   1.00   42.72   E       ATOM   2337   CD   ARG   E   275   28.563   65.885   3.542   1.00   49.94   E       ATOM   2338   NE   ARG   E   275   27.721   64.813   3.043   1.00   65.23   E       ATOM   2339   CZ   ARG   E   275   28.175   63.643   2.627   1.00   67.98   E       ATOM   2340   NH1   ARG   E   275   29.487   63.402   2.644   1.00   65.23   E       ATOM   2341   NH2   ARG   E   275   27.312   62.719   2.220   1.00   66.96   E       ATOM   2342   C   ARG   E   275   29.523   69.149   0.880   1.00   47.12   E       ATOM   2343   O   ARG   E   275   29.007   68.775   −0.184   1.00   46.68   E       ATOM   2344   N   TYR   E   276   30.266   70.245   0.993   1.00   44.28   E       ATOM   2345   CA   TYR   E   276   30.499   71.090   −0.153   1.00   48.82   E       ATOM   2346   CB   TYR   E   276   30.672   72.550   0.262   1.00   47.70   E       ATOM   2347   CG   TYR   E   276   31.082   73.464   −0.881   1.00   49.48   E       ATOM   2348   CD1   TYR   E   276   30.233   73.696   −1.966   1.00   51.80   E       ATOM   2349   CE1   TYR   E   276   30.626   74.537   −3.011   1.00   53.53   E       ATOM   2350   CD2   TYR   E   276   32.330   74.094   −0.874   1.00   51.84   E       ATOM   2351   CE2   TYR   E   276   32.732   74.930   −1.908   1.00   46.44   E       ATOM   2352   CZ   TYR   E   276   31.882   75.150   −2.967   1.00   52.03   E       ATOM   2353   OH   TYR   E   276   32.292   76.002   −3.964   1.00   54.71   E       ATOM   2354   C   TYR   E   276   31.715   70.648   −0.904   1.00   50.90   E       ATOM   2355   O   TYR   E   276   32.775   70.435   −0.309   1.00   53.09   E       ATOM   2356   N   ASP   E   277   31.547   70.510   −2.214   1.00   52.50   E       ATOM   2357   CA   ASP   E   277   32.631   70.114   −3.086   1.00   60.62   E       ATOM   2358   CB   ASP   E   277   32.161   69.120   −4.146   1.00   64.18   E       ATOM   2359   CG   ASP   E   277   33.326   68.424   −4.830   1.00   66.10   E       ATOM   2360   OD1   ASP   E   277   34.220   69.108   −5.385   1.00   60.79   E       ATOM   2361   OD2   ASP   E   277   33.346   67.182   −4.799   1.00   70.36   E       ATOM   2362   C   ASP   E   277   33.175   71.341   −3.782   1.00   60.24   E       ATOM   2363   O   ASP   E   277   32.565   71.860   −4.714   1.00   60.67   E       ATOM   2364   N   ALA   E   278   34.330   71.802   −3.336   1.00   59.71   E       ATOM   2365   CA   ALA   E   278   34.922   72.979   −3.936   1.00   65.16   E       ATOM   2366   CB   ALA   E   278   36.284   73.242   −3.315   1.00   63.99   E       ATOM   2367   C   ALA   E   278   35.041   72.850   −5.458   1.00   68.11   E       ATOM   2368   O   ALA   E   278   34.638   73.744   −6.198   1.00   70.52   E       ATOM   2369   N   GLU   E   279   35.572   71.729   −5.927   1.00   71.62   E       ATOM   2370   CA   GLU   E   279   35.759   71.526   −7.362   1.00   74.80   E       ATOM   2371   CB   GLU   E   279   36.386   70.151   −7.592   1.00   83.39   E       ATOM   2372   CG   GLU   E   279   36.945   69.934   −8.991   1.00   98.26   E       ATOM   2373   CD   GLU   E   279   37.749   68.638   −9.106   1.00   104.83   E       ATOM   2374   OE1   GLU   E   279   37.181   67.553   −8.829   1.00   107.81   E       ATOM   2375   OE2   GLU   E   279   38.948   68.709   −9.473   1.00   103.41   E       ATOM   2376   C   GLU   E   279   34.487   71.679   −8.213   1.00   68.90   E       ATOM   2377   O   GLU   E   279   34.387   72.584   −9.040   1.00   68.62   E       ATOM   2378   N   THR   E   280   33.525   70.790   −7.995   1.00   62.18   E       ATOM   2379   CA   THR   E   280   32.257   70.776   −8.719   1.00   55.38   E       ATOM   2380   CB   THR   E   280   31.582   69.399   −8.584   1.00   53.11   E       ATOM   2381   OG1   THR   E   280   30.881   69.347   −7.337   1.00   59.74   E       ATOM   2382   CG2   THR   E   280   32.607   68.286   −8.571   1.00   50.32   E       ATOM   2383   C   THR   E   280   31.234   71.812   −8.220   1.00   57.07   E       ATOM   2384   O   THR   E   280   30.085   71.817   −8.686   1.00   55.58   E       ATOM   2385   N   ASP   E   281   31.643   72.671   −7.283   1.00   55.91   E       ATOM   2386   CA   ASP   E   281   30.758   73.678   −6.680   1.00   52.78   E       ATOM   2387   CB   ASP   E   281   30.663   74.932   −7.568   1.00   51.99   E       ATOM   2388   CG   ASP   E   281   29.900   76.093   −6.892   1.00   57.39   E       ATOM   2389   OD1   ASP   E   281   30.274   76.520   −5.776   1.00   54.28   E       ATOM   2390   OD2   ASP   E   281   28.924   76.595   −7.490   1.00   60.91   E       ATOM   2391   C   ASP   E   281   29.365   73.081   −6.423   1.00   52.37   E       ATOM   2392   O   ASP   E   281   28.347   73.586   −6.913   1.00   48.32   E       ATOM   2393   N   SER   E   282   29.342   71.998   −5.643   1.00   53.44   E       ATOM   2394   CA   SER   E   282   28.105   71.294   −5.303   1.00   52.09   E       ATOM   2395   CB   SER   E   282   27.960   70.070   −6.200   1.00   49.84   E       ATOM   2396   OG   SER   E   282   28.868   69.068   −5.794   1.00   52.87   E       ATOM   2397   C   SER   E   282   28.031   70.833   −3.832   1.00   50.47   E       ATOM   2398   O   SER   E   282   28.975   70.985   −3.062   1.00   50.07   E       ATOM   2399   N   ILE   E   283   26.889   70.276   −3.452   1.00   46.03   E       ATOM   2400   CA   ILE   E   283   26.705   69.760   −2.109   1.00   45.77   E       ATOM   2401   CB   ILE   E   283   25.578   70.470   −1.370   1.00   44.28   E       ATOM   2402   CG2   ILE   E   283   25.395   69.843   0.008   1.00   38.20   E       ATOM   2403   CG1   ILE   E   283   25.905   71.954   −1.258   1.00   44.46   E       ATOM   2404   CD1   ILE   E   283   24.702   72.840   −1.423   1.00   38.28   E       ATOM   2405   C   ILE   E   283   26.321   68.300   −2.291   1.00   51.61   E       ATOM   2406   O   ILE   E   283   25.237   67.987   −2.785   1.00   56.45   E       ATOM   2407   N   LEU   E   284   27.218   67.408   −1.891   1.00   48.95   E       ATOM   2408   CA   LEU   E   284   26.998   65.984   −2.029   1.00   42.78   E       ATOM   2409   CB   LEU   E   284   28.317   65.239   −1.838   1.00   46.07   E       ATOM   2410   CG   LEU   E   284   28.257   63.712   −1.744   1.00   48.34   E       ATOM   2411   CD1   LEU   E   284   27.765   63.121   −3.055   1.00   43.11   E       ATOM   2412   CD2   LEU   E   284   29.633   63.191   −1.397   1.00   44.44   E       ATOM   2413   C   LEU   E   284   25.997   65.469   −1.032   1.00   43.09   E       ATOM   2414   O   LEU   E   284   26.358   65.177   0.103   1.00   48.13   E       ATOM   2415   N   PHE   E   285   24.744   65.351   −1.452   1.00   39.45   E       ATOM   2416   CA   PHE   E   285   23.699   64.829   −0.575   1.00   39.78   E       ATOM   2417   CB   PHE   E   285   22.365   64.722   −1.329   1.00   37.53   E       ATOM   2418   CG   PHE   E   285   21.562   66.008   −1.379   1.00   36.81   E       ATOM   2419   CD1   PHE   E   285   22.191   67.260   −1.363   1.00   33.71   E       ATOM   2420   CD2   PHE   E   285   20.163   65.960   −1.500   1.00   34.34   E       ATOM   2421   CE1   PHE   E   285   21.438   68.442   −1.472   1.00   28.76   E       ATOM   2422   CE2   PHE   E   285   19.395   67.139   −1.613   1.00   29.05   E       ATOM   2423   CZ   PHE   E   285   20.038   68.380   −1.599   1.00   25.56   E       ATOM   2424   C   PHE   E   285   24.078   63.439   −0.036   1.00   46.86   E       ATOM   2425   O   PHE   E   285   25.044   62.813   −0.488   1.00   47.48   E       ATOM   2426   N   ALA   E   286   23.296   62.956   0.926   1.00   53.92   E       ATOM   2427   CA   ALA   E   286   23.515   61.648   1.547   1.00   58.44   E       ATOM   2428   CB   ALA   E   286   22.754   61.559   2.885   1.00   61.45   E       ATOM   2429   C   ALA   E   286   23.084   60.511   0.620   1.00   56.92   E       ATOM   2430   O   ALA   E   286   23.152   59.340   0.994   1.00   60.75   E       ATOM   2431   N   THR   E   287   22.618   60.870   −0.575   1.00   56.10   E       ATOM   2432   CA   THR   E   287   22.213   59.893   −1.584   1.00   54.00   E       ATOM   2433   CB   THR   E   287   20.861   60.215   −2.240   1.00   48.15   E       ATOM   2434   OG1   THR   E   287   20.899   61.526   −2.832   1.00   44.13   E       ATOM   2435   CG2   THR   E   287   19.749   60.094   −1.234   1.00   40.34   E       ATOM   2436   C   THR   E   287   23.260   59.940   −2.683   1.00   58.66   E       ATOM   2437   O   THR   E   287   22.983   59.660   −3.841   1.00   62.98   E       ATOM   2438   N   ASN   E   288   24.469   60.322   −2.315   1.00   59.74   E       ATOM   2439   CA   ASN   E   288   25.547   60.392   −3.276   1.00   61.45   E       ATOM   2440   CB   ASN   E   288   26.004   58.990   −3.609   1.00   55.68   E       ATOM   2441   CG   ASN   E   288   27.445   58.799   −3.297   1.00   58.87   E       ATOM   2442   OD1   ASN   E   288   28.305   59.406   −3.936   1.00   57.06   E       ATOM   2443   ND2   ASN   E   288   27.734   57.986   −2.287   1.00   58.96   E       ATOM   2444   C   ASN   E   288   25.253   61.169   −4.559   1.00   64.23   E       ATOM   2445   O   ASN   E   288   25.977   61.057   −5.548   1.00   62.43   E       ATOM   2446   N   GLN   E   289   24.187   61.958   −4.533   1.00   65.98   E       ATOM   2447   CA   GLN   E   289   23.807   62.783   −5.669   1.00   65.31   E       ATOM   2448   CB   GLN   E   289   22.279   62.911   −5.729   1.00   69.73   E       ATOM   2449   CG   GLN   E   289   21.509   61.909   −6.583   1.00   67.32   E       ATOM   2450   CD   GLN   E   289   19.988   62.139   −6.498   1.00   75.69   E       ATOM   2451   OE1   GLN   E   289   19.267   61.956   −7.486   1.00   73.62   E       ATOM   2452   NE2   GLN   E   289   19.500   62.536   −5.307   1.00   69.96   E       ATOM   2453   C   GLN   E   289   24.418   64.188   −5.482   1.00   62.08   E       ATOM   2454   O   GLN   E   289   24.241   64.817   −4.435   1.00   64.89   E       ATOM   2455   N   PRO   E   290   25.190   64.673   −6.463   1.00   55.91   E       ATOM   2456   CD   PRO   E   290   26.100   63.884   −7.308   1.00   54.16   E       ATOM   2457   CA   PRO   E   290   25.738   66.021   −6.256   1.00   54.20   E       ATOM   2458   CB   PRO   E   290   26.983   66.024   −7.133   1.00   46.46   E       ATOM   2459   CG   PRO   E   290   27.414   64.593   −7.085   1.00   52.27   E       ATOM   2460   C   PRO   E   290   24.724   67.087   −6.684   1.00   51.49   E       ATOM   2461   O   PRO   E   290   24.237   67.068   −7.814   1.00   55.18   E       ATOM   2462   N   TYR   E   291   24.386   68.003   −5.782   1.00   47.44   E       ATOM   2463   CA   TYR   E   291   23.434   69.053   −6.116   1.00   46.43   E       ATOM   2464   CB   TYR   E   291   22.458   69.290   −4.954   1.00   42.30   E       ATOM   2465   CG   TYR   E   291   21.343   68.263   −4.929   1.00   43.04   E       ATOM   2466   CD1   TYR   E   291   21.631   66.892   −4.802   1.00   37.33   E       ATOM   2467   CE1   TYR   E   291   20.609   65.926   −4.833   1.00   33.09   E       ATOM   2468   CD2   TYR   E   291   20.000   68.644   −5.083   1.00   37.03   E       ATOM   2469   CE2   TYR   E   291   18.971   67.681   −5.110   1.00   33.82   E       ATOM   2470   CZ   TYR   E   291   19.287   66.327   −4.986   1.00   39.67   E       ATOM   2471   OH   TYR   E   291   18.299   65.364   −5.005   1.00   48.43   E       ATOM   2472   C   TYR   E   291   24.173   70.329   −6.468   1.00   48.61   E       ATOM   2473   O   TYR   E   291   25.176   70.660   −5.837   1.00   51.77   E       ATOM   2474   N   THR   E   292   23.686   71.031   −7.489   1.00   48.55   E       ATOM   2475   CA   THR   E   292   24.291   72.282   −7.952   1.00   49.68   E       ATOM   2476   CB   THR   E   292   24.862   72.103   −9.323   1.00   53.56   E       ATOM   2477   OG1   THR   E   292   23.830   71.572   −10.167   1.00   57.88   E       ATOM   2478   CG2   THR   E   292   26.063   71.156   −9.293   1.00   45.92   E       ATOM   2479   C   THR   E   292   23.249   73.395   −8.054   1.00   52.34   E       ATOM   2480   O   THR   E   292   22.073   73.203   −7.705   1.00   53.46   E       ATOM   2481   N   ARG   E   293   23.670   74.561   −8.534   1.00   50.43   E       ATOM   2482   CA   ARG   E   293   22.726   75.667   −8.673   1.00   56.45   E       ATOM   2483   CB   ARG   E   293   23.365   76.840   −9.426   1.00   60.07   E       ATOM   2484   CG   ARG   E   293   22.452   78.055   −9.641   1.00   65.01   E       ATOM   2485   CD   ARG   E   293   23.089   79.128   −10.557   1.00   70.96   E       ATOM   2486   NE   ARG   E   293   24.363   79.662   −10.053   1.00   79.55   E       ATOM   2487   CZ   ARG   E   293   25.568   79.135   −10.291   1.00   83.43   E       ATOM   2488   NH1   ARG   E   293   25.687   78.048   −11.038   1.00   92.10   E       ATOM   2489   NH2   ARG   E   293   26.663   79.689   −9.779   1.00   83.65   E       ATOM   2490   C   ARG   E   293   21.536   75.142   −9.460   1.00   59.86   E       ATOM   2491   O   ARG   E   293   20.395   75.540   −9.225   1.00   58.30   E       ATOM   2492   N   GLU   E   294   21.808   74.231   −10.391   1.00   65.91   E       ATOM   2493   CA   GLU   E   294   20.741   73.671   −11.205   1.00   67.66   E       ATOM   2494   CB   GLU   E   294   21.299   72.777   −12.307   1.00   73.63   E       ATOM   2495   CG   GLU   E   294   20.255   72.425   −13.369   1.00   85.83   E       ATOM   2496   CD   GLU   E   294   20.698   71.291   −14.290   1.00   93.99   E       ATOM   2497   OE1   GLU   E   294   21.813   71.383   −14.859   1.00   90.76   E       ATOM   2498   OE2   GLU   E   294   19.922   70.313   −14.451   1.00   96.20   E       ATOM   2499   C   GLU   E   294   19.819   72.865   −10.317   1.00   66.48   E       ATOM   2500   O   GLU   E   294   18.653   73.228   −10.138   1.00   65.85   E       ATOM   2501   N   SER   E   295   20.357   71.783   −9.752   1.00   63.31   E       ATOM   2502   CA   SER   E   295   19.602   70.891   −8.870   1.00   56.42   E       ATOM   2503   CB   SER   E   295   20.549   70.198   −7.886   1.00   53.80   E       ATOM   2504   OG   SER   E   295   21.735   69.754   −8.527   1.00   56.54   E       ATOM   2505   C   SER   E   295   18.544   71.661   −8.093   1.00   52.70   E       ATOM   2506   O   SER   E   295   17.344   71.397   −8.227   1.00   44.29   E       ATOM   2507   N   TYR   E   296   19.002   72.630   −7.298   1.00   54.21   E       ATOM   2508   CA   TYR   E   296   18.099   73.442   −6.476   1.00   57.94   E       ATOM   2509   CB   TYR   E   296   18.857   74.356   −5.504   1.00   53.51   E       ATOM   2510   CG   TYR   E   296   19.457   73.665   −4.308   1.00   51.18   E       ATOM   2511   CD1   TYR   E   296   20.667   72.962   −4.415   1.00   49.06   E       ATOM   2512   CE1   TYR   E   296   21.254   72.369   −3.310   1.00   45.23   E       ATOM   2513   CD2   TYR   E   296   18.844   73.745   −3.063   1.00   47.02   E       ATOM   2514   CE2   TYR   E   296   19.425   73.156   −1.948   1.00   49.14   E       ATOM   2515   CZ   TYR   E   296   20.631   72.474   −2.079   1.00   47.12   E       ATOM   2516   OH   TYR   E   296   21.234   71.934   −0.968   1.00   47.53   E       ATOM   2517   C   TYR   E   296   17.170   74.315   −7.282   1.00   59.73   E       ATOM   2518   O   TYR   E   296   16.025   74.522   −6.876   1.00   60.23   E       ATOM   2519   N   THR   E   297   17.660   74.854   −8.401   1.00   59.81   E       ATOM   2520   CA   THR   E   297   16.821   75.712   −9.223   1.00   57.01   E       ATOM   2521   CB   THR   E   297   17.584   76.369   −10.373   1.00   57.33   E       ATOM   2522   OG1   THR   E   297   18.672   77.147   −9.855   1.00   60.03   E       ATOM   2523   CG2   THR   E   297   16.653   77.298   −11.131   1.00   52.97   E       ATOM   2524   C   THR   E   297   15.707   74.870   −9.798   1.00   55.04   E       ATOM   2525   O   THR   E   297   14.567   75.316   −9.848   1.00   52.58   E       ATOM   2526   N   VAL   E   298   16.043   73.643   −10.199   1.00   51.86   E       ATOM   2527   CA   VAL   E   298   15.073   72.703   −10.763   1.00   51.10   E       ATOM   2528   CB   VAL   E   298   15.741   71.362   −11.201   1.00   53.10   E       ATOM   2529   CG1   VAL   E   298   14.678   70.404   −11.677   1.00   43.54   E       ATOM   2530   CG2   VAL   E   298   16.770   71.589   −12.315   1.00   52.63   E       ATOM   2531   C   VAL   E   298   13.975   72.362   −9.759   1.00   52.09   E       ATOM   2532   O   VAL   E   298   12.823   72.199   −10.124   1.00   57.65   E       ATOM   2533   N   ALA   E   299   14.334   72.229   −8.493   1.00   55.66   E       ATOM   2534   CA   ALA   E   299   13.346   71.906   −7.473   1.00   57.89   E       ATOM   2535   CB   ALA   E   299   14.035   71.374   −6.239   1.00   65.04   E       ATOM   2536   C   ALA   E   299   12.532   73.127   −7.108   1.00   57.74   E       ATOM   2537   O   ALA   E   299   11.611   73.049   −6.300   1.00   60.91   E       ATOM   2538   N   GLY   E   300   12.893   74.258   −7.698   1.00   53.99   E       ATOM   2539   CA   GLY   E   300   12.196   75.496   −7.413   1.00   56.58   E       ATOM   2540   C   GLY   E   300   12.820   76.312   −6.293   1.00   54.28   E       ATOM   2541   O   GLY   E   300   12.166   77.180   −5.715   1.00   53.41   E       ATOM   2542   N   MET   E   301   14.087   76.048   −5.991   1.00   53.48   E       ATOM   2543   CA   MET   E   301   14.782   76.762   −4.926   1.00   57.30   E       ATOM   2544   CB   MET   E   301   15.327   75.763   −3.901   1.00   59.17   E       ATOM   2545   CG   MET   E   301   14.397   74.603   −3.580   1.00   61.86   E       ATOM   2546   SD   MET   E   301   13.307   74.869   −2.181   1.00   57.45   E       ATOM   2547   CE   MET   E   301   14.421   74.386   −0.828   1.00   68.06   E       ATOM   2548   C   MET   E   301   15.947   77.587   −5.502   1.00   61.19   E       ATOM   2549   O   MET   E   301   16.963   77.816   −4.813   1.00   61.18   E       ATOM   2550   N   GLY   E   302   15.791   78.024   −6.757   1.00   56.02   E       ATOM   2551   CA   GLY   E   302   16.819   78.805   −7.427   1.00   48.70   E       ATOM   2552   C   GLY   E   302   17.229   80.094   −6.728   1.00   48.32   E       ATOM   2553   O   GLY   E   302   18.397   80.503   −6.815   1.00   48.00   E       ATOM   2554   N   ASP   E   303   16.273   80.734   −6.048   1.00   44.95   E       ATOM   2555   CA   ASP   E   303   16.491   81.981   −5.314   1.00   47.27   E       ATOM   2556   CB   ASP   E   303   15.258   82.335   −4.511   1.00   55.66   E       ATOM   2557   CG   ASP   E   303   14.077   82.688   −5.369   1.00   72.49   E       ATOM   2558   OD1   ASP   E   303   12.947   82.695   −4.811   1.00   84.45   E       ATOM   2559   OD2   ASP   E   303   14.269   82.970   −6.577   1.00   74.53   E       ATOM   2560   C   ASP   E   303   17.634   81.883   −4.320   1.00   53.13   E       ATOM   2561   O   ASP   E   303   18.690   82.501   −4.479   1.00   58.14   E       ATOM   2562   N   THR   E   304   17.396   81.104   −3.271   1.00   55.42   E       ATOM   2563   CA   THR   E   304   18.365   80.915   −2.208   1.00   55.06   E       ATOM   2564   CB   THR   E   304   17.707   80.242   −0.980   1.00   56.60   E       ATOM   2565   OG1   THR   E   304   17.117   78.989   −1.360   1.00   62.37   E       ATOM   2566   CG2   THR   E   304   16.648   81.150   −0.407   1.00   54.69   E       ATOM   2567   C   THR   E   304   19.620   80.132   −2.574   1.00   52.08   E       ATOM   2568   O   THR   E   304   20.683   80.376   −2.000   1.00   48.46   E       ATOM   2569   N   VAL   E   305   19.516   79.213   −3.529   1.00   51.67   E       ATOM   2570   CA   VAL   E   305   20.672   78.397   −3.898   1.00   50.53   E       ATOM   2571   CB   VAL   E   305   20.544   77.751   −5.275   1.00   54.93   E       ATOM   2572   CG1   VAL   E   305   20.739   78.814   −6.381   1.00   51.08   E       ATOM   2573   CG2   VAL   E   305   21.594   76.643   −5.401   1.00   47.75   E       ATOM   2574   C   VAL   E   305   22.000   79.113   −3.918   1.00   46.99   E       ATOM   2575   O   VAL   E   305   22.971   78.599   −3.379   1.00   41.23   E       ATOM   2576   N   GLU   E   306   22.065   80.292   −4.530   1.00   46.23   E       ATOM   2577   CA   GLU   E   306   23.350   80.971   −4.595   1.00   46.84   E       ATOM   2578   CB   GLU   E   306   23.287   82.185   −5.513   1.00   51.46   E       ATOM   2579   CG   GLU   E   306   24.683   82.744   −5.884   1.00   61.37   E       ATOM   2580   CD   GLU   E   306   25.688   81.672   −6.364   1.00   65.97   E       ATOM   2581   OE1   GLU   E   306   25.336   80.876   −7.266   1.00   60.45   E       ATOM   2582   OE2   GLU   E   306   26.838   81.639   −5.851   1.00   61.39   E       ATOM   2583   C   GLU   E   306   23.901   81.363   −3.238   1.00   44.73   E       ATOM   2584   O   GLU   E   306   25.074   81.124   −2.965   1.00   40.70   E       ATOM   2585   N   ASP   E   307   23.059   81.953   −2.391   1.00   44.04   E       ATOM   2586   CA   ASP   E   307   23.477   82.340   −1.045   1.00   41.14   E       ATOM   2587   CB   ASP   E   307   22.305   82.889   −0.246   1.00   52.01   E       ATOM   2588   CG   ASP   E   307   21.757   84.161   −0.827   1.00   60.75   E       ATOM   2589   OD1   ASP   E   307   20.814   84.069   −1.652   1.00   62.82   E       ATOM   2590   OD2   ASP   E   307   22.283   85.244   −0.464   1.00   64.89   E       ATOM   2591   C   ASP   E   307   24.043   81.145   −0.297   1.00   36.51   E       ATOM   2592   O   ASP   E   307   25.036   81.263   0.414   1.00   33.26   E       ATOM   2593   N   LEU   E   308   23.386   80.001   −0.445   1.00   32.45   E       ATOM   2594   CA   LEU   E   308   23.827   78.770   0.185   1.00   34.12   E       ATOM   2595   CB   LEU   E   308   22.864   77.639   −0.142   1.00   27.15   E       ATOM   2596   CG   LEU   E   308   21.432   77.848   0.321   1.00   28.39   E       ATOM   2597   CD1   LEU   E   308   20.546   76.727   −0.217   1.00   28.97   E       ATOM   2598   CD2   LEU   E   308   21.406   77.907   1.828   1.00   19.33   E       ATOM   2599   C   LEU   E   308   25.211   78.400   −0.328   1.00   39.79   E       ATOM   2600   O   LEU   E   308   26.143   78.191   0.452   1.00   45.71   E       ATOM   2601   N   LEU   E   309   25.346   78.311   −1.644   1.00   38.81   E       ATOM   2602   CA   LEU   E   309   26.628   77.955   −2.226   1.00   42.34   E       ATOM   2603   CB   LEU   E   309   26.543   77.950   −3.763   1.00   38.54   E       ATOM   2604   CG   LEU   E   309   26.325   76.618   −4.504   1.00   33.64   E       ATOM   2605   CD1   LEU   E   309   26.794   75.427   −3.659   1.00   32.06   E       ATOM   2606   CD2   LEU   E   309   24.858   76.473   −4.851   1.00   27.68   E       ATOM   2607   C   LEU   E   309   27.749   78.896   −1.767   1.00   43.90   E       ATOM   2608   O   LEU   E   309   28.866   78.456   −1.467   1.00   42.98   E       ATOM   2609   N   ARG   E   310   27.440   80.187   −1.711   1.00   42.19   E       ATOM   2610   CA   ARG   E   310   28.412   81.183   −1.307   1.00   40.66   E       ATOM   2611   CB   ARG   E   310   27.777   82.570   −1.380   1.00   40.07   E       ATOM   2612   CG   ARG   E   310   28.591   83.705   −0.806   1.00   44.89   E       ATOM   2613   CD   ARG   E   310   27.831   85.033   −0.902   1.00   58.85   E       ATOM   2614   NE   ARG   E   310   27.653   85.436   −2.295   1.00   69.19   E       ATOM   2615   CZ   ARG   E   310   26.649   85.051   −3.080   1.00   75.43   E       ATOM   2616   NH1   ARG   E   310   25.700   84.251   −2.610   1.00   81.52   E       ATOM   2617   NH2   ARG   E   310   26.609   85.445   −4.350   1.00   74.42   E       ATOM   2618   C   ARG   E   310   28.919   80.888   0.095   1.00   42.89   E       ATOM   2619   O   ARG   E   310   30.127   80.940   0.354   1.00   42.22   E       ATOM   2620   N   PHE   E   311   28.002   80.558   1.000   1.00   43.01   E       ATOM   2621   CA   PHE   E   311   28.385   80.257   2.373   1.00   40.21   E       ATOM   2622   CB   PHE   E   311   27.172   79.873   3.207   1.00   36.06   E       ATOM   2623   CG   PHE   E   311   27.501   79.624   4.641   1.00   36.68   E       ATOM   2624   CD1   PHE   E   311   27.874   80.672   5.469   1.00   36.95   E       ATOM   2625   CD2   PHE   E   311   27.498   78.337   5.152   1.00   35.64   E       ATOM   2626   CE1   PHE   E   311   28.232   80.435   6.780   1.00   41.04   E       ATOM   2627   CE2   PHE   E   311   27.854   78.100   6.457   1.00   37.74   E       ATOM   2628   CZ   PHE   E   311   28.226   79.152   7.273   1.00   38.51   E       ATOM   2629   C   PHE   E   311   29.369   79.103   2.392   1.00   46.01   E       ATOM   2630   O   PHE   E   311   30.416   79.169   3.051   1.00   49.74   E       ATOM   2631   N   CYS   E   312   29.004   78.040   1.674   1.00   42.54   E       ATOM   2632   CA   CYS   E   312   29.825   76.845   1.564   1.00   37.36   E       ATOM   2633   CB   CYS   E   312   29.220   75.874   0.556   1.00   38.37   E       ATOM   2634   SG   CYS   E   312   27.662   75.132   1.048   1.00   39.43   E       ATOM   2635   C   CYS   E   312   31.213   77.229   1.106   1.00   40.16   E       ATOM   2636   O   CYS   E   312   32.201   76.732   1.636   1.00   46.13   E       ATOM   2637   N   ARG   E   313   31.285   78.112   0.112   1.00   44.10   E       ATOM   2638   CA   ARG   E   313   32.567   78.561   −0.423   1.00   42.60   E       ATOM   2639   CB   ARG   E   313   32.372   79.439   −1.652   1.00   42.81   E       ATOM   2640   CG   ARG   E   313   32.170   78.695   −2.958   1.00   47.52   E       ATOM   2641   CD   ARG   E   313   32.289   79.646   −4.137   1.00   42.88   E       ATOM   2642   NE   ARG   E   313   31.119   80.498   −4.330   1.00   40.06   E       ATOM   2643   CZ   ARG   E   313   29.954   80.041   −4.775   1.00   50.01   E       ATOM   2644   NH1   ARG   E   313   29.823   78.742   −5.055   1.00   45.76   E       ATOM   2645   NH2   ARG   E   313   28.938   80.879   −4.977   1.00   43.24   E       ATOM   2646   C   ARG   E   313   33.361   79.340   0.594   1.00   44.06   E       ATOM   2647   O   ARG   E   313   34.555   79.105   0.743   1.00   40.75   E       ATOM   2648   N   HIS   E   314   32.707   80.279   1.281   1.00   45.97   E       ATOM   2649   CA   HIS   E   314   33.386   81.087   2.285   1.00   47.88   E       ATOM   2650   CB   HIS   E   314   32.449   82.171   2.838   1.00   58.09   E       ATOM   2651   CG   HIS   E   314   33.004   82.914   4.021   1.00   69.52   E       ATOM   2652   CD2   HIS   E   314   32.496   83.130   5.258   1.00   72.88   E       ATOM   2653   ND1   HIS   E   314   34.240   83.533   4.006   1.00   78.21   E       ATOM   2654   CE1   HIS   E   314   34.467   84.093   5.180   1.00   75.35   E       ATOM   2655   NE2   HIS   E   314   33.425   83.864   5.960   1.00   76.13   E       ATOM   2656   C   HIS   E   314   33.917   80.210   3.415   1.00   44.87   E       ATOM   2657   O   HIS   E   314   35.002   80.461   3.949   1.00   42.96   E       ATOM   2658   N   MET   E   315   33.171   79.169   3.769   1.00   41.07   E       ATOM   2659   CA   MET   E   315   33.608   78.274   4.843   1.00   46.97   E       ATOM   2660   CB   MET   E   315   32.445   77.374   5.283   1.00   45.05   E       ATOM   2661   CG   MET   E   315   31.303   78.114   5.987   1.00   44.79   E       ATOM   2662   SD   MET   E   315   31.793   78.853   7.570   1.00   49.50   E       ATOM   2663   CE   MET   E   315   32.000   77.438   8.591   1.00   41.10   E       ATOM   2664   C   MET   E   315   34.821   77.428   4.417   1.00   48.06   E       ATOM   2665   O   MET   E   315   35.790   77.237   5.164   1.00   49.75   E       ATOM   2666   N   CYS   E   316   34.755   76.923   3.199   1.00   50.73   E       ATOM   2667   CA   CYS   E   316   35.832   76.124   2.636   1.00   47.71   E       ATOM   2668   CB   CYS   E   316   35.422   75.668   1.244   1.00   49.10   E       ATOM   2669   SG   CYS   E   316   36.479   74.437   0.585   1.00   57.98   E       ATOM   2670   C   CYS   E   316   37.110   76.962   2.556   1.00   44.65   E       ATOM   2671   O   CYS   E   316   38.211   76.458   2.708   1.00   39.70   E       ATOM   2672   N   ALA   E   317   36.935   78.259   2.315   1.00   47.36   E       ATOM   2673   CA   ALA   E   317   38.031   79.214   2.201   1.00   39.33   E       ATOM   2674   CB   ALA   E   317   37.510   80.492   1.694   1.00   31.61   E       ATOM   2675   C   ALA   E   317   38.727   79.445   3.520   1.00   39.45   E       ATOM   2676   O   ALA   E   317   39.917   79.736   3.542   1.00   40.04   E       ATOM   2677   N   MET   E   318   37.973   79.326   4.613   1.00   40.99   E       ATOM   2678   CA   MET   E   318   38.506   79.499   5.964   1.00   38.70   E       ATOM   2679   CB   MET   E   318   37.397   79.880   6.924   1.00   35.12   E       ATOM   2680   CG   MET   E   318   36.922   81.282   6.742   1.00   42.22   E       ATOM   2681   SD   MET   E   318   36.025   81.798   8.198   1.00   49.96   E       ATOM   2682   CE   MET   E   318   34.367   81.205   7.716   1.00   55.22   E       ATOM   2683   C   MET   E   318   39.195   78.252   6.495   1.00   38.83   E       ATOM   2684   O   MET   E   318   39.875   78.295   7.525   1.00   38.43   E       ATOM   2685   N   LYS   E   319   39.001   77.139   5.798   1.00   39.64   E       ATOM   2686   CA   LYS   E   319   39.611   75.891   6.201   1.00   39.52   E       ATOM   2687   CB   LYS   E   319   41.122   76.011   6.052   1.00   36.73   E       ATOM   2688   CG   LYS   E   319   41.584   76.488   4.685   1.00   38.39   E       ATOM   2689   CD   LYS   E   319   43.119   76.570   4.618   1.00   44.38   E       ATOM   2690   CE   LYS   E   319   43.651   77.125   3.265   1.00   53.58   E       ATOM   2691   NZ   LYS   E   319   43.620   76.171   2.090   1.00   49.79   E       ATOM   2692   C   LYS   E   319   39.231   75.592   7.657   1.00   42.19   E       ATOM   2693   O   LYS   E   319   40.092   75.412   8.519   1.00   41.47   E       ATOM   2694   N   VAL   E   320   37.929   75.558   7.921   1.00   42.30   E       ATOM   2695   CA   VAL   E   320   37.404   75.293   9.257   1.00   39.90   E       ATOM   2696   CB   VAL   E   320   35.907   75.750   9.331   1.00   39.08   E       ATOM   2697   CG1   VAL   E   320   35.325   75.516   10.715   1.00   28.09   E       ATOM   2698   CG2   VAL   E   320   35.805   77.219   8.948   1.00   37.65   E       ATOM   2699   C   VAL   E   320   37.517   73.792   9.486   1.00   38.14   E       ATOM   2700   O   VAL   E   320   36.966   73.018   8.720   1.00   40.61   E       ATOM   2701   N   ASP   E   321   38.228   73.357   10.520   1.00   39.20   E       ATOM   2702   CA   ASP   E   321   38.349   71.916   10.739   1.00   38.88   E       ATOM   2703   CB   ASP   E   321   39.713   71.574   11.312   1.00   33.31   E       ATOM   2704   CG   ASP   E   321   39.871   72.017   12.743   1.00   41.47   E       ATOM   2705   OD1   ASP   E   321   40.985   72.438   13.105   1.00   41.07   E       ATOM   2706   OD2   ASP   E   321   38.897   71.929   13.515   1.00   48.12   E       ATOM   2707   C   ASP   E   321   37.262   71.351   11.641   1.00   43.03   E       ATOM   2708   O   ASP   E   321   36.427   72.083   12.166   1.00   50.90   E       ATOM   2709   N   ASN   E   322   37.288   70.043   11.841   1.00   40.47   E       ATOM   2710   CA   ASN   E   322   36.284   69.382   12.656   1.00   39.16   E       ATOM   2711   CB   ASN   E   322   36.584   67.899   12.740   1.00   42.19   E       ATOM   2712   CG   ASN   E   322   36.518   67.246   11.399   1.00   37.40   E       ATOM   2713   OD1   ASN   E   322   36.073   67.861   10.434   1.00   39.07   E       ATOM   2714   ND2   ASN   E   322   36.958   66.007   11.318   1.00   34.55   E       ATOM   2715   C   ASN   E   322   36.044   69.913   14.038   1.00   42.55   E       ATOM   2716   O   ASN   E   322   34.891   70.145   14.410   1.00   45.98   E       ATOM   2717   N   ALA   E   323   37.116   70.090   14.804   1.00   41.77   E       ATOM   2718   CA   ALA   E   323   36.995   70.611   16.165   1.00   39.19   E       ATOM   2719   CB   ALA   E   323   38.353   70.739   16.788   1.00   37.72   E       ATOM   2720   C   ALA   E   323   36.312   71.975   16.150   1.00   41.04   E       ATOM   2721   O   ALA   E   323   35.353   72.233   16.904   1.00   34.72   E       ATOM   2722   N   GLU   E   324   36.811   72.847   15.278   1.00   36.39   E       ATOM   2723   CA   GLU   E   324   36.262   74.186   15.158   1.00   37.10   E       ATOM   2724   CB   GLU   E   324   37.103   74.998   14.173   1.00   42.36   E       ATOM   2725   CG   GLU   E   324   38.579   74.983   14.512   1.00   43.03   E       ATOM   2726   CD   GLU   E   324   39.385   75.848   13.603   1.00   44.29   E       ATOM   2727   OE1   GLU   E   324   39.213   75.716   12.376   1.00   45.28   E       ATOM   2728   OE2   GLU   E   324   40.195   76.651   14.116   1.00   49.48   E       ATOM   2729   C   GLU   E   324   34.812   74.089   14.703   1.00   37.19   E       ATOM   2730   O   GLU   E   324   33.932   74.790   15.219   1.00   36.60   E       ATOM   2731   N   TYR   E   325   34.555   73.212   13.741   1.00   35.43   E       ATOM   2732   CA   TYR   E   325   33.195   73.050   13.280   1.00   33.83   E       ATOM   2733   CB   TYR   E   325   33.112   72.009   12.177   1.00   28.46   E       ATOM   2734   CG   TYR   E   325   32.815   72.613   10.823   1.00   32.50   E       ATOM   2735   CD1   TYR   E   325   31.586   73.223   10.553   1.00   30.26   E       ATOM   2736   CE1   TYR   E   325   31.326   73.781   9.291   1.00   33.88   E       ATOM   2737   CD2   TYR   E   325   33.766   72.577   9.811   1.00   29.44   E       ATOM   2738   CE2   TYR   E   325   33.517   73.127   8.570   1.00   29.18   E       ATOM   2739   CZ   TYR   E   325   32.309   73.728   8.301   1.00   31.70   E       ATOM   2740   OH   TYR   E   325   32.119   74.268   7.039   1.00   33.30   E       ATOM   2741   C   TYR   E   325   32.337   72.631   14.454   1.00   35.84   E       ATOM   2742   O   TYR   E   325   31.389   73.324   14.802   1.00   38.35   E       ATOM   2743   N   ALA   E   326   32.682   71.520   15.093   1.00   31.20   E       ATOM   2744   CA   ALA   E   326   31.881   71.052   16.207   1.00   30.02   E       ATOM   2745   CB   ALA   E   326   32.488   69.798   16.786   1.00   23.95   E       ATOM   2746   C   ALA   E   326   31.696   72.116   17.291   1.00   33.08   E       ATOM   2747   O   ALA   E   326   30.563   72.490   17.625   1.00   32.67   E       ATOM   2748   N   LEU   E   327   32.795   72.626   17.834   1.00   27.98   E       ATOM   2749   CA   LEU   E   327   32.686   73.626   18.894   1.00   30.89   E       ATOM   2750   CB   LEU   E   327   34.055   74.198   19.234   1.00   26.93   E       ATOM   2751   CG   LEU   E   327   34.937   73.266   20.036   1.00   24.04   E       ATOM   2752   CD1   LEU   E   327   36.389   73.677   19.914   1.00   15.58   E       ATOM   2753   CD2   LEU   E   327   34.428   73.266   21.464   1.00   20.01   E       ATOM   2754   C   LEU   E   327   31.776   74.757   18.481   1.00   35.13   E       ATOM   2755   O   LEU   E   327   30.962   75.242   19.267   1.00   39.12   E       ATOM   2756   N   LEU   E   328   31.923   75.170   17.231   1.00   33.20   E       ATOM   2757   CA   LEU   E   328   31.139   76.265   16.709   1.00   35.88   E       ATOM   2758   CB   LEU   E   328   31.634   76.617   15.298   1.00   36.15   E       ATOM   2759   CG   LEU   E   328   31.793   78.091   14.915   1.00   28.33   E       ATOM   2760   CD1   LEU   E   328   32.335   78.935   16.063   1.00   34.96   E       ATOM   2761   CD2   LEU   E   328   32.724   78.144   13.779   1.00   21.29   E       ATOM   2762   C   LEU   E   328   29.654   75.918   16.718   1.00   35.44   E       ATOM   2763   O   LEU   E   328   28.844   76.687   17.234   1.00   32.20   E       ATOM   2764   N   THR   E   329   29.290   74.758   16.179   1.00   33.93   E       ATOM   2765   CA   THR   E   329   27.882   74.389   16.167   1.00   32.32   E       ATOM   2766   CB   THR   E   329   27.595   73.010   15.454   1.00   27.74   E       ATOM   2767   OG1   THR   E   329   27.341   72.023   16.449   1.00   29.80   E       ATOM   2768   CG2   THR   E   329   28.756   72.546   14.579   1.00   17.77   E       ATOM   2769   C   THR   E   329   27.350   74.328   17.609   1.00   33.95   E       ATOM   2770   O   THR   E   329   26.179   74.646   17.848   1.00   33.69   E       ATOM   2771   N   ALA   E   330   28.199   73.937   18.567   1.00   31.78   E       ATOM   2772   CA   ALA   E   330   27.769   73.861   19.969   1.00   33.28   E       ATOM   2773   CB   ALA   E   330   28.817   73.142   20.814   1.00   31.03   E       ATOM   2774   C   ALA   E   330   27.487   75.258   20.547   1.00   35.12   E       ATOM   2775   O   ALA   E   330   26.546   75.438   21.330   1.00   28.86   E       ATOM   2776   N   ILE   E   331   28.306   76.240   20.161   1.00   32.84   E       ATOM   2777   CA   ILE   E   331   28.134   77.623   20.611   1.00   31.63   E       ATOM   2778   CB   ILE   E   331   29.307   78.508   20.087   1.00   28.80   E       ATOM   2779   CG2   ILE   E   331   29.148   79.977   20.529   1.00   14.86   E       ATOM   2780   CG1   ILE   E   331   30.622   77.921   20.594   1.00   22.26   E       ATOM   2781   CD1   ILE   E   331   31.815   78.798   20.411   1.00   22.39   E       ATOM   2782   C   ILE   E   331   26.778   78.152   20.096   1.00   35.90   E       ATOM   2783   O   ILE   E   331   26.099   78.948   20.763   1.00   38.07   E       ATOM   2784   N   VAL   E   332   26.383   77.684   18.911   1.00   36.30   E       ATOM   2785   CA   VAL   E   332   25.123   78.079   18.280   1.00   32.82   E       ATOM   2786   CB   VAL   E   332   25.033   77.598   16.807   1.00   33.28   E       ATOM   2787   CG1   VAL   E   332   23.624   77.856   16.253   1.00   20.84   E       ATOM   2788   CG2   VAL   E   332   26.093   78.298   15.956   1.00   27.39   E       ATOM   2789   C   VAL   E   332   23.951   77.474   19.005   1.00   30.96   E       ATOM   2790   O   VAL   E   332   22.933   78.125   19.224   1.00   38.03   E       ATOM   2791   N   ILE   E   333   24.095   76.208   19.358   1.00   32.15   E       ATOM   2792   CA   ILE   E   333   23.033   75.496   20.042   1.00   33.48   E       ATOM   2793   CB   ILE   E   333   23.396   73.996   20.172   1.00   24.45   E       ATOM   2794   CG2   ILE   E   333   22.414   73.288   21.054   1.00   19.03   E       ATOM   2795   CG1   ILE   E   333   23.403   73.358   18.789   1.00   20.06   E       ATOM   2796   CD1   ILE   E   333   23.824   71.910   18.787   1.00   19.42   E       ATOM   2797   C   ILE   E   333   22.716   76.125   21.404   1.00   33.41   E       ATOM   2798   O   ILE   E   333   21.562   76.100   21.847   1.00   35.50   E       ATOM   2799   N   PHE   E   334   23.732   76.715   22.033   1.00   28.65   E       ATOM   2800   CA   PHE   E   334   23.593   77.355   23.343   1.00   33.67   E       ATOM   2801   CB   PHE   E   334   24.717   76.917   24.278   1.00   32.69   E       ATOM   2802   CG   PHE   E   334   24.639   75.490   24.672   1.00   36.29   E       ATOM   2803   CD1   PHE   E   334   23.507   75.003   25.321   1.00   32.87   E       ATOM   2804   CD2   PHE   E   334   25.686   74.620   24.382   1.00   36.20   E       ATOM   2805   CE1   PHE   E   334   23.409   73.675   25.675   1.00   31.24   E       ATOM   2806   CE2   PHE   E   334   25.598   73.285   24.732   1.00   38.46   E       ATOM   2807   CZ   PHE   E   334   24.450   72.811   25.383   1.00   38.10   E       ATOM   2808   C   PHE   E   334   23.571   78.884   23.290   1.00   39.11   E       ATOM   2809   O   PHE   E   334   24.192   79.576   24.126   1.00   39.08   E       ATOM   2810   N   SER   E   335   22.847   79.410   22.315   1.00   33.86   E       ATOM   2811   CA   SER   E   335   22.742   80.837   22.167   1.00   35.91   E       ATOM   2812   CB   SER   E   335   22.707   81.171   20.689   1.00   32.42   E       ATOM   2813   OG   SER   E   335   23.897   80.693   20.096   1.00   29.88   E       ATOM   2814   C   SER   E   335   21.507   81.354   22.887   1.00   39.38   E       ATOM   2815   O   SER   E   335   20.399   81.149   22.430   1.00   45.11   E       ATOM   2816   N   GLU   E   336   21.707   82.006   24.030   1.00   43.04   E       ATOM   2817   CA   GLU   E   336   20.597   82.545   24.801   1.00   44.80   E       ATOM   2818   CB   GLU   E   336   21.094   83.297   26.021   1.00   49.84   E       ATOM   2819   CG   GLU   E   336   19.978   84.039   26.739   1.00   64.36   E       ATOM   2820   CD   GLU   E   336   20.432   84.685   28.046   1.00   75.48   E       ATOM   2821   OE1   GLU   E   336   19.627   85.429   28.668   1.00   70.40   E       ATOM   2822   OE2   GLU   E   336   21.594   84.443   28.451   1.00   76.31   E       ATOM   2823   C   GLU   E   336   19.723   83.481   23.991   1.00   47.53   E       ATOM   2824   O   GLU   E   336   20.094   84.642   23.735   1.00   49.22   E       ATOM   2825   N   ARG   E   337   18.559   82.953   23.608   1.00   47.43   E       ATOM   2826   CA   ARG   E   337   17.541   83.665   22.845   1.00   41.04   E       ATOM   2827   CB   ARG   E   337   16.787   82.688   21.951   1.00   38.57   E       ATOM   2828   CG   ARG   E   337   17.636   81.673   21.234   1.00   41.45   E       ATOM   2829   CD   ARG   E   337   17.898   82.058   19.792   1.00   38.02   E       ATOM   2830   NE   ARG   E   337   18.855   81.138   19.188   1.00   45.29   E       ATOM   2831   CZ   ARG   E   337   19.432   81.322   18.005   1.00   46.67   E       ATOM   2832   NH1   ARG   E   337   19.142   82.405   17.284   1.00   28.51   E       ATOM   2833   NH2   ARG   E   337   20.308   80.422   17.555   1.00   41.41   E       ATOM   2834   C   ARG   E   337   16.564   84.212   23.894   1.00   43.46   E       ATOM   2835   O   ARG   E   337   16.553   83.743   25.039   1.00   41.16   E       ATOM   2836   N   PRO   E   338   15.711   85.191   23.516   1.00   47.00   E       ATOM   2837   CD   PRO   E   338   15.414   85.666   22.153   1.00   43.34   E       ATOM   2838   CA   PRO   E   338   14.749   85.753   24.479   1.00   42.51   E       ATOM   2839   CB   PRO   E   338   14.112   86.905   23.714   1.00   37.53   E       ATOM   2840   CG   PRO   E   338   14.912   87.033   22.417   1.00   38.31   E       ATOM   2841   C   PRO   E   338   13.743   84.665   24.730   1.00   41.36   E       ATOM   2842   O   PRO   E   338   13.797   83.642   24.058   1.00   50.86   E       ATOM   2843   N   SER   E   339   12.830   84.846   25.674   1.00   43.71   E       ATOM   2844   CA   SER   E   339   11.810   83.807   25.910   1.00   51.70   E       ATOM   2845   CB   SER   E   339   11.104   83.440   24.608   1.00   53.32   E       ATOM   2846   OG   SER   E   339   11.824   82.413   23.939   1.00   58.35   E       ATOM   2847   C   SER   E   339   12.292   82.493   26.545   1.00   52.52   E       ATOM   2848   O   SER   E   339   11.477   81.726   27.052   1.00   55.04   E       ATOM   2849   N   LEU   E   340   13.585   82.189   26.461   1.00   50.66   E       ATOM   2850   CA   LEU   E   340   14.091   80.998   27.121   1.00   46.28   E       ATOM   2851   CB   LEU   E   340   15.599   80.918   26.997   1.00   40.25   E       ATOM   2852   CG   LEU   E   340   16.288   80.182   25.872   1.00   38.30   E       ATOM   2853   CD1   LEU   E   340   17.763   80.548   25.914   1.00   44.30   E       ATOM   2854   CD2   LEU   E   340   16.109   78.696   26.029   1.00   37.84   E       ATOM   2855   C   LEU   E   340   13.768   81.273   28.591   1.00   50.48   E       ATOM   2856   O   LEU   E   340   13.817   82.424   29.027   1.00   51.67   E       ATOM   2857   N   SER   E   341   13.447   80.240   29.361   1.00   50.33   E       ATOM   2858   CA   SER   E   341   13.149   80.444   30.768   1.00   46.30   E       ATOM   2859   CB   SER   E   341   12.533   79.209   31.375   1.00   44.20   E       ATOM   2860   OG   SER   E   341   12.684   79.286   32.778   1.00   52.17   E       ATOM   2861   C   SER   E   341   14.395   80.782   31.570   1.00   49.57   E       ATOM   2862   O   SER   E   341   14.440   81.792   32.264   1.00   51.49   E       ATOM   2863   N   GLU   E   342   15.410   79.930   31.492   1.00   49.30   E       ATOM   2864   CA   GLU   E   342   16.631   80.193   32.230   1.00   46.56   E       ATOM   2865   CB   GLU   E   342   17.078   78.970   32.996   1.00   54.05   E       ATOM   2866   CG   GLU   E   342   16.055   78.360   33.887   1.00   60.75   E       ATOM   2867   CD   GLU   E   342   16.557   77.045   34.412   1.00   67.98   E       ATOM   2868   OE1   GLU   E   342   16.856   76.146   33.578   1.00   72.09   E       ATOM   2869   OE2   GLU   E   342   16.666   76.924   35.650   1.00   69.64   E       ATOM   2870   C   GLU   E   342   17.759   80.602   31.316   1.00   42.61   E       ATOM   2871   O   GLU   E   342   18.784   79.929   31.245   1.00   37.29   E       ATOM   2872   N   GLY   E   343   17.579   81.717   30.627   1.00   40.60   E       ATOM   2873   CA   GLY   E   343   18.623   82.191   29.743   1.00   43.46   E       ATOM   2874   C   GLY   E   343   20.031   82.226   30.335   1.00   39.18   E       ATOM   2875   O   GLY   E   343   20.987   81.757   29.690   1.00   37.87   E       ATOM   2876   N   TRP   E   344   20.162   82.782   31.541   1.00   35.69   E       ATOM   2877   CA   TRP   E   344   21.455   82.894   32.217   1.00   41.77   E       ATOM   2878   CB   TRP   E   344   21.261   83.417   33.644   1.00   46.03   E       ATOM   2879   CG   TRP   E   344   20.536   82.476   34.537   1.00   51.15   E       ATOM   2880   CD2   TRP   E   344   21.122   81.419   35.301   1.00   58.71   E       ATOM   2881   CE2   TRP   E   344   20.058   80.672   35.862   1.00   56.54   E       ATOM   2882   CE3   TRP   E   344   22.448   81.027   35.565   1.00   57.83   E       ATOM   2883   CD1   TRP   E   344   19.182   82.341   34.669   1.00   50.37   E       ATOM   2884   NE1   TRP   E   344   18.887   81.258   35.459   1.00   52.67   E       ATOM   2885   CZ2   TRP   E   344   20.275   79.540   36.657   1.00   56.40   E       ATOM   2886   CZ3   TRP   E   344   22.665   79.897   36.356   1.00   60.15   E       ATOM   2887   CH2   TRP   E   344   21.581   79.169   36.896   1.00   58.16   E       ATOM   2888   C   TRP   E   344   22.235   81.576   32.265   1.00   44.23   E       ATOM   2889   O   TRP   E   344   23.474   81.563   32.209   1.00   44.69   E       ATOM   2890   N   LYS   E   345   21.504   80.469   32.360   1.00   44.02   E       ATOM   2891   CA   LYS   E   345   22.124   79.160   32.429   1.00   47.06   E       ATOM   2892   CB   LYS   E   345   21.127   78.153   33.009   1.00   46.11   E       ATOM   2893   CG   LYS   E   345   21.768   76.843   33.407   1.00   48.67   E       ATOM   2894   CD   LYS   E   345   20.744   75.779   33.786   1.00   58.19   E       ATOM   2895   CE   LYS   E   345   20.045   76.082   35.102   1.00   65.45   E       ATOM   2896   NZ   LYS   E   345   19.499   74.824   35.683   1.00   61.68   E       ATOM   2897   C   LYS   E   345   22.646   78.699   31.057   1.00   51.21   E       ATOM   2898   O   LYS   E   345   23.750   78.140   30.976   1.00   51.22   E       ATOM   2899   N   VAL   E   346   21.867   78.926   29.989   1.00   47.18   E       ATOM   2900   CA   VAL   E   346   22.306   78.552   28.641   1.00   42.50   E       ATOM   2901   CB   VAL   E   346   21.234   78.869   27.546   1.00   37.11   E       ATOM   2902   CG1   VAL   E   346   21.778   78.546   26.199   1.00   34.24   E       ATOM   2903   CG2   VAL   E   346   19.997   78.030   27.726   1.00   35.13   E       ATOM   2904   C   VAL   E   346   23.557   79.390   28.359   1.00   41.56   E       ATOM   2905   O   VAL   E   346   24.545   78.913   27.789   1.00   43.97   E       ATOM   2906   N   GLU   E   347   23.513   80.639   28.798   1.00   38.53   E       ATOM   2907   CA   GLU   E   347   24.616   81.568   28.607   1.00   41.57   E       ATOM   2908   CB   GLU   E   347   24.278   82.881   29.280   1.00   39.84   E       ATOM   2909   CG   GLU   E   347   25.069   84.033   28.792   1.00   49.68   E       ATOM   2910   CD   GLU   E   347   24.494   85.334   29.295   1.00   68.89   E       ATOM   2911   OE1   GLU   E   347   25.028   85.866   30.297   1.00   81.64   E       ATOM   2912   OE2   GLU   E   347   23.499   85.819   28.697   1.00   61.93   E       ATOM   2913   C   GLU   E   347   25.919   81.047   29.176   1.00   43.24   E       ATOM   2914   O   GLU   E   347   26.955   81.047   28.512   1.00   41.17   E       ATOM   2915   N   LYS   E   348   25.844   80.610   30.427   1.00   46.94   E       ATOM   2916   CA   LYS   E   348   26.983   80.085   31.171   1.00   47.97   E       ATOM   2917   CB   LYS   E   348   26.526   79.869   32.613   1.00   52.33   E       ATOM   2918   CG   LYS   E   348   27.545   79.271   33.568   1.00   61.82   E       ATOM   2919   CD   LYS   E   348   26.881   79.124   34.941   1.00   71.46   E       ATOM   2920   CE   LYS   E   348   27.773   78.466   35.978   1.00   75.28   E       ATOM   2921   NZ   LYS   E   348   27.124   78.532   37.323   1.00   75.30   E       ATOM   2922   C   LYS   E   348   27.573   78.795   30.570   1.00   46.87   E       ATOM   2923   O   LYS   E   348   28.794   78.596   30.575   1.00   42.83   E       ATOM   2924   N   ILE   E   349   26.692   77.928   30.065   1.00   43.26   E       ATOM   2925   CA   ILE   E   349   27.082   76.663   29.445   1.00   40.07   E       ATOM   2926   CB   ILE   E   349   25.845   75.789   29.149   1.00   38.98   E       ATOM   2927   CG2   ILE   E   349   26.245   74.532   28.385   1.00   29.15   E       ATOM   2928   CG1   ILE   E   349   25.150   75.440   30.462   1.00   35.25   E       ATOM   2929   CD1   ILE   E   349   23.920   74.598   30.307   1.00   32.85   E       ATOM   2930   C   ILE   E   349   27.807   76.950   28.138   1.00   43.83   E       ATOM   2931   O   ILE   E   349   28.832   76.337   27.818   1.00   42.49   E       ATOM   2932   N   GLN   E   350   27.262   77.888   27.375   1.00   38.97   E       ATOM   2933   CA   GLN   E   350   27.886   78.253   26.126   1.00   39.89   E       ATOM   2934   CB   GLN   E   350   27.056   79.306   25.410   1.00   37.99   E       ATOM   2935   CG   GLN   E   350   27.766   79.885   24.209   1.00   34.17   E       ATOM   2936   CD   GLN   E   350   27.106   81.140   23.749   1.00   35.92   E       ATOM   2937   OE1   GLN   E   350   26.843   82.019   24.552   1.00   39.58   E       ATOM   2938   NE2   GLN   E   350   26.827   81.238   22.461   1.00   31.17   E       ATOM   2939   C   GLN   E   350   29.311   78.773   26.351   1.00   40.10   E       ATOM   2940   O   GLN   E   350   30.212   78.483   25.569   1.00   37.93   E       ATOM   2941   N   GLU   E   351   29.517   79.541   27.416   1.00   39.98   E       ATOM   2942   CA   GLU   E   351   30.843   80.079   27.702   1.00   42.25   E       ATOM   2943   CB   GLU   E   351   30.825   80.814   29.044   1.00   45.08   E       ATOM   2944   CG   GLU   E   351   29.972   82.086   29.014   1.00   66.01   E       ATOM   2945   CD   GLU   E   351   29.961   82.864   30.340   1.00   74.89   E       ATOM   2946   OE1   GLU   E   351   29.392   83.996   30.385   1.00   66.89   E       ATOM   2947   OE2   GLU   E   351   30.522   82.334   31.334   1.00   77.72   E       ATOM   2948   C   GLU   E   351   31.916   78.980   27.690   1.00   42.79   E       ATOM   2949   O   GLU   E   351   33.033   79.180   27.227   1.00   43.40   E       ATOM   2950   N   ILE   E   352   31.573   77.803   28.181   1.00   40.39   E       ATOM   2951   CA   ILE   E   352   32.524   76.703   28.196   1.00   36.14   E       ATOM   2952   CB   ILE   E   352   31.901   75.485   28.860   1.00   38.19   E       ATOM   2953   CG2   ILE   E   352   32.758   74.270   28.640   1.00   23.85   E       ATOM   2954   CG1   ILE   E   352   31.684   75.781   30.336   1.00   39.13   E       ATOM   2955   CD1   ILE   E   352   30.936   74.680   31.072   1.00   46.43   E       ATOM   2956   C   ILE   E   352   33.012   76.312   26.792   1.00   37.13   E       ATOM   2957   O   ILE   E   352   34.195   76.032   26.599   1.00   35.23   E       ATOM   2958   N   TYR   E   353   32.110   76.280   25.815   1.00   36.67   E       ATOM   2959   CA   TYR   E   353   32.509   75.918   24.461   1.00   31.52   E       ATOM   2960   CB   TYR   E   353   31.299   75.528   23.630   1.00   23.57   E       ATOM   2961   CG   TYR   E   353   30.615   74.299   24.164   1.00   33.24   E       ATOM   2962   CD1   TYR   E   353   29.497   74.406   24.997   1.00   33.74   E       ATOM   2963   CE1   TYR   E   353   28.878   73.285   25.519   1.00   33.63   E       ATOM   2964   CD2   TYR   E   353   31.102   73.026   23.866   1.00   30.53   E       ATOM   2965   CE2   TYR   E   353   30.497   71.891   24.381   1.00   33.64   E       ATOM   2966   CZ   TYR   E   353   29.383   72.024   25.209   1.00   38.19   E       ATOM   2967   OH   TYR   E   353   28.772   70.897   25.719   1.00   29.68   E       ATOM   2968   C   TYR   E   353   33.250   77.046   23.783   1.00   30.62   E       ATOM   2969   O   TYR   E   353   34.147   76.815   22.974   1.00   32.71   E       ATOM   2970   N   ILE   E   354   32.871   78.274   24.121   1.00   30.90   E       ATOM   2971   CA   ILE   E   354   33.496   79.463   23.553   1.00   27.81   E       ATOM   2972   CB   ILE   E   354   32.832   80.742   24.097   1.00   19.96   E       ATOM   2973   CG2   ILE   E   354   33.647   81.959   23.696   1.00   15.58   E       ATOM   2974   CG1   ILE   E   354   31.384   80.804   23.626   1.00   22.76   E       ATOM   2975   CD1   ILE   E   354   30.692   82.059   23.946   1.00   14.85   E       ATOM   2976   C   ILE   E   354   34.946   79.452   23.996   1.00   32.14   E       ATOM   2977   O   ILE   E   354   35.873   79.611   23.198   1.00   33.40   E       ATOM   2978   N   GLU   E   355   35.111   79.237   25.297   1.00   33.87   E       ATOM   2979   CA   GLU   E   355   36.399   79.203   25.943   1.00   29.98   E       ATOM   2980   CB   GLU   E   355   36.159   79.130   27.456   1.00   24.91   E       ATOM   2981   CG   GLU   E   355   37.368   79.460   28.311   1.00   49.56   E       ATOM   2982   CD   GLU   E   355   38.095   80.737   27.876   1.00   62.97   E       ATOM   2983   OE1   GLU   E   355   37.526   81.854   28.028   1.00   62.84   E       ATOM   2984   OE2   GLU   E   355   39.244   80.607   27.375   1.00   68.69   E       ATOM   2985   C   GLU   E   355   37.266   78.044   25.401   1.00   33.04   E       ATOM   2986   O   GLU   E   355   38.481   78.203   25.204   1.00   32.75   E       ATOM   2987   N   ALA   E   356   36.657   76.888   25.137   1.00   31.87   E       ATOM   2988   CA   ALA   E   356   37.411   75.765   24.590   1.00   33.45   E       ATOM   2989   CB   ALA   E   356   36.604   74.484   24.673   1.00   31.24   E       ATOM   2990   C   ALA   E   356   37.802   76.057   23.134   1.00   39.40   E       ATOM   2991   O   ALA   E   356   38.849   75.602   22.681   1.00   41.00   E       ATOM   2992   N   LEU   E   357   36.976   76.803   22.394   1.00   36.52   E       ATOM   2993   CA   LEU   E   357   37.327   77.142   21.015   1.00   32.92   E       ATOM   2994   CB   LEU   E   357   36.178   77.825   20.269   1.00   32.06   E       ATOM   2995   CG   LEU   E   357   36.474   78.270   18.827   1.00   25.48   E       ATOM   2996   CD1   LEU   E   357   37.017   77.132   17.985   1.00   18.80   E       ATOM   2997   CD2   LEU   E   357   35.199   78.780   18.219   1.00   22.88   E       ATOM   2998   C   LEU   E   357   38.513   78.083   21.046   1.00   34.90   E       ATOM   2999   O   LEU   E   357   39.450   77.907   20.262   1.00   36.03   E       ATOM   3000   N   LYS   E   358   38.475   79.082   21.940   1.00   34.91   E       ATOM   3001   CA   LYS   E   358   39.597   80.024   22.062   1.00   35.86   E       ATOM   3002   CB   LYS   E   358   39.393   81.073   23.177   1.00   30.78   E       ATOM   3003   CG   LYS   E   358   40.080   82.422   22.858   1.00   35.85   E       ATOM   3004   CD   LYS   E   358   40.114   83.450   24.006   1.00   40.68   E       ATOM   3005   CE   LYS   E   358   40.961   82.961   25.212   1.00   45.86   E       ATOM   3006   NZ   LYS   E   358   40.895   83.850   26.445   1.00   40.64   E       ATOM   3007   C   LYS   E   358   40.848   79.208   22.364   1.00   37.00   E       ATOM   3008   O   LYS   E   358   41.838   79.324   21.652   1.00   35.33   E       ATOM   3009   N   ALA   E   359   40.788   78.367   23.401   1.00   40.86   E       ATOM   3010   CA   ALA   E   359   41.917   77.513   23.788   1.00   39.35   E       ATOM   3011   CB   ALA   E   359   41.493   76.551   24.855   1.00   40.44   E       ATOM   3012   C   ALA   E   359   42.472   76.732   22.609   1.00   40.83   E       ATOM   3013   O   ALA   E   359   43.680   76.688   22.394   1.00   38.57   E       ATOM   3014   N   TYR   E   360   41.576   76.116   21.846   1.00   38.26   E       ATOM   3015   CA   TYR   E   360   41.956   75.317   20.694   1.00   32.22   E       ATOM   3016   CB   TYR   E   360   40.725   74.614   20.125   1.00   27.64   E       ATOM   3017   CG   TYR   E   360   40.977   73.808   18.858   1.00   25.35   E       ATOM   3018   CD1   TYR   E   360   41.381   72.483   18.923   1.00   18.24   E       ATOM   3019   CE1   TYR   E   360   41.611   71.751   17.773   1.00   20.01   E       ATOM   3020   CD2   TYR   E   360   40.807   74.383   17.588   1.00   25.83   E       ATOM   3021   CE2   TYR   E   360   41.037   73.659   16.433   1.00   23.29   E       ATOM   3022   CZ   TYR   E   360   41.436   72.337   16.530   1.00   28.18   E       ATOM   3023   OH   TYR   E   360   41.627   71.583   15.386   1.00   25.99   E       ATOM   3024   C   TYR   E   360   42.609   76.146   19.605   1.00   36.45   E       ATOM   3025   O   TYR   E   360   43.680   75.786   19.119   1.00   39.74   E       ATOM   3026   N   VAL   E   361   41.960   77.245   19.216   1.00   36.88   E       ATOM   3027   CA   VAL   E   361   42.467   78.113   18.146   1.00   40.55   E       ATOM   3028   CB   VAL   E   361   41.450   79.225   17.809   1.00   38.45   E       ATOM   3029   CG1   VAL   E   361   41.931   80.026   16.619   1.00   30.69   E       ATOM   3030   CG2   VAL   E   361   40.089   78.603   17.523   1.00   36.50   E       ATOM   3031   C   VAL   E   361   43.812   78.744   18.484   1.00   42.98   E       ATOM   3032   O   VAL   E   361   44.695   78.825   17.639   1.00   43.97   E       ATOM   3033   N   GLU   E   362   43.964   79.180   19.729   1.00   49.63   E       ATOM   3034   CA   GLU   E   362   45.214   79.775   20.182   1.00   50.89   E       ATOM   3035   CB   GLU   E   362   45.082   80.354   21.587   1.00   42.81   E       ATOM   3036   CG   GLU   E   362   44.453   81.704   21.618   1.00   48.93   E       ATOM   3037   CD   GLU   E   362   44.243   82.207   23.024   1.00   63.80   E       ATOM   3038   OE1   GLU   E   362   43.499   81.561   23.799   1.00   70.08   E       ATOM   3039   OE2   GLU   E   362   44.818   83.262   23.358   1.00   74.63   E       ATOM   3040   C   GLU   E   362   46.320   78.744   20.195   1.00   52.51   E       ATOM   3041   O   GLU   E   362   47.405   79.001   19.690   1.00   53.90   E       ATOM   3042   N   ASN   E   363   46.045   77.574   20.764   1.00   57.67   E       ATOM   3043   CA   ASN   E   363   47.052   76.525   20.841   1.00   57.57   E       ATOM   3044   CB   ASN   E   363   46.683   75.528   21.939   1.00   55.13   E       ATOM   3045   CG   ASN   E   363   47.074   76.027   23.314   1.00   60.47   E       ATOM   3046   OD1   ASN   E   363   48.251   76.028   23.665   1.00   68.73   E       ATOM   3047   ND2   ASN   E   363   46.095   76.475   24.091   1.00   59.89   E       ATOM   3048   C   ASN   E   363   47.414   75.817   19.539   1.00   57.23   E       ATOM   3049   O   ASN   E   363   48.215   74.898   19.549   1.00   60.35   E       ATOM   3050   N   ARG   E   364   46.827   76.229   18.419   1.00   62.49   E       ATOM   3051   CA   ARG   E   364   47.226   75.671   17.129   1.00   71.24   E       ATOM   3052   CB   ARG   E   364   46.214   75.966   16.032   1.00   68.25   E       ATOM   3053   CG   ARG   E   364   44.911   75.255   16.192   1.00   80.52   E       ATOM   3054   CD   ARG   E   364   45.079   73.745   16.101   1.00   88.65   E       ATOM   3055   NE   ARG   E   364   45.647   73.149   17.309   1.00   91.73   E       ATOM   3056   CZ   ARG   E   364   45.827   71.840   17.478   1.00   93.79   E       ATOM   3057   NH1   ARG   E   364   45.481   70.993   16.512   1.00   92.83   E       ATOM   3058   NH2   ARG   E   364   46.345   71.372   18.609   1.00   93.18   E       ATOM   3059   C   ARG   E   364   48.442   76.541   16.879   1.00   81.51   E       ATOM   3060   O   ARG   E   364   48.920   76.647   15.744   1.00   84.85   E       ATOM   3061   N   ARG   E   365   48.893   77.170   17.982   1.00   92.03   E       ATOM   3062   CA   ARG   E   365   50.030   78.117   18.098   1.00   96.21   E       ATOM   3063   CB   ARG   E   365   51.237   77.445   18.803   1.00   95.61   E       ATOM   3064   CG   ARG   E   365   52.264   78.397   19.455   1.00   91.12   E       ATOM   3065   CD   ARG   E   365   51.758   79.135   20.710   1.00   94.23   E       ATOM   3066   NE   ARG   E   365   51.599   78.281   21.899   1.00   104.40   E       ATOM   3067   CZ   ARG   E   365   51.437   78.725   23.156   1.00   105.97   E       ATOM   3068   NH1   ARG   E   365   51.412   80.027   23.432   1.00   100.30   E       ATOM   3069   NH2   ARG   E   365   51.290   77.855   24.154   1.00   106.95   E       ATOM   3070   C   ARG   E   365   50.407   78.678   16.729   1.00   99.02   E       ATOM   3071   O   ARG   E   365   51.579   78.784   16.360   1.00   103.34   E       ATOM   3072   N   LYS   E   366   49.361   79.040   15.992   1.00   99.93   E       ATOM   3073   CA   LYS   E   366   49.463   79.595   14.655   1.00   95.80   E       ATOM   3074   CB   LYS   E   366   48.296   79.085   13.813   1.00   92.63   E       ATOM   3075   CG   LYS   E   366   46.926   79.229   14.505   1.00   81.57   E       ATOM   3076   CD   LYS   E   366   45.835   78.705   13.592   1.00   83.83   E       ATOM   3077   CE   LYS   E   366   44.531   78.450   14.313   1.00   87.71   E       ATOM   3078   NZ   LYS   E   366   43.528   77.810   13.402   1.00   87.24   E       ATOM   3079   C   LYS   E   366   49.362   81.104   14.776   1.00   95.00   E       ATOM   3080   O   LYS   E   366   48.751   81.616   15.721   1.00   97.66   E       ATOM   3081   N   PRO   E   367   49.991   81.842   13.852   1.00   90.48   E       ATOM   3082   CD   PRO   E   367   51.023   81.481   12.867   1.00   85.71   E       ATOM   3083   CA   PRO   E   367   49.866   83.295   13.972   1.00   86.93   E       ATOM   3084   CB   PRO   E   367   50.800   83.803   12.883   1.00   81.22   E       ATOM   3085   CG   PRO   E   367   51.834   82.743   12.807   1.00   80.89   E       ATOM   3086   C   PRO   E   367   48.387   83.621   13.673   1.00   90.72   E       ATOM   3087   O   PRO   E   367   47.611   82.732   13.291   1.00   93.37   E       ATOM   3088   N   TYR   E   368   47.985   84.874   13.843   1.00   88.30   E       ATOM   3089   CA   TYR   E   368   46.604   85.272   13.558   1.00   87.82   E       ATOM   3090   CB   TYR   E   368   46.191   84.850   12.141   1.00   97.22   E       ATOM   3091   CG   TYR   E   368   47.285   84.791   11.088   1.00   100.81   E       ATOM   3092   CD1   TYR   E   368   47.913   83.584   10.786   1.00   101.27   E       ATOM   3093   CE1   TYR   E   368   48.840   83.488   9.773   1.00   103.17   E       ATOM   3094   CD2   TYR   E   368   47.629   85.916   10.338   1.00   100.48   E       ATOM   3095   CE2   TYR   E   368   48.562   85.830   9.310   1.00   103.55   E       ATOM   3096   CZ   TYR   E   368   49.160   84.605   9.032   1.00   105.22   E       ATOM   3097   OH   TYR   E   368   50.056   84.471   7.989   1.00   112.94   E       ATOM   3098   C   TYR   E   368   45.520   84.749   14.514   1.00   80.96   E       ATOM   3099   O   TYR   E   368   44.380   85.211   14.452   1.00   81.08   E       ATOM   3100   N   ALA   E   369   45.865   83.787   15.368   1.00   70.44   E       ATOM   3101   CA   ALA   E   369   44.932   83.191   16.328   1.00   62.48   E       ATOM   3102   CB   ALA   E   369   45.687   82.777   17.564   1.00   55.83   E       ATOM   3103   C   ALA   E   369   43.729   84.062   16.725   1.00   62.51   E       ATOM   3104   O   ALA   E   369   42.578   83.624   16.642   1.00   59.98   E       ATOM   3105   N   THR   E   370   43.973   85.293   17.160   1.00   58.77   E       ATOM   3106   CA   THR   E   370   42.855   86.142   17.549   1.00   56.88   E       ATOM   3107   CB   THR   E   370   43.338   87.422   18.308   1.00   52.55   E       ATOM   3108   OG1   THR   E   370   43.149   88.595   17.492   1.00   40.99   E       ATOM   3109   CG2   THR   E   370   44.797   87.248   18.723   1.00   43.43   E       ATOM   3110   C   THR   E   370   42.013   86.512   16.324   1.00   57.87   E       ATOM   3111   O   THR   E   370   40.783   86.590   16.400   1.00   58.49   E       ATOM   3112   N   THR   E   371   42.667   86.721   15.189   1.00   55.14   E       ATOM   3113   CA   THR   E   371   41.931   87.050   13.982   1.00   53.34   E       ATOM   3114   CB   THR   E   371   42.876   87.608   12.876   1.00   51.68   E       ATOM   3115   OG1   THR   E   371   42.886   89.053   12.954   1.00   39.83   E       ATOM   3116   CG2   THR   E   371   42.436   87.112   11.466   1.00   30.79   E       ATOM   3117   C   THR   E   371   41.148   85.835   13.477   1.00   54.94   E       ATOM   3118   O   THR   E   371   40.052   85.976   12.934   1.00   59.29   E       ATOM   3119   N   ILE   E   372   41.693   84.637   13.660   1.00   52.00   E       ATOM   3120   CA   ILE   E   372   40.982   83.439   13.221   1.00   46.89   E       ATOM   3121   CB   ILE   E   372   41.881   82.188   13.252   1.00   46.50   E       ATOM   3122   CG2   ILE   E   372   41.110   80.989   12.767   1.00   46.12   E       ATOM   3123   CG1   ILE   E   372   43.085   82.388   12.341   1.00   49.39   E       ATOM   3124   CD1   ILE   E   372   44.280   81.540   12.713   1.00   66.77   E       ATOM   3125   C   ILE   E   372   39.797   83.245   14.156   1.00   43.94   E       ATOM   3126   O   ILE   E   372   38.676   83.080   13.705   1.00   50.56   E       ATOM   3127   N   PHE   E   373   40.038   83.281   15.458   1.00   34.23   E       ATOM   3128   CA   PHE   E   373   38.961   83.126   16.430   1.00   33.38   E       ATOM   3129   CB   PHE   E   373   39.517   83.371   17.828   1.00   29.69   E       ATOM   3130   CG   PHE   E   373   38.508   83.204   18.923   1.00   25.05   E       ATOM   3131   CD1   PHE   E   373   38.117   81.945   19.339   1.00   32.12   E       ATOM   3132   CD2   PHE   E   373   37.979   84.318   19.573   1.00   33.08   E       ATOM   3133   CE1   PHE   E   373   37.213   81.799   20.389   1.00   37.40   E       ATOM   3134   CE2   PHE   E   373   37.080   84.185   20.618   1.00   33.02   E       ATOM   3135   CZ   PHE   E   373   36.698   82.928   21.032   1.00   36.20   E       ATOM   3136   C   PHE   E   373   37.781   84.082   16.170   1.00   34.09   E       ATOM   3137   O   PHE   E   373   36.609   83.686   16.230   1.00   29.43   E       ATOM   3138   N   ALA   E   374   38.109   85.345   15.896   1.00   38.16   E       ATOM   3139   CA   ALA   E   374   37.110   86.380   15.628   1.00   39.91   E       ATOM   3140   CB   ALA   E   374   37.767   87.770   15.583   1.00   35.72   E       ATOM   3141   C   ALA   E   374   36.378   86.099   14.322   1.00   38.29   E       ATOM   3142   O   ALA   E   374   35.184   86.340   14.224   1.00   38.07   E       ATOM   3143   N   LYS   E   375   37.097   85.599   13.323   1.00   36.27   E       ATOM   3144   CA   LYS   E   375   36.495   85.266   12.042   1.00   34.18   E       ATOM   3145   CB   LYS   E   375   37.568   84.935   11.021   1.00   36.07   E       ATOM   3146   CG   LYS   E   375   38.357   86.088   10.476   1.00   45.35   E       ATOM   3147   CD   LYS   E   375   39.190   85.560   9.313   1.00   57.63   E       ATOM   3148   CE   LYS   E   375   39.943   86.638   8.568   1.00   64.98   E       ATOM   3149   NZ   LYS   E   375   40.527   86.117   7.286   1.00   71.22   E       ATOM   3150   C   LYS   E   375   35.557   84.054   12.180   1.00   33.41   E       ATOM   3151   O   LYS   E   375   34.530   83.985   11.511   1.00   32.39   E       ATOM   3152   N   LEU   E   376   35.921   83.092   13.031   1.00   32.18   E       ATOM   3153   CA   LEU   E   376   35.093   81.906   13.251   1.00   29.18   E       ATOM   3154   CB   LEU   E   376   35.787   80.883   14.164   1.00   26.70   E       ATOM   3155   CG   LEU   E   376   36.957   80.073   13.575   1.00   30.47   E       ATOM   3156   CD1   LEU   E   376   37.561   79.226   14.664   1.00   35.46   E       ATOM   3157   CD2   LEU   E   376   36.506   79.181   12.428   1.00   15.68   E       ATOM   3158   C   LEU   E   376   33.791   82.341   13.888   1.00   29.09   E       ATOM   3159   O   LEU   E   376   32.717   82.018   13.387   1.00   27.41   E       ATOM   3160   N   LEU   E   377   33.894   83.096   14.979   1.00   27.74   E       ATOM   3161   CA   LEU   E   377   32.716   83.581   15.682   1.00   29.99   E       ATOM   3162   CB   LEU   E   377   33.122   84.445   16.874   1.00   28.77   E       ATOM   3163   CG   LEU   E   377   33.681   83.778   18.120   1.00   27.79   E       ATOM   3164   CD1   LEU   E   377   33.787   84.801   19.236   1.00   20.75   E       ATOM   3165   CD2   LEU   E   377   32.759   82.647   18.523   1.00   23.07   E       ATOM   3166   C   LEU   E   377   31.763   84.382   14.799   1.00   34.20   E       ATOM   3167   O   LEU   E   377   30.549   84.280   14.940   1.00   41.58   E       ATOM   3168   N   SER   E   378   32.313   85.185   13.895   1.00   33.96   E       ATOM   3169   CA   SER   E   378   31.508   86.015   13.009   1.00   32.03   E       ATOM   3170   CB   SER   E   378   32.396   86.822   12.077   1.00   33.38   E       ATOM   3171   OG   SER   E   378   33.048   85.973   11.157   1.00   34.99   E       ATOM   3172   C   SER   E   378   30.591   85.178   12.159   1.00   36.66   E       ATOM   3173   O   SER   E   378   29.522   85.626   11.748   1.00   38.35   E       ATOM   3174   N   VAL   E   379   31.015   83.960   11.868   1.00   37.35   E       ATOM   3175   CA   VAL   E   379   30.197   83.093   11.057   1.00   36.78   E       ATOM   3176   CB   VAL   E   379   30.862   81.728   10.945   1.00   35.51   E       ATOM   3177   CG1   VAL   E   379   29.847   80.651   10.612   1.00   37.59   E       ATOM   3178   CG2   VAL   E   379   31.895   81.805   9.869   1.00   27.07   E       ATOM   3179   C   VAL   E   379   28.793   83.010   11.640   1.00   37.14   E       ATOM   3180   O   VAL   E   379   27.822   82.854   10.902   1.00   40.33   E       ATOM   3181   N   LEU   E   380   28.698   83.172   12.960   1.00   32.84   E       ATOM   3182   CA   LEU   E   380   27.429   83.126   13.685   1.00   28.02   E       ATOM   3183   CB   LEU   E   380   27.692   83.153   15.185   1.00   21.14   E       ATOM   3184   CG   LEU   E   380   28.411   81.949   15.815   1.00   29.29   E       ATOM   3185   CD1   LEU   E   380   28.117   81.968   17.298   1.00   34.75   E       ATOM   3186   CD2   LEU   E   380   27.948   80.612   15.249   1.00   22.54   E       ATOM   3187   C   LEU   E   380   26.438   84.226   13.312   1.00   29.99   E       ATOM   3188   O   LEU   E   380   25.225   84.042   13.434   1.00   38.27   E       ATOM   3189   N   THR   E   381   26.958   85.370   12.881   1.00   25.84   E       ATOM   3190   CA   THR   E   381   26.132   86.484   12.436   1.00   26.88   E       ATOM   3191   CB   THR   E   381   26.969   87.754   12.264   1.00   15.29   E       ATOM   3192   OG1   THR   E   381   27.705   87.998   13.456   1.00   15.98   E       ATOM   3193   CG2   THR   E   383   26.084   88.947   11.974   1.00   16.48   E       ATOM   3194   C   THR   E   381   25.595   86.098   11.052   1.00   32.06   E       ATOM   3195   O   THR   E   381   24.464   86.407   10.677   1.00   33.96   E       ATOM   3196   N   GLU   E   382   26.436   85.429   10.279   1.00   34.87   E       ATOM   3197   CA   GLU   E   382   26.042   85.012   8.961   1.00   30.44   E       ATOM   3198   CB   GLU   E   382   27.227   84.374   8.251   1.00   35.97   E       ATOM   3199   CG   GLU   E   382   26.967   84.073   6.769   1.00   57.41   E       ATOM   3200   CD   GLU   E   382   26.250   85.217   6.015   1.00   63.98   E       ATOM   3201   OE1   GLU   E   382   26.453   86.415   6.402   1.00   59.25   E       ATOM   3202   OE2   GLU   E   382   25.509   84.901   5.026   1.00   47.35   E       ATOM   3203   C   GLU   E   382   24.881   84.040   9.096   1.00   28.38   E       ATOM   3204   O   GLU   E   382   23.946   84.078   8.309   1.00   28.70   E       ATOM   3205   N   LEU   E   383   24.919   83.191   10.118   1.00   28.31   E       ATOM   3206   CA   LEU   E   383   23.845   82.228   10.339   1.00   22.49   E       ATOM   3207   CB   LEU   E   383   24.204   81.302   11.495   1.00   16.97   E       ATOM   3208   CG   LEU   E   383   25.357   80.359   11.141   1.00   26.83   E       ATOM   3209   CD1   LEU   E   383   25.655   79.434   12.289   1.00   20.81   E       ATOM   3210   CD2   LEU   E   383   25.011   79.564   9.884   1.00   21.75   E       ATOM   3211   C   LEU   E   383   22.480   82.887   10.566   1.00   23.24   E       ATOM   3212   O   LEU   E   383   21.463   82.372   10.133   1.00   27.48   E       ATOM   3213   N   ARG   E   384   22.441   84.029   11.236   1.00   22.78   E       ATOM   3214   CA   ARG   E   384   21.167   84.718   11.430   1.00   24.73   E       ATOM   3215   CB   ARG   E   384   21.303   85.993   12.288   1.00   22.96   E       ATOM   3216   CG   ARG   E   384   21.825   85.774   13.671   1.00   27.90   E       ATOM   3217   CD   ARG   E   384   20.953   84.840   14.429   1.00   18.45   E       ATOM   3218   NE   ARG   E   384   21.607   84.408   15.654   1.00   35.88   E       ATOM   3219   CZ   ARG   E   384   21.479   85.008   16.835   1.00   34.93   E       ATOM   3220   NH1   ARG   E   384   20.708   86.084   16.979   1.00   14.64   E       ATOM   3221   NH2   ARG   E   384   22.138   84.515   17.876   1.00   32.02   E       ATOM   3222   C   ARG   E   384   20.558   85.124   10.081   1.00   26.38   E       ATOM   3223   O   ARG   E   384   19.338   85.168   9.950   1.00   33.40   E       ATOM   3224   N   THR   E   385   21.353   85.449   9.070   1.00   19.82   E       ATOM   3225   CA   THR   E   385   20.658   85.822   7.871   1.00   27.51   E       ATOM   3226   CB   THR   E   385   21.451   86.826   6.978   1.00   34.59   E       ATOM   3227   OG1   THR   E   385   22.673   86.246   6.547   1.00   42.75   E       ATOM   3228   CG2   THR   E   385   21.737   88.116   7.737   1.00   36.75   E       ATOM   3229   C   THR   E   385   20.286   84.574   7.103   1.00   30.02   E       ATOM   3230   O   THR   E   385   19.223   84.522   6.494   1.00   36.26   E       ATOM   3231   N   LEU   E   386   21.133   83.553   7.160   1.00   27.82   E       ATOM   3232   CA   LEU   E   386   20.866   82.311   6.445   1.00   26.77   E       ATOM   3233   CB   LEU   E   386   22.080   81.381   6.533   1.00   17.31   E       ATOM   3234   CG   LEU   E   386   23.232   81.678   5.585   1.00   11.79   E       ATOM   3235   CD1   LEU   E   386   24.377   80.771   5.881   1.00   29.55   E       ATOM   3236   CD2   LEU   E   386   22.799   81.476   4.158   1.00   19.90   E       ATOM   3237   C   LEU   E   386   19.634   81.600   7.004   1.00   33.17   E       ATOM   3238   O   LEU   E   386   18.835   81.000   6.261   1.00   32.97   E       ATOM   3239   N   GLY   E   387   19.491   81.674   8.323   1.00   29.30   E       ATOM   3240   CA   GLY   E   387   18.387   81.017   8.979   1.00   31.66   E       ATOM   3241   C   GLY   E   387   17.113   81.760   8.690   1.00   35.31   E       ATOM   3242   O   GLY   E   387   16.025   81.170   8.692   1.00   38.04   E       ATOM   3243   N   ASN   E   388   17.254   83.063   8.465   1.00   35.06   E       ATOM   3244   CA   ASN   E   388   16.124   83.938   8.171   1.00   35.25   E       ATOM   3245   CB   ASN   E   388   16.562   85.393   8.258   1.00   34.73   E       ATOM   3246   CG   ASN   E   388   15.441   86.353   7.972   1.00   35.48   E       ATOM   3247   OD1   ASN   E   388   14.368   86.264   8.554   1.00   38.42   E       ATOM   3248   ND2   ASN   E   388   15.690   87.294   7.080   1.00   40.60   E       ATOM   3249   C   ASN   E   388   15.684   83.613   6.758   1.00   37.77   E       ATOM   3250   O   ASN   E   388   14.496   83.507   6.461   1.00   33.42   E       ATOM   3251   N   MET   E   389   16.678   83.452   5.893   1.00   38.07   E       ATOM   3252   CA   MET   E   389   16.459   83.097   4.507   1.00   33.49   E       ATOM   3253   CB   MET   E   389   17.788   82.928   3.804   1.00   34.37   E       ATOM   3254   CG   MET   E   389   17.674   82.389   2.416   1.00   35.98   E       ATOM   3255   SD   MET   E   389   19.307   82.315   1.703   1.00   61.87   E       ATOM   3256   CE   MET   E   389   19.736   80.608   2.072   1.00   48.34   E       ATOM   3257   C   MET   E   389   15.715   81.779   4.456   1.00   33.16   E       ATOM   3258   O   MET   E   389   14.760   81.614   3.699   1.00   37.81   E       ATOM   3259   N   ASN   E   390   16.146   80.823   5.259   1.00   27.59   E       ATOM   3260   CA   ASN   E   390   15.458   79.562   5.215   1.00   28.20   E       ATOM   3261   CB   ASN   E   390   16.097   78.568   6.166   1.00   30.32   E       ATOM   3262   CG   ASN   E   390   15.584   77.175   5.949   1.00   35.90   E       ATOM   3263   OD1   ASN   E   390   14.735   76.692   6.706   1.00   31.78   E       ATOM   3264   ND2   ASN   E   390   16.082   76.518   4.891   1.00   38.32   E       ATOM   3265   C   ASN   E   390   13.978   79.731   5.519   1.00   28.45   E       ATOM   3266   O   ASN   E   390   13.134   79.201   4.797   1.00   28.72   E       ATOM   3267   N   SER   E   391   13.668   80.483   6.572   1.00   30.90   E       ATOM   3268   CA   SER   E   391   12.282   80.730   6.974   1.00   31.85   E       ATOM   3269   CB   SER   E   391   12.220   81.620   8.217   1.00   32.14   E       ATOM   3270   OG   SER   E   391   12.727   80.950   9.360   1.00   45.82   E       ATOM   3271   C   SER   E   391   11.514   81.393   5.857   1.00   31.51   E       ATOM   3272   O   SER   E   391   10.342   81.097   5.642   1.00   31.42   E       ATOM   3273   N   GLU   E   392   12.196   82.294   5.158   1.00   35.32   E       ATOM   3274   CA   GLU   E   392   11.634   83.027   4.042   1.00   37.79   E       ATOM   3275   CB   GLU   E   392   12.646   84.068   3.560   1.00   45.73   E       ATOM   3276   CG   GLU   E   392   12.050   85.146   2.665   1.00   71.70   E       ATOM   3277   CD   GLU   E   392   10.594   85.493   3.038   1.00   81.65   E       ATOM   3278   OE1   GLU   E   392   10.318   85.713   4.248   1.00   82.26   E       ATOM   3279   OE2   GLU   E   392   9.733   85.551   2.117   1.00   83.41   E       ATOM   3280   C   GLU   E   392   11.292   82.029   2.942   1.00   37.32   E       ATOM   3281   O   GLU   E   392   10.222   82.099   2.357   1.00   40.36   E       ATOM   3282   N   THR   E   393   12.198   81.090   2.676   1.00   34.79   E       ATOM   3283   CA   THR   E   393   11.963   80.045   1.683   1.00   31.23   E       ATOM   3284   CB   THR   E   393   13.169   79.075   1.591   1.00   31.08   E       ATOM   3285   OG1   THR   E   393   14.331   79.765   1.116   1.00   27.30   E       ATOM   3286   CG2   THR   E   393   12.856   77.922   0.647   1.00   27.02   E       ATOM   3287   C   THR   E   393   10.711   79.220   2.074   1.00   32.60   E       ATOM   3288   O   THR   E   393   9.917   78.822   1.235   1.00   36.48   E       ATOM   3289   N   CYS   E   394   10.527   78.956   3.355   1.00   34.75   E       ATOM   3290   CA   CYS   E   394   9.360   78.182   3.769   1.00   37.83   E       ATOM   3291   CB   CYS   E   394   9.454   77.808   5.240   1.00   30.63   E       ATOM   3292   SG   CYS   E   394   10.513   76.386   5.489   1.00   41.29   E       ATOM   3293   C   CYS   E   394   8.066   78.908   3.519   1.00   38.54   E       ATOM   3294   O   CYS   E   394   7.069   78.292   3.163   1.00   35.21   E       ATOM   3295   N   PHE   E   395   8.087   80.223   3.711   1.00   40.13   E       ATOM   3296   CA   PHE   E   395   6.903   81.044   3.505   1.00   37.82   E       ATOM   3297   CB   PHE   E   395   7.205   82.518   3.772   1.00   29.50   E       ATOM   3298   CG   PHE   E   395   6.025   83.420   3.567   1.00   29.76   E       ATOM   3299   CD1   PHE   E   395   4.968   83.421   4.483   1.00   31.00   E       ATOM   3300   CD2   PHE   E   395   5.938   84.232   2.433   1.00   28.66   E       ATOM   3301   CE1   PHE   E   395   3.834   84.215   4.272   1.00   30.82   E       ATOM   3302   CE2   PHE   E   395   4.804   85.032   2.209   1.00   26.06   E       ATOM   3303   CZ   PHE   E   395   3.754   85.022   3.130   1.00   27.11   E       ATOM   3304   C   PHE   E   395   6.459   80.914   2.069   1.00   39.43   E       ATOM   3305   O   PHE   E   395   5.274   80.746   1.785   1.00   39.90   E       ATOM   3306   N   SER   E   396   7.437   80.997   1.174   1.00   34.64   E       ATOM   3307   CA   SER   E   396   7.205   80.937   −0.249   1.00   36.33   E       ATOM   3308   CB   SER   E   396   8.474   81.306   −0.970   1.00   32.84   E       ATOM   3309   OG   SER   E   396   8.784   82.633   −0.581   1.00   51.02   E       ATOM   3310   C   SER   E   396   6.683   79.626   −0.743   1.00   39.02   E       ATOM   3311   O   SER   E   396   5.778   79.600   −1.572   1.00   42.24   E       ATOM   3312   N   LEU   E   397   7.246   78.531   −0.247   1.00   43.94   E       ATOM   3313   CA   LEU   E   397   6.775   77.214   −0.643   1.00   42.57   E       ATOM   3314   CB   LEU   E   397   7.629   76.123   0.000   1.00   37.99   E       ATOM   3315   CG   LEU   E   397   9.079   76.179   −0.432   1.00   31.14   E       ATOM   3316   CD1   LEU   E   397   9.839   75.035   0.159   1.00   35.00   E       ATOM   3317   CD2   LEU   E   397   9.131   76.124   −1.929   1.00   40.62   E       ATOM   3318   C   LEU   E   397   5.330   77.103   −0.173   1.00   41.49   E       ATOM   3319   O   LEU   E   397   4.520   76.450   −0.799   1.00   49.39   E       ATOM   3320   N   LYS   E   398   5.013   77.767   0.928   1.00   37.15   E       ATOM   3321   CA   LYS   E   398   3.675   77.742   1.473   1.00   39.00   E       ATOM   3322   CB   LYS   E   398   3.724   78.275   2.904   1.00   43.96   E       ATOM   3323   CG   LYS   E   398   2.869   77.504   3.889   1.00   52.32   E       ATOM   3324   CD   LYS   E   398   3.114   75.996   3.792   1.00   59.84   E       ATOM   3325   CE   LYS   E   398   1.853   75.225   4.218   1.00   65.06   E       ATOM   3326   NZ   LYS   E   398   1.812   73.819   3.706   1.00   68.83   E       ATOM   3327   C   LYS   E   398   2.709   78.571   0.613   1.00   44.04   E       ATOM   3328   O   LYS   E   398   1.513   78.308   0.579   1.00   47.81   E       ATOM   3329   N   LEU   E   399   3.244   79.569   −0.084   1.00   50.06   E       ATOM   3330   CA   LEU   E   399   2.476   80.464   −0.947   1.00   42.86   E       ATOM   3331   CB   LEU   E   399   3.303   81.714   −1.247   1.00   43.06   E       ATOM   3332   CG   LEU   E   399   2.649   82.840   −2.039   1.00   42.04   E       ATOM   3333   CD1   LEU   E   399   1.534   83.421   −1.201   1.00   37.94   E       ATOM   3334   CD2   LEU   E   399   3.653   83.902   −2.378   1.00   24.82   E       ATOM   3335   C   LEU   E   399   2.181   79.749   −2.246   1.00   43.34   E       ATOM   3336   O   LEU   E   399   1.043   79.720   −2.717   1.00   48.77   E       ATOM   3337   N   LYS   E   400   3.240   79.194   −2.826   1.00   45.96   E       ATOM   3338   CA   LYS   E   400   3.174   78.444   −4.078   1.00   49.43   E       ATOM   3339   CB   LYS   E   400   4.580   78.113   −4.567   1.00   47.72   E       ATOM   3340   CG   LYS   E   400   5.514   79.302   −4.753   1.00   47.05   E       ATOM   3341   CD   LYS   E   400   6.930   78.752   −4.789   1.00   55.17   E       ATOM   3342   CE   LYS   E   400   8.009   79.787   −5.015   1.00   51.25   E       ATOM   3343   NZ   LYS   E   400   9.325   79.087   −4.846   1.00   53.55   E       ATOM   3344   C   LYS   E   400   2.451   77.140   −3.797   1.00   49.29   E       ATOM   3345   O   LYS   E   400   2.167   76.359   −4.698   1.00   48.52   E       ATOM   3346   N   ASN   E   401   2.159   76.926   −2.523   1.00   49.33   E       ATOM   3347   CA   ASN   E   401   1.494   75.722   −2.051   1.00   51.53   E       ATOM   3348   CB   ASN   E   401   0.045   75.690   −2.502   1.00   53.59   E       ATOM   3349   CG   ASN   E   401   −0.762   74.657   −1.740   1.00   60.06   E       ATOM   3350   OD1   ASN   E   401   −1.768   74.151   −2.237   1.00   56.19   E       ATOM   3351   ND2   ASN   E   401   −0.326   74.342   −0.512   1.00   62.85   E       ATOM   3352   C   ASN   E   401   2.187   74.426   −2.497   1.00   50.38   E       ATOM   3353   O   ASN   E   401   1.641   73.654   −3.279   1.00   47.98   E       ATOM   3354   N   ARG   E   402   3.395   74.201   −1.989   1.00   49.15   E       ATOM   3355   CA   ARG   E   402   4.169   73.017   −2.301   1.00   50.62   E       ATOM   3356   CB   ARG   E   402   5.515   73.416   −2.866   1.00   56.48   E       ATOM   3357   CG   ARG   E   402   5.397   74.361   −4.038   1.00   64.09   E       ATOM   3358   CD   ARG   E   402   6.740   74.500   −4.694   1.00   71.64   E       ATOM   3359   NE   ARG   E   402   7.126   73.261   −5.359   1.00   72.37   E       ATOM   3360   CZ   ARG   E   402   8.352   73.003   −5.806   1.00   73.62   E       ATOM   3361   NH1   ARG   E   402   9.320   73.904   −5.649   1.00   65.04   E       ATOM   3362   NH2   ARG   E   402   8.601   71.849   −6.424   1.00   73.00   E       ATOM   3363   C   ARG   E   402   4.334   72.356   −0.965   1.00   53.42   E       ATOM   3364   O   ARG   E   402   4.430   73.057   0.040   1.00   57.21   E       ATOM   3365   N   LYS   E   403   4.362   71.020   −0.951   1.00   54.79   E       ATOM   3366   CA   LYS   E   403   4.461   70.238   0.293   1.00   52.75   E       ATOM   3367   CB   LYS   E   403   4.269   68.743   0.006   1.00   53.56   E       ATOM   3368   CG   LYS   E   403   2.871   68.363   −0.456   1.00   68.79   E       ATOM   3369   CD   LYS   E   403   2.804   66.872   −0.808   1.00   77.87   E       ATOM   3370   CE   LYS   E   403   1.437   66.457   −1.360   1.00   79.58   E       ATOM   3371   NZ   LYS   E   403   1.277   64.966   −1.360   1.00   81.94   E       ATOM   3372   C   LYS   E   403   5.718   70.399   1.142   1.00   49.96   E       ATOM   3373   O   LYS   E   403   6.812   69.931   0.764   1.00   46.03   E       ATOM   3374   N   VAL   E   404   5.556   71.058   2.291   1.00   38.89   E       ATOM   3375   CA   VAL   E   404   6.672   71.223   3.205   1.00   40.29   E       ATOM   3376   CB   VAL   E   404   6.693   72.581   3.922   1.00   41.80   E       ATOM   3377   CG1   VAL   E   404   8.022   72.711   4.686   1.00   24.81   E       ATOM   3378   CG2   VAL   E   404   6.448   73.735   2.944   1.00   39.16   E       ATOM   3379   C   VAL   E   404   6.427   70.189   4.293   1.00   48.27   E       ATOM   3380   O   VAL   E   404   5.442   70.290   5.020   1.00   55.74   E       ATOM   3381   N   PRO   E   405   7.325   69.197   4.440   1.00   45.50   E       ATOM   3382   CD   PRO   E   405   8.679   69.161   3.858   1.00   42.67   E       ATOM   3383   CA   PRO   E   405   7.173   68.154   5.463   1.00   40.57   E       ATOM   3384   CB   PRO   E   405   8.572   67.580   5.571   1.00   41.08   E       ATOM   3385   CG   PRO   E   405   9.123   67.780   4.203   1.00   40.01   E       ATOM   3386   C   PRO   E   405   6.698   68.714   6.803   1.00   45.93   E       ATOM   3387   O   PRO   E   405   7.339   69.593   7.386   1.00   46.37   E       ATOM   3388   N   SER   E   406   5.586   68.195   7.304   1.00   52.64   E       ATOM   3389   CA   SER   E   406   5.045   68.680   8.568   1.00   57.41   E       ATOM   3390   CB   SER   E   406   3.901   67.787   9.032   1.00   56.58   E       ATOM   3391   OG   SER   E   406   3.121   68.480   9.988   1.00   67.22   E       ATOM   3392   C   SER   E   406   6.085   68.814   9.693   1.00   59.81   E       ATOM   3393   O   SER   E   406   6.068   69.798   10.438   1.00   63.18   E       ATOM   3394   N   PHE   E   407   6.983   67.837   9.819   1.00   57.14   E       ATOM   3395   CA   PHE   E   407   8.013   67.877   10.853   1.00   51.13   E       ATOM   3396   CB   PHE   E   407   9.027   66.751   10.625   1.00   48.43   E       ATOM   3397   CG   PHE   E   407   10.186   66.743   11.610   1.00   50.11   E       ATOM   3398   CD1   PHE   E   407   9.961   66.780   12.990   1.00   47.64   E       ATOM   3399   CD2   PHE   E   407   11.501   66.629   11.156   1.00   49.90   E       ATOM   3400   CE1   PHE   E   407   11.019   66.693   13.891   1.00   37.99   E       ATOM   3401   CE2   PHE   E   407   12.559   66.544   12.052   1.00   52.16   E       ATOM   3402   CZ   PHE   E   407   12.314   66.574   13.425   1.00   44.66   E       ATOM   3403   C   PHE   E   407   8.722   69.225   10.820   1.00   49.58   E       ATOM   3404   O   PHE   E   407   8.924   69.855   11.868   1.00   48.50   E       ATOM   3405   N   LEU   E   408   9.087   69.650   9.606   1.00   46.20   E       ATOM   3406   CA   LEU   E   408   9.788   70.907   9.376   1.00   46.76   E       ATOM   3407   CB   LEU   E   408   10.269   70.977   7.928   1.00   40.00   E       ATOM   3408   CG   LEU   E   408   11.276   69.905   7.527   1.00   38.59   E       ATOM   3409   CD1   LEU   E   408   11.706   70.112   6.089   1.00   40.41   E       ATOM   3410   CD2   LEU   E   408   12.468   69.961   8.439   1.00   37.21   E       ATOM   3411   C   LEU   E   408   8.920   72.125   9.701   1.00   52.01   E       ATOM   3412   O   LEU   E   408   9.408   73.132   10.233   1.00   55.68   E       ATOM   3413   N   GLU   E   409   7.634   72.043   9.382   1.00   49.74   E       ATOM   3414   CA   GLU   E   409   6.746   73.145   9.684   1.00   50.76   E       ATOM   3415   CB   GLU   E   409   5.387   72.879   9.039   1.00   52.54   E       ATOM   3416   CG   GLU   E   409   5.512   72.621   7.526   1.00   65.10   E       ATOM   3417   CD   GLU   E   409   4.191   72.709   6.761   1.00   69.80   E       ATOM   3418   OE1   GLU   E   409   3.226   71.997   7.120   1.00   74.10   E       ATOM   3419   OE2   GLU   E   409   4.122   73.489   5.788   1.00   71.29   E       ATOM   3420   C   GLU   E   409   6.663   73.266   11.214   1.00   51.62   E       ATOM   3421   O   GLU   E   409   6.819   74.348   11.775   1.00   47.23   E       ATOM   3422   N   GLU   E   410   6.465   72.130   11.876   1.00   53.40   E       ATOM   3423   CA   GLU   E   410   6.371   72.044   13.335   1.00   52.41   E       ATOM   3424   CB   GLU   E   410   6.220   70.583   13.768   1.00   56.30   E       ATOM   3425   CG   GLU   E   410   5.008   69.847   13.207   1.00   63.66   E       ATOM   3426   CD   GLU   E   410   5.119   68.337   13.360   1.00   65.12   E       ATOM   3427   OE1   GLU   E   410   4.133   67.627   13.076   1.00   57.01   E       ATOM   3428   OE2   GLU   E   410   6.202   67.856   13.755   1.00   75.09   E       ATOM   3429   C   GLU   E   410   7.591   72.599   14.060   1.00   50.63   E       ATOM   3430   O   GLU   E   410   7.465   73.224   15.109   1.00   51.62   E       ATOM   3431   N   ILE   E   411   8.774   72.351   13.508   1.00   44.17   E       ATOM   3432   CA   ILE   E   411   10.016   72.788   14.147   1.00   42.52   E       ATOM   3433   CB   ILE   E   411   11.178   71.838   13.803   1.00   29.79   E       ATOM   3434   CG2   ILE   E   411   12.472   72.388   14.324   1.00   19.62   E       ATOM   3435   CG1   ILE   E   411   10.885   70.464   14.389   1.00   26.63   E       ATOM   3436   CD1   ILE   E   411   12.014   69.562   14.352   1.00   32.83   E       ATOM   3437   C   ILE   E   411   10.455   74.198   13.838   1.00   47.45   E       ATOM   3438   O   ILE   E   411   10.963   74.908   14.710   1.00   45.98   E       ATOM   3439   N   TRP   E   412   10.266   74.596   12.587   1.00   50.84   E       ATOM   3440   CA   TRP   E   412   10.638   75.928   12.158   1.00   47.10   E       ATOM   3441   CB   TRP   E   412   11.106   75.897   10.714   1.00   31.01   E       ATOM   3442   CG   TRP   E   412   12.357   75.111   10.520   1.00   29.88   E       ATOM   3443   CD2   TRP   E   412   12.802   74.514   9.306   1.00   30.53   E       ATOM   3444   CE2   TRP   E   412   14.074   73.964   9.554   1.00   29.64   E       ATOM   3445   CE3   TRP   E   412   12.242   74.378   8.030   1.00   31.08   E       ATOM   3446   CD1   TRP   E   412   13.356   74.909   11.431   1.00   29.83   E       ATOM   3447   NE1   TRP   E   412   14.391   74.226   10.858   1.00   26.29   E       ATOM   3448   CZ2   TRP   E   412   14.804   73.304   8.568   1.00   30.77   E       ATOM   3449   CZ3   TRP   E   412   12.972   73.721   7.051   1.00   33.89   E       ATOM   3450   CH2   TRP   E   412   14.235   73.184   7.328   1.00   34.12   E       ATOM   3451   C   TRP   E   412   9.470   76.872   12.287   1.00   53.01   E       ATOM   3452   O   TRP   E   412   9.598   78.044   11.975   1.00   59.24   E       ATOM   3453   N   ASP   E   413   8.334   76.356   12.749   1.00   60.21   E       ATOM   3454   CA   ASP   E   413   7.127   77.155   12.904   1.00   65.98   E       ATOM   3455   CB   ASP   E   413   7.357   78.308   13.886   1.00   65.12   E       ATOM   3456   CG   ASP   E   413   7.976   77.848   15.206   1.00   73.02   E       ATOM   3457   OD1   ASP   E   413   7.517   76.827   15.778   1.00   69.22   E       ATOM   3458   OD2   ASP   E   413   8.918   78.522   15.682   1.00   71.14   E       ATOM   3459   C   ASP   E   413   6.800   77.709   11.529   1.00   73.27   E       ATOM   3460   O   ASP   E   413   6.734   78.919   11.332   1.00   79.88   E       ATOM   3461   N   VAL   E   414   6.617   76.810   10.572   1.00   78.65   E       ATOM   3462   CA   VAL   E   414   6.313   77.195   9.201   1.00   83.57   E       ATOM   3463   CB   VAL   E   414   7.148   76.388   8.201   1.00   81.07   E       ATOM   3464   CG1   VAL   E   414   6.874   76.876   6.782   1.00   78.91   E       ATOM   3465   CG2   VAL   E   414   8.605   76.474   8.565   1.00   83.03   E       ATOM   3466   C   VAL   E   414   4.861   76.936   8.841   1.00   91.08   E       ATOM   3467   O   VAL   E   414   4.515   75.832   8.421   1.00   98.61   E       ATOM   3468   N   VAL   E   415   3.998   77.924   9.002   1.00   93.34   E       ATOM   3469   CA   VAL   E   415   2.611   77.707   8.614   1.00   94.81   E       ATOM   3470   CB   VAL   E   415   1.706   77.355   9.848   1.00   90.47   E       ATOM   3471   CG1   VAL   E   415   1.624   75.834   10.020   1.00   78.74   E       ATOM   3472   CG2   VAL   E   415   2.269   77.985   11.119   1.00   82.74   E       ATOM   3473   C   VAL   E   415   2.101   78.944   7.876   1.00   97.73   E       ATOM   3474   O   VAL   E   415   2.139   78.927   6.624   1.00   97.64   E       ATOM   3475   OXT   VAL   E   415   1.716   79.926   8.541   1.00   98.46   E       ATOM   3476   O1   PON   A   1   21.880   64.675   1.836   1.00   39.29   A       ATOM   3477   O2   PON   A   1   19.250   68.890   4.074   1.00   49.48   A       ATOM   3478   O3   PON   A   1   24.588   66.480   7.635   1.00   41.10   A       ATOM   3479   O4   PON   A   1   24.235   64.175   5.968   1.00   45.83   A       ATOM   3480   O6   PON   A   1   18.231   74.846   1.917   1.00   33.99   A       ATOM   3481   O7   PON   A   1   20.248   73.129   1.273   1.00   33.86   A       ATOM   3482   C1   PON   A   1   24.365   67.114   5.289   1.00   35.43   A       ATOM   3483   C2   PON   A   1   23.687   66.508   6.523   1.00   38.34   A       ATOM   3484   C3   PON   A   1   23.150   65.064   6.265   1.00   36.40   A       ATOM   3485   C4   PON   A   1   22.176   65.084   5.024   1.00   33.74   A       ATOM   3486   C5   PON   A   1   22.927   65.679   3.758   1.00   31.18   A       ATOM   3487   C6   PON   A   1   21.955   65.657   2.563   1.00   33.89   A       ATOM   3488   C7   PON   A   1   21.097   66.795   2.300   1.00   28.82   A       ATOM   3489   C8   PON   A   1   21.130   67.924   3.082   1.00   37.62   A       ATOM   3490   C9   PON   A   1   22.125   68.074   4.307   1.00   31.36   A       ATOM   3491   C10   PON   A   1   23.441   67.156   4.046   1.00   29.60   A       ATOM   3492   C11   PON   A   1   22.560   69.547   4.592   1.00   32.32   A       ATOM   3493   C12   PON   A   1   21.489   70.626   4.357   1.00   38.09   A       ATOM   3494   C13   PON   A   1   20.762   70.529   2.973   1.00   36.47   A       ATOM   3495   C14   PON   A   1   20.134   69.048   2.915   1.00   39.30   A       ATOM   3496   C15   PON   A   1   19.155   69.066   1.737   1.00   40.89   A       ATOM   3497   C16   PON   A   1   18.747   70.529   1.546   1.00   39.22   A       ATOM   3498   C17   PON   A   1   19.416   71.300   2.743   1.00   35.47   A       ATOM   3499   C18   PON   A   1   21.769   70.748   1.787   1.00   32.19   A       ATOM   3500   C19   PON   A   1   24.255   67.664   2.827   1.00   24.46   A       ATOM   3501   C20   PON   A   1   19.466   72.863   2.472   1.00   35.95   A       ATOM   3502   C21   PON   A   1   20.120   73.624   3.669   1.00   36.02   A       ATOM   3503   C22   PON   A   1   18.054   73.441   2.175   1.00   32.10   A       ATOM   3504   C23   PON   A   1   16.966   73.306   3.300   1.00   27.82   A       ATOM   3505   C24   PON   A   1   15.596   73.682   2.708   1.00   19.20   A       ATOM   3506   C25   PON   A   1   14.375   73.327   3.427   1.00   28.59   A       ATOM   3507   C26   PON   A   1   13.612   72.211   2.623   1.00   27.63   A       ATOM   3508   C27   PON   A   1   13.497   74.515   3.656   1.00   26.34   A       ATOM   3509   P   PO4       1   20.235   86.852   20.495   1.00   30.27       ATOM   3510   O1   PO4       1   20.367   87.795   21.734   1.00   30.23       ATOM   3511   O2   PO4       1   21.496   86.086   20.199   1.00   24.49       ATOM   3512   O3   PO4       1   19.795   87.730   19.291   1.00   36.16       ATOM   3513   O4   PO4       1   19.068   85.895   20.750   1.00   32.97       ATOM   3514   P   PO4       2   39.059   93.718   35.395   1.00   78.13       ATOM   3515   O1   PO4       2   40.205   94.770   35.302   1.00   80.90       ATOM   3516   O2   PO4       2   39.127   92.675   34.321   1.00   73.64       ATOM   3517   O3   PO4       2   37.709   94.500   35.366   1.00   80.87       ATOM   3518   O4   PO4       2   39.152   93.072   36.788   1.00   87.72       ATOM   3519   P   PO4       3   15.547   99.875   0.242   1.00   66.29       ATOM   3520   O1   PO4       3   14.096   99.637   −0.237   1.00   69.21       ATOM   3521   O2   PO4       3   16.172   98.596   0.756   1.00   58.29       ATOM   3522   O3   PO4       3   15.467   101.019   1.344   1.00   49.78       ATOM   3523   O4   PO4       3   16.339   100.404   −1.015   1.00   64.10       ATOM   3524   P   PO4       4   20.453   67.865   −11.707   1.00   75.67       ATOM   3525   O1   PO4       4   20.348   66.382   −12.180   1.00   76.23       ATOM   3526   O2   PO4       4   20.722   67.960   −10.231   1.00   79.04       ATOM   3527   O3   PO4       4   19.108   68.571   −12.112   1.00   66.80       ATOM   3528   O4   PO4       4   21.613   68.530   −12.504   1.00   62.79       END