CRYSTAL OF SM3 ANTIBODY (FRAGMENT) AND RECOGNIZING EPITOPE, ITS PREPARATION, ENCODED DATA STORAGE MEDIUM CONTAINING ITS COORDINATES AND ITS DIAGNOSTICAL OR MEDICAL USE

Abstract: A process for preparing a crystal using cadmium. Structure factors or structural coordinates obtained from the crystal of SM3 antibody bound to an epitope can be used to design mimics of the antibody or epitope. Such mimics can be used in the diagnosis or therapy of cancer.

Description: CRYSTAL OF SM3 ANTIBODY (FRAGMENT) AND RECOGNIZING EPITOPE, ITS PREPARATION, ENCODED DATA STORAGE MEDIUM CONTAINING ITS COORDINATES AND ITS DIAGNOSTICAL OR MEDICAL USE The present invention relates to a process for preparing a crystal, to the use of structural coordinates of a crystal comprising the epitope binding fragment of an antibody bound to a peptide, to mimics of the antibody and peptide, to products recognisable by mimics of the antibody or which recognise mimics of the peptide, to engineered antibodies and to their use in diagnosis or therapy. Introduction The monoclonal antibody SM3 (secreted by the hybridoma HSM3 deposited with ECACC on 7 January 1987 under accession no. 87010701) binds to a tumour associated epitope on the epithelial mucin MUCl ( O-A- 88/05054, WO 90/05142) . The MUCl epithelial mucin is a transmembrane glycoprotein with the extracellular domain made up largely of exact tandem repeats of 20 amino acids, each of which contains five potential glycosylation sites (Gendler et al . 1988, 1990; see Figure 1). In breast and other carcinomas MUCl is over-expressed and is aberrantly glycosylated making it antigenically distinct from the normally processed mucin. In breast cancers, the 0- glycans which are added are shorter (Hanish et al . , 1989; Hull et al . , 1989; Lloyd et al . , 1996), resulting in the exposure of epitopes which are normally masked on the core protein (Burchell and Taylor-Papadimitriou, 1993). Such epitopes are called cryptic epitopes. The SM3 antibody was raised against MUCl stripped of its carbohydrate (Burchell et al . , 1987). SM3 recognises such a cryptic epitope, and shows high selectivity in reacting specifically with the carcinoma associated mucin in more than 90% of breast carcinomas (Girling et al . , 1989) . The high specificity of the SM3 antibody makes it a potentially useful tool in the diagnosis and treatment of breast cancer (Granowska et al . , 1996). The sequence of the repeating unit of the core protein of MUCl contains doublets of threonine and serine, bounding a highly immunogenic domain (Burchell et al . , 1989; see Figure 1). A three-dimensional NMR structure for three multiple MUCl peptide repeats reveals repeating "knob-like" structures, corresponding to the immunogenic domains which are connected by extended spacers (Fontenot et al . , 1995). The epitope for SM3 has been mapped using overlapping peptides and found to correspond to just five contiguous amino acids, Pro-Asp- Thr-Arg-Pro (Burchell et al . , 1989, hereafter referred to as the MUCl epitope) lying within the "knob-like" domain and between the potential serine and threonine glycosylation sites. In vi tro studies using recombinant GalNAc transferase which adds the first sugar to Ser or Thr suggest that Thr 1 Ser 12 and Thr 13 are glycosylated, while Thr 6 (within the MUCl epitope) and Ser 2 are not (Wandall et al . , 1997). The inventors have crystallised a fragment of SM3 bound to a peptide, subjected the crystal to X-ray diffraction studies and measured the structure factors. From the structure factors they have solved the structural coordinates. These may be used to generate new diagnostic and therapeutic materials and for other investigative purposes . The invention includes the use of the structure factors and/or structural coordinates to identify, characterise, design or screen chemical entities, which have uses in diagnosis and therapy, as will be discussed below. In one aspect the present invention provides the use of the structure factors and/or structural coordinates obtainable by subjecting a crystal comprising at least the epitope binding fragment of the SM3 antibody, bound to a peptide recognised by the epitope binding site of SM3 to X-ray diffraction measurements and optionally thereafter analysing the diffraction measurements to deduce structural coordinates. The invention particularly provides a use of the structural coordinates of a moiety which comprises at least the epitope binding fragment of the SM3 antibody or a substantially similar fragment bound to a peptide such as the crystal peptide. The moiety may be whole SM3 antibody, or a Fab fragment derived from the digestion of whole SM3 antibody by papain. The moiety may comprise a modified form of whole SM3 or a modified form of a fragment of SM3. Such modifications include the insertion or deletion of amino acids, or replacement of amino acids by other amino acids. Other chemical modifications may be made. The peptide may comprise the sequence Pro-Asp-Thr- Arg-Pro, or any longer portion of the MUCl tandem repeat, for instance the sequence Thr-Ser-Ala-Pro-Asp-Thr-Arg- Pro-Ala-Pro-Gly-Ser-Thr . The invention provides the use of the structure factors and/or structural coordinates of a crystal of the Fab fragment of SM3 bound to the crystal peptide. The structure factors of such a crystal obtained as in the Examples are shown in Table 1 and the structural coordinates are shown in Tables 2a and 2b. The structural coordinates shown in each of Tables 2a and 2b are derived from the structure factors . However the coordinates shown in Table 2b have been calculated to a higher refinement and include additional protein atoms. The invention provides the use of the structural coordinates shown in Table 2a and/or Table 2b. The structural coordinates indicate the positions of individual atoms within the crystal and indicate the B factor for each atom which gives some information about the mobility of the atoms. The structure factors may be used to derive additional information about the mobility of any individual atom or group of atoms within the crystal. This additional information, for instance, anisotropic B factors, may concern the direction of movement possible for each atom. The structure factors and structural coordinates thus give an indication of the available space for adjusting the position of individual atoms when designing mimics of the peptide or antibody. Mimics of SM3 The invention provides the use of structure factors and/or structural coordinates to identify, characterise, design or screen mimics of SM3. The structural coordinates allow the epitope binding site bound to the peptide to be shown as a two dimensional representation, for example as in the LIGPLOTs of Figures 8 to 11 or a three dimensional representation by physical models or as displayed on a computer screen. Such representation can be used to design modifications of SM3. Such modifications includes modifications to increase the avidity of the epitope binding site for the bound peptide. This modification may preferentially increase the avidity of the epitope binding site for abnormally glycosylated MUCl. The avidity may be increased by modifying the epitope binding site structure to increase the amount and number of interactions favourable to peptide binding and/or diminish unfavourable interactions between the peptide and antibody. Favourable interactions may be increased by extending the structure of the epitope binding site into spaces which are shown in the two dimensional or three dimensional representations to be unoccupied or filled with water molecules . Such water molecules may include those which are shown in Figures 8 to 11. The representations of the structures may be used in other ways to modify the structure of SM3. It is believed that SM3 may bind the peptide by an "induced fit" method which requires that conformation changes occur in the structure of SM3 during the process of binding the peptide. The SM3 binding site, or other parts of SM3 may be modified to allow such changes to occur more easily. Alternatively the mimic of SM3 may comprise the SM3 epitope binding site constrained in the conformation it adopts when it binds the peptide. The representations of the epitope binding site may be used to model such constraints by the putative introduction of covalent bonds between the atoms of SM3 which come close together when SM3 binds the peptide; one or more chemical linkers may be used between atoms of SM3 to constrain the epitope binding site to the required conformation, and/or one or more amino acids of SM3 may be replaced by analogues of the natural amino acids which help to constrain the conformation of the epitope binding site. On the basis of such modelling SM3 mimics may be identified, characterised, designed or screened. It is believed that the reason why SM3 has a low avidity for aberrantly glycosylated MUCl is steric hindrance between residues close to or in the epitope binding site and carbohydrate moieties attached to positions 1, 12 and 13 of the peptide as shown in Figure 1. The representation of the epitope binding site bound to the peptide may be used to predict which residues of SM3 are likely to be involved in the steric hindrance. One such residue may be Proline 56 of SM3. Such residues may be modified, replaced or deleted to decrease the steric hindrance in order to increase avidity. Mimics of SM3 may for instance be obtained by computer modelling techniques . Using the structural coordinates a three dimensional representation of the surface of the epitope binding site bound to the peptide can be produced using Catalyst Software such as Catalyst/SHAPE, Catalyst/COMPARE, DBServer HipHop Ludi, MCSS and Hook which are available from Molecular Simulations Ltd., 240/250 The Quorum, Barnwell Road, Cambridge, England. Mimics of SM3 can be produced either by computationally identifying compounds which have a similar surface to the binding site of SM3, or by computationally designing compounds with surfaces which are likely to bind the peptide. Various methods can then be used to produce a three dimensional surface which is the same or similar to the epitope binding surface. Based on this shape, packages such as Catalyst/SHAPE and Catalyst/COMPARE can be used to select compounds from databases which have a similar three dimensional shape to the epitope binding site. The epitope binding site surface may be described in more detail by analysis of the functional groups present to produce a pharmacophore . Based on a pharmacophore, packages such as DBServerl and HipHop can be used to search databases for compounds whose surfaces are described by similar pharmacophores . The databases that can be searched include ACD, NCI, Maybridge, Derwent World Index and BioByte . Packages such as Ludi and MCSS can be used to select fragments or chemical entities from databases which can then be positioned in a variety of orientations, or "docked" with the surface of the peptide. Once suitable chemical entities or fragments which bind sites on the surface of the peptide have been identified bridging fragments and framework structure are chosen with the correct size and geometry to support the che ical entities and fragments in the favourable orientation and location and to form the mimic of SM3. Packages such as Hook can be used to select framework structures . Once a candidate mimic of SM3 has been designed or selected by the above methods, the efficiency with which that mimic may bind to the peptide may be tested and optimized using computational or experimental evaluation. Various parameters can be optimized depending on the desired result. These include, but are not limited to, specificity, avidity, on/off rates, and other characteristics readily identifiable by the skilled artisan . The computational means may employ packages such as Catalyst/SHAPE, Catalyst/COMPARE, DBServer, HipHop, Ludi and MCSS to evaluate selected candidate SM3 mimics. The experimental means may comprise ELISA methods such as detailed below using GST-MUC1 ELISA plates or the techniques described in Bynum et al . Thus, one may optionally make substitutions, deletions, or insertions in some of the components of the SM3 mimics in order to improve or modify the binding properties. Generally, initial substitutions are conservative, i.e. the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original component. Such modified mimics can be computationally or experimentally evaluated in the same manner as the first candidate SM3 mimics, and if necessary further modifications can be made. This process of evaluating and modifying may be iterated any number of times . The term aberrantly glycosylated MUCl is used throughout this specification to refer to MUCl which has a different level of glycosylation than is normally found on MUCl from a particular tissue. The different level of glycosylation may be a decrease in the level of glycosylation. MUCl with such decreased levels of glycosylation may be produced by a tumour cell, such as an adenocarcinoma cell for instance a cell from an epithelial tumour of colon, lung, ovary, pancreas or especially a breast tumour cell. Mimics of SM3 preferably have a high avidity for aberrantly glycosylated MUCl. Such an avidity may be higher than that of SM3. They may have a higher selectivity towards aberrantly glycosylated MUCl in preference to normally glycosylated MUCl than SM3. The avidity of the mimic of SM3 to bind aberrantly glycosylated MUCl can be tested in an ELISA assay as detailed below: GST-Muc-1 ELISA Method Preparation of GST-Muc-1 Batch 5 ELISA plate. DNA coding for the seven tandem repeats of the 20 amino acid peptide epitope was cloned into a GST fusion vector, pGEX-2T (Pharmacia) in the E.Coli strain TGI . The cells were grown in L broth (lOOmg/ml ampicillin) overnight and then IPTG was added to a final concentration of 0.5 mM followed by a further incubation of 4 hr at 37 C The cells were pelleted (20min/10000rpm) , washed x2 with PBSa and resuspended in 25mM TRIS pH 8, 25mM Glucose, 10 mM EDTA containing lyzozyme (4mg/ml) and left for 30 min at RT . 5ml of lysis buffer was then added and incubated on ice for 5 min. After centrifugation the supernatant was loaded onto a Glutathione Sepharose 4B column (Pharmacia) equilibrated in lysis buffer. The fusion protein product was eluted in PBSa/15mM Glutathione and stored at 4 C until required. SDS-PAGE and FPLC Superose 6 (Pharmacia) size separation showed a single species mwt 43 K. Preparation of GST-Muc-1 Batch 5 ELISA Plates The GST-Muc-1 was diluted in PBSa to 50mg/ml and 50ml added to each well of a 96 well plate The plates were incubated overnight at 4 C, blocked with 200ml 2% BSA/PBSa for 2 hr at RT . and stored at -70 C until required . REAGENTS/BUFFERS Alkaline Phosphatase -Goat anti-mouse (Fc Specific) Sigma No. A-2429 BSA - Albumin Bovine, Fraction V powder, RIA grade, Sigma No A-7888 ELISA Plates - Nunc-Immuno Plates No. 442404 ELISA Substrate Buffer - Diethanolamine buffer pH 9-8 400ml Diethanolamine (Sigma D-2286) 24.5 mg MgC12 BHD (Anala R) pH 9.8 with HCl and make up to 500ml with distilled water EDTA Ethylenediamine tetra acetic acid BDH Anala R Glutathione Reduced ICN 101814 IPTG Isopropylthio-b-D-galactoside Promega Lysis Buffer 150mM NaCl, 16 mM Na2HP04, 4mM NaH2P04, lOOmM EDTA, 1% Triton X (BDH Anala R) 2 mM PMSF (Phenylmethylsulfonyl fluoride) (Sigma ) pNPP - p-Nitrophenyl Phosphate Sigma No. N-9389 PBSAa- Phosphate Buffered Saline (ICRF) TWEEN 20 - Polyoxyethylene (20) Sorbitan monolaurate BDH 66368 GST-Muc-1 (a Glutathione-S-transferase fusion protein containing seven copies of the 20 amino acid tandem repeat (non-glycosylated) ELISA plates are stored @ -70°C pre blocked with 2% BSA/PBSA. (PBSA- Phosphate Buffered Saline BSA- Bovine Serum Albumin, Fraction V powder, RIA grade, Sigma No. A-7888.) 1. Thaw out a plate at room temperature (RT) . 2. Test antibody samples are diluted in PBSA/ 0.02% Tween 20 (PBSA/T). e.g. SM3 from 100-0.001 mg/ml. 3. Wash the plate three times with PBSA/T. Add samples in a volume of 50 ml, in triplicate and leave at RT for 1 hour. 4. Remove the antibody samples carefully by aspiration and add 200 ml of PBSA/T to each well. Remove by aspiration and repeat. Then wash again twice with PBSA/T. 5. Add 50 ml of 1/2000 (diluted PBSA/T) Goat anti-mouse (Fc Specific) Alkaline Phosphatase (Sigma No. A-24209) to each well and incubate at R . for 1 hour. 6. Wash the plate three times with PBSA/T and then add 50ml of substrate which is p-Dinitrophenyl Phosphate (Sigma N-2765) at lmg/ml in Diethanolamine Buffer pH 9.8, (400ml distilled water, 48ml diethanolamine, 24.5mg MgCl 2 , pH 9.8 with HCl and make up to 500ml with distilled water) . 7. Incubate at RT . for 15 min and read the OD at 405 nm on the Labsystems Multiscan Plate reader. The avidity of the mimic of SM3 can also be measured using methods described in Bynum et al . These techniques may also be used to test the specificity of the mimic of SM3 by testing the avidity of the mimic for aberrantly glycosylated MUCl and for normally glycosylation MUCl. A histological screen using the mimic of SM3 can be performed using tumour tissue from a breast tumour and normal tissue, for example, as described in Girling et al . , 1989. This can be used to determine if the mimic is specific for the aberrantly glycosylated MUCl and therefore suitable for use in a method of diagnosing breast cancer. The mimic can also be tested against live tumour cells which are not fixed. Cells which have MUCl with reduced levels of glycosylation can be produced by the use of metabolic inhibitors of O-linked chain extension, such as 0- benzylgalactosamine . Such cells can be used to study the effects of low levels of glycosylation of MUCl on the avidity of the mimics of SM3. Mimics of SM3 may be used in a diagnostic test to detect the presence of tumour cells in a tissue sample, for example in a histological screening. Mimics used in this manner may be labelled with a detectable label. Alternatively agents able to specifically bind such mimics may be used to detect the presence of the mimics once the mimics have bound the aberrantly glycosylated. The mimics of SM3 may be used in vivo for the detection of tumour cells. They may be used in tumour imaging in vivo . Generally, such mimics would be labelled with a detectable label. The mimics of SM3 can be used in a method of therapy against cancer, particularly adenocarcinomas such as ovary, colon, lung, pancreas and breast epithelial cancers, especially breast cancers. Mimics which are antibodies or substantially similar to antibodies or fragments of antibodies may bind to aberrantly glycosylated MUCl on the surface of tumour cells and aid the killing of the tumour cells by recruiting the patients immune system. Mimics of SM3 may be chemically linked to a cytotoxic agents such as a toxin or a radioisotope . Binding of such toxin linked mimics to the tumour cells would lead to the killing of the tumour cell. It is believed that high levels of MUCl or aberrantly glycosylated forms of MUCl may have an immunosuppressive effect. Tumour cells may have high levels of MUCl on their surface and/or aberrantly glycosylated forms. Therefore in the method of therapy of the invention a mimic of SM3 could be used to bind to MUCl in vivo and prevent or decrease its immunosuppressive effects. The types of immunosuppressive effects that may be prevented or decreased are discussed below in relation to mimics of the MUCl epitope. Such a mimic could be administered in conjunction with an anti- tumour agent, such as an anti-tumour vaccine, and may have an adjuvant-like effect (the mimic may increase the immune response generated by the vaccine) . The anti- tumour agent could be a mimic of the SM3 epitope. The mimic of SM3 could be administered at any time in relation to the administration of the anti-tumour agent, for example before, with or after the administration of the anti-tumour agent. Thus the invention provides a mimic of SM3 for use in a method for treatment of the human or animal body by surgery or therapy or in a diagnostic method practised on the human or animal body, such as in anti-cancer therapy. The invention also provides a product comprising a mimic of SM3 and an anti-tumour agent as a combined preparation for simultaneous, separate or sequential use in anti- cancer therapy. The invention provides a use of a mimic of SM3 in the production of a pharmaceutical composition for use in the methods discussed above. The invention provides a pharmaceutical composition containing a mimic of SM3 and a diluent or carrier. The invention provides a method of treating or diagnosing cancer by administering to a human or non-human animal in need thereof an effective non- toxic amount of a mimic of SM3. The production of mimics of SM3 and the methods, routes and dosages for use of the mimics of SM3 are discussed below. Mimics of MUCl epitope peptides The invention allows the use of the structure factors and the structural coordinates to identify, characterise or design a mimic of the MUCl epitope peptides. Such a mimic may be used to produce a specific binding agent which has a desired association with aberrantly glycosylated MUCl. The mimic of the peptide can be used to select a specific binding agent from a library on the basis of its affinity to the mimic. Such a library may be a microbial display library, such as a phage display library. The specific binding agent may bind aberrantly glycosylated MUCl, and therefore be used in a similar manner to the mimics of SM3. The mimic of the peptide may be used in a vaccine administered to a human or animal. Such a vaccine would stimulate the production of antibodies able to bind aberrantly glycosylated MUCl. Such a vaccine could therefore be used as a therapy against cancer, for example to prevent or treat cancer. Thus the invention provides a mimic of the MUCl epitope, a mimic of the MUCl epitope for use a method for treatment of the human or animal body by surgery or therapy or in a diagnostic method practised on the human or animal body, such as in anti-cancer therapy. The invention also provides a use of such a mimic in the production of a pharmaceutical composition for use in such a method. The invention provides a pharmaceutical composition containing a mimic of the MUCl epitope and a diluent or carrier therefor. The invention provides a method of diagnosing or treating cancer by administrating an effective non-toxic amount of a mimic of the MUCl epitope to a human or non-human animal in need thereof. The production of mimics of the MUCl epitope and methods, routes and dosages for use of the mimics of the MUCl epitope are discussed below. The MUCl epitope mimics may also be administered to an animal preferably a laboratory mammal, such as a rodent, for instance a mouse, in order to induce an antibody response. Antibody secreting cells may be recovered from the animal and hybridoma technology may then be used to produce a hybridoma using such recovered cells. The hybridoma or any other antibody expression system would be a source of monoclonal antibodies capable of recognising the mimic and preferably the MUCl epitope and thus have diagnostic and therapeutic utilities as for the SM3 mimics described above. As described above it is believed that MUCl may cause immunosuppressive effects. Thus the mimic of the epitope may be capable of causing an immunosuppressive effect, and thus may be used to cause such an effect in a human or animal. The immunosuppressive effect may be caused by the mimic decreasing the activity of T cells, such as CD4 or CD8 T cells. The T cells may be polyclonal . The mimic may cause a decrease in (i)the proliferation of the T cells, (ii) their secretion of cytokines, (iii) their interaction with other cells, such as interaction mediated by ICAM-1 on the T cell surface, and/or (iv) their cytotoxic activity. The mimic may cause the cross-linking of a surface molecule on the T cells, such as ICAM-1. The mimic may cause T cells to become anergic. The effects of the mimic may be reversible by the addition of IL-2 or anti-CD28 antibody. Thus the mimic may be used to decrease or prevent an immune response, particularly when the response has a deleterious effect on the body. Thus the mimic may be used in the therapy (i.e. to treat or prevent) of diseases caused by autoimmune responses (such as arthritis, multiple sclerosis, asthma or diabetes), allergies, inflammatory disorders or transplant rejections, such as graft versus host disease. Thus the invention provides a mimic of the MUCl epitope for use in therapy which prevents or decreases an immune response, and so can treat or prevent a disease caused by an immune response. The invention also provides a use of such a mimic in the production of a pharmaceutical composition for use in such a method. The invention provides a method of treating a disease caused by an immune response, such as autoimmune disease, allergy, inflammatory disorder or transplant rejection; by administrating an effective non-toxic amount of a mimic of the MUCl epitope to a human or non-human animal in need thereof. As with the mimics of SM3 the two dimensional and three dimensional representations of the epitope binding site bound to the peptide mentioned previously can be used to design a mimic which is, for instance, a peptide or a derivative thereof or an analogue of a peptide comprising the sequence Pro-Asp-Thr-Arg-Pro or the sequence Thr-Ser-Ala-Pro-Asp-Thr-Arg-Pro-Ala-Pro-Gly-Ser constrained in the conformation approximately that which the crystal peptide adopts when bound to SM3. The sequence can be constrained by the introduction of covalent bonds between atoms which come close together in the conformation adopted when bound to SM3. Alternatively a chemical linker may be used to join such atoms together. The sequences may be constrained by cyclisation of a peptide in which the relevant sequence is present. The peptides may also be constrained by replacement of one or more amino acids by analogues of natural amino acids which cause the peptide analogue to adopt the required conformation when they are introduced. Hydrogen bonds, such as intra-peptide hydrogen bonds may be introduced into the mimic. These may help to constrain the mimic to a particular conformation, such as the conformation adopted when bound to SM3. The structural coordinates allow the epitope binding site bound to the crystal peptide to be shown as a two dimensional representation, for example the LIGPLOTs of Figures 8 to 11 or a three dimensional representation on a computer screen. Such representation can be used to design modifications to the MUCl epitope which may increase its avidity for SM3, for example, by increasing the "on rate" relative to the crystal peptide and decreasing the "off rate" . The avidity of the MUCl epitope mimic for the epitope binding site may be increased using a similar strategy as used to design mimics of SM3. The mimic can be modified to increase the amount and number of favourable interactions with SM3, for example by extending the structure of the MUCl epitope into spaces which are shown to be unoccupied or filled with water molecules. Such water molecules may include those shown in Figures 8 to 11. It is appreciated that such mimics of the MUCl epitope which are designed to have an increased avidity with the epitope binding site of SM3 may not cause the production of antibodies with a higher avidity to aberrantly glycosylated MUCl than SM3 has, however such mimics may lead to the stimulation of an increased antibody response due to their higher avidity to the antibody. The two dimensional and three dimensional representation of the epitope binding site bound to the crystal peptide can as mentioned previously be used to determine why SM3 binds the peptide with a low avidity. This information can then be used to design mimics of the MUCl epitope which can select from a library those mimics of SM3 which have a high avidity to aberrantly glycosylated MUCl. Such mimics, when administered in a vaccine may also stimulate the production of antibodies with a higher avidity to aberrantly glycosylated MUCl than SM3. Such mimics of the MUCl epitope may for example be designed by modifying the structure of the crystal peptide which binds SM3 in those areas where unfavourable interactions occur between the crystal peptide and epitope binding site which cause a lowering of avidity. For example the structure of the MUCl epitope may be extended in those areas where steric hinderance occurs between the carbohydrates on the aberrantly glycosylated MUCl and the epitope binding site. Use of such a mimic may lead to the selection of specific binding agents (as described above) from a library or the stimulation of antibodies which have a reduced level of steric hinderance with the carbohydrate and therefore a higher avidity for aberrantly glycosylated MUCl. Mimics of the MUCl epitope may be designed by computer modelling techniques in a similar manner to the designing of mimics of SM3 using these techniques. Again, packages such as Catalyst/SHAPE and Catalyst/COMPARE can be used to select compounds with a similar three dimensional shape to the peptide when it is bound to SM3. Packages such as DBServer and HipHop can be used to find compounds with similar pharmacophores to the peptide and packages such as Ludi, MCSS and Hook can be used to design a mimic which is predicted to bind well to the epitope binding site of SM3. Once a candidate mimic has been designed or selected by the above methods, the efficiency with which that mimic may bind to the SM3 epitope binding site may be tested and optimized using computational or experimental evaluation. As described previously packages such as Catalyst/SHAPE, Catalyst/COMPARE, DBServer, Ludi and MCSS may be used to computationally evaluate the mimic. The mimic may be experimentally evaluated in the competition ELISA assay described below. Various parameters can be optimized depending on the desired result. These include, but are not limited to, specificity, avidity, on/off rates, and other characteristics readily identifiable by the skilled artisan . Thus, one may optionally make substitutions, deletions, or insertions in some of the components of the MUCl epitope in order to improve or modify the binding properties. Generally, initial substitutions are conservative, i.e. the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original component. As with the mimic of SM3 the process of evaluation and modification can be iterated any number of times. The mimic of the MUCl epitope may be glycosylated. The mimic may have an intra-peptide hydrogen bond. This may be between the residues equivalent to Pro 4 and Thr 6 of the MUCl epitope or between the residues equivalent to Asp 5 and Arg 7. The atoms involved in the hydrogen bond may be the equivalent of Pro 4 (atom 0) , Thr 6 (atom N) , Asp 5 (atom OD1) and/or Arg 7 (atom N) . The mimic of the MUCl epitope may have higher avidity to SM3 than aberrantly glycosylated MUCl, or a low avidity or may not bind at all. The avidity of the mimic can be tested in a competition ELISA assay in which a MUCl peptide such as aberrantly glycosylated MUCl, deglycosylated MUCl or the fully stripped core protein or a fragment thereof is attached to the plate and SM3 is added in the presence of the mimic of the MUCl epitope. By measuring the ability of the mimic to inhibit the binding of the antibody to the MUCl peptide the avidity of the mimic for SM3 can be measured. Preferred mimics include those which lead to the selection of specific binding agents from a library which bind aberrantly glycosylated MUCl with a higher avidity and/or higher selectivity than SM3. Preferred mimics of the MUCl epitope are also those which stimulate the production of antibodies in vivo which have a higher affinity than SM3. As discussed above specific binding agents include those which have been selected from a library, which may include antibodies, or those antibodies produced by B cells which bind the mimic of the peptide. Preferred specific binding agents are those which bind aberrantly glycosylated MUCl with an avidity and/or specificity higher than SM3. The specific binding agents may be used in a diagnostic test to detect the presence of tumour cells in a tissue sample, for example in a histological screening. Specific binding agents used in this manner may be labelled with a detectable label. Alternatively moieties able to specifically bind such mimics may be used to detect the presence of the specific binding agents once the specific binding agents have bound the aberrantly glycosylated. The specific binding agents may be used in vivo for the detection of tumour cells. They may be used in tumour imaging in vivo . Generally, such specific binding agents would be labelled with a detectable label. The specific binding agents may be used to prevent or decrease immunosuppression caused by MUCl. The specific binding agents can be used in a method of therapy against cancer, particularly breast cancer. Specific binding agents which are antibodies or substantially similar to antibodies or fragments of antibodies may bind to aberrantly glycosylated MUCl on the surface of tumour cells and aid the killing of the tumour cells by the immune system. Specific binding agents may be chemically linked to a cytotoxic agents such as a toxin or a radioisotope . Binding of such toxin linked specific binding agents to the tumour cells would lead the killing of the tumour cell . Thus the invention provides a specific binding agent for use a method for treatment of the human or animal body by surgery or therapy or in a diagnostic method practised on the human or animal body, such as in anti-cancer therapy. The invention also provides a use of a specific binding agent in the production of a pharmaceutical composition for use in such a method. The invention provides a pharmaceutical composition containing a specific binding agent and a diluent or carrier therefor. The invention also provides a method of diagnosing or treating cancer by administering an effective non-toxic amount of a specific binding agent to a human or non-human animal in need thereof. The invention also provides a product comprising a specific binding agent and an anti-tumour agent as a combined preparation for simultaneous, separate or sequential use in anti-cancer therapy. The production of such specific binding agents and of the MUCl epitope mimics and methods, routes and dosages for use of the agents and mimics are discussed below. When administered to an animal or human the mimic of SM3 may lead to the production of antibodies which recognise the mimic. B cells from the animal or human may be used in conjunction with hybridoma technology to produce such antibodies as monoclonal antibodies. Such antibodies may have a epitope binding site which is similar in shape to the crystal peptide. The administration of such antibodies to an animal or human may lead to the production of antibodies which recognise aberrantly glycosylated MUCl. Therefore the antibodies which recognise SM3 may be used as a vaccine or may be used to produce a vaccine against cancer. The antibodies or fragments thereof which recognise aberrantly glycosylated MUCl produced in response to the anti-mimic of SM3 antibody may themselves be used in an anti-cancer treatment or in a diagnostic method. Thus the invention also provides such an antibody or fragment thereof for use in a method for treatment of the human or animal body by surgery or therapy or in a diagnostic method practised on the human or animal body, such as in anti-cancer therapy. The invention also provides use of such an antibody or fragment thereof in the production of a pharmaceutical composition for use in such a method. The invention provides a pharmaceutical composition containing such an antibody or fragment thereof and a diluent or carrier therefor. The invention also provides a method of diagnosing or treating cancer by administering an effective non-toxic amount of such an antibody or fragment thereof to a human or non-human animal in need thereof. The invention provides the use of H3 chain of SM3 as a therapeutic or diagnostic agent. The invention also provides the use of HI chain of SM3 as a therapeutic or diagnostic agent. Thus the invention also provides such an H3 or HI chain for use in a method for treatment of the human or animal body by surgery or therapy or in a diagnostic method practised on the human or animal body, such as in anti-cancer therapy. The invention also provides use of such an Hi or H3 chain in the production of a pharmaceutical composition for use in such a method. The invention provides a pharmaceutical composition containing such an HI or H3 chain and a diluent or carrier therefor. The invention also provides a method of diagnosing or treating cancer by administering an effective non-toxic amount of such an HI or H3 chain to a human or non-human animal in need thereof. The invention provides the use of the structure factors and/or structural coordinates to solve structural coordinates of other crystals. Such a crystal may comprise an antibody or antibody fragment. In particular the structural coordinates can be used to solve the structural coordinates of a crystal comprising an antibody which has a non-proline cis peptide bond. The cis peptide bond may be in the H3 chain of the antibody. The invention provides the use of the structure factors and/or structural coordinates to engineer, design or modify an antibody. The engineering may be for the purpose of humanising the antibody. The engineering may comprise the replacement of portions of the antibody. The portions of the antibody may be replaced with portions from another protein, such as a human protein, for instance a human antibody. Two dimensional and three dimensional representations, such as those discussed previously, may be used during the engineering of the antibody to ensure that the epitope binding site of the antibody is the same or substantially similar to the antibody binding site of SM3. The engineering of the antibody may be for the purpose of increasing the contribution made by the H3 and HI chains in the binding of the epitope. The invention provides the use of an engineered glycine in a protein to insert a non-proline cis peptide bond into the protein. The insertion of the glycine may enable the protein to undergo conformational change, for instance in connection with a specific binding reaction where the affinity, avidity or selectivity of the specific binding reaction is modified by adoption of a cis peptide bond adjacent to the engineered glycine. The engineered glycine can be inserted using site directed mutation techniques, such as those described in Short Protocols in Molecular Biology, 3rd edition, published by John Wiley and Sons, Inc., USA. The protein may be an antibody or fragment of a antibody. The engineered glycine may be in a CDR loop of the antibody. The insertion of the engineered glycine in an antibody will generally affect the binding of the antibody to an epitope . The invention also provides a method of producing a crystal which comprises the use of cadmium. Generally the method comprises contacting any one of the moieties to be crystallised with cadmium such as by use of a solution of a cadmium salt. The cadmium ions may be present in the solution in which the crystal is grown. In the case where the mimic of SM3, the mimic of the MUCl epitope or the specific binding agent comprise a peptide then such agents may be delivered to animal or human by the admimistration of a nucleic acid which encodes such a peptide. Transcription and translation or merely translation of the nucleic acid would lead to the production of the peptide in vivo. It is appreciated by the skilled artisan that the nucleic acid may be within a suitable vector, especially an expression vector, for instance a virus or an organism which is administered, such as a Vaccinia virus, for instance an attenuated Vaccinia virus or the nucleic acid may be administered in the presence of a suitable diluent or carrier as in the use of "naked DNA" . Nucleic acids encoding such peptides form a further aspect of the present invention as do their uses in cancer therapy and pharmaceutical compositions containing them. Thus the invention also provides such nucleic acids for use in a method for treatment of the human or animal body by surgery or therapy or in a diagnostic method practised on the human or animal body, such as in anti- cancer therapy. The invention also provides use of such nucleic acids in the production of a pharmaceutical composition for use in such a method. The invention provides a pharmaceutical composition containing such nucleic acids and a diluent or carrier therefor. The invention also provides a method of diagnosing or treating cancer by administering an effective non-toxic amount of such nucleic acids to a human or non-human animal in need thereof. The mimic of SM3 , mimics of the MUCl epitope, selective binding agents, nucleic acids, viruses or organisms containing nucleic acids of the invention (hereafter referred to as substances of the invention) may be formulated for clinical administration by mixing them with a pharmaceutically acceptable carrier or diluent. For example the substances can be formulated for topical, parenteral, intravenous, intramuscular, subcutaneous, or transdermal administration. They may be mixed with any vehicle, e.g. a diluent or carrier which is pharmaceutically acceptable and appropriate for the desired route of administration. The pharmaceutical carrier or diluent for injection may be, for example, a sterile or isotonic solution such as Water for Injection or physiological saline. The dose may be adjusted to deliver an effective non-toxic amount and according to various parameters, especially according to the nature and efficacy of the substance used; the age, weight and condition of the patient to be treated; the mode of administration used; the conditions to be treated; and the required clinical regimen. As a guide, the amount of therapeutic substance such as a polypeptide to be administered by injection will generally be from 10 to lOOOμg. For instance 100 to 500μg. For in vivo diagnostic imaging purposes in particular, the dose will depend on similar factors but may need to be much larger in order to generate an appropriate image. The routes of administration and dosages described are intended only as a guide since a skilled practitioner will be able to determine readily the optimum route of administration and dosage for any particular patient and condition. The substances of the invention may be produced by conventional techniques well known to those skilled in the relevant arts. Peptides may be synthesised de novo or produced by transcription and translation of DNA or translation of RNA in a suitable expression system by conventional methods. Nucleic acids may be produced by de novo synthesis, obtained from natural sources such as by conventional probing and cloning techniques or generated from natural sources by modification by well known methods. Antibodies may be made by suitable immunisation protocols and purified from immunised animals by conventional techniques, or they may be made by hybridomas and similar antibody secreting cell lines cultured in vi tro or they may be obtained by expression from suitable nucleic acids. Hybridomas and other antibody secreting cells may be obtained, cultured and used to produce antibodies by conventional methods. Chemical modification of such materials as peptides and antibodies may be achieved by well known methods. Fragments of antibodies may be produced by known chemical or enzymatic digestions or by expression from suitably modified nucleic acids. New chemical entities such as mimics of the MUCl epitope may be produced by the well known techniques of synthetic organic chemistry. The substance of the invention does not include those peptides disclosed in WO-A-88/05054 or in WO-A- 90/05142. The present invention is illustrated by the figures of the accompanying drawings which are described below: Brief Description of the Drawings Figure 1 shows the amino acid sequence of the MUCl tandem repeat . Figures 2 and 3 show experimental electron density maps and the refined atomic models of the epitope binding site of SM3 and part of the crystal peptide. Figure 4 shows a comparison of the conformations of the unbound and bound peptide . Figures 5 and 6 show molecular surface features of the SM3-crystal peptide interaction. Figure 7 is a stereo view of the non-proline cis- peptide bond in CDR H3. Figures 8, 9, 10 and 11 are LIGPLOTs of the peptide binding site. Figure 12 shows experimental density maps of the cis- peptide conformation in H3. Figure 13 shows a Ramachandran plot for the H3 fragment . Figure 14 shows the main chain temperature factors of the fragment from H3. Figure 15 shows a stereo view of the MUCl peptide in the antibody combining site. Figure 16 shows a stereo view of the non-proline cis- peptide bond in H3. Detailed Description of the Drawings Figure 1 shows MUCl tandem repeat sequence written from N- to C-terminal using the Internationally recognised 3-letter code (which is used throughout this specification) . The epitope recognised by SM3 is shown in bold (Pro-Asp-Thr-Arg-Pro) with the immunodominant region indicated by the double headed arrow. The probable glycosylation sites are shown in bold italics. The peptide used for the crystallisation studies (Thr-Ser- Ala-Pro-Asp-Thr-Arg-Pro-Ala-Pro-Gly-Ser-Thr) is underlined (and is herein referred to as "the crystal peptide" ) . Figures 2 and 3 show experimental electron density maps and refined atomic models calculated using the o observed structure factors (30 to 1.95 A) and calculated phases after solvent modification. The maps are contoured at 1.0 σ. Figure 2 shows part of the MUCl peptide antigen showing the immunodominant region. The numbering refers to Figure 1. Figure 3 shows the cis- peptide bond in CDR H3 between residues Gly96H and Gln97H. Two water molecules are shown forming hydrogen bonds to amide nitrogens. Figure 4 shows the unbound and bound peptide. The unbound peptide is shown on the left. The structure represents the "knob-like" region and was determined in solution by NMR; it includes the whole of one tandem repeat and parts of the two flanking repeats (Fontenot et al . , 1995). The conformation of the crystal peptide as bound by SM3 is shown on the right. There appears to be a conformational transition of the "knob-like" region upon SM3 binding, which leads to a more extended peptide conformation. The main differences can be attributed to the Ψ angles of Asp5P and Arg7P. Figure 5 shows a CPK model of the SM3 combining site with the individual CDR loops labelled. The crystal peptide is shown contacting all of the CDR's except H2. Figure 6 shows electrostatic surface potential representation of the SM3 peptide complex. The surface was calculated using GRASP (Nicholls et al . , 1991). The crystal peptide is shown as a stick model. Figure 7 shows the cis-peptide bond in H3. The interactions between the residues Gly96H-Gln97 and the crystal peptide (solid) are shown. Hydrogen bonds are dotted (drawn using MOLSCRIPT; Kraulis, 1991) . Figures 8, 9, 10 and 11 are LIGPLOTS showing the main interactions which occur between the SM3 binding site, the crystal peptide and water molecules. KEY: Non-ligand residues involved in hydrophobic Hydrogen bond and its length " ' Corresponding atoms involved in hydrophobic contact(s) @ WAT = water Figure 12 shows experimental electron density maps calculated using the observed structure factors (30 to 1.95 A and calculated phases after solvent modification, contoured at 1.0 σ level (2Fo-Fc) and 2.0 σ (Fo-Fc). Residue numbering as in the text. The model with this cis - peptide bond is coloured according to atom type. (A) 2Fo-Fc difference density, calculated for the refined model with a trans Gly96H-Gln97H peptide bond. (B) 2Fo- Fc and Fo-Fc (residual negative electron density; and positive density) map, calculated for the refined model with a cis Gly96H-Gln97H peptide bond. (C) 2Fo-Fc difference electron density map around the final cis Gly96H-Gly97H fragment, showing the hydrogen bonds which appear to stabilise the cis - peptide conformation. Figure 13 shows a Ramachandran plot for the H3 fragment refined with cis and trans, Gly96H-Gly97H peptide bond. Residues are labelled accordingly. Created by PROCHECK, Laskowski et al . , 1993. Figure 14 shows the main chain temperature factors of the fragment from H3 which contains the non-proline cis- peptide bond between Gly96H and Gln97H. Values for the refined cis - confirmation are shown as open boxes (solid line), while those for the trans are indicated with closed circles (dashed line) . Figure 15 shows a view of the MUCl peptide in the antibody combining site. The peptide antigen is labelled and is shown in bold. SM3 Fab residues which interact with the peptide are labelled. Hydrogen bonds are shown as dotted lines with water molecules as black spheres. Drawn by MOLSCRIPT (Kraulis, 1991) . Figure 16 shows the cis peptide bond. The interactions between the residues Gly96H-Gln97H and part of the peptide antigen (bold) are shown. Hydrogen bonds are dotted and waters are represented as black spheres, (drawn using MOLSCRIPT; Kraulis, 1991) . The hydrogen bond between Gly96H (N) and the peptide antigen, as mediated via a water molecule, is lost for a trans - peptide conformation for Gly96H-Gln96H . The invention is further illustrated by the Examples : Example 1 Assessment of the Binding of the MUCl epitope to SM3. The sequence of the MUCl peptide in the context of the MUCl repeat is shown in Figure 1. The region of the MUCl repeat for the co-crystallisation studies was chosen to keep the peptide as soluble as possible, while maintaining most of the tertiary structure of the knob region as based upon the NMR structure of the mucin repeats [Fontenot, J.D., Mariappan, S.V.S., Catasti, P., Domenech, N., Finn, O.J. and Gupta, G.J. Biomol . Struct , and Dynam . 13, (1995) 245-260] . The binding of the MUCl epitope to SM3 was assessed by inhibition in an ELISA assay. The assay involved SM3 binding to a recombinant fusion protein containing seven copies of the MUCl tandem repeat, a lμg/ml concentration of SM3 was incubated with increasing concentrations of peptide, a 50% inhibition was achieved at a peptide concentration of approximately 30μg/ml (Apparent Ka~24μM) . In contrast a peptide of the same composition but different sequence (Ala-Arg-Pro-Thr- Gly-Thr-Ser-Asp-Pro-Thr-Pro-Ala-Ser) gave no detectable inhibition at the same concentration. Example 2 Preparation of the SM3 Fab fragments. SM3 at 4mg/ml in 100 mM sodium acetate pH 6.0, 3mM EDTA, 50mM cysteine was incubated with 160 μg/ml of papain for 4 hr at 37°C. Fabs were purified by gel filtration on Superose 6 in PBS, followed by dialysis into 20mM Tris pH 8.0 and then Mono Q ion exchange chromatography. Fractions were analyzed by SDS PAGE and Fab fractions concentrated to 4 mg/ml in lOmM Tris pH 8.0. The overall yield was 22%. Example 3 Crystallisation of the SM3 Fab fragment bound to the MUCl epitope. The SM3 Fab fragments were mixed with concentrated solution of the peptide at a molar ratio 1:5, incubated for 3 hours at 37°C, and then concentrated to 9.5 mg/ml. The crystallisation trials were conducted using the hanging drop method. A wide range of conditions were tested using commercial screens, namely Hampton Research I and II [Jancarik, J. and Kim, S.H. J. Appl . Cryst . 24, (1991) 409-411 and Cudney, R., Patel, S., Weisgraber K., Newhouse, Y., and McPherson, A. Acta Crys t . D50, (1994) 414-423] . Although the initial screens did not give crystals, they indicated that polyethylene glycol (PEG) was the most promising precipitant. In subsequent trials we varied the molecular weight of PEG, buffer pH range (4-9) and effect of salts. Finally, a shower of tiny needles appeared in the drops equilibrated against a solution of PEG 4000 as a precipitant and acetate buffer, pH 5.0-7.0, with aggregated prisms appearing at higher pH, 6.5-7.5. However, all of these original crystals were too small for data collection. As seeding attempts were unsuccessful, we tried other ways to improve the crystal morphology and size, including a metal ion screen. Addition of cadmium chloride gave larger crystals which were often twinned or aggregated. However, occasionally single crystals could be separated, one of which was used for data collection. The final conditions were; 2.5μl of the antibody-antigen complex mixed with 2.5μl of the well solution containing 0.2 M CdCl 2 , 19% w/v of PEG 4000, and 0.1 M acetate buffer, pH 6.0. Example 4 Diffraction measurements of the SM3 Fab fragment/MUCl epitope crystal. A monocrystal of dimensions 0.4 x 0.2 x 0.03 mm was used for the diffraction measurements at the Xll outstation of the DESY synchrotron in Hamburg. Analysis of the diffraction data showed that the crystal belongs to the monoclinic P2,_ space group with unit cell dimensions a=42.2, £>=83.9, c=64.5 A, and β=93.4°. Assuming one complex molecule per asymmetric unit, the o specific volume V ra =2.50 A 3 /Da of protein corresponds to a solvent content of 51% (Matthews, 1968). Since the number of available crystals was limited, data collection was carried out at 110 K. The crystal was transferred to a glycerol-enriched mother liquor (10% of the water in mother liquor was substituted by glycerol) and then flash-frozen using standard techniques (Teng, 1990) in a stream of nitrogen gas produced by an Oxford Cryosystem. A complete dataset up to 1.95 A resolution was collected using synchrotron radiation at wavelength 0.912 A (Table 3). The data was collected in 1.0° oscillation frames over 180° oscillation range on an 18cm MAR Research image plate from a single crystal. The frames were processed with DENZO software (Otwinowski, 1993) resulting in 111,363 observations with I>1.0 σ(I). Further scaling with the CCP4 suite gave 33,093 independent reflections with R merge of 6.9%. Example 5 Structure Determination and Model Refinement . The CCP4 package [Collaborative Computational Project, No. 4 Acta Crystallogr . D50, (1994) 760-763]. was used for all crystallographic calculations unless otherwise stated. The structure of the SM3-MUC1 peptide complex was solved by the Molecular Replacement method as implemented in the program AMoRe [Navazza, J. Acta Crystallogr . A50, (1994) 157-163], using the Murine SE155-4 Fab fragment complexed with the dodecasaccharide [Cygler, M., Rose, D.R. and Bundle, D.R. Science 253, (1991) 442-445] as a search model. A consistent solution for the rotation and translation function was obtained only after removing the bound antigen, CDRs and N- and C- termini . Replacing all non-conserved residues with alanines and performing rigid body refinement with X-PLOR [Brunger, A.T. (1992) X-PLOR, A System for Crystallography and NMR (Yale Univ. Press, New Haven, CT) Version 3.1] resulted in a crystallographic R-factor of 40%, with R-free of 49% as calculated against a randomly selected set of reflections [Brunger, A.T. Acta Crystallogr . D49, (1993) 24-36] . At this stage, several omit maps were calculated covering the whole molecule, and the model was manually rebuilt using the program 0 [Jones, T.A. and Kjeldgaard, M. (1994) 0 - The Manual. Uppsala University, Sweden] . Further refinement of the model was performed with the standard X-PLOR simulated annealing protocol with resolution cut-off at 3.0 A, followed by manual rebuilding with 0 and Turbo-Frodo [A. Russel and C. Cambillau, Marseille, France] . The R- factor converged to 34% (R-free 43%) and substantial, continuously positive, electron density close to the CDRs became visible which corresponded to residues 2-10 of the peptide. The peptide was built into the density and further alternative rounds of refinement, DM solvent modification [Cowtan, K. Protein Crystallography 31, (1994) 34-38] and manual rebuilding was carried out using REFMAC as implemented in the CCP4 package and X-PLOR, o gradually increasing the resolution to 1.95 A. Inspection of the 2Fo-Fc and Fo-Fc difference Fourier maps showed significant positive electron density corresponding to eight cadmium ions and a large number of solvent molecules. Several iterative refinement cycles were carried out, and the water and cadmium positions were checked after each cycle. All atoms were refined with individual isotropic B-factors. The Engh-Huber parameters [Engh, R.A. and Huber, R. (1991) Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr . A47, 392-400] as used in X-PLOR were altered to allow the Gly96H-Gln97H bond to adopt a cis conformation. No electron density was visible for residues 128-133 of heavy chain as well as some terminal residues (L2, L209-212, H214, PI and Pll- 13) . For the same reason residues Asp4lL, Glul23L, Glnl63L, GlnlH, Glu42H, Glu6lH, Glu85H, Serl34H, Serl60H, Serl72H, Aspl73H, Ser203H, Lys208H and Ser2P were modelled as Alanines. The final model contains 3227 atoms including the peptide, 333 water molecules, two chlorine and eight cadmium ions and the final refinement statistics are shown in Table 4. The overall quality of the model was checked with PROCHECK program. [Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M. J. Appl . Crystallogr . 26, (1993) 283-291]. Buried contact surface areas were calculated with the program PDBAREA [Lee et al.J. Mol. Biol (1971), 55, 379-400 ]. It was noted that during the refinement and manual rebuilding procedures, some of the SM3 primary sequence was incorrect. A cDNA corresponding the SM3 Fab region was sequenced confirming the errors in the SM3 sequence. The peptide was unambiguously built into the electron density from difference Fourier maps. Since the MUCl peptide is almost symmetrical, it was necessary to confirm the correct orientation for the peptide in the electron density. This was done by modelling the peptide backwards which resulted in a poorer fit into the density, and a higher R-Free and crystallographic R- factor after one round of refinement. The correctness of the cis-bond was confirmed by trying to refine it as a trans-bond. This resulted in a significant increase in main chain B-factors for Gly96H and subsequently poor quality electron density maps in this region (data not shown) . In addition, some potential hydrogen bonds between the peptide and antibody are not possible if the peptide bond is in trans conformation. Unrestrained refinement using REFMAC (CCP4, 1994) always resulted in a cis-conformation for the Gly96H-Gln97H peptide bond, the electron density for which is shown in Figure 3. Example 6 The SM3 Fab fragment/MUCl epitope structure. The structure of the SM3-peptide antigen complex has revealed a number of unexpected and new insights into how antibodies recognise peptide antigens. In particular CDR loop H3 contains a non-proline cis-peptide bond. The structure of the SM3 fab fragment/MUCl epitope was checked to a resolution of 1.95 A. All of the residues of the epitope lie within favoured regions of the Ramachandran plot (data not shown) except for two residues (Thr51L, Ser93L) on CDRs (L2 and L3) , both of which are involved in interactions with the bound peptide. The individual atomic B-factors are within o reasonable limits (average 16.3A 2 ), showing higher values only in residues located on mobile loops or solvent- exposed fragments (data not shown) . The quality of the density corresponding to nine residues of the MUCl peptide antigen is shown in Figure 2A. The peptide o residues have average atomic B-factors of 15.3A 2 indicating that the observed peptide is well ordered. There are eight cadmium sites in the SM3-peptide, five with full occupancy, and three with relative occupancy of 0.75. They are mainly making contacts with the nitrogen atoms of histidines and carboxylic group of Glu or Asp residues between symmetry related molecules and/or chains (data not shown) . All have distorted octahedral co-ordination completed by bound waters and chloride ions. It appears that the cadmium ions stabilise contacts between chains or molecules and contribute to the crystal packing since crystallisation in the absence of cadmium produces tiny needles, too small for diffraction experiments. The SM3-cadmium structure is an unusual example of a crystal structure in which cadmium ions were introduced directly and not simply by replacing other bound metal ions. SM3 - MUCl peptide antigen interactions The MUCl peptide forms two intra-peptide hydrogen bonds: Pro 4 (atom 0) to Thr 6 (atom N) and Asp 5 (atom OD1) to Arg 7 (atom N) . The MUCl peptide sits in an elongated groove of the SM3 antibody and is surrounded by all six CDR loops . The peptide is anchored by the electrostatic interactions of Asp5P and Arg7P and is bound to the SM3 antibody primarily by hydrophobic contacts (Table 4). All six CDRs of the SM3 antibody participate to some degree in the MUCl peptide binding, although of the residues on the H2 chain only Arg52H makes contact with the peptide, and this through a water mediated interaction. The major contribution to antigen binding comes from HI, of which three residues Asn31H, Tyr32H, Trp33H are making contacts with seven residues of the peptide (Table 4). These interactions cover 38% of the total CDRs surface area which is buried upon antibody-peptide binding, and are mainly hydrophobic, although there are some hydrogen bonds and salt bridges. The cis-peptide bond between Gly96H and Gln97H plays a crucial role in antigen binding (Table 4) . The nitrogen atom of Gly96H forms hydrogen bonds with both the carbonyl oxygen of Asp5P and the OD2 carboxyl group via a water molecule. The hydrophobic part of the Gln97H side chain interacts with Pro4P which is oriented between Trp33H (HI) and Tyr32L (LI) . Pro4P also stacks against Trp91L (L3) , making Pro4P the most buried residue of the whole peptide antigen. The polar headgroup of Gln97H hydrogen bonds directly with residues of LI, L2 and Asp5P. The important antigenic residue Arg7P interacts with Tyr32H (HI) and Asn31H (HI) whilst the C-terminal residues of the peptide sit in a hydrophobic pocket surrounded by Pro56L (L2) , Phe27H (HI) and Tyrl02H (H3) . In summary, there are a number of direct water-mediated hydrogen bonds between the peptide and antibody (Table 4). The rest of the SM3-peptide interactions are primarily hydrophobic. Hydrophobic contacts are dominant at the SM3 antibody combining face since out of a total 185 A 2 o antigen-antibody contact area, 128 A 2 is covered by hydrophobic interactions (Table 5) . A similarly high ratio is also observed for the peptide antigen where 66% of the buried surface area (total 603 A 2 ) is represented by non-polar residues. Such high ratios would suggest that hydrophobic interactions are the main driving force in SM3-peptide complex formation. The average Fab provides space for binding about 10 residues of peptide antigen, leaving the rest highly mobile and hence very often disordered and unobserved in electron density maps. There is a clear surface complementarity between the SM3 antibody and peptide antigen. Of particular interest is the surface complementarity around Pro4P which appears to be facilitated by the presence of the cis-peptide bond within H3 (see later) . A fragment search against a library of all antibody structures deposited in the Brookhaven database (Bernstein et al . , 1977) was unable to find a suitable replacement for H3. The best solution of the search, which used distances across the base of H3, placed the o fragment Ca atoms at 2.6 A root mean squared separation from the equivalent crystal structure co-ordinates of H3. However, it is well known that conformations of CDR H3 are difficult to classify and predict (Reczko et al . , 1995; Shirai et al . , 1996). In the SM3-peptide antigen structure, residues from CDRs HI and to a lesser extent H3 are the major contributors to the binding of peptide antigen (Table 4) . This is in contrast to other antibody-peptide complexes where L3 and H3 (MacCallum et al . , 1996) or H2 and H3 (Stanfield and Wilson, 1993) are the main contributors to antigen binding. One obvious conclusion from this is that it would be difficult to predict, without a crystal structure of a complex, the expected contributions of each of the CDRs to peptide antigen binding. The presence of non-proline cis-peptide bonds within proteins is very rare with an estimated 0.05% of known protein structures containing such bonds (Stewart et al . , 1990; Herzberg and Moult, 1991). To our knowledge, the SM3-peptide complex represents the first such example in a hypervariable loop region of an antibody combining site. Non-proline cis-peptide links have however, been found in the active sites of a number of hydrolases (Perrakis et al . , 1994). In these examples, the cis-peptide conformation is probably involved in facilitating contact and/or recognition of the substrate (Perrakis et al . , 1994). Interestingly, to date, all of the antibody-peptide structures contain a cis-proline residue within CDR L3, which is important for peptide-antigen binding. The reasons for the conservation of the cis-Pro is unclear, although it is, interesting that the two residues on either side of the cis-Pro, make at least one direct peptide contact and a second indirect contact, via other residue of the CDRs. The SM3 structure however, does not contain the equivalent proline in L3, but appears to have the cis- peptide bond, albeit non-proline, on the opposite side of the antibody combining face in H3. At least two conclusions can be drawn from these observations: (1) A cis-peptide bond within the antibody-antigen combining site is an important and common feature of peptide- antigen binding; (2) The SM3-peptide complex differs from all other antibody-peptide complexes in that the cis- peptide bond is non-proline and is located in another CDR loop. As to the role of the cis-peptide bond, it may relate to specific interactions with the hydrophobic surface on the peptide antigen. An additional reason for this bond to be cis rather than trans, may be due to the small size of H3 resulting from the extended peptide antigen epitope running across its upper surface. A small all-trans CDR would have less degrees of freedom to accommodate such a change. Comparison of bound and unbound MUCl peptide antigen A comparison of the SM3 bound MUCl peptide with the unbound solution structure obtained from NMR studies of three MUCl repeats (Fontenot et ai . , 1995) is shown in Figure 4. The structure of the core region within each repeat in the solution structure is different to that of the antibody-bound peptide antigen. The overall geometry of the "knob-like" protrusion has changed from two consecutive type II β-turns as observed in solution (Fontenot et al . , 1995) to that of an essentially extended geometry when bound to the SM3 antibody. There are differences in all of the phi and psi torsion angles between the bound and unbound peptide, with the main differences centred on the phi angles of Asp5P and Arg7P, which together make a significant percentage of the total peptide-contacts (Table 4). This rearrangement could keep the charged head groups partially solvated on antibody binding, thereby presenting a predominantly hydrophobic surface to the SM3 antibody combining site. Thus, if the NMR structure of the MUCl repeats represents the most prominent conformation in vivo (Fontenot et al . , 1995), then the SM3 antibody induces a conformational change in the mucin molecule upon binding, at least within the region of the peptide epitope. This would suggest that SM3-peptide recognition is by an "induced fit" mechanism. References Bernstein, F.C., Koetzle, T.F., Williams, G.J.B., Meyer, E.F., Jr., Brice, M.D., Rogers, J.R., Kennard, O., Shimanouchi, T., Tasumi, M. (1977) The protein data bank: A computer based archival file for macromolecular structures. /. Mol. Biol. 112, 535-542 Brunger, A.T. 19992) X-PLOR, A System for Crystallography and NMR (Yale Univ. Press, New Haven, CT) Version 3.1 Brunger, A.T. (1993) Assessment of phase accuracy by cross validation - the free R- value - methods and applications. Acta Crystallogr. D49, 24-36 Burchell, J. and Taylor-Papadimitriou, J. (1993) Effect of modification of carbohydrate side chains on the reactivity of antibodies with core-protein epitopes of the MUCl gene product. Epithelial Cell Biol. 2, 155-162. Burchell, J., Gendler, s., Taylor-Papadimitriou, J., Girling, A., Lewis, A., Millis, R. and Lamport, D. (1987) Development and characterisation of breast cancer reactive monoclonal antibodies directed to the core protein of the human milk mucin. Cancer Res. 47, 5476-5482. Burchell, J., Taylor-Papadimitriou, J., Boshell, M., Gendler, D. and Duhig, T. 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D50, 414-423 Cygler, M., Rose, D.R. and Bundle, D.R. (1991) Recognition of a cell-surface oligosaccharide of pathogenic salmonella by an antibody fab fragment. Science 253, 442-445. Dokurno, P., Lally, J.M., Bates, P.A., Taylor-Papadimitriou, J., Band, H.A., Sanry, D. and Freemont, P.S. (1997) Crystallisation of an atitumour antibody SM3 complexed with a peptide epitope. Acta Crystallogr. D (in press). Engh, R.A. and Huber, R. (1991) Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A47, 392-400. Fontenot, J.D., Mariappan, S.V.S., Catasti, P., Domenech, N., Finn, O.J. and Gupta, G. (1995) Structure of the tumor associated antigen containing a tandemly repeated immunodominant epitope./. Biomol. Struct. andDynam. 13, 245-260. Gendler, S., Taylor-Papadimitriou, J., Duhig, T., Rothbard, J. and Burchell, J. (1988) A highly immunogenic region of a human polymorphic epithelial mucin expressed by carcinomas is made up of tandem repeats. / Biol. Chem. 263, 12820- 12823. Gendler, S.J., Lancaster, C.A., Taylor-Papadimitriou, J., Duhig, T., Peat, N.Burchell, J., Pemberton, L., Lalani, E.-N. and Wilson, D. (1990) Molecular cloning and expression of the human tumour-associated polymorphic epithelial mucin. / Biol. Chem. 265, 15286-15293. Ghiara, J.B., Ferguson, D.C., Satterthwait, A.C., Dyson, H.J. and Wilson, A. (1997) Structure-based design of a constrained peptide mimic of the HIV-1 V3 loop neutralization site. / Mol. Biol. 266, 31-39. Girling, A., Bartkova, J., Burchell, J., Gendler, S., Gillett, C. and Taylor- Papadimitriou, J. (1989) A core protein epitope of the polymorphic epithelial mucin detected by the momoclonal-antibody sm-3 is selectively exposed in a range of primary carcinomas. Int. J. Cancer 43, 1072-1076. Granowska, M., Biassoni, L., Carroll, M.J., Howell, R., Mather, S.J., Ellison, d., Granowski, A. and Britton, K.E. (1996) Breast cancer 99m Tc SM3 radioimmunoscintigraphy ct Oncologica 35, 319-321. 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(1994) Antibody-antigen interactions: new structures and new conformational changes. Curr. Opin. Struct. Biol. 4, 857-867. Table 1 Structure factors of the SM3 fragment/crystal peptide crystal which is described in the Examples This table is shown below. The data is arranged in four separate columns as below. Each row of a column consisting of five numbers describes the results of a single reflection. Reading left to right, the first three numbers represent h, k and 1 respectively and are the crystallographic reflection indices. The fourth number represents the structure factor F(hkl) defined as the computed sum of the Fourier series for each reflection hkl . As multiple measurements are made of the same reflection a standard deviation for each structure factor has been provided as the fifth number in the row. Tables 2a and 2b Structure (atomic coordinates) of the SM3 fragment/crystal peptide crystal which is described in the Examples These tables are shown below. The top row, called CRYST1, defines the spacegroup and crystal cell dimensions. Scale 1, Scale 2 and Scale 3 define an orthogonalisation matrix which when applied to the individual coordinates puts them into an orthogonal axis system i.e. 90 degrees between each of the axes x, y and z . Below these rows reading left to right the second row gives the chemical symbol of the atom. OH2 represents a water molecule. The letter following indicates the position of the atom in the amino acid residue using a convention recognised by a skilled partisan. The letter refers to the equivalent Greek symbol (i.e. A for alpha, B for beta etc.) . The third column gives the identity of the residue in which the atom is present. WAT represents a water molecule. The fifth column gives the number of the amino acid in the protein. The sixth, seventh and eighth columns give the spatial position of the atom as x, y and z coordinates respectively. The ninth column shows the occupancy of that atom which will be 1.0 for present and 0.0 for absent (i.e. not observed) and the tenth column gives the B-factor which refers to the mobility. Table l . -21 8 1 50.2 16.3 -20 4 5 40.9 16.3 -20 10 1 35.7 13.5 -21 0 1 132.8 9.3 -21 8 2 46.7 13.3 -20 4 6 1 18.7 8.2 -20 10 2 25.4 1 1.6 -21 0 2 172.8 12.6 -21 8 3 30.7 13.4 -20 4 7 49.1 14.0 -20 10 3 89.3 7.8 -21 0 3 124.7 10.3 -21 8 4 134.5 7.9 -20 4 8 74.8 6.8 -20 10 4 44.2 16.7 -21 0 4 183.9 7.7 -21 8 5 89.1 7.5 -20 4 9 39.5 12.9 -20 10 5 39.8 14.3 -21 0 5 160.3 19.4 -21 8 6 45.5 13.4 -20 4 10 181.5 6.0 -20 10 6 27.9 12.9 -21 0 6 152.0 14.3 -21 8 7 28.3 14.1 -20 4 1 1 137.8 5.3 -20 10 7 21.4 10.2 -21 0 7 87.1 1 1.0 -21 9 2 34.4 14.6 -20 4 12 88.2 6.2 -20 10 8 70.8 10.1 -21 0 8 96.3 9.2 -21 9 3 1 19.1 6.5 -20 4 13 151.8 5.7 -20 10 9 76.1 8.8 -21 0 9 41.4 19.9 -21 9 5 1 18.5 6.9 -20 4 14 31.1 12.9 -20 10 10 54.9 13.8 -21 0 10 1 14.6 15.0 -21 9 6 85.0 13.0 -20 5 1 89.1 8.7 -20 10 1 1 21.7 10.2 -21 1 1 22.8 1 1.0 -21 10 1 126.7 13.0 -20 5 2 36.5 14.5 -20 10 12 72.9 9.1 -21 1 2 109.3 1 1.7 -21 10 2 113.5 1 1.6 -20 5 3 98.3 7.1 -20 1 1 1 138.6 10.6 -21 1 3 46.8 18.7 -21 10 3 30.0 13.8 -20 5 4 19.0 9.4 -20 1 1 2 107.6 6.4 -21 1 4 58.2 13.4 -20 0 2 1 12.0 9.3 -20 5 5 168.0 5.4 -20 1 1 3 62.9 14.6 -21 1 5 102.7 10.0 -20 0 3 42.6 19.1 -20 5 6 106.6 7.0 -20 1 1 4 152.7 10.5 -21 1 6 21.7 10.7 -20 0 4 35.9 24.8 -20 5 8 95.6 6.6 -20 11 5 92.7 1 1.1 -21 1 7 60.1 12.3 -20 0 5 46.1 28.7 -20 5 9 88.3 7.4 -20 1 1 6 94.9 13.5 -21 1 8 73.2 7.8 -20 0 6 19.5 13.6 -20 5 10 170.3 5.3 -20 1 1 7 74.5 8.1 -21 1 10 95.2 18.3 -20 0 7 110.2 9.1 -20 5 11 92.9 7.3 -20 1 1 8 104.8 5.7 -21 2 1 63.4 12.1 -20 0 8 1 11.9 6.9 -20 5 12 63.6 13.0 -20 1 1 9 103.8 5.7 -21 2 2 77.5 17.8 -20 0 9 169.2 5.9 -20 5 13 1 14.7 5.0 -20 1 1 10 48.7 13.6 -21 2 3 42.2 15.8 -20 0 10 156.5 6.8 -20 5 14 24.0 10.9 -20 11 1 1 160.7 4.8 -21 2 4 1 17.3 10.0 -20 0 1 1 18.3 13.1 -20 6 1 70.6 14.9 -20 12 1 24.5 1 1.8 -21 2 5 73.3 15.1 -20 0 12 176.6 6.8 -20 6 2 29.0 12.8 -20 12 2 135.3 12.7 -21 2 6 89.8 10.2 -20 0 13 31.9 17.7 -20 6 3 112.6 7.5 -20 12 3 172.3 9.8 -21 2 7 54.3 12.8 -20 0 14 48.5 18.8 -20 6 4 99.3 8.2 -20 12 4 20.9 10.1 -21 2 8 18.0 9.0 -20 1 1 71.0 11.0 -20 6 5 99.5 6.7 -20 12 5 58.3 16.1 -21 2 9 36.7 14.5 -20 1 2 28.6 12.6 -20 6 6 190.6 7.1 -20 12 6 73.2 20.2 -21 2 10 109.9 13.3 -20 1 3 102.6 6.4 -20 6 8 43.7 13.0 -20 12 7 84.8 8.3 -21 3 1 75.6 9.7 -20 1 4 137.5 13.5 -20 6 9 112.5 6.2 -20 12 8 29.2 12.8 -21 3 2 77.7 18.4 -20 1 5 85.8 20.6 -20 6 10 69.2 9.3 -20 12 9 78.7 8.0 -21 3 3 32.4 13.9 -20 1 6 101.1 7.9 -20 6 1 1 141.8 5.1 -20 12 10 76.3 10.3 -21 3 4 34.7 13.7 -20 1 7 104.1 6.3 -20 6 12 66.2 12.1 -20 13 1 197.7 9.6 -21 3 5 42.5 14.0 -20 1 8 86.4 7.4 -20 6 13 84.8 6.7 -20 13 2 149.6 7.2 -21 3 6 173.0 6.9 -20 1 9 39.8 13.3 -20 6 14 190.8 7.0 -20 13 3 48.4 13.7 -21 3 7 67.2 1 1.0 -20 1 10 62.3 14.0 -20 7 1 173.9 9.1 -20 13 4 83.5 7.5 -21 3 8 104.2 5.9 -20 1 1 1 141.0 5.5 -20 7 2 111.4 14.2 -20 13 5 94.3 6.4 -21 3 9 37.4 14.8 -20 1 12 18.8 9.1 -20 7 3 59.0 17.7 -20 13 6 99.3 12.0 -21 4 1 30.9 13.4 -20 1 13 179.3 8.7 -20 7 4 125.5 7.5 -20 13 7 119.9 6.5 -21 4 2 21.8 10.5 -20 1 14 54.1 13.8 -20 7 5 186.8 4.8 -20 13 8 73.6 9.9 -21 4 3 76.4 10.8 -20 2 1 41.6 16.7 -20 7 6 96.2 7.6 -20 13 9 94.8 6.6 -21 4 4 149.5 6.1 -20 2 2 62.9 13.2 -20 7 7 189.9 1 1.2 -20 14 1 63.5 14.4 -21 4 5 24.9 1 1.7 -20 2 3 65.6 12.3 -20 7 8 21.3 10.7 -20 14 2 1 14.4 6.8 -21 4 6 41.2 15.4 -20 2 4 73.6 22.9 -20 7 9 110.5 6.9 -20 14 3 51.2 15.4 -21 4 7 53.1 15.6 -20 2 5 61.2 22.0 -20 7 10 89.4 6.8 -20 14 5 44.6 13.1 -21 4 8 93.8 9.6 -20 2 6 51.8 15.1 -20 7 1 1 51.7 12.3 -20 14 6 159.5 8.2 -21 4 9 22.2 10.7 -20 2 7 26.5 12.0 -20 7 12 130.5 6.0 -20 14 7 17.7 8.9 -21 5 1 27.8 13.0 -20 2 8 144.3 4.6 -20 7 13 33.8 12.7 -20 14 8 57.1 15.6 -21 5 2 113.4 11.7 -20 2 9 88.2 6.5 -20 8 1 179.9 8.5 -20 15 1 84.4 8.5 -21 5 3 44.4 18.1 -20 2 10 40.1 14.6 -20 8 2 171.7 8.0 -20 15 2 108.2 7.2 -21 * 5 4 54.6 16.2 -20 2 1 1 94.4 10.7 -20 8 3 223.0 8.0 -20 15 3 29.9 13.4 -21 5 5 64.2 13.2 -20 2 12 28.5 12.1 -20 8 4 83.0 8.6 -20 15 4 79.3 21.3 -21 5 6 152.4 10.5 -20 2 13 147.0 4.8 -20 8 5 23.5 1 1.0 -20 15 5 25.3 1 1.5 -21 5 7 107.0 22.2 -20 2 14 151.0 4.7 -20 8 6 98.3 6.1 -20 15 6 26.1 1 1.9 -21 5 8 26.8 12.0 -20 3 1 78.7 14.1 -20 8 7 46.7 16.9 -20 15 7 34.4 15.1 -21 5 9 117.3 5.8 -20 3 2 87.6 7.8 -20 8 8 67.9 1 1.0 -20 16 1 125.5 9.0 -21 6 1 87.8 8.1 -20 3 3 51.3 13.6 -20 8 9 90.5 7.2 -20 16 2 65.7 12.9 -21 6 2 41.2 15.9 -20 3 4 106.2 11.4 -20 8 10 88.8 6.9 -20 16 3 38.7 18.0 -21 6 3 90.2 1 1.7 -20 3 5 92.5 1 1.6 -20 8 1 1 97.2 6.0 -20 16 4 81.4 12.3 -21 6 4 81.2 8.7 -20 3 6 36.9 13.6 -20 8 12 45.0 13.3 -19 0 2 29.0 19.3 -21 6 6 62.7 13.0 -20 3 7 143.2 6.8 -20 8 13 96.2 7.2 -19 0 3 71.9 24.8 -21 6 7 23.2 1 1.6 -20 3 8 82.7 7.3 -20 9 1 58.1. 11.6 -19 0 4 46.3 28.7 -21 6 8 47.6 13.1 -20 3 9 20.2 9.6 -20 9 2 126.0 6.2 -19 0 5 183.1 14.1 -21 7 1 132.5 12.4 -20 3 1 1 125.4 5.7 -20 9 3 153.5 6.9 -19 0 6 266.6 7.7 -21 7 2 71.7 10.6 -20 3 12 63.0 8.5 -20 9 4 86.1 10.8 -19 0 7 209.2 5.6 -21 7 3 153.7 7.8 -20 3 13 127.1 7.6 -20 9 5 25.9 11.6 -19 0 8 76.4 9.5 -21 7 4 44.0 15.4 -20 3 14 55.1 13.6 -20 9 7 35.8 13.2 -19 0 9 40.4 18.1 -21 7 5 57.1 11.3 -20 4 1 108.5 9.5 -20 9 8 100.4 7.0 -19 0 10 11 1.1 7.1 -21 7 6 68.6 9.3 -20 4 2 60.3 12.0 -20 9 10 62.6 9.3 -19 0 11 127.2 6.7 -21 7 7 34.3 13.8 -20 4 3 33.2 13.2 -20 9 1 1 74.7 7.7 -19 0 12 94.7 10.3 -21 7 8 59.1 17.2 -20 4 4 104.1 7.3 -20 9 12 23.0 10.9 -19 0 13 88.2 9.9 -19 0 14 165.1 6.0 -19 5 3 144.5 6.1 -19 9 8 86.4 9.4 -19 14 4204.1 8.9 -19 0 15 125.5 11.3 -19 5 4 105.2 14.3 -19 9 9 124.7 6.3 -19 14 5 184.7 9.5 -19 0 16 172.3 6.3 -19 5 5 106.5 8.0 -19 9 10 97.6 6.7 -19 14 6 143.3 5.3 -19 0 17 14.1 10.4 -19 5 6218.2 4.5 -19 9 11 81.7 8.1 -19 14 7 63.9 9.7 -19 0 18 68.9 19.1 -19 5 7 121.5 6.1 -19 9 12 105.2 5.4 -19 14 8 32.9 13.7 -19 1 1 31.0 12.1 -19 5 8 79.7 8.8 -19 9 13 129.1 5.7 -19 14 9 79.6 10.1 -19 1 3 28.7 14.0 -19 5 9 149.1 4.4 -19 9 14 110.9 13.3 -19 14 10 81.3 7.4 -19 1 4 34.7 16.4 -19 5 10 117.5 5.5 -19 9 15 64.9 9.6 -1914 11 110.2 5.2 -19 1 5 97.5 15.1 -19 5 11 17.3 8.7 -19 9 16 42.9 12.0 -19 14 12 114.0 5.0 -19 1 6 129.6 4.9 -19 5 12 110.1 6.5 -19 10 1 38.4 13.5 -19 14 13 65.2 7.9 -19 1 7 85.5 5.5 -19 5 13 82.4 7.7 -19 10 2 34.6 16.0 -19 15 1 141.1 7.4 -19 1 8 85.3 5.7 -19 5 14 32.9 13.0 -19 10 3 76.8 9.6 -19 15 2 168.2 10.1 -19 1 9 109.3 5.4 -19 5 15 95.6 9.0 -19 10 4 50.0 13.3 -19 15 3 142.7 11.6 -19 1 10 49.3 11.9 -19 5 16 28.7 12.3 -19 10 5 29.8 12.8 -19 15 4 141.2 6.6 -19 1 11 31.9 13.4 -19 5 17 118.5 7.8 -19 10 6 110.9 6.1 -19 15 5 161.3 8.0 -19 1 12 116.3 7.3 -19 6 1 96.2 6.1 -1910 7 45.5 11.9 -1915 6 66.3 7.9 -19 1 13 115.4 5.5 -19 6 2 59.1 11.0 -19 10 8 52.4 14.0 -19 15 7 73.0 7.8 -19 1 14 127.0 11.7 -19 6 3 26.3 12.3 -19 10 9 123.5 4.8 -19 15 8 65.9 7.0 -19 1 15 92.0 6.2 -19 6 4 38.8 12.9 -19 10 10 118.0 5.9 -19 15 9 57.6 9.1 -19 1 16 96.8 12.8 -19 6 5 150.5 6.5 -191011 99.3 7.5 -19 15 10112.0 5.6 -19 1 17 54.1 12.1 -19 6 6 68.8 10.3 -19 10 12 20.1 10.1 -19 15 11 36.8 14.3 -19 1 18 75.3 8.3 -19 6 7 122.4 5.6 -19 10 13 109.3 8.8 -19 15 12 54.9 11.9 -19 2 1 177.5 5.3 -19 6 8 119.3 6.7 -19 10 14 148.3 4.1 -19 16 1 56.4 15.6 -19 2 4 76.1 19.1 -19 6 9 73.9 7.1 -191015 26.0 11.5 -19 16 2 66.1 10.9 -19 2 5 89.2 17.1 -19 6 10 34.2 12.8 -19 10 16 32.1 13.8 -19 16 3 33.6 13.3 -19 2 6 134.8 5.4 -19 6 11 130.5 6.7 -19 11 1 78.3 9.9 -19 16 4 151.6 8.5 -19 2 7 86.0 6.0 -19 6 12 59.4 9.5 -19 11 2 167.9 8.0 -19 16 5 87.9 9.0 -19 2 8 93.1 5.1 -19 6 13 153.1 6.3 -1911 3 84.3 13.9 -19 16 6 32.0 15.3 -19 2 9 86.5 9.6 -19 6 14 114.6 5.9 -19 11 4 106.3 10.6 -19 16 7 105.9 19.9 -19 2 10 82.0 7.1 -19 6 15237.7 4.7 -19 11 5 20.4 10.1 -19 16 8 81.5 5.5 -19 211 80.7 6.2 -19 616 86.3 5.8 -1911 6 73.5 9.9 -19 16 9164.0 4.0 -19 2 12 28.2 13.1 -19 6 17 22.2 10.6 -19 11 7 22.6 10.5 -1916 10 84.7 8.3 -19 2 13 103.9 6.4 -19 7 1 96.2 6.0 -19 11 8 20.1 9.7 -19 16 11 89.3 6.7 -19 2 14167.4 8.0 -19 7 2 106.0 5.8 -1911 9 52.2 11.0 -19 16 12 143.6 5.5 -19 2 15 137.6 5.9 -19 7 3 90.1 6.8 -1911 10 82.5 6.8 -1917 1 122.2 7.5 -19 2 16 29.2 14.0 -19 7 4 27.4 11.5 -19 11 11 17.5 8.7 -19 17 2 78.4 9.6 -19 2 17 69.3 11.1 -19 7 5 44.0 14.8 -19 11 12 57.5 13.9 -1917 3 95.8 6.6 -19 2 18 110.4 8.3 -19 7 6 155.1 6.2 -1911 13 52.4 11.9 -19 17 4 77.2 10.9 -19 3 2 99.6 8.7 -19 7 7 97.7 6.7 -1911 14100.7 5.4 -1917 5 41.8 15.6 -19 3 4 75.3 19.9 -19 7 8 99.8 8.5 -1911 15 121.8 4.4 -19 17 6 18.4 9.3 -19 3 5 53.9 19.6 -19 7 9 43.5 13.3 -19 12 1 67.4 8.7 -19 17 7 126.7 6.6 -19 3 6 40.7 14.4 -19 7 10 93.9 7.5 -1912 2 107.8 7.3 -19 17 8 33.1 13.9 -19 3 7 131.6 4.4 -19 7 11 140.3 4.7 -1912 3 103.4 6.1 -1917 9 26.1 12.2 -19 3 8 61.2 8.3 -19 7 12 158.4 6.3 -19 12 4 26.7 11.6 -19 17 10 18.2 9.1 -19 3 9 43.8 12.2 -19 7 13 137.1 5.3 -19 12 5 128.4 9.5 -19 18 1 44.8 12.5 -19 3 10 113.9 5.0 -19 7 14 94.3 7.2 -19 12 6 96.6 9.6 -19 18 2 28.3 12.4 -19 3 11 67.5 6.7 -19 7 15 94.5 8.2 -19 12 7 78.1 11.4 -19 18 3 132.1 13.1 -19 3 12 23.1 11.3 -19 7 16 76.0 6.3 -19 12 8 88.1 6.7 -19 18 4 101.1 9.1 -19 3 13 103.2 7.5 -19 7 17 192.4 4.4 -19 12 9140.2 6.9 -1918 5 88.5 6.9 -19 3 15 71.4 7.7 -19 8 1 127.2 5.5 -19 1210 38.5 12.0 -19 18 6 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51.5 6.5 -102920 90.4 5.1 -102020 125.8 4.5 -1023 15308.9 4.4 -1026 15 161.7 10.3 -1030 1 117.3 3.6 -102021 105.7 4.3 -1023 16 80.4 4.0 -1026 16268.7 4.4 -1030 2 44.4 7.0 -102022 88.0 5.4 -1023 17109.3 3.7 -102617153.4 3.6 -1030 3 176.6 4.0 -102023 105.0 4.5 -1023 18 146.0 9.0 -1026 18 103.5 3.7 -1030 4 140.9 4.6 -102024 144.9 3.9 -1023 19 160.4 3.4 -102619 71.8 6.0 -1030 5 77.5 6.9 -102025 143.1 4.1 -102320253.7 4.0 -102620146.8 3.5 -1030 6111.6 3.2 -10 * 2026 20.8 9.5 -102321 34.6 10.8 -102621 106.2 4.0 -1030 7 12.1 6.1 -1021 1 159.6 3.6 -102322 93.6 4.5 -102622105.1 4.2 -1030 8 92.0 6.9 -1021 2223.4 3.7 -102323 187.5 3.7 -102623 28.5 10.2 -1030 9205.6 8.3 -1021 3 74.8 7.5 -102324 155.3 4.0 -1027 1 45.6 5.1 -1030 10 145.2 3.1 -1021 4 116.7 3.3 -102325 93.1 5.1 -1027 2 158.0 3.3 -1030 11 105.0 3.9 -1021 5267.6 3.9 -1024 1 140.1 4.6 -1027 3 98.1 5.4 -103012 90.9 3.5 -1021 6 139.3 2.7 -1024 2216.0 4.1 -1027 4 185.0 3.1 -1030 13 20.4 9.0 -1021 7 172.0 3.0 -1024 3216.3 4.1 -1027 5 135.0 3.2 -1030 14 79.9 4.7 -1021 8137.2 2.8 -1024 4 32.5 8.9 -1027 6208.9 3.3 -103015 62.5 6.2 -1021 9 90.6 3.2 -1024 5 106.4 2.5 -1027 7 89.6 3.3 -103016 70.3 7.0 -1021 10 118.6 3.4 -1024 6 88.3 2.9 -1027 8 128.8 2.8 -103017 48.8 7.7 -1021 11461.5 6.0 -1024 7 127.0 2.7 -1027 9107.0 2.8 -1030 18 54.7 6.6 -1021 12 109.0 2.8 -1024 8 94.9 2.8 -1027 10139.5 3.5 -1030 19 97.3 4.4 -1021 13 159.3 2.9 -1024 9 83.8 4.1 -102711 72.2 3.6 -1031 2 15.8 7.7 -1021 14 129.0 3.0 -1024 10 115.3 3.5 -1027 12 163.9 2.9 -1031 3 21.8 10.7 -1021 15 114.9 5.1 -102411 92.5 2.9 -102713 71.2 5.6 -1031 4108.1 7.5 -1021 16122.6 3.2 -102412275.8 4.0 -102714243.9 7.8 -1031 5 155.0 8.3 -1021 17247.2 3.8 -1024 13220.6 3.3 -1027 15 116.4 4.1 -1031 6 170.9 5.5 -1021 18414.7 5.3 -102414154.2 3.1 -102716263.9 4.1 -1031 7210.7 4.0 -1021 19 119.9 3.7 -1024 15 171.5 3.2 -1027 17149.7 3.4 -1031 8262.4 3.6 -102120 185.9 9.0 -1024 16227.1 3.6 -1027 18258.8 4.4 -1031 9 87.6 3.5 ■ 10 31 10 108.8 3.5 - 10 36 7 101.5 8.7 -9 1 26 97.7 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10417.4 6.5 -820 26 85.8 6.9 -8 13 15293.4 4.5 -8 1527 93.5 6.7 -8 18 11318.2 5.2 -82027 98.7 5.2 -8 13 16332.7 5.5 -8 1528202.0 4.2 -8 18 12281.2 3.8 -820 28 24.4 11.2 -8 13 17256.7 4.1 -8 1529 80.3 7.0 -8 18 13 167.3 2.9 -821 1 224.5 4.5 -8 13 18 170.7 3.9 -8 15 30 60.6 9.3 -8 18 14 176.9 3.1 -821 2234.7 4.0 -8 13 19217.1 3.5 -8 16 1 164.7 5.2 -8 18 15251.1 3.6 -821 3 241.5 3.8 -8 1320214.1 3.6 -8 16 3487.3 10.3 -8 18 16195.2 3.3 -821 4131.2 2.6 -8 13 21 276.6 4.4 -8 16 4624.0 11.3 -8 18 17 61.8 4.8 -821 5236.2 3.5 -8 1322 90.1 5.8 -8 16 5337.8 5.9 -8 18 18 71.1 5.0 -821 6354.4 5.4 -8 13 23 53.4 8.1 -8 16 6425.2 7.0 -8 18 19 113.7 3.6 -821 7241.3 3.3 -8 1324 145.2 3.5 -8 16 7200.3 3.4 -8 1820205.0 3.6 -821 8293.8 4.4 -8 1325 107.0 5.1 -8 16 8 134.9 3.2 -8 1821 65.6 4.5 -821 9306.9 4.3 -8 1326287.6 7.1 -8 16 9514.5 8.7 -8 1822248.5 4.1 -821 10215.2 3.4 -8 13 27225.9 4.1 -8 16 10 44.3 5.8 -8 1824 159.3 4.3 -821 11 344.3 4.9 -8 1328238.7 4.3 -8 16 11 333.6 5.3 -8 1825 150.3 4.3 -821 12281.1 4.0 -8 13 29 71.1 7.6 -8 16 12 104.5 3.7 -8 1826 188.5 3.9 -821 13 98.1 3.1 -8 1330 67.4 9.9 -8 16 13273.8 3.7 -8 1827 22.6 10.3 -821 14272.5 3.9 -8 14 1 185.2 4.1 -8 16 14 73.5 3.9 -8 1828 161.2 4.8 -821 15 10.8 5.4 -8 14 2260.2 4.0 -8 16 15473.4 6.7 -8 1829299.9 5.1 -821 16 50.1 5.9 -8 14 3 136.7 4.9 -8 16 16201.5 3.5 -8 19 1 320.3 6.0 -821 17 24.1 9.1 -8 14 4359.7 4.8 -8 16 17318.1 5.4 -8 19 2 104.1 3.7 -821 18208.9 3.1 -8 21 19 37.9 8.8 -8 24 1 1 225.5 3.2 -8 27 7 48.2 5.6 -8 30 10 141.2 2.7 -8 21 20 141.8 3.7 -8 24 12 100.5 3.0 -8 27 8 139.9 2.5 -8 30 1 1 81.1 4.1 -8 21 21 28.1 1 1.4 -8 24 13 144.0 2.8 -8 27 9 182.2 2.7 -8 30 12 82.7 4.1 -8 21 22 224.1 7.8 -8 24 14 61.6 5.5 -8 27 10 137.7 2.6 -8 30 13 226.7 7.9 -8 21 23 20.0 9.0 -8 24 15 232.9 3.4 -8 27 1 1 209.1 3.0 -8 30 14 95.0 4.0 -8 21 24 93.8 6.6 -8 24 16 162.2 2.9 -8 27 12 1 10.6 3.0 -8 30 15 108.6 2.9 -8 21 25 54.0 10.7 -8 24 17 212.8 3.4 -8 27 13 128.6 3.0 -8 30 16 1 15.0 3.4 -8 21 26 131.4 4.9 -8 24 18 38.6 8.5 -8 27 14 64.4 4.3 -8 30 17 206.5 3.6 -8 21 27 66.0 8.4 -8 24 19 227.0 3.6 -8 27 15 235.6 3.8 -8 30 18 129.9 3.7 -8 22 1 275.5 7.6 -8 24 20 73.2 9.9 -8 27 16 160.9 1 J .J -8 30 19 41.3 8.6 -8 22 2 276.7 4.7 -8 24 21 218.9 4.2 -8 27 17 370.4 9.8 -8 30 20 205.8 3.6 -8 22 3 184.2 3.6 -8 24 22 1 17.9 3.9 -8 27 18 207.8 3.5 -8 30 21 183.4 3.4 -8 22 4 205.2 3.5 -8 24 23 92.8 5.1 -8 27 19 18.5 8.4 -8 31 1 290.7 5.7 -8 22 5 263.9 3.5 -8 24 24 228.7 4.0 -8 27 20 78.0 5.6 -8 31 2 254.3 5.2 -8 22 6 545.5 6.7 -8 24 25 161.0 3.7 -8 27 21 51.0 6.9 -8 31 3 205.5 4.2 -8 22 7 386.6 5.6 -8 24 26 125.5 4.4 -8 27 22 124.4 3.8 -8 31 4 300.0 6.9 -8 22 8 210.0 3.3 -8 25 1 133.0 4.0 -8 27 23 127.6 4.8 -8 31 5 284.4 9.1 -8 22 9 74.6 3.9 -8 25 2 252.1 5.1 -8 27 24 33.7 12.7 -8 31 6 135.6 2.9 -8 22 10 101.3 3.3 -8 25 3 210.3 4.6 -8 28 1 82.3 5.0 -8 31 7 140.5 3.0 -8 22 1 1 202.5 4.5 -8 25 4 193.2 3.4 -8 28 2 236.0 4.6 -8 31 8 136.9 2.5 -8 22 12 50.5 4.8 -8 25 5 201.2 2.9 -8 28 3 269.4 5.2 -8 31 9 171.7 2.8 -8 22 13 96.4 3.4 -8 25 6 136.8 2.8 -8 28 4 91.0 3.4 -8 31 10 137.9 2.9 -8 22 14 23.5 10.3 -8 25 7 209.4 3.0 -8 28 5 66.0 4.6 -8 31 1 1 158.8 8.5 -8 22 15 66.9 4.4 -8 25 8 56.0 4.9 -8 28 6 1 17.5 2.5 -8 31 12 50.9 10.8 -8 22 16 65.4 4.7 -8 25 9 362.8 5.0 -8 28 7 132.3 2.6 -8 31 13 222.0 3.3 -8 22 17 196.5 3.6 -8 25 10 173.1 2.8 -8 28 8 141.0 2.5 -8 31 14 30.4 9.6 -8 22 18 76.5 3.9 -8 25 1 1 130.5 2.8 -8 28 9 56.6 4.7 -8 31 15 97.0 4.3 -8 22 19 184.0 3.7 -8 25 12 153.8 3.4 -8 28 10 59.3 3.6 -8 31 16 296.4 4.7 -8 22 20 1 1 1.3 3.4 -8 25 13 124.8 J.J -8 28 1 1 64.0 4.4 -8 31 17 83.9 4.0 -8 22 21 98.6 1 1.8 -8 25 14 198.8 3.1 -8 28 12 52.6 4.5 -8 31 18 18.8 8.8 -8 22 22 151.6 3.7 -8 25 15 281.9 4.1 -8 28 13 149.3 3.3 -8 31 19 207.7 3.7 -8 22 23 26.9 10.9 -8 25 16 148.4 2.8 -8 28 14 208.8 3.4 -8 31 20 24.9 9.6 -8 22 24 1 10.8 4.5 -8 25 17 95.6 4.0 -8 28 15 194.0 3.9 -8 32 1 95.1 4.4 -8 22 25 156.1 3.7 -8 25 18 181.2 3.1 -8 28 16 141.4 8.2 -8 32 2 1 12.6 3.8 -8 22 26 108.1 4.7 -8 25 19 188.2 9.4 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107.6 3.0 -8 26 8 183.0 2.7 -8 29 8 1 16.7 2.5 -8 32 17 1 13.0 3.8 -8 23 14 273.8 4.3 -8 26 9 45.4 5.8 -8 29 9 206.7 3.9 -8 32 18 169.6 3.6 -8 23 15 213.9 3.4 -8 26 10 175.4 2.9 -8 29 10 224.9 3.5 -8 32 19 83.9 4.7 -8 23 16 53.6 5.6 -8 26 1 1 157.5 2.6 -8 29 1 1 152.4 2.8 -8 33 1 215.5 4.6 -8 23 17 215.8 3.4 -8 26 12 64.8 3.4 -8 29 12 75.4 4.8 -8 33 2 14.3 7.2 -8 23 18 62.8 4.8 -8 26 13 81.4 4.5 -8 29 13 48.4 6.8 -8 33 3 13.4 6.8 -8 23 19 127.5 3.2 -8 26 14 25.3 8.8 -8 29 14 32.5 12.7 -8 33 4 46.0 10.3 -8 23 20 142.5 4.0 -8 26 15 355.2 5.0 -8 29 15 100.3 7.3 -8 33 5 151.3 4.7 -8 23 21 16.9 8.2 -8 26 16 68.1 5.3 -8 29 16 182.7 3.1 -8 33 6 221.2 10.8 -8 23 22 55.9 8.1 -8 26 17 98.9 3.8 -8 29 17 187.1 3.3 -8 33 7 126.3 6.9 -8 23 23 1 15.4 3.7 -8 26 18 193.5 7.8 -8 29 18 237.4 4.5 -8 33 8 161.9 3.0 -8 23 24 135.2 4.0 -8 26 19 224.0 3.7 -8 29 19 86.0 4.9 -8 33 9 140.6 3.2 -8 23 25 82.5 6.4 -8 26 20 184.4 3.4 -8 29 20 20.3 9.0 -8 33 10 139.6 3.3 -8 23 26 68.8 7.4 -8 26 21 246.7 4.3 -8 29 21 22.7 9.4 -8 33 1 1 61.2 4.0 -8 24 1 160.0 3.0 -8 26 22 42.6 10.2 -8 29 22 36.0 1 1.1 -8 33 12 75.8 3.7 -8 24 2 51 1.2 8.3 -8 26 23 142.6 3.8 -8 30 1 163.3 4.0 -8 33 13 81.1 3.9 -8 24 3 209.3 4.6 -8 26 24 239.8 4.3 -8 30 2 159.2 3.7 -8 33 14 163.4 3.2 -8 24 4 176.2 4.2 -8 26 25 84.6 5.5 -8 30 3 96.7 2.9 -8 33 15 90.6 3.6 -8 24 5 141.0 2.5 -8 27 1 118.7 4.0 -8 30 4 19.6 7.9 -8 33 16 213.7 3.1 -8 24 6 142.6 2.5 -8 27 2 94.2 4.1 -8 30 5 225.1 3.6 -8 33 17 63.8 7.1 -8 24 7 125.6 2.5 -8 27 3 49.4 4.8 -8 30 6 163.9 3.2 -8 33 18 109.6 4.5 -8 24 8 193.2 2.9 -8 27 4 432.4 7.5 -8 30 7 199.4 3.8 -8 34 1 79.6 7.2 -8 24 9 61.8 3.3 -8 27 5 94.4 2.5 -8 30 8 1 19.8 2.7 -8 34 2 71.2 8.0 -8 24 10 320.0 5.1 -8 27 6 1 13.0 2.8 -8 30 9 112.3 3.2 -8 34 3 86.2 8.4 -8 34 4 79.4 5.6 -8 39 7 172.7 9.0 -7 2 6 321.3 5.1 -7 4 13 370.1 5.2 -8 34 5 96.6 5.4 -7 0 1 15.3 9.8 -7 2 7 226.7 3.7 -7 4 14 424.6 5.8 -8 34 6 149.8 3.1 -7 0 2 429.2 8.1 -7 2 8 242.3 3.3 -7 4 15 355.9 5.9 -8 34 7 194.9 3.2 -7 0 3 191.8 3.9 -7 2 9 219.6 3.2 -7 4 16 614.3 9.7 -8 34 8 63.2 4.1 -7 0 4 292.8 4.9 -7 2 10 740.6 9.8 -7 4 17 423.3 7.1 -8 34 9 130.9 2.7 -7 0 5 203.7 4.3 -7 2 1 1 436.5 6.4 -7 4 18 231.0 3.9 -8 34 10 243.1 5.0 -7 0 6 667.4 14.2 -7 2 12 658.4 8.9 -7 4 19 257.4 3.9 -8 34 1 1 90.4 3.8 -7 0 7 277.9 6.0 -7 2 13 342.8 5.4 -7 4 20 127.3 3.9 -8 34 12 273.5 4.6 -7 0 8 327.4 6.1 -7 2 14 498.2 6.9 -7 4 21 1 18.4 3.9 -8 34 13 176.4 3.5 -7 0 9 302.9 5.6 -7 2 15 442.2 6.4 -7 4 22 179.7 3.6 -8 34 14 173.7 3.2 -7 0 10 77.8 5.8 -7 2 16 254.4 4.3 -7 4 23 177.0 3.4 -8 34 15 92.4 3.7 -7 0 1 1 383.3 7.8 -7 2 17 356.0 5.7 -7 4 24 171.4 3.4 -8 34 16 109.8 3.5 -7 0 12 12.8 9.0 -7 2 18 323.0 5.0 -7 4 25 248.5 4.1 -8 34 17 98.3 4.0 -7 0 13 93.7 5.8 -7 2 19 146.4 4.4 -7 4 26 218.3 3.7 -8 35 1 134.3 4.1 -7 0 14 269.7 5.9 -7 2 20 254.6 4.4 -7 4 27 231.4 3.9 -8 35 2 1 19.6 3.7 -7 0 15 195.7 10.1 -7 2 21 140.6 4.9 -7 4 28 1 14.0 12.6 -8 35 3 65.3 6.6 -7 0 16 90.0 5.3 -7 2 22 190.0 3.7 -7 4 29 196.1 4.1 -8 35 4 261.8 5.5 -7 0 17 357.8 7.8 -7 2 23 50.1 8.0 -7 4 30 83.5 6.0 -8 35 5 82.9 5.4 -7 0 18 155.4 4.8 -7 2 24 210.0 3.7 -7 4 31 142.8 5.1 -8 35 6 84.5 6.4 -7 0 19 98.6 6.5 -7 2 25 16.3 7.9 -7 4 32 105.0 6.1 -8 35 7 177.7 3.2 -7 0 20 104.7 5.1 -7 2 26 186.5 3.5 -7 4 33 43.0 13.1 -8 35 8 157.0 3.4 -7 0 21 257.9 5.9 -7 2 27 107.3 5.0 -7 5 1 136.5 3.6 -8 35 9 171.3 2.8 -7 0 22 356.8 7.2 -7 2 28 164.8 6.6 -7 5 2 287.9 4.0 -8 35 10 203.7 3.7 -7 0 23 204.0 4.9 -7 2 29 139.9 4.1 -7 5 3 270.3 3.7 -8 35 1 1 1 19.9 3.2 -7 0 24 339.7 7.4 -7 2 30 1 17.6 5.8 -7 5 4 518.9 7.7 -8 35 12 161.9 3.4 -7 0 25 219.7 5.5 -7 2 31 222.4 4.9 -7 5 5 498.1 6.9 -8 35 13 129.0 3.1 -7 0 26 120.0 5.5 -7 2 32 72.9 8.9 -7 5 6 668.1 8.8 -8 35 14 74.4 4.4 -7 0 27 303.6 7.3 -7 2 33 38.6 13.0 -7 5 7 267.0 3.3 -8 35 15 172.9 3.0 -7 0 28 14.6 10.8 -7 3 1 521.3 9.9 -7 5 8 679.4 9.2 -8 35 16 106.3 4.7 -7 0 29 13.7 10.2 -7 3 2 304.5 4.2 -7 5 9 375.1 5.5 -8 36 1 62.0 5.6 -7 0 30 60.9 15.7 -7 3 3 217.4 4.0 -7 5 10 985.9 13.7 -8 36 2 58.1 6.9 -7 0 31 229.6 6.6 -7 3 4 387.3 6.5 -7 5 11 236.5 3.7 -8 36 3 154.1 4.2 -7 0 32 15.4 11.0 -7 3 5 112.0 2.5 -7 5 12 270.6 5.6 -8 36 4 93.2 4.8 -7 0 33 128.0 7.5 -7 3 6 340.8 5.0 -7 5 13 255.6 4.1 -8 36 5 1 16.7 4.4 -7 1 1 348.5 4.1 -7 3 7 529.9 8.0 -7 5 14 276.6 4.1 -8 36 6 120.5 5.7 -7 1 2 90.7 2.5 -7 3 8 300.8 4.2 -7 5 15 197.5 3.8 -8 36 7 65.7 5.1 -7 1 3 190.5 2.6 -7 3 9 688.7 8.9 -7 5 16 216.1 3.8 -8 36 8 42.6 5.6 -7 1 4 251.5 3.1 -7 3 10 390.0 5.1 -7 5 17 255.9 4.5 -8 36 9 230.7 3.5 -7 1 5 254.8 4.0 -7 3 1 1 150.0 2.8 -7 5 18 278.8 4.4 -8 36 10 95.9 3.5 -7 1 6 228.8 3.5 -7 3 12 231.1 3.3 -7 5 19 164.9 3.5 -8 36 1 1 296.5 5.1 -7 1 7 513.8 8.0 -7 3 13 23.9 9.6 -7 5 20 207.4 3.9 -8 36 12 124.6 3.4 -7 1 8 536.4 6.9 -7 3 14 58.5 9.2 -7 5 21 304.4 4.8 -8 36 13 82.5 3.6 -7 1 9 438.6 6.8 -7 3 15 298.4 5.8 -7 5 22 201.8 3.6 -8 36 14 19.5 9.1 -7 1 10 187.7 3.1 -7 3 16 365.8 5.7 -7 5 23 263.1 4.2 -8 37 1 102.9 4.0 -7 1 1 1 140.1 2.8 -7 3 17 330.5 5.5 -7 5 24 143.7 4.0 -8 37 2 221.4 4.3 -7 1 12 162.3 2.9 -7 3 18 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16 88.8 4.9 0 5 29 134.2 5.9 0 8 2 660.6 23.4 0 10 8 355.7 7.0 0 12 17 405.3 8.0 0 5 31 109.1 7.1 0 8 3 221.8 3.4 0 10 9 200.6 3.4 0 12 18 177.7 5.9 0 5 32 187.1 6.6 0 8 4 473.0 9.0 0 10 10 935.3 14.4 0 12 19 142.7 5.5 0 5 33 134.6 6.0 0 8 5 250.2 3.7 0 10 1 1 593.4 9.3 0 12 20 1 18.1 4.0 0 5 34 94.6 6.4 0 8 6 217.7 2.7 0 10 12 227.4 4.5 0 12 21 171.5 3.8 0 6 1 295.8 6.8 0 8 7 210.2 3.4 0 10 13 232.5 4.8 0 12 22 139.8 4.7 0 6 2 530.7 10.2 0 8 8 507.1 7.8 0 10 14 526.9 8.5 0 12 23 187.4 5.1 0 6 3 671.8 13.8 0 8 9 1 1 1.7 2.8 0 10 15 668.4 1 1.6 0 12 24 333.9 5.0 0 6 4 835.7 13.4 0 8 10 258.4 4.0 0 10 16 1 185.8 16.2 0 12 25 129.8 4.1 0 6 5 461.7 6.7 0 8 11 572.9 8.2 0 10 17 524.3 6.8 0 12 26 194.8 4.3 0 6 6 395.2 6.1 0 8 12 48.9 7.1 0 10 18 259.2 5.4 0 12 27 145.8 4.0 0 6 7 508.8 8.5 0 8 13 932.2 15.8 0 10 19 654.9 12.3 0 12 28 86.4 17.3 0 6 8 224.3 4.1 0 8 14 1 14.9 4.4 0 10 20 291.4 4.7 0 12 29 212.5 5.6 0 6 9 106.5 2.6 0 8 15 247.1 5.8 0 10 21 277.1 4.2 0 12 30 173.9 4.4 0 6 10 436.0 6.3 0 8 16 375.3 6.4 0 10 22 190.6 4.3 0 12 31 120.0 7.1 0 6 11 43.0 7.8 0 8 17 492.7 8.0 0 10 23 166.8 3.4 0 12 32 46.4 1 1.7 0 6 12 418.3 5.8 0 8 18 328.6 5.2 0 10 24 36.5 1 1.8 0 12 33 94.2 6.4 0 6 13 127.1 3.3 0 8 19 398.6 6.9 0 10 25 158.8 3.9 0 13 2 80.6 2.6 0 6 14 190.3 3.5 0 8 20 166.0 5.0 0 10 26 256.5 4.3 0 13 3 233.1 3.7 0 6 15 386.0 6.6 0 8 21 281.2 4.5 0 10 27 21 1.2 4.3 0 13 4 326.4 4.9 0 6 16 495.0 8.1 0 8 22 374.3 5.2 0 10 28 194.1 4.6 0 13 5 278.6 4.6 0 6 17 324.7 7.1 0 8 23 297.9 4.5 0 10 29 250.4 9.7 0 13 6 448.3 5.9 0 6 18 435.7 8.8 0 8 24 412.3 6.4 0 10 30 39.4 14.2 0 13 7 84.3 2.7 0 6 19 465.4 7.6 0 8 25 282.4 4.3 0 10 31 43.6 13.6 0 13 8 609.5 8.1 0 6 20 417.9 7.8 0 8 26 180.7 4.5 0 10 32 96.0 8.7 0 13 9 294.5 4.5 0 6 21 238.7 5.9 0 8 27 272.3 5.3 0 10 33 165.8 5.3 0 13 10 331.6 4.5 0 6 22 432.5 6.9 0 8 28 94.4 7.8 0 1 1 2 109.4 2.1 0 13 1 1 405.3 5.6 0 6 23 200.2 3.9 0 8 29 168.3 13.7 0 1 1 3 482.9 6.8 0 13 12 508.7 7.3 0 6 24 75.5 6.4 0 8 30 247.5 5.0 0 11 4 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70.3 7.9 0 7 5 202.1 3.1 0 9 12 315.4 5.5 0 1 1 19 204.8 4.6 0 13 28 334.2 7.4 0 7 6 257.0 3.4 0 9 13 273.1 4.3 0 1 1 20 198.6 3.8 0 13 29 178.8 4.1 0 7 7 638.4 8.1 0 9 14 444.4 7.0 0 1 1 21 1 13.3 4.3 0 13 30 169.7 4.9 0 7 8 49.8 4.0 0 9 15 305.1 5.9 0 11 22 62.4 11.4 0 13 31 269.6 4.7 0 7 9 492.1 6.5 0 9 16 598.9 9.9 0 1 1 23 167.1 3.5 0 13 32 108.0 6.7 0 7 10 222.3 3.2 0 9 17 366.6 8.9 0 11 24 126.8 4.3 0 14 2 160.8 2.8 0 7 1 1 506.4 8.1 0 9 18 193.2 3.9 0 1 1 25 197.7 4.4 0 14 3 302.0 3.7 0 7 12 591.6 9.1 0 9 19 452.4 8.5 0 1 1 26 74.6 7.2 0 14 4 269.4 3.6 0 7 13 359.0 5.3 0 9 20 306.9 5.5 0 11 27 34.6 11.5 0 14 5 128.3 2.5 0 7 14 292.2 5.3 0 9 21 419.9 7.1 0 11 28 22.5 10.2 0 14 6 816.6 12.7 0 7 15 436.7 7.0 0 9 22 325.0 6.4 0 1 1 30 266.2 4.8 0 14 7 382.5 7.1 0 7 16 387.0 6.0 0 9 23 86.0 5.1 0 11 31 32.8 13.3 0 14 8 392.3 5.4 0 7 17 296.9 4.5 0 9 24 420.0 6.1 0 1 1 32 94.8 9.7 0 14 9 974.8 13.1 0 7 18 466.4 6.7 0 9 25 109.7 6.2 0 11 33 37.5 12.1 0 14 10 602.7 7.4 0 7 19 188.5 4.5 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4 9 18 342.7 5.2 4 3 1 140.7 3.0 4 5 8 182.3 2.9 4 7 13 430.5 5.8 4 9 19 170.4 3.9 4 3 2 364.2 5.0 4 5 9 101.7 3.1 4 7 14 407.7 5.6 4 9 20 338.3 5.7 4 3 3 444.9 7.2 4 5 10 455.2 6.3 4 7 15 316.8 4.6 4 9 21 197.5 3.9 4 3 4 50.7 4.3 4 5 11 102.3 3.5 4 7 16 239.1 7.0 4 9 22 113.5 5.1 4 3 5 173.2 2.9 4 5 12 316.7 4.8 4 7 17 200.0 4.1 4 9 23 204.5 3.8 4 3 6 357.0 5.5 4 5 13 512.3 6.6 4 7 18 243.3 5.2 4 9 24 257.2 4.4 4 3 7 318.6 5.1 4 5 14 580.6 8.0 4 7 19 123.4 5.3 4 9 25 76.0 7.4 4 3 8 45.9 5.5 4 5 15 150.8 13.7 4 7 20 319.5 5.2 4 9 26 228.5 4.2 4 3 9 452.5 6.1 4 5 16 195.2 4.6 4 7 21 147.5 3.7 4 9 27 105.2 8,5 4 3 10 325.2 4.3 4 5 17 304.1 4.3 4 7 22 274.8 4.7 4 9 28 350.4 10.2 4 3 1 1 184.1 3.0 4 5 18 206.9 4.8 4 7 23 181.9 3.8 4 9 29 202.2 5.6 4 3 12 321.3 4.4 4 5 19 69.5 9.3 4 7 24 168.1 3.8 4 9 30 147.4 6.8 4 3 13 426.9 5.7 4 5 20 310.5 5.2 4 7 25 95.6 6.3 4 9 31 32.4 14.5 4 3 14 518.7 7.3 4 5 21 477.0 6.9 4 7 26 239.9 4.5 4 9 32 169.3 8.3 4 3 15 419.3 6.0 4 5 22 222.3 3.9 4 7 27 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4 17 18 200.5 3.6 4 10 29 153.2 7.2 4 13 2 386.4 4.7 4 15 10 41.5 17.3 4 17 19 26.5 10.5 4 10 30 307.3 5.4 4 13 3 163.9 2.6 4 15 11 362.8 5.4 4 17 20 335.1 6.4 4 10 31 118.5 7.7 4 13 4 495.3 6.8 4 15 12 865.8 1 1.8 4 17 21 141.1 3.8 4 10 32 168.6 6.4 4 13 5 241.6 3.2 4 15 13 507.9 7.5 4 17 22 189.8 3.7 4 1 1 0 128.8 2.6 4 13 6 309.9 4.5 4 15 14 208.6 4.1 4 17 23 107.1 4.7 4 11 1 276.8 5.0 4 13 7 809.8 11.0 4 15 15 433.8 5.9 4 17 24 42.5 13.6 4 1 1 2 654.4 9.0 4 13 8 189.4 3.0 4 15 16 72.2 6.1 4 17 25 191.9 5.1 4 1 1 3 404.8 5.5 4 13 9 124.2 2.9 4 15 17 220.7 3.5 4 17 26 178.5 6.2 4 11 4 97.8 2.2 4 13 10 649.2 8.3 4 15 18 145.9 3.9 4 17 27 78.0 7.5 4 1 1 5 159.2 2.6 4 13 1 1 299.5 4.4 4 15 19 44.0 10.7 4 17 28 135.7 5.8 4 1 1 6 378.4 4.7 4 13 12 524.0 6.9 4 15 20 287.7 4.4 4 17 29 80.7 9.2 4 11 7 516.1 6.9 4 13 13 224.0 4.6 4 15 21 186.4 3.9 4 17 30 111.1 7.8 4 1 1 8 319.4 4.7 4 13 14 430.0 6.0 4 15 22 222.4 4.0 4 18 0 186.5 3.8 4 1 1 9 598.3 9.6 4 13 15 211.6 3.8 4 15 23 209.3 3.9 4 18 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29.6 13.5 1722 5 83.1 14.9 18 2 12 20.1 10.1 17 12 3 66.1 8.0 17 1615 21.9 10.8 1722 6 30.3 13.3 18 2 13 131.4 8.5 17 12 4 20.0 9.9 1717 1 84.0 6.6 1722 7 95.7 11.5 18 2 14 50.4 16.9 17 12 5 114.7 6.6 1717 2 87.3 8.2 1722 8 90.5 14.3 18 2 15 28.6 13.3 17 12 6 116.1 9.6 17 17 3 100.7 8.5 1722 9 50.8 14.9 18 2 16 86.6 12.3 17 12 7272.4 12.9 17 17 4 21.2 10.4 1722 10 26.7 13.5 18 2 17 22.8 1 1.4 1712 9 38.5 16.2 1717 5 67.9 8.3 1723 0113.6 5.1 18 3 0 136.7 6.2 17 12 10 32.6 13.8 17 17 6137.0 4.6 1723 2 113.2 6.2 18 3 1 121.7 6.8 17 12 11 42.6 14.4 17 17 7 95.1 6.3 1723 3 80.1 7.0 18 3 2 91.1 9.6 17 12 12 26.4 12.4 17 17 8 98.3 7.6 1723 4 97.0 5.4 18 3 3 70.9 25.4 17 12 13 169.2 18.8 1717 9 23.4 11.4 1723 5 59.8 8.3 18 3 4 100.0 12.8 17 12 14 34.0 15.9 17 17 10 98.0 11.3 1723 6 49.4 12.0 18 3 5 20.2 10.2 17 12 15 111.4 9.9 17 17 11 17.7 8.9 1723 7 178.2 5.8 18 3 6 409.5 15.9 17 12 16 44.5 18.2 17 17 12 72.5 14.7 1723 8 29.8 13.9 18 3 7 285.7 15.1 17 12 17 61.5 19.0 17 17 13 77.2 11.5 1724 1 83.3 13.2 18 3 9 38.5 15.1 18 3 10 87.2 11.6 18 7 15 30.1 13.8 18 12 11 34.5 15.7 18 18 1 120.7 7.5 18 3 11 120.0 7.5 18 7 16 39.3 16.3 18 12 12 23.3 11.5 18 18 2 106.7 7.6 18 3 12 75.2 12.0 18 8 0 15.2 7.7 18 12 13 87.7 10.0 18 18 3 113.7 9.1 18 3 13 111.3 9.7 18 8 1 133.1 7.9 18 12 14 58.0 17.2 18 18 4 106.1 5.7 18 3 14 25.8 12.7 18 8 2 67.5 9.4 18 13 0 50.8 13.9 18 18 5 84.4 7.8 18 3 15 28.7 13.4 18 8 3 266.6 20.1 18 13 1 102.0 8.2 18 18 6 51.1 11.6 18 3 16 80.0 15.4 18 8 4360.8 13.3 18 13 2 28.5 12.3 18 18 7 23.8 10.7 18 3 17 32.5 14.7 18 8 5 19.2 9.7 18 13 3 112.2 6.7 18 18 8 101.8 9.4 18 4 0 51.6 11.9 18 8 6 32.1 13.9 18 13 4 133.4 7.2 18 18 9 64.0 15.2 18 4 1 105.5 8.5 18 8 7 86.5 10.4 18 13 5 106.1 6.3 18 18 10 26.5 13.2 18 4 2 143.1 16.5 18 8 8 94.0 9.1 18 13 6 31.2 13.9 18 19 0 90.0 9.3 18 4 3 39.8 18.9 18 8 9 135.3 6.4 18 13 7 54.2 13.0 18 19 1 78.6 9.0 18 4 4 88.2 9.3 18 8 10 122.0 8.1 18 13 8 71.0 13.1 18 19 2 124.6 7.1 18 4 5 133.5 6.1 18 8 11 28.5 13.3 18 13 9 70.5 16.8 18 19 3 63.0 23.5 18 4 6398.3 12.3 18 8 12235.4 5.3 18 13 10 41.0 17.5 18 19 4247.2 6.1 18 4 7247.5 22.8 18 8 13 83.8 13.2 18 13 11 36.4 15.5 18 19 5 29.2 14.4 18 4 8 64.1 13.5 18 8 14 62.2 12.4 18 13 12 26.8 13.4 18 19 6 100.7 15.3 18 4 9 136.2 6.4 18 8 15 112.3 10.6 18 13 14 21.3 10.6 18 19 7 49.8 12.8 18 4 10 51.1 18.9 18 8 16 34.8 15.5 18 14 0 159.2 6.6 18 19 8 27.9 12.4 18 4 11 111.7 8.5 18 9 1 95.2 12.5 18 14 1 72.6 13.8 18 19 9 67.5 13.3 18 4 12 106.3 11.1 18 9 2332.6 14.7 18 14 2 80.8 9.2 18 20 0 29.8 13.0 18 4 13 161.1 7.0 18 9 3448.4 14.4 18 14 3 130.0 6.7 18 20 1 47.8 15.3 18 4 14 38.0 16.7 18 9 4 62.2 24.4 18 14 4 66.2 12.1 18 20 2 151.0 8.4 18 4 15 28.5 13.4 18 9 5 20.9 10.6 18 14 5 59.9 9.3 18 20 3 116.4 7.5 18 4 16 97.2 9.8 18 9 6 55.4 13.4 18 14 6 85.1 8.6 18 20 4 158.9 6.6 18 4 17 96.9 11.5 18 9 7 26.8 12.7 18 14 7 148.6 6.5 18 20 5 123.6 10.5 18 5 0 133.5 7.6 18 9 8 100.6 12.1 18 14 8 138.4 6.9 18 20 6 31.2 12.1 18 5 1 63.0 18.1 18 9 9 94.5 9.7 18 14 9 80.6 12.4 18 20 7 82.9 9.2 18 5 2 155.7 17.3 18 9 10 89.3 13.1 18 14 10 40.4 17.5 18 20 8 25.5 12.8 18 5 3 37.1 14.8 18 9 11 33.1 14.3 18 14 11 46.9 15.4 18 21 0 75.5 11.9 18 5 4 50.9 14.2 18 9 12249.2 8.4 18 14 12 35.6 16.2 18 21 1 166.9 5.5 18 5 5 115.9 12.2 18 9 13 92.9 12.8 18 14 13 79.1 14.1 18 21 2 54.4 14.5 18 5 6 156.0 7.5 18 9 14 34.3 13.9 18 15 0 59.9 12.4 18 21 3 68.6 11.1 18 5 7 45.0 18.7 18 9 15 48.8 15.3 18 15 1 89.4 8.5 18 21 4 42.8 12.5 18 5 8 29.5 13.2 18 10 0311.7 11.0 18 15 2 134.9 5.9 18 21 5 18.7 9.2 18 5 9 78.2 9.9 18 10 1 349.2 10.0 18 15 3 34.8 16.0 18 21 6 74.5 8.1 18 5 10 198.2 8.9 18 10 2263.7 9.6 18 15 4 73.3 8.1 18 21 7 48.8 13.9 18 5 11 77.0 16.2 18 10 3 155.0 9.8 18 15 5 88.9 7.5 18 22 0 124.9 5.3 18 5 12 28.3 14.0 18 10 5 134.3 6.6 18 15 6 83.3 11.1 18 22 1 78.1 8.1 18 5 13 126.0 8.1 18 10 6 63.1 8.5 18 15 7 156.4 13.7 18 22 2 136.2 6.4 18 5 14 98.0 11.7 18 10 8 192.0 6.1 18 15 8 136.3 8.3 18 22 3 20.0 10.0 18 5 16 86.3 12.8 18 10 9 71.4 14.6 18 15 9 114.5 11.8 18 22 4 98.9 14.5 18 6 0248.3 5.6 18 10 10 135.9 9.0 18 15 10 29.1 13.8 18 22 5 44.4 18.9 18 6 1 26.3 12.7 18 10 11 148.3 7.4 18 15 11 112.3 9.2 18 23 0 25.9 12.0 18 6 2 149.3 4.6 18 10 12 149.8 7.5 18 15 12 52.0 18.5 18 23 1 109.9 6.1 18 6 3 173.5 5.4 18 10 13 57.4 15.7 18 15 13 124.8 9.8 18 23 3 79.2 17.3 18 6 4 124.5 9.3 18 10 14 147.3 11.9 18 16 0 131.6 4.5 19 0 0 14.9 11.0 18 6 5242.4 12.2 18 11 0254.6 11.3 18 16 1 22.0 10.1 19 0 1 12.0 9.0 18 6 6 174.3 5.2 18 11 1 99.5 9.5 18 16 2 167.2 8.3 19 0 2 24.4 15.3 18 6 7 91.1 13.4 18 11 2 22.6 10.9 18 16 3 151.8 5.8 19 0 3 76.5 35.1 18 6 8 144.0 5.7 18 11 3 113.5 5.6 18 16 4 87.4 9.2 19 0 4 86.1 35.0 18.6 9 56.1 15.6 18 11 4 177.2 4.6 18 16 5 137.4 7.9 19 0 5 129.9 7.7 18 6 10 159.1 6.7 18 11 5 18.2 9.1 18 16 6 29.9 13.0 19 0 6203.9 7.3 18 6 11 115.9 10.6 18 11 6 108.0 5.9 18 16 7421.3 59.6 19 0 7 22.9 16.7 18 6 12 101.3 9.8 18 11 7 111.6 8.3 18 16 8 51.1 16.1 19 0 8 67.5 21.5 18 6 13 119.8 9.2 18 11 8 137.3 8.6 18 16 9 136.4 8.0 19 0 9 108.2 18.4 18 6 14 28.7 13.5 18 11 9 91.7 12.6 18 16 10 136.3 8.3 19 0 10 117.8 15.1 18 6 15 35.7 16.3 18 11 10 60.7 19.7 18 16 11 83.9 13.4 19 0 11 194.2 15.8 18 6 16 111.5 9.7 18 11 11 361.6 17.9 18 16 12 26.7 12.7 19 0 12 63.2 21.8 18 7 0 64.5 9.3 18 11 12 69.6 14.5 18 17 0 121.0 6.8 19 0 13 125.8 12.2 18 7 1 99.2 6.5 18 11 14 30.6 13.5 18 17 1 54.2 12.7 19 0 14 85.1 25.1 18 7 3 36.2 13.9 18 11 15 25.8 12.7 18 17 2 106.1 12.8 19 1 0 101.1 7.4 18 7 4 185.2 9.4 18 12 1 114.8 5.6 18 17 3 54.4 16.5 19 1 1 77.7 8.2 18 7 5 308.5 15.8 18 12 2 144.6 5.9 18 17 4 95.0 10.6 19 1 2 109.6 5.7 18 7 7 34.7 14.7 18 12 3 20.9 10.2 18 17 5 132.6 5.8 19 1 3 33.2 16.4 18 7 8 51.7 13.9 18 12 4 45.4 14.4 18 17 6 186.8 10.8 19 1 4 86.5 20.4 18 7 9 30.9 14.0 18 12 5 139.6 5.6 18 17 7 17.1 8.6 19 1 5 147.0 11.6 18 7 10 98.7 10.8 18 12 6 29.0 12.1 18 17 8 127.4 11.4 19 1 6 50.9 16.2 18 7 11 83.5 12.3 18 12 7 91.4 9.8 18 17 9 26.7 12.5 19 1 7 55.2 19.2 18 7 12 29.0 13.9 18 12 8 91.9 8.4 18 17 10 18.0 9.2 19 1 8 115.5 7.9 18 7 13 186.1 7.1 18 12 9 108.0 12.3 18 17 11 144.7 8.6 19 1 9 122.0 11.5 18 7 14 87.0 10.7 18 12 10 193.5 9.6 18 18 0 153.9 5.9 19 1 10 139.6 7.8 19 1 11 522 206 19 6 9 1709 67 19 12 3 1498 73 20 0 1 401 269 19 1 12 512 160 19 6 10 1305 121 19 12 4 958 76 20 0 2 665 147 19 1 13 1112 107 19 6 11 974 107 19 12 5 1826 61 20 0 3 1134 94 19 1 14 388 165 19 6 12 470 201 19 12 6 671 122 20 0 4 1625 85 19 2 0 189 94 19 6 13 393 165 19 12 7 280 128 20 0 52372 142 19 2 1 431 155 19 7 0 1122 63 19 12 8 1061 105 20 0 6 1535 204 19 2 2 804 97 19 7 1 914 74 19 12 9 969 99 20 0 7 659 220 19 2 3 837 123 19 7 2 553 199 1912 10 266 133 20 0 8 997 168 19 2 4 1353 140 19 7 3 1178 88 19 12 11 208 104 20 0 9 886 228 19 2 5 599 95 19 7 4 1293 77 19 13 0 170 86 20 0 10 425 261 19 2 6 1056 65 19 7 5 1113 133 19 13 1 902 97 20 0 11 293 191 19 2 7 721 194 19 7 6 555 208 1913 2 247 119 20 1 0 824 214 19 2 8 987 90 19 7 7 590 145 19 13 3 1261 74 20 1 1 678 140 19 2 9 684 162 19 7 8 275 133 19 13 42320 87 20 1 2 430 136 19 2 10 1314 88 19 7 9 1372 96 19 13 5 296 135 20 1 3 252 120 19 2 11 301 151 19 7 10 262 130 19 13 6 301 126 20 1 4 1556 62 19 2 12 284 138 19 7 11 727 168 1913 7 716 178 20 1 5 578 148 19 2 13 701 159 19 7 12 282 137 19 13 8 427 158 20 1 6 882 122 19 3 0 348 130 19 7 13 254 126 19 13 9 333 149 20 1 7 240 120 19 3 1 511 158 19 8 0 1346 88 19 13 10 1272 144 20 1 8 634 141 19 3 2 308 134 19 8 1 353 148 1914 0 422 140 20 1 9 503 185 19 3 3 1299 83 19 8 2 744 134 1914 1 1900 50 20 1 10 336 157 19 3 4 334 132 19 8 3 358 143 19 14 2 1157 61 20 1 11 395 173 19 3 5 743 77 19 8 4 423 138 19 14 3 1671 84 20 2 0 484 210 19 3 6 400 137 19 8 5 639 122 19 14 4 1584 90 20 2 1 543 179 19 3 72417 93 19 8 6 401 140 1914 5 1428 72 20 2 2 210 101 19 3 8 1643 61 19 8 7 212 105 19 14 6 1312 130 20 2 3 1917 68 19 3 9 1369 82 19 8 8 1651 76 19 14 7 690 113 20 2 4 1198 77 19 3 102141 105 19 8 9 1789 72 1914 8 673 139 20 2 5 741 142 19 3 11 455 185 19 8 10 687 150 1914 9 291 137 20 2 6 329 154 19 3 12 883 114 19 8 11 441 187 19 14 10 317 148 20 2 7 500 177 19 3 13 1288 89 19 8 12 343 157 1915 0 1538 96 20 2 8 371 164 19 3 14 445 170 19 8 13 215 109 19 15 12020 79 20 2 9 623 187 19 4 0 693 81 19 9 0 476 169 19 15 2 1522 82 20 2 10 702 181 19 4 1 1504 48 19 9 1 356 138 1915 3 295 133 20 2 11 543 217 19 4 2 1530 90 19 9 2 838 85 19 15 41546 52 20 3 0 374 184 19 4 3 1198 91 19 9 3 1161 64 19 15 5 1353 120 20 3 1 1426 85 19 4 4 329 146 19 9 4 499 145 19 15 6 1475 94 20 3 2 883 79 19 4 5 170 85 19 9 5 1183 125 1915 71637 108 20 3 3 1438 87 19 4 6 1033 68 19 9 7 758 116 1915 8 314 135 20 3 42247 81 19 4 7 1339 127 19 9 8 1108 112 19 15 9 225 113 20 3 5 1378 119 19 4 8 866 103 19 9 9 750 109 19 16 0 399 155 20 3 62495 105 19 4 9 1420 78 19 9 10 1154 115 1916 1 186 94 20 3 7 514 175 19 4 10 931 126 19 911 979 116 1916 2 809 109 20 3 8 1524 84 19 4 11 233 116 19 9 12 1154 87 1916 3 381 145 20 3 9 405 169 19 4 12 477 166 19 10 0 393 140 19 16 4 239 116 20 3 10 538 220 19 4 13 1152 81 19 10 1 1804 48 19 16 5 618 132 20 4 0 1117 101 19 414 233 116 1910 2 934 64 19 16 61421 108 20 4 1 717 114 19 5 0 1521 59 19 10 3 445 139 1916 7 772 95 20 4 2 699 91 19 5 1 612 95 19 10 4 471 145 19 16 8 573 152 20 4 3 1887 56 19 5 2 1688 58 19 10 5 816 271 19 17 0 972 91 20 4 4 716 151 19.5 3 771 148 1910 6 1135 85 1917 1 300 126 20 4 5 671 120 19 5 4 944 84 1910 72758 83 1917 2 802 97 20 4 6 365 176 19 5 5 1348 57 19 10 8 745 215 1917 32569 61 20 4 7 614 216 19 5 6 1002 79 19 10 10 1475 75 1917 4 1612 112 20 4 8 834 125 19 5 7 1055 146 19 10 11 451 168 19 17 5 212 103 20 4 9 567 182 19 5 8 1224 106 1910 121216 94 1917 6 762 84 20 5 0 480 162 19 5 9 1682 84 19 11 0 670 130 19 17 7 1015 203 20 5 1 1427 114 19 5 10 1711 76 19 11 1 466 130 1918 0 1575 98 20 5 2 1622 105 19 5 11 357 173 19 11 2 461 165 19 18 1 1582 111 20 5 32240 110 19 5 12 645 152 19 11 3 1586 63 19 18 2 383 145 20 5 4 1140 140 19 5 13 535 171 1911 4 474 132 1918 3 1104 90 20 5 5 808 134 19 5 14 1463 84 19 11 5 358 138 1918 4 397 145 20 5 6 1598 109 19 6 0 1019 79 1911 6 868 93 19 18 5 370 132 20 5 7 932 99 19 6 1 374 137 19 11 7 1553 114 1918 6 703 157 20 5 8 568 167 19 6 2 659 136 19 11 8 1274 93 1919 0 998 80 20 5 9 559 165 19 6 3 1225 147 19 11 10 309 141 1919 2 199 99 20 5 10 286 139 19 6 4 748 93 19 11 11 311 151 19 19 3 1373 65 20 6 0 930 84 19 6 5 329 138 19 11 12 282 142 1919 4 435 163 20 6 1 855 95 19 6 6 1119 84 19 12 0 195 98 1920 0 180 91 20 6 2 731 107 19 6 7 617 138 1912 1 284 142 1920 1 241 121 20 6 3 1469 79 19 6 8 789 130 19 12 2 676 136 20 0 0 479 300 20 6 4 487 134 20 6 5 25.4 12.8 20 15 3 36.6 15.4 20 6 6 38.3 14.4 20 16 0 50.7 17.6 20 6 7 38.7 15.6 21 0 0 135.7 7.8 20 6 8 65.7 20.8 21 0 1 133.3 17.4 20 6 9 36.6 15.1 21 0 2 74.5 17.5 20 7 0 144.2 5.8 21 0 3 158.3 24.1 20 7 1 188.1 7.5 21 0 4 148.2 11.7 20 7 2 137.2 12.6 21 0 5 70.0 18.3 20 7 3 151.4 12.0 21 1 0 125.7 5.7 20 7 4 134.4 6.1 21 1 1 113.3 8.1 20 7 5 38.6 15.9 21 1 2 57.5 14.1 20 7 6 27.1 12.3 21 1 3 60.6 13.5 20 7 7 70.6 10.4 21 1 4 64.3 14.4 20 7 8 128.5 17.6 21 1 5 28.2 12.5 20 8 0 105.4 6.7 21 2 0 130.6 11.0 20 8 1 69.1 15.2 21 2 1 85.8 10.6 20 8 2 185.4 16.6 21 2 2 25.1 11.9 20 8 3 20.6 10.1 21 2 3 19.4 9.7 20 8 5 99.3 15.6 21 2 4 21.3 10.6 20 8 6 17.3 8.8 21 2 5 54.6 15.2 20 8 7 73.8 11.2 21 3 0 96.9 10.5 20 8 8 24.7 12.2 21 3 1 43.9 15.3 20 8 9 47.3 17.5 21 3 2 64.4 15.3 20 9 0 113.0 7.0 21 3 3 44.5 18.3 20 9 1 62.0 16.4 21 3 5 37.9 16.0 20 9 2 82.2 10.4 21 4 0 65.6 13.6 20 9 3 68.4 10.4 21 4 1 80.6 10.6 20 9 4 23.9 11.4 21 4 2 76.7 10.9 20 9 5 101.2 9.4 21 4 3 53.7 18.1 20 9 6 32.7 14.2 21 4 4 36.5 17.2 20 9 7 48.0 19.6 21 4 5 42.7 17.3 20 9 8 39.3 14.4 21 5 0 36.6 14.9 20 10 0 68.1 12.6 21 5 1 66.1 13.5 20 10 1 83.0 17.8 21 5 3 41.1 16.5 20 10 2 53.0 16.4 21 5 5 38.5 16.0 20 10 3 92.6 15.0 21 6 0 41.7 16.8 20 10 4 118.9 9.0 21 6 1 22.9 11.3 20 10 5 51.3 15.6 21 6 2 32.1 13.3 20 10 6 67.3 11.1 21 6 3 76.9 17.5 20 10 7 41.9 16.5 21 6 4 158.1 18.5 20 10 8 80.6 10.5 21 7 1 86.5 17.7 20 11 0210.9 5.3 21 7 2 61.9 14.1 20 11 1 56.8 15.2 21 7 3 64.2 17.4 20 11 2 42.1 16.1 21 7 4 44.0 17.8 20 11 3 80.6 12.1 21 8 0 31.0 13.3 20 11 4 77.6 10.2 21 8 1 50.7 12.6 20 11 5 97.2 14.2 21 8 2 58.5 14.5 20 11 6 23.4 11.0 21 9 0 112.8 6.9 20 11 7 22.6 11.2 21 9 1 23.5 11.2 20 12 0 71.3 10.7 20 12 1 41.4 14.6 2042 2 25.2 11.7 20 12 3 171.2 10.7 20 12 4 77.8 11.9 20 12 5 131.0 12.7 20 12 6 76.2 10.1 20 12 7 37.1 16.5 20 13 0 108.0 8.8 20 13 1 222.7 5.3 20 13 2 107.3 7.5 20 13 3 103.8 7.9 20 13 4 165.7 11.2 20 13 5 165.4 13.6 20 13 6 27.9 13.9 20 14 0 146.0 12.4 20 14 1 114.1 16.2 20 14 2 34.9 13.2 20 14 3 26.4 12.2 20 14 4 29.2 14.2 20 15 0 31.1 13.5 20 15 1 27.1 12.7 20 15 2 24.2 11.8 Table 2a. CRYSTl 42.196 83.729 67.23790.0093.3090.00 P21 SCALEl 0.0236990.0000000.001366 0.00000 SCALE2 0.0000000.0119430.000000 0.00000 SCALE3 0.0000000.0000000.014897 0.00000 ATOM CB ILEL 31.902 -1.191 8.768 1.0022.21 ATOM CG2 ILE L 30.875 -2.276 8.525 1.0027.45 ATOM CGI ILEL 31.406 0.116 8.180 1.0024.21 ATOM 4 CD ILEL 3 32.355 1.270 8.270 1.0025.48 ATOM 5 C ILEL 3 30.888 -0.418 10.820 1.0021.44 ATOM 6 O ILEL 3 29.871 -1.082 10.995 1.0020.56 ATOM 9 N ILEL 3 32.253 -2.429 10.853 1.0020.99 ATOM 11 CA ILEL 3 32.105 -1.078 10.243 1.0021.17 ATOM 12 N VALL 4 30.990 0.881 11.105 1.0020.05 ATOM 14 CA VALL 4 29.896 1.599 11.741 1.0020.43 ATOM 15 CB VALL 4 30.381 2.218 13.048 1.0017.54 ATOM 16 CGI VALL 4 29.197 2.800 13.811 1.0019.60 ATOM 17 CG2VALL 4 31.096 1.156 13.881 1.0017.28 ATOM 18 C VALL 4 29.326 2.701 10.850 1.0020.60 ATOM 19 O VALL 4 30.054 3.606 10.449 1.0020.97 ATOM 20 N VALL 5 28.011 2.621 10.592 1.0020.30 ATOM 22 CA VALL 5 27.315 3.571 9.733 1.0017.97 ATOM 23 CB VALL 5 26.358 2.798 8.809 1.0017.56 ATOM 24 CGI VALL 5 25.506 3.735 7.957 1.0016.02 ATOM 25 CG2VALL 5 27.175 1.852 7.930 1.0017.98 ATOM 26 C VALL 5 26.543 4.542 10.611 1.0018.99 ATOM 27 O VALL 5 25.657 4.124 11.342 1.0018.18 ATOM 28 N THRL 6 26.884 5.823 10.548 1.0017.10 ATOM 30 CA THRL 6 26.268 6.830 11.456 1.0016.73 ATOM 31 CB THRL 6 27.382 7.654 12.134 1.0015.12 ATOM 32 OG1THRL 6 28.147 6.801 12.972 1.0017.77 ATOM 34 CG2THRL 6 26.834 8.782 12.972 1.0020.38 ATOM 35 C THRL 6 25.301 7.783 10.753 1.0015.26 ATOM 36 O THRL 6 25.593 8.273 9.658 1.0014.60 ATOM 37 N GLNL 7 24.149 8.058 11.416 1.0014.21 ATOM 39 CA GLNL 23.142 8.992 10.920 1.009.76 ATOM 40 CB GLNL 21.885 8.241 10.518 1.008.55 ATOM 41 CG GLNL 22.057 7.199 9.423 1.003.66 ATOM 42 CD GLN L 20.729 6.615 9.060 1.004.16 ATOM 43 OE1 GLN L 20.464 5.462 9.328 1.0010.06 ATOM 44 NE2 GLN L 19.846 7.417 8.477 1.002.55 ATOM 47 C GLNL 22.792 9.979 12.041 1.0012.95 ATOM 48 O GL L 23.187 9.761 13.186 1.0012.95 ATOM 49 N GLUL 22.069 11.059 11.708 1.0014.59 ATOM 51 CA GLUL 21.637 12.040 12.711 1.009.44 ATOM 52 CB GLUL 21.113 13.314 12.073 1.003.83 ATOM 53 CG GLUL 22.174 14.132 11.394 1.008.12 ATOM 54 CD GLUL 22.252 13.870 9.886 1.0012.60 ATOM 55 OE1 GLU L 21.617 12.890 9.417 1.008.76 ATOM 56 OE2 GLU L 22.962 14.647 9.168 1.0012.58 ATOM 57 C GLUL 8 20.521 11.441 13.515 1.009.97 ATOM 58 O GLUL 19.632 10.819 12.949 1.0010.41 ATOM 59 N SERL 20.492 11.676 14.825 1.0011.56 ATOM 61 CA SERL 19.452 11.049 15.611 1.008.58 ATOM 62 CB SERL 9 19.753 11.118 17.124 1.0014.23 ATOM 63 OG SERL 9 20.332 12.351 17.498 1.0021.30 ATOM 65 C SERL 9 18.098 11.562 15.319 1.007.24 ATOM 66 O SERL 9 17.176 10.785 15.235 1.006.90 ATOM 67 N ALAL 10 17.926 12.851 15.161 1.006.82 ATOM 69 CA ALAL 10 16.586 13.348 14.866 1.006.68 ATOM 70 CB ALAL 10 15.775 13.505 16.147 1.009.20 ATOM 71 C ALAL 10 16.689 14.682 14.231 1.006.99 ATOM 72 O ALAL 10 17.644 15.388 14.502 1.008.81 ATOM 73 N LEUL 11 15.696 15.040 13.440 1.007.46 ATOM 75 CA LEU L 11 15.657 16.351 12.799 1.006.63 ATOM 76 CB LEUL 11 16.162 16.267 11.333 1.0010.52 ATOM 77 CG LEUL 11 17.513 15.589 11.044 1.0010.17 ATOM 78 CD1 LEUL 11 17.767 15.551 9.544 1.008.53 ATOM 79 CD2LEUL 11 18.631 16.325 11.724 1.007.59 ATOM 80 C LEUL 11 14.205 16.806 12.766 1.00 5.60 ATOM O LEUL 11 13.331 15.972 12.663 1.007.61 ATOM 82 N THRL 12 13.961 18.126 12.816 1.004.15 ATOM 84 CA THRL 12 12.600 18.697 12.814 1.006.68 ATOM 85 CB THRL 12 12.357 19.494 14.139 1.0010.20 ATOM 86 OG1 THRL 12 12.556 18.628 15.276 1.0010.18 ATOM 88 CG2THRL 12 10.95520.089 14.157 1.004.50 ATOM 89 C THRL 12 12.442 19.705 11.661 1.009.42 ATOM 90 O THRL 12 13.343 20.532 11.404 1.0011.76 ATOM 91 N THRL 13 11.321 19.713 11.016 1.0012.34 ATOM 93 CA THRL 13 11.16020.652 9.956 1.0013.42 ATOM 94 CB THRL 13 11.70920.016 8.626 1.0015.26 ATOM 95 OG1 THRL 13 12.053 21.031 7.672 1.0019.73 ATOM 97 CG2THRL 13 10.695 19.089 8.020 1.0015.31 ATOM 98 C THRL 13 9.703 21.053 9.814 1.0013.88 ATOM 99 O THRL 13 8.76620.263 10.131 1.0012.15 ATOM 100 N SERL 14 9.47422.296 9.389 1.00 8.75 ATOM 102 CA SERL 14 8.11922.684 9.120 1.0010.75 ATOM 103 CB SERL 14 7.96424.220 9.106 1.0015.90 ATOM 104 OG SERL 14 8.79424.839 10.126 1.0021.10 ATOM 106 C SERL 14 7.80222.124 7.784 1.0010.99 ATOM 107 O SERL 14 8.70321.910 6.981 1.0010.06 ATOM 108 N PROL 15 6.56021.807 7.514 1.0011.57 ATOM 109 CD PROL 15 5.41721.894 8.417 1.0011.51 ATOM 110 CA PROL 15 6.211 21.264 6.210 1.0013.73 ATOM 111 CB PROL 15 4.71220.965 6.322 1.0012.67 ATOM 112 CG PROL 15 4.25721.810 7.463 1.0013.25 ATOM 113 C PROL 15 6.56222.287 5.106 1.0015.44 ATOM 114 O PROL 15 6.62023.482 5.388 1.0014.98 ATOM 115 N GLYL 16 6.84921.806 3.887 1.0012.73 ATOM 117 CA GLYL 16 7.18422.686 2.796 1.0011.86 ATOM 118 C GLYL 16 8.64523.047 2.740 1.0011.99 ATOM 119 O GLYL 16 9.09723.650 1.786 1.0016.69 ATOM 120 N GLUL 17 9.40522.729 3.739 1.0010.28 ATOM 122 CA GLUL 17 10.801 23.014 3.660 1.008.33 ATOM 123 CB GLUL 17 11.31923.510 5.002 1.006.44 ATOM 124 CG GLUL 17 10.64824.808 5.438 1.0011.47 ATOM 125 CD GLUL 17 10.76625.875 4.353 1.005.30 ATOM 126 OE1 GLU L 17 11.94926.218 3.967 1.006.09 ATOM 127 OE2 GLU L 17 9.681 26.343 3.900 1.007.10 ATOM 128 C GLUL 17 11.55321.772 3.219 1.008.34 ATOM 129 O GLUL 17 10.99520.665 3.241 1.0010.48 ATOM 130 N THRL 18 12.821 21.961 2.861 1.007.25 ATOM 132 CA THRL 18 13.68220.866 2.407 1.006.74 ATOM 133 CB THRL 18 14.57621.383 1.236 1.003.14 ATOM 134 OG1 THRL 18 13.71821.634 0.084 1.002.24 ATOM 136 CG2THRL 18 15.70820.418 0.909 1.005.50 ATOM 137 C THRL 18 14.58720.422 3.544 1.005.28 ATOM 138 O THRL 18 15.12921.265 4.271 1.004.15 ATOM 139 N VALL 19 14.815 19.121 3.646 1.005.05 ATOM 141 CA VALL 19 15.711 18.587 4.662 1.006.85 ATOM 142 CB VALL 19 14.934 17.754 5.770 1.008.11 ATOM 143 CGI VALL 19 14.554 18.573 6.983 1.0012.22 ATOM 144 CG2VALL 19 13.670 17.120 5.170 1.0011.25 ATOM 145 C VALL 19 16.695 17.609 4.010 1.007.00 ATOM 146 O VALL 19 16.323 16.856 3.123 1.008.38 ATOM 147 N THRL 20 17.897 17.588 4.511 1.007.91 ATOM 149 CA THRL 20 18.861 16.618 4.098 1.0010.04 ATOM 150 CB THRL 20 20.046 17.270 3.319 1.008.38 ATOM 151 OG1THRL 20 19.553 17.736 2.053 1.0010.18 ATOM 153 CG2THRL 20 21.188 16.287 3.104 1.007.29 ATOM 154 C THRL 20 19.379 15.843 5.324 1.0010.78 ATOM 155 O THRL 20 19.752 16.441 6.354 1.0014.77 ATOM 156 N LEUL 21 19.313 14.510 5.201 1.008.97 ATOM 158 CA LEUL 21 19.829 13.570 6.174 1.005.71 ATOM 159 CB LEUL 21 18.819 12.417 6.324 1.007.30 ATOM 160 CG LEUL 21 17.448 12.710 6.922 1.003.52 ATOM 161 CD1 LEUL 21 16.618 13.549 5.972 1.0012.30 ATOM 162 CD2 LEU L 21 16.726 11.431 7.221 1.005.61 ATOM 163 C LEUL 21 21.108 13.008 5.612 1.005.00 ATOM 164 O LEUL 21 21.155 12.736 4.403 1.006.66 ATOM 165 N THRL 22 22.151 12.817 6.426 1.004.47 ATOM 167 CA THRL 22 23.366 12.204 5.920 1.008.68 ATOM 168 CB THRL 22 24.593 13.096 6.059 1.008.60 ATOM 169 OG 1 THR L 22 24.910 13.29- ! 7.446 1.00 13.20 ATOM 171 CG2 THR L 22 24.362 14.415 i 5.379 1.00 12.92 ATOM 172 C THR L 22 3.674 10.813 6.543 1.00 12.45 ATOM 173 O THR L 22 2 33..007799 10.380 7.573 1.00 12.78 ATOM 174 N CYS L 23 24 4..660088 10.148 5.934 1.00 9.70 ATOM 176 CA CYS L 23 2 244..995522 8.812 6.315 1.00 12.79 ATOM 177 CB CYS L 23 2 '44..111144 7.891 5.444 1.00 1 1.70 ATOM 178 SG CYS L 23 2 >44..557733 6.172 5.437 1.00 14.38 ATOM 179 C CYS L 23 26 5..442255 8.616 ι 6.085 1 1.00 1 1.83 ATOM 180 O CYS L 23 26 6..888800 8.699 4.961 1.00 13.63 ATOM N ARG L 24 2 .77..220011 8.397 7.146 1.00 13.74 ATOM 183 CA ARG L 24 2288..663388 8.236 6.965 1.00 15.34 ATOM 184 CB ARG L 24 2 299..444422 9.275 7.741 1.00 17.58 ATOM 185 CG ARG L 24 2299..117711 9.346 9.214 1.00 23.61 ATOM 186 CD ARG L 24 3300..117777 10.263 9.89C 1 1.00 27.66 ATOM 187 NE ARG L 24 3 311..555588 9.839 9.613 1.00 30.74 ATOM 189 CZ ARG L 24 3 322..550088 10.677 9.195 0.01 28.45 ATOM 190 NH1 ARG L 24 3333..772299 10.222 8.952 0.01 28.77 ATOM 193 NH2 ARG L 24 32.247 1 1.970 9.031 0.01 27.96 ATOM 196 C ARG L 24 29.123 6.869 7.327 1.00 16.36 ATOM 197 O ARG L 24 28.461 6.146 8.081 1.00 15.58 ATOM 198 N SER L 25 30.274 6.517 6.760 1.00 14.90 ATOM 200 CA SER L 25 30.900 5.237 7.014 1.00 15.33 ATOM 201 CB SER L 25 31.273 4.582 5.683 1.00 20.16 ATOM 202 OG SER L 25 32.252 3.571 5.852 1.00 23.32 ATOM 204 C SER L 25 32.145 5.470 7.869 1.00 14.75 ATOM 205 O SER L 25 32.859 6.422 7.653 1.00 16.1 1 ATOM 206 N SER L 26 32.381 4.626 8.851 1.00 15.20 ATOM 208 CA SER L 26 33.555 4.767 9.720 1.00 19.00 ATOM 209 CB SER L 26 33.381 3.884 10.959 1.00 16.96 ATOM 210 OG SER L 26 33.196 2.519 10.578 1.00 19.34 ATOM 212 C SER L 26 34.858 4.349 9.001 1.00 19.93 ATOM 213 O SER L 26 35.936 4.445 9.570 1.0023.14 ATOM 214 N THR L 27 34.768 3.853 7.781 1.00 20.53 ATOM 216 CA THR L 27 35.958 3.362 7.120 1.00 19.87 ATOM 217 CB THR L 27 35.651 2.067 6.419 1.00 21.22 ATOM 218 OG1 THR L 27 34.472 2.209 5.633 1.00 24.06 ATOM 220 CG2 THR L 27 35.417 0.987 7.453 1.00 23.05 ATOM 221 C THR L 27 36.536 4.375 6.153 1.00 19.65 ATOM 222 O THR L 27 37.728 4.343 5.822 1.00 20.98 ATOM 223 N GLY L 27A 35.697 5.293 5.715 1.00 20.47 ATOM 225 CA GLY L 27A 36.148 6.333 4.827 1.00 15.37 ATOM 226 C GLY L 27A 34.981 6.909 4.102 1.00 14.56 ATOM 227 O GLY L 27A 33.871 6.786 4.564 1.00 16.44 ATOM 228 N ALA L 27B 35.237 7.538 2.959 1.00 14.44 ATOM 230 CA ALA L 27B 34.183 8.158 2.158 1.00 13.84 ATOM 231 CB ALA L 27B 34.801 8.852 0.922 1.00 10.44 ATOM 232 C ALA L 27B 33.157 7.151 1.678 1.00 14.20 ATOM 233 O ALA L 27B 33.507 6.028 1.294 1.00 16.84 ATOM 234 N VAL L 27C 31.915 7.550 1.682 1.00 12.61 ATOM 236 CA VAL L 27C 30.894 6.755 1.040 1.00 14.17 ATOM 237 CB VAL L 27C 29.533 7.077 1.632 1.00 13.42 ATOM 238 CGI VAL L 27C 28.465 6.232 0.979 1.00 14.92 ATOM 239 CG2 VAL L 27C 29.592 6.828 3.130 1.00 14.29 ATOM 240 C VAL L 27C 30.903 7.081 -0.471 1.00 16.22 ATOM 241 O VAL L 27C 30.837 8.264 -0.849 1.00 16.42 ATOM 242 N THR L 28 31.047 6.039 -1.322 1.00 15.73 ATOM 244 CA THR L 28 31.068 6.215 -2.805 1.00 14.38 ATOM 245 CB THR L 28 32.386 5.725 -3.453 1.00 12.94 ATOM 246 OG1 THR L 28 32.412 4.313 -3.470 1.00 13.65 ATOM 248 CG2 THR L 28 33.597 6.211 -2.699 1.00 11.90 ATOM 249 C THR L 28 29.924 5.439 -3.450 1.00 12.92 ATOM 250 O THR L 28 29.103 4.824 -2.764 1.00 9.64 ATOM 251 N THR L 29 29.850 5.474 -4.765 1.00 12.65 ATOM 253 CA THR L 29 28.780 4.786 -5.461 1.00 14.40 ATOM 254 CB THR L 29 28.797 5.088 -6.978 1.00 15.28 ATOM 255 OG1 THR L 29 30.146 4.883 -7.468 1.00 16.73 ATOM 257 CG2 THR L 29 28.337 6.524 -7.253 1.00 16.74 ATOM 258 C THR L 29 28.904 3.287 -5.275 1.00 14.04 ATOM 259 O THR L 29 27.939 2.555 -5.436 1.00 17.19 ATOM 260 N SER L 30 30.085 2.840 -4.924 1.00 14.83 ATOM 262 CA SER L 30 30.306 1.429 -4.697 1.00 16.69 ATOM 263 CB SER L 30 31.790 1.168 -4.607 1.00 18.52 ATOM 264 OG SER L 30 32.399 1.455 -5.845 1.00 22.73 ATOM 266 C SER L 30 29.628 0.939 -: 3.418 1.00 18.22 ATOM 267 O SER L 30 29.565 -< 0.247 - 3.177 1.00 17.69 ATOM 268 N ASN L 31 29.154 1.843 - ■2.585 1.00 16.05 ATOM 270 CA ASN L 31 28.467 1.432 -1.358 1.00 12.29 ATOM 271 CB ASN L 31 28.710 2.456 -0.265 1.00 9.73 ATOM 272 CG ASN L 31 30.118 2.424 0.219 1.00 5.99 ATOM 273 OD1 ASN L 31 30.833 3.398 0.1 17 1.00 9.76 ATOM 274 ND2 ASN L 31 30.548 1.320 0.741 1.00 3.79 ATOM 277 C ASN L 31 26.988 1.277 - 1.585 1.00 10.21 ATOM 278 O ASN L 31 26.242 0.937 - 0.663 1.00 9.59 ATOM 279 N TYR L 32 26.575 1.527 - 2.829 1.00 8.64 ATOM 281 CA TYR L 32 25.176 1.475 -3.21 1 1.00 7.71 ATOM 282 CB TYR L 32 24.830 0.081 -3.773 1.00 1 1.29 ATOM 283 CG TYR L 32 25.721 -0.367 -4.925 1.00 1 1.41 ATOM 284 CD 1 TYR L 32 27.019 -0.834 -4.681 1.00 14.39 ATOM 285 CE1 TYR L 32 27.869 -1.196 -5.71 1 1.00 14.44 ATOM 286 CD2 TYR L 32 25.296 -0.298 -6.259 1.00 17.67 ATOM 287 CE2 TYR L 32 26.145 -0.666 -7.326 1.00 1 1.36 ATOM 288 CZ TYR L 32 27.437 -1.108 -7.043 1.00 17.13 ATOM 289 OH TYR L 32 28.334 -1.419 -8.085 1.00 21.48 ATOM 291 C TYR L 32 24.228 1.852 - 2.055 1.00 1 1.23 ATOM 292 O TYR L 32 23.288 1.105 - ■1.733 1.00 6.50 ATOM 293 N ALA L 33 24.445 3.043 ■ ■1.455 1.00 1 1.42 ATOM 295 CA ALA L 33 23.624 3.480 -0.308 1.00 1 1.19 ATOM 296 CB ALA L 33 23.921 4.926 0.065 1.00 10.80 ATOM 297 C ALA L 33 22.133 3.371 - •0.547 1.00 10.34 ATOM 298 O ALA L 33 21.660 3.893 ■ -1.543 1.00 8.45 ATOM 299 N ASN L 34 21.401 2.715 0.396 1.00 7.12 ATOM 301 CA ASN L 34 19.925 2.664 0.367 1.00 5.84 ATOM 302 CB ASN L 34 19.388 1.251 0.564 1.00 3.46 ATOM 303 CG ASN L 34 19.488 0.414 -0.691 1.00 7.07 ATOM 304 OD1 ASN L 34 18.487 -0.063 -1.223 1.00 5.20 ATOM 305 ND2 ASN L 34 20.700 0.240 -1.163 1.00 5.40 ATOM 308 C ASN L 34 19.318 3.528 1.458 1.00 5.10 ATOM 309 O ASN L 34 19.964 3.789 2.435 1.00 6.58 ATOM 310 N TR L 35 18.076 3.957 1.259 1.00 5.01 ATOM 312 CA TRP L 35 17.339 4.694 2.278 1.00 6.70 ATOM 313 CB TRP L 35 17.175 6.215 1.933 1.00 7.73 ATOM 314 CG TRP L 35 18.477 6.997 1.932 1.00 7.1 1 ATOM 315 CD2 TRP L 35 19.075 7.641 3.080 1.00 8.09 ATOM 316 CE2 TRP L 35 20.330 8.11 1 2.697 1.00 5.38 ATOM 317 CE3 TRP L 35 18.654 7.858 4.418 1.00 10.50 ATOM 318 CD1 TRP L 35 19.373 7.125 0.894 1.00 4.99 ATOM 319 NE1 TRP L 35 20.472 7.780 1.351 1.00 6.98 ATOM 321 CZ2 TRP L 35 21.206 8.791 3.595 1.00 5.76 ATOM 322 CZ3 TRP L 35 19.526 8.534 5.295 1.00 6.19 ATOM 323 CH2 TRP L 35 20.785 8.990 4.879 1.00 3.95 ATOM 324 C TRP L 35 16.000 ■ 4.036 : 2.414 1.00 6.29 ATOM 325 O TRP L 35 15.314 3.796 1.403 1.00 6.53 ATOM 326 N VAL L 36 15.674 3.704 3.665 1.00 5.99 ATOM 328 CA VAL L 36 14.479 2.971 4.045 1.00 5.23 ATOM 329 CB VAL L 36 14.826 1.555 4.651 1.00 6.23 ATOM 330 CGI VAL L 36 13.540 ι 0.839 » 5.092 1.00 2.37 ATOM 331 CG2 VAL L 36 15.571 0.693 3.605 1.00 3.99 ATOM 332 C VAL L 36 13.692 3.769 5.086 1.00 4.86 ATOM 333 O VAL L 36 14.255 4.313 6.025 1.00 7.07 ATOM 334 N GLN L 37 12.395 3.803 4.906 1.00 5.26 ATOM 336 CA GLN L 37 1 1.512 4.532 5.786 1.00 10.98 ATOM 337 CB GLN L 37 10.505 5.305 4.967 1.00 10.61 ATOM 338 CG GLN L 37 9.720 6.295 5.788 1.00 10.14 ATOM 339 CD GLN L 37 8.601 6.850 4.987 1.00 15.44 ATOM 340 OE1 GLN L 37 7.787 6.096 4.465 1.00 18.50 ATOM 341 NE2 GLN L 37 8.553 8.166 4.858 1.00 15.77 ATOM 344 C GLN L 37 10.723 3.613 6.694 1.00 11.84 ATOM 345 O GLN L 37 10.134 2.657 6.222 1.00 15.29 ATOM 346 N GLU L 38 10.689 3.945 7.989 1.00 13.42 ATOM 348 CA GLU L 38 9.861 3.213 8.930 1.00 12.58 ATOM 349 CB GLU L 38 10.678 2.719 10.133 1.00 12.59 ATOM 350 CG GLU L 38 9.830 1.991 1 1.202 1.00 11.75 ATOM 351 CD GLU L 38 10.622 1.505 12.384 1.00 9.26 ATOM 352 OE1 GLU L 38 1 1.751 1.915 12.540 1.00 12.30 ATOM 353 OE2 GLU L 38 10.103 0.690 13.161 1.00 17.41 ATOM 354 C GLU L 38 8.719 4.098 9.460 1.00 14.00 ATOM 355 O GLU L 38 8.964 5.098 10.173 1.00 12.02 ATOM 356 N LYS L 39 7.488 3.747 9.1 17 1 .00 13.36 ATOM 358 CA LYS L 39 6.363 4.431 9.687 1.00 15.90 ATOM 359 CB LYS L 39 5.353 4.768 8.628 1.00 14.39 ATOM 360 CG LYS L 39 5.795 5.954 7.803 1.00 15.78 ATOM 361 CD LYS L 39 4.651 6.478 6.961 1.00 22.14 ATOM 362 CE LYS L 39 5.167 7.451 5.905 1.00 25.73 ATOM 363 NZ LYS L 39 4.106 7.921 4.959 1.00 27.82 ATOM 367 C LYS L 39 5.723 3.624 10.838 1.00 20.86 ATOM 368 O LYS L 39 5.775 2.359 10.890 1.00 18.39 ATOM 369 N PRO L 40 5.128 4.335 1 1.810 1.00 25.47 ATOM 370 CD PRO L 40 4.973 5.792 1 1.884 1.00 28.62 ATOM 371 CA PRO L 40 4.486 3.717 12.952 1.00 28.32 ATOM 372 CB PRO L 40 3.528 4.812 13.494 1.00 28.73 ATOM 373 CG PRO L 40 3.578 5.887 12.458 1.00 30.27 ATOM 374 C PRO L 40 3.779 2.403 12.593 1.00 28.70 ATOM 375 O PRO L 40 2.898 2.341 1 1.688 1.00 25.53 ATOM 376 N ALA L 41 4.276 1.365 13.295 1.00 30.46 ATOM 378 CA ALA L 41 3.803 -0.018 13.225 1.00 28.13 ATOM 379 CB ALA L 41 2.411 -0.129 12.599 1.00 29.92 ATOM 380 C ALA L 41 4.789 -0.885 12.485 1.00 24.45 ATOM 381 O ALA L 41 4.403 -1.889 1 1.908 1.00 26.51 ATOM 382 N HIS L 42 6.069 -0.51 1 12.499 1.00 22.07 ATOM 384 CA HIS L 42 7.079 -1.337 1 1.853 1.00 20.06 ATOM 385 CB HIS L 42 7.082 -2.734 12.472 1.00 20.43 ATOM 386 CG HIS L 42 7.624 -2.730 13.832 1.00 17.71 ATOM 387 CD2 HIS L 42 7.030 -2.688 15.058 1.00 17.56 ATOM 388 ND1 HIS L 42 8.958 -2.573 14.058 1.00 21.55 ATOM 390 CE1 HIS L 42 9.230 -2.422 15.333 1.00 19.46 ATOM 391 NE2 HIS L 42 8.081 -2.487 15.944 1.00 17.49 ATOM 393 C HIS L 42 6.815 -1.469 10.375 1.00 21.88 ATOM 394 O HIS L 42 7.010 -2.542 9.809 1.00 22.22 ATOM 395 N LEU L 43 6.335 -0.401 9.749 1.00 20.03 ATOM 397 CA LEU L 43 6.067 -0.450 8.339 1.00 20.01 ATOM 398 CB LEU L 43 4.849 0.389 8.019 1.00 24.58 ATOM 399 CG LEU L 43 3.599 0.015 8.814 1.00 27.32 ATOM 400 CD1 LEU L 43 2.559 1.122 8.684 1.00 26.38 ATOM 401 CD2 LEU L 43 3.071 -1.374 8.380 1.00 24.37 ATOM 402 C LEU L 43 7.271 0.088 7.621 1.00 18.27 ATOM 403 O LEU L 43 7.582 1.270 7.742 1.00 18.64 ATOM 404 N PHE L 44 7.977 -0.790 6.930 1.00 17.14 ATOM 406 CA PHE L 44 9.188 -0.404 6.239 1.00 13.89 ATOM 407 CB PHE L 44 10.276 -1.395 6.558 1.00 10.76 ATOM 408 CG PHE L 44 10.863 1.268 7.932 1.00 8.20 ATOM 409 CD1 PHE L 44 10.285 -1.925 9.005 1.00 10.99 ATOM 410 CD2 PHE L 44 12.017 -0.526 8.135 1.00 13.17 ATOM 411 CE1 PHE L 44 10.834 -1.852 10.273 1.00 11.48 ATOM 412 CE2 PHE L 44 12.588 -0.445 9.399 1.00 12.05 ATOM 413 CZ PHE L 44 1 1.987 -1.110 10.476 1.00 12.67 ATOM 414 C PHE L 44 8.981 -0.332 4.726 1.00 14.13 ATOM 415 O PHE L 44 8.262 -1.129 4.142 1.00 14.69 ATOM 416 N THR L 45 9.634 0.619 4.092 1.00 14.63 ATOM 418 CA THR L 45 9.508 0.771 2.678 1.00 12.14 ATOM 419 CB THR L 45 8.295 1.652 2.352 1.00 14.73 ATOM 420 OG1 THR L 45 8.083 1.684 0.944 1.00 25.05 ATOM 422 CG2 THR L 45 8.519 3.065 2.828 1.00 19.97 ATOM 423 C THR L 45 10.773 1.398 2.181 1.00 11.69 ATOM 424 O THR L 45 11.316 2.253 2.826 1.00 9.53 ATOM 425 N GLY L 46 1 1.293 0.878 1.083 1.00 11.34 ATOM 427 CA GLY L 46 12.521 1.398 0.526 1.00 7.20 ATOM 428 C GLY L 46 12.252 2.593 -0.331 1.00 7.78 ATOM 429 O GLY L 46 11.283 2.595 -1.140 1.00 10.42 ATOM 430 N LEU L 47 13.092 3.602 -0.166 1.00 7.54 ATOM 432 CA LEU L 47 12.929 4.861 -0.890 1.00 7.47 ATOM 433 CB LEU L 47 13.071 6.050 0.080 1.00 6.90 ATOM 434 CG LEU L 47 12.253 5.969 1.362 1.00 6.26 ATOM 435 CD1 LEU L 47 12.782 6.944 2.383 1.00 1 1.14 ATOM 436 CD2 LEU L 47 10.785 6.173 1.052 1.00 2.41 ATOM 437 C LEU L 47 13.968 4.989 -2.015 1.00 5.84 ATOM 438 O LEU L 47 13.597 5.286 -3.141 1.00 8.92 ATOM 439 N ILEL 48 15.239 4.746 -1.673 i .00 9.03 ATOM 441 CA ILE L 48 16.377 4.909 -2.566 1.00 7.03 ATOM 442 CB ILE L 48 17.287 6.078 -2.094 1.00 7.21 ATOM 443 CG2 ILE L 48 18.552 6.176 -2.934 1.00 9.51 ATOM 444 CGI ILEL 48 16.524 7.405 -2.047 1.00 8.82 ATOM 445 CD ILE L 48 16.013 7.933 -3.364 1.00 7.80 ATOM 446 C ILE L 48 17.245 3.644 -2.530 1.00 8.61 ATOM 447 O ILEL 48 17.458 3.068 -1.462 1.0010.60 ATOM 448 N GLY L 49 17.755 3.237 3.704 1.00 7.04 ATOM 450 CA GLY L 49 18.697 2.142 -3.805 1.00 2.00 ATOM 451 C GLY L 49 19.833 2.550 - 4.716 1.00 7.57 ATOM 452 O GLY L 49 19.716 3.479 •5.538 1.0014.41 ATOM 453 N GLY L 50 20.941 1.930 ■ 4.590 1.009.91 ATOM 455 CA GLYL 50 22.036 2.293 -5.431 1.00 9.21 ATOM 456 C GLYL 50 22.299 3.789 5.458 1.0012.31 ATOM 457 O GLY L 50 22.341 4.370 ■ 6.518 1.0012.48 ATOM 458 N THRL 51 22.465 4.390 ■4.284 1.0010.33 ATOM 460 CA THRL 51 22.795 5.834 -4.116 1.0012.06 ATOM 461 CB THRL 51 24.092 6.281 -4.869 1.0011.87 ATOM 462 OG1 THRL 51 25.226 5.464 4.501 1.00 7.57 ATOM 464 CG2THRL 51 24.409 7.726 -4.514 1.0011.63 ATOM 465 C THRL 51 21.672 6.817 -4.460 1.0011.67 ATOM 466 O THRL 51 21.343 7.660 -3.638 1.0011.93 ATOM 467 N ASNL 52 21.046 6.703 -5.637 1.0012.21 ATOM 469 CA ASNL 52 20.092 7.718 -6.054 1.0013.73 ATOM 470 CB ASNL 52 20.824 8.824 -6.808 1.0018.43 ATOM 471 CG ASNL 52 21.621 8.271 -7.967 1.0024.37 ATOM 472 OD1 ASN L 52 21.164 7.364 -8.639 1.0022.65 ATOM 473 ND2ASNL 52 22.842 8.774 -8.182 1.0028.21 ATOM 476 C ASNL 52 18.964 7.205 -6.914 1.0015.37 ATOM 477 O ASNL 52 18.318 7.975 -7.594 1.0013.37 ATOM 478 N ASNL 53 18.730 5.916 -6.901 1.0016.28 ATOM 480 CA ASNL 53 17.652 5.350 -7.676 1.0017.34 ATOM 481 CB ASNL 53 18.079 3.979 -8.239 1.0024.00 ATOM 482 CG ASNL 53 17.187 3.406 -9.349 1.0027.36 ATOM 483 OD1 ASNL 53 17.659 2.594-10.168 1.0033.10 ATOM 484 ND2 ASN L 53 15.911 3.799 -9.410 1.0031.42 ATOM 487 C ASNL 53 16.415 5.210 -6.781 1 .0017.91 ATOM 488 O ASNL 53 16.352 4.394 -5.893 1 1.0018.29 ATOM 489 N ARGL 54 15.447 6.010 -7.022 1.0015.93 ATOM 491 CA ARG L 54 14.283 5 5..997777 -6.241 1.0018.87 ATOM 492 CB ARGL 54 13.500 77..223333 -6.541 1 1..00002222..3333 ATOM 493 CG ARG L 54 12.109 77..227733 -5.975 11..00002255..5555 ATOM 494 CD ARGL 54 11.778 88..668811 -5.615 11..00002299..5544 ATOM 495 NE ARGL 54 12.126 99..558822 -6.671 11..00002277..8822 ATOM 497 CZ ARGL 54 11.288 99..889900 -7.630 11..00003322..1199 ATOM 498 NH1 ARG L 54 11.669 10.739 -8.561 1.0035.27 ATOM 501 NH2ARGL 54 10.071 9.344 ■7.673 1.0031.58 ATOM 504 C ARGL 54 13.483 4.725 -6.552 1.0021.41 ATOM 505 O ARGL 54 13.273 4.403 -7.738 1.0021.21 ATOM 506 N ALAL 55 13.061 4.010 -5.489 1.0020.79 ATOM 508 CA ALAL 55 12.237 2.803 -5.629 1.0021.50 ATOM 509 CB ALAL 55 12.004 2.154 -4.262 1.0018.92 ATOM 510 C ALAL 55 10.932 3.185 6.282 1.0022.01 ATOM 511 O ALAL 55 10.488 4.307 ■ 6.147 1.0023.44 ATOM 512 N PROL 56 10.264 2.268 ■ 6.972 1.0025.55 ATOM 513 CD PROL 56 10.602 0.823 -7.094 1.0026.77 ATOM 514 CA PROL 56 9.019 2.583 -7.664 1.0024.82 ATOM 515 CB PROL 56 8.690 1.270 -8.406 1.0027.53 ATOM 516 CG PROL 56 9.286 0.224 -7.522 1.0027.71 ATOM 517 C PROL 56 7.914 3.046 -6.720 1.0025.91 ATOM 518 O PROL 56 7.749 2.531 -5.608 1.0026.27 ATOM 519 N GLYL 57 7.148 4.025 7.182 1.0026.28 ATOM 521 CA GLYL 57 6.054 4.562 -6.382 1.0022.74 ATOM 522 C GLYL 57 6.486 5.620 5.373 1.0020.96 ATOM 523 O GLYL 57 5.666 6.381 •4.908 1.0023.79 ATOM 524 N VAL L 58 7.764 5.662 ■5.014 1.0020.25 ATOM 526 CA VALL 58 8.231 6.660 -4.079 1.0018.53 ATOM 527 CB VALL 58 9.680 6.382 -3.699 1.0015.29 ATOM 528 CGI VALL 58 10.238 7.551 -2.940 1.0011.07 ATOM 529 CG2VALL 58 9.750 5.103 -2.874 1.0012.65 ATOM 530 C VALL 58 8.119 8.077 -4.675 1.0022.04 ATOM 531 O VALL 58 8.583 8.324 -5.803 1.0022.18 ATOM 532 N PRO L 59 7.524 9.045 - 3.894 1.0021.50 ATOM 533 CD PRO L 59 6.983 8.863 -2.521 1.0020.50 ATOM 534 CA PROL 59 7.336 10.449 -4.315 1.0017.94 ATOM 535 CB PRO L 59 6.841 11.133 -3.057 1.0018.92 ATOM 536 CG PROL 59 6.054 10.043 -2.414 1.0018.97 ATOM 537 C PROL 59 8.583 11.092 -4.837 1.0016.82 ATOM 538 O PROL 59 9.706 10.918 - -4 4..331111 11..00001155..4466 ATOM 539 N ALA L 60 8.370 11.873 - -5 5..885544 11..00001133..0055 ATOM 541 CA ALA L 60 9.447 12.523 -6.521 11..00001144..8833 ATOM 542 CB ALA L 60 8.871 13.289 -7.696 11..00001144..6699 ATOM 543 C ALA L 60 10.233 13.424 -5.570 11..00001133..4444 ATOM 544 O ALA L 60 11.407 13.633 -5.776 11..00001122..1144 ATOM 545 N ARGL 61 9.593 13.928 - •4.489 11..00001155..3300 ATOM 547 CA ARGL 61 10.309 14.825 -3.522 11..00001122..5599 ATOM 548 CB ARGL 61 9.349 15.408 -2.470 11..00001111..7722 ATOM 549 CG ARGL 61 8.620 14.397 - -11..558866 11..00001144..7799 ATOM 550 CD ARGL 61 7.890 15.077 - -00..441199 11..00001144..0000 ATOM 551 NE ARGL 61 7.226 14.114 0 0..447766 11..00001100..9999 ATOM 553 CZ ARGL 61 6.131 13.465 0 0..111144 11..00001111..7799 ATOM 554 NH1 ARGL 61 5.556 12.582 0 0..990088 11..00001100..7755 ATOM 557 NH2ARGL 61 5.624 13.684 -1.059 1.009.70 ATOM 560 C ARGL 61 11.500 14.173 -2.811 1.0012.82 ATOM 561 O ARGL 61 12.291 14.876 -2.112 1.0014.41 ATOM 562 N PHEL 62 11.649 12.845 - ■2.959 1.0011.27 ATOM 564 CA PHEL 62 12.749 12.133 -2.305 1.0010.94 ATOM 565 CB PHEL 62 12.274 10.739 -1.775 1.009.35 ATOM 566 CG PHEL 62 11.263 10.787 -0.649 1.009.62 ATOM 567 CD1 PHEL 62 11.683 10.906 0.690 1.005.49 ATOM 568 CD2PHEL 62 9.897 10.704 -0.919 1.006.68 ATOM 569 CE1 PHE L 62 10.760 10.943 1.698 1.002.51 ATOM 570 CE2PHEL 62 8.968 10.742 0.110 1.007.73 ATOM 571 CZ PHEL 62 9.399 10.864 1.419 1.004.66 ATOM 572 C PHEL 62 1 133..991144 1111..993388 - •3.265 1.009.16 ATOM 573 O PHEL 62 1133..669922 1111..442299 ■ ■4.340 1.008.82 ATOM 574 N SERL 63 1155..116600 1122..332255 - ■2.864 1.004.85 ATOM 576 CA SERL 63 1 166..330077 1122..111122 -3.733 1.008.59 ATOM 577 CB SERL 63 16.671 13.353 -4.534 1.007.17 ATOM 578 OG SERL 63 17.269 14.319 -3.694 1.0012.90 ATOM 580 C SERL 63 17.511 11.689 2.946 1.007.30 ATOM 581 O SERL 63 17.703 12.187 -1.852 1.009.45 ATOM 582 N GLYL 64 18.286 10.728 -3.503 1.005.56 ATOM 584 CA GLYL 64 19.495 10.269 -2.889 1.004.07 ATOM 585 C GLY L 64 20.676 10.881 -3.568 1.009.49 ATOM 586 O GLYL 64 20.620 11.246 -4.766 1.0012.20 ATOM 587 N SERL 65 21.758 11.031 -2.872 1.006.73 ATOM 589 CA SERL 65 22.865 11.665 -3.485 1.009.75 ATOM 590 CB SERL 65 22.581 13.171 -3.683 1.008.17 ATOM 591 OG SERL 65 22.791 13.906 -2.475 1.0010.45 ATOM 593 C SERL 65 24.064 11.437 -2.652 1.0010.16 ATOM 594 O SERL 65 23.978 10.692 -1.662 1.0010.96 ATOM 595 N LEUL 66 25.182 12.009 -3.085 1.0010.68 ATOM 597 CA LEU L 66 26.453 11.877 -2.394 1.009.69 ATOM 598 CB LEUL 66 27.441 11.114 -3.317 1.0013.61 ATOM 599 CG LEUL 66 28.218 9.861 -2.820 1.009.87 ATOM 600 CD1 LEU L 66 27.385 8.987 -1.932 1.008.09 ATOM 601 CD2 LEU L 66 28.680 9.048 -4.022 1.008.69 ATOM 602 C LEUL 66 26.918 13.316 ■2.147 1.0012.92 ATOM 603 O LEUL 66 27.054 14.087 -3.082 1.0010.87 ATOM 604 N ILEL 67 27.091 13.694 -0.865 1.0012.45 ATOM 606 CA ILEL 67 27.534 15.048 -0.518 1.0011.66 ATOM 607 CB ILEL 67 26.437 15.786 0.334 1.0012.96 ATOM 608 CG2 ILE L 67 26.820 17.222 0.568 1.0013.30 ATOM 609 CGI ILEL 67 25.074 15.750 -0.357 1.0013.53 ATOM 610 CD ILEL 67 23.962 16.437 0.419 1.0011.05 ATOM 611 C ILEL 67 28.837 14.913 0.268 1.0012.31 ATOM 612 O ILEL 67 28.856 14.332 1.339 1.0013.03 ATOM 613 N GLYL 68 29.946 15.384 -0.274 1.0013.08 ATOM 615 CA GLYL 68 31.199 15.196 0.416 1.0012.32 ATOM 616 C GLYL 68 31.463 13.701 0.568 1.0017.92 ATOM 617 O GLY L 68 31.201 12.934 -0.393 1.0016.67 ATOM 618 N ASP L 69 31.962 13.259 1.747 1.00 16.48 ATOM 620 CA ASP L 69 32.244 11.827 1.941 1.00 18.10 ATOM 621 CB ASP L 69 33.350 11.576 2.960 1.00 24.05 ATOM 622 CG ASP L 69 34.617 12.363 2.730 1.00 31.27 ATOM 623 OD1 ASP L 69 35.202 12.302 I 1.597 ' 1.00 32.40 ATOM 624 OD2 ASP L 69 35.038 13.053 5 3.707 ' 1.00 39.08 ATOM 625 C ASP L 69 31.040 11.041 2.429 1.00 14.56 ATOM 626 O ASP L 69 31.213 9.925 2.886 1.00 16.00 ATOM 627 N LYS L 70 29.837 11.573 2.321 1.00 1 1.13 ATOM 629 CA LYS L 70 28.693 10.853 2.847 1.00 1 1.46 ATOM 630 CB LYS L 70 28.125 11.600 4.028 1.00 1 1.39 ATOM 631 CG LYS L 70 29.012 11.550 5.248 1.00 18.50 ATOM 632 CD LYS L 70 28.263 12.078 6.455 1.00 20.15 ATOM 633 CE LYS L 70 28.152 13.574 6.391 1.00 22.74 ATOM 634 NZ LYS L 70 29.502 14.187 6.360 1.00 27.69 ATOM 638 C LYS L 70 27.593 10.635 1.869 1.00 10.75 ATOM 639 O LYS L 70 27.478 11.366 0.879 1.00 1 1.35 ATOM 640 N ALA L 71 26.759 9.619 2.144 1.00 6.32 ATOM 642 CA ALA L 71 25.537 9.475 1.385 1.00 2.44 ATOM 643 CB ALA L 71 25.056 8.033 1.399 1.00 2.00 ATOM 644 C ALA L 71 24.483 10.396 2.027 1.00 6.77 ATOM 645 O ALA L 71 24.518 10.670 3.253 1.00 6.10 ATOM 646 N ALA L 72 23.557 10.888 1.235 1.00 5.00 ATOM 648 CA ALA L 72 22.570 11.814 [ 1.741 1.00 6.21 ATOM 649 CB ALA L 72 23.042 13.257 ' 1.524 1.00 3.82 ATOM 650 C ALA L 72 21.215 11.570 1.100 1.00 4.44 ATOM 651 O ALA L 72 21.109 11.043 -0.045 1.00 6.60 ATOM 652 N LEU L 73 20.186 11.854 1.883 1.00 5.08 ATOM 654 CA LEU L 73 18.799 11.765 1.446 1.00 4.01 ATOM 655 CB LEU L 73 17.970 10.823 2.319 1.00 4.42 ATOM 656 CG LEU L 73 16.494 10.793 1.959 1.00 4.74 ATOM 657 CD1 LEU L 73 16.290 9.999 0.667 1.00 4.42 ATOM 658 CD2 LEU L 73 15.684 10.194 3.100 1.00 8.67 ATOM 659 C LEU L 73 18.198 13.141 1.576 1.00 5.38 ATOM 660 O LEU L 73 18.297 13.756 2.622 1.00 9.62 ATOM 661 N THR L 74 17.617 13.635 0.531 1.00 7.72 ATOM 663 CA THR L 74 17.024 14.935 0.566 1.00 6.80 ATOM 664 CB THR L 74 17.721 15.910 -0.447 1.00 9.87 ATOM 665 OG1 THR L 74 19.099 16.158 -0.011 1.00 4.69 ATOM 667 CG2 THR L 74 16.961 17.216 -0.538 1.00 4.65 ATOM 668 C THR L 74 15.593 14.857 0.275 1.00 7.31 ATOM 669 O THR L 74 15.182 14.221 -0.672 1.00 6.60 ATOM 670 N ILE L 75 14.816 15.472 1.136 1.00 8.15 ATOM 672 CA ILE L 75 13.413 15.560 0.923 1.00 9.10 ATOM 673 CB ILE L 75 12.620 15.131 2.171 1.00 11.95 ATOM 674 CG2 ILE L 75 1 1.148 15.053 1.822 1.00 12.49 ATOM 675 CGI ILE L 75 13.146 13.794 2.729 1.00 16.99 ATOM 676 CD ILE L 75 12.335 13.263 3.909 1.00 15.52 ATOM 677 C ILE L 75 13.092 17.018 0.628 1.00 12.05 ATOM 678 O ILE L 75 13.192 17.866 1.520 1.00 10.42 ATOM 679 N THR L 76 12.722 17.309 -0.627 1.00 13.27 ATOM 681 CA THR L 76 12.393 18.674 -1.039 1.00 1 1.86 ATOM 682 CB THR L 76 12.724 18.884 -2.519 1.00 8.49 ATOM 683 OG1 THR L 76 14.092 18.564 -2.749 1.00 7.34 ATOM 685 CG2 THR L 76 12.480 20.309 -2.892 1.00 8.93 ATOM 686 C THR L 76 10.907 18.987 -0.848 1.00 15.75 ATOM 687 O THR L 76 10.051 18.407 -1.523 1.00 19.95 ATOM 688 N GLY L 77 10.593 19.939 0.038 1.00 17.30 ATOM 690 CA GLY L 77 9.197 20.267 0.278 1.00 15.95 ATOM 691 C GLY L 77 8.573 19.198 1.109 1.00 16.40 ATOM 692 O GLY L 77 7.498 18.704 0.788 1.00 17.47 ATOM 693 N ALA L 78 9.247 18.836 2.189 1.00 16.13 ATOM 695 CA ALA L 78 8.771 17.740 3.065 1.00 16.88 ATOM 696 CB ALA L 78 9.672 17.614 4.284 1.00 15.72 ATOM 697 C ALA L 78 7.304 17.900 3.476 1.00 17.09 ATOM 698 O ALA L 78 6.803 19.006 3.676 1.00 20.02 ATOM 699 N GLN L 79 6.596 16.779 3.543 1.00 16.23 ATOM 701 CA GLN L 79 5.203 16.781 3.933 1.00 14.31 ATOM 702 CB GLN L 79 4.426 16.047 2.865 1.00 13.55 ATOM 703 CG GLN L 79 4.481 16.789 1.539 1.00 17.28 ATOM 704 CD GLN L 79 3.673 16.137 0.434 1.00 22.72 ATOM 705 OE1 GLN L 79 3.812 16.51 1 -0.749 1.00 28.20 ATOM 706 NE2 GLN L 79 2.814 15.173 0.777 1.0022.58 ATOM 709 C GLN L 79 4.997 16.154 5.332 1.0014.89 ATOM 710 O GLNL 79 5.885 15.484 5.845 1.0014.38 ATOM 711 N THRL 80 3.836 16.376 5.932 1.0012.50 ATOM 713 CA THRL 80 3.593 15.907 7.302 1.0018.91 ATOM 714 CB THRL 80 2.233 16.385 7.818 1.0017.20 ATOM 715 OG1 THRL 80 1.228 15.959 6.895 1.0021.04 ATOM 717 CG2THRL 80 2.207 17.905 7.935 1.0019.65 ATOM 718 C THRL 80 3.631 14.391 7.375 1.0019.00 ATOM 719 O THRL 80 4.022 13.822 8.414 1.0021.72 ATOM 720 N GLUL 81 3.227 13.766 6.258 1.0018.63 ATOM 722 CA GLUL 81 3.239 12.330 6.113 1.0019.81 ATOM 723 CB GLUL 81 2.562 11.959 4.811 1.0024.17 ATOM 724 CG GLUL 81 3.364 12.403 3.595 1.0034.44 ATOM 725 CD GLUL 81 2.692 12.102 2.262 1.0040.56 ATOM 726 OE1 GLUL 81 1.653 12.768 1.948 1.0044.10 ATOM 727 OE2GLUL 81 3.204 11.208 1.517 1.0043.81 ATOM 728 C GLUL 81 4.662 11.783 6.107 1.0018.55 ATOM 729 O GLUL 81 4.842 10.589 6.074 1.0020.36 ATOM 730 N ASPL 82 5.677 12.654 6.111 1.0014.45 ATOM 732 CA ASPL 82 7.037 12.191 6.090 1.0011.96 ATOM 733 CB ASPL 82 7.919 13.129 5.269 1.0011.90 ATOM 734 CG ASPL 82 7.522 13.200 3.796 1.0013.46 ATOM 735 OD1 ASP L 82 6.770 12.333 3.312 1.0016.83 ATOM 736 OD2ASPL 82 7.942 14.138 3.146 1.0013.86 ATOM 737 C ASPL 82 7.618 12.080 7.489 1.0012.84 ATOM 738 O ASPL 82 8.815 11.743 7.640 1.009.40 ATOM 739 N GLUL 83 6.854 12.472 8.523 1.0013.25 ATOM 741 CA GLUL 83 7.368 12.247 9.879 1.0013.46 ATOM 742 CB GLUL 83 6.377 12.778 10.935 1.0017.14 ATOM 743 CG GLUL 83 6.860 12.654 12.394 1.0021.93 ATOM 744 CD GLU L 83 6.084 13.563 13.357 1.0026.14 ATOM 745 OE1 GLU L 83 5.765 14.702 12.969 1.0022.27 ATOM 746 OE2GLUL 83 5.784 13.135 14.508 1.0027.48 ATOM 747 C GLUL 83 7.524 10.722 9.983 1.009.35 ATOM 748 O GLUL 83 6.546 9.998 9.788 1.0012.41 ATOM 749 N ALA L 84 8.726 10.256 10.222 1.009.86 ATOM 751 CA ALAL 84 8.997 8.822 10.227 1.008.78 ATOM 752 CB ALAL 84 8.687 8.250 8.849 1.007.20 ATOM 753 C ALAL 84 10.444 8.637 10.557 1.008.36 ATOM 754 O ALAL 84 11.129 9.618 10.780 1.0011.79 ATOM 755 N ILEL 85 10.930 7.406 10.620 1.00 8.82 ATOM 757 CA ILEL 85 12.365 7.197 10.876 1.007.36 ATOM 758 CB ILEL 85 12.576 6.149 11.967 1.005.25 ATOM 759 CG2 ILE L 85 14.058 5.950 12.279 1.009.66 ATOM 760 CGI ILEL 85 11.829 6.632 13.216 1.0013.36 ATOM 761 CD ILEL 85 11.520 5.579 14.233 1.0010.12 ATOM 762 C ILEL 85 12.980 6.752 9.547 1.005.85 ATOM 763 O ILEL 85 12.301 6.101 8.761 1.006.76 ATOM 764 N TYRL 86 14.179 7.216 9.269 1.004.42 ATOM 766 CA TYRL 86 14.865 6.907 7.980 1.007.23 ATOM 767 CB TYRL 86 15.171 8.183 7.182 1.006.83 ATOM 768 CG TYRL 86 13.929 8.853 6.706 1.008.61 ATOM 769 CD1 TYRL 86 13.203 9.680 7.591 1.005.73 ATOM 770 CE1TYRL 86 11.959 10.169 7.242 1.008.65 ATOM 771 CD2TYRL 86 13.378 8.552 5.435 1.005.92 ATOM 772 CE2TYRL 86 12.118 9.046 5.095 1.006.08 ATOM 773 CZ TYRL 86 11.411 9.853 6.010 1.008.14 ATOM 774 OH TYRL 86 10.125 10.288 5.715 1.006.40 ATOM 776 C TYRL 86 16.156 6.236 8.237 1.002.00 ATOM 777 O TYRL 86 16.988 6.765 8.973 1.008.00 ATOM 778 N PHEL 87 16.316 5.060 7.681 1.005.92 ATOM 780 CA PHEL 87 17.574 4.313 7.849 1.004.34 ATOM 781 CB PHEL 87 17.276 2.846 8.207 1.008.38 ATOM 782 CG PHEL 87 16.579 2.690 9.499 1.009.99 ATOM 783 CD1 PHEL 87 17.303 2.497 10.645 1.006.06 ATOM 784 CD2PHEL 87 15.190 2.725 9.551 1.0013.30 ATOM 785 CE1 PHEL 87 16.642 2.328 11.868 1.0010.61 ATOM 786 CE2PHEL 87 14.523 2.562 10.757 1.0014.04 ATOM 787 CZ PHEL 87 15.261 2.361 11.919 1.008.48 ATOM 788 C PHEL 87 18.331 4.301 6.563 1.003.22 ATOM 789 O PHEL 87 17.698 4.278 5.518 1.002.51 ATOM 790 N CYS L 88 19.647 4.308 6.639 1.00 5.93 ATOM 792 CA CYS L 81 20.437 4.146 5.446 1.00 9.35 ATOM 793 CB CYS L 8i 21.402 5.306 5.236 1.00 5.49 ATOM 794 SG CYS L 88 22.756 5.378 6.415 1.00 15.50 ATOM 795 C CYS L 88 21.214 2.859 5.589 1.00 8.53 ATOM 796 O CYS L 88 21.502 2.427 6.714 1.00 8.84 ATOM 797 N ALA L 89 21.496 2.220 4.494 1.00 8.42 ATOM 799 CA ALA L 89 22.252 0.975 4.532 1.00 8.94 ATOM 800 CB ALA L 89 21.301 -0.198 4.197 1.00 6.42 ATOM 801 C ALA L 89 23.390 1.092 3.510 1.00 1 1.22 ATOM 802 O ALA L 89 23.172 1.603 2.416 1.00 10.12 ATOM 803 N LEU L 90 24.596 0.666 3.877 1.00 12.71 ATOM 805 CA LEU L 90 25.735 0.737 2.984 1.00 12.28 ATOM 806 CB LEU L 90 26.856 1.594 3.591 1.00 13.85 ATOM 807 CG LEU L 90 26.572 3.096 3.773 1.00 10.32 ATOM 808 CD1 LEU L 90 27.881 3.801 4.146 1.00 7.96 ATOM 809 CD2 LEU L 90 25.963 3.678 2.485 1.00 10.49 ATOM 810 C LEU L 90 26.279 -0.668 2.683 1.00 14.32 ATOM 811 O LEU L 90 26.363 -1.520 3.607 1.00 14.08 ATOM 812 N TRP L 91 26.664 - 0.881 1.385 1.00 10.21 ATOM 814 CA TRP L 91 27.175 -2.175 0.892 1.00 9.56 ATOM 815 CB TRP L 91 26.710 -2.415 -0.556 1.00 13.24 ATOM 816 CG TRP L 91 27.344 -3.582 -1.305 1.00 16.93 ATOM 817 CD2 TRP L 91 26.959 -5.000 -1.258 1.00 18.28 ATOM 818 CE2 TRP L 91 27.643 -5.656 -2.300 1.00 18.63 ATOM 819 CE3 TRP L 91 26.093 -5.774 -0.450 1.00 18.52 ATOM 820 CD1 TRP L 91 28.238 -3.469 -2.337 1.00 18.74 ATOM 821 NE1 TRP L 91 28.401 -4.692 -2.918 1.00 18.84 ATOM 823 CZ2 TRP L 91 27.502 -7.049 -2.570 1.00 17.39 ATOM 824 CZ3 TRP L 91 25.947 -7.155 -0.717 1.00 20.45 ATOM 825 CH2 TRP L 91 26.658 -7.779 -1.778 1.00 18.96 ATOM 826 C TRP L 91 28.657 - 2.194 0.947 1.00 8.96 ATOM 827 O TRP L 91 29.308 •1.254 0.489 1.00 9.38 ATOM 828 N TYR L 92 29.194 -3.229 1.552 1.00 9.41 ATOM 830 CA TYR L 92 30.624 -3.377 1.642 1.00 10.88 ATOM 831 CB TYR L 92 31.083 -3.349 3.115 1.00 13.13 ATOM 832 CG TYR L 92 30.867 -2.023 3.840 1.00 12.25 ATOM 833 CD 1 TYR L 92 29.721 -1.780 4.606 1.00 15.61 ATOM 834 CE1 TYR L 92 29.514 -0.552 5.234 1.00 11.01 ATOM 835 CD2 TYR L 92 31.808 -1.003 3.741 1.00 14.35 ATOM 836 CE2 TYR L 92 31.607 0.208 4.358 1.00 12.95 ATOM 837 CZ TYR L 92 30.464 0.437 5.090 1.00 11.34 ATOM 838 OH TYR L 92 30.246 1.701 5.613 1.00 14.51 ATOM 840 C TYR L 92 31.048 -4.687 0.967 1.00 15.14 ATOM 841 O TYR L 92 31.339 -5.693 1.650 1.00 14.53 ATOM 842 N SER L 93 31.013 -4.663 0.383 1.00 16.81 ATOM 844 CA SER L 93 31.449 -5.786 -1.249 1.00 18.41 ATOM 845 CB SER L 93 32.878 -6.169 -0.907 1.00 19.53 ATOM 846 OG SER L 93 33.736 -5.094 -1.258 1.00 25.55 ATOM 848 C SER L 93 30.564 7.029 1.238 1.00 20.20 ATOM 849 O SER L 93 30.249 •7.587 -2.322 1.00 17.43 ATOM 850 N ASN L 94 30.202 -7.492 -0.025 1.00 19.09 ATOM 852 CA ASN L 94 29.415 -8.690 0.109 1.00 19.31 ATOM 853 CB ASN L 94 30.341 -9.916 0.037 1.00 18.06 ATOM 854 CG ASN L 94 31.359 -9.928 1.153 1.00 22.80 ATOM 855 OD1 ASN L 94 31.378 -9.025 2.026 1.00 22.03 ATOM 856 ND2 ASN L 94 32.210 -10.949 1.157 1.00 21.52 ATOM 859 C ASN L 94 28.595 -8.688 1.403 1.00 20.27 ATOM 860 O ASN L 94 28.147 -9.737 1.863 1.0022.39 ATOM 861 N HIS L 95 28.396 - 7.508 1.999 1.00 19.53 ATOM 863 CA HIS L 95 27.529 -7.400 3.161 1.00 18.65 ATOM 864 CB HIS L 95 28.237 -7.853 4.407 1.00 16.28 ATOM 865 CG HIS L 95 29.404 -7.005 4.792 1.00 19.96 ATOM 866 CD2 HIS L 95 30.622 -6.861 4.235 1.00 17.79 ATOM 867 ND1 HIS L 95 29.430 -6.221 5.938 1.00 20.98 ATOM 869 CE1 HIS L 95 30.606 -5.630 6.085 1.00 22.66 ATOM 870 NE2 HIS L 95 31.326 -6.018 5.055 1.00 20.00 ATOM 872 C HIS L 95 27.016 - 5.983 3.353 1.00 17.00 ATOM 873 O HIS L 95 27.555 -5.053 2.798 1.00 16.62 ATOM 874 N TRP L 96 25.973 -5.841 4.146 1.00 15.07 ATOM 876 CA TRP L 96 25.375 -4.539 4.379 1.00 13.84 ATOM 877 CB TRP L 96 23.874 -4.536 4.055 1.00 12.09 ATOM 878 CG TRP L 96 23.538 -4.737 2.603 1.00 14.83 ATOM 879 CD2 TRP L 96 23.352 -3.708 1.608 1.00 12.10 ATOM 880 CE2 TRP L 96 22.935 -4.340 0.424 1.00 13.36 ATOM 881 CE3 TRP L 96 23.490 -2.310 1.610 1.00 11.19 ATOM 882 CD1 TRP L 96 23.243 -5.913 1.998 1.00 15.53 ATOM 883 NE1 TRP L 96 22.883 -5.675 0.705 1.00 14.17 ATOM 885 CZ2 TRP L 96 22.659 -3.631 -0.762 1.00 9.46 ATOM 886 CZ3 TRP L 96 23.208 -1.605 0.441 1.00 7.52 ATOM 887 CH2 TRP L 96 22.800 -2.264 -0.725 1.00 1 1.56 ATOM 888 C TRP L 96 25.495 -4.170 5.810 1.00 14.61 ATOM 889 O TRP L 96 25.427 -5.064 6.666 1.00 12.87 ATOM 890 N VAL L 97 25.684 -2.861 6.040 1.00 11.97 ATOM 892 CA VAL L 97 25.622 -2.286 7.380 1.00 13.35 ATOM 893 CB VAL L 97 26.975 -1.797 7.840 1.00 12.63 ATOM 894 CGI VAL L 97 26.871 -1.164 9.220 1.00 14.09 ATOM 895 CG2 VAL L 97 27.888 -3.005 7.873 1.00 8.66 ATOM 896 C VAL L 97 24.605 -1.151 7.396 1.00 14.93 ATOM 897 O VAL L 97 24.590 -0.314 6.485 1.00 9.72 ATOM 898 N PHE L 98 23.668 -1.219 8.353 1.00 13.01 ATOM 900 CA PHE L 98 22.630 -0.221 8.460 1.00 12.29 ATOM 901 CB PHE L 98 21.310 -0.843 8.887 1.00 9.91 ATOM 902 CG PHE L 98 20.504 -1.468 7.803 1.00 7.44 ATOM 903 CD1 PHE L 98 20.808 -2.728 7.341 1.00 9.14 ATOM 904 CD2 PHE L 98 19.386 -0.836 7.316 1.00 6.37 ATOM 905 CE1 PHE L 98 20.000 -3.337 6.425 1.00 6.90 ATOM 906 CE2 PHE L 98 18.560 -1.438 6.388 1.00 8.01 ATOM 907 CZ PHE L 98 18.866 -2.696 5.939 1.00 7.78 ATOM 908 C PHE L 98 23.038 0.846 9.456 1.00 1 1.91 ATOM 909 O PHE L 98 23.874 0.594 10.318 1.00 11.43 ATOM 910 N GLY L 99 22.533 2.062 9.247 1.00 14.08 ATOM 912 CA GLY L 99 22.804 3.151 10.148 1.00 12.11 ATOM 913 C GLY L 99 21.820 3.098 11.296 1.00 11.79 ATOM 914 O GLY L 99 20.893 2.304 1 1.265 1.00 10.46 ATOM 915 N GLY L 100 22.005 3.957 12.289 1.00 12.00 ATOM 917 CA GLY L 100 21.125 3.950 13.458 1.00 8.79 ATOM 918 C GLY L 100 19.739 4.511 13.254 1.00 9.23 ATOM 919 O GLY L 100 18.840 4.293 14.098 1.00 12.86 ATOM 920 N GLY L 101 19.513 5.213 12.163 1.00 7.60 ATOM 922 CA GLY L 101 18.185 5.779 1 1.930 1.00 4.00 ATOM 923 C GLY L 101 18.156 7.209 12.445 1.00 7.52 ATOM 924 O GLY L 101 18.921 7.549 13.417 1.00 7.76 ATOM 925 N THR L 102 17.414 8.053 1 1.698 1.00 8.12 ATOM 927 CA THR L 102 17.192 9.492 12.014 1.00 7.96 ATOM 928 CB THR L 102 17.613 10.425 10.805 1.00 7.52 ATOM 929 OG1 THR L 102 19.020 10.319 10.576 1.00 4.45 ATOM 931 CG2 THR L 102 17.266 11.885 1 1.056 1.00 4.44 ATOM 932 C THR L 102 15.707 9.657 12.212 1.00 10.01 ATOM 933 O THR L 102 14.965 9.257 11.330 1.00 11.13 ATOM 934 N LYS L 103 15.221 10.188 13.349 1.00 10.41 ATOM 936 CA LYS L 103 13.779 10.404 13.436 1.00 11.36 ATOM 937 CB LYS L 103 13.226 10.449 14.887 1.00 14.52 ATOM 938 CG LYS L 103 1 1.770 11.006 14.917 1.00 16.54 ATOM 939 CD LYS L 103 11.191 1 1.143 16.337 1.00 12.70 ATOM 940 CE LYS L 103 9.718 11.536 16.299 1.00 14.64 ATOM 941 NZ LYS L 103 8.869 10.602 15.451 1.00 17.17 ATOM 945 C LYS L 103 13.446 11.719 12.778 1.00 10.60 ATOM 946 O LYS L 103 14.022 12.721 13.143 1.00 12.19 ATOM 947 N LEU L 104 12.508 1 1.730 11.847 1.00 9.69 ATOM 949 CA LEU L 104 12.168 12.978 1 1.228 1.00 11.35 ATOM 950 CB LEU L 104 12.128 12.887 9.693 1.00 9.61 ATOM 951 CG LEU L 104 11.734 14.219 9.032 1.00 10.81 ATOM 952 CD1 LEU L 104 12.879 15.223 9.204 1.00 2.00 ATOM 953 CD2 LEU L 104 11.370 13.998 7.591 1.00 10.86 ATOM 954 C LEU L 104 10.849 13.494 11.718 1.00 10.04 ATOM 955 O LEU L 104 9.857 12.786 1 1.669 1.00 16.01 ATOM 956 N THR L 105 10.832 14.730 12.221 1.00 1 1.71 ATOM 958 CA THR L 105 9.581 15.367 12.551 1.00 7.07 ATOM 959 CB THR L 105 9.634 16.082 13.932 1.00 9.46 ATOM 960 OG1 THR L 105 9.752 15.104 14.961 1.00 12.27 ATOM 962 CG2 THR L 105 8.383 16.936 14.168 1.00 2.15 ATOM 963 C THR L 105 9.232 16.415 11.493 1.00 7.56 ATOM 964 O THR L 105 10.043 17.245 11.158 1.00 9.71 ATOM 965 N VAL L 106 8.045 16.320 10.958 1.009.73 ATOM 967 CA VALL 106 7.502 17.366 10.095 1.0011.58 ATOM 968 CB VAL L 106 7.077 16.862 8.710 1.009.06 ATOM 969 CGI VALL 106 6.497 18.013 7.899 1.006.52 ATOM 970 CG2 VALL 106 8.310 16.244 8.006 1.0010.40 ATOM 971 C VALL 106 6.301 17.925 10.847 1.0011.09 ATOM 972 O VALL 106 5.207 17.320 10.868 1.0013.54 ATOM 973 N LEU L 106 A 6.577 19.053 11.520 1.0012.43 ATOM 975 CA LEUL106A 5.642 19.701 12.379 1.0012.13 ATOM 976 CB LEUL106A 6.113 21.124 12.661 1.009.12 ATOM 977 CG LEU L 106 A 7.48721.216 13.339 1.007.72 ATOM 978 CD1LEUL106A 7.97722.640 13.275 1.009.05 ATOM 979 CD2LEUL106A 7.42520.710 14.802 1.006.98 ATOM 980 C LEUL106A 4.312 19.671 11.757 1.0013.07 ATOM 981 O LEUL106A 4.07920.351 10.783 1.0018.75 ATOM 982 N GLY L 107 3.459 18.809 12.289 1.0014.91 ATOM 984 CA GLY L 107 2.110 18.678 11.759 1.0016.40 ATOM 985 C GLYL 107 1.061 19.131 12.754 1.0015.29 ATOM 986 O GLYL 107 -0.116 18.916 12.541 1.0016.64 ATOM 987 N SERL 108 1.523 19.749 13.846 1.0018.60 ATOM 989 CA SERL 108 0.65420.252 14.900 1.0018.91 ATOM 990 CB SERL 108 0.113 19.115 15.777 1.0021.02 ATOM 991 OG SERL 108 1.150 18.546 16.571 1.0027.15 ATOM 993 C SERL 108 1.46621.163 15.756 1.0017.58 ATOM 994 O SERL 108 2.68921.205 15.631 1.0017.99 ATOM 995 N GLUL 109 0.79621.813 16.676 1.0017.83 ATOM 997 CA GLU L 109 1.42822.764 17.513 1.0016.58 ATOM 998 CB GLU L 109 0.331 23.558 18.218 1.0021.42 ATOM 999 CG GLUL 109 -0.49324.469 17.312 1.0026.54 ATOM 1000 CD GLUL 109 -1.29323.737 16.2380.5027.76 ATOM 1001 OE1 GLUL 109 -1.72422.605 16.5120.5028.73 ATOM 1002 OE2GLUL109 -1.49524.302 15.1130.5026.82 ATOM 1003 C GLUL 109 2.29722.034 18.519 1.0017.20 ATOM 1004 O GLUL 109 1.92020.963 18.969 1.0014.41 ATOM 1005 N LYSL 110 3.43722.590 18.885 1.0016.72 ATOM 1007 CA LYS LI 10 4.26521.907 19.855 1.0020.99 ATOM 1008 CB LYSL 110 5.61022.57620.013 1.0022.20 ATOM 1009 CG LYS LI 10 6.48522.357 18.796 1.0024.75 ATOM 1010 CD LYS LI 10 7.79023.103 18.889 1.0025.15 ATOM 1011 CE LYSL 110 8.52823.039 17.563 1.0030.78 ATOM 1012 NZ LYSL 110 9.92823.555 17.661 1.0032.12 ATOM 1016 C LYSL 110 3.55721.79021.192 1.0021.68 ATOM 1017 O LYSL 110 2.75322.651 21.562 1.0022.35 ATOM 1018 N SERL 111 3.83620.68721.879 1.0022.71 ATOM 1020 CA SER L 111 3.20520.37223.162 1.0021.05 ATOM 1021 CB SERL 111 2.148 19.30822.923 1.0022.18 ATOM 1022 OG SERL 111 1.301 19.14924.046 1.0023.73 ATOM 1024 C SERL 111 4.276 19.861 24.147 1.0021.55 ATOM 1025 O SERL 111 5.085 18.98923.799 1.0021.72 ATOM 1026 N SERL 112 4.34720.47325.339 1.0019.80 ATOM 1028 CA SERL 112 5.31720.07726.346 1.0017.43 ATOM 1029 CB SERL 112 5.38921.17427.397 1.0020.85 ATOM 1030 OG SERL 112 6.341 22.16527.033 1.0029.98 ATOM 1032 C SERL 112 4.918 18.74926.998 1.0014.25 ATOM 1033 O SERL 112 3.726 18.42727.069 1.0019.12 ATOM 1034 N PROL 113 5.860 17.94627.492 1.0010.92 ATOM 1035 CD PROL 113 7.314 18.15927.548 1.007.81 ATOM 1036 CA PROL 113 5.491 16.69628.117 1.0012.79 ATOM 1037 CB PROL 113 6.794 15.98228.227 1.008.93 ATOM 1038 CG PROL 113 7.734 17.08828.499 1.009.20 ATOM 1039 C PROL 113 4.824 16.89629.483 1.0013.59 ATOM 1040 O PROL 113 5.181 17.79930.251 1.0013.35 ATOM 1041 N SERL 114 3.810 16.11629.741 1.0015.55 ATOM 1043 CA SERL 114 3.233 16.06631.058 1.0015.08 ATOM 1044 CB SERL 114 1.734 15.863 30.975 1.0017.33 ATOM 1045 OG SERL 114 1.142 15.94732.273 1.0025.09 ATOM 1047 C SERL 114 3.904 14.92231.825 1.0016.29 ATOM 1048 O SERL 114 3.795 13.73231.458 1.0015.53 ATOM 1049 N VALL 115 4.628 15.301 32.864 1.0012.98 ATOM 1051 CA VAL LI 15 5.425 14.37433.668 1.0012.33 ATOM 1052 CB VALL 115 6.750 15.00533.997 1.006.39 ATOM 1053 CGI VALL 115 7.689 13.95734.586 1.003.44 ATOM 1054 CG2 VAL L 115 7.329 15.64932.742 1.009.96 ATOM 1055 C VALL 115 4.770 13.99935.000 1.0013.58 ATOM 1056 O VALL 115 4.200 14.83735.678 1.0013.43 ATOM 1057 N THRL 116 4.877 12.751 35.360 1.0012.99 ATOM 1059 CA THRL 116 4.395 12.291 36.646 1.0011.92 ATOM 1060 CB THRL 116 3.063 11.54436.555 1.0010.15 ATOM 1061 OG1THRL 116 2.131 12.353 35.844 1.005.53 ATOM 1063 CG2 THR LI 16 2.518 11.24237.963 1.0010.07 ATOM 1064 C THRL 116 5.424 11.33937.206 1.0013.44 ATOM 1065 O THRL 116 5.890 10.42036.477 1.0013.00 ATOM 1066 N LEUL 117 5.817 11.57438.463 1.009.86 ATOM 1068 CA LEUL 117 6.772 10.69739.109 1.0010.48 ATOM 1069 CB LEUL 117 7.979 11.49439.504 1.00 8.99 ATOM 1070 CG LEUL 117 9.092 10.70840.182 1.0013.84 ATOM 1071 CD1 LEUL 117 9.754 9.741 39.203 1.0010.30 ATOM 1072 CD2 LEU L 117 10.103 11.68340.772 1.0017.17 ATOM 1073 C LEU LI 17 6.129 9.96940.328 1.009.98 ATOM 1074 O LEUL 117 5.449 10.57541.149 1.0012.16 ATOM 1075 N PHEL 118 6.314 8.67640.398 1.009.99 ATOM 1077 CA PHEL 118 5.728 7.871 41.449 1.009.51 ATOM 1078 CB PHEL 118 4.868 6.75640.872 1.006.53 ATOM 1079 CG PHEL 118 3.648 7.20940.167 1.006.03 ATOM 1080 CD1 PHEL 118 2.533 7.61740.889 1.004.85 ATOM 1081 CD2 PHEL 118 3.574 7.14838.760 1.003.25 ATOM 1082 CE1PHEL 118 1.345 7.94740.244 1.006.00 ATOM 1083 CE2PHEL 118 2.398 7.48438.118 1.002.00 ATOM 1084 CZ PHEL 118 1.272 7.881 38.861 1.003.81 ATOM 1085 C PHEL 118 6.816 7.22542.272 1.009.33 ATOM 1086 O PHEL 118 7.836 6.72641.745 1.009.88 ATOM 1087 N PROL 119 6.624 7.22743.591 1 .009.00 ATOM 1088 CD PROL 119 5.458 7.83744.283 1.007.59 ATOM 1089 CA PROL 119 7.582 6.62244.541 1.008.55 ATOM 1090 CB PROL 119 7.173 7.28345.851 1.009.62 ATOM 1091 CG PROL 119 5.685 7.38045.703 1.009.04 ATOM 1092 C PROL 119 7.379 5.121 44.603 1.004.72 ATOM 1093 O PROL 119 6.383 4.64744.105 1.006.50 ATOM 1094 N PRO L 120 8.311 4.36345.159 1.003.79 ATOM 1095 CD PROL 120 9.661 4.78445.473 1.006.28 ATOM 1096 CA PROL 120 8.158 2.91045.301 1.006.76 ATOM 1097 CB PROL 120 9.507 2.41645.767 1.009.39 ATOM 1098 CG PROL 120 10.194 3.621 46.269 1.005.45 ATOM 1099 C PROL 120 7.032 2.55246.267 1.0010.87 ATOM 1100 O PROL 120 6.788 3.26347.246 1.0011.35 ATOM 1101 N SERL 121 6.276 1.51845.944 1.0012.02 ATOM 1103 CA SERL 121 5.172 1.10546.811 1.0014.15 ATOM 1104 CB SERL 121 4.160 0.18746.055 1.0013.52 ATOM 1105 OG SERL 121 4.706 -1.08345.758 1.0014.31 ATOM 1107 C SERL 121 5.737 0.41548.061 1.0015.89 ATOM 1108 O SERL 121 6.916 0.00548.087 1.0014.68 ATOM 1109 N SERL 122 4.923 0.34249.116 1.0015.71 ATOM 1111 CA SER L 122 5.363 -0.30850.339 1.0017.27 ATOM 1112 CB SER L 122 4.334 -0.05751.448 1.0017.69 ATOM 1113 OG SERL 122 3.023 -0.391 51.004 1.0025.59 ATOM 1115 C SERL 122 5.512 - ■1.801 50.069 1.0014.07 ATOM 1116 O SERL 122 6.481 - -2.42650.529 1.0016.14 ATOM 1117 N ALAL 123 4.559 -2.33849.272 1.0011.63 ATOM 1119 CA ALA L 123 4.558 3.76948.934 1.0010.10 ATOM 1120 CB ALA L 123 3.319 -4.10648.130 1.0013.01 ATOM 1121 C ALAL 123 5.828 ■ 4.14848.204 1.009.75 ATOM 1122 O ALAL 123 6.478 ■5.13448.560 1.006.87 ATOM 1123 N GLU L 124 6.253 ■3.321 47.225 1.008.37 ATOM 1125 CA GLU L 124 7.493 -3.60246.545 1.007.57 ATOM 1126 CB GLU LI 24 7.789 -2.65345.377 1.009.85 ATOM 1127 CG GLU LI 24 9.123 -2.99244.703 1.009.19 ATOM 1128 CD GLUL 124 9.466 -2.11743.521 1.008.89 ATOM 1129 OE1 GLU L 124 8.843 -1.07943.377 1.0011.65 ATOM 1130 OE2 GLU L 124 10.370 -2.461 42.741 1.0010.96 ATOM 1131 C GLUL 124 8.653 -3.53747.482 1.008.44 ATOM 1132 O GLUL 124 9.501 -4.43547.473 1.007.83 ATOM 1133 N LEU L 125 8.701 -2.48448.325 1.0010.06 ATOM 1135 CA LEU L 125 9.842 -2.28749.268 1.008.99 ATOM 1136 CB LEU L 125 9.576 -1.04950.147 1.006.82 ATOM 1137 CG LEUL 125 9.871 0.27949.439 1.00 8.44 ATOM 1138 CD1 LEUL 125 9.200 1.466 50.110 1.0010.23 ATOM 1139 CD2 LEU L 125 11.373 0.47549.349 1.0010.82 ATOM 1140 C LEUL 125 10.121 -3.49450.150 1.007.68 ATOM 1141 O LEUL 125 11.288 -3.78650.519 1.006.19 ATOM 1142 N GLUL 126 9.069 -4.188 50.506 1.009.15 ATOM 1144 CA GLUL 126 9.227 -5.365 51.341 1.0012.67 ATOM 1145 CB GLUL 126 7.899 •6.02051.519 1.0015.98 ATOM 1146 CG GLUL 126 6.888 -5.13752.171 1.0019.89 ATOM 1147 CD GLUL 126 5.648 -5.90752.484 1.0022.91 ATOM 1148 OE1 GLUL 126 5.696 -7.17452.467 1.0024.59 ATOM 1149 OE2 GLU L 126 4.612 ■5.25452.744 1.0026.87 ATOM 1150 C GLUL 126 10.169 ■6.36850.702 1.0014.63 ATOM 1151 O GLUL 126 10.842 -7.13251.421 1.0012.25 ATOM 1152 N THRL 127 10.179 -6.38849.326 1.0013.98 ATOM 1154 CA THRL 127 11.054 -7.31248.549 1.0013.13 ATOM 1155 CB THRL 127 10.542 -7.57047.086 1.0011.80 ATOM 1156 OG1 THRL 127 10.753 -6.41246.267 1.0010.21 ATOM 1158 CG2 THR L 127 9.068 -7.92647.066 1.0012.12 ATOM 1159 C THRL 127 12.460 -6.77548.453 1.0012.72 ATOM 1160 O THRL 127 13.266 -7.31647.715 1.0014.85 ATOM 1161 N ASNL 128 12.740 -5.70649.208 1.0013.49 ATOM 1163 CA ASNL 128 14.045 -5.05749.225 1.0013.82 ATOM 1164 CB ASNL 128 15.145 -6.04849.663 1.0019.63 ATOM 1165 CG ASNL 128 15.125 -6.27051.168 1.0023.79 ATOM 1166 OD1 ASN L 128 14.932 -7.391 51.638 1.0026.72 ATOM 1167 ND2 ASN L 128 15.314 -5.191 51.937 1.0025.77 ATOM 1170 C ASNL 128 14.399 -4.36947.910 1.0014.19 ATOM 1171 O ASNL 128 15.595 -4.13047.597 1.0013.24 ATOM 1172 N LYS L 129 13.354 -4.00047.173 1.0017.87 ATOM 1174 CA LYSL 129 13.501 -3.31845.900 1.0018.00 ATOM 1175 CB LYSL 129 13.046 -4.22944.745 1.0022.35 ATOM 1176 CG LYSL 129 13.716 -5.59844.695 1.0024.95 ATOM 1177 CD LYSL 129 15.206 -5.46444.537 1.0028.22 ATOM 1178 CE LYS L 129 15.848 -6.81544.346 1.0030.22 ATOM 1179 NZ LYS L 129 15.385 -7.42543.073 1.0034.30 ATOM 1183 C LYSL 129 12.666 -2.03745.876 1.0016.78 ATOM 1184 O LYSL 129 11.603 -1.95646.464 1.0015.40 ATOM 1185 N ALAL 130 13.165 - 1.04545.172 1.0016.40 ATOM 1187 CA ALAL 130 12.452 0.22445.009 1.0015.30 ATOM 1188 CB ALAL 130 12.995 1.27845.962 1.0010.48 ATOM 1189 C ALAL 130 12.575 0.72943.554 1.0013.30 ATOM 1190 O ALAL 130 13.692 0.97643.062 1.0013.88 ATOM 1191 N THRL 131 11.420 0.82542.873 1.0010.24 ATOM 1193 CA THRL 131 11.369 1.33841.527 1.008.65 ATOM 1194 CB THRL 131 10.689 0.363 40.539 1.009.65 ATOM 1195 OG1 THRL 131 11.282 -0.95340.646 1.0010.61 ATOM 1197 CG2 THR L 131 10.801 0.90239.092 1.008.13 ATOM 1198 C THRL 131 10.568 2.60341.513 1.004.73 ATOM 1199 O THRL 131 9.464 2.621 42.019 1.007.42 ATOM 1200 N LEUL 132 11.149 3.64740.968 1.005.79 ATOM 1202 CA LEU L 132 10.449 4.90440.787 1.008.20 ATOM 1203 CB LEU L 132 11.386 6.08641.075 1.007.00 ATOM 1204 CG LEUL 132 11.799 6.37842.544 1.009.11 ATOM 1205 CD1 LEU L 132 12.650 5.25843.104 1.006.00 ATOM 1206 CD2 LEU L 132 12.609 7.67842.596 1.008.20 ATOM 1207 C LEUL 132 9.976 4.97039.341 1.007.07 ATOM 1208 O LEUL 132 10.743 4.665 38.440 1.0010.93 ATOM 1209 N VALL 133 8.742 5.331 39.116 1.007.44 ATOM 1211 CA VALL 133 8.234 5.363 37.756 1.007.69 ATOM 1212 CB VALL 133 6.923 4.59837.629 1.005.71 ATOM 1213 CGI VALL 133 6.392 4.69036.194 1.005.28 ATOM 1214 CG2 VAL L 133 7.145 3.13838.022 1.0010.59 ATOM 1215 C VALL 133 7.970 6.77937.300 1.008.68 ATOM 1216 O VALL 133 7.296 7.541 37.962 1.008.54 ATOM 1217 N CYSL 134 8.448 7.11736.140 1.0012.17 ATOM 1219 CA CYSL 134 8.204 8.45735.595 1.009.67 ATOM 1220 CB CYS LI 34 9.558 9.12035.346 1.008.40 ATOM 1221 SG CYSL 134 9.463 10.81234.680 1.0010.83 ATOM 1222 C CYSL 134 7.451 8.30834.295 1.009.67 ATOM 1223 O CYSL 134 8.004 7.70633.371 1.0010.89 ATOM 1224 N THRL 135 6.195 8.745 34.238 1.006.29 ATOM 1226 CA THRL 135 5.469 8.655 33.028 1.005.35 ATOM 1227 CB THRL 135 4.012 8.195 33.246 1.005.71 ATOM 1228 OG1 THRL 135 3.231 9.21933.891 1.0011.96 ATOM 1230 CG2 THRL 135 3.984 6.92034.095 1.002.00 ATOM 1231 C THRL 135 5.547 9.98732.316 1.009.71 ATOM 1232 O THRL 135 5.826 11.01232.949 1.0011.41 ATOM 1233 N ILEL 136 5.426 9.98330.994 1 .009.98 ATOM 1235 CA ILEL 136 5.672 11.22830.205 1.0011.09 ATOM 1236 CB ILEL 136 7.150 11.26829.663 1.0012.20 ATOM 1237 CG2ILEL 136 7.420 12.60228.960 1.0010.90 ATOM 1238 CGI ILEL 136 8.166 11.011 30.783 1.0010.97 ATOM 1239 CD ILEL 136 9.578 10.69730.284 1.0011.49 ATOM 1240 C ILEL 136 4.723 11.21529.019 1.0010.64 ATOM 1241 O ILEL 136 4.806 10.32628.215 1.0011.08 ATOM 1242 N THRL 137 3.795 12.15428.927 1.0010.77 ATOM 1244 CA THRL 137 2.811 12.071 27.890 1.009.97 ATOM 1245 CB THRL 137 1.469 11.49928.449 1.0011.90 ATOM 1246 OG1 THRL 137 0.866 12.381 29.434 1.0011.66 ATOM 1248 CG2 THRL 137 1.724 10.16429.119 1.0012.72 ATOM 1249 C THRL 137 2.596 13.41727.221 1.0013.30 ATOM 1250 O THRL 137 3.181 14.431 27.670 1.0010.45 ATOM 1251 N ASPL 138 1.825 13.36326.116 1.0012.35 ATOM 1253 CA ASPL 138 1.342 14.541 25.354 1.0014.23 ATOM 1254 CB ASPL 138 0.325 15.323 26.180 1.0012.77 ATOM 1255 CG ASP L 138 -0.778 14.45226.713 1.0016.64 ATOM 1256 OD1 ASPL 138 -1.699 14.08425.926 1.0015.94 ATOM 1257 OD2 ASPL 138 -0.734 14.12727.929 1.0016.10 ATOM 1258 C ASPL 138 2.407 15.49924.869 1.0012.96 ATOM 1259 O ASPL 138 2.181 16.69824.879 1.0013.42 ATOM 1260 N PHEL 139 3.568 15.00424.439 1.0015.33 ATOM 1262 CA PHEL 139 4.590 15.91423.899 1.0012.61 ATOM 1263 CB PHEL 139 5.988 15.68524.488 1.0013.93 ATOM 1264 CG PHEL 139 6.452 14.24924.550 1.0017.51 ATOM 1265 CD1 PHEL 139 6.016 13.40725.571 1.0014.06 ATOM 1266 CD2 PHE L 139 7.344 13.74723.599 1.0018.44 ATOM 1267 CE1 PHEL 139 6.450 12.11425.644 1.0015.91 ATOM 1268 CE2 PHE L 139 7.781 12.44023.674 1.0017.97 ATOM 1269 CZ PHEL 139 7.331 11.61624.701 1.0019.08 ATOM 1270 C PHEL 139 4.671 15.82222.398 1.0014.58 ATOM 1271 O PHEL 139 4.364 14.77921.822 1.0013.97 ATOM 1272 N TYRL 140 5.003 16.96721.771 1.0014.53 ATOM 1274 C A TYR LI 40 5.221 17.04320.317 1.0015.96 ATOM 1275 CB TYRL 140 3.934 17.281 19.554 1.009.65 ATOM 1276 CG TYRL 140 4.165 17.225 18.059 1.0017.09 ATOM 1277 CD 1 TYRL 140 4.137 16.015 17.390 1.0018.26 ATOM 1278 CE1 TYRL 140 4.377 15.939 16.022 1.0018.78 ATOM 1279 CD2 TYRL 140 4.445 18.376 17.314 1.0017.33 ATOM 1280 CE2 TYRL 140 4.691 18.309 15.948 1.0017.98 ATOM 1281 CZ TYRL 140 4.650 17.083 15.318 1.0019.92 ATOM 1282 OH TYRL 140 4.861 17.000 13.970 1.0021.97 ATOM 1284 C TYRL 140 6.157 18.19520.052 1.0014.90 ATOM 1285 O TYR L 140 5.831 19.28620.462 1.0017.79 ATOM 1286 N PROL 141 7.343 18.014 19.373 1.0017.44 ATOM 1287 CD PROL 141 8.353 19.083 19.188 1.0018.49 ATOM 1288 CA PROL 141 7.859 16.742 18.793 1.0016.51 ATOM 1289 CB PROL 141 9.251 17.124 18.303 1.0016.41 ATOM 1290 CG PROL 141 9.134 18.569 18.033 1.0018.35 ATOM 1291 C PROL 141 7.977 15.581 19.781 1.0017.49 ATOM 1292 O PROL 141 8.147 15.78421.000 1.0016.25 ATOM 1293 N GLY L 142 7.918 14.379 19.234 1.0016.47 ATOM 1295 CA GLY L 142 8.090 13.19220.037 1.0017.96 ATOM 1296 C GLY L 142 9.530 12.88620.377 1.0017.11 ATOM 1297 O GLY L 142 9.975 11.75720.259 1.0020.37 ATOM 1298 N VAL L 143 10.292 13.85420.777 1.0017.91 ATOM 1300 CA VAL L 143 11.632 13.55221.210 1.0020.37 ATOM 1301 CB VAL L 143 12.695 13.97220.179 1.0025.23 ATOM 1302 CGI VAL L 143 12.502 15.421 19.764 1.0027.03 ATOM 1303 CG2 VAL L 143 14.083 13.76520.778 1.0023.81 ATOM 1304 C VALL 143 11.921 14.20522.557 1.0020.36 ATOM 1305 O VALL 143 11.713 15.41622.712 1.0018.56 ATOM 1306 N VALL 144 12.396 13.381 23.522 1.0018.00 ATOM 1308 CA VAL L 144 12.718 13.84524.891 1.0018.09 ATOM 1309 CB VAL L 144 1 1.582 13.532 25.913 1.00 15.31 ATOM 13 10 CG I VAL L 144 10.334 14.306 25.602 1.00 13.05 ATOM 131 1 CG2 VAL L 144 1 1.282 12.036 25.925 1.00 15.08 ATOM 1312 C VAL L 144 13.941 13.125 25.397 1.00 17.23 ATOM 1313 O VAL L 144 14.189 1 1.991 24.992 1.00 15.86 ATOM 1314 N THR L 145 14.744 13.798 26.217 1.00 16.98 ATOM 1316 CA THR L 145 15.795 13.107 26.924 1.00 17.36 ATOM 1317 CB THR L 145 17.233 13.739 26.775 1.00 22.21 ATOM 1318 OG 1 THR L 145 17.569 14.568 27.897 1.00 22.36 ATOM 1320 CG2 THR L 145 17.366 14.530 25.486 1.00 19.06 ATOM 1321 C THR L 145 15.378 13.091 28.392 1.00 19.55 ATOM 1322 O THR L 145 14.813 14.077 28.871 1.00 15.45 ATOM 1323 N VAL L 146 15.578 1 1.946 29.064 1.00 19.67 ATOM 1325 CA VAL L 146 15.185 1 1.787 30.463 1.00 17.75 ATOM 1326 CB VAL L 146 14.353 10.502 30.668 1.00 15.39 ATOM 1327 CGI VAL L 146 14.100 10.249 32.158 1.00 16.28 ATOM 1328 CG2 VAL L 146 13.051 10.633 29.945 1.00 12.45 ATOM 1329 C VAL L 146 16.429 11.709 31.327 1.00 18.57 ATOM 1330 O VAL L 146 17.354 10.986 31.018 1.00 20.82 ATOM 1331 N ASP L 147 16.442 12.464 32.396 1.00 16.64 ATOM 1333 CA ASP L 147 17.574 12.502 33.271 1.00 16.87 ATOM 1334 CB ASP L 147 18.284 13.862 33.104 1.00 22.38 ATOM 1335 CG ASP L 147 19.067 13.963 31.791 1.00 25.15 ATOM 1336 OD1 ASP L 147 20.153 13.344 31.712 1.00 25.53 ATOM 1337 OD2 ASP L 147 18.586 14.651 30.843 1.00 24.06 ATOM 1338 C ASP L 147 17.104 12.315 34.710 1.00 13.63 ATOM 1339 O ASP L 147 16.220 13.032 35.167 1.00 17.40 ATOM 1340 N TR L 148 17.676 1 1.358 35.399 1.00 12.32 ATOM 1342 CA TR L 148 17.287 1 1.061 36.792 1.00 8.34 ATOM 1343 CB TRP L 148 17.209 9.521 36.985 1.00 7.75 ATOM 1344 CG TRP L 148 16.010 8.879 36.377 1.00 9.41 ATOM 1345 CD2 TRP L 148 14.738 8.705 37.013 1.00 7.75 ATOM 1346 CE2 TRP L 148 13.895 8.079 36.088 1.00 9.98 ATOM 1347 CE3 TRP L 148 14.241 9.019 38.304 1.00 11.38 ATOM 1348 CD1 TRP L 148 15.889 8.362 35.116 1.00 5.30 ATOM 1349 NE1 TRP L 148 14.627 7.895 34.964 1.00 10.25 ATOM 1351 CZ2 TRP L 148 12.576 7.750 36.379 1.00 10.62 ATOM 1352 CZ3 TRP L 148 12.929 8.690 38.606 1.00 8.84 ATOM 1353 CH2 TRP L 148 12.106 8.061 37.642 1.00 9.81 ATOM 1354 C TRP L 148 18.328 11.611 37.741 1.00 10.55 ATOM 1355 O TRP L 148 19.526 11.572 37.440 1.00 11.66 ATOM 1356 N LYS L 149 17.904 12.113 38.891 1.00 10.12 ATOM 1358 CA LYS L 149 18.858 12.592 39.860 1.00 10.24 ATOM 1359 CB LYS L 149 18.985 14.121 39.739 1.00 9.85 ATOM 1360 CG LYS L 149 19.879 14.486 38.551 1.00 15.84 ATOM 1361 CD LYS L 149 19.786 15.934 38.146 1.00 20.45 ATOM 1362 CE LYS L 149 20.968 16.327 37.251 1.00 25.03 ATOM 1363 NZ LYS L 149 21.280 15.297 36.192 1.00 26.83 ATOM 1367 C LYS L 149 18.508 12.120 41.265 1.00 9.83 ATOM 1368 O LYS L 149 17.341 11.959 41.593 1.00 8.42 ATOM 1369 N VAL L 150 19.554 1 1.804 42.034 1.00 12.70 ATOM 1371 CA VAL L 150 19.402 11.385 43.438 1.00 13.13 ATOM 1372 CB VAL L 150 19.928 9.952 43.602 1.00 14.08 ATOM 1373 CGI VAL L I 50 20.396 9.706 45.001 1.00 9.65 ATOM 1374 CG2 VAL L 150 18.814 8.969 43.242 1.00 12.12 ATOM 1375 C VAL L 150 20.157 12.351 44.369 1.00 13.82 ATOM 1376 O VAL L 150 21.401 12.411 44.353 1.00 11.33 ATOM 1377 N ASP L 151 19.404 13.120 45.185 1.00 15.72 ATOM 1379 CA ASP L 151 20.015 14.144 46.055 1.00 13.64 ATOM 1380 CB ASP L 151 20.890 13.514 47.148 1.00 17.87 ATOM 1381 CG ASP L 151 20.098 12.911 48.300 1.00 18.72 ATOM 1382 OD1 ASP L 151 18.864 13.024 48.312 1.00 17.99 ATOM 1383 OD2 ASP L 151 20.716 12.318 49.203 1.00 20.12 ATOM 1384 C ASP L 151 20.831 15.094 45.207 1.00 12.12 ATOM 1385 O ASP L 151 21.950 15.539 45.548 1.00 14.72 ATOM 1386 N GLY L 152 20.291 15.366 44.072 1.00 13.53 ATOM 1388 CA GLY L 152 20.915 16.310 43.184 1.00 15.70 ATOM 1389 C GLY L 152 21.962 15.737 42.261 1.00 16.31 ATOM 1390 O GLY L 152 22.367 16.417 41.334 1.00 17.83 ATOM 1391 N THR L 153 22.402 14.503 42.469 1.00 18.56 ATOM 1393 CA THR L 153 23.470 13.953 41.618 1.00 18.43 ATOM 1394 CB THR L 153 24.506 13.187 42.455 1.00 19.60 ATOM 1395 OG 1 THR L 153 23.922 1 1.995 42.976 1.00 25.85 ATOM 1397 CG2 THR L 153 24.950 14.035 43.642 1.00 23.47 ATOM 1398 C THR L 153 22.898 13.092 40.464 1.00 18.68 ATOM 1399 O THR L 153 21.884 12.405 40.595 1.00 18.23 ATOM 1400 N PRO L 154 23.513 13.163 39.280 1.00 18.73 ATOM 1401 CD PRO L 154 24.731 13.947 38.974 1.00 19.95 ATOM 1402 CA PRO L 154 23.033 12.415 38.103 1.00 18.94 ATOM 1403 CB PRO L 154 23.849 13.028 36.966 1.00 18.59 ATOM 1404 CG PRO L 154 25.139 13.351 37.660 1.00 18.89 ATOM 1405 C PRO L 154 23.197 10.907 38.242 1.00 15.33 ATOM 1406 O PRO L 154 24.228 10.437 38.673 1.00 16.30 ATOM 1407 N VAL L 155 22.154 10.137 37.959 1.00 16.59 ATOM 1409 CA VAL L 155 22.332 8.695 38.029 1.00 19.40 ATOM 1410 CB VAL L 155 21.085 7.954 38.622 1.00 19.34 ATOM 141 1 CGI VAL L 155 20.152 8.939 39.284 1.00 18.37 ATOM 1412 CG2 VAL L 155 20.364 7.120 37.576 1.00 18.74 ATOM 1413 C VAL L 155 22.758 8.134 36.630 1.00 21.02 ATOM 1414 O VAL L 155 22.403 8.683 35.565 1.00 19.02 ATOM 1415 N THR L 156 23.590 7.103 36.649 1.00 22.42 ATOM 1417 CA THR L 156 24.084 6.518 35.421 1.00 23.32 ATOM 1418 CB THR L 156 25.572 6.776 35.297 1.00 23.16 ATOM 1419 OG1 THR L 156 26.227 6.308 36.480 1.0025.01 ATOM 1421 CG2 THR L 156 25.825 8.259 35.140 1.00 25.87 ATOM 1422 C THR L 156 23.868 5.030 35.422 1.00 25.17 ATOM 1423 O THR L 156 24.366 4.330 34.557 1.00 28.73 ATOM 1424 N GLN L 157 23.119 4.542 36.379 1.00 23.46 ATOM 1426 CA GLN L 157 22.91 1 3.142 36.481 1.00 23.50 ATOM 1427 CB GLN L 157 23.955 2.603 37.417 1.00 29.55 ATOM 1428 CG GLN L 157 24.082 1.104 37.377 1.00 37.55 ATOM 1429 CD GLN L 157 25.314 0.646 38.1 17 1.00 43.33 ATOM 1430 OE1 GLN L 157 25.777 1.317 39.059 1.00 43.65 ATOM 1431 NE2 GLN L 157 25.865 -0.493 37.685 1.00 45.54 ATOM 1434 C GLN L 157 21.518 2.866 37.002 1.00 19.92 ATOM 1435 O GLN L 157 21.011 3.632 37.773 1.00 18.81 ATOM 1436 N GLY L 158 20.889 1.810 36.538 1.00 18.99 ATOM 1438 CA GLY L 158 19.556 1.472 37.015 1.00 20.19 ATOM 1439 C GLY L 158 18.384 2.250 36.379 1.00 22.36 ATOM 1440 O GLY L 158 17.258 2.080 36.791 1.00 22.31 ATOM 1441 N MET L 159 18.624 3.105 35.392 1.00 24.81 ATOM 1443 CA MET L 159 17.529 3.817 34.750 1.00 22.88 ATOM 1444 CB MET L 159 17.796 5.327 34.682 1.00 23.15 ATOM 1445 CG MET L 159 18.824 5.803 33.688 1.00 26.34 ATOM 1446 SD MET L 159 20.513 5.742 34.305 1.00 34.44 ATOM 1447 CE MET L 159 21.012 4.154 33.640 1.00 31.53 ATOM 1448 C MET L 159 17.266 3.230 33.363 1.00 23.01 ATOM 1449 O MET L 159 18.173 2.800 32.688 1.00 24.49 ATOM 1450 N GLU L 160 16.020 3.191 32.958 1.00 19.49 ATOM 1452 CA GLU L 160 15.666 2.598 31.715 1.00 19.70 ATOM 1453 CB GLU L 160 15.367 1.118 31.969 1.00 21.50 ATOM 1454 CG GLU L 160 14.549 0.400 30.931 1.00 24.34 ATOM 1455 CD GLU L I 60 15.309 0.068 29.669 1.00 30.12 ATOM 1456 OE1 GLU L 160 16.548 -0.128 29.774 1.00 28.32 ATOM 1457 OE2 GLU L 160 14.660 0.005 28.567 1.00 30.69 ATOM 1458 C GLU L 160 14.484 3.332 31.146 11.00 19.64 ATOM 1459 O GLU L 160 13.438 3.390 31.774 1.00 18.31 ATOM 1460 N THR L 161 14.663 3.904 29.945 1.00 20.21 ATOM 1462 C A THR L 161 13.606 4.711 29.285 1.00 18.39 ATOM 1463 CB THR L 161 14.152 6.135 28.966 1.00 19.35 ATOM 1464 OG 1 THR L 161 14.634 6.725 30.180 1.00 15.43 ATOM 1466 CG2 THR L 161 13.085 7.028 28.361 1.00 13.84 ATOM 1467 C THR L 161 13.089 4.048 27.992 1.00 18.90 ATOM 1468 O THR L 161 13.855 3.391 27.282 1.00 18.53 ATOM 1469 N THR L 162 11.776 4.198 27.724 1.00 17.02 ATOM 1471 CA THR L 162 1 1.162 3.604 26.558 1.00 14.46 ATOM 1472 CB THR L 162 9.771 3.023 26.877 1.00 9.31 ATOM 1473 OG1 THR L 162 8.882 4.060 27.343 1.00 8.44 ATOM 1475 CG2 THR L I 62 9.890 1.934 27.939 1.00 8.50 ATOM 1476 C THR L 162 11.080 4.614 25.407 1.00 15.09 ATOM 1477 O THR L 162 1 1.086 5.838 25.608 1.00 14.93 ATOM 1478 N ALA L 163 11.055 4.106 24.190 1.00 12.96 ATOM 1480 CA ALA L 163 1 1.045 4.973 23.048 1.00 10.76 ATOM 1481 CB ALA L 163 11.436 4.206 21.765 1.00 15.08 ATOM 1482 C ALA L 163 9.71 1 5.563 22.914 1.00 8.59 ATOM 1483 O ALA L 163 8.730 4.859 22.998 1.00 1 1.96 ATOM 1484 N PRO L 164 9.639 6.885 22.727 1.00 1 1.37 ATOM 1485 CD PRO L 164 10.782 7.823 22.601 1.00 12.89 ATOM 1486 CA PRO L 164 8.372 7.584 22.589 1.00 1 1.21 ATOM 1487 CB PRO L 164 8.786 8.958 22.082 1.00 1 1.04 ATOM 1488 CG PRO L 164 10.083 9.139 22.783 1.00 1 1.07 ATOM 1489 C PRO L 164 7.506 6.838 21.620 1.00 12.84 ATOM 1490 O PRO L 164 8.003 6.161 20.722 1.00 17.44 ATOM 1491 N SER L 165 6.241 6.881 21.819 1.00 14.17 ATOM 1493 CA SER L 165 5.355 6.186 20.922 1.00 16.08 ATOM 1494 CB SER L 165 4.917 4.813 21.480 1.00 17.01 ATOM 1495 OG SER L 165 3.832 4.924 22.378 1.00 22.35 ATOM 1497 C SER L 165 4.220 7.095 20.722 1.00 15.78 ATOM 1498 O SER L 165 3.950 7.910 21.590 1.00 15.19 ATOM 1499 N LYS L 166 3.597 7.013 19.588 1.00 17.84 ATOM 1501 CA LYS L 166 2.582 7.984 19.248 1.00 19.88 ATOM 1502 CB LYS L 166 2.391 8.017 17.746 1.00 22.34 ATOM 1503 CG LYS L 166 2.325 9.408 17.139 1.00 21.36 ATOM 1504 CD LYS L 166 2.273 9.317 15.606 1.00 25.05 ATOM 1505 CE LYS L 166 2.601 10.656 14.965 0.01 22.27 ATOM 1506 NZ LYS L 166 2.538 10.600 13.475 0.01 22.15 ATOM 1510 C LYS L 166 1.282 7.698 19.914 1.00 21.48 ATOM 151 1 O LYS L 166 0.893 6.541 20.046 1.00 23.82 ATOM 1512 N GLN L 167 0.624 8.768 20.360 1.00 20.46 ATOM 1514 CA GLN L 167 -0.706 8.663 20.929 1.00 19.43 ATOM 1515 CB GLN L 167 -0.959 9.744 21.957 1.00 19.09 ATOM 1516 CG GLN L 167 0.073 9.829 23.070 1.00 13.91 ATOM 1517 CD GLN L 167 -0.173 10.995 24.012 1.00 12.43 ATOM 1518 OE1 GLN L 167 0.487 11.132 25.070 1.00 12.78 ATOM 1519 NE2 GLN L 167 -1.121 1 1.854 23.651 1.00 12.35 ATOM 1522 C GLN L 167 -1.691 8.864 19.808 1.00 20.58 ATOM 1523 O GLN L 167 -1.337 9.390 18.777 1.00 19.43 ATOM 1524 N SER L 168 -2.917 8.477 20.015 1.00 24.20 ATOM 1526 CA SER L 168 -3.932 8.620 18.983 1.00 28.22 ATOM 1527 CB SER L 168 -5.283 8.203 19.551 1.00 29.04 ATOM 1528 OG SER L 168 -5.480 8.808 20.824 1.00 34.62 ATOM 1530 C SER L 168 -4.005 10.061 18.471 1.00 30.48 ATOM 1531 O SER L 168 -4.452 10.321 17.331 1.00 34.63 ATOM 1532 N ASN L 169 -3.569 1 1.002 19.285 1.00 26.12 ATOM 1534 CA ASN L 169 -3.650 12.370 18.871 1.00 25.93 ATOM 1535 CB ASN L 169 -4.070 13.284 20.021 1.00 29.63 ATOM 1536 CG ASN L 169 -3.094 13.375 21.169 1.00 29.04 ATOM 1537 OD1 ASN L 169 -2.067 12.703 21.217 1.00 31.37 ATOM 1538 ND2 ASN L 169 -3.431 14.220 22.100 1.00 31.92 ATOM 1541 C ASN L 169 -2.362 12.794 18.299 1.00 25.86 ATOM 1542 O ASN L 169 -2.067 13.967 18.208 1.00 26.70 ATOM 1543 N ASN L 170 -1.592 1 1.830 17.924 1.00 23.96 ATOM 1545 CA ASN L 170 -0.328 12.075 17.287 1.00 23.68 ATOM 1546 CB ASN L 170 -0.560 12.714 15.923 1.00 25.27 ATOM 1547 CG ASN L 170 -1.128 1 1.651 14.991 1.00 28.14 ATOM 1548 OD1 ASN L 170 -0.430 10.692 14.635 1.00 30.35 ATOM 1549 ND2 ASN L 170 -2.403 1 1.769 14.642 1.00 29.66 ATOM 1552 C ASN L 170 0.675 12.826 18.1 13 1.00 22.90 ATOM 1553 O ASN L 170 1.705 13.241 17.610 1.00 25.60 ATOM 1554 N LYS L 171 0.396 13.038 19.371 1.00 21.22 ATOM 1556 CA LYS L 171 1.449 13.518 20.252 1.00 19.04 ATOM 1557 CB LYS L 171 0.892 14.301 21.438 1.00 17.22 ATOM 1558 CG LYS L 171 0.172 15.582 21.119 1.00 17.62 ATOM 1559 CD LYS L 171 -0.349 16.198 22.418 1.00 15.1 1 ATOM 1560 CE LYS L 171 -1.324 17.333 22.147 1.00 18.27 ATOM 1561 NZ LYS L 171 -1.550 18.177 23.353 1.00 14.34 ATOM 1565 C LYS L 171 2.139 12.244 20.757 1.00 17.36 ATOM 1566 O LYS L 171 1.728 1 1.151 20.397 1.00 17.98 ATOM 1567 N TYR L 172 3.136 12.351 21.587 1.00 14.79 ATOM 1569 CA TYR L 172 3.861 11.169 21.974 1.00 14.85 ATOM 1570 CB TYR L 172 5.296 1 1.312 21.506 1.00 15.82 ATOM 1571 CG TYR L 172 5.439 1 1.262 20.008 1.00 17.24 ATOM 1572 CD1 TYR L 172 5.187 12.380 19.192 1.00 15.15 ATOM 1573 CE1 TYR L 172 5.340 12.297 17.802 1.00 18.45 ATOM 1574 CD2 TYR L 172 5.834 10.084 19.402 1.00 17.80 ATOM 1575 CE2 TYR L 172 5.986 9.997 18.025 1.00 20.12 ATOM 1576 CZ TYRL 172 5.748 11.093 17.223 1.0018.23 ATOM 1577 OH TYRL 172 5.957 10.976 15.856 1.0013.35 ATOM 1579 C TYRL 172 3.841 10.900 23.464 1.0015.41 ATOM 1580 O TYRL 172 3.602 11.815 24.277 1.0014.17 ATOM 1581 N METL 173 4.112 9.631 23.818 1.0013.34 ATOM 1583 CA METL 173 4.194 9.23425.193 1.009.55 ATOM 1584 CB METL 173 2.931 8.486 25.587 1.0010.24 ATOM 1585 CG METL 173 2.794 7.099 24.973 1.0015.16 ATOM 1586 SD METL 173 1.458 6.141 25.711 1.0020.11 ATOM 1587 CE METL 173 0.057 6.915 24.983 1.0012.86 ATOM 1588 C METL 173 5.456 8.378 25.432 1.0010.38 ATOM 1589 O METL 173 6.004 7.76524.500 1.0010.40 ATOM 1590 N ALAL 174 5.930 8.34326.659 1.007.39 ATOM 1592 CA ALAL 174 7.129 7.58727.004 1.007.66 ATOM 1593 CB ALAL 174 8.390 8.33826.542 1.004.47 ATOM 1594 C ALAL 174 7.156 7.37428.522 1.008.50 ATOM 1595 O ALA L 174 6.346 7.96829.237 1.007.42 ATOM 1596 N SERL 175 8.060 6.52728.988 1.008.85 ATOM 1598 CA SERL 175 8.159 6.23030.403 1.009.69 ATOM 1599 CB SERL 175 7.271 5.021 30.757 1.008.09 ATOM 1600 OG SERL 175 7.689 3.81430.105 1.0012.41 ATOM 1602 C SERL 175 9.605 5.95430.779 1.0010.11 ATOM 1603 O SERL 175 10.411 5.52529.919 1.009.58 ATOM 1604 N SERL 176 9.977 6.23432.047 1.006.07 ATOM 1606 CA SERL 176 11.314 5.93232.491 1.003.46 ATOM 1607 CB SERL 176 12.184 7.16432.459 1.002.00 ATOM 1608 OG SERL 176 13.552 6.85832.672 1.002.00 ATOM 1610 C SERL 176 11.231 5.31633.891 1.005.39 ATOM 1611 O SERL 176 10.250 5.49034.564 1.007.78 ATOM 1612 N TYRL 177 12.225 4.52734.231 1.006.76 ATOM 1614 CA TYRL 177 12.241 3.75635.441 1.008.12 ATOM 1615 CB TYRL 177 12.040 2.273 35.114 1.006.07 ATOM 1616 CG TYRL 177 10.666 1.87634.571 1.006.17 ATOM 1617 CD1 TYRL 177 9.606 1.58835.440 1.006.94 ATOM 1618 CE1 TYRL 177 8.349 1.23734.936 1.008.14 ATOM 1619 CD2TYRL 177 10.422 1.793 33.200 1.006.52 ATOM 1620 CE2TYRL 177 9.168 1.44532.703 1.007.03 ATOM 1621 CZ TY L 177 8.134 1.17033.568 1.006.45 ATOM 1622 OH TYRL 177 6.868 0.863 33.077 1.006.11 ATOM 1624 C TYRL 177 13.563 3.87736.093 1.006.87 ATOM 1625 O TYRL 177 14.572 3.831 35.422 1.009.13 ATOM 1626 N LEUL 178 13.555 4.03037.390 1.006.48 ATOM 1628 CA LEUL 178 14.757 3.98938.155 1.006.11 ATOM 1629 CB LEUL 178 14.992 5.30438.851 1.006.46 ATOM 1630 CG LEU L 178 16.223 5.44239.717 1.007.03 ATOM 1631 CD1 LEU L 178 17.486 5.05038.981 1.0010.30 ATOM 1632 CD2LEUL 178 16.302 6.871 40.214 1.0013.82 ATOM 1633 C LEU L 178 14.621 2.881 39.154 1.00 8.35 ATOM 1634 O LEU L 178 13.684 2.853 39.899 1.0010.42 ATOM 1635 N THRL 179 15.562 1.96939.137 1.0011.56 ATOM 1637 CA THRL 179 15.533 0.803 39.975 1.0013.47 ATOM 1638 CB THRL 179 15.700 -0.45839.109 1.0015.12 ATOM 1639 OG1 THRL 179 14.533 -0.59438.335 1.0014.73 ATOM 1641 CG2 THRL 179 15.877 -1.731 39.945 1.0019.56 ATOM 1642 C THRL 179 16.622 0.89941.026 1.0016.41 ATOM 1643 O THRL 179 17.818 1.131 40.717 1.0015.41 ATOM 1644 N LEUL 180 16.179 0.75442.267 1.0016.98 ATOM 1646 CA LEUL 180 17.023 0.921 43.402 1.0017.38 ATOM 1647 CB LEUL 180 16.617 2.19844.178 1.0017.62 ATOM 1648 CG LEUL 180 16.662 3.55443.451 1.0018.66 ATOM 1649 CD1 LEUL 180 16.088 4.65244.341 1.0015.82 ATOM 1650 CD2 LEUL 180 18.095 3.911 43.065 1.0019.60 ATOM 1651 C LEUL 180 16.795 -0.231 44.317 1.0015.89 ATOM 1652 O LEU L 180 15.745 -0.86944.249 1.0020.00 ATOM 1653 N THRL 181 17.772 -0.50545.141 1.0016.39 ATOM 1655 CA THRL 181 17.568 -1.42946.251 1.0016.84 ATOM 1656 CB THRL 181 18.896 -1.82346.933 1.0015.01 ATOM 1657 OG1 THRL 181 19.588 -0.63247.377 1.0018.96 ATOM 1659 CG2 THRL 181 19.784 -2.61945.988 1.0016.62 ATOM 1660 C THRL 181 16.757 -0.65947.281 1.0014.44 ATOM 1661 O THRL 181 16.709 0.58047.225 1.0016.04 ATOM 1662 N ALAL 182 16.125 -1.33348.209 1.0015.12 ATOM 1664 CA ALA L 182 15.433 -0.599 49.267 1.00 13.02 ATOM 1665 CB ALA L 182 14.687 - 1.565 50.182 1.00 13.78 ATOM 1666 C ALA L 182 16.448 0.264 50.092 1.00 14.39 ATOM 1667 O ALA L 182 16.130 1.387 50.509 1.00 16.28 ATOM 1668 N ARG L 183 17.676 -0.237 50.310 1.00 14.52 ATOM 1670 CA ARG L 183 18.648 0.523 51.082 1.00 16.24 ATOM 1671 CB ARG L 183 19.921 0.291 51.326 1.00 19.45 ATOM 1672 CG ARG L 183 21.102 0.533 51.850 1.00 24.50 ATOM 1673 CD ARG L 183 22.136 -0.338 52.559 1.00 29.62 ATOM 1674 NE ARG L 183 23.493 0.292 52.608 1.00 35.27 ATOM 1676 CZ ARG L 183 24.446 -0.025 53.534 1.00 35.81 ATOM 1677 NH1 ARG L 183 25.675 0.517 53.472 .00 35.30 ATOM 1680 NH2 ARG L 183 24.152 -0.841 54.534 1.00 36.43 ATOM 1683 C ARG L 183 18.953 1.862 50.414 1.00 18.26 ATOM 1684 O ARG L 183 18.907 2.894 51.070 1.00 19.19 ATOM 1685 N ALA L 184 19.225 1.853 49.099 1.00 16.18 ATOM 1687 CA ALA L 184 19.485 3.073 48.394 1.00 10.91 ATOM 1688 CB ALA L 184 19.784 2.741 46.944 1.00 9.98 ATOM 1689 C ALA L 184 18.280 4.006 48.509 1.00 12.19 ATOM 1690 O ALA L 184 18.419 5.219 48.696 1.00 11.01 ATOM 1691 N TRP L 185 17.086 3.448 48.419 1.00 10.53 ATOM 1693 CA TRP L 185 15.876 4.254 48.476 1.00 1 1.80 ATOM 1694 CB TRP L 185 14.661 3.373 48.247 1.00 1 1.64 ATOM 1695 CG TRP L 185 13.419 4.037 48.677 1.00 9.64 ATOM 1696 CD2 TRP L 185 12.835 5.234 48.127 1.00 14.47 ATOM 1697 CE2 TRP L 185 1 1.640 5.477 48.834 1.00 14.89 ATOM 1698 CE3 TRP L 185 13.193 6.124 47.097 1.00 14.90 ATOM 1699 CD 1 TRP L 185 12.589 3.618 49.671 1.00 15.33 ATOM 1700 NE1 TRP L 185 11.530 4.481 49.749 1.00 15.12 ATOM 1702 CZ2 TRP L 185 10.804 6.560 48.553 1.00 15.58 ATOM 1703 CZ3 TRP L 185 12.368 7.185 46.812 1.00 12.52 ATOM 1704 CH2 TRP L 185 1 1.186 7.397 47.541 1.00 12.84 ATOM 1705 C TRP L 185 15.702 5.014 49.807 1.00 16.85 ATOM 1706 O TRP L 185 15.357 6.209 49.81 1 1.00 15.42 ATOM 1707 N GLU L 186 15.928 4.327 50.930 1.00 16.92 ATOM 1709 CA GLU L I 86 15.739 4.959 52.239 1.00 19.08 ATOM 1710 CB GLU L 186 15.777 3.908 53.352 1.00 21.77 ATOM 1711 CG GLU L 186 14.991 2.625 53.087 1.00 25.99 ATOM 1712 CD GLU L 186 15.309 1.533 54.128 0.50 26.59 ATOM 1713 OE1 GLU L 186 16.198 1.755 54.966 0.50 23.57 ATOM 1714 OE2 GLU L 186 14.674 0.457 54.095 0.50 23.36 ATOM 1715 C GLU L 186 16.831 5.972 52.544 1.00 20.25 ATOM 1716 O GLU L 186 16.675 6.841 53.407 1.00 20.91 ATOM 1717 N ARG L 187 17.952 5.850 51.875 1.00 18.94 ATOM 1719 CA ARG L 187 19.087 6.649 52.227 1.00 18.58 ATOM 1720 CB ARG L 187 20.330 5.943 51.777 1.00 20.96 ATOM 1721 CG ARG L 187 21.508 6.859 51.649 1.00 27.24 ATOM 1722 CD ARG L I 87 22.605 6.165 50.910 1.00 36.91 ATOM 1723 NE ARG L 187 23.278 5.168 51.730 1.00 39.36 ATOM 1725 CZ ARG L 187 24.599 5.050 51.731 1.00 42.54 ATOM 1726 NH1 ARG L 187 25.192 4.147 52.498 1.00 45.47 ATOM 1729 NH2 ARG L 187 25.330 5.841 50.948 1.00 46.06 ATOM 1732 C ARG L 187 19.054 8.072 51.679 1.00 18.28 ATOM 1733 O ARG L 187 19.749 8.944 52.205 1.0020.00 ATOM 1734 N HIS L 188 18.277 8.324 50.623 1.00 17.48 ATOM 1736 CA HIS L 188 18.250 9.671 50.014 1.00 16.15 ATOM 1737 CB HIS L 188 18.574 9.596 48.475 1.00 13.42 ATOM 1738 CG HIS L 188 19.894 8.957 48.210 1.00 14.37 ATOM 1739 CD2 HIS L 188 20.268 7.652 48.233 1.00 15.01 ATOM 1740 ND1 HIS L 188 21.083 9.664 48.217 1.00 14.95 ATOM 1742 CE1 HIS L 188 22.132 8.871 48.278 1.00 13.98 ATOM 1743 NE2 HIS L 188 21.646 7.644 48.301 1.00 15.86 ATOM 1745 C HIS L 188 16.898 10.317 50.245 1.00 16.60 ATOM 1746 O HIS L 188 15.897 9.616 50.404 1.00 18.56 ATOM 1747 N SER L 189 16.868 1 1.658 50.300 1.00 18.06 ATOM 1749 CA SER L 189 15.605 12.392 50.478 1.00 17.30 ATOM 1750 CB SER L 189 15.809 13.590 51.419 1.00 20.51 ATOM 1751 OG SER L 189 16.974 14.322 51.095 1.00 18.48 ATOM 1753 C SER L 189 15.061 12.894 49.153 1.00 18.08 ATOM 1754 O SER L 189 13.853 12.896 48.923 1.00 21.50 ATOM 1755 N SER L 190 15.967 13.277 48.262 1.00 17.95 ATOM 1757 CA SER L 190 15.582 13.885 46.984 1.00 17.18 ATOM 1758 CB SER L 190 16.455 15.103 46.722 1.00 14.84 ATOM 1759 OG SER L 190 15.885 15.899 45.705 1.00 24.95 ATOM 1761 C SER L 190 15.694 12.933 45.810 1.00 15.72 ATOM 1762 O SER L 190 16.732 12.295 45.605 1.00 16.39 ATOM 1763 N TYR L 191 14.628 12.850 45.058 1.00 15.74 ATOM 1765 CA TYR L 191 14.620 12.066 43.81 1 1.00 18.47 ATOM 1766 CB TYR L 191 13.883 10.737 44.028 1.00 20.26 ATOM 1767 CG TYR L 191 14.571 9.846 45.036 1.00 20.87 ATOM 1768 CD1 TYR L 191 15.609 9.014 44.623 1.00 23.39 ATOM 1769 CE1 TYR L 191 16.310 8.223 45.512 1.00 22.95 ATOM 1770 CD2 TYR L 191 14.227 9.864 46.412 1.00 24.18 ATOM 1771 CE2 TYR L 191 14.929 9.066 47.317 1.00 26.25 ATOM 1772 CZ TYR L 191 15.986 8.247 46.847 1.00 26.73 ATOM 1773 OH TYR L 191 16.779 7.529 47.725 1.00 30.08 ATOM 1775 C TYR L 191 13.935 12.894 42.700 1.00 17.55 ATOM 1776 0 TYR L 191 12.932 13.528 42.950 1.00 14.74 ATOM 1777 N SER L 192 14.465 12.884 41.473 1.00 16.33 ATOM 1779 CA SER L 192 13.898 13.735 40.454 1.00 15.90 ATOM 1780 CB SER L 192 14.701 15.039 40.443 1.00 18.03 ATOM 1781 OG SER L 192 14.126 15.961 39.550 1.00 23.10 ATOM 1783 C SER L 192 13.953 13.134 39.074 1.00 12.29 ATOM 1784 O SER L 192 14.990 12.656 38.672 1.00 14.68 ATOM 1785 N CYS L 193 12.855 13.191 38.355 1.00 11.59 ATOM 1787 CA CYS L 193 12.853 12.802 36.945 1.00 14.23 ATOM 1788 CB CYS L 193 1 1.629 1 1.969 36.620 1.00 15.78 ATOM 1789 SG CYS L 193 1 1.551 1 1.355 34.910 1.00 15.09 ATOM 1790 C CYS L 193 12.850 14.061 36.089 1.00 12.46 ATOM 1791 O CYS L 193 11.931 14.841 36.189 1.00 14.42 ATOM 1792 N GLN L 194 13.866 14.264 35.249 1.00 14.04 ATOM 1794 CA GLN L 194 13.938 15.495 34.451 1.00 14.30 ATOM 1795 CB GLN L 194 15.219 16.234 34.720 1.00 20.47 ATOM 1796 CG GLN L 194 15.534 16.382 36.170 1.00 26.89 ATOM 1797 CD GLN L 194 16.720 17.269 36.375 1.00 33.09 ATOM 1798 OE1 GLN L 194 16.900 17.827 37.468 1.00 36.67 ATOM 1799 NE2 GLN L 194 17.551 17.413 35.332 1.00 36.22 ATOM 1802 C GLN L 194 13.882 15.206 32.984 1.00 13.96 ATOM 1803 O GLN L 194 14.743 14.534 32.463 1.00 1 1.43 ATOM 1804 N VAL L 195 12.885 15.763 32.339 1.00 13.39 ATOM 1806 CA VAL L 195 12.624 15.500 30.942 1.00 15.15 ATOM 1807 CB VAL L 195 11.177 15.057 30.783 1.00 13.26 ATOM 1808 CGI VAL L 195 10.871 14.802 29.321 1.00 12.28 ATOM 1809 CG2 VAL L 195 10.912 13.829 31.659 1.00 8.74 ATOM 1810 C VAL L 195 12.836 16.749 30.071 1.00 16.35 ATOM 181 1 O VAL L 195 12.025 17.685 30.106 1.00 15.34 ATOM 1812 N THR L 196 13.925 16.755 29.301 1.00 16.92 ATOM 1814 CA THR L 196 14.195 17.864 28.382 1.00 15.93 ATOM 1815 CB THR L 196 15.708 18.008 28.168 1.00 18.12 ATOM 1816 OG1 THR L 196 16.349 18.212 29.431 1.00 22.55 ATOM 1818 CG2 THR L 196 16.022 19.183 27.264 1.00 21.24 ATOM 1819 C THR L 196 13.507 17.634 27.035 1.00 16.18 ATOM 1820 O THR L 196 13.738 16.581 26.401 1.00 14.99 ATOM 1821 N HIS L 197 12.654 18.626 26.614 1.00 14.43 ATOM 1823 CA HIS L 197 11.933 18.569 25.350 1.00 13.60 ATOM 1824 CB HIS L 197 10.444 18.344 25.574 1.00 12.56 ATOM 1825 CG HIS L 197 9.598 18.345 24.318 1.00 9.47 ATOM 1826 CD2 HIS L 197 9.559 17.496 23.283 1.00 8.75 ATOM 1827 ND1 HIS L 197 8.524 19.223 24.096 1.00 13.69 ATOM 1829 CE1 HIS L 197 7.874 18.920 22.993 1.00 10.65 ATOM 1830 NE2 HIS L I 97 8.493 17.880 22.507 1.00 13.24 ATOM 1832 C HIS L 197 12.079 19.889 24.609 1.00 19.15 ATOM 1833 O HIS L 197 11.361 20.879 24.932 1.00 21.46 ATOM 1834 N GLU L 198 12.904 19.875 23.571 1.00 19.88 ATOM 1836 CA GLU L 198 13.178 21.067 22.771 1.00 23.30 ATOM 1837 CB GLU L 198 1 1.897 21.658 22.160 1.00 25.45 ATOM 1838 CG GLU L 198 1 1.074 20.703 21.325 1.00 25.96 ATOM 1839 CD GLU L 198 11.437 20.714 19.863 1.0029.67 ATOM 1840 OE1 GLU L 198 12.403 20.003 19.479 1.00 31.64 ATOM 1841 OE2 GLU L 198 10.744 21.423 19.089 1.00 27.15 ATOM 1842 C GLU L 198 13.840 22.126 23.632 1.00 25.19 ATOM 1843 O GLU L 198 13.378 23.250 23.683 1.00 25.37 ATOM 1844 N GLY L 199 14.874 21.736 24.360 1.00 26.71 ATOM 1846 CA GLY L 199 15.647 22.699 25.107 1.00 28.67 ATOM 1847 C GLY L 199 15.025 23.177 26.398 1.00 30.20 ATOM 1848 O GLY L 199 15.631 24.007 27.078 1.00 31.36 ATOM 1849 N HIS L 200 13.821 22.685 26.738 1.00 29.31 ATOM 1851 CA HIS L 200 13.164 23.095 27.979 1.00 29.70 ATOM 1852 CB HIS L 200 1 1.788 23.748 27.741 1.00 34.13 ATOM 1853 CG HIS L 200 1 1.606 24.407 26.407 1.00 42.18 ATOM 1854 CD2 HIS L 200 12.497 24.946 25.537 1.00 44.52 ATOM 1855 ND1 HIS L 200 10.379 24.476 25.758 1.00 45.60 ATOM 1857 CE1 HIS L 200 10.501 25.004 24.543 1.00 46.26 ATOM 1858 NE2 HIS L 200 1 1.777 25.293 24.405 1.00 46.19 ATOM 1860 C HIS L 200 12.959 21.876 28.832 1.00 27.60 ATOM 1861 O HIS L 200 12.335 20.909 28.372 1.00 27.65 ATOM 1862 N THR L 201 13.458 21.932 30.064 1.00 27.03 ATOM 1864 CA THR L 201 13.375 20.797 30.979 1.00 25.96 ATOM 1865 CB THR L 201 14.629 20.751 31.867 1.00 22.54 ATOM 1866 OG 1 THR L 201 15.756 20.698 31.036 1.00 21.22 ATOM 1868 CG2 THR L 201 14.670 19.519 32.748 1.00 22.94 ATOM 1869 C THR L 201 12.109 20.851 31.845 1.00 26.78 ATOM 1870 O THR L 201 1 1.855 21.863 32.498 1.00 29.53 ATOM 1871 N VAL L 202 11.274 19.784 31.774 1.00 25.81 ATOM 1873 CA VAL L 202 10.113 19.636 32.674 1.00 22.79 ATOM 1874 CB VAL L 202 8.877 19.139 31.905 1.00 24.16 ATOM 1875 CGI VAL L 202 7.656 19.088 32.826 1.00 24.52 ATOM 1876 CG2 VAL L 202 8.621 20.060 30.717 1.00 24.14 ATOM 1877 C VAL L 202 10.492 18.614 33.772 1.00 21.74 ATOM 1878 O VAL L 202 10.951 17.538 33.472 1.00 19.01 ATOM 1879 N GLU L 203 10.315 1188..994499 3355..004444 1.00 20.40 ATOM 1881 CA GLU L 203 10.780 1188..007777 3366..007788 1.00 19.67 ATOM 1882 CB GLU L 203 12.018 1188..771133 3366..770088 1.00 22.14 ATOM 1883 CG GLU L 203 12.565 1177..993366 3377..887766 1.00 27.78 ATOM 1884 CD GLU L 203 13.321 1188..881155 3388..885566 0.50 30.15 ATOM 1885 OE1 GLU L 203 14.570 1188..990022 3388..773366 0.50 30.52 ATOM 1886 OE2 GLU L 203 12.662 1199..441188 3399..774488 0.50 30.93 ATOM 1887 C GLU L 203 9.736 1177..775577 3377..115555 1.00 18.69 ATOM 1888 O GLU L 203 8.856 1188..555566 3377..446655 1.00 19.41 ATOM 1889 N LYS L 204 9.810 1166..555522 3377..667766 1.00 16.36 ATOM 1891 CA LYS L 204 9.052 1166..119977 3388..884433 1.00 14.59 ATOM 1892 CB LYS L 204 7.969 15.235 3388..554422 1.00 15.55 ATOM 1893 CG LYS L 204 6.861 15.888 3377..776699 1.00 21.54 ATOM 1894 CD LYS L 204 6.406 17.133 3388..448811 1.00 21.69 ATOM 1895 CE LYS L 204 5.275 17.775 3377..772200 1.00 22.39 ATOM 1896 NZ LYS L 204 4.051 16.981 3377..887711 1.00 20.85 ATOM 1900 C LYS L 204 9.994 15.617 3399..885544 1.00 15.55 ATOM 1901 O LYS L 204 1 1.022 14.984 39.499 1.00 13.34 ATOM 1902 N SER L 205 9.673 15.854 41.125 1.00 17.28 ATOM 1904 CA SER L 205 10.536 15.433 42.199 1.00 16.96 ATOM 1905 CB SER L 205 1 1.321 16.626 42.766 1.00 18.69 ATOM 1906 OG SER L 205 12.422 16.990 41.919 1.00 25.46 ATOM 1908 C SER L 205 9.743 14.825 43.299 1.00 16.29 ATOM 1909 O SER L 205 8.584 15.118 43.445 1.00 12.40 ATOM 1910 N LEU L 206 10.409 13.959 44.032 1.00 17.28 ATOM 1912 CA LEU L 206 9.869 13.340 45.223 1.00 20.60 ATOM 1913 CB LEU L 206 9.926 1 1.804 45.106 1.00 18.66 ATOM 1914 CG LEU L 206 9.060 1 1.155 44.021 1.00 17.51 ATOM 1915 CD1 LEU L 206 9.529 9.738 43.756 1.00 19.23 ATOM 1916 CD2 LEU L 206 7.587 11.167 44.424 1.00 16.04 ATOM 1917 C LEU L 206 10.748 13.756 46.392 1.00 22.29 ATOM 1918 O LEU L 206 11.966 13.806 46.263 1.00 20.72 ATOM 1919 N SER L 207 10.137 14.1 14 47.488 1.00 26.92 ATOM 1921 CA SER L 207 10.898 14.334 48.709 1.00 33.08 ATOM 1922 CB SER L 207 10.508 15.631 49.412 1.00 32.95 ATOM 1923 OG SER L 207 1 1.284 15.814 50.584 1.00 35.61 ATOM 1925 C SER L 207 10.580 13.160 49.618 1.00 35.86 ATOM 1926 O SER L 207 9.401 12.806 49.798 1.00 38.31 ATOM 1927 N ARG L 208 11.603 12.538 50.143 1.00 36.32 ATOM 1929 CA ARG L 208 11.421 11.382 50.977 1.00 36.19 ATOM 1930 CB ARG L 208 12.244 10.21 1 50.365 1.00 33.25 ATOM 1931 CG ARG L 208 1 1.945 8.857 50.961 1.00 31.97 ATOM 1932 CD ARG L 208 13.215 8.1 17 51.322 1.00 32.82 ATOM 1933 NE ARG L 208 13.075 7.314 52.547 1.00 37.28 ATOM 1935 CZ ARG L 208 13.873 7.494 53.619 1.00 43.16 ATOM 1936 NH1 ARG L 208 13.749 6.729 54.723 1.0043.30 ATOM 1939 NH2 ARG L 208 4.794 8.46053.596 1.0045.46 ATOM 1942 C ARGL 208 11.855 11.78852.407 1.0037.35 ATOM 1943 OT1 ARGL 208 12.824 11.19652.969 1.0038.30 ATOM 1944 OT2 ARG L 208 11.246 12.77452.926 1.0037.56 ATOM 1945 CB ALA H -0.771 -4.993 -4.626 1.0035.02 ATOM 1946 C ALAH 1.178 -6.505 -4.919 1.0032.62 ATOM 1947 O ALAH 0.788 -7.588 -4.494 1.0032.59 ATOM 1950 N ALAH -0.545 -6.367 -6.682 1.0037.70 ATOM 1952 CA ALAH 0.204 -5.591 -5.634 1.0034.79 ATOM 1953 N VALH 2.429 -6.057 -4.804 1.0029.87 ATOM 1955 CA VALH 2 3.463 -6.831 -4.147 1.0028.68 ATOM 1956 CB VALH 2 4.806 -6.124 -4.242 1.0027.24 ATOM 1957 CGI VALH 2 5.892 -6.933 -3.552 1.0030.14 ATOM 1958 CG2 VAL H 2 5.136 -5.894 -5.708 1.0030.41 ATOM 1959 C VALH 2 3.135 -7.053 -2.694 1.0027.59 ATOM 1960 O VALH 2 2.532 -6.207 -2.034 1.0027.26 ATOM 1961 N GLNH 3 3.506 -8.200 -2.213 1.0025.47 ATOM 1963 CA GLNH 3.315 -8.504 -0.833 1.0024.24 ATOM 1964 CB GLNH 1.885 -9.027 -0.578 1.0026.56 ATOM 1965 CG GLNH 1.609 -9.380 0.905 1.0033.26 ATOM 1966 CD GLNH 0.370-10.261 1.157 1.0038.06 ATOM 1967 OE1 GLNH 0.094-11.216 0.415 1.0040.20 ATOM 1968 NE2 GLN H -0.369 -9.958 2.240 1.0038.60 ATOM 1971 C GLNH 3 4.334 -9.535 -0.380 1.0021.45 ATOM 1972 O GLNH 3 4.464-10.584 -0.995 1.0022.59 ATOM 1973 N LEUH 4 5.099 -9.192 0.641 1.0019.37 ATOM 1975 CA LEUH 4 5.998-10.150 1.300 1.0016.61 ATOM 1976 CB LEUH 4 7.394 -9.545 1.486 1.0013.50 ATOM 1977 CG LEUH 4 8.174 -9.232 0.194 1.008.19 ATOM 1978 CD 1 LEUH 4 9.510 -8.607 0.523 1.003.80 ATOM 1979 CD2 LEU H 4 8.394-10.506 -0.603 1.008.33 ATOM 1980 C LEUH 4 5.388-10.500 2.669 1.0015.88 ATOM 1981 O LEUH 4 4.960 -9.611 3.396 1.0015.82 ATOM 1982 N GLNH 5 5.324-11.767 3.017 1.0014.17 ATOM 1984 CA GLNH 5 4.655-12.155 4.267 1.0015.42 ATOM 1985 CB GLNH 5 3.283 -12.680 3.908 1.0016.35 ATOM 1986 CG GLNH 5 2.311-12.925 5.035 1.0022.48 ATOM 1987 CD GLNH 5 1.003-13.532 4.494 1.0029.57 ATOM 1988 OE1 GLN H 5 0.366-14.355 5.154 1.0035.66 ATOM 1989 NE2 GLN H 5 0.593-13.150 3.278 1.0031.58 ATOM 1992 C GLNH 5 5.470-13.205 5.002 1.0013.97 ATOM 1993 O GLNH 5 5.590-14.349 4.539 1.009.52 ATOM 1994 N GLUH 6 6.059-12.801 6.131 1.0013.08 ATOM 1996 CA GLUH 6 6.917-13.705 6.900 1.009.47 ATOM 1997 CB GLUH 6 7.848-12.956 7.823 1.00 9.95 ATOM 1998 CG GLUH 6 8.813-12.021 7.131 1.009.95 ATOM 1999 CD GLU H 6 8.237-10.662 6.799 1.005.17 ATOM 2000 OE1GLUH 6 9.055 -9.778 6.461 1.008.80 ATOM 2001 OE2 GLU H 6 6.983 -10.462 6.843 1.004.90 ATOM 2002 C GLUH 6 6.088 -14.632 7.736 1.0012.71 ATOM 2003 O GLUH 6 4.884-14.408 7.914 1.0013.94 ATOM 2004 N SERH 7 6.742-15.650 8.270 1.0013.48 ATOM 2006 CA SERH 7 6.095-16.642 9.106 1.0013.96 ATOM 2007 CB SERH 7 5.381 -17.653 8.220 1.0015.10 ATOM 2008 OG SERH 7 4.049-17.289 8.102 1.0023.26 ATOM 2010 C SERH 7 7.104-17.404 9.919 1.0012.29 ATOM 2011 O SERH 7 8.268-17.411 9.591 1.0013.84 ATOM 2012 N GLYH 8 6.622-18.093 10.961 1.0012.53 ATOM 2014 CA GLYH 8 7.462-19.033 11.663 1.0010.51 ATOM 2015 C GLYH 8 8.096-18.494 12.907 1.0012.14 ATOM 2016 O GLYH 8.763-19.233 13.581 1.0016.56 ATOM 2017 N GLYH 9 7.903-17.217 13.236 1.0010.59 ATOM 2019 CA GLY H 9 8.527-16.709 14.450 1.0014.05 ATOM 2020 C GLYH 9 7.920-17.295 15.753 1.0016.57 ATOM 2021 O GLYH 9 6.760-17.800 15.770 1.0017.72 ATOM 2022 N GLYH 10 8.667-17.200 16.843 1.0016.58 ATOM 2024 CA GLYH 10 8.149-17.666 18.129 1.0015.33 ATOM 2025 C GLYH 10 9.140-17.445 19.220 1.0012.28 ATOM 2026 O GLYH 10 10.150-16.758 19.006 1.0011.60 ATOM 2027 N LEUH 11 8.841 -18.04220.383 1.0013.95 ATOM 2029 CA LEUH 11 9.706-17.99521.590 1.0014.48 ATOM 2030 CB LEUH 11 8.814-18.09622.825 1.0014.29 ATOM 2031 CG LEUH 11 9.200-17.43324.155 1.0013.64 ATOM 2032 CD1 LEUH 11 8.420-18.16925.235 1.0013.85 ATOM 2033 CD2 LEU H 11 10.696-17.44524.479 1.004.07 ATOM 2034 C LEUH 11 10.586-19.22921.577 1.0014.46 ATOM 2035 O LEU H 11 10.096-20.29021.346 1.0015.77 ATOM 2036 N VALH 12 11.855-19.09621.901 1.0018.00 ATOM 2038 CA VALH 12 12.774-20.22021.888 1.0015.52 ATOM 2039 CB VALH 12 13.455-20.29720.469 1.0018.43 ATOM 2040 CGI VALH 12 14.970-20.23720.592 1.0013.84 ATOM 2041 CG2VALH 12 13.024-21.558 19.726 1.0016.77 ATOM 2042 C VALH 12 13.832-20.013 22.992 1.0015.38 ATOM 2043 O VALH 12 14.172-18.87523.352 1.0013.69 ATOM 2044 N GLNH 13 14.355-21.09023.558 1.0016.57 ATOM 2046 CA GLNH 13 15.372-20.93424.580 1.0015.98 ATOM 2047 CB GLNH 13 15.310-22.083 25.580 1.0019.24 ATOM 2048 CG GLNH 13 14.104-22.07426.537 1.0026.05 ATOM 2049 CD GLN H 13 14.446-22.62927.939 1.0028.25 ATOM 2050 OE1 GLNH 13 15.429-23.36728.124 1.0031.14 ATOM 2051 NE2 GLN H 13 13.645-22.25928.945 1.0033.04 ATOM 2054 C GLNH 13 16.729-20.92423.920 1.0014.00 ATOM 2055 O GLNH 13 16.870-21.34422.773 1.0015.42 ATOM 2056 N PROH 14 17.722-20.35624.540 1.0012.23 ATOM 2057 CD PROH 14 17.659-19.51225.729 1.0012.38 ATOM 2058 CA PROH 14 19.046-20.37223.965 1.0012.75 ATOM 2059 CB PROH 14 19.907-19.76925.057 1.0010.09 ATOM 2060 CG PROH 14 18.951 -18.75725.601 1.0013.06 ATOM 2061 C PROH 14 19.398-21.81723.621 1.0014.12 ATOM 2062 O PROH 14 19.080-22.73424.394 1.0016.21 ATOM 2063 N GLYH 15 20.019-22.01322.451 1.0010.07 ATOM 2065 CA GLYH 15 20.300-23.35521.945 1.007.80 ATOM 2066 C GLYH 15 19.221-23.78920.965 1.005.91 ATOM 2067 O GLYH 15 19.394-24.74420.198 1.006.43 ATOM 2068 N GLYH 16 18.137-23.04820.952 1.002.35 ATOM 2070 CA GLYH 16 17.015-23.40620.134 1.006.43 ATOM 2071 C GLYH 16 17.260-23.284 18.627 1.006.38 ATOM 2072 O GLYH 16 18.264-22.765 18.168 1.006.92 ATOM 2073 N SERH 17 16.262-23.672 17.887 1.0012.18 ATOM 2075 CA SERH 17 16.323-23.705 16.436 1.0011.41 ATOM 2076 CB SERH 17 16.774-25.123 16.079 1.0015.73 ATOM 2077 OG SERH 17 16.883-25.332 14.702 1.0022.31 ATOM 2079 C SERH 17 14.909-23.414 15.882 1.0012.78 ATOM 2080 O SERH 17 13.930-23.826 16.500 1.0016.32 ATOM 2081 N METH 18 14.783-22.667 14.769 1.00 8.79 ATOM 2083 CA METH 18 13.488-22.464 14.117 1.0010.28 ATOM 2084 CB METH 18 12.565-21.433 14.815 1.0013.63 ATOM 2085 CG METH 18 13.176-20.133 15.324 1.0016.88 ATOM 2086 SD METH 18 11.965-19.096 16.237 1.0027.06 ATOM 2087 CE METH 18 10.504-20.163 16.269 1.003.15 ATOM 2088 C METH 18 13.665-22.059 12.668 1.009.07 ATOM 2089 O METH 18 14.738-21.626 12.254 1.0010.49 ATOM 2090 N LYSH 19 12.612-22.185 11.907 1.0010.93 ATOM 2092 CA LYSH 19 12.675-21.815 10.531 1.0011.83 ATOM 2093 CB LYSH 19 12.600-23.056 9.625 1.0014.90 ATOM 2094 CG LYSH 19 12.550-22.773 8.094 1.0017.52 ATOM 2095 CD LYSH 19 13.043 -23.984 7.299 1.0020.23 ATOM 2096 CE LYSH 19 12.526 -24.038 5.865 1.0019.51 ATOM 2097 NZ LYSH 19 11.280-24.851 5.769 1.0022.58 ATOM 2101 C LYSH 19 11.572-20.843 10.207 1.0013.18 ATOM 2102 O LYSH 19 10.395-21.073 10.502 1.0012.84 ATOM 2103 N LEUH 20 11.995-19.731 9.610 1.0012.76 ATOM 2105 CA LEUH 20 11.094-18.710 9.160 1.009.79 ATOM 2106 CB LEUH 20 11.700-17.326 9.443 1.0011.85 ATOM 2107 CG LEUH 20 12.231-17.080 10.874 1.009.81 ATOM 2108 CD1 LEU H 20 12.775 -15.658 10.967 1.004.16 ATOM 2109 CD2 LEU H 20 11.135-17.333 11.908 1.004.65 ATOM 2110 C LEUH 20 10.855-18.856 7.673 1.009.78 ATOM 2111 O LEU H 20 11.714-19.325 6.922 1.008.56 ATOM 2112 N SERH 21 9.699-18.478 7.281 1.009.36 ATOM 2114 CA SERH 21 9.317-18.520 5.911 1.0013.01 ATOM 2115 CB SERH 21 8.269-19.586 5.707 1.0014.00 ATOM 2116 OG SERH 21 8.803 -20.857 5.993 1.0019.15 ATOM 2118 C SERH 21 8.764-17.193 5.469 1.0013.78 ATOM 2119 O SERH 21 8.160-16.471 6.260 1.0018.18 ATOM 2120 N CYS H 22 9.003-16.860 4.194 1.0016.70 ATOM 2122 CA CYS H 22 8.497-15.627 3.596 1.0013.01 ATOM 2123 CB CYS H 22 9.603-14.560 3.511 1.0011.58 ATOM 2124 SG CYS H 22 9.160-13.148 2.429 1.0013.80 ATOM 2125 C CYS H 22 7.993-15.912 2.193 1.0011.47 ATOM 2126 O CYS H 22 8.708-16.423 1.375 1.0013.22 ATOM 2127 N VAL H 23 6.768-15.578 1.938 1.0014.16 ATOM 2129 CA VAL H 23 6.184-15.802 0.639 1.0016.31 ATOM 2130 CB VALH 23 4.857-16.604 0.748 1.0017.85 ATOM 2131 CGI VALH 23 5.151 -17.911 1.457 1.0021.18 ATOM 2132 CG2VALH 23 3.799-15.822 1.518 1.0019.36 ATOM 2133 C VAL H 23 5.922-14.476 -0.023 1.0016.44 ATOM 2134 O VAL H 23 5.303-13.570 0.574 1.0012.06 ATOM 2135 N ALA H 24 6.400-14.380 -1.263 1.0019.48 ATOM 2137 CA ALA H 24 6.275-13.152 -2.068 1.0019.91 ATOM 2138 CB ALA H 24 7.604-12.884 -2.748 1.0018.96 ATOM 2139 C ALA H 24 5.182-13.278 -3.117 1.0021.31 ATOM 2140 O ALA H 24 4.953-14.374 -3.667 1.0024.23 ATOM 2141 N SERH 25 4.500-12.194 -3.409 1.0019.69 ATOM 2143 CA SERH 25 3.488-12.248 -4.429 1.0020.48 ATOM 2144 CB SERH 25 2.159-12.558 -3.789 1.0019.79 ATOM 2145 OG SERH 25 1.875-11.574 -2.821 1.0022.03 ATOM 2147 C SERH 25 3.390-10.925 -5.133 1.0020.75 ATOM 2148 O SERH 25 3.863 -9.909 -4.618 1.0020.32 ATOM 2149 N GLYH 26 2.746-10.932 -6.294 1.0022.48 ATOM 2151 CA GLY H 26 2.508 -9.680 -7.010 1.0024.12 ATOM 2152 C GLYH 26 3.713 -9.139 -7.796 1.0025.02 ATOM 2153 O GLY H 26 3.709 -7.955 -8.176 1.0022.99 ATOM 2154 N PHEH 27 4.728-10.018 -8.013 1.0024.04 ATOM 2156 CA PHE H 27 5.932 -9.707 -8.790 1.0022.13 ATOM 2157 CB PHE H 27 6.819 -8.649 -8.091 1.0023.23 ATOM 2158 CG PHEH 27 7.740 -9.173 -6.996 1.0020.65 ATOM 2159 CD1 PHE H 27 9.114 -9.356 -7.245 1.0019.81 ATOM 2160 CD2 PHE H 27 7.255 -9.425 -5.712 1.0019.64 ATOM 2161 CE1 PHEH 27 9.970 -9.775 -6.231 1.0018.67 ATOM 2162 CE2PHEH 27 8.117 -9.832 -4.703 1.0016.42 ATOM 2163 CZ PHEH 27 9.464-10.010 -4.959 1.0016.29 ATOM 2164 C PHEH 27 6.736-10.993 -9.003 1.0022.10 ATOM 2165 O PHEH 27 6.519-12.007 -8.308 1.0025.47 ATOM 2166 N THRH 28 7.689-10.939 -9.919 1.0017.46 ATOM 2168 CA THRH 28 8.483 -12.084 -10.233 1.0016.95 ATOM 2169 CB THRH 28 9.046-11.951 -11.625 1.0018.84 ATOM 2170 OG1 THRH 28 7.939-11.733-12.511 1.0019.87 ATOM 2172 CG2 THR H 28 9.793-13.214-12.017 1.0017.78 ATOM 2173 C THRH 28 9.594-12.306 -9.258 1.0016.32 ATOM 2174 O THRH 28 10.757-11.907 -9.499 1.0013.29 ATOM 2175 N PHEH 29 9.237-13.013 -8.176 1.0017.39 ATOM 2177 CA PHEH 29 10.185-13.319 -7.092 1.0012.65 ATOM 2178 CB PHE H 29 9.520 - 14.291 - 66..009999 .0014.38 ATOM 2179 CG PHEH 29 10.415 ■ -14.836 --55..001K0 1.0013.29 ATOM 2180 CD1 PHEH 29 10.570 -14.135 --33..88002 1.0017.17 ATOM 2181 CD2 PHE H 29 11.067 -16.058 --55..11559 1.0011.79 ATOM 2182 CE1PHEH 29 11.370 -14.654 --22..77665 1.0016.24 ATOM 2183 CE2 PHE H 29 11.864 -16.586 --44..11338 1.008.50 ATOM 2184 CZ PHE H 29 12.022 ■ ■15.887 --22..99446< 1.0014.16 ATOM 2185 C PHE H 29 11.482 - 13.895 -7.605 1.0011.31 ATOM 2186 O PHE H 29 12.555-13.533 -7.112 1.0011.15 ATOM 2187 N SERH 30 11.385-14.789 -8.631 1.0010.88 ATOM 2189 CA SERH 30 12.565 -15.474 -9.210 1.0010.24 ATOM 2190 CB SERH 30 12.113-16.379-10.389 1.0010.59 ATOM 2191 OG SERH 30 10.698-16.481-10.425 1.0020.09 ATOM 2193 C SERH 30 13.661 -14.529 -9.727 1.008.21 ATOM 2194 O SERH 30 14.839-14.924 -9.823 1.006.56 ATOM 2195 N ASNH 31 13.257-13.299-10.109 1.0010.86 ATOM 2197 CA ASNH 31 14.172 -12.323 -10.737 1.0010.45 ATOM 2198 CB ASNH 31 13.378-11.306-11.569 1.0013.88 ATOM 2199 CG ASNH 31 12.865-11.830-12.887 1.0017.90 ATOM 2200 OD1 ASNH 31 13.200-12.948-13.307 1.0017.77 ATOM 2201 ND2 ASN H 31 12.035-11.023-13.549 1.0020.48 ATOM 2204 C ASNH 31 15.033-11.520 -9.762 1.0011.11 ATOM 2205 O ASNH 31 15.987-10.848-10.199 1.0011.57 ATOM 2206 N TYRH 32 14.689-11.518 8.473 1.0010.42 ATOM 2208 CA TYRH 32 15.459-10.727 -7.512 1.007.72 ATOM 2209 CB TYRH 32 14.575 -9.640 ■6.921 1.0010.35 ATOM 2210 CG TYRH 32 13.995 -8.726 -7.958 1.0010.12 ATOM 2211 CD1 TYRH 32 12.717 -8.975 -8.451 1.0011.35 ATOM 2212 CE1 TYR H 32 12.192 -8.238 -9.513 1.0013.96 ATOM 2213 CD2TYRH 32 14.752 -7.703 -8.543 1.0010.05 ATOM 2214 CE2TYRH 32 14.232 -6.947 -9.624 1.0010.42 ATOM 2215 CZ TYRH 32 12.948 -7.222- 10.096 1.0013.65 ATOM 2216 OH TYRH 32 12.367 -6.454-11.099 1.0013.93 ATOM 2218 C TYRH 32 16.069-11.541 -6.376 1.008.75 ATOM 2219 O TYRH 32 15.564-12.610 -5.991 1.008.92 ATOM 2220 N TRPH 33 17.176-11.022 -5.853 1.007.78 ATOM 2222 CA TRPH 33 17.752-11.580 -4.698 1.006.34 ATOM 2223 CB TR H 33 19.106-10.961 -4.343 1.003.32 ATOM 2224 CG TRPH 33 20.136-10.905 -5.409 1.005.31 ATOM 2225 CD2 TRP H 33 21.486-10.435 -5.224 1.002.32 ATOM 2226 CE2 TRP H 33 22.122-10.485 -6.481 1.003.83 ATOM 2227 CE3 TRP H 33 22.204 -9.973 -4.111 1.005.74 ATOM 2228 CD1 TRPH 33 19.998-11.225 -6.740 1.002.00 ATOM 2229 NE1 TRP H 33 21.192-10.969 -7.368 1.003.99 ATOM 2231 CZ2 TRP H 33 23.432-10.079 -6.667 1.005.36 ATOM 2232 CZ3 TRP H 33 23.509 -9.569 -4.289 1.008.48 ATOM 2233 CH2 TRP H 33 24.108 -9.621 -5.564 1.007.99 ATOM 2234 C TRP H 33 16.815-11.212 - 3.551 1.008.26 ATOM 2235 O TRPH 33 16.037-10.228 ■ ■3.655 11.006.24 ATOM 2236 N METH 34 16.909-11.993 -2.473 1.007.22 ATOM 2238 CA METH 34 16.136-11.747 -1.260 1.008.81 ATOM 2239 CB METH 34 15.113-12.849 -1.097 1.007.01 ATOM 2240 CG METH 34 13.926-12.741 -2.048 1.0010.07 ATOM 2241 SD METH 34 12.892-11.274 -1.831 1.0017.49 ATOM 2242 CE METH 34 11.950-11.773 -0.390 1.0017.44 ATOM 2243 C METH 34 17.089-11.678 0.049 1.007.51 ATOM 2244 O METH 34 18.193-12.255 -0.093 1.0010.32 ATOM 2245 N ASNH 35 16.724-10.902 0.988 1.006.44 ATOM 2247 CA ASNH 35 17.570-10.757 2.181 1.004.54 ATOM 2248 CB ASN H 35 18.186 -9.341 2.317 1.005.78 ATOM 2249 CG ASNH 35 18.891 -8.806 1.076 1.003.57 ATOM 2250 OD1 ASNH 35 20.129 -8.691 1.016 1.002.44 ATOM 2251 ND2ASNH 35 18.102 -8.488 0.09Ϊ ; LOO 2.oo ATOM 2254 C ASNH 35 16.725 -10.942 3.442 1.004.23 ATOM 2255 O ASNH 35 15.486-10.826 3.400 1.002.00 ATOM 2256 N TRPH 36 17.398-11.276 4.537 1.004.82 ATOM 2258 CA TRPH 36 1 166..774466-- •1111..224400 5 5..883344 1 1..000066..5511 ATOM 2259 CB TRPH 36 1 166..886644--1 122..555588 6 6..660011 1 1..000044..1155 ATOM 2260 CG TRPH 36 1 155..887722-- ■1133..556688 6 6..110033 1 1..000066..1177 ATOM 2261 CD2 TRP H 36 1 144..448877- -1133..775566 6 6..550011 I 11..000055..5599 ATOM 2262 CE2 TRP H 36 1 133..995544- -1144..775555 5 5..666666 . 11..000077..6688 ATOM 2263 CE3 TRP H 36 1 133..662211 - -1133..118877 7 7..447744 ; 11..000033..5555 ATOM 2264 CD1TRPH 36 1 166..110000- -1144..443333 5 5..00887: J 11..000077..4433 ATOM 2265 NE1 TRP H 36 1 144..996633- -1155..112233 4 4..884432 1 11..00001111..3311 ATOM 2267 CZ2 TRP H 36 1 122..662255- -1155..221166 5 5..774455 i 11..000077..4422 ATOM 2268 CZ3 TRP H 36 1 122..227744- -1133..664499 7 7..555511 1 1..000022..6611 ATOM 2269 CH2 TRP H 36 1 111..779988- -1144..664422 , 66..669981 i 11..000055..7755 ATOM 2270 C TRPH 36 1 177..337755--110 0..110077 6.625 1.003.69 ATOM 2271 O TRPH 36 18.599 - 9.923 6.618 1.003.88 ATOM 2272 N VALH 37 16.546 -9.299 7.239 1.008.04 ATOM 2274 CA VALH 37 17.063 -8.196 8.049 1.004.88 ATOM 2275 CB VALH 37 16.851 -6.839 7.327 1.007.93 ATOM 2276 CGI VALH 37 17.141 -5.666 8.291 1.005.70 ATOM 2277 CG2VALH 37 17.755 i -6.752 6.084 1.004.88 ATOM 2278 C VALH 37 16.264 ■ -8.195 9.353 1.007.96 ATOM 2279 O VALH 37 15.041 -8.274 9.288 1.0010.89 ATOM 2280 N ARGH 38 1 166..992200 -8.092 10.498 1.004.79 ATOM 2282 CA ARG H 38 1166..117799 -8.134 11.783 1.006.19 ATOM 2283 CB ARGH 38 16.710 -9.288 12.699 1.002.00 ATOM 2284 CG ARGH 38 18.086 -9.070 13.392 1.005.85 ATOM 2285 CD ARGH 38 18.656 -10.358 14.059 1.007.03 ATOM 2286 NE ARGH 38 20.110-10.251 14.276 1.005.02 ATOM 2288 CZ ARGH 38 20.873-11.259 14.656 1.007.94 ATOM 2289 NH1 ARGH 38 22.155-11.056 14.911 1.008.02 ATOM 2292 NH2ARGH 38 20.371 -12.477 14.749 1.0010.78 ATOM 2295 C ARG H 38 16.218 -6.778 12.557 1.00 9.00 ATOM 2296 O ARG H 38 17.166 -5.974 12.456 1.00 7.20 ATOM 2297 N GLN H 39 15.192 -6.533 13.332 1.00 10.07 ATOM 2299 CA GLN H 39 15.154 -5.306 14.106 1.00 13.88 ATOM 2300 CB GLN H 39 13.927 -4.499 13.692 1.00 12.70 ATOM 2301 CG GLN H 39 13.871 -3.134 14.351 1.00 13.88 ATOM 2302 CD GLN H 39 12.577 -2.435 14.096 1.00 10.90 ATOM 2303 OE1 GLN H 39 11.578 -3.045 13.669 1.00 14.02 ATOM 2304 NE2 GLN H 39 12.570 -1.148 14.354 1.00 19.33 ATOM 2307 C GLN H 39 15.104 -5.631 15.638 11.00 17.21 ATOM 2308 O GLN H 39 14.152 -6.292 16.096 1.00 1 1.06 ATOM 2309 N SER H 40 16.149 -5.178 16.387 1.00 20.54 ATOM 2311 CA SER H 40 16.224 -5.375 17.840 1.00 25.32 ATOM 2312 CB SER H 40 17.438 -6.241 18.210 1.00 24.24 ATOM 2313 OG SER H 40 18.604 -5.445 18.333 1.00 26.93 ATOM 2315 C SER H 40 16.372 -4.024 18.534 1.00 26.35 ATOM 2316 O SER H 40 17.020 -3.133 17.987 1.00 27.60 ATOM 2317 N PRO H 41 15.807 -3.856 19.773 1.00 29.80 ATOM 2318 CD PRO H 41 15.073 -4.886 20.544 0.50 26.67 ATOM 2319 CA PRO H 41 15.898 -2.583 20.548 1.00 29.86 ATOM 2320 CB PRO H 41 15.219 -2.942 21.868 0.50 28.55 ATOM 2321 CG PRO H 41 15.354 -4.430 21.937 0.50 27.83 ATOM 2322 C PRO H 41 17.364 -2.097 20.737 1.00 33.07 ATOM 2323 O PRO H 41 17.739 -0.945 20.398 1.00 33.27 ATOM 2324 N ALA H 42 18.195 -3.003 21.209 1.00 34.06 ATOM 2326 CA ALA H 42 19.604 -2.687 21.463 1.00 37.51 ATOM 2327 CB ALA H 42 20.217 -3.817 22.304 1.00 37.30 ATOM 2328 C ALA H 42 20.448 -2.486 20.178 1.00 37.45 ATOM 2329 O ALA H 42 21.615 -2.062 20.265 1.00 38.47 ATOM 2330 N LYS H 43 19.875 -2.769 18.997 1.00 36.93 ATOM 2332 CA LYS H 43 20.689 -2.786 17.797 1.00 35.11 ATOM 2333 CB LYS H 43 21.042 -4.231 17.444 1.00 36.81 ATOM 2334 CG LYS H 43 21.939 -4.939 18.459 1.00 40.66 ATOM 2335 CD LYS H 43 22.518 -6.260 17.908 1.00 40.17 ATOM 2336 CE LYS H 43 21.551 -7.452 18.065 1.00 38.65 ATOM 2337 NZ LYS H 43 22.189 -8.748 17.670 1.00 34.06 ATOM 2341 C LYS H 43 20.078 -2.132 16.570 1.00 32.32 ATOM 2342 O LYS H 43 20.735 -2.094 15.541 1.00 32.74 ATOM 2343 N GLY H 44 18.867 -1.613 16.648 1.0028.07 ATOM 2345 CA GLY H 44 18.254 -1.086 15.428 1.00 26.41 ATOM 2346 C GLY H 44 18.243 -2.166 14.329 1.00 22.61 ATOM 2347 O GLY H 44 18.060 -3.372 14.656 1.00 21.36 ATOM 2348 N LEU H 45 18.487 -1.765 13.052 1.00 18.78 ATOM 2350 CA LEU H 45 18.452 -2.735 1 1.913 1.00 14.74 ATOM 2351 CB LEU H 45 18.017 -2.075 10.586 1.00 10.90 ATOM 2352 CG LEU H 45 16.517 -1.769 10.423 1.00 7.35 ATOM 2353 CD1 LEU H 45 16.263 -1.084 9.109 1.00 8.68 ATOM 2354 CD2 LEU H 45 15.661 -3.020 10.517 1.00 4.89 ATOM 2355 C LEU H 45 19.768 -3.456 1 1.710 1.00 13.85 ATOM 2356 O LEU H 45 20.871 -2.869 11.727 1.00 11.97 ATOM 2357 N GLU H 46 19.674 -4.761 1 1.517 1 .00 13.05 ATOM 2359 CA GLU H 46 20.873 -5.546 1 1.302 1.00 10.92 ATOM 2360 CB GLU H 46 21.260 -6.307 12.583 1.00 12.86 ATOM 2361 CG GLU H 46 22.733 -6.645 12.659 1.00 21.14 ATOM 2362 CD GLU H 46 23.067 -7.738 13.653 1.00 24.52 ATOM 2363 OE1 GLU H 46 22.400 -7.816 14.716 1.00 28.63 ATOM 2364 OE2 GLU H 46 24.015 -8.510 13.375 1.00 25.36 ATOM 2365 C GLU H 46 20.648 -6.540 10.150 1.00 9.90 ATOM 2366 O GLU H 46 19.726 -7.366 10.196 1 00 6.95 ATOM 2367 N TRP H 47 21.476 -6.428 9.123 1.00 7.54 ATOM 2369 CA TRP H 47 21.355 -7.311 7.982 1.00 7.90 ATOM 2370 CB TRP H 47 22.064 •6.701 6 6..774400 1.00 10.76 ATOM 2371 CG TRP H 47 22.169 -7.636 5 5..556655 1.00 5.45 ATOM 2372 CD2 TRP H 47 23.313 -8.463 5 5..2244.2 1.00 3.79 ATOM 2373 CE2 TRP H 47 23.012 -9.172 4 4..008833 ι 1.00 2.00 ATOM 2374 CE3 TRP H 47 24.572 -8.670 5 5..884455 1 1.00 3.96 ATOM 2375 CDI TRP H 47 21.210 -7.873 4 4..6600.2 » 1.00 4.22 ATOM 2376 NE1 TRP H 47 21.740 -8.799 3 3..7711c8 ! 1.00 5.25 ATOM 2378 CZ2 TRP H 47 23.913 •10.066 > 3 3..5500:2 2 1.00 2.56 ATOM 2379 CZ3 TRP H 47 25.451 -9.562 5.268 1.00 2.00 ATOM 2380 CH2 TRP H 47 25.1 16 -10.235 4.1 10 1.00 2.00 ATOM 238 1 C TRP H 47 21.937 - 8.650 8.367 1.00 2.55 ATOM 2382 O TRP H 47 22.989 -8.736 8.994 1.005.06 ATOM 2383 N VALH 48 21.234 -9.664 8.006 1.006.21 ATOM 2385 CA VAL H 48 21.553-10.994 8.436 1.007.94 ATOM 2386 CB VAL H 48 20.271 -11.532 9.165 1.007.86 ATOM 2387 CGI VALH 48 20.199-13.039 9.174 1.0010.48 ATOM 2388 CG2 VAL H 48 20.244-10.967 10.598 1.004.08 ATOM 2389 C VAL H 48 22.056-11.928 7.267 1.008.81 ATOM 2390 O VAL H 48 23.101 -12.618 7.404 1.005.89 ATOM 2391 N ALA H 49 21.351 - 11.914 6.127 1.006.18 ATOM 2393 CA ALA H 49 21.700 -12.813 5.035 1.004.66 ATOM 2394 CB ALA H 49 21.208 -14.203 5.342 1.002.00 ATOM 2395 C ALA H 49 21.057- 12.384 3.736 1.005.58 ATOM 2396 O ALA H 49 20.010- 11.747 3.745 1.007.99 ATOM 2397 N GLUH 50 21.711 - 12.787 2.620 1.007.04 ATOM 2399 CA GLUH 50 21.177 -12.560 1.275 1.008.25 ATOM 2400 CB GLUH 50 21.983 -11.507 0.518 1.009.60 ATOM 2401 CG GLUH 50 23.415 -11.900 0.271 1.007.83 ATOM 2402 CD GLUH 50 24.059 -11.043 -0.762 1.0013.01 ATOM 2403 OE1GLUH 50 24.860 -11.574 -1.536 1.009.53 ATOM 2404 OE2 GLU H 50 23.750 -9.830 ■ ■0.806 1.0013.19 ATOM 2405 C GLUH 50 21.287- 13.872 0.493 1.006.87 ATOM 2406 O GLUH 50 22.120- 14.702 0.832 1.005.50 ATOM 2407 N ILEH 51 20.423-14.049 -0.489 1.007.46 ATOM 2409 CA ILEH 51 20.525-15.201 -1.407 1.006.66 ATOM 2410 CB ILEH 51 19.542-16.318 -1.060 1.003.45 ATOM 2411 CG2ILEH 51 18.094-15.845 -1.218 1.009.97 ATOM 2412 CGI ILEH 51 19.820-17.559 -1.892 1.002.00 ATOM 2413 CD ILEH 51 18.849-18.673 -1.582 1.002.00 ATOM 2414 C ILEH 51 20.265-14.716 -2.841 1.005.59 ATOM 2415 O ILEH 51 19.323-13.991 -3.108 1.005.07 ATOM 2416 N ARGH 52 21.116-15.123 3.745 1.006.35 ATOM 2418 CA ARG H 52 21.016-14.633 -5.108 ■ 1.008.96 ATOM 2419 CB ARGH 52 22.421 -14.501 - -55..668844 1.005.72 ATOM 2420 CG ARGH 52 23.496-14.350 --44..559911 1.0012.48 ATOM 2421 CD ARGH 52 24.049-12.963 --44..442266 i 1.0013.83 ATOM 2422 NE ARGH 52 25.266-12.784 --55..116633 1.0012.25 ATOM 2424 CZ ARGH 52 26.261 -11.942 --44..883311 1.0012.96 ATOM 2425 NH1 ARG H 52 27.292-11.867 - -55..66007 7 1.0011.49 ATOM 2428 NH2ARGH 52 26.235-11.166 - -33..77665 5 1.0014.67 ATOM 2431 C ARGH 52 20.091 -15.492 -5 5..995599 1.0010.32 ATOM 2432 O ARGH 52 19.256-16.204 -5 5..441166 1.008.96 ATOM 2433 N LEUH 52A 20.247-15.437 -7.310 1.009.13 ATOM 2435 CA LEUH 52A 19.293-16.088 -8.198 1.009.35 ATOM 2436 CB LEUH 52A 19.218-15.294 -9.498 1.008.23 ATOM 2437 CG LEUH 52A 19.030-13.759 -9.350 1.004.43 ATOM 2438 CD1 LEUH 52A 19.087-13.099-10.721 1.009.87 ATOM 2439 CD2LEUH 52A 17.701 -13.450 -8.694 1.004.72 ATOM 2440 C LEUH 52A 19.642-17.538 -8.507 1.006.27 ATOM 2441 O LEUH 52A 20.735-18.003 -8.227 1.006.95 ATOM 2442 N LYSH 52B 18.707-18.240 -9.087 1.007.45 ATOM 2444 CA LYS H 52B 19.002-19.570 -9.564 1.0011.04 ATOM 2445 CB LYSH 52B 17.851 -20.082 -10.394 1.0013.40 ATOM 2446 CG LYSH 52B 18.080-21.505-10.842 1.0018.86 ATOM 2447 CD LYSH 52B 16.950-22.008-11.699 1.0021.41 ATOM 2448 CE LYS H 52B 17.363-23.307-12.408 1.0027.85 ATOM 2449 NZ LYSH 52B 16.327-23.728-13.385 1.0034.07 ATOM 2453 C LYSH 52B 20.277-19.571-10.407 1.0011.82 ATOM 2454 O LYSH 52B 21.175 -20.365 -10.168 1.0010.65 ATOM 2455 N SERH 52C 20.364-18.627-11.377 1.0010.14 ATOM 2457 CA SERH 52C 21.522-18.520-12.231 1.008.75 ATOM 2458 CB SERH 52C 21.276-17.513-13.352 1.0011.63 ATOM 2459 OG SERH 52C 20.872-16.286-12.838 1.0015.43 ATOM 2461 C SERH 52C 22.788-18.173-11.499 1.0011.06 ATOM 2462 O SERH 52C 23.851-18.241-12.089 1.009.23 ATOM 2463 N ASNH 53 22.694-17.799-10.197 1.0010.74 ATOM 2465 CA ASNH 53 23.902-17.544 -9.381 1.0011.27 ATOM 2466 CB ASNH 53 23.666-16.359 -8.458 1.0010.94 ATOM 2467 CG ASNH 53 23.335-15.136 -9.252 1.008.42 ATOM 2468 OD1 ASN H 53 22.251 -14.580 -9.150 1.0012.13 ATOM 2469 ND2ASNH 53 24.262-14.729-10.060 1.0010.17 ATOM 2472 C ASNH 53 24.216-18.790 -8.543 1.0010.33 ATOM 2473 O ASNH 53 25.160-18.808 -7.705 1.009.92 ATOM 2474 N ASN H 54 23.439-19.852 - 8.826 1.0010.20 ATOM 2476 CA ASNH 54 23.551 -21.163 -8.120 1.0010.20 ATOM 2477 CB ASN H 54 25.011 -21.606 -7.986 1.006.42 ATOM 2478 CG ASNH 54 25.726-21.683 -9.341 1.008.73 ATOM 2479 OD1 ASNH 54 25.244-22.312 -10.274 1.00 8.04 ATOM 2480 ND2 ASN H 54 26.858-21.024 -9.453 1.004.73 ATOM 2483 C ASNH 54 22.950-21.062 6.718 1.0011.89 ATOM 2484 O ASN H 54 23.297-21.860 -5.839 1.0012.26 ATOM 2485 N TYRH 55 22.046-20.090 -6.524 1.009.38 ATOM 2487 CA TYRH 55 21.484-19.806 -5.175 1.008.46 ATOM 2488 CB TYRH 55 20.698-21.003 -4.697 1.002.42 ATOM 2489 CG TYRH 55 19.528-21.295 -5.577 1.008.11 ATOM 2490 CD1 TYRH 55 19.514-22.432 -6.404 1.009.49 ATOM 2491 CE1 TYRH 55 18.407-22.701 -7.215 1.0012.87 ATOM 2492 CD2TYRH 55 18.427-20.461 -5.589 1.004.03 ATOM 2493 CE2TYRH 55 17.335-20.717 -6.381 1.0011.68 ATOM 2494 CZ TYRH 55 17.325-21.845 -7.207 1.0015.91 ATOM 2495 OH TYRH 55 16.234-22.076 -8.070 1.0020.99 ATOM 2497 C TYRH 55 22.609-19.434 -4.168 1.008.90 ATOM 2498 O TYRH 55 22.572-19.819 -2.968 1.0012.11 ATOM 2499 N ALA H 56 23.598-18.646 - •4.647 1.005.77 ATOM 2501 CA ALAH 56 24.707-18.204 -3.818 1.007.06 ATOM 2502 CB ALAH 56 25.729-17.514 -4.713 1.0011.84 ATOM 2503 C ALAH 56 24.215-17.266 - 2.660 1.007.10 ATOM 2504 O ALAH 56 23.166-16.609 - ■2.757 1.005.63 ATOM 2505 N THRH 57 24.970-17.229 - 1.566 1.007.85 ATOM 2507 CA THRH 57 24.513 -16.532 -0.373 1.006.03 ATOM 2508 CB THRH 57 23.978-17.545 0.679 1.004.33 ATOM 2509 OG1THRH 57 25.028-18.473 1.037 1.003.89 ATOM 2511 CG2THRH 57 22.769-18.316 0.163 1.003.87 ATOM 2512 C THRH 57 25.632-15.814 0.287 1.004.64 ATOM 2513 O THRH 57 26.812-16.091 0.021 1.007.15 ATOM 2514 N HISH 58 25.284-14.850 1.141 1.005.83 ATOM 2516 CA HISH 58 26.293-14.231 2.021 1.002.00 ATOM 2517 CB HISH 58 26.921 -12.931 1.497 1.004.50 ATOM 2518 CG HISH 58 27.572-13.120 0.170 1.004.63 ATOM 2519 CD2 HIS H 58 28.846-13.287 -0.205 1.007.27 ATOM 2520 ND1 HIS H 58 26.845-13.170 0.966 1.005.48 ATOM 2522 CE1 HIS H 58 27.570-13.365 -2.011 1.008.70 ATOM 2523 NE2HISH 58 28.800-13.435 -1.577 1.009.97 ATOM 2525 C HISH 58 25.601 -13.989 3.345 1.002.00 ATOM 2526 O HISH 58 24.381 -13.898 3.362 1.002.00 ATOM 2527 N TYRH 59 26.384-13.96 4.399 1.003.87 ATOM 2529 CA TYRH 59 25.864 13.906 5.777 1.006.14 ATOM 2530 CB TYRH 59 26.107 ■ 15.252 6.467 1.004.65 ATOM 2531 CG TYRH 59 25.271 16.347 5.898 1.002.93 ATOM 2532 CD1 TYRH 59 25.758 -17.152 4.887 1.007.71 ATOM 2533 CE1 TYRH 59 24.947 ■18.093 4.278 1.005.29 ATOM 2534 CD2TYRH 59 23.946 -16.515 6.295 1.004.20 ATOM 2535 CE2TYRH 59 23.149 -17.452 5.690 1.005.04 ATOM 2536 CZ TYRH 59 23.678 • ■18.232 4.673 1.005.90 ATOM 2537 OH TYRH 59 22.939 -19.182 4.123 1.009.69 ATOM 2539 C TYRH 59 26.594 - 12.892 6.574 1.006.82 ATOM 2540 O TYRH 59 27.761 - 12.666 6.335 1.007.72 ATOM 2541 N ALAH 60 25.931 - 12.299 7.550 1.008.95 ATOM 2543 CA ALA H 60 26.650 -11.388 8.438 1.006.79 ATOM 2544 CB ALAH 60 25.673 -10.579 9.283 1.008.53 ATOM 2545 C ALAH 60 27.503 - 12.219 9.336 1.0010.22 ATOM 2546 O ALAH 60 27.113 - 13.351 9.701 1.0011.26 ATOM 2547 N ALAH 61 28.650 - 11.676 9.743 1.0013.53 ATOM 2549 CA ALAH 61 29.577 -12.429 10.584 1.0014.91 ATOM 2550 CB ALAH 61 30.802 -11.573 10.930 1.0014.40 ATOM 2551 C ALAH 61 28.908 - 12.963 11.864 1.0017.24 ATOM 2552 O ALAH 61 29.237 - 14.047 12.320 1.0021.67 ATOM 2553 N SERH 62 27.932-12.239 12.405 1.0018.88 ATOM 2555 CA SERH 62 27.306-12.631 13.682 1.0020.00 ATOM 2556 CB SERH 62 26.509-11.457 14.200 1.0016.39 ATOM 2557 OG SERH 62 25.622-10.968 13.202 1.0018.61 ATOM 2559 C SERH 62 26.370-13.836 13.548 1.0021.12 ATOM 2560 O SERH 62 25.769-14.313 14.527 1.0019.05 ATOM 2561 N VALH 63 26.256-14.333 12.352 1.0018.08 ATOM 2563 CA VALH 63 25.250-15.311 12.067 1.0017.68 ATOM 2564 CB VALH 63 24.137-14.526 11.349 1.0018.65 ATOM 2565 CGI VALH 63 23.649-15.184 10.084 1.0016.99 ATOM 2566 CG2 VAL H 63 23.022-14.241 12.351 1.0012.88 ATOM 2567 C VAL H 63 25.837-16.469 11.264 1.0015.76 ATOM 2568 O VALH 63 25.280-17.560 11.194 1.0014.97 ATOM 2569 N LYS H 64 27.015-16.231 10.750 1.0018.14 ATOM 2571 CA LYS H 64 27.685-17.200 9.940 1.0020.28 ATOM 2572 CB LYSH 64 29.060-16.647 9.528 1.0022.43 ATOM 2573 CG LYSH 64 29.192-16.198 8.089 1.0020.56 ATOM 2574 CD LYSH 64 30.621 -15.730 7.833 1.0023.16 ATOM 2575 CE LYSH 64 30.812-15.238 6.413 0.0121.98 ATOM 2576 NZ LYSH 64 32.230-14.876 6.1340.0123.60 ATOM 2580 C LYSH 64 27.845-18.489 10.730 1.0018.78 ATOM 2581 O LYS H 64 28.206-18.455 11.907 1.0020.26 ATOM 2582 N GLYH 65 27.545-19.606 10.084 1.0017.68 ATOM 2584 CA GLY H 65 27.676-20.907 10.732 1.0016.07 ATOM 2585 C GLYH 65 26.461 -21.337 11.563 1.0014.30 ATOM 2586 O GLYH 65 26.362 -22.497 11.930 1.0014.97 ATOM 2587 N ARGH 66 25.536-20.421 11.858 1.0014.24 ATOM 2589 CA ARG H 66 24.324 -20.777 12.607 1.0010.28 ATOM 2590 CB ARGH 66 24.245 -19.925 13.845 1.007.89 ATOM 2591 CG ARGH 66 25.480-20.014 14.692 1.007.93 ATOM 2592 CD ARGH 66 25.663-18.698 15.446 1.0014.73 ATOM 2593 NE ARGH 66 24.524-18.447 16.242 1.0017.33 ATOM 2595 CZ ARGH 66 23.908-17.292 16.364 1.0017.22 ATOM 2596 NH1 ARGH 66 22.878-17.269 17.125 1.0018.44 ATOM 2599 NH2 ARG H 66 24.306-16.173 15.772 1.0015.39 ATOM 2602 C ARGH 66 23.078 -20.588 11.793 1.009.54 ATOM 2603 O ARGH 66 22.054-21.264 12.017 1.0011.68 ATOM 2604 N PHEH 67 23.098-19.625 10.874 1.009.08 ATOM 2606 CA PHEH 67 21.902-19.383 10.053 1.008.27 ATOM 2607 CB PHEH 67 21.489-17.883 10.070 1.0014.66 ATOM 2608 CG PHEH 67 20.947-17.325 11.376 1.0011.27 ATOM 2609 CD1 PHEH 67 20.920-18.097 12.555 1.0016.10 ATOM 2610 CD2PHEH 67 20.467-16.026 11.430 1.0012.21 ATOM 2611 CE1PHEH 67 20.433-17.564 13.746 1.0015.15 ATOM 2612 CE2PHEH 67 19.982-15.490 12.625 1.0016.05 ATOM 2613 CZ PHEH 67 19.968-16.259 13.774 1.0014.19 ATOM 2614 C PHEH 67 22.159-19.801 8.590 1.008.04 ATOM 2615 O PHEH 67 23.317-19.732 8.113 1.007.14 ATOM 2616 N THRH 68 21.076-20.208 7.898 1.005.55 ATOM 2618 CA THRH 68 21.144-20.637 6.500 1.006.31 ATOM 2619 CB THRH 68 21.151-22.179 6.428 1.0010.66 ATOM 2620 OG1 THRH 68 22.306 -22.665 7.128 1.008.86 ATOM 2622 CG2THRH 68 21.133-22.687 4.978 1.0010.19 ATOM 2623 C THRH 68 19.917-20.126 5.738 1.006.07 ATOM 2624 O THRH 68 18.767-20.466 6.071 1.009.45 ATOM 2625 N ILEH 69 20.141-19.270 4.750 : .004.87 ATOM 2627 CA ILEH 69 19.049-18.764 3.958 1.002.00 ATOM 2628 CB ILE H 69 19.310-17.256 3.524 1.006.99 ATOM 2629 CG2ILEH 69 20.538-17.123 2.645 1.007.03 ATOM 2630 CGI ILEH 69 18.097-16.669 2.798 1.002.00 ATOM 2631 CD ILEH 69 18.320-15.236 2.400 1.002.00 ATOM 2632 C ILEH 69 18.897-19.669 2.718 1.002.51 ATOM 2633 O ILEH 69 19.876-20.196 2.252 1.002.38 ATOM 2634 N SERH 70 17.680-19.873 2.253 1.002.57 ATOM 2636 CA SERH 70 17.469-20.669 1.076 1.006.14 ATOM 2637 CB SERH 70 17.380-22.175 1.448 1.009.52 ATOM 2638 OG SERH 70 16.268 -22.503 2.279 1.0010.39 ATOM 2640 C SERH 70 16.207-20.196 0.385 1.006.48 ATOM 2641 O SERH 70 15.460-19.431 0.959 1.007.77 ATOM 2642 N ARGH 71 15.973 -20.612 --0.858 1.007.82 ATOM 2644 CA ARGH 71 14.761 -20.181 -1.550 1.008.16 ATOM 2645 CB ARGH 71 15.000-18.914 -2.446 1.0010.92 ATOM 2646 CG ARGH 71 15.996-19.087 -3.614 1.008.76 ATOM 2647 CD ARGH 71 16.362-17.741 -4.294 1.004.61 ATOM 2648 NE ARGH 71 15.191-17.036 -4.849 1.007.09 ATOM 2650 CZ ARGH 71 15.228-15.735 -5.189 1.007.29 ATOM 2651 NH1 ARGH 71 14.156-15.124 -5.665 1.008.76 ATOM 2654 NH2ARGH 71 16.331 -15.058 -5.011 1.003.13 ATOM 2657 C ARGH 71 14.174-21.274 -2.383 1.009.04 ATOM 2658 O ARGH 71 14.844-22.180 -2.800 1.0011.10 ATOM 2659 N ASPH 72 12.918-21.163 -2.626 1.008.40 ATOM 2661 CA ASPH 72 12.289-22.068 -3.482 1.0013.86 ATOM 2662 CB ASPH 72 11.481-23.065 -2.666 1.0018.00 ATOM 2663 CG ASPH 72 10.864-24.131 -3.538 1.0022.29 ATOM 2664 OD1 ASPH 72 9.974-23.794 -4.325 1.0018.82 ATOM 2665 OD2ASPH 72 11.258-25.307 -3.419 1.0029.08 ATOM 2666 C ASPH 72 11.420-21.246 -4.406 1.0012.87 ATOM 2667 O ASPH 72 10.344-20.782 -4.047 11.0011.56 ATOM 2668 N ASPH 73 11.919-21.035 -5.587 11.0014.62 ATOM 2670 CA ASPH 73 11.199-20.236 -6.513 1.0012.47 ATOM 2671 CB ASPH 73 12.041 -19.914 -7.757 1.0014.32 ATOM 2672 CG ASPH 73 13.310-19.140 -7.394 1.0012.44 ATOM 2673 OD1 ASPH 73 13.277-18.373 -6.416 1.0013.98 ATOM 2674 OD2ASPH 73 14.341 -19.316 -8.059 1.0014.38 ATOM 2675 C ASPH 73 9.931 -20.899 -6.869 1.0015.39 ATOM 2676 O ASP H 73 8.975-20.159 -7.118 1.0017.19 ATOM 2677 N SERH 74 9.856-22.293 -6.824 1.0016.30 ATOM 2679 CA SERH 74 8.538-22.984 -7.156 1.0017.45 ATOM 2680 CB SERH 74 8.532-24.599 -7.050 1.0015.19 ATOM 2681 OG SERH 74 9.312-25.282 -6.029 1.002.00 ATOM 2683 C SERH 74 7.418-22.406 -6.305 1.0019.15 ATOM 2684 O SERH 74 6.276-22.222 -6.769 1.0016.07 ATOM 2685 N LYSH 75 7.797-22.022 -5.063 1.0020.59 ATOM 2687 CA LYSH 75 6.840-21.532 -4.071 1.0022.07 ATOM 2688 CB LYSH 75 7.137-22.236 -2.744 1.0022.73 ATOM 2689 CG LYSH 75 7.181 -23.747 -2.878 1.0030.86 ATOM 2690 CD LYSH 75 8.082 -24.387 -1.825 1.0034.56 ATOM 2691 CE LYSH 75 7.988 -25.896 -1.899 1.0036.81 ATOM 2692 NZ LYSH 75 6.598 -26.374 -1.597 1.0038.63 ATOM 2696 C LYSH 75 6.880-20.022 -3.865 1.0021.01 ATOM 2697 O LYS H 75 6.121 -19.481 -3.032 1.0018.31 ATOM 2698 N SERH 76 7.737-19.329 -4.598 1.0018.64 ATOM 2700 CA SERH 76 7.852-17.876 -4.417 1.0016.65 ATOM 2701 CB SERH 76 6.539-17.182 -4.738 1.0018.03 ATOM 2702 OG SERH 76 6.413-16.873 -6.103 1.0023.00 ATOM 2704 C SERH 76 8.154-17.593 -2.969 1.0015.08 ATOM 2705 O SERH 76 7.553-16.704 -2.411 1.0013.71 ATOM 2706 N SERH 77 9.089-18.353 -2.376 1.0012.40 ATOM 2708 CA SERH 77 9.333-18.222 -0.957 1.0011.32 ATOM 2709 CB SERH 77 8.666-19.385 -0.235 1.005.62 ATOM 2710 OG SERH 77 7.244-19.338 -0.349 1.0011.83 ATOM 2712 C SERH 77 10.801 -18.209 -0.653 1.0011.23 ATOM 2713 O SERH 77 11.586-18.826 -1.386 1.0010.52 ATOM 2714 N VALH 78 11.178-17.438 0.380 1.0011.36 ATOM 2716 CA VALH 78 12.557-17.449 0.908 1.009.82 ATOM 2717 CB VALH 78 13.284-16.055 0.778 1.002.05 ATOM 2718 CGI VALH 78 12.638-15.004 1.613 1.008.95 ATOM 2719 CG2 VAL H 78 14.736-16.175 1.126 1.006.47 ATOM 2720 C VALH 78 12.439-17.924 2.378 1.0010.77 ATOM 2721 O VALH 78 11.339- 17.884 2.943 1.0010.22 ATOM 2722 N TYRH 79 13.510 - 18.447 2.962 1.009.85 ATOM 2724 CA TYRH 79 13.401 -19.059 4.298 1.0011.42 ATOM 2725 CB TYRH 79 13.279 -20.578 4.167 1.008.95 ATOM 2726 CG TYRH 79 12.223 -21.091 3.208 1.009.83 ATOM 2727 CD 1 TYRH 79 10.890 -21.229 3.592 1.0013.08 ATOM 2728 CE1 TYR H 79 9.939 - 21.770 2.734 1.0013.31 ATOM 2729 CD2 TYR H 79 12.569 -21.502 1.923 1.0016.54 ATOM 2730 CE2TYRH 79 11.640 -22.047 1.060 1.0013.14 ATOM 2731 CZ TYRH 79 10.327 ■ -22.194 1.470 1.0015.87 ATOM 2732 OH TYRH 79 9.436 - -22.916 0.674 1.0021.63 ATOM 2734 C TYRH 79 14.652 - 18.789 5.081 1.008.87 ATOM 2735 O TYRH 79 15.679- 18.519 4.485 1.007.96 ATOM 2736 N LEUH 80 14.561 - 18.851 6.418 1.00 ' 7.68 ATOM 2738 CA LEUH 80 15.758 -18.726 7.275 1.00 6.13 ATOM 2739 CB LEUH 80 15.864 -17.318 7.922 1.00 3.75 ATOM 2740 CG LEUH 80 17.142 -17.034 8.797 1.00 5.89 ATOM 2741 CD1 LEU H 80 18.360 -16.802 7.906 1.00 7.66 ATOM 2742 CD2LEUH 80 16.934 -15.797 9.679 1.00 7.64 ATOM 2743 C LEUH 80 15.721 - 19.813 8.388 1.00 l 5.11 ATOM 2744 O LEUH 80 14.831- 19.837 9.212 1.0010.81 ATOM 2745 N GLNH 81 16.662-: 20.692 8.332 1.00 9.34 ATOM 2747 CA GLNH 81 16.836 -21.742 9.294 1.00 7.35 ATOM 2748 CB GLNH 81 17.458-22.950 8.601 1.0010.80 ATOM 2749 CG GLNH 81 17.874-24.108 9.496 1.007.67 ATOM 2750 CD GLNH 81 16.703-24.581 10.254 1.0012.30 ATOM 2751 OE1 GLNH 81 15.676-24.859 > 9.669 1.009.50 ATOM 2752 NE2GLNH 81 16.824-24.628 i 11.577 1.0014.89 ATOM 2755 C GLN H 81 17.772-21.246 10.299 1.007.63 ATOM 2756 O GL H 81 18.925-20.973 9.982 1.006.37 ATOM 2757 N METH 82 17.327-21.119 11.526 1.008.18 ATOM 2759 CA METH 82 18.231 -20.598 12.573 1.00 8.53 ATOM 2760 CB METH 82 17.574-19.407 13.273 1.0011.01 ATOM 2761 CG METH 82 17.021 -18.404 12.305 1.0012.29 ATOM 2762 SD METH 82 15.941 -17.230 13.061 1.0013.74 ATOM 2763 CE METH 82 14.457-18.124 12.844 1.0014.37 ATOM 2764 C METH 82 18.512-21.687 13.592 1.008.43 ATOM 2765 O METH 82 17.574-22.300 14.079 1.005.71 ATOM 2766 N ASNH 82A 19.784-21.874 13.889 1.008.95 ATOM 2768 CA ASNH 82A 20.240 -22.876 5 14.802 1.0011.83 ATOM 2769 CB ASNH 82A 21.152-23.871 I 14.094 \ 1.0014.31 ATOM 2770 CG ASNH 82A 20.435-24.642 13.030 1.0014.14 ATOM 2771 ODIASNH 82 A 19.202-24.697 13.022 1.0020.53 ATOM 2772 ND2 ASN H 82A 21.186-25.207 12.109 1.0019.33 ATOM 2775 C ASNH 82A 21.062-22.227 15.874 1.0014.07 ATOM 2776 O ASNH 82A 21.560-21.114 15.685 1.0012.90 ATOM 2777 N ASNH 82B 21.232-22.938 16.971 1.0013.76 ATOM 2779 CA ASN H 82B 22.088-22.462 18.073 1.0017.95 ATOM 2780 CB ASNH 82B 23.590-22.671 17.708 1.0020.73 ATOM 2781 CG ASNH 82B 23.871-24.023 16.988 1.0029.83 ATOM 2782 OD1 ASN H 82B 23.782-25.129 17.563 1.0032.41 ATOM 2783 ND2ASNH 82B 24.219-23.953 15.704 1.0033.10 ATOM 2786 C ASNH 82B 21.759-20.982 18.397 1.0015.91 ATOM 2787 O ASN H 82B 22.633-20.118 18.520 1.0012.49 ATOM 2788 N LEUH 82C 20.445-20.717 18.497 1.0014.84 ATOM 2790 CA LEUH 82C 19.944-19.382 18.758 1.0013.25 ATOM 2791 CB LEUH 82C 18.409-19.392 18.668 1.007.42 ATOM 2792 CG LEUH 82C 17.787-19.362 17.248 1.007.73 ATOM 2793 CD1 LEUH 82C 16.312-19.737 17.258 1.004.66 ATOM 2794 CD2LEUH 82C 17.920-17.971 16.669 1.002.94 ATOM 2795 C LEUH 82C 20.473-18.83820.110 1.0016.15 ATOM 2796 O LEUH 82C 20.775-19.59621.050 1.0017.22 ATOM 2797 N ARGH 83 20.641-17.52520.163 1.0016.23 ATOM 2799 CA ARGH 83 21.147-16.83821.318 1.0016.47 ATOM 2800 CB ARGH 83 22.474-16.221 21.000 1.0017.57 ATOM 2801 CG ARGH 83 23.503-17.15920.472 1.0023.38 ATOM 2802 CD ARGH 83 24.656-16.319 19.994 1.0029.30 ATOM 2803 NE ARG H 83 25.722-17.091 19.407 1.0030.53 ATOM 2805 CZ ARGH 83 26.685-16.527 18.696 1.0033.66 ATOM 2806 NH1 ARG H 83 27.658-17.280 18.201 1.0037.56 ATOM 2809 NH2ARGH 83 26.680-15.199 18.477 1.0035.33 ATOM 2812 C ARGH 83 20.185-15.71521.668 1.0017.82 ATOM 2813 O ARGH 83 19.461 -15.22620.798 1.0019.55 ATOM 2814 N ALAH 84 20.185-15.25522.900 1.0014.91 ATOM 2816 CA ALAH 84 19.254-14.17323.249 1.0016.48 ATOM 2817 CB ALAH 84 19.366-13.83724.723 1.0015.35 ATOM 2818 C ALAH 84 19.493-12.90922.384 1.0014.44 ATOM 2819 O ALAH 84 18.559-12.12922.125 1.0016.17 ATOM 2820 N ALAH 85 20.748-12.73521.929 1.0015.72 ATOM 2822 CA ALAH 85 21.104-11.59621.076 1.0015.91 ATOM 2823 CB ALAH 85 22.628-11.49920.932 1.0011.61 ATOM 2824 C ALAH 85 20.433-11.691 19.678 1.0015.42 ATOM 2825 O ALAH 85 20.438-10.694 18.921 1.0014.28 ATOM 2826 N ASPH 86 19.877-12.880 19.335 1.0012.78 ATOM 2828 CA ASPH 86 19.172-13.064 18.045 1.0010.42 ATOM 2829 CB ASPH 86 19.198-14.509 17.571 1.004.96 ATOM 2830 CG ASPH 86 20.590-15.028 17.411 1.0010.01 ATOM 2831 OD1 ASP H 86 20.820-16.182 17.780 1.0012.26 ATOM 2832 OD2ASPH 86 21.453-14.293 16.934 1.008.11 ATOM 2833 C ASPH 86 17.739-12.640 18.142 1.008.78 ATOM 2834 O ASPH 86 16.999-12.683 17.168 1.0012.52 ATOM 2835 N THRH 87 17.331 -12.241 19.311 1.008.30 ATOM 2837 CA THRH 87 15.957-11.796 19.500 1.008.21 ATOM 2838 CB THRH 87 15.706-11.463 21.037 1.007.33 ATOM 2839 OG1 THRH 87 15.888-12.65521.802 1.006.98 ATOM 2841 CG2THRH 87 14.304-10.96021.286 1.005.67 ATOM 2842 C THRH 87 15.687-10.575 18.603 1.009.42 ATOM 2843 O THRH 87 16.557 -9.719 18.446 1.0013.23 ATOM 2844 N GLYH 88 14.533-10.533 17.980 1.007.71 ATOM 2846 CA GLYH 88 14.193 -9.374 17.192 1.009.10 ATOM 2847 C GLYH 88 13.113 -9.691 16.243 1.009.84 ATOM 2848 O GLYH 88 12.644-10.824 16.234 1.007.86 ATOM 2849 N ILEH 89 12.655 -8.677 15.485 1.009.11 ATOM 2851 CA ILEH 89 11.644 -8.885 14.456 1.0010.31 ATOM 2852 CB ILEH 89 10.781 ■7.639 14.300 1.0011.02 ATOM 2853 CG2 ILE H 89 9.724 ■7.873 13.233 1.0010.51 ATOM 2854 CGI ILEH 89 10.139 -7.330 15.659 1.0011.28 ATOM 2855 CD ILEH 89 9.284 6.073 15.682 1.0017.09 ATOM 2856 C ILEH 89 12.385 -9.170 13.146 1.0011.03 ATOM 2857 O ILEH 89 13.322 -8.442 12.807 1.0011.03 ATOM 2858 N TYRH 90 12.039- 10.285 12.488 1.0011.24 ATOM 2860 CA TYRH 90 12.742 -10.687 11.281 1.009.58 ATOM 2861 CB TYRH 90 13.136 -12.141 11.35 1.004.73 ATOM 2862 CG TYRH 90 14.348 -12.417 12.227 1.004.17 ATOM 2863 CD1 TYRH 90 14.286 -12.296 13.633 1.002.00 ATOM 2864 CE1 TYRH 90 15.385 -12.594 14.426 1.002.00 ATOM 2865 CD2TYRH 90 15.539 -12.851 11.669 1.002.40 ATOM 2866 CE2TYRH 90 16.635 -13.147 12.465 1.002.17 ATOM 2867 CZ TYRH 90 16.544--13.008 13.855 1.002.00 ATOM 2868 OH TYRH 90 17.665 -13.223 14.644 1.002.45 ATOM 2870 C TYRH 90 11.923-10.416 10.062 1.009.22 ATOM 2871 O TYRH 90 10.740- 10.839 9.964 1.0012.19 ATOM 2872 N TYRH 91 12.547 -9.679 9.131 1.008.92 ATOM 2874 CA TYRH 91 11.874 -9.271 7.878 1.006.94 ATOM 2875 CB TYRH 91 11.967 -7.735 7.705 1.008.51 ATOM 2876 CG TYRH 91 11.498 -6.910 8.859 1.007.13 ATOM 2877 CD1 TYRH 91 10.185 -6.466 8.912 1.006.14 ATOM 2878 CE1TYRH 91 9.718 -5.698 9.980 1.007.31 ATOM 2879 CD2TYRH 91 12.358 -6.571 9.896 1.004.90 ATOM 2880 CE2TYRH 91 11.889 -5.806 10.981 1.008.04 ATOM 2881 CZ TYRH 91 10.566 -5.379 11.012 1.005.99 ATOM 2882 OH TYRH 91 10.080 -4.630 12.114 1.0013.80 ATOM 2884 C TYRH 91 12.588 - 9.873 6.643 1.005.68 ATOM 2885 O TYRH 91 13.811 • •9.911 6.613 1.0010.68 ATOM 2886 N CYS H 92 11.858-10.371 5.667 1.005.92 ATOM 2888 CA CYSH 92 12.504-10.601 4.362 1.009.62 ATOM 2889 CB CYSH 92 11.878-11.758 3.625 1.008.20 ATOM 2890 SG CYSH 92 10.133-11.548 3.675 1.0016.35 ATOM 2891 C CYS H 92 12.266 -9.322 3.536 1.007.60 ATOM 2892 O CYSH 92 11.183 -8.723 3.585 1.008.00 ATOM 2893 N THRH 93 13.239 -8.913 2.792 1.008.87 ATOM 2895 CA THRH 93 13.129 -7.658 2.043 1.009.75 ATOM 2896 CB THRH 93 13.594 -6.438 2.916 1.007.13 ATOM 2897 OG1 THRH 93 13.882 -5.296 2.069 1.008.11 ATOM 2899 CG2 THR H 93 14.829 -6.781 3.713 1.006.38 ATOM 2900 C THRH 93 13.999 -7.733 0.801 1.009.01 ATOM 2901 O THRH 93 15.047 -8.368 0.860 1.008.92 ATOM 2902 N GLYH 94 13.576 -7.103 -0.311 1.008.19 ATOM 2904 CA GLYH 94 14.410 -7.128 -1.482 1.009.97 ATOM 2905 C GLYH 94 13.978 -6.140 -2.538 1.0011.34 ATOM 2906 O GLYH 94 13.075 -5.369 -2.322 1.008.22 ATOM 2907 N VAL H 95 14.692 -6.178 -3.672 1.0013.48 ATOM 2909 CA VALH 95 14.458 -5.332 -4.849 1.0010.59 ATOM 2910 CB VALH 95 13.011 -5.255 -5.260 1.009.92 ATOM 2911 CGI VALH 95 12.943 -4.461 -6.543 1.0012.93 ATOM 2912 CG2 VAL H 95 12.405 -6.638 -5.477 1.0012.57 ATOM 2913 C VALH 95 14.999 -3.909 -4.732 1.0012.91 ATOM 2914 O VALH 95 14.430 -3.040 -4.058 1.0016.60 ATOM 2915 N GLYH 96 16.114 -3.704 -5.374 1.0014.72 ATOM 2917 CA GLYH 96 16.735 -2.365 -5.516 1.0017.50 ATOM 2918 C GLY H 96 16.907 -1.394 -4.292 1.0015.41 ATOM 2919 O GLY H 96 16.437 -0.244 -4.355 1.0016.20 ATOM 2920 N GLNH 97 17.519 -1.780 -3.174 1.0013.46 ATOM 2922 CA GLNH 97 17.941 -3.130 -2.865 1.0013.51 ATOM 2923 CB GLNH 97 19.422 -3.160 -2.463 1.0011.95 ATOM 2924 CG GLNH 97 20.404 -3.131 -3.631 1.0015.05 ATOM 2925 CD GLNH 97 20.374 -1.861 -4.476 1.0016.43 ATOM 2926 OE1 GLN H 97 20.856 -0.810 -4.064 1.0017.08 ATOM 2927 NE2 GLN H 97 19.826 1.965 -5.675 1.0018.31 ATOM 2930 C GLN H 97 17.071 ■ -3.627 ■ -1.687 1.0010.81 ATOM 2931 O GLN H 97 17.133 -4.792 -1.295 1.00 8.86 ATOM 2932 N PHEH 98 16.232 - •2.733 - ■1.171 1.008.60 ATOM 2934 CA PHEH 98 15.370 -3.030 -0.030 1.00 8.66 ATOM 2935 CB PHEH 98 16.036 -2.546 1.263 1.0011.54 ATOM 2936 CG PHEH 98 17.347 -3.195 1.612 1.009.16 ATOM 2937 CD1 PHEH 98 17.375 -4.422 2.262 1.006.51 ATOM 2938 CD2 PHE H 98 18.559 -2.584 1.291 1.009.14 ATOM 2939 CE1 PHEH 98 18.590 -5.041 2.585 1.009.69 ATOM 2940 CE2 PHE H 98 19.764 -3.190 1.617 1.008.35 ATOM 2941 CZ PHEH 98 19.785 -4.432 2.266 1.006.22 ATOM 2942 C PHEH 98 14.061 - ■2.278 - 0.191 1.0010.16 ATOM 2943 O PHEH 98 13.591 - ■ 1.636 0.736 1.0011.80 ATOM 2944 N ALAH 101 13.475 -2.339 -1.365 1.009.29 ATOM 2946 CA ALAH 101 12.250 -1.634 -1.622 1.008.04 ATOM 2947 CB ALAH 101 11.991 -1.549 -3.111 1.006.69 ATOM 2948 C ALAH 101 11.074 -2.298 -0.962 1.0011.49 ATOM 2949 O ALAH 101 10.142 -1.595 -0.529 1.0011.63 ATOM 2950 N TYRH 102 11.101 -3.645 -0.923 1.008.89 ATOM 2952 CA TYRH 102 9.998 -4.417 -0.365 1.0013.48 ATOM 2953 CB TYRH 102 9.566 -5.515 -1.327 1.0017.64 ATOM 2954 CG TYRH 102 9.270 -5.035 -2.711 1.0019.49 ATOM 2955 CD1 TYRH 102 8.742 -3.765 -2.921 1.0019.65 ATOM 2956 CE1 TYRH 102 8.440 -3.311 -4.190 1.0019.68 ATOM 2957 CD2 TYRH 102 9.498 -5.856 -3.816 1.0021.83 ATOM 2958 CE2 TYRH 102 9.193 -5.399 -5.093 1.0024.66 ATOM 2959 CZ TYRH 102 8.658 -4.126 -5.266 1.0021.57 ATOM 2960 OH TYRH 102 8.255 -3.706 -6.526 1.0029.25 ATOM 2962 C TYRH 102 10.410 -5.062 0.923 1.0010.63 ATOM 2963 O TYRH 102 11.507 -5.608 1.019 1.0010.52 ATOM 2964 N TRP H 103 9.522 -4.971 1.884 1.0012.90 ATOM 2966 CA TRPH 103 9.734 -5.491 3.246 1.0012.06 ATOM 2967 CB TRP H 103 9.979 -4.325 4.256 1.0010.97 ATOM 2968 CG TRP H 103 11.293 -3.613 4.125 1.007.64 ATOM 2969 CD2 TRPH 103 12.445 •3.715 5.028 1.007.34 ATOM 2970 CE2 TRP H 103 13.461 -2.945 4.476 1.002.00 ATOM 2971 CE3 TRPH 103 12.692 -4.388 6.241 1.002.00 ATOM 2972 CD1 TR H 103 11.676 -2.790 3.109 1.002.00 ATOM 2973 NE1 TRPH 103 12.957 -2.399 3.334 1.005.49 ATOM 2975 CZ2 TRPH 103 14.718 -2.824 5.073 1.006.14 ATOM 2976 CZ3 TRP H 103 13.922 -4.274 6.837 1.004.72 ATOM 2977 CH2 TR H 103 14.930 -3.503 6.264 1.004.93 ATOM 2978 C TRP H 103 8.450 -6.196 3.663 1.0010.58 ATOM 2979 O TR H 103 7.349 -5.699 3.367 1.0012.28 ATOM 2980 N GLYH 104 8.555 -7.366 4.288 1.009.92 ATOM 2982 CA GLYH 104 7.338 -7.982 4.799 1.00 8.86 ATOM 2983 C GLY H 104 6.892 -7.280 6.088 1.0011.03 ATOM 2984 O GLY H 104 7.500 -6.276 6.495 1.007.62 ATOM 2985 N GLNH 105 5.872 -7.822 6.744 1.0014.11 ATOM 2987 CA GLNH 105 5.368 -7.248 7.997 1.0013.52 ATOM 2988 CB GLNH 105 3.900 -7.701 8.254 1.0016.08 ATOM 2989 CG GLN H 105 3.725 -9.073 8.885 1.0016.34 ATOM 2990 CD GLN H 105 4.174-10.239 8.022 1.0017.73 ATOM 2991 OE1 GLN H 105 4.238-10.158 6.808 1.0021.14 ATOM 2992 NE2 GLN H 105 4.489-11.338 8.655 1.0022.59 ATOM 2995 C GLNH 105 6.271 -7.593 9.179 1.0013.99 ATOM 2996 O GLN H 105 6.235 -6.907 10.203 1.0012.82 ATOM 2997 N GLY H 106 7.108 -8.638 9.007 1.0013.67 ATOM 2999 CA GLYH 106 8.032 -9.058 10.049 1.0011.11 ATOM 3000 C GLY H 106 7.440 - •10.150 10.927 1.0012.32 ATOM 3001 O GLYH 106 6.213 -10.266 11.071 1.0011.02 ATOM 3002 N THRH 107 8.303 -10.969 11.489 1.0014.65 ATOM 3004 CA THRH 107 7.861 -12.050 12.387 1.0012.73 ATOM 3005 CB THRH 107 7.916-13.415 11.638 1.0010.15 ATOM 3006 OG1 THRH 107 7.388-14.451 12.478 1.0015.55 ATOM 3008 CG2 THRH 107 9.320-13.770 11.204 1.004.69 ATOM 3009 C THRH 107 8.746-12.030 13.619 1.0010.17 ATOM 3010 O THRH 107 9.951 -11.941 13.485 1.0010.87 ATOM 3011 N THRH 108 8.174-12.063 14.843 1.0012.24 ATOM 3013 CA THRH 108 9.036-11.947 16.022 1.0010.94 ATOM 3014 CB THRH 108 8.392-11.090 17.206 1.0012.32 ATOM 3015 OG1 THRH 108 9.309-10.902 18.318 1.0013.78 ATOM 3017 CG2 THRH 108 7.162-11.704 17.736 1.0015.73 ATOM 3018 C THRH 108 9.597-13.283 16.497 1.009.14 ATOM 3019 O THRH 108 8.928-14.325 16.556 1.006.78 ATOM 3020 N VALH 109 10.857-13.228 16.755 1.00 8.85 ATOM 3022 CA VALH 109 11.603-14.334 17.259 1.009.39 ATOM 3023 CB VALH 109 12.782-14.660 16.313 1.0011.58 ATOM 3024 CGI VALH 109 13.746-15.632 16.965 1.005.51 ATOM 3025 CG2 VALH 109 12.254-15.239 14.982 1.0010.69 ATOM 3026 C VALH 109 12.175-13.884 18.594 1.0012.15 ATOM 3027 O VALH 109 12.918-12.923 18.638 1.0012.01 ATOM 3028 N THRH 110 11.785-14.562 19.680 1.0011.46 ATOM 3030 CA THRH 110 12.309-14.24921.010 1.0011.24 ATOM 3031 CB THRH 110 11.175-14.06022.037 1.009.63 ATOM 3032 OG1 THRH 110 10.208-13.12721.544 1.0010.83 ATOM 3034 CG2 THRH 110 11.740-13.573 23.346 1.008.99 ATOM 3035 C THRH 110 13.144-15.40521.498 1.007.60 ATOM 3036 O THRH 110 12.661-16.51921.509 1.0012.38 ATOM 3037 N VAL Hill 14.372-15.151 21.857 1.009.00 ATOM 3039 CA VAL Hill 15.227-16.19222.420 1.0012.99 ATOM 3040 CB VAL Hill 16.640-16.28221.736 1.0010.01 ATOM 3041 CGI VAL Hill 17.398-17.48422.286 1.008.99 ATOM 3042 CG2 VAL Hill 16.505-16.383 20.206 1.0014.22 ATOM 3043 C VAL Hill 15.458-15.89523.918 1.0013.42 ATOM 3044 O VAL Hill 16.267-15.051 24.277 1.0014.03 ATOM 3045 N SER H 112 14.806-16.61824.779 1.0015.10 ATOM 3047 CA SERH 112 14.993-16.38026.185 1.0017.45 ATOM 3048 CB SER H 112 13.871 -15.49626.699 1.0017.57 ATOM 3049 OG SERH 112 14.114-15.13628.034 1.0018.71 ATOM 3051 C SERH 112 14.966-17.66726.953 1.0018.74 ATOM 3052 O SERH 112 14.136-18.52526.687 1.0021.32 ATOM 3053 N SERH 113 15.847-17.79527.926 1.0022.03 ATOM 3055 CA SERH 113 15.794-18.95728.828 1.0026.34 ATOM 3056 CB SERH 113 17.205-19.27329.321 1.0028.00 ATOM 3057 OG SERH 113 17.811 -18.10929.887 1.0035.95 ATOM 3059 C SERH 113 14.818-18.75930.049 1.0026.98 ATOM 3060 O SERH 113 14.673-19.66630.891 1.0026.75 ATOM 3061 N ALAH 114 14.144-17.58330.119 1.0025.34 ATOM 3063 CA ALA HI 14 13.242-17.263 31.218 1.0023.14 ATOM 3064 CB ALA H 114 12.860-15.78631.184 1.0022.38 ATOM 3065 C ALAH 114 11.977-18.113 31.210 1.0024.60 ATOM 3066 O ALA H 114 11.415-18.43830.137 1.0024.23 ATOM 3067 N LYSH 115 11.514-18.44932.436 1.0023.35 ATOM 3069 CA LYSH 115 10.315-19.24432.615 1.0023.70 ATOM 3070 CB LYSH 115 10.461-20.13633.834 1.0024.56 ATOM 3071 CG LYS HI 15 11.658-21.03933.758 1.0031.61 ATOM 3072 CD LYSH 115 11.624-22.08534.863 1.0037.03 ATOM 3073 CE LYSH 115 12.721-23.133 34.688 1.0036.28 ATOM 3074 NZ LYSH 115 12.668-24.16235.769 1.0037.66 ATOM 3078 C LYSH 115 9.095-18.361 32.786 1.0021.83 ATOM 3079 O LYS HI 15 9.202-17.20733.182 1.0019.35 ATOM 3080 N THRH 116 7.929-18.915 32.513 1.0022.54 ATOM 3082 CA THRH 116 6.719-18.14532.646 1.0025.02 ATOM 3083 CB THRH 116 5.481-18.99232.343 1.0028.05 ATOM 3084 OG1 THRH 116 5.582-19.47730.988 1.0031.99 ATOM 3086 CG2 THR HI 16 4.195-18.183 32.500 1.0025.98 ATOM 3087 C THRH 116 6.667-17.60234.036 1.0023.95 ATOM 3088 O THRH 116 7.072-18.27434.977 1.0023.92 ATOM 3089 N THRH 117 6.225-16.38534.168 1.0024.46 ATOM 3091 CA THRH 117 6.255-15.70635.461 1.0022.17 ATOM 3092 CB THRH 117 7.605-15.005 35.649 1.0022.94 ATOM 3093 OG1 THRH 117 8.671 -15.961 35.443 1.0019.91 ATOM 3095 CG2 THRH 117 7.730-14.41437.043 1.0025.03 ATOM 3096 C THRH 117 5.135-14.68635.504 1.0022.41 ATOM 3097 O THRH 117 5.031-13.80634.631 1.0022.33 ATOM 3098 N PROH 118 4.236-14.811 36.481 1.0021.47 ATOM 3099 CD PROH 118 4.285-15.77937.622 1.0024.37 ATOM 3100 CA PROH 118 3.128-13.88636.620 1.0019.44 ATOM 3101 CB PROH 118 2.249-14.585 37.664 1.0021.47 ATOM 3102 CG PROH 118 3.274-15.19838.569 1.0023.59 ATOM 3103 C PROH 118 3.744-12.593 37.114 1.0016.22 ATOM 3104 O PROH 118 4.804-12.62437.750 1.0013.84 ATOM 3105 N PROH 119 3.181 -11.44236.814 1.0014.35 ATOM 3106 CD PROH 119 1.959-11.20736.027 1.0014.96 ATOM 3107 CA PROH 119 3.775-10.19237.278 1.0014.79 ATOM 3108 CB PROH 119 3.119 -9.16736.378 1.0013.18 ATOM 3109 CG PROH 119 1.742 -9.71636.246 1.0013.05 ATOM 3110 C PROH 119 3.420 -9.95438.716 1.0013.65 ATOM 3111 O PROH 119 2.351 -10.39239.166 1.0014.64 ATOM 3112 N THRH 120 4.281 -9.29039.445 1.0013.96 ATOM 3114 CA THRH 120 3.852 -8.82540.759 1.0012.82 ATOM 3115 CB THRH 120 4.974 -8.76641.783 1.005.50 ATOM 3116 OG1 THRH 120 5.854 -7.76641.423 1.0020.74 ATOM 3118 CG2 THRH 120 5.743-10.04441.845 1.008.80 ATOM 3119 C THRH 120 3.343 -7.45440.486 1.00 8.85 ATOM 3120 O THRH 120 4.065 -6.66239.870 1.0010.44 ATOM 3121 N VALH 121 2.070 -7.20840.783 1.0011.59 ATOM 3123 CA VALH 121 1.455 -5.89640.488 1.00 8.52 ATOM 3124 CB VALH 121 0.011 -6.06440.025 1.006.26 ATOM 3125 CGI VALH 121 -0.610 -4.713 39.693 1.003.84 ATOM 3126 CG2 VALH 121 -0.004 -6.98738.822 1.009.50 ATOM 3127 C VALH 121 1.522 -4.96841.701 1.0012.01 ATOM 3128 O VALH 121 1.283 -5.38842.839 1.0010.41 ATOM 3129 N TYRH 122 1.871 -3.71541.459 1.0011.35 ATOM 3131 CA TYRH 122 2.094 -2.76842.551 1.0011.02 ATOM 3132 CB TYRH 122 3.597 -2.47542.697 1.007.81 ATOM 3133 CG TYRH 122 4.422 -3.681 43.099 1.0015.44 ATOM 3134 CD1 TYRH 122 4.080 -4.43644.244 1.0016.70 ATOM 3135 CE1 TYRH 122 4.846 -5.52344.662 1.0012.55 ATOM 3136 CD2 TYRH 122 5.553 -4.05742.382 1.007.91 ATOM 3137 CE2 TYR H 122 6.328 -5.12842.784 1.008.28 ATOM 3138 CZ TYRH 122 5.977 -5.861 43.932 1.0011.52 ATOM 3139 OH TYRH 122 6.815 -6.85044.397 1.0011.02 ATOM 3141 C TYRH 122 1.359 -1.50442.255 1.0012.61 ATOM 3142 O TYRH 122 1.438 -0.97341.184 1.0011.44 ATOM 3143 N PROH 123 0.606 ■1.001 43.195 1.0018.80 ATOM 3144 CD PRO H 123 0.485 -1.48944.591 1.0019.13 ATOM 3145 CA PROH 123 -0.164 0.223 43.008 1.0018.57 ATOM 3146 CB PRO H 123 -1.109 0.18244.199 1.0015.86 ATOM 3147 CG PROH 123 -0.191 -0.31945.247 1.0019.34 ATOM 3148 C PRO H 123 0.769 1.40343.074 1.0018.37 ATOM 3149 O PROH 123 1.773 1.37343.802 1.0024.31 ATOM 3150 N LEUH 124 0.477 2.41642.305 1.0017.89 ATOM 3152 CA LEUH 124 1.270 3.62842.346 1.0018.57 ATOM 3153 CB LEUH 124 1.954 3.89841.015 1.0017.71 ATOM 3154 CG LEU H 124 2.962 2.83840.535 1.0020.67 ATOM 3155 CD1 LEUH 124 3.662 3.341 39.297 1.0018.20 ATOM 3156 CD2 LEUH 124 3.950 2.45941.651 1.0018.24 ATOM 3157 C LEU H 124 0.396 4.80542.758 1.0018.06 ATOM 3158 O LEUH 124 -0.483 5.27241.994 1.0014.26 ATOM 3159 N ALA H 125 0.589 5.21444.013 1.0018.65 ATOM 3161 CA ALA H 125 -0.168 6.31444.583 1.0016.82 ATOM 3162 CB ALA H 125 -0.580 6.00746.029 1.0013.74 ATOM 3163 C ALAH 125 0.682 7.54844.523 1.0015.68 ATOM 3164 O ALAH 125 1.896 7.46244.551 1.0016.41 ATOM 3165 N PRO H 126 0.059 8.70444.406 1.0016.40 ATOM 3166 CD PRO H 126 -1.415 8.89344.331 1.0013.85 ATOM 3167 CA PRO H 126 0.771 9.97844.333 1.0016.02 ATOM 3168 CB PRO H 126 -0.372 11.00044.314 1.0015.53 ATOM 3169 CG PRO H 126 -1.481 10.22443.672 1.0014.07 ATOM 3170 C PROH 126 1.740 10.18845.498 1.0018.31 ATOM 3171 O PROH 126 1.461 9.84846.671 1.0016.34 ATOM 3172 N GLY H 127 2878 10.73645.166 1.0022.48 ATOM 3174 CA GLY H 127 3.860 11.01246.166 1.0030.63 ATOM 3175 C GLYH 127 3.583 12.32646.845 1.0033.75 ATOM 3176 OT1 GLY H 127 4.359 13.28346.589 1.0039.27 ATOM 3177 OT2 GLY H 127 2.581 12.40947.625 1.0035.28 ATOM 3178 CB ALA H 134 -7.921 19.96239.302 1.0021.74 ATOM 3179 C ALAH 134 -8.377 17.51039.469 1.0025.40 ATOM 3180 O ALAH 134 -9.457 16.953 39.269 1.0026.02 ATOM 3183 N ALAH 134 -7.261 18.73241.332 1.0024.67 ATOM 3185 CA ALA H 134 -8.291 18.83540.244 1.0023.36 ATOM 3186 N METH 135 -7.229 17.05938.997 1.0024.22 ATOM 3188 CA MET H 135 -7.095 15.775 38.333 1.00 26.09 ATOM 3189 CB MET H 135 -6.684 15.971 36.852 1.00 30.45 ATOM 3 190 CG MET H 135 -7.835 16.193 35.855 1.00 34.99 ATOM 3191 SD MET H 135 -8.958 14.753 35.759 1.00 46.83 ATOM 3192 CE MET H 135 -8.784 14.216 34.059 1.00 42.78 ATOM 3193 C MET H 135 -5.978 15.070 39.074 1.00 25.74 ATOM 3194 O MET H 135 -5.028 15.734 39.523 1.00 25.90 ATOM 3195 N VAL H 136 -6.074 13.773 39.258 1.00 22.09 ATOM 3197 CA VAL H 136 -5.001 13.072 39.935 1.00 18.97 ATOM 3198 CB VAL H 136 -5.429 12.618 41.367 1.00 16.24 ATOM 3199 CG I VAL H 136 -6.694 1 1.797 41.355 1.00 15.37 ATOM 3200 CG2 VAL H 136 -4.297 1 1.870 42.020 1.00 16.51 ATOM 3201 C VAL H 136 -4.555 1 1.889 39.100 1.00 17.30 ATOM 3202 O VAL H 136 -5.397 1 1.220 38.485 1.00 17.97 ATOM 3203 N THR H 137 -3.245 1 1.643 39.035 1.00 17.82 ATOM 3205 CA THR H 137 -2.783 10.483 38.276 1.00 18.38 ATOM 3206 CB THR H 137 - 1.731 10.855 37.238 1.00 15.72 ATOM 3207 OG1 THR H 137 -2.313 1 1.857 36.384 1.00 16.58 ATOM 3209 CG2 THR H 137 -1.374 9.644 36.382 1.00 13.21 ATOM 3210 C THR H 137 -2.287 9.336 39.164 1.00 16.41 ATOM 3211 O THR H 137 -1.405 9.514 40.023 1.00 14.38 ATOM 3212 N LEU H 138 -2.924 8.182 38.940 1.00 13.46 ATOM 3214 CA LEU H 138 -2.617 6.950 39.647 1.00 11.93 ATOM 3215 CB LEU H 138 -3.897 6.401 40.222 1.00 9.54 ATOM 3216 CG LEU H 138 -4.690 7.402 41.030 1.00 9.64 ATOM 3217 CD1 LEU H 138 -5.943 6.750 41.531 1.00 11.85 ATOM 3218 CD2 LEU H 138 -3.839 7.920 42.174 1.00 6.56 ATOM 3219 C LEU H 138 -2.046 5.964 38.649 1.00 12.78 ATOM 3220 O LEU H 138 -2.281 6.106 37.457 1.00 10.57 ATOM 3221 N GLY H 139 -1.316 4.988 39.106 1.00 11.80 ATOM 3223 CA GLY H 139 -0.770 4.041 38.174 1.00 11.77 ATOM 3224 C GLY H 139 -0.578 2.682 38.763 1.00 14.58 ATOM 3225 O GLY H 139 -0.863 2.452 39.936 1.00 14.52 ATOM 3226 N CYS H 140 -0.090 1.781 37.952 1.00 13.05 ATOM 3228 CA CYS H 140 0.182 0.447 38.375 1.00 12.15 ATOM 3229 CB CYS H 140 -0.942 -0.487 37.970 1.00 15.82 ATOM 3230 SG CYS H 140 -1.991 -0.935 39.377 1.00 30.05 ATOM 3231 C CYS H 140 1.438 -0.028 37.762 1.00 9.66 ATOM 3232 O CYS H 140 1.589 0.121 36.548 1.00 8.35 ATOM 3233 N LEU H 141 2.337 -0.555 38.594 1.00 6.85 ATOM 3235 CA LEU H 141 3.554 -1.210 38.112 1.00 10.45 ATOM 3236 CB LEU H 141 4.728 -1.024 39.075 1.00 3.00 ATOM 3237 CG LEU H 141 6.061 -1.672 38.701 1.00 7.34 ATOM 3238 CD1 LEU H 141 6.581 -1.153 37.363 1.00 7.63 ATOM 3239 CD2 LEU H 141 7.091 -1.374 39.751 1.00 2.28 ATOM 3240 C LEU H 141 3.299 -2.708 37.948 1.00 9.22 ATOM 3241 O LEU H 141 2.819 -3.363 38.869 1.00 8.85 ATOM 3242 N VAL H 142 3.550 -3.220 36.751 1.00 10.01 ATOM 3244 CA VAL H 142 3.449 -4.641 36.484 1.00 7.47 ATOM 3245 CB VAL H 142 2.629 -4.891 35.208 1.00 10.12 ATOM 3246 CGI VAL H 142 2.421 -6.409 34.967 1.00 8.96 ATOM 3247 CG2 VAL H 142 1.282 -4.167 35.330 1.00 6.58 ATOM 3248 C VAL H 142 4.880 -5.167 36.351 1.00 11.16 ATOM 3249 O VAL H 142 5.513 -5.101 35.263 1.00 6.29 ATOM 3250 N LYS H 143 5.393 -5.690 37.460 1.00 9.75 ATOM 3252 CA LYS H 143 6.804 -6.016 37.537 1.00 12.16 ATOM 3253 CB LYS H 143 7.348 -5.453 38.844 1.00 9.61 ATOM 3254 CG LYS H 143 8.868 -5.354 38.937 1.00 9.64 ATOM 3255 CD LYS H 143 9.275 -4.918 40.340 1.00 11.17 ATOM 3256 CE LYS H 143 10.793 -4.938 40.495 1.00 15.36 ATOM 3257 NZ LYS H 143 11.200 -5.003 41.925 1.00 13.08 ATOM 3261 C LYS H 143 7.158 -7.514 37.403 1.00 14.70 ATOM 3262 O LYS H 143 6.437 -8.400 37.861 1.00 17.80 ATOM 3263 N GLY H 144 8.250 -7.745 36.687 1.00 16.56 ATOM 3265 CA GLY H 144 8.881 -9.067 36.594 1.00 18.62 ATOM 3266 C GLY H 144 8.089 -10.220 36.006 1.00 16.58 ATOM 3267 O GLY H 144 8.190 -11.328 36.517 1.00 20.26 ATOM 3268 N TYR H 145 7.362 -10.004 34.922 1.00 15.03 ATOM 3270 CA TYR H 145 6.614 -1 1.103 34.286 1.00 12.99 ATOM 3271 CB TYR H 145 5.208 -10.660 33.827 1.00 10.99 ATOM 3272 CG TYR H 145 5.135 -9.584 32.771 1.00 13.14 ATOM 3273 CD1 TYR H 145 5.416 -8.267 33.096 1.00 15.73 ATOM 3274 CE1 TYRH 145 5.282 -7.25832.165 1.0012.07 ATOM 3275 CD2 TYRH 145 4.716 -9.85031.460 1.0015.71 ATOM 3276 CE2 TYR H 145 4.582 -8.82630.509 1.009.54 ATOM 3277 CZ TYR H 145 4.873 -7.53430.876 1.0010.77 ATOM 3278 OH TYRH 145 4.831 -6.49729.946 1.009.76 ATOM 3280 C TYR H 145 7.377-11.65433.088 1.0013.49 ATOM 3281 O TYRH 145 8.359-11.07432.659 1.0012.72 ATOM 3282 N PHE H 146 6.944-12.803 32.602 1.0016.82 ATOM 3284 CA PHE H 146 7.473-13.38231.370 1.0018.55 ATOM 3285 CB PHE H 146 8.904-13.87831.511 1.0018.86 ATOM 3286 CG PHE H 146 9.412-14.45830.205 1.0023.23 ATOM 3287 CD1 PHEH 146 10.213-13.70029.365 1.0025.00 ATOM 3288 CD2 PHEH 146 8.973-15.715 29.749 1.0024.90 ATOM 3289 CE1 PHE H 146 10.555-14.16228.084 1.0026.32 ATOM 3290 CE2 PHE H 146 9.304-16.18528.488 1.0026.32 ATOM 3291 CZ PHEH 146 10.092-15.40727.646 1.0025.16 ATOM 3292 C PHE H 146 6.649-14.55631.022 1.0019.54 ATOM 3293 O PHE H 146 6.362-15.325 31.931 1.0018.10 ATOM 3294 N PRO H 147 6.212-14.74629.719 1.0021.47 ATOM 3295 CD PRO H 147 4.947-15.42729.403 1.0021.60 ATOM 3296 CA PRO H 147 6.425-13.87028.551 1.0021.86 ATOM 3297 CB PRO H 147 6.189-14.88427.403 1.0021.39 ATOM 3298 CG PRO H 147 5.240-15.91228.012 1.0019.80 ATOM 3299 C PRO H 147 5.429-12.69528.485 1.0018.87 ATOM 3300 O PRO H 147 4.635-12.51729.377 1.0015.77 ATOM 3301 N GLUH 148 5.418-11.983 27.333 1.0019.05 ATOM 3303 CA GLU H 148 4.398-10.98227.056 1.0019.21 ATOM 3304 CB GLU H 148 4.970 -9.89726.157 1.0017.80 ATOM 3305 CG GLU H 148 6.120 -9.14926.752 1.0015.35 ATOM 3306 CD GLU H 148 6.491 -7.96025.920 1.0019.90 ATOM 3307 OE1 GLUH 148 7.608 -7.95725.354 1.0023.72 ATOM 3308 OE2 GLU H 148 5.670 -7.01525.826 1.0017.13 ATOM 3309 C GLU H 148 3.287-11.66626.280 1.0019.80 ATOM 3310 O GLUH 148 3.495-12.76625.824 1.0021.47 ATOM 3311 N PRO H 149 2.074-11.08526.123 1.0019.34 ATOM 3312 CD PRO H 149 0.842-11.841 25.966 1.0015.47 ATOM 3313 CA PRO H 149 1.637 -9.81226.659 1.0018.47 ATOM 3314 CB PROH 149 0.524 -9.46025.678 1.0018.21 ATOM 3315 CG PRO H 149 0.018-10.82425.214 1.0017.16 ATOM 3316 C PROH 149 1.103 -9.88728.117 1.0018.85 ATOM 3317 O PROH 149 1.155-10.89928.823 1.0016.35 ATOM 3318 N VALH 150 0.418 -8.81428.427 1.0019.66 ATOM 3320 CA VALH 150 -0.234 -8.57229.679 1.0016.78 ATOM 3321 CB VALH 150 0.816 -7.97730.670 1.0016.55 ATOM 3322 CGI VALH 150 0.488 -6.56631.077 1.0017.59 ATOM 3323 CG2 VALH 150 0.998 -8.87831.854 1.0013.17 ATOM 3324 C VALH 150 -1.324 -7.58029.302 1.0016.49 ATOM 3325 O VALH 150 -1.165 -6.83228.343 1.0018.33 ATOM 3326 N THRH 151 -2.459 -7.653 29.919 1.0014.32 ATOM 3328 CA THRH 151 -3.527 -6.71629.637 1.0014.69 ATOM 3329 CB THRH 151 -4.778 -7.44829.097 1.0017.81 ATOM 3330 OG1 THRH 151 -5.351 -8.263 30.141 1.0022.14 ATOM 3332 CG2 THRH 151 -4.396 -8.36427.922 1.0020.30 ATOM 3333 C THRH 151 -3.899 -5.97830.920 1.0013.72 ATOM 3334 O THRH 151 -4.195 -6.613 31.921 1.0013.94 ATOM 3335 N VALH 152 -3.912 -4.65730.864 1.0012.98 ATOM 3337 CA VALH 152 -4.175 -3.843 32.041 1.0012.73 ATOM 3338 CB VALH 152 -2.967 -2.94732.373 1.0011.49 ATOM 3339 CGI VALH 152 -3.279 -2.10833.610 1.0011.37 ATOM 3340 CG2 VALH 152 -1.719 -3.79232.608 1.009.03 ATOM 3341 C VALH 152 -5.401 -2.965 31.864 1.0015.95 ATOM 3342 O VALH 152 -5.481 -2.17030.914 1.0019.74 ATOM 3343 N THRH 153 -6.370 -3.12432.770 1.0019.44 ATOM 3345 CA THRH 153 -7.587 -2.32432.746 1.0019.80 ATOM 3346 CB THRH 153 -8.820 -3.223 32.528 1.0021.72 ATOM 3347 OG1 THRH 153 -8.652 -4.41233.286 1.0026.52 ATOM 3349 CG2 THRH 153 -8.974 -3.59731.063 1.0021.56 ATOM 3350 C THRH 153 -7.761 -1.521 34.064 1.0017.98 ATOM 3351 O THRH 153 -7.047 -1.74435.043 1.0017.86 ATOM 3352 N TRPH 154 -8.681 -0.56234.054 1.0018.02 ATOM 3354 CA TRPH 154 -8.954 0.231 35.232 1.0016.37 ATOM 3355 CB TRPH 154 -8.438 1.62035.052 1.0015.29 ATOM 3356 CG TRP H 154 -6.960 1.649 34.987 1.00 14.01 ATOM 3357 CD2 TRP H 154 -6.070 1.827 36.097 1.00 14.22 ATOM 3358 CE2 TRP H 154 -4.766 1.906 35.577 1.00 12.55 ATOM 3359 CE3 TRP H 154 -6.261 1.950 37.493 1.00 13.71 ATOM 3360 CD1 TRP H 154 -6.189 1.608 33.866 1.00 13.72 ATOM 3361 NE1 TRP H 154 -4.881 1.763 34.225 1.00 14.65 ATOM 3363 CZ2 TR H 154 -3.652 2.112 36.377 1.00 1 1.60 ATOM 3364 CZ3 TRP H 154 -5.153 2.164 38.288 1.00 13.74 ATOM 3365 CH2 TRP H 154 -3.865 2.247 37.720 1.00 15.50 ATOM 3366 C TRP H 154 - 10.423 0.226 35.482 1.00 16.57 ATOM 3367 O TRP H 154 - 1 1.208 0.444 34.565 1.00 19.07 ATOM 3368 N ASN H 155 - 10.781 -0.062 36.722 1.00 18.63 ATOM 3370 CA ASN H 155 -12.177 -0.278 37.1 17 1.00 19.34 ATOM 3371 CB ASN H 155 -12.895 1.047 37.330 1.00 19.07 ATOM 3372 CG ASN H 155 - 12.499 1.668 38.658 1.00 19.37 ATOM 3373 OD1 ASN H 155 -1 1.818 1.048 39.479 1.00 17.72 ATOM 3374 ND2 ASN H 155 -12.904 2.898 38.869 1.00 21.85 ATOM 3377 C ASN H 155 -12.902 -1.167 36.1 14 1.00 20.59 ATOM 3378 O ASN H 155 -13.989 -0.851 35.645 1.00 19.83 ATOM 3379 N SER H 156 -12.232 -2.290 35.767 1.00 22.94 ATOM 3381 CA SER H 156 -12.740 -3.255 34.801 1.00 23.80 ATOM 3382 CB SER H 156 -14.028 -3.890 35.333 1.00 24.08 ATOM 3383 OG SER H 156 -13.778 -4.574 36.550 1.00 23.19 ATOM 3385 C SER H 156 - 12.968 -2.650 33.393 1.00 26.88 ATOM 3386 O SER H 156 -13.730 -3.185 32.575 1.00 29.20 ATOM 3387 N GLY H 157 -12.293 -1.561 33.090 1.00 26.24 ATOM 3389 CA GLY H 157 -12.488 -0.966 31.798 1.00 28.52 ATOM 3390 C GLY H 157 -13.553 0.129 31.789 1.00 28.13 ATOM 3391 O GLY H 157 -13.793 0.740 30.741 1.00 28.70 ATOM 3392 N SER H 158 -14.194 0.371 32.945 1.00 27.82 ATOM 3394 CA SER H 158 -15.164 1.445 33.049 1.00 27.17 ATOM 3395 CB SER H 158 -16.045 1.301 34.334 1.00 28.51 ATOM 3396 OG SER H 158 -15.342 1.560 35.537 1.00 25.88 ATOM 3398 C SER H 158 -14.420 2.768 33.007 1.00 27.55 ATOM 3399 O SER H 158 -14.947 3.772 32.555 1.00 28.23 ATOM 3400 N LEU H 159 -13.177 2.753 33.491 1.00 29.42 ATOM 3402 CA LEU H 159 -12.295 3.898 33.352 1.00 30.68 ATOM 3403 CB LEU H 159 -1 1.288 3.966 34.495 1.00 31.18 ATOM 3404 CG LEU H 159 -1 1.756 4.650 35.788 1.00 29.87 ATOM 3405 CD 1 LEU H I 59 -10.635 4.657 36.819 1.00 34.45 ATOM 3406 CD2 LEU H 159 -12.186 6.067 35.491 1.00 29.03 ATOM 3407 C LEU H 159 -1 1.571 3.717 32.042 1.00 31.97 ATOM 3408 O LEU H 159 -10.554 3.036 31.980 1.00 31.21 ATOM 3409 N ALA H 160 -12.168 4.261 30.990 1.00 34.61 ATOM 341 1 CA ALA H 160 -1 1.634 4.120 29.629 1.00 35.80 ATOM 3412 CB ALA H 160 -12.804 3.926 28.668 1.00 34.51 ATOM 3413 C ALA H 160 - 10.776 5.337 29.226 1.00 35.27 ATOM 3414 O ALA H 160 -9.611 5.209 28.796 1.00 34.38 ATOM 3415 N SER H 161 -1 1.347 6.517 29.381 1.00 33.77 ATOM 3417 CA SER H 161 -10.624 7.747 29.083 1.00 33.98 ATOM 3418 CB SER H 161 -1 1.613 8.91 1 29.028 1.00 33.96 ATOM 3419 OG SER H 161 -12.943 8.420 28.847 1.00 38.30 ATOM 3421 C SER H 161 -9.560 8.020 30.155 1.00 30.88 ATOM 3422 O SER H 161 -9.693 7.603 31.314 1.00 32.73 ATOM 3423 N GLY H 162 -8.502 8.702 29.765 1.00 28.58 ATOM 3425 CA GLY H 162 -7.480 9.082 30.742 1.00 23.36 ATOM 3426 C GLY H 162 -6.467 8.005 31.081 1.00 19.44 ATOM 3427 O GLY H 162 -5.669 8.193 32.016 1.00 17.19 ATOM 3428 N VAL H 163 -6.462 6.913 30.296 1.00 16.90 ATOM 3430 CA VAL H 163 -5.546 5.808 30.529 1.00 14.28 ATOM 3431 CB VAL H 163 -6.243 4.469 30.285 1.00 1 1.19 ATOM 3432 CGI VAL H 163 -5.256 3.321 30.477 1.00 9.55 ATOM 3433 CG2 VAL H 163 -7.402 4.343 31.259 1.00 8.14 ATOM 3434 C VAL H 163 -4.318 5.896 29.644 1.00 16.70 ATOM 3435 O VAL H 163 -4.409 6.341 28.504 1.00 20.46 ATOM 3436 N HIS H 164 -3.190 5.493 30.176 1.00 12.44 ATOM 3438 CA HIS H 164 -1.964 5.449 29.434 1.00 12.24 ATOM 3439 CB HIS H 164 -1.048 6.574 29.835 1.00 12.04 ATOM 3440 CG HIS H 164 -1.363 7.839 29.187 1.00 17.45 ATOM 3441 CD2 HIS H 164 -1.795 9.016 29.683 1.00 16.45 ATOM 3442 ND1 HIS H 164 -1.1 1 1 8.058 27.848 1.00 19.78 ATOM 3444 CE1 HIS H 164 -1.345 9.283 27.520 1.00 18.88 ATOM 3445 NE2 HIS H 164 -1.749 9.88328.620 1.0019.92 ATOM 3447 C HISH 164 -1.249 4.20229.775 1.0012.66 ATOM 3448 O HIS H 164 -0.920 4.01030.928 1.0012.50 ATOM 3449 N THRH 165 -1.023 3.32728.830 1.0012.38 ATOM 3451 CA THRH 165 -0.198 2.17629.140 1.0010.10 ATOM 3452 CB THRH 165 -0.932 0.85928.952 1.009.55 ATOM 3453 OG1 THRH 165 -2.129 0.91929.729 1.0011.21 ATOM 3455 CG2 THRH 165 -0.086 -0.30729.427 1.008.04 ATOM 3456 C THRH 165 1.047 2.22728.313 1.0011.67 ATOM 3457 O THRH 165 0.973 2.441 27.118 1.0010.32 ATOM 3458 N PHEH 166 2.188 2.05728.992 11.0011.57 ATOM 3460 CA PHEH 166 3.508 2.19628.398 1.0012.01 ATOM 3461 CB PHEH 166 4.399 2.95729.415 1.009.65 ATOM 3462 CG PHE H 166 3.773 4.28629.831 1.008.07 ATOM 3463 CD1 PHE H 166 2.850 4.34930.874 1.004.17 ATOM 3464 CD2 PHEH 166 4.009 5.45929.082 1.0010.68 ATOM 3465 CE1 PHEH 166 2.156 5.54231.164 1.008.24 ATOM 3466 CE2 PHEH 166 3.318 6.65929.363 1.0011.02 ATOM 3467 CZ PHEH 166 2.385 6.69930.401 1.005.44 ATOM 3468 C PHEH 166 4.110 0.82028.001 1.0015.40 ATOM 3469 O PHEH 166 3.559 -0.23728.381 1.0016.48 ATOM 3470 N PROH 167 5.212 0.823 27.173 1.0014.51 ATOM 3471 CD PROH 167 5.834 2.01926.553 1.0014.57 ATOM 3472 CA PRO H 167 5.902 -0.39426.687 1.0013.56 ATOM 3473 CB PRO H 167 6.851 0.14025.578 1.0015.95 ATOM 3474 CG PROH 167 6.300 1.47525.231 1.0015.19 ATOM 3475 C PROH 167 6.713 -1.111 27.754 1.0013.70 ATOM 3476 O PROH 167 7.304 -0.46728.629 1.008.91 ATOM 3477 N ALAH 168 6.768 -2.44627.620 1.0014.48 ATOM 3479 CA ALAH 168 7.525 -3.29028.526 1.0013.11 ATOM 3480 CB ALA H 168 7.259 -4.76828.238 1.0012.04 ATOM 3481 C ALAH 168 8.998 -3.01528.403 1.0015.12 ATOM 3482 O ALA H 168 9.510 -2.693 27.324 1.0014.20 ATOM 3483 N VALH 169 9.674 -3.04829.527 1.0014.23 ATOM 3485 CA VALH 169 11.092 -2.93529.530 1.0011.53 ATOM 3486 CB VALH 169 11.646 -1.80930.491 1.0010.77 ATOM 3487 CGI VAL HI 69 11.409 -0.43229.901 1.005.38 ATOM 3488 CG2 VAL H 169 10.977 -1.881 31.846 1.008.65 ATOM 3489 C VALH 169 11.580 -4.29029.967 1.0014.43 ATOM 3490 O VALH 169 10.866 • •4.98430.681 1.0013.16 ATOM 3491 N LEUH 170 12.733 - 4.69829.458 1.0016.49 ATOM 3493 CA LEUH 170 13.360 -5.93429.890 1.0020.55 ATOM 3494 CB LEUH 170 13.982 -6.69028.693 1.0017.41 ATOM 3495 CG LEU H 170 14.389 -8.16928.931 1.0016.89 ATOM 3496 CD1 LEU H 170 13.177 -8.97829.315 1.0011.20 ATOM 3497 CD2 LEU H 170 15.030 -8.77727.681 1.0013.43 ATOM 3498 C LEUH 170 14.432 - 5.611 30.913 1.0021.20 ATOM 3499 O LEU H 170 15.435 - •4.96730.608 1.0023.98 ATOM 3500 N GLNH 171 14.191 - 6.00232.149 1.0025.48 ATOM 3502 CA GLNH 171 15.171 -5.80433.183 1.0027.97 ATOM 3503 CB GLNH 171 14.922 -4.48633.992 1.0033.14 ATOM 3504 CG GLNH 171 13.467 -4.03234.231 1.0035.78 ATOM 3505 CD GLNH 171 13.348 -2.49834.464 1.0041.72 ATOM 3506 OE1 GLNH 171 14.208 -1.71834.023 1.0043.19 ATOM 3507 NE2 GLN H 171 12.286 -2.04935.139 1.0039.50 ATOM 3510 C GLNH 171 15.236 - 7.03234.075 1.0030.85 ATOM 3511 O GLNH 171 14.308 - 7.30934.845 1.0030.30 ATOM 3512 N ALA H 172 16.311 ■ 7.811 33.886 1.0030.98 ATOM 3514 CA ALAH 172 16.565 -9.035 34.683 1.0032.89 ATOM 3515 CB ALAH 172 16.048 -8.87036.135 1.0034.56 ATOM 3516 C ALAH 172 15.964 ■10.29634.037 1.0032.42 ATOM 3517 O ALAH 172 15.562-11.243 34.745 1.0033.51 ATOM 3518 N ALA H 173 15.975-10.31632.681 1.0028.84 ATOM 3520 CA ALA H 173 15.362-11.38831.898 1.0024.12 ATOM 3521 CB ALA H 173 15.866-12.773 32.316 1.0024.73 ATOM 3522 C ALA H 173 13.846-11.34031.998 1.0022.90 ATOM 3523 O ALA H 173 13.168-12.16931.422 1.0024.63 ATOM 3524 N LEUH 174 13.301 -10.353 32.701 1.0019.03 ATOM 3526 CA LEU H 174 11.859-10.28632.881 1.0016.09 ATOM 3527 CB LEU H 174 11.495-10.523 34.374 1.0013.53 ATOM 3528 CG LEU H 174 11.811 -11.911 35.012 1.0013.70 ATOM 3529 CD1 LEU H 174 11.331 -11.91036.473 1.0013.19 ATOM 3530 CD2 LEU H 174 11.119-13.04434.233 1.007.07 ATOM 3531 C LEUH 174 11.362 -8.938 32.423 1.0011.64 ATOM 3532 O LEUH 174 12.101 -7.99232.465 1.0013.03 ATOM 3533 N TYRH 175 10.141 -8.88531.993 1.0011.45 ATOM 3535 CA TYRH 175 9.528 -7.64731.500 1.0013.69 ATOM 3536 CB TYRH 175 8.486 -7.93930.415 1.0013.82 ATOM 3537 CG TYRH 175 9.037 -8.57029.180 1.0014.75 ATOM 3538 CD1 TYRH 175 9.958 -7.891 28.408 1.0017.41 ATOM 3539 CE1 TYRH 175 10.501 -8.43827.254 1.0018.34 ATOM 3540 CD2 TYRH 175 8.648 -9.83428.779 1.0018.01 ATOM 3541 CE2 TYRH 175 9.177-10.401 27.619 1.0020.37 ATOM 3542 CZ TYRH 175 10.111 -9.68926.860 1.0019.65 ATOM 3543 OH TYRH 175 10.636-10.221 25.713 1.0021.14 ATOM 3545 C TYRH 175 8.792 -6.86032.607 1.0016.88 ATOM 3546 O TYRH 175 8.132 -7.44033.503 1.0015.69 ATOM 3547 N THRH 176 8.837 -5.53732.473 1.0014.27 ATOM 3549 CA THRH 176 8.140 -4.643 33.386 1.0013.28 ATOM 3550 CB THRH 176 9.132 -3.92834.356 1.0011.07 ATOM 3551 OG1 THRH 176 9.739 -4.86235.272 1.009.99 ATOM 3553 CG2 THRH 176 8.402 -2.85935.144 1.007.94 ATOM 3554 C THRH 176 7.416 -3.57532.590 1.0011.40 ATOM 3555 O THRH 176 8.006 -2.98231.696 1.0010.96 ATOM 3556 N LEUH 177 6.149 -3.35432.842 1.009.44 ATOM 3558 CA LEUH 177 5.521 -2.19932.219 1.0011.96 ATOM 3559 CB LEUH 177 4.761 -2.52230.908 1.0012.44 ATOM 3560 CG LEU H 177 3.533 -3.42630.906 1.0013.51 ATOM 3561 CD1 LEUH 177 2.348 -2.763 31.614 1.0016.92 ATOM 3562 CD2 LEUH 177 3.147 -3.70929.455 1.0019.97 ATOM 3563 C LEUH 177 4.690 -1.441 33.227 1.0011.72 ATOM 3564 O LEU H 177 4.676 -1.805 34.410 1.0012.02 ATOM 3565 N SERH 178 4.086 -0.36632.806 1.009.83 ATOM 3567 CA SERH 178 3.269 0.43033.698 1.0012.66 ATOM 3568 CB SERH 178 4.026 1.65734.240 1.0016.23 ATOM 3569 OG SERH 178 5.018 1.303 35.164 1.0021.15 ATOM 3571 C SERH 178 2.070 0.94432.978 1.0011.78 ATOM 3572 O SERH 178 2.032 0.97831.750 1.0012.05 ATOM 3573 N SERH 179 1.112 1.35033.755 1.0010.09 ATOM 3575 CA SERH 179 -0.072 1.97533.256 1.009.78 ATOM 3576 CB SERH 179 -1.203 0.965 33.162 1.007.12 ATOM 3577 OG SERH 179 -2.348 1.47932.502 1.0013.99 ATOM 3579 C SERH 179 -0.424 3.06034.240 1.0011.73 ATOM 3580 O SERH 179 0.023 3.02835.402 1.0010.99 ATOM 3581 N SERH 180 -1.190 4.00833.791 1.0012.62 ATOM 3583 CA SERH 180 -1.623 5.095 34.634 1.0011.78 ATOM 3584 CB SERH 180 -0.620 6.25734.502 1.0015.26 ATOM 3585 OG SERH 180 -0.740 6.935 33.258 1.0015.98 ATOM 3587 C SERH 180 -3.036 5.54234.226 1.0011.26 ATOM 3588 O SERH 180 -3.404 5.33733.078 1.0012.64 ATOM 3589 N VALH 181 -3.845 6.053 35.189 1.0012.70 ATOM 3591 CA VALH 181 -5.145 6.681 34.903 1.0012.65 ATOM 3592 CB VALH 181 -6.398 6.141 35.610 1.0014.52 ATOM 3593 CGI VALH 181 -7.464 5.805 34.614 1.008.51 ATOM 3594 CG2 VALH 181 -6.095 5.06936.613 1.0015.67 ATOM 3595 C VALH 181 -5.132 8.053 35.502 1.0013.40 ATOM 3596 O VALH 181 -4.566 8.24036.557 1.0010.66 ATOM 3597 N THRH 182 -5.823 8.97934.847 1.0015.42 ATOM 3599 CA THRH 182 -6.030 10.28935.405 1.0012.05 ATOM 3600 CB THRH 182 -5.479 11.385 34.498 1.0012.00 ATOM 3601 OG1 THRH 182 -4.067 11.17834.367 1.0012.34 ATOM 3603 CG2 THRH 182 -5.725 12.775 35.097 1.0010.88 ATOM 3604 C THRH 182 -7.500 10.451 35.616 1.0015.30 ATOM 3605 O THRH 182 -8.317 10.22434.692 1.0015.69 ATOM 3606 N VALH 183 -7.839 10.74936.868 1.0015.89 ATOM 3608 CA VALH 183 -9.228 10.91637.295 1.0015.70 ATOM 3609 CB VALH 183 -9.692 9.76438.256 1.0013.11 ATOM 3610 CGI VALH 183 -9.836 8.46437.491 1.0016.73 ATOM 3611 CG2 VALH 183 -8.703 9.58639.372 1.007.49 ATOM 3612 C VALH 183 -9.376 12.22538.045 1.0014.30 ATOM 3613 O VALH 183 -8.403 12.765 38.527 1.0015.26 ATOM 3614 N PROH 184 -10.595 12.76638.162 1.0015.74 ATOM 3615 CD PROH 184 -11.858 12.23437.661 1.0015.39 ATOM 3616 CA PROH 184 -10.802 14.00438.892 1.0016.30 ATOM 3617 CB PROH 184 -12.304 14.27438.739 1.0015.06 ATOM 3618 CG PROH 184 -12.679 13.48437.534 1.0015.56 ATOM 3619 C PROH 184 -10.444 13.70440.330 1.0015.62 ATOM 3620 O PROH 184 -10.863 12.70240.860 1.0017.90 ATOM 3621 N SERH 185 -9.670 14.53940.949 1.0021.17 ATOM 3623 CA SERH 185 -9.293 14.31942.331 1.0023.69 ATOM 3624 CB SERH 185 -8.349 15.42842.797 1.0026.61 ATOM 3625 OG SERH 185 -8.816 16.703 42.357 1.0031.23 ATOM 3627 C SERH 185 -10.519 14.25543.250 1.0026.32 ATOM 3628 O SERH 185 -10.428 13.761 44.375 1.0029.50 ATOM 3629 N SERH 186 -11.680 14.74442.806 1.0025.25 ATOM 3631 CA SERH 186 -12.862 14.63943.647 1.0025.46 ATOM 3632 CB SERH 186 -14.002 15.50943.091 1.0026.27 ATOM 3633 OG SERH 186 -14.525 15.01841.851 1.0029.82 ATOM 3635 C SERH 186 -13.341 13.17343.770 1.0024.07 ATOM 3636 O SERH 186 -14.195 12.88844.575 1.0024.17 ATOM 3637 N THRH 187 -12.784 12.24942.971 1.0021.70 ATOM 3639 CA THRH 187 -13.287 10.86242.968 1.0021.99 ATOM 3640 CB THRH 187 -13.730 10.44241.555 1.0020.90 ATOM 3641 OG1 THRH 187 -12.589 10.451 40.677 1.0018.99 ATOM 3643 CG2 THRH 187 -14.774 11.40741.023 1.0018.74 ATOM 3644 C THRH 187 -12.261 9.84843.494 1.0023.01 ATOM 3645 O THRH 187 -12.477 8.62843.470 1.0023.61 ATOM 3646 N TRPH 188 -11.140 10.36343.936 1.0020.48 ATOM 3648 CA TRPH 188 -10.135 9.55644.546 1.0021.24 ATOM 3649 CB TRPH 188 -9.142 8.94343.524 1.0015.29 ATOM 3650 CG TR H 188 -8.158 7.98244.185 1.0011.67 ATOM 3651 CD2 TRPH 188 -6.862 8.30444.783 1.008.04 ATOM 3652 CE2 TRP HI 88 -6.334 7.11545.311 1.008.99 ATOM 3653 CE3 TRPH 188 -6.107 9.48744.935 1.008.90 ATOM 3654 CD1 TRP H 188 -8.345 6.63044.385 1.0013.61 ATOM 3655 NE1 TRP HI 88 -7.250 6.131 45.054 1.0014.95 ATOM 3657 CZ2 TRPH 188 -5.089 7.06645.964 1.0012.53 ATOM 3658 CZ3 TRPH 188 -4.885 9.441 45.589 1.0010.52 ATOM 3659 CH2 TRP H 188 -4.381 8.23246.093 1.0012.29 ATOM 3660 C TRPH 188 -9.392 10.44945.511 1.0020.69 ATOM 3661 O TRPH 188 -8.948 11.53445.134 1.0020.70 ATOM 3662 N PROH 189 -9.142 9.96046.713 1.0020.09 ATOM 3663 CD PROH 189 -8.341 10.63947.755 1.0022.74 ATOM 3664 CA PROH 189 -9.520 8.61247.148 1.0020.72 ATOM 3665 CB PROH 189 -8.458 8.31648.180 1.0022.60 ATOM 3666 CG PROH 189 -8.350 9.62748.879 1.0020.47 ATOM 3667 C PROH 189 -10.913 8.37247.708 1.0021.08 ATOM 3668 O PROH 189 -11.095 7.38848.390 1.0022.85 ATOM 3669 N SERH 190 -11.898 9.20547.432 11.0023.42 ATOM 3671 CA SERH 190 -13.249 8.93447.944 1.0021.96 ATOM 3672 CB SERH 190 -14.176 10.09847.640 1.0023.31 ATOM 3673 OG SER H 190 -14.449 10.18946.244 1.0023.23 ATOM 3675 C SERH 190 -13.824 7.671 47.323 1.0024.54 ATOM 3676 O SERH 190 -14.591 6.93947.994 1.0025.15 ATOM 3677 N GLU H 191 -13.505 7.44446.003 1.0025.58 ATOM 3679 CA GLUH 191 -13.961 6.23545.287 1.0023.69 ATOM 3680 CB GLUH 191 -14.754 6.55443.999 1.0025.22 ATOM 3681 CG GLUH 191 -15.884 7.58844.164 1.0028.53 ATOM 3682 CD GLUH 191 -16.949 7.22545.207 1.0028.30 ATOM 3683 OE1 GLUH 191 -16.826 6.16445.856 1.0031.06 ATOM 3684 OE2 GLU H 191 -17.917 8.00645.375 1.0026.40 ATOM 3685 C GLUH 191 -12.796 5.36644.937 1.0023.74 ATOM 3686 O GLUH 191 -11.652 5.82444.872 1.0021.49 ATOM 3687 N THRH 192 -13.097 4.11544.698 1.0020.79 ATOM 3689 CA THRH 192 -12.071 3.13344.454 1.0021.97 ATOM 3690 CB THRH 192 -12.594 1.711 44.731 1.0023.80 ATOM 3691 OG1 THRH 192 -13.011 1.62846.109 1.0029.80 ATOM 3693 CG2 THRH 192 -11.496 0.67744.486 1.0027.22 ATOM 3694 C THRH 192 -11.549 3.16943.053 1.0018.87 ATOM 3695 O THRH 192 -12.317 3.26842.099 1.0015.94 ATOM 3696 N VALH 193 -10.239 3.09442.950 1.0016.81 ATOM 3698 CA VAL H 193 -9.591 2.91741.671 1.0016.97 ATOM 3699 CB VALH 193 -8.778 4.19441.194 1.0016.54 ATOM 3700 CGI VAL H 193 -7.944 3.90439.924 1.0011.61 ATOM 3701 CG2 VALH 193 -9.780 5.32640.894 1.0014.87 ATOM 3702 C VALH 193 -8.725 1.64341.776 1.0016.78 ATOM 3703 O VALH 193 -7.889 1.501 42.643 1.0014.37 ATOM 3704 N THRH 194 -9.032 0.68740.931 1.0018.51 ATOM 3706 CA THRH 194 -8.347 -0.57440.934 1.0019.26 ATOM 3707 CB THRH 194 -9.341 -1.66541.316 1.0019.05 ATOM 3708 OG1 THRH 194 -10.064 -1.24842.490 1.0022.10 ATOM 3710 CG2 THRH 194 -8.644 -2.98341.590 1.0017.95 ATOM 3711 C THRH 194 -7.867 -0.855 39.526 1.0020.35 ATOM 3712 O THRH 194 -8.574 -0.55638.558 1.0018.99 ATOM 3713 N CYS H 195 -6.671 -1.38839.397 1.0022.03 ATOM 3715 CA CYSH 195 -6.231 -1.85038.101 1.0021.55 ATOM 3716 CB CYS H 195 -4.827 -1.383 37.796 1.0022.21 ATOM 3717 SG CYS H 195 -3.518 -2.34238.560 1.0026.24 ATOM 3718 C CYS H 195 -6.308 -3.36638.063 1.0020.83 ATOM 3719 O CYSH 195 -6.010 -4.06439.046 1.0021.96 ATOM 3720 N ASN H 196 -6.718 -3.85536.927 1.0019.29 ATOM 3722 CA ASNH 196 -6.918 -5.285 36.687 1.0016.40 ATOM 3723 CB ASN H 196 -8.285 -5.44436.035 1.0016.17 ATOM 3724 CG ASNH 196 -9.245 -4.40236.544 1.0013.27 ATOM 3725 OD1 ASN H 196 -9.644 -3.47835.833 1.0020.19 ATOM 3726 ND2 ASN H 196 -9.601 -4.52937.793 1.0011.17 ATOM 3729 C ASNH 196 -5.865 -5.76235.703 1.0016.19 ATOM 3730 O ASN H 196 -5.877 -5.335 34.560 1.0013.42 ATOM 3731 N VALH 197 -4.938 -6.59436.149 1.0015.57 ATOM 3733 CA VAL H 197 -3.888 -7.06535.275 1.0014.42 ATOM 3734 CB VAL H 197 -2.508 -6.855 35.888 1.009.60 ATOM 3735 CGI VALH 197 -1.452 -7.39434.943 1.007.11 ATOM 3736 CG2 VALH 197 -2.269 -5.38236.162 1.0012.01 ATOM 3737 C VALH 197 -4.036 -8.543 34.954 1.0016.35 ATOM 3738 O VAL H 197 -4.130 -9.37035.872 1.0014.56 ATOM 3739 N ALAH 198 -4.039 -8.871 33.646 1.0017.13 ATOM 3741 CA ALAH 198 -4.125-10.26733.222 1.0016.34 ATOM 3742 CB ALAH 198 -5.306-10.47032.319 1.0017.48 ATOM 3743 C ALAH 198 -2.866-10.68032.506 1.0018.98 ATOM 3744 O ALAH 198 -2.326 -9.92831.688 1.0018.73 ATOM 3745 N HIS H 199 -2.355-11.85032.864 1.0018.76 ATOM 3747 CA HIS H 199 -1.185-12.41032.209 1.0017.07 ATOM 3748 CB HIS H 199 -0.031-12.50733.168 1.008.69 ATOM 3749 CG HISH 199 1.221-12.95832.491 1.0013.16 ATOM 3750 CD2 HIS HI 99 1.798-12.59431.293 1.0011.24 ATOM 3751 ND1 HISH 199 2.094-13.865 33.052 1.0012.67 ATOM 3753 CE1 HISH 199 3.159-14.05432.275 1.0015.05 ATOM 3754 NE2 HIS H 199 2.979-13.293 31.211 1.009.04 ATOM 3756 C HISH 199 -1.561-13.80431.708 1.0020.77 ATOM 3757 O HISH 199 -1.319-14.821 32.406 1.0022.61 ATOM 3758 N PROH 200 -2.194-13.86530.504 1.0023.38 ATOM 3759 CD PRO H 200 -2.490-12.70829.606 1.0023.82 ATOM 3760 CA PROH 200 -2.642-15.11829.886 1.0022.74 ATOM 3761 CB PROH 200 -2.776-14.74228.420 1.0023.09 ATOM 3762 CG PRO H 200 -3.296-13.34428.504 1.0023.84 ATOM 3763 C PROH 200 -1.680-16.26730.112 1.0022.03 ATOM 3764 O PROH 200 -2.105-17.30630.542 1.0025.71 ATOM 3765 N ALAH 201 -0.392-16.05929.881 1.0021.74 ATOM 3767 CA ALAH 201 0.595-17.135 30.006 1.0022.02 ATOM 3768 CB ALAH 201 1.975-16.601 29.722 1.0021.34 ATOM 3769 C ALAH 201 0.587-17.84031.379 1.0025.49 ATOM 3770 O ALAH 201 0.600-19.08631.456 1.0027.00 ATOM 3771 N SERH 202 0.590-17.05632.458 1.0023.97 ATOM 3773 CA SERH202 0.551-17.62033.806 1.0023.02 ATOM 3774 CB SERH 202 1.084-16.58034.768 1.0020.89 ATOM 3775 OG SERH 202 0.362-15.375 34.574 1.0022.36 ATOM 3777 C SERH 202 -0.886-17.95034.191 1.0022.44 ATOM 3778 O SERH 202 -1.162-18.40635.288 1.0024.26 ATOM 3779 N ALA H 203 -1.795-17.69833.281 1.0023.52 ATOM 3781 CA ALA H 203 -3.211-17.83433.554 1.0024.82 ATOM 3782 CB ALAH 203 -3.592-19.31233.629 1.0025.98 ATOM 3783 C ALAH 203 -3.609-17.06234.843 1.0028.71 ATOM 3784 O ALAH 203 -4.389-17.541 35.682 1.0033.42 ATOM 3785 N THRH204 -3.105-15.84435.003 1.0027.17 ATOM 3787 CA THRH 204 -3.456-15.06936.191 1.0027.24 ATOM 3788 CB THRH 204 -2.236-14.71836.997 1.0026.73 ATOM 3789 OG1 THRH 204 -1.363-13.91436.205 1.0029.32 ATOM 3791 CG2THRH204 -1.511-15.983 37.415 1.0030.85 ATOM 3792 C THRH 204 -4.184-13.77435.844 1.0028.10 ATOM 3793 O THRH 204 -4.013-13.205 34.749 1.0027.08 ATOM 3794 N LYSH 205 -4.988-13.32536.796 1.0029.70 ATOM 3796 CA LYSH 205 -5.789-12.10736.657 1.0029.70 ATOM 3797 CB LYS H 205 -7.157-12.46536.050 1.0026.59 ATOM 3798 CG LYS H 205 -8.091 -11.30435.756 1.0030.12 ATOM 3799 CD LYS H 205 -7.386-10.115 35.126 1.0032.29 ATOM 3800 CE LYS H 205 -8.357 -9.001 34.726 1.0028.46 ATOM 3801 NZ LYS H 205 -9.140 -9.32933.482 1.0032.30 ATOM 3805 C LYS H 205 -5.905-11.46838.047 1.0029.50 ATOM 3806 O LYSH 205 -6.666-11.93738.903 1.0029.82 ATOM 3807 N VALH 206 -5.086-10.42738.273 1.0027.91 ATOM 3809 CA VALH 206 -5.028 -9.77739.556 1.0027.55 ATOM 3810 CB VALH 206 -3.558 -9.75240.106 1.0027.51 ATOM 3811 CGI VALH 206 -2.894-11.10239.902 1.0029.90 ATOM 3812 CG2 VAL H 206 -2.746 -8.64739.462 1.0025.31 ATOM 3813 C VALH 206 -5.608 -8.34939.561 1.0026.86 ATOM 3814 O VALH 206 -5.512 -7.615 38.590 1.0025.39 ATOM 3815 N ASPH 207 -6.237 -7.99640.683 1.0027.63 ATOM 3817 CA ASPH 207 -6.741 -6.65040.923 1.0025.50 ATOM 3818 CB ASPH 207 -8.170 -6.68741.430 1.0028.55 ATOM 3819 CG ASPH 207 -9.155 -6.93740.330 1.0029.54 ATOM 3820 OD1 ASPH 207 -8.722 -7.00739.163 1.0036.07 ATOM 3821 OD2 ASP H 207 -10.359 -7.06440.621 1.0032.67 ATOM 3822 C ASPH 207 -5.917 -6.00441.988 1.0024.44 ATOM 3823 O ASPH 207 -5.558 -6.68242.958 1.0023.66 ATOM 3824 N ALAH 208 -5.604 -4.711 41.808 1.0021.43 ATOM 3826 CA ALAH 208 -4.900 -3.94942.830 1.0017.91 ATOM 3827 CB ALAH 208 -3.418 -3.791 42.505 1.0020.11 ATOM 3828 C ALAH 208 -5.549 -2.57743.033 1.0016.62 ATOM 3829 O ALAH 208 -5.643 -1.75442.093 1.0010.62 ATOM 3830 N LYSH 209 -6.048 -2.36044.266 1.0016.90 ATOM 3832 CA LYSH 209 -6.670 -1.07744.630 1.0015.48 ATOM 3833 CB LYS H 209 -7.658 -1.22345.807 1.0010.13 ATOM 3834 CG LYS H 209 -8.246 0.11046.1950.5010.96 ATOM 3835 CD LYS H 209 -9.147 -0.01547.4000.5014.26 ATOM 3836 CE LYS H 209 -9.549 1.35247.9080.5012.83 ATOM 3837 NZ LYS H 209 -10.556 1.24248.9900.5014.36 ATOM 3841 C LYS H 209 -5.614 -0.01044.948 1.0012.92 ATOM 3842 O LYSH 209 -4.631 -0.26645.641 1.0010.83 ATOM 3843 N ILEH 210 -5.785 1.17844.388 1.0012.54 ATOM 3845 CA ILEH 210 -4.840 2.24944.672 1.0014.57 ATOM 3846 CB ILEH 210 -4.665 3.261 43.478 .0010.03 ATOM 3847 CG2 ILEH 210 -3.416 4.06643.683 1.009.58 ATOM 3848 CGI ILEH 210 -4.626 2.54442.096 1.0011.38 ATOM 3849 CD ILEH 210 -3.475 1.591 41.874 1.009.16 ATOM 3850 C ILEH 210 -5.370 2. 97245.914 1.0016.98 ATOM 3851 O ILEH 210 -6.520 3.46245.931 1.0018.38 ATOM 3852 N VALH 211 -4.544 2.94546.936 1.0019.13 ATOM 3854 CA VALH 211 -4.827 3.52448.248 1.0020.34 ATOM 3855 CB VALH 211 -4.668 2.41249.313 1.0021.28 ATOM 3856 CGI VALH 211 -4.884 2.97250.722 1.0025.89 ATOM 3857 CG2 VALH 211 -5.624 1.26849.025 1.0018.88 ATOM 3858 C VALH 211 -3.794 4.62848.528 1.0019.87 ATOM 3859 O VALH 211 -2.612 4.46748.205 1.0020.58 ATOM 3860 N PROH 212 -4.185 5.76449.138 1.0021.21 ATOM 3861 CD PROH 212 -5.552 6.10849.602 1.0018.81 ATOM 3862 CA PROH 212 -3.239 6.87949.416 1.0020.72 ATOM 3863 CB PROH 212 -4.124 7.92450.083 1.0018.51 ATOM 3864 CG PROH 212 -5.473 7.60849.550 1.0018.18 ATOM 3865 C PROH 212 -2.105 6.45450.335 1.0023.63 ATOM 3866 O PROH 212 -2.305 5.56951.173 1.0027.07 ATOM 3867 N ARGH 213 -0.907 7.05050.156 1.0024.57 ATOM 3869 CA ARGH 213 0.202 6.76851.064 1.0026.72 ATOM 3870 CB ARGH 213 1.594 6.82050.368 1.0027.15 ATOM 3871 CG ARGH 213 1.881 7.96449.394 1.0033.85 ATOM 3872 CD ARGH 213 3.294 7.83348.788 1.0033.12 ATOM 3873 NE ARGH 213 3.507 6.48848.238 1.0040.88 ATOM 3875 CZ ARGH 213 4.598 5.71348.492 1.0040.65 ATOM 3876 NH1 ARGH 213 4.653 4.47947.981 1.0039.58 ATOM 3879 NH2 ARGH 213 5.635 6.171 49.213 1.0037.54 ATOM 3882 C ARGH 213 0.157 7.70052.274 1.0027.92 ATOM 3883 OT1 ARGH 213 0.571 7.25753.377 1.0031.74 ATOM 3884 OT2 ARGH 213 -0.333 8.846 52.120 1.0029.09 ATOM 3885 CB ALAP 2 31.230 -8.005 -6.156 1.0023.82 ATOM 3886 C ALAP 2 29.841 5.882 -6.164 1.0018.78 ATOM 3887 O ALAP 2 29.790 -5.466 -5.014 1.0018.94 ATOM 3890 N ALAP 2 32.320 -5.788 -6.175 1.0024.56 ATOM 3892 CA ALAP 2 31.130 6.567 -6.663 1.0020.94 ATOM 3893 N ALAP 3 28.823 -5.793 -7.033 1.0015.73 ATOM 3895 CA ALAP 3 27.589 -5.071 -6.738 1.0014.42 ATOM 3896 CB ALAP 3 27.052 -4.456 -8.026 1.0013.90 ATOM 3897 C ALAP 3 26.482 -5.937 -6.142 1.0014.34 ATOM 3898 O ALAP 3 26.488 -7.186 -6.247 1.0012.83 ATOM 3899 N PROP 4 25.526 -5.262 -5.467 1.0012.41 ATOM 3900 CD PROP 4 25.574 -3.831 -5.096 1.0010.70 ATOM 3901 CA PROP 4 24.357 -5.901 -4.882 1.009.09 ATOM 3902 CB PROP 4 23.878 -4.858 -3.887 1.0010.23 ATOM 3903 CG PROP 4 24.156 -3.611 -4.622 1.0010.28 ATOM 3904 C PROP 4 23.348 6.156 -6.006 1.008.50 ATOM 3905 O PROP 4 23.721 -6.099 -7.155 1.0012.29 ATOM 3906 N ASPP 5 22.112 -6.430 -5.714 1.003.44 ATOM 3908 CA ASPP 5 21.183 -6.689 -6.752 1.006.24 ATOM 3909 CB ASPP 5 19.985 -7.497 -6.235 1.004.87 ATOM 3910 CG ASPP 5 18.944 -7.827 -7.325 1.00 8.73 ATOM 3911 OD1 ASPP 5 19.267 -7.802 -8.566 1.005.17 ATOM 3912 OD2 ASP P 5 17.791 -8.100 -6.961 1.006.00 ATOM 3913 C ASPP 5 20.723 -5.380 -7.397 1.0011.49 ATOM 3914 O ASPP 5 19.844 -4.711 -6.901 1.0013.66 ATOM 3915 N THRP 6 21.312 -5.037 -8.536 1.0013.74 ATOM 3917 CA THRP 6 20.982 -3.798 -9.202 1.0013.90 ATOM 3918 CB THRP 6 22.265 -3.139 -9.756 1.0013.32 ATOM 3919 OG1THRP 6 22.906 -3.998-10.711 1.0019.82 ATOM 3921 CG2THRP 6 23.249 -2.904 -8.618 1.0017.80 ATOM 3922 C THRP 6 19.950 -3.963-10.307 1.0013.91 ATOM 3923 O THRP 6 19.797 -3.065-11.140 1.0016.59 ATOM 3924 N ARGP 7 19.218 -5.085-10.346 1.0012.22 ATOM 3926 CA ARGP 7 18.215 -5.219-11.389 1.0012.33 ATOM 3927 CB ARGP 7 17.668 -6.648-11.528 1.0011.79 ATOM 3928 CG ARGP 7 16.434 -6.709-12.418 1.0014.75 ATOM 3929 CD ARGP 7 15.734 -8.048-12.427 1.0018.52 ATOM 3930 NE ARGP 7 16.524 -9.011 -13.140 1.0027.19 ATOM 3932 CZ ARGP 7 16.088 -9.705-14.179 1.0026.31 ATOM 3933 NH1 ARG P 16.917-10.544-14.764 1.0031.37 ATOM 3936 NH2 ARG P 14.850 -9.578-14.628 1.0025.93 ATOM 3939 C ARGP 17.075 -4.264-11.100 1.0015.83 ATOM 3940 O ARGP 16.766 -4.007 -9.921 1.0015.84 ATOM 3941 N PROP ! 16.456 -3.660-12.161 1.0015.86 ATOM 3942 CD PROP 16.842 -3.743-13.611 1.0015.67 ATOM 3943 CA PROP 8 15.351 -2.743-11.991 1.0011.60 ATOM 3944 CB PROP 8 15.111 -2.160-13.407 1.0016.26 ATOM 3945 CG PROP 8 16.425 -2.376-14.102 1.0012.50 ATOM 3946 C PROP 8 14.108 - 3.457-11.438 1.0015.08 ATOM 3947 O PROP 8 13.722 - 4.583 -11.855 1.007.39 ATOM 3948 N ALAP 9 13.531 ■ -2.772-10.458 1.0014.65 ATOM 3950 CA ALAP 9 12.334 -3.191 -9.773 1.0016.28 ATOM 3951 CB ALAP 9 12.055 -2.157 -8.654 1.0013.79 ATOM 3952 C ALAP 9 11.159 - -3.193-10.733 1.0017.17 ATOM 3953 O ALAP 9 11.212 -2.524-11.754 1.0019.75 ATOM 3954 N PROP 10 10.139 -4.010-10.493 1.0017.47 ATOM 3955 CD PROP 10 10.126 -5.169 -9.587 1.0017.04 ATOM 3956 CA PRO P 10 8.958 -3.975-11.315 1.0020.33 ATOM 3957 CB PROP 10 8.080 -5.081 -10.728 1.0014.66 ATOM 3958 CG PROP 10 8.673 -5.374 -9.408 1.0018.16 ATOM 3959 C PROP 10 8.307 -2.555-11.248 1.0023.98 ATOM 3960 OT1PROP 10 8.684 -1.768-10.339 1.0029.12 ATOM 3961 OT2PROP 10 7.456 -2.226-12.120 1.0032.81 ATOM 3962 OH2 WAT W 6.426 14.867 -4.480 1.0014.28 ATOM 3965 OH2 WAT W 17.532-23.833 -4.169 1.0021.81 ATOM 3968 OH2 WAT W 18.622 4.07058.161 1.006.32 ATOM 3971 OH2 WAT W 25.532 3.202 -6.059 1.0013.58 ATOM 3974 OH2 WAT W 16.979 -5.181 -7.499 1.0013.00 ATOM 3977 OH2 WAT W 24.971-23.001 6.210 1.0030.37 ATOM 3980 OH2 WAT W 21.577-21.666 -1.335 1.003.40 ATOM 3983 OH2 WAT W 8 -3.006 - ■3.287 28.222 11.00 30.92 ATOM 3986 OH2 WAT W 9 28.986 - 1 1.555 3.882 1.00 9.44 ATOM 3989 OH2 WAT W 10 - 1.960 1 1.31 1 49.070 1.00 32.00 ATOM 3992 OH2 WAT W 1 1 8.423 - 21.487 8.622 1.00 13.78 ATOM 3995 OH2 WAT W 12 13.684 27.060 30.432 1.00 39.32 ATOM 3998 OH2 WAT W 13 3.579 4.654 44.81 1 1.00 13.19 ATOM 4001 OH2 WAT W 14 1.208 15.938 14.282 1.00 22.53 ATOM 4004 OH2 WAT W 15 12.850 -17.174 34.625 1.00 19.15 ATOM 4007 OH2 WAT W 16 10.906 -8.230 -12.637 1.00 21.26 ATOM 4010 OH2 WAT W 17 8.121 - 14.509 21.168 1.00 37.92 ATOM 4013 OH2 WAT W 18 21.322 7.473 14.563 1.00 18.86 ATOM 4016 OH2 WAT W 19 -1.612 1.908 47.043 1.00 15.06 ATOM 4019 OH2 WAT W 20 16.800 9.409 27.271 1.00 14.21 ATOM 4022 OH2 WAT W 21 20.637 12.454 -7.154 1.00 16.36 ATOM 4025 OH2 WAT W 22 7.902 - 12.529 25.324 1.00 10.64 ATOM 4028 OH2 WAT W 23 -3.580 16.239 24.865 1.00 33.41 ATOM 4031 OH2 WAT W 24 33.184 3.198 45.354 1.00 8.24 ATOM 4034 OH2 WAT W 25 -12.001 -7.854 37.177 1.00 26.57 ATOM 4037 OH2 WAT W 26 25.811 12.550 -5.985 1.00 21.74 ATOM 4040 OH2 WAT W 27 -2.669 4.036 26.084 1.00 17.07 ATOM 4043 OH2 WAT W 28 7.584 17.991 41.795 1.00 22.01 ATOM 4046 OH2 WAT W 29 23.880 -14.784 24.981 1.00 8.54 ATOM 4049 OH2 WAT W 30 31.343 -2.339 -1.788 1.00 19.31 ATOM 4052 OH2 WAT W 31 17.604 7.877 16.208 1.00 28.03 ATOM 4055 OH2 WAT W 32 6.000 - 12.613 39.963 1.00 20.30 ATOM 4058 OH2 WAT W 33 5.465 -1.162 17.848 1.00 34.15 ATOM 4061 OH2 WAT W 34 1 1.035 -16.416 36.570 1.00 16.42 ATOM 4064 OH2 WAT W 35 6.472 - 14.869 -8.218 1.00 16.12 ATOM 4067 OH2 WAT W 36 9.170 0.957 -2.297 1 1.00 22.74 ATOM 4070 OH2 WAT W 37 4.454 -4.651 10.416 1.00 20.60 ATOM 4073 OH2 WAT W 38 20.460 -25.521 7.764 1.00 26.25 ATOM 4076 OH2 WAT W 39 7.681 -2.544 1.721 1 LOO 13.86 ATOM 4079 OH2 WAT W 40 21.029 -25.146 -8.372 1.00 17.33 ATOM 4082 OH2 WAT W 41 14.028 -12.601 28.828 1.00 15.39 ATOM 4085 OH2 WAT W 42 25.022 -8.547 16.118 1.00 16.92 ATOM 4088 OH2 WAT W 43 18.057 -3.215 49.932 1.00 25.44 ATOM 4091 OH2 WAT W 44 8.711 - 22.401 12.910 1.00 22.95 ATOM 4094 OH2 WAT W 45 12.338 -7.514 37.880 1.00 26.88 ATOM 4097 OH2 WAT W 46 3.271 - •16.775 -4.316 1.00 19.56 ATOM 4100 OH2 WAT W 47 0.541 0.196 50.275 1.00 30.33 ATOM 4103 OH2 WAT W 48 19.1 10 -25.008 2.771 1.00 5.88 ATOM 4106 OH2 WAT W 49 19.857 5.736 -10.627 1.00 15.25 ATOM 4109 OH2 WAT W 50 27.580 -18.786 1.731 1.00 12.48 ATOM 41 12 OH2 WAT W 51 18.435 -0.552 -10.469 1.00 26.95 ATOM 41 15 OH2 WAT W 52 14.333 -24.451 3.097 1.00 21.65 ATOM 41 18 OH2 WAT W 53 15.425 -11.850 25.550 1.00 19.62 ATOM 4121 OH2 WAT W 54 7.024 -3.615 7.466 1.00 10.22 ATOM 4124 OH2 WAT W 55 8.753 - ■20.576 29.006 1.00 24.86 ATOM 4127 OH2 WAT W 56 7.171 14.326 47.574 1.00 38.64 ATOM 4130 OH2 WAT W 57 27.936 -19.870 -6.755 1.00 5.62 ATOM 4133 OH2 WAT W 58 25.912 -19.577 7.753 1.00 10.53 ATOM 4136 OH2 WAT W 59 21.018 -23.427 -10.452 '. 1.00 13.82 ATOM 4139 OH2 WAT W 60 27.633 -1.667 12.559 1.00 16.07 ATOM 4142 OH2 WAT W 61 4.313 ■ ■13.120 12.150 1.00 29.58 ATOM 4145 OH2 WAT W 62 10.813 -25.473 15.402 : 1.00 30.70 ATOM 4148 OH2 WAT W 63 16.114 5.482 14.710 1.00 33.54 ATOM 4151 OH2 WAT W 64 18.745 -2.391 28.646 1.00 29.04 ATOM 4154 OH2 WAT W 65 1 1.904 1.212 24.223 1.00 27.66 ATOM 4157 OH2 WAT W 66 20.618 0.166 12.936 1.00 13.20 ATOM 4160 OH2 WAT W 67 2.553 2.198 49.034 1.00 25.99 ATOM 4163 OH2 WAT W 68 18.383 -9.766 -9.807 1.00 8.99 ATOM 4166 OH2 WAT W 69 12.289 -2.356 38.708 1.00 18.95 ATOM 4169 OH2 WAT W 70 28.530 -9.247 -6.290 1.00 15.87 ATOM 4172 OH2 WAT W 71 7.140 2.348 42.142 1.00 24.77 ATOM 4175 OH2 WAT W 72 5.506 -6.185 1.158 1.00 25.37 ATOM 4178 OH2 WAT W 73 27.109 -2.182 -10.612 1.00 35.24 ATOM 4181 OH2 WAT W 74 23.698 -4.681 9.146 1.00 10.39 ATOM 4184 OH2 WAT W 75 21.899 -8.055 -10.315 1.00 19.23 ATOM 4187 OH2 WAT W 76 9.190 21.320 27.616 1.00 22.97 ATOM 4190 OH2 WAT W 77 -1.064 9.065 47.775 1.00 17.17 ATOM 4193 OH2 WAT W 78 23.562 -2.845 10.941 1.00 11.39 ATOM 4196 OH2 WAT W 79 14.925 -18.028 -13.375 1.00 38.75 ATOM 4199 OH2 WAT W 80 18.839 -22.015 -1.607 1.00 16.43 ATOM 4202 OH2 WAT W 81 6.261 9.572 3.405 1.00 10.35 ATOM 4205 OH2 WAT W 82 8.820 -8.947 40.170 1.00 19.41 ATOM 4208 OH2 WAT W 83 14.036 26.574 5.609 1.00 30.50 ATOM 4211 OH2 WAT W 84 14.876 15.952 -3.144 1.00 14.73 ATOM 4214 OH2 WAT W 85 22.298 -12.049 -10.100 1.00 12.02 ATOM 4217 OH2 WAT W 86 1 1.954 -24.973 2.713 1.00 17.04 ATOM 4220 OH2 WAT W 87 14.498 -25.610 19.360 1.00 12.97 ATOM 4223 OH2 WAT W 88 26.234 0.908 12.149 1.00 14.84 ATOM 4226 OH2 WAT W 89 3.924 18.064 34.080 1 1..0000 1144..9922 ATOM 4229 OH2 WAT W 90 2.892 ■ ■12.720 -0.149 11..0000 3300..3355 ATOM 4232 OH2 WAT W 91 21.001 -0.118 -7.935 11..0000 1111..4455 ATOM 4235 OH2 WAT W 92 1 177..773355 4.125 55.330 11..0000 2233..0033 ATOM 4238 OH2 WAT W 93 3300..990099 -19.022 0.239 11..0000 1188..1122 ATOM 4241 OH2 WAT W 94 8 8..223344 0.633 -1 1.962 11..0000 3355..8877 ATOM 4244 OH2 WAT W 95 --00..113366 11.812 40.540 11..0000 1199..0099 ATOM 4247 OH2 WAT W 96 2255..448855 1 1.712 48.976 11..0000 3399..9933 ATOM 4250 OH2 WAT W 97 1133..443300 9.938 61.213 11..0000 1177..4488 ATOM 4253 OH2 WAT W 98 3311..770000 7.812 -5.575 11..0000 1199..5588 ATOM 4256 OH2 WAT W 99 15.210 0.308 35.919 1.00 1 1.83 ATOM 4259 OH2 WAT W 100 -5.288 -15.339 38.902 1.00 16.58 ATOM 4262 OH2 WAT W 101 1.823 -1.479 48.170 1.00 29.29 ATOM 4265 OH2 WAT W 102 -10.016 4.695 47.612 1.00 27.17 ATOM 4268 OH2 WAT W 103 6.921 1.076 30.534 1.00 21.69 ATOM 4271 OH2 WAT W 104 20.055 0.656 43.920 1.00 28.97 ATOM 4274 OH2 WAT W 105 6.463 6.212 15.982 1.00 21.65 ATOM 4277 OH2 WAT W 106 13.122 23.767 -4.210 1.00 9.47 ATOM 4280 OH2 WAT W 107 -9.026 -5.522 44.747 1.00 32.78 ATOM 4283 OH2 WAT W 108 29.646 -16.41 1 0.821 1.00 23.02 ATOM 4286 OH2 WAT W 109 1.361 12.084 -0.538 1.00 27.33 ATOM 4289 OH2 WAT W HO 32.303 10.466 -1.708 1.00 22.13 ATOM 4292 OH2 WAT W i l l 28.782 -8.621 8.705 1.00 16.73 ATOM 4295 OH2 WAT W 112 24.255 5.940-10.096 1.00 17.97 ATOM 4298 OH2 WAT W 113 13.049 -12.03926.267 1.00 17.02 ATOM 4301 OH2 WAT W 1 14 23.675 -12.526 16.932 1.00 18.85 ATOM 4304 OH2 WAT W 115 28.157 2.239-10.357 1.00 57.76 ATOM 4307 OH2 WAT W 1 16 16.617 -26.364 6.730 1.00 14.43 ATOM 4310 OH2 WAT W 117 25.797 11.257 9.549 1.00 20.54 ATOM 4313 OH2 WAT W 118 32.533 10.022 -4.580 1.00 28.60 ATOM 4316 OH2 WAT W 1 19 32.447 4.104 -6.869 1.00 45.04 ATOM 4319 OH2 WAT W 120 -1 1.651 12.202 46.743 1.00 24.53 ATOM 4322 OH2 WAT W 121 2.087 • ■13.590 -7.699 1.00 34.84 ATOM 4325 OH2 WAT W 122 5.697 -8.611 46.172 1.00 13.18 ATOM 4328 OH2 WAT W 123 15.700 -9.174 24.055 1.00 30.63 ATOM 4331 OH2 WAT W 124 27.694 -17.178 14.423 1.00 14.55 ATOM 4334 OH2 WAT W 125 -17.440 6.655 48.327 1.00 17.20 ATOM 4337 OH2 WAT W 126 23.385 -13.61 1 22.762 1.00 26.67 ATOM 4340 OH2 WAT W 127 17.644 1.422 26.967 1.00 47.02 ATOM 4343 OH2 WAT W 128 14.055 5.694 21.684 1.00 23.91 ATOM 4346 OH2 WAT W 129 -9.680 0.519 31.262 1.00 16.36 ATOM 4349 OH2 WAT W 130 5.299 -6.710 -15.375 1.00 38.16 ATOM 4352 OH2 WAT W 131 31.933 8.550 5.211 1.00 13.75 ATOM 4355 OH2 WAT W 132 14.320 -2.736 27.730 1.00 27.48 ATOM 4358 OH2 WAT W 133 34.024 -3.394 1.152 1.00 28.35 ATOM 4361 OH2 WAT W 134 8.372 -8.434 - 11.747 1.00 16.01 ATOM 4364 OH2 WAT W 135 21.336 -24.763 25.455 1.00 21.80 ATOM 4367 OH2 WAT W 136 38.405 7.861 2.254 1.00 18.43 ATOM 4370 OH2 WAT W 137 7.136 11.670 49.549 1.00 16.91 ATOM 4373 OH2 WAT W 138 22.371 8.145 -1.106 1.00 3.60 ATOM 4376 OH2 WAT W 139 -0.599 13.866 38.934 1.00 53.27 ATOM 4379 OH2 WAT W 140 3.559 20.513 33.347 1.00 25.23 ATOM 4382 OH2 WAT W 141 26.012 -21.730 3.659 1.00 8.89 ATOM 4385 OH2 WAT W 142 16.747 19.742 12.697 1.00 12.58 ATOM 4388 OH2 WAT W 143 22.905 1.078 •9.223 1.00 33.61 ATOM 4391 OH2 WAT W 144 13.909 -25.966 12.927 1.00 18.24 ATOM 4394 OH2 WAT W 145 -1.880 -13.590 5.375 1.0022.46 ATOM 4397 OH2 WAT W 146 31.991 -3.241 6.307 1.00 21.74 ATOM 4400 OH2 WAT W 147 -4.296 -0.541 28.947 1.00 26.69 ATOM 4403 OH2 WAT W 148 21.118 -26.880 23.879 1.00 16.34 ATOM 4406 OH2 WAT W 149 21.937 7.882 -11.795 1.00 26.06 ATOM 4409 OH2 WAT W 150 10.669 -24.334 12.632 1.00 21.28 ATOM 4412 OH2 WAT W 151 4.579 13.840 -6.207 1.00 7.70 ATOM 4415 OH2 WATW 152 30.211 6.160 11.009 1.0016.94 ATOM 4418 OH2 WATW 153 24.991 -7.106 9.808 .0017.58 ATOM 4421 OH2 WATW 154 11.324 -3.831 36.762 1.0023.50 ATOM 4424 OH2 WATW 155 -15.285 3.50841.805 1.0035.32 ATOM 4427 OH2 WATW 156 15.119 -24.580 -4.682 1.0018.53 ATOM 4430 OH2 WATW 157 1.432 ■ -5.537 7.573 1.0023.51 ATOM 4433 OH2 WATW 158 -11.941 17.13441.007 1.0030.42 ATOM 4436 OH2 WATW 159 6.869- ■18.83228.614 1.0019.33 ATOM 4439 OH2 WATW 160 12.995 -0.64926.156 1.0021.36 ATOM 4442 OH2 WATW 161 33.416 -5.676 6.213 1.0023.60 ATOM 4445 OH2 WATW 162 14.01424.63631.376 1.0036.78 ATOM 4448 OH2 WATW 163 1.227- 14.93826.127 1.0029.62 ATOM 4451 OH2 WATW 164 24.359 -8.407 -9.667 1.0015.70 ATOM 4454 OH2 WATW 165 3.110 11.62242.033 1.0020.46 ATOM 4457 OH2 WATW 166 10.68822.835 -4.459 1.0013.45 ATOM 4460 OH2 WATW 167 -6.717 -5.18646.427 1.0031.64 ATOM 4463 OH2 WATW 168 5.512 -4.116 17.944 1.0032.66 ATOM 4466 OH2 WATW 169 -20.353 5.80345.273 1.0011.80 ATOM 4469 OH2 WATW 170 18.354 -6.705 -2.499 1.003.86 ATOM 4472 OH2 WATW 171 29.217 -15.191 3.806 1.0014.16 ATOM 4475 OH2 WATW 172 15.303 12.18754.784 1.0037.54 ATOM 4478 OH2 WATW 173 17.118 -25.005 -9.465 1.0035.04 ATOM 4481 OH2 WATW 174 8.913 -1.469 19.169 1.0036.48 ATOM 4484 OH2 WATW 175 32.173 -8.909 4.706 1.0019.69 ATOM 4487 OH2 WATW 176 28.509 -17.036 -2.194 1.005.68 ATOM 4490 OH2 WATW 177 6.008 25.018 11.066 1.0022.81 ATOM 4493 OH2 WATW 178 20.228 3.12740.490 1.0023.82 ATOM 4496 OH2 WATW 179 -0.663- -13.68240.615 1.0030.50 ATOM 4499 OH2 WATW 180 34.602 -2.615 5.839 1.0021.60 ATOM 4502 OH2 WATW 181 7.201 4.59525.466 1.0015.09 ATOM 4505 OH2 WATW 182 -4.692 11.60631.073 1.0020.86 ATOM 4508 OH2 WATW 183 21.437 -23.456 9.533 1.0031.82 ATOM 4511 OH2 WATW 184 13.849 17.69846.008 1.0021.96 ATOM 4514 OH2 WATW 185 17.169 -16.870 -12.443 1.0020.68 ATOM 4517 OH2 WATW 186 19.737 -21.287-14.670 1.0027.48 ATOM 4520 OH2 WATW 187 12.044 14.653 15.347 1.0019.96 ATOM 4523 OH2 WATW 188 5.432 -6.588 -12.779 1.0035.66 ATOM 4526 OH2 WATW 189 4.591 13.681 39.908 1.0020.33 ATOM 4529 OH2 WATW 190 21.602 5.34641.670 1.0036.13 ATOM 4532 OH2 WATW 191 29.191 -21.778 7.396 1.0020.15 ATOM 4535 OH2 WATW 192 18.030 -9.96924.699 1.0036.15 ATOM 4538 OH2 WATW 193 12.481 -28.048 4.388 1.0018.19 ATOM 4541 OH2 WATW 194 12.908 10.09721.791 1.0038.97 ATOM 4544 OH2 WATW 195 25.645 8.68249.741 1.0027.52 ATOM 4547 OH2 WATW 196 24.782 10.751 46.034 1.0010.14 ATOM 4550 OH2 WATW 197 28.043 -17.199 -7.803 1.0047.72 ATOM 4553 OH2 WATW 198 26.889 3.77548.529 1.0027.25 ATOM 4556 OH2 WATW 199 15.947 0.435 -1.489 1.0013.61 ATOM 4559 OH2 WATW 200 5.673 -3.78825.327 1.0030.04 ATOM 4562 OH2 WATW 201 23.387 6.262 13.666 1.0011.98 ATOM 4565 OH2 WAT W 202 4.263 5.267 17.454 1.0021.77 ATOM 4568 OH2 WATW 203 0.248 -9.25242.163 1.0015.59 ATOM 4571 OH2 WATW 204 25.046 2.931 -8.777 1.0019.57 ATOM 4574 OH2 WATW 205 20.186 1.205 -9.775 1.0034.32 ATOM 4577 OH2 WATW 206 -3.206 8.91232.847 1.006.08 ATOM 4580 OH2 WATW 207 16.094 -17.057 -8.819 1.0022.31 ATOM 4583 OH2 WATW 208 19.191 8.829 -10.872 1.0042.96 ATOM 4586 OH2 WATW 209 1.679 -6.92645.370 1.0037.43 ATOM 4589 OH2 WATW 210 -8.601 4.48249.821 1.0025.82 ATOM 4592 OH2 WATW 211 3.765 -7.431 27.914 1.0027.19 ATOM 4595 OH2 WATW 212 23.683 -2.641 -13.590 1.0028.44 ATOM 4598 OH2 WATW 213 29.132 12.371 -6.415 1.0038.04 ATOM 4601 OH2WATW214 23.909 -20.852 2.386 1.005.04 ATOM 4604 OH2 WATW 215 27.253 3.77737.228 1.0024.05 ATOM 4607 OH2 WATW 216 5.162 -12.163 14.867 1.0013.79 ATOM 4610 OH2 WATW 217 7.513 3.997 14.327 1.0026.14 ATOM 4613 OH2 WATW 218 20.390 10.391 8.341 1.002.00 ATOM 4616 OH2 WATW 219 17.322 -1.860 -8.500 1.0018.45 ATOM 4619 OH2 WAT W 220 6.864 18.400 -1.951 1.0018.17 ATOM 4622 OH2 WATW 221 30.509 -17.379 -8.974 1.009.31 ATOM 4625 OH2 WATW 222 1.115 13.85228.538 1.0022.20 ATOM 4628 OH2 WAT W 223 4.674 4.61524.939 1.0014.99 ATOM 463 1 OH2 WAT W 224 0.142 17.456 18.372 1.00 24.15 ATOM 4634 OH2 WAT W 225 9.859 - 27.543 -4.527 1.00 24.23 ATOM 4637 OH2 WAT W 226 17.960 7.797 29.085 1.00 26.71 ATOM 4640 OH2 WAT W 227 26.317 5.155 -2.166 1.00 7.58 ATOM 4643 OH2 WAT W 228 16.430 -0.855 25.960 1.00 51.29 ATOM 4646 OH2 WAT W 229 8.210 - 1 1.591 39.186 1.00 24.13 ATOM 4649 OH2 WAT W 230 -0.777 1 1.927 32.428 1.00 14.96 ATOM 4652 OH2 WAT W 231 10.186 -6.629 43.558 1.00 27.57 ATOM 4655 OH2 WAT W 232 0.958 9.102 32.585 1.00 24.54 ATOM 4658 OH2 WAT W 233 2.553 1 1.712 32.867 1.00 21.65 ATOM 4661 OH2 WAT W 234 6.680 ■ -0.006 43.521 1.00 10.20 ATOM 4664 OH2 WAT W 235 18.239 -24.609 5.252 1.00 1 1.95 ATOM 4667 OH2 WAT W 236 8.204 6.152 12.418 1.00 21.41 ATOM 4670 OH2 WAT W 237 23.369 13.641 49.71 1 1.00 30.08 ATOM 4673 OH2 WAT W 238 17.028 -7.732 -4.387 1.00 15.78 ATOM 4676 OH2 WAT W 239 30.807 -10.059 6.565 1.00 27.21 ATOM 4679 OH2 WAT W 240 -6.71 1 -6.520 32.290 1.00 29.81 ATOM 4682 OH2 WAT W 241 16.555 ■ -12.917 28.106 1.00 36.06 ATOM 4685 OH2 WAT W 242 12.165 . -24.551 -7.873 1.00 19.39 ATOM 4688 OH2 WAT W 243 21.126 12.813 35.206 1.00 24.60 ATOM 4691 OH2 WAT W 244 18.219 -8.460 20.415 1.00 23.62 ATOM 4694 OH2 WAT W 245 20.193 10.009 34.435 1.00 1 1.86 ATOM 4697 OH2 WAT W 246 29.732 9.455 -8.377 1.00 34.43 ATOM 4700 OH2 WAT W 247 13.170 2.121 14.946 1.00 24.74 ATOM 4703 OH2 WAT W 248 23.497 -25.395 4.299 1.00 13.44 ATOM 4706 OH2 WAT W 249 14.041 -22.771 -6.627 1.00 17.30 ATOM 4709 OH2 WAT W 250 10.31 1 0.550 16.295 1.00 41.70 ATOM 4712 OH2 WAT W 251 13.522 2.361 -9.507 1.00 20.28 ATOM 4715 OH2 WAT W 252 13.590 -26.409 -3.831 1.00 15.20 ATOM 4718 OH2 WAT W 253 24.905 10.098 -7.007 1.00 29.35 ATOM 4721 OH2 WAT W 254 13.023 -15.944 -13.638 1.00 26.25 ATOM 4724 OH2 WAT W 255 - 15.059 5.616 39.922 1.00 39.38 ATOM 4727 OH2 WAT W 256 16.372 15.953 31.052 1.00 19.01 ATOM 4730 OH2 WAT W 257 12.577 -9.193 43.694 1.00 20.05 ATOM 4733 OH2 WAT W 258 13.243 -8.179 23.993 1.00 41.00 ATOM 4736 OH2 WAT W 259 14.788 0.546 -10.706 1.00 28.58 ATOM 4739 OH2 WAT W 260 19.882 -1.770 -13.479 1.00 35.1 1 ATOM 4742 OH2 WAT W 261 31.349 -15.664 0.850 1.00 26.24 ATOM 4745 OH2 WAT W 262 14.405 -13.078 -16.126 1.00 16.37 ATOM 4748 OH2 WAT W 263 22.733 13.041 16.231 1.00 21.47 ATOM 4751 OH2 WAT W 264 16.542 21.606 39.036 1.00 26.03 ATOM 4754 OH2 WAT W 265 -6.590 -9.660 42.823 1.00 26.79 ATOM 4757 OH2 WAT W 266 32.784 6.735 -7.882 1.00 26.76 ATOM 4760 OH2 WAT W 267 7.826 14.049 16.469 1.00 18.53 ATOM 4763 OH2 WAT W 268 35.586 1.152 10.429 1.00 31.99 ATOM 4766 OH2 WAT W 269 13.273 -7.774 41.272 1.00 27.81 ATOM 4769 OH2 WAT W 270 26.613 -16.200 -10.31 1 1.00 24.35 ATOM 4772 OH2 WAT W 271 9.380 21.735 36.262 1.00 26.21 ATOM 4775 OH2 WAT W 272 2.143 -1.862 26.631 1.00 19.18 ATOM 4778 OH2 WAT W 273 4.996 - •16.490 24.247 1.00 21.38 ATOM 4781 OH2 WAT W 274 -3.681 11.524 26.326 1.00 32.16 ATOM 4784 OH2 WAT W 275 -0.488 20.208 19.551 1.00 28.61 ATOM 4787 OH2 WAT W 276 20.222 13.839 -1.397 1.00 6.13 ATOM 4790 OH2 WAT W 277 7.951 8.338 14.092 1.00 26.36 ATOM 4793 OH2 WAT W 278 -0.102 -4.099 27.252 1.00 22.58 ATOM 4796 OH2 WAT W 279 6.465 - ■12.539 22.787 1.00 39.32 ATOM 4799 OH2 WAT W 280 27.940 -9.420 1 1.870 1.00 21.31 ATOM 4802 OH2 WAT W 281 18.053 -5.607 47.195 1.00 28.13 ATOM 4805 OH2 WAT W 282 27.663 -20.337 5.833 1.00 29.05 ATOM 4808 OH2 WAT W 283 7.299 3.352 5.485 1.00 15.35 ATOM 481 1 OH2 WAT W 284 -1.957 14.568 1.632 1.00 30.36 ATOM 4814 OH2 WAT W 285 1 1.592 -3.121 17.799 1.00 19.72 ATOM 4817 OH2 WAT W 286 21.824 -21.684 1.192 1.00 14.10 ATOM 4820 OH2 WAT W 287 21.037 -6.590 -2.851 1.00 10.76 ATOM 4823 OH2 WAT W 288 15.218 0.054 17.590 1.00 23.02 ATOM 4826 OH2 WAT W 289 17.319 -6.704 54.240 1.0023.81 ATOM 4829 OH2 WAT W 290 22.151 -16.769 24.819 1.00 26.10 ATOM 4832 OH2 WAT W 291 1 1.461 -1.517 - 14.214 1.00 17.37 ATOM 4835 OH2 WAT W 292 9.524 1.11523.430 1.0018.75 ATOM 4838 OH2 WAT W 293 13.384 17.54321.896 1.0032.59 ATOM 4841 OH2 WAT W 294 26.874 -7.117 7.979 1.0019.34 ATOM 4844 OH2 WAT W 295 21.770 -13.114-13.708 1.0029.49 ATOM 4847 OH2 WAT W 296 11.447 -7.221 35.170 1.0022.34 ATOM 4850 OH2 WAT W 297 18.712 0.549 -7.664 1.0016.39 ATOM 4853 OH2 WAT W 298 -15.915 3.391 44.805 1.0037.24 ATOM 4856 OH2 WATW 299 8.370 -8.29742.696 1.0028.38 ATOM 4859 OH2 WATW 300 2.495 -9.28623.003 1.0035.16 ATOM 4862 OH2 WATW 301 22.017 -7.975 -0.795 1.006.11 ATOM 4865 OH2 WATW 302 21.946-24.501 2.086 1.008.66 ATOM 4868 OH2 WATW 303 20.054-25.320 17.657 1.009.01 ATOM 4871 OH2 WATW 304 16.993-22.098 5.024 1.005.97 ATOM 4874 OH2 WAT W 305 5.968 -7.519 14.076 1.0041.33 ATOM 4877 OH2 WAT W 306 32.836-13.233 -1.523 1.007.51 ATOM 4880 OH2 WAT W 307 -7.127 13.28328.100 1.0026.60 ATOM 4883 OH2 WATW 308 6.091-19.633 20.653 1.0034.63 ATOM 4886 OH2 WAT W 309 5.315 8.969 12.397 1.0019.78 ATOM 4889 OH2 WATW 310 12.008 2.607 52.956 1.0021.69 ATOM 4892 OH2 WAT W 311 10.006 19.903 41.503 1.0033.05 ATOM 4895 OH2WATW312 13.090-23.821-10.159 1.0036.76 ATOM 4898 OH2 WATW 313 8.580-24.171 7.883 1.0034.91 ATOM 4901 OH2WATW314 29.016 -9.885 -3.451 1.0029.41 ATOM 4904 OH2 WATW 315 14.762 -9.28446.366 1.0040.86 ATOM 4907 OH2 WATW 316 7.23626.011 3.913 1.0028.36 ATOM 4910 OH2 WATW 317 24.009 5.88639.309 1.0021.45 ATOM 4913 OH2 WATW 318 8.878 7.302 16.729 1.0036.71 ATOM 4916 OH2 WATW 319 -1.085 -7.73723.652 1.0040.27 ATOM 4919 OH2 WATW 320 22.737 3.02244.290 1.0031.90 ATOM 4922 OH2 WATW 321 11.113 -9.661 22.079 1.0038.45 ATOM 4925 OH2 WATW 322 22.328 0.316-12.103 1.0023.98 ATOM 4928 OH2 WATW 323 6.697 14.352 -9.527 1.0045.55 ATOM 4931 OH2 WATW 324 -8.008 -4.161 27.922 1.0029.83 ATOM 4934 OH2 WATW 325 1.400 17.96234.791 1.0030.61 ATOM 4937 OH2 WATW 326 19.807 10.03725.470 1.0033.30 ATOM 4940 OH2 WAT W 327 2.104 14.448 12.247 1.0037.11 ATOM 4943 OH2 WATW 328 15.269 -4.273 25.237 1.0029.17 ATOM 4946 OH2 WAT W 329 12.99728.11824.336 1.0030.90 ATOM 4949 OH2 WAT W 330 1.930 -6.05827.027 1.0018.90 ATOM 4952 OH2 WATW 331 20.207 17.49933.744 1.0041.90 ATOM 4955 CD HET I 1 -3.670 11.89728.662 1.0034.52 ATOM 4956 CD HET I 2 7.058 -2.556 18.576 1.0056.55 ATOM 4957 CD HET I 3 -18.942 6.31546.932 1.0025.08 ATOM 4958CD HETI 4 31.184-13.965 -2.378 1.0017.70 ATOM 4959 CD HETI 5 7.095 -7.647-14.341 1.0057.21 ATOM 4960 CD HETI 6 9.33821.68424.9970.7548.85 ATOM 4961 CD HETI 7 22.060 5.827-10.2700.7526.79 ATOM 4962 CD HETI 8 17.857 -0.59827.6820.7556.40 ATOM 4963 CL CHLI 1 -19.060 3.94748.046 1.0022.14 ATOM 4964 CL CHLI 2 30.936-12.255 -4.119 1.0026.88 Table 2b CRYST 1 42.196 83.729 67.23790.0093.3090.00 P21 SCALE 1 0.0236990.0000000.001366 0.00000 SCALE2 0.0000000.011943 0.000000 0.00000 SCALE3 0.0000000.0000000.014897 0.00000 ATOM 1 CB ILEL 3 31.905 -1.198 8.770 1.0022.21 ATOM 2 CG2ILEL 3 30.889 -2.301 8.558 1.0027.45 ATOM 3 CGI ILEL 3 31.377 0.099 8.176 1.0024.21 ATOM 4 CD ILEL 3 32.325 1.259 8.206 1.0025.48 ATOM 5 C ILEL 3 : 30.908 -0.419 10.822 1.0021.44 ATOM 6 O ILEL 3 29.898 -1.093 10.998 1.0020.56 ATOM 9 N ILEL 3 32.310 -2.410 10.862 1.0020.99 ATOM 11 CA ILEL 3 32.131 -1.068 10.239 1.0021.17 ATOM 12 N VALL 4 31.004 0.881 11.110 1.0020.05 ATOM 14 CA VALL 4 29.901 1.600 11.728 1.0020.43 ATOM 15 CB VALL 4 30.358 2.220 13.042 1.0017.54 ATOM 16 CGI VALL 4 29.161 2.832 13.761 1.0019.60 ATOM 17 CG2VALL 4 31.020 1.155 13.907 1.0017.28 ATOM 18 C VALL 4 29.350 2.705 10.834 1.0020.60 ATOM 19 O VALL 4 30.091 3.599 10.429 1.0020.97 ATOM 20 N VALL 5 28.037 2.646 10.593 1.0020.30 ATOM 22 CA VALL 5 27.341 3.599 9.739 1.0017.97 ATOM 23 CB VALL 5 26.378 2.823 8.824 1.0017.56 ATOM 24 CGI VALL 5 25.504 3.752 7.989 1.0016.02 ATOM 25 CG2VALL 5 27.188 1.881 7.940 1.0017.98 ATOM 26 C VALL 5 26.565 4.566 10.620 1.0018.99 ATOM 27 O VALL 5 25.672 4.143 11.342 1.0018.18 ATOM 28 N THRL 6 26.898 5.849 10.560 1.0017.10 ATOM 30 CA THRL 6 26.267 6.854 11.460 1.0016.73 ATOM 31 CB THRL 6 27.374 7.687 12.137 1.0015.12 ATOM 32 OG1THRL 6 28.157 6.832 12.966 1.0017.77 ATOM 34 CG2THRL 6 26.816 8.801 12.988 1.0020.38 ATOM 35 C THRL 6 25.290 7.797 10.746 1.0015.26 ATOM 36 O THRL 6 25.573 8.275 9.635 1.0014.60 ATOM 37 N GLNL 7 24.135 8.069 11.409 1.0014.21 ATOM 39 CA GLNL 7 23.121 9.003 10.914 1.009.76 ATOM 40 CB GLNL 7 21.856 8.252 10.519 1.008.55 ATOM 41 CG GLNL 7 22.020 7.230 9.405 1.003.66 ATOM 42 CD GLN L 7 20.712 6.612 9.060 1.004.16 ATOM 43 OE1 GLN L 7 20.484 5.461 9.343 1.0010.06 ATOM 44 NE2GLNL 7 19.805 7.378 8.473 1.002.55 ATOM 47 C GLN L 7 22.787 9.986 12.037 1.0012.95 ATOM 48 O GLNL 7 23.200 9.764 13.175 1.0012.95 ATOM 49 N GLUL 8 22.072 11.070 11.713 1.0014.59 ATOM 51 CA GLUL 8 21.644 12.044 12.720 1.009.44 ATOM 52 CB GLUL 8 21.124 13.317 12.081 1.003.83 ATOM 53 CG GLUL 8 22.179 14.142 11.390 1.008.12 ATOM 54 CD GLUL 8 22.261 13.874 9.885 1.0012.60 ATOM 55 OE1 GLU L 8 21.670 12.870 9.432 1.008.76 ATOM 56 OE2GLUL 8 22.936 14.667 9.156 1.0012.58 ATOM 57 C GLUL 8 20.520 11.439 13.522 1.009.97 ATOM 58 O GLUL 8 19.634 10.812 12.954 1.0010.41 ATOM 59 N SERL 9 20.478 11.677 14.833 1.0011.56 ATOM 61 CA SERL 9 19.438 11.043 15.608 1.008.58 ATOM 62 CB SERL 9 19.742 11.078 17.117 1.0014.23 ATOM 63 OG SERL 9 20.274 12.318 17.522 1.0021.30 ATOM 65 C SERL 9 18.090 11.570 15.330 1.007.24 ATOM 66 O SERL 9 17.164 10.799 15.246 1.006.90 ATOM 67 N ALAL 10 17.922 12.864 15.189 1.006.82 ATOM 69 CA ALAL 10 16.587 13.364 14.882 1.006.68 ATOM 70 CB ALAL 10 15.774 13.542 16.158 1.009.20 ATOM 71 C ALAL 10 16.692 14.689 14.233 1.006.99 ATOM 72 O ALAL 10 17.644 15.397 14.502 1.00 8.81 ATOM 73 N LEUL 11 15.711 15.033 13.431 1.007.46 ATOM 75 CA LEUL 11 15.669 16.344 12.794 1.006.63 ATOM 76 CB LEUL 11 16.167 16.277 11.323 1.0010.52 ATOM 77 CG LEUL 11 17.504 15.576 11.023 1.0010.17 ATOM 78 CD1LEUL 11 17.757 15.548 9.520 1.008.53 ATOM 79 CD2LEUL 11 18.639 16.275 11.718 1.007.59 ATOM 80 C LEUL 11 14.217 16.796 12.773 1.005.60 ATOM 81 O LEUL 11 13.341 15.965 12.677 1.007.61 ATOM 82 N THRL 12 13.973 18.114 12.826 1.004.15 ATOM 84 CA THRL 12 12.609 18.685 12.814 1.006.68 ATOM 85 CB THRL 12 12.361 19.471 14.143 1.0010.20 ATOM 86 OG1THRL 12 12.509 18.579 15.267 1.0010.18 ATOM 88 CG2THRL 12 10.97520.098 14.149 1.004.50 ATOM 89 C THRL 12 12.461 19.702 11.663 1.009.42 ATOM 90 O THRL 12 13.361 20.537 11.422 1.0011.76 ATOM 91 N THRL 13 11.347 19.705 11.003 1.0012.34 ATOM 93 CA THRL 13 11.17920.647 9.945 1.0013.42 ATOM 94 CB THRL 13 11.70720.011 8.610 1.0015.26 ATOM 95 OG1THRL 13 11.99721.027 7.647 1.0019.73 ATOM 97 CG2THRL 13 10.696 19.059 8.027 1.0015.31 ATOM 98 C THRL 13 9.71921.052 9.816 1.0013.88 ATOM 99 O THRL 13 8.78720.272 10.151 1.0012.15 ATOM 100 N SERL 14 9.47922.283 9.368 1.008.75 ATOM 102 CA SERL 14 8.12422.660 9.114 1.0010.75 ATOM 103 CB SERL 14 7.95024.194 9.110 1.0015.90 ATOM 104 OG SERL 14 8.79824.824 10.110 1.0021.10 ATOM 106 C SERL 14 7.80222.100 7.778 1.0010.99 ATOM 107 O SERL 14 8.69721.878 6.976 1.0010.06 ATOM 108 N PROL 15 6.561 21.792 7.514 1.0011.57 ATOM 109 CD PROL 15 5.423 21.907 8.418 1.0011.51 ATOM 110 CA PROL 15 6.20221.253 6.217 1.0013.73 AT M 111 CB PROL 15 4.70320.978 6.340 1.0012.67 ATOM 112 CG PROL 15 4.26721.855 7.461 1.0013.25 ATOM 113 C PROL 15 6.55922.283 5.121 1.0015.44 ATOM 114 O PROL 15 6.623 23.473 5.418 1.0014.98 ATOM 115 N GLYL 16 6.85221.807 3.898 1.0012.73 ATOM 117 CA GLYL 16 7.18922.698 2.804 1.0011.86 ATOM 118 C GLYL 16 8.65423.047 2.741 1.0011.99 ATOM 119 O GLYL 16 9.10823.638 1.781 1.0016.69 ATOM 120 N GLUL 17 9.41222.738 3.747 1.0010.28 ATOM 122 CA GLUL 17 10.80723.015 3.671 1.008.33 ATOM 123 CB GLUL 17 11.32823.510 5.013 1.006.44 ATOM 124 CG GLUL 17 10.66924.816 5.440 1.0011.47 ATOM 125 CD GLUL 17 10.78025.884 4.351 1.005.30 ATOM 126 OE1GLUL 17 11.953 26.232 3.965 1.006.09 ATOM 127 OE2GLUL 17 9.701 26.346 3.902 1.007.10 ATOM 128 C GLUL 17 11.56021.779 3.226 1.008.34 ATOM 129 O GLUL 17 11.00620.676 3.238 1.0010.48 ATOM 130 N THRL 18 12.825 21.968 2.878 1.007.25 ATOM 132 CA THRL 18 13.67620.874 2.418 1.006.74 ATOM 133 CB THRL 18 14.56921.384 1.242 1.003.14 ATOM 134 OG1 THRL 18 13.715 21.629 0.088 1.002.24 ATOM 136 CG2THRL 18 15.70820.416 0.919 1.00 5.50 ATOM 137 C THRL 18 14.57920.429 3.555 1.005.28 ATOM 138 0 THRL 18 15.121 21.267 4.286 1.004.15 ATOM 139 N VALL 19 14.815 19.129 3.652 1.005.05 ATOM 141 CA VALL 19 15.714 18.598 4.666 1.006.85 ATOM 142 CB VALL 19 14.949 17.763 5.781 1.00 8.11 ATOM 143 CGI VALL 19 14.478 18.604 6.951 1.0012.22 ATOM 144 CG2VALL 19 13.748 17.040 5.167 1.0011.25 ATOM 145 C VALL 19 16.693 17.624 4.009 1.007.00 ATOM 146 O VALL 19 16.323 16.880 3.113 1.008.38 ATOM 147 N THRL 20 17.894 17.605 4.503 1.007.91 ATOM 149 CA THRL 20 18.852 16.632 4.094 1.0010.04 ATOM 150 CB THRL 20 20.042 17.279 3.312 1.008.38 ATOM 151 OG1 THRL 20 19.537 17.742 2.053 1.0010.18 ATOM 153 CG2THRL 20 21.179 16.295 3.071 1.007.29 ATOM 154 C THRL 20 19.360 15.859 5.320 1.0010.78 ATOM 155 O THRL 20 19.729 16.451 6.353 1.0014.77 ATOM 156 N LEUL 21 19.296 14.530 5.192 1.008.97 ATOM 158 CA LEUL 21 19.814 13.586 6.162 1.005.71 ATOM 159 CB LEUL 21 18.807 12.431 6.310 1.007.30 ATOM 160 CG LEUL 21 17.445 12.710 6.929 1.003.52 ATOM 161 CD1 LEUL 21 16.597 13.551 5.999 1.0012.30 ATOM 162 CD2LEUL 21 16.737 11.422 7.224 1.005.61 ATOM 163 C LEUL 21 21.092 13.017 5.599 1.005.00 ATOM 164 O LEUL 21 21.132 12.728 4.388 1.006.66 ATOM 165 N THRL 22 22.136 12.830 6.414 1.004.47 ATOM 167 CA THRL 22 23.353 12.205 5.913 1.008.68 ATOM 168 CB THRL 22 24.584 13.092 6.055 1.008.60 ATOM 169 OG1 THRL 22 24.895 13.288 7.446 1.0013.20 ATOM 171 CG2THRL 22 24.361 14.408 5.365 1.0012.92 ATOM 172 C THRL 22 23.656 10.817 6.538 1.0012.45 ATOM 173 O THRL 22 23.039 10.375 7.556 1.0012.78 ATOM 174 N CYSL 23 24.623 10.165 5.949 1.009.70 ATOM 176 CA CYS L 23 24.969 8.822 6.322 1.0012.79 ATOM 177 CB CYS L 23 24.119 7.903 5.457 1.0011.70 ATOM 178 SG CYSL 23 24.572 6.174 5.429 1.0014.38 ATOM 179 C CYSL 23 26.443 8.613 6.089 1.0011.83 ATOM 180 O CYSL 23 26.903 8.673 4.959 1.0013.63 ATOM 181 N ARGL 24 27.216 8.399 7.154 1.0013.74 ATOM 183 CA ARGL 24 28.651 8.235 6.975 1.0015.34 ATOM 184 CB ARGL 24 29.459 9.273 7.740 1.0017.58 ATOM 185 CG ARGL 24 29.196 9.359 9.212 1.0023.61 ATOM 186 CD ARGL 24 30.230 10.251 9.878 1.0027.66 ATOM 187 NE ARGL 24 31.602 9.792 9.607 1.0030.74 ATOM 189 CZ ARGL 24 32.571 10.611 9.1990.0128.45 ATOM 190 NH1 ARG L 24 33.788 10.139 8.9720.0128.77 ATOM 193 NH2ARGL 24 32.325 11.905 9.0150.0127.96 ATOM 196 C ARG L 24 29.134 6.869 7.335 1.0016.36 ATOM 197 O ARGL 24 28.469 6.140 8.083 1.0015.58 ATOM 198 N SERL 25 30.284 6.522 6.765 1.0014.90 ATOM 200 CA SERL 25 30.913 5.239 7.014 1.0015.33 ATOM 201 CB SERL 25 31.289 4.603 5.681 1.0020.16 ATOM 202 OG SERL 25 32.145 3.490 5.853 1.0023.32 ATOM 204 C SERL 25 32.156 5.467 7.879 1.0014.75 ATOM 205 O SERL 25 32.869 6.421 7.673 1.0016.11 ATOM 206 N SERL 26 32.385 4.616 8.864 1.0015.20 ATOM 208 CA SERL 26 33.552 4.747 9.736 1.0019.00 ATOM 209 CB SER L 26 33.376 3.841 10.960 1.0016.96 ATOM 210 OG SERL 26 33.203 2.482 10.552 1.0019.34 ATOM 212 C SERL 26 34.856 4.349 9.012 1.0019.93 ATOM 213 O SERL 26 35.939 4.489 9.559 1.0023.14 ATOM 214 N THRL 27 34.761 3.836 7.800 1.0020.53 ATOM 216 CA THRL 27 35.952 3.358 7.128 1.0019.87 ATOM 217 CB THRL 27 35.633 2.079 6.411 1.0021.22 ATOM 218 OG1 THRL 27 34.457 2.255 5.626 1.0024.06 ATOM 220 CG2 THR L 27 35.388 0.990 7.430 1.0023.05 ATOM 221 C THRL 27 36.520 4.385 6.163 1.0019.65 ATOM 222 O THRL 27 37.711 4.370 5.825 1.0020.98 ATOM 223 N GLY L 27A 35.672 5.287 5.721 1.0020.47 ATOM 225 CA GLY L 27A 36.115 6.334 4.835 1.0015.37 ATOM 226 C GLY L 27A 34.954 6.903 4.102 1.0014.56 ATOM 227 O GLY L 27A 33.832 6.766 4.539 1.0016.44 ATOM 228 N ALA L 27B 35.225 7.549 2.975 1.0014.44 ATOM 230 CA ALA L 27B 34.181 8.166 2.158 1.0013.84 ATOM 231 CB ALAL 27B 34.819 8.849 0.926 1.0010.44 ATOM 232 C ALAL 27B 33.160 7.161 1.671 1.0014.20 ATOM 233 O ALAL 27B 33.516 6.038 1.285 1.0016.84 ATOM 234 N VAL L 27C 31.911 7.559 1.666 1.0012.61 ATOM 236 CA VALL 27C 30.898 6.761 1.026 1.0014.17 ATOM 237 CB VALL 27C 29.531 7.067 1.621 1.0013.42 ATOM 238 CGI VAL L 27C 28.472 6.199 0.983 1.0014.92 ATOM 239 CG2 VAL L 27C 29.592 6.824 3.116 1.0014.29 ATOM 240 C VALL 27C 30.907 7.097 -0.478 1.0016.22 ATOM 241 O VALL 27C 30.841 8.282 -0.851 1.0016.42 ATOM 242 N THR L 28 31.067 6.061 -1.325 1.0015.73 ATOM 244 CA THRL 28 31.082 6.232 -2.803 1.0014.38 ATOM 245 CB THRL 28 32.401 5.745 -3.445 1.0012.94 ATOM 246 OG1 THRL 28 32.448 4.336 -3.415 1.0013.65 ATOM 248 CG2 THRL 28 33.606 6.278 -2.713 1.0011.90 ATOM 249 C THRL 28 29.940 5.448 -3.447 1.0012.92 ATOM 250 O THRL 28 29.134 4.821 -2.760 1.009.64 ATOM 251 N THRL 29 29.859 5.480 -4.763 1.0012.65 ATOM 253 CA THRL 29 28.776 4.795 -5.453 1.0014.40 ATOM 254 CB THRL 29 28.778 5.093 -6.972 1.0015.28 ATOM 255 OG1THRL 29 30.119 4.879 -7.479 1.0016.73 ATOM 257 CG2 THRL 29 28.322 6.530 -7.249 1.0016.74 ATOM 258 C THRL 29 28.891 3.296 -5.273 1.0014.04 ATOM 259 O THRL 29 27.922 2.566 -5.455 1.0017.19 ATOM 260 N SERL 30 30.066 2.849 -4.912 1.0014.83 ATOM 262 CA SERL 30 30.284 1.440 -4.697 1.0016.69 ATOM 263 CB SERL 30 31.769 1.177 -4.630 1.0018.52 ATOM 264 OG SERL 30 32.359 1.484 -5.874 1.0022.73 ATOM 266 C SERL 30 29.621 0.945 -3.416 1.0018.22 ATOM 267 O SERL 30 29.584 -0.237 -3.168 1.0017.69 ATOM 268 N ASNL 31 29.127 1.846 -2.590 1.0016.05 ATOM 270 CA ASNL 31 28.449 1.434 -1.355 1.0012.29 ATOM 271 CB ASN L 31 28.704 2.472 -0.271 1.009.73 ATOM 272 CG ASN L 31 30.112 2.426 0.212 1.00 5.99 ATOM 273 OD1 ASNL 31 30.847 3.384 0.091 1.009.76 ATOM 274 ND2ASNL 31 30.523 1.324 0.761 1.003.79 ATOM 277 C ASN L 31 26.972 1.276 - 1.580 1.0010.21 ATOM 278 O ASN L 31 26.222 0.938 - 0.658 1.009.59 ATOM 279 N TYRL 32 26.555 1.527 - 2.830 1.008.64 ATOM 281 CA TYRL 32 25.160 1.473 -3.217 1.007.71 ATOM 282 CB TYRL 32 24.818 0.076 -3.775 1.0011.29 ATOM 283 CG TYRL 32 25.710 -0.373 -4.931 1.0011.41 ATOM 284 CD1 TYRL 32 27.010 -0.830 -4.688 1.0014.39 ATOM 285 CE1 TYRL 32 27.859 -1.197 -5.716 1.0014.44 ATOM 286 CD2TYRL 32 25.282 -0.310 -6.262 1.0017.67 ATOM 287 CE2 TYR L 32 26.131 -0.680 -7.329 1.0011.36 ATOM 288 CZ TYRL 32 27.425 -1.114 -7.045 1.0017.13 ATOM 289 OH TYRL 32 28.323 -1.410 -8.087 1.0021.48 ATOM 291 C TYRL 32 24.203 1.855 - 2.063 1.0011.23 ATOM 292 O TYRL 32 23.269 1.105 - 1.741 1.006.50 ATOM 293 N ALA L 33 24.408 3.053 - •1.461 1.0011.42 ATOM 295 CA ALAL 33 23.576 3.476 -0.310 1.0011.19 ATOM 296 CB ALAL 33 23.873 4.918 0.090 1.0010.80 ATOM 297 C ALAL 33 22.086 3.359 - 0.549 1.0010.34 ATOM 298 O ALAL 33 21.603 3.857 ■ ■1.555 1.008.45 ATOM 299 N ASNL 34 21.357 2.711 0.404 1.007.12 ATOM 301 CA ASNL 34 19.892 2.659 0.373 1.005.84 ATOM 302 CB ASNL 34 19.358 1.247 0.571 1.003.46 ATOM 303 CG ASN L 34 19.466 0.414 -0.680 1.007.07 ATOM 304 OD1 ASNL 34 18.468 -0.071 -1.209 1.005.20 ATOM 305 ND2ASNL 34 20.684 0.244 -1.154 1.005.40 ATOM 308 C ASNL 34 19.299 3.525 1.459 1.005.10 ATOM 309 O ASNL 34 19.956 3.794 2.431 1.006.58 ATOM 310 N TRPL 35 18.064 3.959 1.259 1.005.01 ATOM 312 CA TRPL 35 17.332 4.692 2.283 1.006.70 ATOM 313 CB TRPL 35 17.171 6.216 1.946 1.007.73 ATOM 314 CG TRPL 35 18.477 6.997 1.949 1.007.11 ATOM 315 CD2TRPL 35 19.085 7.645 3.093 1.008.09 ATOM 316 CE2TRPL 35 20.339 8.113 2.703 1.005.38 ATOM 317 CE3 TRP L 35 18.678 7.870 4.430 1.0010.50 ATOM 318 CD1 TRPL 35 19.367 7.124 0.911 1.004.99 ATOM 319 NE1TRPL 35 20.473 7.778 1.362 1.006.98 ATOM 321 CZ2TRPL 35 21.221 8.799 3.589 1.005.76 ATOM 322 CZ3 TRP L 35 19.551 8.549 5.297 1.006.19 ATOM 323 CH2TRPL 35 20.810 9.005 4.874 1.003.95 ATOM 324 C TRPL 35 16.000 4.031 : 2.417 1.006.29 ATOM 325 O TRPL 35 15.325 3.778 1.405 1.006.53 ATOM 326 N VALL 36 15.672 3.703 3.666 1.005.99 ATOM 328 CA VALL 36 14.478 2.972 4.045 1.005.23 ATOM 329 CB VAL L 36 14.813 1.554 4.655 1.006.23 ATOM 330 CGI VALL 36 13.50c: i 0.851 5.082 1.002.37 ATOM 331 CG2VALL 36 15.564 1 0.684 \ 3.614 1.003.99 ATOM 332 C VAL L 36 13.691 3.768 5.084 1.004.86 ATOM 333 O VALL 36 14.248 4.303 6.022 1.007.07 ATOM 334 N GLN L 37 12.399 3.809 4.899 1.005.26 ATOM 336 CA GLNL 37 11.519 4.533 5.779 1.0010.98 ATOM 337 CB GLN L 37 10.525 5.309 4.957 1.0010.61 ATOM 338 CG GLN L 37 9.741 6.290 5.782 1.0010.14 ATOM 339 CD GLN L 37 8.607 6.827 4.999 1.00 15.44 ATOM 340 OE1 GLN L 37 7.788 6.066 4.504 1.00 18.50 ATOM 341 NE2 GLN L 37 8.549 8.139 4.859 1.00 15.77 ATOM 344 C GLN L 37 10.722 3.614 6.683 1.00 1 1.84 ATOM 345 O GLN L 37 10.126 2.656 6.21 1 1.00 15.29 ATOM 346 N GLU L 38 10.675 3.956 7.976 1.00 13.42 ATOM 348 CA GLU L 38 9.853 3.223 8.919 1.00 12.58 ATOM 349 CB GLU L 38 10.677 2.724 10.1 18 1.00 12.59 ATOM 350 CG GLU L 38 9.839 1.948 1 1.160 1.00 1 1.75 ATOM 351 CD GLU L 38 10.618 1.491 12.372 1.00 9.26 ATOM 352 OE1 GLU L 38 1 1.747 1.908 12.546 1.00 12.30 ATOM 353 OE2 GLU L 38 10.081 1 0.690 13.157 1.00 17.41 ATOM 354 C GLU L 38 8.713 4.100 9.455 1.00 14.00 ATOM 355 0 GLU L 38 8.958 5.094 10.163 1.00 12.02 ATOM 356 N LYS L 39 7.484 3.742 9.126 1.00 13.36 ATOM 358 CA LYS L 39 6.358 4.424 9.695 1.00 15.90 ATOM 359 CB LYS L 39 5.348 4.743 8.626 1.00 14.39 ATOM 360 CG LYS L 39 5.777 5.942 7.806 1.00 15.78 ATOM 361 CD LYS L 39 4.645 6.445 6.935 1.00 22.14 ATOM 362 CE LYS L 39 5.167 7.426 5.888 1.00 25.73 ATOM 363 NZ LYS L 39 4.104 7.912 4.945 1.00 27.82 ATOM 367 C LYS L 39 5.728 3.607 10.852 1.00 20.86 ATOM 368 O LYS L 39 5.778 2.341 10.896 1.00 18.39 ATOM 369 N PRO L 40 5.134 4.308 1 1.828 1.00 25.47 ATOM 370 CD PRO L 40 4.954 5.763 11.895 1.00 28.62 ATOM 371 CA PRO L 40 4.505 3.681 12.975 1.00 28.32 ATOM 372 CB PRO L 40 3.543 4.770 13.526 1.00 28.73 ATOM 373 CG PRO L 40 3.563 5.834 12.480 1.00 30.27 ATOM 374 C PRO L 40 3.804 2.365 12.616 1.00 28.70 ATOM 375 O PRO L 40 2.930 2.301 1 1.709 1.00 25.53 ATOM 376 N ALA L 41 4.290 1.328 13.333 1.00 30.46 ATOM 378 CA ALA L 41 3.831 -0.059 13.244 1.00 28.13 ATOM 379 CB ALA L 41 2.435 -0.174 12.622 1.00 29.92 ATOM 380 C ALA L 41 4.819 -0.905 12.481 1.00 24.45 ATOM 381 O ALA L 41 4.434 -1.889 1 1.871 1.00 26.51 ATOM 382 N HIS L 42 6.101 -ι 0.531 12.505 1.00 22.07 ATOM 384 CA HIS L 42 7.107 -1.346 11.839 1.00 20.06 ATOM 385 CB HIS L 42 7.123 ■ -2.746 12.437 1.00 20.43 ATOM 386 CG HIS L 42 7.624 -2.738 13.806 1.00 17.71 ATOM 387 CD2 HIS L 42 6.999 -2.731 15.013 1.00 17.56 ATOM 388 ND1 HIS L 42 8.945 -2.550 14.068 1.00 21.55 ATOM 390 CE1 HIS L 42 9.186 -2.412 15.347 1.00 19.46 ATOM 391 NE2 HIS L 42 8.025 -2.519 15.929 1.00 17.49 ATOM 393 C HIS L 42 6.823 - 1.474 10.366 1.00 21.88 ATOM 394 O HIS L 42 6.999 - 2.549 9.799 1.00 22.22 ATOM 395 N LEU L 43 6.326 -0.408 9.750 1.00 20.03 ATOM 397 CA LEU L 43 6.057 -0.452 8.337 1.00 20.01 ATOM 398 CB LEU L 43 4.844 0.394 8.018 1.00 24.58 ATOM 399 CG LEU L 43 3.587 0.058 8.828 1.00 27.32 ATOM 400 CD1 LEU L 43 2.565 i 1.181 8.678 1.00 26.38 ATOM 401 CD2 LEU L 43 3.027 ' -1.328 8.423 1.00 24.37 ATOM 402 C LEU L 43 7.264 0.087 7.623 1.00 18.27 ATOM 403 O LEU L 43 7.576 1.266 7.750 1.00 18.64 ATOM 404 N PHE L 44 7.966 -0.785 6.919 1.00 17.14 ATOM 406 CA PHE L 44 9.184 -0.395 6.237 1.00 13.89 ATOM 407 CB PHE L 44 10.265 -1.388 6.547 1.00 10.76 ATOM 408 CG PHEL 44 10.846 -1.269 7.917 1.008.20 ATOM 409 CD1 PHEL 44 10.255 -1.929 8.985 1.0010.99 ATOM 410 CD2PHEL 44 12.002 -0.541 8.127 1.0013.17 ATOM 411 CE1 PHEL 44 10.796 -1.866 10.252 1.0011.48 ATOM 412 CE2PHEL 44 12.566 -0.471 9.394 1.0012.05 ATOM 413 CZ PHEL 44 11.954 -1.135 10.462 1.0012.67 ATOM 414 C PHEL 44 8.986 -1 3.319 4.731 1.0014.13 ATOM 415 O PHEL 44 8.261 - 1.106 4.146 1.0014.69 ATOM 416 N THRL 45 9.655 0.615 4.100 1.0014.63 ATOM 418 CA THRL 45 9.527 0.762 2.686 1.0012.14 ATOM 419 CB THRL 45 8.316 1.644 2.361 1.0014.73 ATOM 420 OG1 THRL 45 8.095 1.663 0.958 1.0025.05 ATOM 422 CG2 THR L 45 8.557 3.064 2.814 1.0019.97 ATOM 423 C THRL 45 10.787 1.386 2.187 1.0011.69 ATOM 424 O THRL 45 11.314 2.243 2.824 1.009.53 ATOM 425 N GLY L 46 11.317 0.861 1.096 1.0011.34 ATOM 427 CA GLYL 46 12.535 1.388 0.532 1.007.20 ATOM 428 C GLY L 46 12.250 2.581 -0.326 1.007.78 ATOM 429 O GLY L 46 11.266 2.582 -1.130 1.0010.42 ATOM 430 N LEU L 47 13.086 3.592 -0.168 1.007.54 ATOM 432 CA LEU L 47 12.912 4.859 -0.884 1.007.47 ATOM 433 CB LEU L 47 13.083 6.035 0.087 1.006.90 ATOM 434 CG LEU L 47 12.285 5.959 1.375 1.006.26 ATOM 435 CD1 LEU L 47 12.862 : 6.905 2.403 1.0011.14 ATOM 436 CD2 LEU L 47 10.820 ι 6.197 1.085 1.002.41 ATOM 437 C LEU L 47 13.940 4.988 -2.015 1.005.84 ATOM 438 O LEU L 47 13.563 5.288 -3.139 1.008.92 ATOM 439 N ILEL 48 5.209 4.749 -1.675 1.009.03 ATOM 441 CA ILEL 48 16.350 4.907 -2.568 1.007.03 ATOM 442 CB ILEL 48 17.257 6.079 -2.090 1.007.21 ATOM 443 CG2 ILE L 48 18.525 6.173 -2.924 1.009.51 ATOM 444 CGI ILEL 48 16.497 7.409 -2.042 1.008.82 ATOM 445 CD ILEL 48 16.008 7.937 -3.363 1.007.80 ATOM 446 C ILE L 48 7.230 : 3.640 -2.525 1.008.61 ATOM 447 0 ILEL 48 17.458 3.073 -1.451 1.0010.60 ATOM 448 N GLYL 49 17.740 3.224 -3.700 1.007.04 ATOM 450 CA GLYL 49 18.702 2.140 -3.794 1.002.00 ATOM 451 C GLYL 49 19.833 2.557 -4.709 1.007.57 ATOM 452 O GLYL 49 19.696 3.467 -5.544 1.0014.41 ATOM 453 N GLYL 50 20.957 1.959 -4.582 1.009.91 ATOM 455 CA GLYL 50 22.027 2.316 -5.453 1.009.21 ATOM 456 C GLYL 50 22.297 3.805 -5.479 1.0012.31 ATOM 457 O GLYL 50 22.358 4.388 -6.535 1.0012.48 ATOM 458 N THRL 51 22.456 4.402 -4.305 1.0010.33 ATOM 460 CA THRL 51 22.787 5.841 -4.140 1.0012.06 ATOM 461 CB THRL 51 24.098 6.283 -4.882 1.0011.87 ATOM 462 OG1 THRL 51 25.218 5.449 -4.521 1.007.57 ATOM 464 CG2 THRL 51 24.449 7.719 -4.497 1.0011.63 ATOM 465 C THRL 51 21.668 6.825 -4.481 1.0011.67 ATOM 466 O THRL 51 21.346 7.664 -3.651 1.0011.93 ATOM 467 N ASNL 52 21.034 6.712 -5.662 1.0012.21 ATOM 469 CA ASNL 52 20.063 7.719 -6.076 1.0013.73 ATOM 470 CB ASNL 52 20.764 8.826 -6.841 1.0018.43 ATOM 471 CG ASNL 52 21.598 8.273 -7.968 1.0024.37 ATOM 472 OD1 ASNL 52 21.193 7.327 -8.623 1.0022.65 ATOM 473 ND2ASNL 52 22.788 8.821 -8.173 1.0028.21 ATOM 476 C ASN L 52 18.943 7.197 -6.931 1.00 15.37 ATOM 477 O ASN L 52 18.295 7.964 -7.613 1.00 13.37 ATOM 478 N ASN L 53 18.726 5.906 -6.928 1.00 16.28 ATOM 480 CA ASN L 53 17.637 5.343 -7.691 1.00 17.34 ATOM 481 CB ASN L 53 18.056 3.969 -8.244 1.00 24.00 ATOM 482 CG ASN L 53 17.181 3.420 -9.373 1.00 27.36 ATOM 483 OD1 ASN L 53 17.664 2.624 - 10.199 1.00 33.10 ATOM 484 ND2 ASN L 53 15.903 3.812 -9.439 1.00 31.42 ATOM 487 C ASN L 53 16.409 5.216 -6.784 1.00 17.91 ATOM 488 O ASN L 53 16.369 4.427 -5.870 1.00 18.29 ATOM 489 N ARG L 54 15.431 6.003 -7.032 1.00 15.93 ATOM 491 CA ARG L 54 14.269 5.978 -6.237 1.00 18.87 ATOM 492 CB ARG L 54 13.494 7.239 -6.542 1.00 22.33 ATOM 493 CG ARG L 54 12.1 14 7.315 -5.958 1.00 25.55 ATOM 494 CD ARG L 54 1 1.818 8.740 -5.619 1.00 29.54 ATOM 495 NE ARG L 54 12.156 9.61 1 -6.703 1.00 27.82 ATOM 497 CZ ARG L 54 11.305 9.903 -7.653 1.00 32.19 ATOM 498 NH 1 ARG L 54 1 1.676 10.713 -8.622 1.00 35.27 ATOM 501 NH2 ARG L 54 10.080 9.380 -7.644 1.00 31.58 ATOM 504 C ARG L 54 13.462 4.730 -6.545 1.00 21.41 ATOM 505 O ARG L 54 13.238 4.418 -7.734 1.00 21.21 ATOM 506 N ALA L 55 13.049 4.008 -5.480 1.00 20.79 ATOM 508 CA ALA L 55 12.226 2.802 -5.620 1.00 21.50 ATOM 509 CB ALA L 55 1 1.976 2.164 -4.253 1.00 18.92 ATOM 510 C ALA L 55 10.925 3.180 -6.285 1.00 22.01 ATOM 511 O ALA L 55 10.492 4.31 1 -6.184 1.00 23.44 ATOM 512 N PRO L 56 10.249 2.257 -6.952 1.00 25.55 ATOM 513 CD PRO L 56 10.577 0.805 -7.061 1.00 26.77 ATOM 514 CA PRO L 56 9.009 2.580 -7.645 1.00 24.82 ATOM 515 CB PRO L 56 8.686 1.274 -8.405 1.00 27.53 ATOM 516 CG PRO L 56 9.270 0.215 -7.526 1.00 27.71 ATOM 517 C PRO L 56 7.903 3.030 -6.696 1.00 25.91 ATOM 518 O PRO L 56 7.736 2.500 -5.588 1.00 26.27 ATOM 519 N GLY L 57 7.138 4.016 -7.146 1.00 26.28 ATOM 521 CA GLY L 57 6.045 4.544 -6.338 1.00 22.74 ATOM 522 C GLY L 57 6.471 5.629 -5.360 1.00 20.96 ATOM 523 O GLY L 57 5.654 6.415 -4.928 1.00 23.79 ATOM 524 N VAL L 58 7.749 5.670 -4.998 1.00 20.25 ATOM 526 CA VAL L 58 8.228 6.677 -4.084 1.00 18.53 ATOM 527 CB VAL L 58 9.676 6.383 -3.720 1.00 15.29 ATOM 528 CGI VAL L 58 10.261 7.548 -2.974 1.00 1 1.07 ATOM 529 CG2 VAL L 58 9.742 5.104 -2.893 1.00 12.65 ATOM 530 C VAL L 58 8.120 8.092 -4.688 1.00 22.04 ATOM 531 O VAL L 58 8.591 8.337 -5.814 1.00 22.18 ATOM 532 N PRO L 59 7.523 9.061 -3.910 1.00 21.50 ATOM 533 CD PRO L 59 6.971 8.873 -2.543 1.00 20.50 ATOM 534 CA PRO L 59 7.338 10.464 -4.326 1.00 17.94 ATOM 535 CB PRO L 59 6.866 1 1.147 -3.063 1.00 18.92 ATOM 536 CG PRO L 59 6.066 10.068 -2.423 1.00 18.97 ATOM 537 C PRO L 59 8.586 1 1.100 -4.852 1.00 16.82 ATOM 538 O PRO L 59 9.708 10.921 -4.327 1.00 15.46 ATOM 539 N ALA L 60 8.374 11.880 -5.867 1.00 13.05 ATOM 541 CA ALA L 60 9.448 12.535 -6.530 1.00 14.83 ATOM 542 CB ALA L 60 8.866 13.317 -7.685 1.00 14.69 ATOM 543 C ALA L 60 10.238 13.427 -5.574 1.00 13.44 ATOM 544 O ALA L 60 1 1.412 13.644 -5.782 1.00 12.14 ATOM 545 N ARGL 61 9.601 13.919 - 4.488 1.0015.30 ATOM 547 CA ARGL 61 10.313 14.815 -3.524 1.0012.59 ATOM 548 CB ARGL 61 9.351 15.398 -2.478 1.0011.72 ATOM 549 CG ARGL 61 8.625 14.385 -1.596 1.0014.79 ATOM 550 CD ARGL 61 7.915 15.063 -0.415 1.0014.00 ATOM 551 NE ARGL 61 7.241 14.100 0.466 1.0010.99 ATOM 553 CZ ARGL 61 6.124 13.482 0.102 1.0011.79 ATOM 554 NH1 ARGL 61 5.532 12.600 0.889 1.0010.75 ATOM 557 NH2ARGL 61 5.617 13.726 -1.066 1.009.70 ATOM 560 C ARGL 61 11.499 14.160 -2.810 1.0012.82 ATOM 561 O ARGL 61 12.289 14.863 -2.103 1.0014.41 ATOM 562 N PHEL 62 11.648 12.826 -2.955 1.0011.27 ATOM 564 CA PHEL 62 12.755 12.125 -2.302 1.0010.94 ATOM 565 CB PHEL 62 12.288 10.734 -1.773 1.009.35 ATOM 566 CG PHEL 62 11.285 10.782 -0.645 1.009.62 ATOM 567 CD1 PHEL 62 11.712 10.900 0.694 1.005.49 ATOM 568 CD2 PHE L 62 9.924 10.700 -0.909 1.006.68 ATOM 569 CE1 PHEL 62 10.780 10.933 1.709 1.002.51 ATOM 570 CE2 PHE L 62 8.998 10.735 0.116 1.007.73 ATOM 571 CZ PHEL 62 9.424 10.854 1.425 1.004.66 ATOM 572 C PHEL 62 13.913 11.936 -3.265 1.009.16 ATOM 573 O PHEL 62 13.679 11.434 -4.344 1.00 8.82 ATOM 574 N SERL 63 15.160 12.336 -2.872 1.004.85 ATOM 576 CA SERL 63 16.310 12.117 -3.737 1.008.59 ATOM 577 CB SERL 63 16.686 13.360 -4.530 1.007.17 ATOM 578 OG SERL 63 17.272 14.327 -3.676 1.0012.90 ATOM 580 C SERL 63 17.512 11.684 -2.949 1.007.30 ATOM 581 O SERL 63 17.714 12.184 -1.861 1.009.45 ATOM 582 N GLY L 64 18.284 10.714 -3.503 1.005.56 ATOM 584 CA GLY L 64 19.500 10.258 -2.891 1.004.07 ATOM 585 C GLYL 64 20.685 10.879 -3.565 1.009.49 ATOM 586 O GLYL 64 20.628 11.253 -4.757 1.0012.20 ATOM 587 N SERL 65 21.761 11.034 -2.869 1.006.73 ATOM 589 CA SERL 65 22.876 11.673 -3.482 1.009.75 ATOM 590 CB SERL 65 22.603 13.184 -3.669 1.008.17 ATOM 591 OG SERL 65 22.777 13.907 -2.443 1.0010.45 ATOM 593 C SERL 65 24.064 11.432 -2.648 1.0010.16 ATOM 594 O SERL 65 23.959 10.685 -1.670 1.0010.96 ATOM 595 N LEU L 66 25.194 11.991 -3.078 1.0010.68 ATOM 597 CA LEUL 66 26.460 11.858 -2.382 1.009.69 ATOM 598 CB LEUL 66 27.453 11.096 -3.303 1.0013.61 ATOM 599 CG LEU L 66 28.203 9.827 -2.816 1.009.87 ATOM 600 CD1 LEUL 66 27.339 8.952 -1.958 1.008.09 ATOM 601 CD2LEUL 66 28.667 9.029 -4.026 1.008.69 ATOM 602 C LEUL 66 26.931 13.303 -2.134 1.0012.92 ATOM 603 O LEUL 66 27.044 14.080 -3.070 1.0010.87 ATOM 604 N ILEL 67 27.136 13.678 -0.858 1.0012.45 ATOM 606 CA ILEL 67 27.577 15.035 -0.515 1.0011.66 ATOM 607 CB ILEL 67 26.479 15.768 0.341 1.0012.96 ATOM 608 CG2 ILE L 67 26.874 17.196 0.608 1.0013.30 ATOM 609 CGI ILEL 67 25.123 15.753 -0.357 1.0013.53 ATOM 610 CD ILEL 67 24.013 16.437 0.425 1.0011.05 ATOM 611 C ILEL 67 28.879 14.904 0.276 1.0012.31 ATOM 612 O ILEL 67 28.896 14.327 1.350 1.0013.03 ATOM 613 N GLYL 68 29.987 15.387 -0.260 1.0013.08 ATOM 615 CA GLYL 68 31.238 15.196 0.431 1.0012.32 ATOM 616 C GLYL 68 31.485 13.701 0.579 1.0017.92 ATOM 617 O GLYL 68 31.193 12.939 -0.379 1.0016.67 ATOM 618 N ASPL 69 31.987 13.249 1.750 1.0016.48 ATOM 620 CA ASP L 69 32.247 11.813 1.933 1.0018.10 ATOM 621 CB ASPL 69 33.366 11.533 2.931 1.0024.05 ATOM 622 CG ASPL 69 34.618 12.344 2.727 1.0031.27 ATOM 623 OD1 ASP L 69 35.210 12.318 1.596 1.0032.40 ATOM 624 OD2ASPL 69 35.021 13.019 3.724 1.0039.08 ATOM 625 C ASPL 69 31.040 11.037 2.437 1.0014.56 ATOM 626 O ASPL 69 31.214 9.924 : 2.915 1.0016.00 ATOM 627 N LYS L 70 29.837 11.568 2.319 1.0011.13 ATOM 629 CA LYS L 70 28.688 10.854 2.852 1.0011.46 ATOM 630 CB LYSL 70 28.116 11.608 4.037 1.0011.39 ATOM 631 CG LYSL 70 28.992 11.536 5.269 1.0018.50 ATOM 632 CD LYS L 70 28.255 12.102 6.467 1.0020.15 ATOM 633 CE LYS L 70 28.208 13.604 6.394 1.0022.74 ATOM 634 NZ LYS L 70 29.587 14.158 6.382 1.0027.69 ATOM 638 C LYS L 70 27.589 10.639 1.872 1.0010.75 ATOM 639 O LYSL 70 27.473 11.369 0.883 1.0011.35 ATOM 640 N ALAL 71 26.762 9.623 2.137 1.006.32 ATOM 642 CA ALAL 71 25.546 9.487 1.377 1.002.44 ATOM 643 CB ALAL 71 25.071 8.044 1.378 1.002.00 ATOM 644 C ALAL 71 24.490 10.404 2.020 1.006.77 ATOM 645 O ALAL 71 24.528 10.675 3.251 1.006.10 ATOM 646 N ALAL 72 23.549 10.888 1.230 1.005.00 ATOM 648 CA ALAL 72 22.564 11.807 1.736 1.006.21 ATOM 649 CB ALAL 72 23.027 13.252 1.512 1.003.82 ATOM 650 C ALAL 72 21.207 11.564 1.102 1.004.44 ATOM 651 O ALAL 72 21.089 11.053 -0.049 1.006.60 ATOM 652 N LEUL 73 20.183 11.857 1.885 1.005.08 ATOM 654 CA LEUL 73 18.796 11.776 1.446 1.004.01 ATOM 655 CB LEUL 73 17.970 10.826 2.307 1.004.42 ATOM 656 CG LEUL 73 16.498 10.785 1.936 1.004.74 ATOM 657 CD1 LEUL 73 16.312 9.970 0.656 1.004.42 ATOM 658 CD2LEUL 73 15.675 10.211 3.083 1.00 8.67 ATOM 659 C LEUL 73 18.191 13.148 1.579 1.005.38 ATOM 660 O LEUL 73 18.287 13.764 2.621 1.009.62 ATOM 661 N THRL 74 17.593 13.629 0.537 1.007.72 ATOM 663 CA THRL 74 16.998 14.928 0.562 1.006.80 ATOM 664 CB THRL 74 17.695 15.896 -0.460 1.009.87 AfOM 665 OGITHRL 74 19.076 16.149 -0.017 1.004.69 ATOM 667 CG2THRL 74 16.936 17.208 -0.559 1.004.65 ATOM 668 C THRL 74 15.571 14.855 0.277 1.007.31 ATOM 669 O THRL 74 15.153 14.227 -0.676 1.006.60 ATOM 670 N ILEL 75 14.799 15.464 1.142 1.008.15 ATOM 672 CA ILEL 75 13.396 15.553 0.932 1.009.10 ATOM 673 CB ILEL 75 12.611 15.126 2.187 1.0011.95 ATOM 674 CG2 ILEL 75 11.132 15.053 1.856 1.0012.49 ATOM 675 CGI ILEL 75 13.152 13.789 2.734 1.0016.99 ATOM 676 CD ILEL 75 12.418 13.281 3.963 1.0015.52 ATOM 677 C ILEL 75 13.081 17.010 0.632 1.0012.05 ATOM 678 O ILEL 75 13.212 17.857 1.514 1.0010.42 ATOM 679 N THRL 76 12.693 17.302 -0.620 1.0013.27 ATOM 681 CA THRL 76 12.379 18.674 -1.036 1.0011.86 ATOM 682 CB THRL 76 12.740 18.887 -2.519 1.008.49 ATOM 683 OGITHRL 76 14.102 18.539 -2.723 1.007.34 ATOM 685 CG2THRL 76 12.54620.321 -2.892 1.00 8.93 ATOM 686 C THRL 76 10.893 18.986 -0.861 1.0015.75 ATOM 687 O THRL 76 10.044 18.392 -1.538 1.0019.95 ATOM 688 N GLYL 77 10.567 19.944 0.019 1.0017.30 ATOM 690 CA GLY L 77 9.16720.257 0.271 1.0015.95 ATOM 691 C GLYL 77 8.560 19.175 1.109 1.0016.40 ATOM 692 O GLY L 77 7.497 18.653 0.784 1.0017.47 ATOM 693 N ALAL 78 9.237 18.824 2.193 1.0016.13 ATOM 695 CA ALA L 78 8.765 17.723 3.068 1.0016.88 ATOM 696 CB ALAL 78 9.674 17.601 4.282 1.0015.72 ATOM 697 C ALAL 78 7.298 17.890 3.483 1.0017.09 ATOM 698 O ALAL 78 6.811 18.996 3.691 1.0020.02 ATOM 699 N GLN L 79 6.571 16.773 3.535 1.0016.23 ATOM 701 CA GLNL 79 5.184 16.787 3.933 1.0014.31 ATOM 702 CB GLNL 79 4.397 16.061 2.875 1.0013.55 ATOM 703 CG GLN L 79 4.447 16.805 1.555 1.0017.28 ATOM 704 CD GLNL 79 3.680 16.127 0.447 1.0022.72 ATOM 705 OE1 GLNL 79 3.849 16.479 -0.737 1.0028.20 ATOM 706 NE2 GLN L 79 2.817 15.163 0.790 1.0022.58 ATOM 709 C GLNL 79 4.972 16.160 5.327 1.0014.89 ATOM 710 O GLNL 79 5.861 15.498 5.849 1.0014.38 ATOM 711 N THRL 80 3.796 16.364 5.919 1.0012.50 ATOM 713 CA THRL 80 3.552 15.895 7.291 1.0018.91 ATOM 714 CB THRL 80 2.186 16.359 7.810 1.0017.20 ATOM 715 OG1 THRL 80 1.189 15.931 6.884 1.0021.04 ATOM 717 CG2THRL 80 2.139 17.881 7.940 1.0019.65 ATOM 718 C THRL 80 3.606 14.380 7.362 1.0019.00 ATOM 719 O THRL 80 4.000 13.812 8.394 1.0021.72 ATOM 720 N GLUL 81 3.215 13.759 6.252 1.0018.63 ATOM 722 CA GLUL 81 3.235 12.325 6.104 1.0019.81 ATOM 723 CB GLUL 81 2.555 11.956 4.801 1.0024.17 ATOM 724 CG GLUL 81 3.338 12.428 3.585 1.0034.44 ATOM 725 CD GLUL 81 2.657 12.143 2.251 1.0040.56 ATOM 726 OE1 GLUL 81 1.603 12.792 1.960 1.0044.10 ATOM 727 OE2GLUL 81 3.180 11.280 1.479 1.0043.81 ATOM 728 C GLUL 81 4.660 11.785 6.097 1.0018.55 ATOM 729 O GLUL 81 4.853 10.588 6.062 1.0020.36 ATOM 730 N ASP L 82 5.665 12.663 6.113 1.0014.45 ATOM 732 CA ASPL 82 7.027 12.212 6.091 1.0011.96 ATOM 733 CB ASPL 82 7.902 13.160 5.268 1.0011.90 ATOM 734 CG ASPL 82 7.523 13.214 3.783 1.0013.46 ATOM 735 OD1 ASP L 82 6.822 12.310 3.288 1.0016.83 ATOM 736 OD2ASPL 82 7.906 14.176 3.131 1.0013.86 ATOM 737 C ASPL 82 7.608 12.087 7.492 1.0012.84 ATOM 738 O ASPL 82 8.798 11.739 7.639 1.009.40 ATOM 739 N GLUL 83 6.844 12.479 8.535 1.0013.25 ATOM 741 CA GLUL 83 7.360 12.253 9.890 1.0013.46 ATOM 742 CB GLUL 83 6.371 12.783 10.953 1.0017.14 ATOM 743 CG GLUL 83 6.849 12.635 12.411 1.0021.93 ATOM 744 CD GLUL 83 6.097 13.555 13.389 1.0026.14 ATOM 745 OE1 GLU L 83 5.812 14.703 13.018 1.0022.27 ATOM 746 OE2GLUL 83 5.781 13.123 14.531 1.0027.48 ATOM 747 C GLU L 83 7.522 10.729 9.996 1.009.35 ATOM 748 O GLUL 83 6.538 10.002 9.819 1.0012.41 ATOM 749 N ALA L 84 8.733 10.261 10.224 1.009.86 ATOM 751 CA ALAL 84 9.002 8.826 10.218 1.008.78 -9?J- ATOM 752 CB ALAL 84 8.680 8.265 8.839 1.007.20 ATOM 753 C ALA L 84 10.451 8.635 10.544 1.00 8.36 ATOM 754 O ALAL 84 11.142 9.614 10.771 1.0011.79 ATOM 755 N ILEL 85 10.935 7.404 10.597 1.008.82 ATOM 757 CA ILEL 85 12.374 7.195 10.869 1.007.36 ATOM 758 CB ILEL 85 12.587 6 ι 6..115555 111 1..997722 1 1..00005 5..2255 ATOM 759 CG2 ILE L 85 14.073 5 5..999900 1 122..330044 1 1..00009 9.M66 ATOM 760 CGI ILEL 85 11.812 6 6..663311 1 i 133..220066 1 1..00001 133..336ι ATOM 761 CD ILEL 85 11.467 5 5..556688 114 4..220011 1 1..00001 100..1122 ATOM 762 C ILEL 85 2.996 6.745 9.551 1.005.85 ATOM 763 O ILEL 85 2.329 6.082 8.770 1.006.76 ATOM 764 N TYRL 86 14.192 7.215 < 275 1.00 4.42 ATOM 766 CA TYRL 86 14.866 6.918 7.986 1.00 7.23 ATOM 767 CB TYRL 86 15.159 8.203 7.200 1.00 6.83 ATOM 768 CG TYRL 86 13.913 8.870 6.716 1.00 8.61 ATOM 769 CD1 TYRL 86 13.172 9.704 7 7..558866 ι 11..00C0 155..77:3 ATOM 770 CE1 TYRL 86 11.924 10.187 77..221118 ? 11..00(0 ) 88..665 ATOM 771 CD2TYRL 86 13.369 8.555 55..444499 ' 11..00C0 l 55..99:2 ATOM 772 CE2TYRL 86 12.111 9.039 55..009922 11..0000 66..00.8 ATOM 773 CZ TYRL 86 11.391 9.850 5 5..998899 11..0000 88..1144 ATOM 774 OH TYRL 86 10.104 10.252 55..668811 11..00(0 ) 66..440 ATOM 776 C TYRL 86 16.153 6.242 1 8 5..223333 11..00002 2..0000 ATOM 777 O TYRL 86 16.996 6.769 8.949 1.008.00 ATOM 778 N PHEL 87 16.301 5.063 7.681 1.005.92 ATOM 780 CA PHEL 87 17.557 4.307 7.841 1.004.34 ATOM 781 CB PHEL 87 17.251 2.842 8.184 1.008.38 ATOM 782 CG PHEL 87 16.602 2.687 9.499 1.009.99 ATOM 783 CD1 PHEL 87 17.366 2.481 10.618 1.006.06 ATOM 784 CD2PHEL 87 15.220 2.729 9.601 1.0013.30 ATOM 785 CE1PHEL 87 16.743 2.308 11.862 1.0010.61 ATOM 786 CE2PHEL 87 14.595 2.562 10.826 1.0014.04 ATOM 787 CZ PHEL 87 15.365 2.348 11.957 1.008.48 ATOM 788 C PHEL 87 18.328 4.303 6.562 1.003.22 ATOM 789 O PHEL 87 17.707 4.281 5.510 1.002.51 ATOM 790 N CYS L 88 19.641 4.310 6.649 1.005.93 ATOM 792 CA CYSL 88 20.434 4.144 5.459 1.009.35 ATOM 793 CB CYSL 88 21.404 5.297 5.251 1.005.49 ATOM 794 SG CYSL 88 22.767 5.371 6.415 1.0015.50 ATOM 795 C CYSL 88 21.204 2.852 5.597 1.008.53 ATOM 796 O CYSL 88 21.483 2.413 6.720 1.008.84 ATOM 797 N ALA L 89 21.489 2.213 4.498 1.008.42 ATOM 799 CA ALA L 89 22.254 0.975 4.533 1.008.94 ATOM 800 CB ALAL 89 21.298 -0.202 4.212 1.006.42 ATOM 801 C ALAL 89 23.388 1.099 3.503 1.0011.22 ATOM 802 O ALAL 89 23.165 1.628 2.418 1.0010.12 ATOM 803 N LEUL 90 24.596 0.655 3.854 1.0012.71 ATOM 805 CA LEU L 90 25.735 0.735 2.957 1.0012.28 ATOM 806 CB LEUL 90 26.855 1.595 3.564 1.0013.85 ATOM 807 CG LEU L 90 26.569 3.094 3.774 1.0010.32 ATOM 808 CD1 LEUL 90 27.882 3.794 4.141 1.007.96 ATOM 809 CD2LEUL 90 25.941 3.694 2.503 1.0010.49 ATOM 810 C LEU L 90 26.287 -0.669 2.660 1.0014.32 ATOM 811 O LEUL 90 26.362 -1.520 3.582 1.0014.08 ATOM 812 N TRPL 91 26.696 -0.882 1.373 1.0010.21 ATOM 814 CA TRPL 91 27.201 -2.184 0.894 1.009.56 ATOM 815 CB TRPL 91 26.734 -2.435 -0.548 1.0013.24 ATOM 816 CG TRPL 91 27.370 -3.606 -1.295 1.0016.93 ATOM 817 CD2TRPL 91 26.974 -5.018 -1.253 1.0018.28 ATOM 818 CE2TRPL 91 27.660 -5.679 -2.291 1.0018.63 ATOM 819 CE3TRPL 91 26.094 -5.782 -0.455 1.0018.52 ATOM 820 CD1 TRPL 91 28.273 -3.498 -2.320 1.0018.74 ATOM 821 NE1 TRPL 91 28.432 -4.721 -2.902 1.0018.84 ATOM 823 CZ2TRPL 91 27.509 -7.069 -2.564 1.0017.39 ATOM 824 CZ3TR L 91 25.935 -7.162 -0.726 1.0020.45 ATOM 825 CH2TRPL 91 26.650 -7.793 -1.782 1.0018.96 ATOM 826 C TRPL 91 28.684 - -2.211 0.955 1.00 8.96 ATOM 827 O TRPL 91 29.339 ■ -1.272 0.509 1.009.38 ATOM 828 N TYRL 92 29.220 -3.247 1.556 1.009.41 ATOM 830 CA TYRL 92 30.649 3.389 1.630 1.0010.88 ATOM 831 CB TYRL 92 31.124 -3.365 3.095 1.0013.13 ATOM 832 CG TYRL 92 30.902 -2.043 3.827 1.0012.25 ATOM 833 CD1 TYRL 92 29.753 -1.810 4.591 1.0015.61 ATOM 834 CE1 TYRL 92 29.535 -0.583 5.219 1.0011.01 ATOM 835 CD2TYRL 92 31.836 -1.015 3.730 1.0014.35 ATOM 836 CE2 TYR L 92 31.622 0.197 4.345 1.0012.95 ATOM 837 CZ TYRL 92 30.472 0.415 5.077 1.0011.34 ATOM 838 OH TYRL 92 30.237 1.671 5.601 1.0014.51 ATOM 840 C TYRL 92 31.066 -4.693 0.951 1.0015.14 ATOM 841 O TYRL 92 31.333 -5.699 1.630 1.0014.53 ATOM 842 N SERL 93 31.044 -4.664 -0.393 1.0016.81 ATOM 844 CA SERL 93 31.475 -5.795 -1.251 1.0018.41 ATOM 845 CB SERL 93 32.907 -6.178 -0.911 1.0019.53 ATOM 846 OG SERL 93 33.774 -5.132 -1.332 1.0025.55 ATOM 848 C SERL 93 30.582 -7.038 -1.232 1.0020.20 ATOM 849 O SERL 93 30.266 -7.607 -2.311 1.0017.43 ATOM 850 N ASNL 94 30.200 -7.482 -0.020 1.0019.09 ATOM 852 CA ASN L 94 29.417 -8.684 0.119 1.0019.31 ATOM 853 CB ASN L 94 30.343 -9.906 0.036 1.0018.06 ATOM 854 CG ASNL 94 31.362 -9.915 1.145 1.0022.80 ATOM 855 OD1 ASN L 94 31.381 -9.018 2.021 1.0022.03 ATOM 856 ND2 ASN L 94 32.219-10.924 1.140 1.0021.52 ATOM 859 C ASNL 94 28.618 -8.688 1.425 1.0020.27 ATOM 860 O ASNL 94 28.207 -9.740 1.908 1.0022.39 ATOM 861 N HISL 95 28.396 -7.508 2.003 1.0019.53 ATOM 863 CA HIS L 95 27.542 -7.405 3.172 1.0018.65 ATOM 864 CB HIS L 95 28.273 -7.846 4.411 1.0016.28 ATOM 865 CG HIS L 95 29.434 -6.995 4.785 1.0019.96 ATOM 866 CD2 HIS L 95 30.655 -6.852 4.227 1.0017.79 ATOM 867 ND1 HIS L 95 29.472 -6.234 5.944 1.0020.98 ATOM 869 CE1 HIS L 95 30.652 -5.659 6.104 1.0022.66 ATOM 870 NE2 HIS L 95 31.371 -6.031 5.064 1.0020.00 ATOM 872 C HIS L 95 27.026 -5.989 3.352 1.0017.00 ATOM 873 O HISL 95 27.564 -5.066 2.790 1.0016.62 ATOM 874 N TRP L 96 25.985 -5.837 4.147 1.0015.07 ATOM 876 CA TRPL 96 25.383 -4.537 4.360 1.0013.84 ATOM 877 CB TRPL 96 23.884 -4.547 4.040 1.0012.09 ATOM 878 CG TRPL 96 23.550 -4.745 2.591 1.0014.83 ATOM 879 CD2TRPL 96 23.350 -3.711 1.602 1.0012.10 ATOM 880 CE2 TRP L 96 22.934 -4.340 0.417 1.0013.36 ATOM 881 CE3TRPL 96 23.475 -2.311 1.612 1.0011.19 ATOM 882 CD1 TRPL 96 23.265 -5.919 1.979 1.0015.53 ATOM 883 NE1 TRP L 96 22.893 -5.677 0.692 1.0014.17 ATOM 885 CZ2 TRP L 96 22.643 -3.626 -0.760 1.009.46 ATOM 886 CZ3 TRP L 96 23.181 -1.602 0.451 1.007.52 ATOM 887 CH2 TRP L 96 22.774 -2.257 -0.716 1.0011.56 ATOM 888 C TRPL 96 25.501 -4.165 5.786 1.0014.61 ATOM 889 O TRPL 96 25.451 -5.057 6.646 1.0012.87 ATOM 890 N VALL 97 25.664 -2.859 6.014 1.0011.97 ATOM 892 CA VAL L 97 25.612 -2.292 7.355 1.0013.35 ATOM 893 CB VAL L 97 26.971 -1.817 7.809 1.0012.63 ATOM 894 CGI VALL 97 26.881 -1.178 9.180 1.0014.09 ATOM 895 CG2 VAL L 97 27.865 -3.039 7.849 1.008.66 ATOM 896 C VAL L 97 24.600 -1.158 7.382 1.0014.93 ATOM 897 O VAL L 97 24.581 -0.311 6.477 1.009.72 ATOM 898 N PHEL 98 23.666 -1.233 8.342 1.0013.01 ATOM 900 CA PHEL 98 22.629 -0.239 8.458 1.0012.29 ATOM 901 CB PHEL 98 21.317 -0.875 8.885 1.009.91 ATOM 902 CG PHEL 98 20.505 -1.489 7.798 1.007.44 ATOM 903 CD1 PHEL 98 20.799 -2.748 7.325 1.009.14 ATOM 904 CD2 PHE L 98 19.392 -0.848 7.326 1.006.37 ATOM 905 CE1 PHEL 98 19.985 -3.342 6.410 1.006.90 ATOM 906 CE2 PHE L 98 18.557 -1.432 6.398 1.008.01 ATOM 907 CZ PHEL 98 18.849 -2.688 5.932 1.007.78 ATOM 908 C PHEL 98 23.034 0.838 9.452 1.0011.91 ATOM 909 O PHEL 98 23.871 0.596 10.313 1.0011.43 ATOM 910 N GLYL 99 22.517 2.053 9.239 1.0014.08 ATOM 912 CA GLYL 99 22.775 3.153 10.134 1.0012.11 ATOM 913 C GLYL 99 21.797 3.085 11.289 1.0011.79 ATOM 914 O GLYL 99 20.892 2.267 11.267 1.0010.46 ATOM 915 N GLYL 100 21.971 3.955 12.280 1.0012.00 ATOM 917 CA GLYL 100 21.103 3.943 13.451 1.008.79 ATOM 918 C GLYL 100 19.723 4.507 13.256 1.009.23 ATOM 919 O GLYL 100 18.832 4.282 14.101 1.0012.86 ATOM 920 N GLY L 101 19.494 5.204 12.159 1.007.60 ATOM 922 CA GLYL 101 18.172 5.776 11.925 1.004.00 ATOM 923 C GLYL 101 18.149 7.204 12.428 1.007.52 ATOM 924 O GLYL 101 18.914 7.549 13.399 1.007.76 ATOM 925 N THRL 102 17.410 8.046 11.676 1.008.12 ATOM 927 CA THRL 102 17.197 9.482 11.996 1.007.96 ATOM 928 CB THRL 102 17.621 10.421 10.792 1.007.52 ATOM 929 OG1 THRL 102 19.018 10.307 10.564 1.004.45 ATOM 931 CG2THRL 102 17.291 11.883 11.056 1.004.44 ATOM 932 C THRL 102 15.717 9.657 12.207 1.0010.01 ATOM 933 O THRL 102 14.961 9.267 11.332 1.0011.13 ATOM 934 N LYS L 103 15.248 10.189 13.349 1.0010.41 ATOM 936 CA LYS L 103 13.807 10.407 13.447 1.0011.36 ATOM 937 CB LYS L 103 13.261 10.443 14.902 1.0014.52 ATOM 938 CG LYS L 103 11.801 10.989 14.933 1.0016.54 ATOM 939 CD LYS L 103 11.212 11.110 16.350 1.0012.70 ATOM 940 CE LYS L 103 9.750 11.551 16.305 1.0014.64 ATOM 941 NZ LYSL 103 8.858 10.636 15.481 1.0017.17 ATOM 945 C LYSL 103 13.468 11.724 12.798 1.0010.60 ATOM 946 O LYSL 103 14.030 12.728 13.180 1.0012.19 ATOM 947 N LEUL 104 12.546 11.725 11.853 1.009.69 ATOM 949 CA LEUL 104 12.183 12.968 11.229 1.0011.35 ATOM 950 CB LEUL 104 12.125 12.864 9.693 1.009.61 ATOM 951 CG LEUL 104 11.724 14.187 9.012 1.0010.81 ATOM 952 CD1 LEUL 104 12.847 15.212 9.199 1.002.00 ATOM 953 CD2 LEUL 104 11.408 13.947 7.560 1.0010.86 ATOM 954 C LEUL 104 10.866 13.484 11.728 1.0010.04 ATOM 955 O LEUL 104 9.862 12.794 11.656 1.0016.01 ATOM 956 N THRL105 10.861 14.711 12.251 1.0011.71 ATOM 958 CA THRL 105 9.614 15.361 12.576 1.007.07 ATOM 959 CB THRL 105 9.682 16.091 13.949 1.009.46 ATOM 960 OGITHRL 105 9.844 15.129 14.983 1.0012.27 ATOM 962 CG2THRL105 8.415 16.918 14.200 1.002.15 ATOM 963 C THRL 105 9.271 16.410 11.513 1.007.56 ATOM 964 O THRL 105 10.093 17.241 11.182 1.009.71 ATOM 965 N VAL L 106 8.084 16.320 10.974 1.009.73 ATOM 967 CA VALL 106 7.541 17.364 10.106 1.0011.58 ATOM 968 CB VAL L 106 7.106 16.851 8.725 1.009.06 ATOM 969 CGI VALL 106 6.526 18.000 7.911 1.006.52 ATOM 970 CG2 VALL 106 8.329 16.228 8.011 1.0010.40 ATOM 971 C VALL 106 6.335 17.931 10.856 1.0011.09 ATOM 972 O VALL 106 5.242 17.324 10.877 1.0013.54 ATOM 973 N LEU L 106 A 6.601 19.071 11.521 1.0012.43 ATOM 975 CA LEUL106A 5.655 19.710 12.378 1.0012.13 ATOM 976 CB LEU L 106 A 6.11621.132 12.666 1.009.12 ATOM 977 CG LEU L 106A 7.48821.225 13.349 1.007.72 ATOM 978 CD1LEUL106A 7.99022.640 13.270 1.009.05 ATOM 979 CD2LEUL106A 7.41320.730 14.816 1.006.98 ATOM 980 C LEUL106A 4.325 19.678 11.752 1.0013.07 ATOM 981 O LEUL106A 4.09420.360 10.779 1.0018.75 ATOM 982 N GLYL 107 3.468 18.816 12.284 1.0014.91 ATOM 984 CA GLY L 107 2.117 18.689 11.760 1.0016.40 ATOM 985 C GLYL 107 1.065 19.137 12.762 1.0015.29 ATOM 986 O GLYL 107 -0.112 18.925 12.547 1.0016.64 ATOM 987 N SERL 108 1.523 19.742 13.859 1.0018.60 ATOM 989 CA SERL 108 0.64720.251 14.907 1.0018.91 ATOM 990 CB SERL 108 0.095 19.123 15.790 1.0021.02 ATOM 991 OG SERL 108 1.115 18.543 16.596 1.0027.15 ATOM 993 C SERL 108 1.453 21.165 15.760 1.0017.58 ATOM 994 O SERL 108 2.67621.208 15.641 1.0017.99 ATOM 995 N GLU L 109 0.77621.825 16.671 1.0017.83 ATOM 997 CA GLU L 109 1.40922.775 17.516 1.0016.58 ATOM 998 CB GLUL 109 0.30523.562 18.224 1.0021.42 ATOM 999 CG GLU L 109 -0.52524.468 17.320 1.0026.54 ATOM 1000 CD GLUL 109 -1.31923.742 16.2340.5027.76 ATOM 1001 OE1 GLUL 109 -1.76422.614 16.5020.5028.73 ATOM 1002 OE2 GLU LI 09 -1.50224.309 15.1040.5026.82 ATOM 1003 C GLUL 109 2.28722.041 18.513 1.0017.20 ATOM 1004 O GLUL 109 1.91520.964 18.956 1.0014.41 ATOM 1005 N LYS LI 10 3.43022.599 18.883 1.0016.72 ATOM 1007 CA LYSL 110 4.26621.914 19.845 1.0020.99 ATOM 1008 CB LYSL 110 5.61822.584 19.993 1.0022.20 ATOM 1009 CG LYS LI 10 6.47722.377 18.759 1.0024.75 ATOM 1010 CD LYSL 110 7.78623.126 18.835 1.0025.15 ATOM 1011 CE LYS LI 10 8.531 23.023 17.513 1.0030.78 ATOM 1012 NZ LYSL 110 9.941 23.516 17.611 1.0032.12 ATOM 1016 C LYSL110 3.56621.80421.187 1.0021.68 ATOM 1017 O LYSL 110 2.76922.67321.557 1.0022.35 ATOM 1018 N SERL 111 3.83420.69921.876 1.0022.71 ATOM 1020 CA SERL 111 3.19620.39523.158 1.0021.05 ATOM 1021 CB SERL 111 2.113 19.35422.921 1.0022.18 ATOM 1022 OG SER L 111 1.309 19.14824.070 1.0023.73 ATOM 1024 C SER L 111 4.253 19.85924.139 1.0021.55 ATOM 1025 O SER L 111 5.049 18.97923.790 1.0021.72 ATOM 1026 N SER LI 12 4.31820.45725.339 1.0019.80 ATOM 1028 CA SERL 112 5.27220.04726.347 1.0017.43 ATOM 1029 CB SERL 112 5.37021.141 27.399 1.0020.85 ATOM 1030 OG SERL 112 6.32222.11427.001 1.0029.98 ATOM 1032 C SERL 112 4.864 18.72726.995 1.0014.25 ATOM 1033 O SERL 112 3.669 18.40927.067 1.0019.12 ATOM 1034 N PROL 113 5.812 17.92927.481 1.0010.92 ATOM 1035 CD PROL 113 7.264 18.153 27.529 1.007.81 ATOM 1036 CA PROL 113 5.463 16.67728.106 1.0012.79 ATOM 1037 CB PROL 113 6.784 15.97928.215 1.008.93 ATOM 1038 CG PRO LI 13 7.704 17.09228.478 1.009.20 ATOM 1039 C PRO LI 13 4.802 16.881 29.473 1.0013.59 ATOM 1040 O PROL 113 5.173 17.78230.241 1.0013.35 ATOM 1041 N SERL 114 3.781 16.101 29.736 1.0015.55 ATOM 1043 CA SERL 114 3.219 16.05231.062 1.0015.08 ATOM 1044 CB SERL 114 1.722 15.84431.000 1.0017.33 ATOM 1045 OG SERL 114 1.154 15.90832.312 1.0025.09 ATOM 1047 C SERL 114 3.903 14.913 31.831 1.0016.29 ATOM 1048 O SERL 114 3.804 13.71831.467 1.0015.53 ATOM 1049 N VALL 115 4.617 15.29532.871 1.0012.98 ATOM 1051 CA VALL 115 5.426 14.37033.674 1.0012.33 ATOM 1052 CB VALL 115 6.752 15.00933.988 1.006.39 ATOM 1053 CGI VAL LI 15 7.709 13.97934.583 1.003.44 ATOM 1054 CG2VALL 115 7.306 15.645 32.716 1.009.96 ATOM 1055 C VALL 115 4.779 13.99635.004 1.0013.58 ATOM 1056 O VALL 115 4.226 14.83735.693 1.0013.43 ATOM 1057 N THRL 116 4.880 12.74835.361 1.0012.99 ATOM 1059 CA THRL 116 4.398 12.29536.649 1.0011.92 ATOM 1060 CB THRL 116 3.062 11.55736.565 1.0010.15 ATOM 1061 OG1 THRL 116 2.138 12.351 35.833 1.005.53 ATOM 1063 CG2THRL 116 2.519 11.28437.978 1.0010.07 ATOM 1064 C THRL 116 5.419 11.33637.207 1.0013.44 ATOM 1065 O THRL 116 5.864 10.40736.480 1.0013.00 ATOM 1066 N LEU LI 17 5.820 11.57438.463 1.009.86 ATOM 1068 CA LEUL 117 6.777 10.703 39.114 1.0010.48 ATOM 1069 CB LEUL 117 7.978 11.51439.513 1.008.99 ATOM 1070 CG LEUL 117 9.092 10.73840.197 1.0013.84 ATOM 1071 CD1LEUL 117 9.766 9.77939.216 1.0010.30 ATOM 1072 CD2 LEUL 117 10.091 11.72040.799 1.0017.17 ATOM 1073 C LEUL 117 6.142 9.97040.330 1.009.98 ATOM 1074 O LEUL 117 5.456 10.56441.158 1.0012.16 ATOM 1075 N PHEL 118 6.332 8.67640.390 1.009.99 ATOM 1077 CA PHEL 118 5.750 7.86441.440 1.009.51 ATOM 1078 CB PHEL 118 4.876 6.751 40.867 1.006.53 ATOM 1079 CG PHEL 118 3.652 7.20840.172 1.006.03 ATOM 1080 CD1 PHEL 118 2.538 7.60340.901 1.004.85 ATOM 1081 CD2PHEL 118 3.569 7.161 38.762 1.003.25 ATOM 1082 CE1PHEL 118 1.345 7.93340.264 1.006.00 ATOM 1083 CE2 PHEL 118 2.385 7.501 38.128 1.002.00 ATOM 1084 CZ PHEL 118 1.263 7.883 38.881 1.003.81 ATOM 1085 C PHEL 118 6.835 7.21642.272 1.009.33 ATOM 1086 O PHEL 118 7.864 6.711 41.759 1.009.88 ATOM 1087 N PROL 119 6.623 7.22843.586 1.009.00 ATOM 1088 CD PROL 119 5.434 7.83944.252 1.007.59 ATOM 1089 CA PROL 119 7.553 6.62944.549 1.00 8.55 ATOM 1090 CB PROL 119 7.113 7.29345.852 1.009.62 ATOM 1091 CG PROL 119 5.627 7.381 45.676 1.009.04 ATOM 1092 C PROL 119 7.347 5.12844.604 1.004.72 ATOM 1093 O PROL 119 6.358 4.65644.103 1.006.50 ATOM 1094 N PROL 120 8.278 4.37345.160 1.003.79 ATOM 1095 CD PROL 120 9.622 4.80345.475 1.006.28 ATOM 1096 CA PRO L 120 8.131 2.92345.298 1.006.76 ATOM 1097 CB PROL 120 9.489 2.431 45.730 1.009.39 ATOM 1098 CG PROL 120 10.182 : 3.62746.233 1.005.45 ATOM 1099 C PROL 120 7.022 2.55246.275 1.0010.87 ATOM 1100 O PROL 120 6.768 3.26647.252 1.0011.35 ATOM 1101 N SERL 121 6.290 1.50545.965 1.0012.02 ATOM 1103 CA SERL 121 5.183 1.08846.829 1.0014.15 ATOM 1104 CB SERL 121 4.178 0.15546.082 1.0013.52 ATOM 1105 OG SERL 121 4.763 -1.08445.722 1.0014.31 ATOM 1107 C SERL 121 5.748 0.403 48.072 1.0015.89 ATOM 1108 O SERL 121 6.927 ■ -0.00848.091 1.0014.68 ATOM 1109 N SERL 122 4.932 0.33249.125 1.0015.71 ATOM 1111 CA SERL 122 5.367 -0.32050.342 1.0017.27 ATOM 1112 CB SERL 122 4.344 -0.069 51.454 1.0017.69 ATOM 1113 OG SERL 122 3.021 -0.31950.990 1.0025.59 ATOM 1115 C SERL 122 5.508 ■ -1.80950.072 1.0014.07 ATOM 1116 O SERL 122 6.469 -2.43650.541 1.0016.14 ATOM 1117 N ALAL 123 4.563 -2.34449.269 1.0011.63 ATOM 1119 CA ALAL 123 4.568 -3.77548.940 1.0010.10 ATOM 1120 CB ALA L 123 3.326 -4.12648.147 1.0013.01 ATOM 1121 C ALAL 123 5.839 -4.151 48.206 1.009.75 ATOM 1122 O ALAL 123 6.494 -5.13448.561 1.006.87 ATOM 1123 N GLUL 124 6.260 -3.32547.226 1.008.37 ATOM 1125 CA GLU L 124 7.492 -3.60446.547 1.007.57 ATOM 1126 CB GLU L 124 7.788 -2.65345.376 1.009.85 ATOM 1127 CG GLU L 124 9.105 -3.01644.693 1.009.19 ATOM 1128 CD GLU L 124 9.483 -2.12943.532 1.008.89 ATOM 1129 OE1 GLUL 124 8.883 -1.08043.391 1.0011.65 ATOM 1130 OE2 GLUL 124 10.390 -2.47842.764 1.0010.96 ATOM 1131 C GLUL 124 8.648 -3.53747.490 1.00 8.44 ATOM 1132 O GLUL 124 9.501 -4.42847.481 1.007.83 ATOM 1133 N LEU L 125 8.687 -2.48948.336 1.0010.06 ATOM 1135 CA LEU L 125 9.820 -2.29049.278 1.008.99 ATOM 1136 CB LEU L 125 9.562 -1.051 50.156 1.006.82 ATOM 1137 CG LEU L 125 9.870 0.27849.456 1.008.44 ATOM 1138 CD1 LEUL 125 9.233 1.465 50.157 1.0010.23 ATOM 1139 CD2 LEUL 125 11.372 0.45749.354 1.0010.82 ATOM 1140 C LEUL 125 10.101 -3.50050.160 1.007.68 ATOM 1141 O LEUL 125 11.267 -3.78650.516 1.006.19 ATOM 1142 N GLU L 126 9.055 -4.20850.514 1.009.15 ATOM 1144 CA GLU L 126 9.226 -5.38951.339 1.0012.67 ATOM 1145 CB GLU L 126 7.906 -6.055 51.525 1.0015.98 ATOM 1146 CG GLU L 126 6.902 -5.183 52.204 1.0019.89 ATOM 1147 CD GLU L 126 5.648 -5.941 52.477 1.0022.91 ATOM 1148 OE1 GLUL 126 5.674 -7.203 52.445 1.0024.59 ATOM 1149 OE2 GLUL 126 4.627 -5.28652.726 1.0026.87 ATOM 1150 C GLUL 126 10.169 -6.381 50.692 1.0014.63 ATOM 1151 O GLUL 126 10.849 -7.14751.409 1.0012.25 ATOM 152 N THRL 127 10.177 -6.39449.316 1.0013.98 ATOM 154 CA THRL 127 11.063 -7.30848.538 1.0013.13 ATOM 155 CB THRL 127 10.565 -7.55747.071 1.0011.80 ATOM 156 OG1 THRL 127 10.749 -6.38446.266 1.0010.21 ATOM 158 CG2THRL 127 9.095 -7.94047.045 1.0012.12 ATOM 159 C THRL 127 12.468 -6.77348.455 1.0012.72 ATOM 160 O THRL 127 13.278 -7.31947.728 1.0014.85 ATOM 161 N ASNL 128 12.744 -5.701 49.209 1.0013.49 ATOM 163 CA ASN L 128 14.053 -5.04949.228 1.0013.82 ATOM 164 CB ASN L 128 15.159 -6.03549.674 1.0019.63 ATOM 165 CG ASN L 128 15.148 -6.262 51.183 1.0023.79 ATOM 166 OD1 ASNL 128 14.978 -7.388 51.646 1.0026.72 ATOM 167 ND2 ASN L 128 15.329 -5.18651.962 1.0025.77 ATOM 170 C ASNL 128 14.414 -4.36747.901 1.0014.19 ATOM 171 O ASNL 128 15.611 -4.11947.595 1.0013.24 ATOM 172 N LYS L 129 13.375 -4.01847.146 1.0017.87 ATOM 174 CA LYSL 129 13.534 -3.32745.875 1.0018.00 ATOM 175 CB LYSL 129 13.092 -4.22944.705 1.0022.35 ATOM 176 CG LYSL 129 13.737 -5.60944.662 1.0024.95 ATOM 177 CD LYSL 129 15.231 -5.50244.540 1.0028.22 ATOM 178 CE LYSL 129 15.855 -6.861 44.340 1.0030.22 ATOM 179 NZ LYSL 129 15.417 -7.44043.042 1.0034.30 ATOM 183 C LYSL 129 12.686 -2.05045.854 1.0016.78 ATOM 184 O LYSL 129 11.623 -1.98046.448 1.0015.40 ATOM 185 N ALAL 130 13.173 -1.04845.154 1.0016.40 ATOM 187 CA ALAL 130 12.448 0.21444.999 1.0015.30 ATOM 188 CB ALAL 130 12.977 1.26745.964 1.0010.48 ATOM 189 C ALAL 130 12.572 0.72743.545 1.0013.30 ATOM 190 O ALA L 130 13.691 0.98843.056 1.0013.88 ATOM 191 N THRL 131 11.412 0.80842.863 1.0010.24 ATOM 193 CA THRL 131 11.349 1.32341.522 1.008.65 ATOM 194 CB THRL 131 10.665 0.34640.546 1.009.65 ATOM 195 OG1 THRL 131 11.277 -0.96440.640 1.0010.61 ATOM 197 CG2THRL 131 10.733 0.89739.099 1.008.13 ATOM 198 C THRL 131 10.550 2.59441.507 1.004.73 ATOM 199 O THRL 131 9.443 2.621 42.017 1.007.42 ATOM 1200 N LEU L 132 11.136 3.63740.962 1.005.79 ATOM 1202 CA LEUL 132 10.436 4.89940.780 1.00 8.20 ATOM 1203 CB LEUL 132 11.372 6.08541.065 1.007.00 ATOM 1204 CG LEU L 132 11.780 6.38542.529 1.009.11 ATOM 1205 CD1 LEUL 132 12.638 5.27443.087 1.006.00 ATOM 1206 CD2LEUL 132 12.583 7.69442.582 1.008.20 ATOM 1207 C LEU L 132 9.971 4.96739.336 1.007.07 ATOM 1208 O LEUL 132 10.752 4.681 38.446 1.0010.93 ATOM 1209 N VALL 133 8.735 5.30939.105 1.007.44 ATOM 1211 CA VALL 133 8.228 5.345 37.740 1.007.69 ATOM 1212 CB VALL 133 6.906 4.58637.603 1.005.71 ATOM 1213 CGI VALL 133 6.388 4.65936.159 1.005.28 ATOM 1214 CG2 VALL 133 7.115 3.12238.014 1.0010.59 ATOM 1215 C VALL 133 7.979 6.76737.291 1.008.68 ATOM 1216 O VALL 133 7.319 7.53037.961 1.008.54 ATOM 1217 N CYSL 134 8.460 7.10936.130 1.0012.17 ATOM 1219 CA CYSL 134 8.218 8.45035.589 1.009.67 ATOM 1220 CB CYSL 134 9.569 9.11935.343 1.008.40 ATOM 1221 SG CYSL 134 9.446 10.80434.667 1.0010.83 ATOM 1222 C CYSL 134 7.465 8.30234.290 1.009.67 ATOM 1223 O CYSL 134 8.017 7.705 33.364 1.0010.89 ATOM 1224 N THRL 135 6.209 8.73734.238 1.006.29 ATOM 1226 CA THRL 135 5.480 8.651 33.029 1.005.35 ATOM 1227 CB THRL 135 4.031 8.17733.248 1.005.71 ATOM 1228 OG1 THRL 135 3.243 9.19633.888 1.0011.96 ATOM 1230 CG2 THRL 135 4.020 6.90434.103 1.002.00 ATOM 1231 C THRL 135 5.549 9.98832.324 1.009.71 ATOM 1232 O THRL 135 5.820 11.015 32.958 1.0011.41 ATOM 1233 N ILEL 136 5.440 9.98931.002 1.009.98 ATOM 1235 CA ILEL 136 5.696 11.23730.220 1.0011.09 ATOM 1236 CB ILE L 136 7.171 11.27029.677 1.0012.20 ATOM 1237 CG2ILEL 136 7.447 12.60628.973 1.0010.90 ATOM 1238 CGI ILEL 136 8.185 11.00830.796 1.0010.97 ATOM 1239 CD ILEL 136 9.585 10.663 30.291 1.0011.49 ATOM 1240 C ILEL 136 4.750 11.23029.030 1.0010.64 ATOM 1241 O ILEL 136 4.856 10.351 28.213 1.0011.08 ATOM 1242 N THRL 137 3.811 12.16528.941 1.0010.77 ATOM 1244 CA THRL 137 2.822 12.07227.911 1.009.97 ATOM 1245 CB THRL 137 1.480 11.50828.492 1.0011.90 ATOM 1246 OG1 THRL 137 0.871 12.40729.467 1.0011.66 ATOM 1248 CG2 THRL 137 1.739 10.17729.180 1.0012.72 ATOM 1249 C THRL 137 2.603 13.41227.228 1.0013.30 ATOM 1250 O THRL 137 3.179 14.43227.673 1.0010.45 ATOM 1251 N ASPL 138 1.843 13.35026.118 1.0012.35 ATOM 1253 CA ASP L 138 1.351 14.531 25.355 1.0014.23 ATOM 1254 CB ASPL 138 0.323 15.30626.176 1.0012.77 ATOM 1255 CG ASPL 138 -0.780 14.43626.702 1.0016.64 ATOM 1256 OD1 ASPL 138 -1.708 14.07825.914 1.0015.94 ATOM 1257 OD2 ASPL 138 -0.734 14.10027.912 1.0016.10 ATOM 1258 C ASPL 138 2.413 15.50224.881 1.0012.96 ATOM 1259 O ASPL 138 2.186 16.70524.905 1.0013.42 ATOM 1260 N PHEL 139 3.568 15.011 24.444 1.0015.33 ATOM 1262 CA PHEL 139 4.597 15.91723.904 1.0012.61 ATOM 1263 CB PHEL 139 5.991 15.68224.506 1.0013.93 ATOM 1264 CG PHEL 139 6.464 14.24824.548 1.0017.51 ATOM 1265 CD1 PHEL 139 6.004 13.38225.535 1.0014.06 ATOM 1266 CD2 PHEL 139 7.387 13.775 23.609 1.0018.44 ATOM 1267 CE1 PHEL 139 6.444 12.08825.589 1.0015.91 ATOM 1268 CE2 PHE L 139 7.829 12.46723.665 1.0017.97 ATOM 1269 CZ PHEL 139 7.354 11.61824.659 1.0019.08 ATOM 1270 C PHE L 139 4.685 15.81022.403 1.0014.58 ATOM 1271 O PHEL 139 4.391 14.75721.835 1.0013.97 ATOM 1272 N TYRL 140 5.010 16.951 21.763 1.0014.53 ATOM 1274 CA TYR L 140 5.219 17.02220.306 1.0015.96 ATOM 1275 CB TYR L 140 3.929 17.256 19.548 1.009.65 ATOM 1276 CG TYR LI 40 4.150 17.200 18.050 1.0017.09 ATOM 1277 CD 1 TYRL 140 4.110 15.993 17.372 1.0018.26 ATOM 1278 CE1 TYRL 140 4.355 15.923 16.003 1.0018.78 ATOM 1279 CD2 TYR L 140 4.443 18.351 17.312 1.0017.33 ATOM 1280 CE2 TYR L 140 4.691 18.289 15.945 1.0017.98 ATOM 1281 CZ TYRL 140 4.639 17.069 15.307 1.0019.92 ATOM 1282 OH TYR L 140 4.842 16.999 13.958 1.0021.97 ATOM 1284 C TYRL 140 6.148 18.17420.045 1.0014.90 ATOM 1285 O TYR L 140 5.815 19.26420.460 1.0017.79 ATOM 1286 N PROL 141 7.336 18.004 19.364 1.0017.44 ATOM 1287 CD PROL 141 8.342 19.079 19.203 1.0018.49 ATOM 1288 CA PROL 141 7.877 16.736 18.791 1.0016.51 ATOM 1289 CB PROL 141 9.278 17.128 18.347 1.0016.41 ATOM 1290 CG PROL 141 9.148 18.569 18.067 1.0018.35 ATOM 1291 C PROL 141 7.979 15.574 19.770 1.0017.49 ATOM 1292 O PROL 141 8.111 15.77720.988 1.0016.25 ATOM 1293 N GLYL 142 7.960 14.373 19.221 1.0016.47 ATOM 1295 CA GLY L 142 8.127 13.18220.027 1.0017.96 ATOM 1296 C GLY L 142 9.568 12.873 20.379 1.0017.11 ATOM 1297 O GLY L 142 10.011 11.74020.287 1.0020.37 ATOM 1298 N VALL 143 10.332 13.84620.753 1.0017.91 ATOM 1300 CA VALL 143 11.674 13.54821.201 1.0020.37 ATOM 1301 CB VALL 143 12.750 13.98920.189 1.0025.23 ATOM 1302 CGI VALL 143 12.526 15.434 19.776 1.0027.03 ATOM 1303 CG2 VAL L 143 14.139 13.811 20.807 1.0023.81 ATOM 1304 C VALL 143 11.937 14.19422.555 1.0020.36 ATOM 1305 O VALL 143 11.696 15.39422.719 1.0018.56 ATOM 1306 N VALL 144 12.421 13.37523.518 1.0018.00 ATOM 1308 CA VALL 144 12.729 13.83724.885 1.0018.09 ATOM 1309 CB VALL 144 11.586 13.52025.905 1.0015.31 ATOM 1310 CGI VALL 144 10.361 14.33625.624 1.0013.05 ATOM 1311 CG2 VALL 144 11.246 12.03425.879 1.0015.08 ATOM 1312 C VALL 144 13.952 13.12425.398 1.0017.23 ATOM 1313 O VALL 144 14.204 11.98724.997 1.0015.86 ATOM 1314 N THRL 145 14.747 13.803 26.217 1.0016.98 ATOM 1316 CA THRL 145 15.794 13.11626.930 1.0017.36 ATOM 1317 CB THRL 145 17.242 13.73426.774 1.0022.21 ATOM 1318 OG1 THRL 145 17.616 14.51827.914 1.0022.36 ATOM 1320 CG2 THRL 145 17.364 14.57025.512 1.0019.06 ATOM 1321 C THRL 145 15.373 13.10528.394 1.0019.55 ATOM 1322 O THRL 145 14.797 14.08528.864 1.0015.45 ATOM 1323 N VALL 146 15.581 11.96629.070 1.0019.67 ATOM 1325 CA VALL 146 15.178 11.79930.468 1.0017.75 ATOM 1326 CB VALL 146 14.336 10.511 30.665 1.0015.39 ATOM 1327 CGI VALL 146 14.047 10.26232.148 1.0016.28 ATOM 1328 CG2 VALL 146 13.047 10.641 29.918 1.0012.45 ATOM 1329 C VALL 146 16.425 11.70231.322 1.0018.57 ATOM 1330 O VALL 146 17.336 10.96430.998 1.0020.82 ATOM 1331 N ASPL 147 16.464 12.47032.388 1.0016.64 ATOM 1333 CA ASPL 147 17.595 12.483 33.267 1.0016.87 ATOM 1334 CB ASPL 147 18.330 13.83433.113 1.0022.38 ATOM 1335 CG ASPL 147 19.078 13.95531.783 1.0025.15 ATOM 1336 OD1 ASPL 147 20.155 13.33931.665 1.0025.53 ATOM 1337 OD2 ASP L 147 18.579 14.65630.862 1.0024.06 ATOM 1338 C ASPL 147 17.111 12.29734.702 1.0013.63 ATOM 1339 O ASPL 147 16.206 13.00735.146 1.0017.40 ATOM 1340 N TRPL 148 17.692 11.353 35.403 1.0012.32 ATOM 1342 CA TRPL 148 17.296 11.05936.799 1.008.34 ATOM 1343 CB TRPL 148 17.205 9.517 37.013 1.007.75 ATOM 1344 CG TRPL 148 16.011 8.871 36.393 1.009.41 ATOM 1345 CD2 TRPL 148 14.735 8.685 37.020 1.007.75 ATOM 1346 CE2 TRP L 148 13.897 8.085 36.079 1.009.98 ATOM 1347 CE3 TRP L 148 14.234 8.974 38.312 1.0011.38 ATOM 1348 CD1 TRP L 148 15.894 8.383 35.122 1.005.30 ATOM 1349 NE1 TRP L 148 14.636 7.923 34.955 1.0010.25 ATOM 1351 CZ2TRPL 148 12.570 7.753 36.354 1.0010.62 ATOM 1352 CZ3 TRP L 148 12.921 8.645 38.604 1.008.84 ATOM 1353 CH2TRPL 148 12.095 8.04037.623 1.009.81 ATOM 1354 C TRPL 148 18.339 11.61037.747 1.0010.55 ATOM 1355 0 TRPL 148 19.536 11.57037.449 1.0011.66 ATOM 1356 N LYSL 149 17.912 12.10738.895 1.0010.12 ATOM 1358 CA LYSL 149 18.860 12.58639.861 1.0010.24 ATOM 1359 CB LYSL 149 18.984 14.11739.736 1.009.85 ATOM 1360 CG LYS L 149 19.865 14.47738.528 1.0015.84 ATOM 1361 CD LYSL 149 19.782 15.92938.126 1.0020.45 ATOM 1362 CE LYSL 149 20.998 16.333 37.272 1.0025.03 ATOM 1363 NZ LYSL 149 21.311 15.34436.170 1.0026.83 ATOM 1367 C LYSL 149 18.493 1 2.11441.261 1.009.83 ATOM 1368 O LYSL 149 17.327 11.93941.568 1.008.42 ATOM 1369 N VALL 150 19.529 11.821 42.045 1.0012.70 ATOM 1371 CA VALL 150 19.363 11.40043.445 1.0013.13 ATOM 1372 CB VALL 150 19.874 9.95843.597 1.0014.08 ATOM 1373 CGI VALL 150 20.311 9.69045.000 1.009.65 ATOM 1374 CG2 VALL 150 18.760 8.99043.198 1.0012.12 ATOM 1375 C VALL 150 20.137 12.35744.381 1.0013.82 ATOM 1376 O VALL 150 21.379 12.391 44.371 1.0011.33 ATOM 1377 N ASPL 151 19.393 13.15645.184 1.0015.72 ATOM 1379 CA ASPL 151 20.020 14.16646.056 1.0013.64 ATOM 1380 CB ASPL 151 20.884 13.51647.141 1.0017.87 ATOM 1381 CG ASPL 151 20.085 12.90848.292 1.0018.72 ATOM 1382 OD1 ASPL 151 18.851 13.01448.304 1.0017.99 ATOM 1383 OD2ASPL 151 20.701 12.32049.195 1.0020.12 ATOM 1384 C ASPL 151 20.841 15.10745.202 1.0012.12 ATOM 1385 O ASPL 151 21.967 15.54645.535 1.0014.72 ATOM 1386 N GLYL 152 20.285 15.373 44.070 1.0013.53 ATOM 1388 CA GLYL 152 20.889 16.31343.159 1.0015.70 ATOM 1389 C GLYL 152 21.951 15.74542.250 1.0016.31 ATOM 1390 O GLYL 152 22.364 16.42441.322 1.0017.83 ATOM 1391 N THRL 153 22.399 14.51542.476 1.0018.56 ATOM 1393 CA THRL 153 23.473 13.95841.634 1.0018.43 ATOM 1394 CB THRL 153 24.498 13.19042.480 1.0019.60 ATOM 1395 OG1 THRL 153 23.896 12.01243.019 1.0025.85 ATOM 1397 CG2 THRL 153 24.964 14.05543.650 1.0023.47 ATOM 1398 C THRL 153 22.904 13.09440.482 1.0018.68 ATOM 1399 O THRL 153 21.899 12.39340.614 1.0018.23 ATOM 1400 N PROL 154 23.516 13.173 39.299 1.0018.73 ATOM 1401 CD PROL 154 24.730 13.96738.997 1.0019.95 ATOM 1402 CA PROL 154 23.038 12.42438.120 1.0018.94 ATOM 1403 CB PROL 154 23.865 13.03036.987 1.0018.59 ATOM 1404 CG PROL 154 25.150 13.36037.688 1.0018.89 ATOM 1405 C PRO L 154 23.196 10.91438.253 1.0015.33 ATOM 1406 O PROL 154 24.232 10.443 38.662 1.0016.30 ATOM 1407 N VALL 155 22.150 10.14737.978 1.0016.59 ATOM 1409 CA VAL L 155 22.323 8.703 38.040 1.0019.40 ATOM 1410 CB VALL 155 21.065 7.96238.617 1.0019.34 ATOM 1411 CGI VALL 155 20.124 8.94739.276 1.0018.37 ATOM 1412 CG2VALL 155 20.353 7.13237.558 1.0018.74 ATOM 1413 C VALL 155 22.760 8.141 36.641 1.0021.02 ATOM 1414 O VALL 155 22.397 8.681 35.565 1.0019.02 ATOM 1415 N THRL 156 23.606 7.121 36.664 1.0022.42 ATOM 1417 CA THRL 156 24.093 6.53235.438 1.0023.32 ATOM 1418 CB THRL 156 25.579 6.77035.317 1.0023.16 ATOM 1419 OG1 THRL 156 26.227 6.27636.494 1.0025.01 ATOM 1421 CG2 THR L 156 25.845 8.249 35.181 1.00 25.87 ATOM 1422 C THR L 156 23.858 5.049 35.421 1.00 25.17 ATOM 1423 O THR L 156 24.327 4.357 34.533 1.00 28.73 ATOM 1424 N GLN L 157 23.1 19 4.554 36.376 1.00 23.46 ATOM 1426 CA GLN L 157 22.909 3.152 36.465 1.00 23.50 ATOM 1427 CB GLN L 157 23.954 2.603 37.389 1.00 29.55 ATOM 1428 CG GLN L 157 24.032 1.102 37.399 1.00 37.55 ATOM 1429 CD GLN L 157 25.281 0.639 38.106 1.00 43.33 ATOM 1430 OE1 GLN L 157 25.750 1.288 39.060 1.00 43.65 ATOM 1431 NE2 GLN L 157 25.845 -0.472 37.631 1.00 45.54 ATOM 1434 C GLN L 157 21.525 2.871 36.994 1.00 19.92 ATOM 1435 O GLN L 157 21.025 3.631 37.778 1.00 18.81 ATOM 1436 N GLY L 158 20.895 1.817 36.526 1.00 18.99 ATOM 1438 CA GLY L 158 19.569 1.471 37.010 1.00 20.19 ATOM 1439 C GLY L 158 18.397 2.250 36.382 1.00 22.36 ATOM 1440 O GLY L 158 17.281 2.099 36.815 1.00 22.31 ATOM 1441 N MET L 159 18.630 3.080 35.374 1.00 24.81 ATOM 1443 CA MET L 159 17.539 3.802 34.741 1.00 22.88 ATOM 1444 CB MET L 159 17.810 5.312 34.684 1.00 23.15 ATOM 1445 CG MET L 159 18.833 5.795 33.687 1.00 26.34 ATOM 1446 SD MET L 159 20.522 5.748 34.304 1.00 34.44 ATOM 1447 CE MET L 159 21.030 4.165 33.643 1.00 31.53 ATOM 1448 C MET L 159 17.277 3.230 33.351 1.00 23.01 ATOM 1449 O MET L 159 18.188 2.833 32.662 1.00 24.49 ATOM 1450 N GLU L 160 16.026 3.169 32.960 1.00 19.49 ATOM 1452 CA GLU L 160 15.670 2.591 31.710 1.00 19.70 ATOM 1453 CB GLU L 160 15.366 1.107 31.939 1.00 21.50 ATOM 1454 CG GLU L 160 14.501 0.431 30.913 1.00 24.34 ATOM 1455 CD GLU L 160 15.230 0.049 29.644 1.00 30.12 ATOM 1456 OE1 GLU L 160 16.464 -0.184 29.733 1.00 28.32 ATOM 1457 OE2 GLU L 160 14.558 -0.021 28.551 1.00 30.69 ATOM 1458 C GLU L 160 14.491 3.326 31.156 1.00 19.64 ATOM 1459 O GLU L 160 13.446 3.366 31.785 1.00 18.31 ATOM 1460 N THR L 161 14.667 3.908 29.959 1.00 20.21 ATOM 1462 CA THR L 161 13.61 1 4.715 29.300 1.00 18.39 ATOM 1463 CB THR L 161 14.163 6.137 28.972 1.00 19.35 ATOM 1464 OG 1 THR L 161 14.627 6.741 30.188 1.00 15.43 ATOM 1466 CG2 THR L 161 13.107 7.025 28.342 1.00 13.84 ATOM 1467 C THR L 161 13.091 4.047 28.007 1.00 18.90 ATOM 1468 O THR L 161 13.859 3.391 27.292 1.00 18.53 AfOM 1469 N THR L 162 1 1.777 4.198 27.738 1.00 17.02 ATOM 1471 CA THR L 162 11.163 3.603 26.573 1.00 14.46 ATOM 1472 CB THR L 162 9.768 3.023 26.890 1.00 9.31 ATOM 1473 OG1 THR L 162 8.866 4.067 27.336 1.00 8.44 ATOM 1475 CG2 THR L 162 9.880 1.940 27.965 1.00 8.50 ATOM 1476 C THR L 162 1 1.085 4.614 25.421 1.00 15.09 ATOM 1477 O THR L 162 1 1.083 5.834 25.624 1.00 14.93 ATOM 1478 N ALA L 163 1 1.071 4.110 24.200 1.00 12.96 ATOM 1480 CA ALA L 163 1 1.054 4.983 23.052 1.00 10.76 ATOM 1481 CB ALA L 163 11.434 4.212 21.768 1.00 15.08 ATOM 1482 C ALA L 163 9.719 5.567 22.921 1.00 8.59 ATOM 1483 O ALA L 163 8.749 4.856 23.017 1.00 11.96 ATOM 1484 N PRO L 164 9.632 6.894 22.721 1.00 1 1.37 ATOM 1485 CD PRO L 164 10.762 7.849 22.597 1.00 12.89 ATOM 1486 CA PRO L 164 8.352 7.578 22.587 1.00 11.21 ATOM 1487 CB PRO L 164 8.746 8.956 22.069 1.00 1 1.04 ATOM 1488 CG PROL 164 10.047 9.16022.761 1.0011.07 ATOM 1489 C PROL 164 7.488 6.825 21.632 1.0012.84 ATOM 1490 O PROL 164 7.986 6.13020.746 1.0017.44 ATOM 1491 N SERL 165 6.221 6.87821.829 1.0014.17 ATOM 1493 CA SERL 165 5.334 6.18820.925 1.0016.08 ATOM 1494 CB SERL 165 4.889 4.81021.470 1.0017.01 ATOM 1495 OG SERL 165 3.841 4.92222.407 1.0022.35 ATOM 1497 C SERL 165 4.201 7.09920.724 1.0015.78 ATOM 1498 0 SERL 165 3.927 7.92021.584 1.0015.19 ATOM 1499 N LYS L 166 3.588 7.018 19.594 1.0017.84 ATOM 1501 CA LYSL 166 2.573 7.988 19.257 1.0019.88 ATOM 1502 CB LYS L 166 2.382 8.012 17.758 1.0022.34 ATOM 1503 CG LYSL 166 2.308 9.398 17.150 1.0021.36 ATOM 1504 CD LYS L 166 2.292 9.300 15.619 1.0025.05 ATOM 1505 CE LYS L 166 2.623 10.640 14.981 0.0122.27 ATOM 1506 NZ LYS L 166 2.568 10.579 13.495 0.0122.15 ATOM 1510 C LYSL 166 1.276 7.704 19.925 1.0021.48 ATOM 1511 O LYSL 166 0.893 6.54720.063 1.0023.82 ATOM 1512 N GLNL 167 0.614 8.77020.372 1.0020.46 ATOM 1514 CA GLNL 167 -0.716 8.65820.935 1.0019.43 ATOM 1515 CB GLNL 167 -0.983 9.72921.969 1.0019.09 ATOM 1516 CG GLN L 167 0.047 9.821 23.080 1.0013.91 ATOM 1517 CD GLNL 167 -0.193 10.99224.017 1.0012.43 ATOM 1518 OE1 GLNL 167 0.488 11.14525.066 1.0012.78 ATOM 1519 NE2 GLNL 167 -1.157 11.83423.670 1.0012.35 ATOM 1522 C GLN L 167 -1.702 8.865 19.814 1.0020.58 ATOM 1523 O GLNL 167 -1.347 9.393 18.782 1.0019.43 ATOM 1524 N SERL 168 -2.929 8.49420.029 1.0024.20 ATOM 1526 CA SERL 168 -3.955 8.647 19.009 1.0028.22 ATOM 1527 CB SERL 168 -5.305 8.283 19.615 1.0029.04 ATOM 1528 OG SERL 168 -5.428 8.88020.904 1.0034.62 ATOM 1530 C SERL 168 -3.996 10.085 18.468 1.0030.48 ATOM 1531 O SERL 168 -4.401 10.335 17.308 1.0034.63 ATOM 1532 N ASNL 169 -3.579 11.035 19.279 1.0026.12 ATOM 1534 CA ASN L 169 -3.644 12.398 18.848 1.0025.93 ATOM 1535 CB ASNL 169 -4.066 13.329 19.982 1.0029.63 ATOM 1536 CG ASN L 169 -3.125 13.38621.158 1.0029.04 ATOM 1537 OD1 ASNL 169 -2.107 12.70421.219 1.0031.37 ATOM 1538 ND2 ASNL 169 -3.479 14.21422.099 1.0031.92 ATOM 1541 C ASNL 169 -2.351 12.815 18.283 1.0025.86 ATOM 15420 ASNL 169 -2.052 13.991 18.186 1.0026.70 ATOM 1543 N ASNL 170 -1.578 11.847 17.927 1.0023.96 ATOM 1545 CA ASN L 170 -0.314 12.085 17.286 1.0023.68 ATOM 1546 CB ASNL 170 -0.543 12.718 15.919 1.0025.27 ATOM 1547 CG ASN L 170 -1.095 11.647 14.987 1.0028.14 ATOM 1548 OD1 ASNL 170 -0.390 10.682 14.651 1.0030.35 ATOM 1549 ND2 ASN LI 70 -2.362 11.765 14.614 1.0029.66 ATOM 1552 C ASNL 170 0.690 12.837 18.108 1.0022.90 ATOM 1553 O ASNL 170 1.720 13.248 17.607 1.0025.60 ATOM 1554 N LYSL 171 0.407 13.049 19.361 1.0021.22 ATOM 1556 CA LYS L 171 1.452 13.52420.244 1.0019.04 ATOM 1557 CB LYSL 171 0.888 14.29621.429 1.0017.22 ATOM 1558 CG LYSL 171 0.207 15.595 21.112 1.0017.62 ATOM 1559 CD LYS L 171 -0.340 16.19822.407 1.0015.11 ATOM 1560 CE LYSL 171 -1.277 17.35822.132 1.0018.27 ATOM 1561 NZ LYS L 171 -1.526 18.18723.347 1.0014.34 ATOM 1565 C LYSL 171 2.140 12.24720.744 1.0017.36 ATOM 1566 O LYSL 171 1.728 1 11.15620.373 1.0017.98 ATOM 1567 N TYRL 172 3.132 12.353 21.586 1.0014.79 ATOM 1569 CA TYRL 172 3.863 11.17821.976 1.0014.85 ATOM 1570 CB TYRL 172 5.301 11.331 21.516 1.0015.82 ATOM 1571 CG TYRL 172 5.451 11.261 20.022 1.0017.24 ATOM 1572 CD 1 TYRL 172 5.218 12.372 19.196 1.0015.15 ATOM 1573 CE1 TYRL 172 5.377 12.281 17.812 1.0018.45 ATOM 1574 CD2 TYRL 172 5.836 10.071 19.427 1.0017.80 ATOM 1575 CE2TYRL 172 5.995 9.974 18.053 1.0020.12 ATOM 1576 CZ TYRL 172 5.773 11.070 17.242 1.0018.23 ATOM 1577 OH TYRL 172 5.968 10.945 15.874 1.0013.35 ATOM 1579 C TYRL 172 3.838 10.90723.461 1.0015.41 ATOM 1580 O TYRL 172 3.585 11.82024.271 1.0014.17 ATOM 1581 N METL 173 4.111 9.63923.811 1.0013.34 ATOM 1583 CA METL 173 4.195 9.241 25.192 1.009.55 ATOM 1584 CB METL 173 2.927 8.49825.600 1.0010.24 ATOM 1585 CG METL 173 2.767 7.121 24.973 1.0015.16 ATOM 1586 SD METL 173 1.450 6.14925.719 1.0020.11 ATOM 1587 CE METL 173 0.045 6.91024.992 1.0012.86 ATOM 1588 C METL 173 5.455 8.38625.429 1.0010.38 ATOM 1589 O METL 173 6.005 7.77824.500 1.0010.40 ATOM 1590 N ALAL 174 5.935 8.35426.658 1.007.39 ATOM 1592 CA ALAL 174 7.131 7.59427.005 1.007.66 ATOM 1593 CB ALAL 174 8.410 8.32526.532 1.004.47 ATOM 1594 C ALAL 174 7.164 7.38328.521 1.008.50 ATOM 1595 O ALA L 174 6.371 7.983 29.240 1.007.42 ATOM 1596 N SERL 175 8.055 6.51928.984 1.008.85 ATOM 1598 CA SERL 175 8.163 6.231 30.404 1.009.69 ATOM 1599 CB SERL 175 7.275 5.031 30.782 1.008.09 ATOM 1600 OG SERL 175 7.633 3.83830.073 1.0012.41 ATOM 1602 C SERL 175 9.606 5.94930.777 1.0010.11 ATOM 1603 O SERL 175 10.408 5.513 29.919 1.009.58 ATOM 1604 N SERL 176 9.975 6.223 32.048 1.006.07 ATOM 1606 CA SERL 176 11.313 5.91832.495 1.003.46 ATOM 1607 CB SERL 176 12.179 7.15232.471 1.002.00 ATOM 1608 OG SERL 176 13.547 6.85232.684 1.002.00 ATOM 1610 C SERL 176 11.221 5.30533.892 1.005.39 ATOM 1611 O SERL 176 10.237 5.48734.558 1.007.78 ATOM 1612 N TYRL 177 12.212 4.513 34.237 1.006.76 ATOM 1614 CA TYRL 177 12.235 3.75835.455 1.008.12 ATOM 1615 CB TYRL 177 12.051 2.273 35.151 1.006.07 ATOM 1616 CG TYRL 177 10.695 1.871 34.600 1.006.17 ATOM 1617 CD1 TYRL 177 9.630 1.57735.457 1.006.94 ATOM 1618 CE1 TYRL 177 8.371 1.231 34.938 1.008.14 ATOM 1619 CD2 TYRL 177 10.461 1.79933.224 1.006.52 ATOM 1620 CE2 TYR LI 77 9.212 1.45932.716 1.007.03 ATOM 1621 CZ TYRL 177 8.169 1.17833.568 1.006.45 ATOM 1622 OH TYR LI 77 6.901 0.89433.061 1.006.11 ATOM 1624 C TYRL 177 13.560 3.88636.100 1.006.87 ATOM 1625 O TYRL 177 14.563 3.83635.428 1.009.13 ATOM 1626 N LEU L 178 13.558 4.03437.400 1.006.48 ATOM 1628 CA LEU L 178 14.761 3.993 38.156 1.006.11 ATOM 1629 CB LEU L 178 14.999 5.31238.847 1.006.46 ATOM 1630 CG LEU L 178 16.228 5.44839.722 1.007.03 ATOM 1631 CD1 LEU L 178 17.496 5.055 38.993 1.0010.30 ATOM 1632 CD2 LEU L 178 16.308 6.878 40.219 1.00 13.82 ATOM 1633 C LEU L 178 14.618 2.885 39.156 1.00 8.35 ATOM 1634 0 LEU L 178 13.687 2.862 39.902 1.00 10.42 ATOM 1635 N THR L 179 15.550 1.969 39.130 1.00 1 1.56 ATOM 1637 CA THR L 179 15.522 0.802 39.963 1.00 13.47 ATOM 1638 CB THR L 179 15.703 -0.456 39.096 1.00 15.12 ATOM 1639 OG 1 THR 179 14.558 -0.594 38.292 1.00 14.73 ATOM 1641 CG2 THR L 179 15.847 - 1.722 39.940 1.00 19.56 ATOM 1642 C THR L 179 16.613 0.903 41.008 1.00 16.41 ATOM 1643 O THR L 179 17.808 1.133 40.693 1.00 15.41 ATOM 1644 N LEU L 180 16.177 0.755 42.248 1.00 16.98 ATOM 1646 CA LEU L 180 17.021 0.929 43.383 1.00 17.38 ATOM 1647 CB LEU L 180 16.614 2.210 44.155 1.00 17.62 ATOM 1648 CG LEU L 180 16.667 3.566 43.424 1.00 18.66 ATOM 1649 CD1 LEU L 180 16.074 4.662 44.300 1.00 15.82 ATOM 1650 CD2 LEU L 180 18.108 3.926 43.067 1.00 19.60 ATOM 1651 C LEU L 180 16.793 -0.217 44.300 1.00 15.89 ATOM 1652 O LEU L 180 15.742 -0.853 44.241 1.00 20.00 ATOM 1653 N THR L 181 17.766 -0.482 45.130 1.00 16.39 ATOM 1655 CA THR L 181 17.562 -1.407 46.238 1.00 16.84 ATOM 1656 CB THR L 181 18.888 -1.803 46.924 1.00 15.01 ATOM 1657 OGI THR L 181 19.566 -0.615 47.398 1.00 18.96 ATOM 1659 CG2 THR L 181 19.791 -2.578 45.975 1.00 16.62 ATOM 1660 C THR L 181 16.753 -0.634 47.265 1.00 14.44 ATOM 1661 O THR L 181 16.705 0.607 47.201 1.00 16.04 ATOM 1662 N ALA L 182 16.120 -1.307 48.192 1.00 15.12 ATOM 1664 CA ALA L 182 15.421 -0.582 49.249 1.00 13.02 ATOM 1665 CB ALA L 182 14.687 -1.564 50.157 1.00 13.78 ATOM 1666 C ALA L 182 16.427 0.289 50.076 1.00 14.39 ATOM 1667 O ALA L 182 16.11 1 1.422 50.478 1.00 16.28 ATOM 1668 N ARG L 183 17.645 -0.219 50.307 1.00 14.52 ATOM 1670 CA ARG L 183 18.623 0.535 51.069 1.00 16.24 ATOM 1671 CB ARG L 183 19.894 -0.287 51.295 1.00 19.45 ATOM 1672 CG ARG L 183 21.080 0.527 51.825 1.00 24.50 ATOM 1673 CD ARG L 183 22.102 -0.351 52.538 1.00 29.62 ATOM 1674 NE ARG L 183 23.465 0.263 52.582 1.00 35.27 ATOM 1676 CZ ARG L 183 24.403 -0.026 53.535 1.00 35.81 ATOM 1677 NH1 ARG L 183 25.633 0.509 53.470 1.00 35.30 ATOM 1680 NH2 ARG L 183 24.098 -0.817 54.555 1.00 36.43 ATOM 1683 C ARG L 183 18.930 1.869 50.400 1.00 18.26 ATOM 1684 O ARG L 183 18.887 2.903 51.049 1.00 19.19 ATOM 1685 N ALA L 184 19.195 1.857 49.091 1.00 16.18 ATOM 1687 CA ALA L 184 19.460 3.076 48.392 1.00 10.91 ATOM 1688 CB ALA L 184 19.774 2.735 46.955 1.00 9.98 ATOM 1689 C ALA L 184 18.248 4.012 48.496 1.00 12.19 ATOM 1690 O ALA L 184 18.383 5.227 48.667 1.00 11.01 ATOM 1691 N TRP L 185 17.057 3.453 48.408 1.00 10.53 ATOM 1693 CA TRP L 185 15.851 4.264 48.467 1.00 11.80 ATOM 1694 CB TRP L 185 14.630 3.391 48.243 1.00 1 1.64 ATOM 1695 CG TRP L 185 13.402 4.062 48.687 1.00 9.64 ATOM 1696 CD2 TRP L 185 12.818 5.261 48.138 1.00 14.47 ATOM 1697 CE2 TRP L 185 1 1.622 5.500 48.840 1.00 14.89 ATOM 1698 CE3 TRP L 185 13.177 6.149 47.109 1.00 14.90 ATOM 1699 CD1 TRP L 185 12.572 3.639 49.683 1.00 15.33 ATOM 1700 NE1 TRP L 185 11.511 4.503 49.757 1.00 15.12 ATOM 1702 CZ2 TRP L 185 10.783 6.583 48.556 1.00 15.58 ATOM 1703 CZ3 TRP L 185 12.349 7.209 46.821 1.00 12.52 ATOM 1704 CH2 TRP L 185 1 1.162 7.419 47.544 1.00 12.84 ATOM 1705 C TRP L 185 15.693 5.024 49.798 1.00 16.85 ATOM 1706 O TRP L 185 15.351 6.222 49.809 1.00 15.42 ATOM 1707 N GLU L 186 15.942 4.343 50.918 1.00 16.92 ATOM 1709 CA GLU L 186 15.757 4.979 52.223 1.00 19.08 ATOM 1710 CB GLU L 186 15.767 3.927 53.332 1.00 21.77 ATOM 171 1 CG GLU L 186 14.962 2.655 53.073 1.00 25.99 ATOM 1712 CD GLU L 186 15.288 1.566 54.1 10 0.50 26.59 ATOM 1713 OE1 GLU L 186 16.183 1.799 54.944 0.50 23.57 ATOM 1714 OE2 GLU L 186 14.663 0.485 54.086 0.50 23.36 ATOM 1715 C GLU L 186 16.871 5.975 52.537 1.00 20.25 ATOM 1716 O GLU L 186 16.733 6 6..882244 5 533..442211 1 1..0000 2200..9911 ATOM 1717 N ARG L 187 17.991 5 5..885522 5 511..886611 1 1..0000 1188..9944 ATOM 1719 CA ARG L 187 19.129 6 6..665511 5 522..221166 1 1..0000 1188..5588 ATOM 1720 CB ARG L 187 20.376 5 5..994499 5 511..776600 1 1..0000 2200..9966 ATOM 1721 CG ARG L 187 21.574 6 6..884488 ; 5511..770022 1 1..0000 2277..2244 ATOM 1722 CD ARG L 187 22.687 6 6..115566 ι 5500..997722 1 1..0000 3366..9911 ATOM 1723 NE ARG L 187 23.339 5 5..114466 ■ 5511..779933 1 1..0000 3399..3366 ATOM 1725 CZ ARG L 187 24.660 5 5..003322 5 511..883344 1 1..0000 4422..5544 ATOM 1726 NH1 ARG L 187 25.231 4 4..11224 4 5522..66007' 7 11..0000 4455..4477 ATOM 1729 NH2 ARG L 187 25.415 i 5.827 51.08 1 1.0046.06 ATOM 1732 C ARG L 187 19.089 8.077 51.671 1.00 18.28 ATOM 1733 O ARG L 187 19.798 8.946 52.176 1.00 20.00 ATOM 1734 N HIS L 188 18.281 8.333 50.647 1.00 17.48 ATOM 1736 CA HIS L 188 18.247 9.674 50.027 1.00 16.15 ATOM 1737 CB HIS L 188 1 188..555599 9.585 48.486 1 1..0000 1133..4422 ATOM 1738 CG HIS L 188 1 199..888800 8.962 48.214 11..0000 1144..3377 ATOM 1739 CD2 HIS L 188 2 200..226677 7.658 48.229 11..0000 1155..0011 ATOM 1740 ND1 HIS L 188 2 211..006600 9.680 48.221 11..0000 1144..9955 ATOM 1742 CE1 HIS L 188 2 222..11 1188 8.897 48.281 11..0000 1133..9988 ATOM 1743 NE2 HIS L 188 2 211..664466 7.663 48.299 11..0000 1155..8866 ATOM 1745 C HIS L 188 16.893 10.318 50.255 1.00 16.60 ATOM 1746 O HIS L 188 15.897 9.614 50.431 1.00 18.56 ATOM 1747 N SER L 189 16.855 1 1.660 50.285 1.00 18.06 ATOM 1749 CA SER L 189 15.587 12.384 50.467 1.00 17.30 ATOM 1750 CB SER L 189 15.790 13.568 51.425 1.00 20.51 ATOM 1751 OG SER L 189 16.943 14.314 51.086 1.00 18.48 ATOM 1753 C SER L 189 15.038 12.891 49.144 1.00 18.08 ATOM 1754 O SER L 189 13.827 12.891 48.917 1.00 21.50 ATOM 1755 N SER L 190 15.942 13.272 48.248 1.00 17.95 ATOM 1757 CA SER L 190 15.557 13.876 46.968 1.00 17.18 ATOM 1758 CB SER L 190 16.428 15.100 46.714 1.00 14.84 ATOM 1759 OG SER L 190 15.884 15.885 45.679 1.00 24.95 ATOM 1761 C SER L 190 15.684 12.922 45.798 1.00 15.72 ATOM 1762 O SER L 190 16.726 12.282 45.606 1.00 16.39 ATOM 1763 N TYR L 191 14.629 12.845 45.031 1.00 15.74 ATOM 1765 CA TYR L 191 14.623 12.054 43.793 1.00 18.47 ATOM 1766 CB TYR L 191 13.878 10.730 44.016 1.00 20.26 ATOM 1767 CG TYR L 191 14.562 9.836 45.023 1.00 20.87 ATOM 1768 CD1 TYR L 191 15.601 9.008 44.61 1 1.00 23.39 ATOM 1769 CE1 TYR L 191 16.300 8.219 45.503 1.00 22.95 ATOM 1770 CD2 TYR L 191 14.217 9.856 46.395 1.00 24.18 ATOM 1771 CE2 TYR L 191 14.919 9.060 47.302 1.00 26.25 ATOM 1772 CZ TYR L 191 15.972 8.245 46.835 1.00 26.73 ATOM 1773 OH TYR L 191 16.740 7.505 47.709 1.00 30.08 ATOM 1775 C TYRL 191 13.939 12.88042.683 1.0017.55 ATOM 1776 O TYRL 191 12.923 13.50542.929 1.0014.74 ATOM 1777 N SER L 192 14.477 12.88341.464 1.0016.33 ATOM 1779 CA SERL 192 13.909 13.741 40.451 1.0015.90 ATOM 1780 CB SERL 192 14.734 15.031 40.432 1.0018.03 ATOM 1781 OG SERL 192 14.167 15.951 39.536 1.0023.10 ATOM 1783 C SERL 192 13.938 13.135 39.071 1.0012.29 ATOM 1784 O SERL 192 14.958 12.641 38.661 1.0014.68 ATOM 1785 N CYS L 193 12.839 13.20838.359 1.0011.59 ATOM 1787 CA CYS L 193 12.832 12.81736.950 1.0014.23 ATOM 1788 CB CYSL 193 11.604 11.98536.621 1.0015.78 ATOM 1789 SG CYS L 193 11.540 11.36034.913 1.0015.09 ATOM 1790 C CYSL 193 12.834 14.075 36.093 1.0012.46 ATOM 1791 O CYSL 193 11.918 14.86736.192 1.0014.42 ATOM 1792 N GLN L 194 13.849 14.261 35.247 1.0014.04 ATOM 1794 CA GLNL 194 13.936 15.485 34.450 1.0014.30 ATOM 1795 CB GLNL 194 15.225 16.20934.730 1.0020.47 ATOM 1796 CG GLN L 194 15.471 16.453 36.182 1.0026.89 ATOM 1797 CD GLN L 194 16.704 17.28236.393 1.0033.09 ATOM 1798 OE1 GLNL 194 16.913 17.828 37.488 1.0036.67 ATOM 1799 NE2 GLNL 194 17.538 17.39235.352 1.0036.22 ATOM 1802 C GLNL 194 13.873 15.20032.978 1.0013.96 ATOM 1803 O GLNL 194 14.730 14.52632.449 1.0011.43 ATOM 1804 N VALL 195 12.867 15.763 32.335 1.0013.39 ATOM 1806 CA VALL 195 12.608 15.511 30.936 1.0015.15 ATOM 1807 CB VALL 195 11.165 15.065 30.770 1.0013.26 ATOM 1808 CGI VALL 195 10.866 14.80729.311 1.0012.28 ATOM 1809 CG2 VALL 195 10.902 13.83931.643 1.008.74 ATOM 1810 C VALL 195 12.823 16.76430.072 1.0016.35 ATOM 1811 O VALL 195 12.012 17.70230.111 1.0015.34 ATOM 1812 N THRL 196 13.904 16.76329.295 1.0016.92 ATOM 1814 CA THRL 196 14.192 17.87628.379 1.0015.93 ATOM 1815 CB THRL 196 15.716 17.99228.176 1.0018.12 ATOM 1816 OGITHRL 196 16.349 18.183 29.443 1.0022.55 ATOM 1818 CG2 THRL 196 16.071 19.15627.273 1.0021.24 ATOM 1819 C THRL 196 13.507 17.64727.035 1.0016.18 ATOM 1820 O THRL 196 13.746 16.59826.400 1.0014.99 ATOM 1821 N HIS L 197 12.638 18.62526.619 1.0014.43 ATOM 1823 CA HIS L 197 11.923 18.56325.348 1.0013.60 ATOM 1824 CB HIS L 197 10.429 18.34525.566 1.0012.56 ATOM 1825 CG HIS L 197 9.581 18.33624.308 1.009.47 ATOM 1826 CD2 HISL 197 9.549 17.47923.275 1.008.75 ATOM 1827 ND1 HISL 197 8.492 19.191 24.088 1.0013.69 ATOM 1829 CE1 HISL 197 7.842 18.87322.994 1.0010.65 ATOM 1830 NE2 HISL 197 8.472 17.84222.506 1.0013.24 ATOM 1832 C HIS L 197 12.084 19.88224.607 1.0019.15 ATOM 1833 O HIS L 197 11.393 20.88224.950 1.0021.46 ATOM 1834 N GLUL 198 12.900 19.86523.560 1.0019.88 ATOM 1836 CA GLU L 198 13.18021.05822.766 1.0023.30 ATOM 1837 CB GLUL 198 11.89921.64222.147 1.0025.45 ATOM 1838 CG GLU L 198 11.07620.681 21.322 1.0025.96 ATOM 1839 CD GLU L 198 11.42520.689 19.856 1.0029.67 ATOM 1840 OE1 GLUL 198 12.387 19.979 19.468 1.0031.64 ATOM 1841 OE2GLUL198 10.72521.393 19.086 1.0027.15 ATOM 1842 C GLU L 198 13.83422.12623.630 1.0025.19 ATOM 1843 O GLUL 198 13.36623.251 23.670 1.0025.37 ATOM 1844 N GLY L 199 14.863 21.74224.369 1.0026.71 ATOM 1846 CA GLYL 199 15.63622.70925.110 1.0028.67 ATOM 1847 C GLYL 199 15.01923.191 26.406 1.0030.20 ATOM 1848 O GLY L 199 15.62324.02827.078 1.0031.36 ATOM 1849 N HIS L 200 13.825 22.693 26.755 1.0029.31 ATOM 1851 CA HISL 200 13.16823.10827.996 1.0029.70 ATOM 1852 CB HISL 200 11.79323.76627.747 1.0034.13 ATOM 1853 CG HIS L 200 11.62024.41026.399 1.0042.18 ATOM 1854 CD2 HISL 200 12.51724.95225.533 1.0044.52 ATOM 1855 ND1 HISL 200 10.401 24.45625.729 1.0045.60 ATOM 1857 CE1 HISL200 10.53724.971 24.507 1.0046.26 ATOM 1858 NE2 HISL 200 11.811 25.27424.385 1.0046.19 ATOM 1860 C HISL 200 12.96021.88828.849 1.0027.60 ATOM 1861 O HISL 200 12.33520.92728.385 1.0027.65 ATOM 1862 N THRL 201 13.45721.938 30.084 1.0027.03 ATOM 1864 CA THRL 201 13.37220.79630.993 1.0025.96 ATOM 1865 CB THRL 201 14.63520.73231.874 1.0022.54 ATOM 1866 OG1 THRL 201 15.75820.71031.032 1.0021.22 ATOM 1868 CG2 THRL 201 14.693 19.47732.724 1.0022.94 ATOM 1869 C THRL 201 12.10820.84631.863 1.0026.78 ATOM 1870 O THRL 201 11.84721.85732.522 1.0029.53 ATOM 1871 N VAL L 202 11.279 19.77731.789 1.0025.81 ATOM 1873 CA VALL 202 10.124 19.623 32.694 1.0022.79 ATOM 1874 CB VALL 202 8.881 19.13831.929 1.0024.16 ATOM 1875 CGI VALL 202 7.668 19.06732.862 1.0024.52 ATOM 1876 CG2 VALL 202 8.61220.091 30.773 1.0024.14 ATOM 1877 C VAL L 202 10.507 18.59833.784 1.0021.74 ATOM 1878 O VALL 202 10.960 17.51933.480 1.0019.01 ATOM 1879 N GLUL 203 10.340 18.93435.055 1.0020.40 ATOM 1881 CA GLUL 203 10.807 18.063 36.086 1.0019.67 ATOM 1882 CB GLU L 203 12.045 18.70036.717 1.0022.14 ATOM 1883 CG GLUL 203 12.600 17.91937.883 1.0027.78 ATOM 1884 CD GLUL 203 13.320 18.803 38.8860.5030.15 ATOM 1885 OE1 GLUL 203 14.564 18.93438.7770.5030.52 ATOM 1886 OE2 GLUL 203 12.636 19.36939.785 0.5030.93 ATOM 1887 C GLU L 203 9.760 17.75437.162 1.0018.69 ATOM 1888 O GLU L 203 8.894 18.56937.477 1.0019.41 ATOM 1889 N LYSL 204 9.814 16.55037.679 1.0016.36 ATOM 1891 CA LYS L 204 9.046 16.21038.837 1.0014.59 ATOM 1892 CB LYSL 204 7.953 15.26238.527 1.0015.55 ATOM 1893 CG LYSL 204 6.869 15.915 37.724 1.0021.54 ATOM 1894 CD LYSL 204 6.405 17.16638.415 1.0021.69 ATOM 1895 CE LYSL 204 5.248 17.76637.666 1.0022.39 ATOM 1896 NZ LYSL 204 4.040 16.96237.885 1.0020.85 ATOM 1900 C LYSL 204 9.977 15.621 39.853 1.0015.55 ATOM 1901 O LYSL204 11.004 14.995 39.505 1.0013.34 ATOM 1902 N SERL205 9.650 15.85241.124 1.0017.28 ATOM 1904 CA SERL205 10.512 15.42842.198 1.0016.96 ATOM 1905 CB SERL 205 11.296 16.62242.760 1.0018.69 ATOM 1906 OG SERL 205 12.404 16.97241.916 1.0025.46 ATOM 1908 C SERL205 9.722 14.82643.299 1.0016.29 ATOM 1909 O SERL 205 8.568 15.11743.445 1.0012.40 ATOM 1910 N LEUL206 10.389 13.96744.035 1.0017.28 ATOM 1912 CA LEUL206 9.856 13.36045.233 1.0020.60 ATOM 1913 CB LEUL206 9.911 11.82545.136 1.0018.66 ATOM 1914 CG LEUL206 9.048 11.16044.061 1.0017.51 ATOM 1915 CD1 LEUL 206 9.516 9.73843.844 1.0019.23 ATOM 1916 CD2 LEU L 206 7.572 11.19244.444 1.0016.04 ATOM 1917 C LEUL 206 10.746 13.77646.393 1.0022.29 ATOM 1918 O LEUL 206 11.965 13.81246.254 1.0020.72 ATOM 1919 N SERL 207 10.140 14.15547.487 1.0026.92 ATOM 1921 CA SERL 207 10.896 14.35548.713 1.0033.08 ATOM 1922 CB SERL 207 10.498 15.64049.434 1.0032.95 ATOM 1923 OG SERL 207 11.247 15.78750.628 1.0035.61 ATOM 1925 C SERL 207 10.579 13.15749.602 1.0035.86 ATOM 1926 O SERL 207 9.404 12.76049.734 1.0038.31 ATOM 1927 N ARGL 208 11.601 12.563 50.163 1.0036.32 ATOM 1929 CA ARGL 208 11.422 11.391 50.979 1.0036.19 ATOM 1930 CB ARGL 208 12.255 10.23050.361 1.0033.25 ATOM 1931 CG ARGL 208 11.930 8.86050.912 1.0031.97 ATOM 1932 CD ARG L 208 13.184 8.10751.300 1.0032.82 ATOM 1933 NE ARG L 208 13.021 7.32952.540 1.0037.28 ATOM 1935 CZ ARG L 208 13.846 7.47853.597 1.0043.16 ATOM 1936 NH1 ARGL 208 13.703 6.735 54.711 1.0043.30 ATOM 1939 NH2 ARG L 208 14.811 8.395 53.547 1.0045.46 ATOM 1942 C ARG L 208 11.840 11.77952.420 1.0037.35 ATOM 1943 OT1 ARG L 208 12.794 11.173 52.989 1.0038.30 ATOM 1944 OT2 ARG L 208 11.231 12.763 52.940 1.0037.56 ATOM 1945 CB ALAH 1 -0.820 -5.033 -4.579 1.0035.02 ATOM 1946 C ALAH 1 1.166 -6.495 -4.905 1.0032.62 ATOM 1947 O ALAH 1 0.782 -7.582 -4.499 1.0032.59 ATOM 1950 N ALAH 1 -0.539 -6.302 -6.690 1.0037.70 ATOM 1952 CA ALAH 1 0.184 -5.565 -5.595 1.0034.79 ATOM 1953 N VALH 2 2.419 -6.048 -4.790 1.0029.87 ATOM 1955 CA VALH 2 3.463 -6.829 -4.153 1.0028.68 ATOM 1956 CB VALH 2 4.803 -6.111 -4.242 1.0027.24 ATOM 1957 CGI VALH 2 5.901 -6.933 -3.589 1.0030.14 ATOM 1958 CG2VALH 2 5.116 -5.835 -5.701 1.0030.41 ATOM 1959 C VALH 2 3.149 -7.059 -2.701 1.0027.59 ATOM 1960 O VALH 2 2.553 -6.216 -2.033 1.0027.26 ATOM 1961 N GLNH 3 3.531 -8.199 -2.220 1.0025.47 ATOM 1963 CA GLNH 3 3.343 -8.497 -0.838 1.0024.24 ATOM 1964 CB GLNH 3 1.917 -9.019 -0.574 1.0026.56 ATOM 1965 CG GLNH 3 1.653 -9.370 0.912 1.0033.26 ATOM 1966 CD GLN H 3 0.397-10.222 1.180 1.0038.06 ATOM 1967 OE1 GLN H 3 0.071 -11.150 0.423 1.0040.20 ATOM 1968 NE2GLNH 3 -0.306 -9.919 2.289 1.0038.60 ATOM 1971 C GLNH 3 4.357 -9.524 -0.384 1.0021.45 ATOM 1972 O GLNH 3 4.500-10.565 -1.013 1.0022.59 ATOM 1973 N LEUH 4 5.102 -9.185 0.652 1.0019.37 ATOM 1975 CA LEUH 4 5.999-10.140 1.312 1.0016.61 ATOM 1976 CB LEUH 4 7.398 -9.539 1.501 1.0013.50 ATOM 1977 CG LEUH 4 8.171 -9.234 0.201 1.008.19 ATOM 1978 CD1 LEU H 4 9.498 -8.580 0.509 1.003.80 ATOM 1979 CD2LEUH 4 8.404-10.519 -0.575 1.008.33 ATOM 1980 C LEUH 4 5.379-10.490 2.673 1.0015.88 ATOM 1981 O LEUH 4 4.921 -9.604 3.387 1.0015.82 ATOM 1982 N GLNH 5 5.342-11.758 3.027 1.0014.17 ATOM 1984 CA GLNH 5 4.665-12.158 4.271 1.0015.42 ATOM 1985 CB GLNH 5 3.297-12.694 3.909 1.0016.35 ATOM 1986 CG GLNH 5 2.309-12.889 5.034 1.0022.48 ATOM 1987 CD GLN H 5 1.010-13.514 4.506 1.0029.57 ATOM 1988 OE1 GLNH 5 0.404-14.362 5.167 1.0035.66 ATOM 1989 NE2 GLN H 5 0.575-13.126 3.295 1.0031.58 ATOM 1992 C GLNH 5 5.480-13.205 5.006 1.0013.97 ATOM 1993 O GLNH 5 5.597-14.352 4.546 1.009.52 ATOM 1994 N GLUH 6 6.070-12.798 6.134 1.0013.08 ATOM 1996 CA GLU H 6 6.934-13.696 6.901 1.009.47 ATOM 1997 CB GLUH 6 7.857-12.941 7.828 1.009.95 ATOM 1998 CG GLU H 6 8.818-12.002 7.134 1.009.95 ATOM 1999 CD GLUH 6 8.227-10.652 6.796 1.00 5.17 ATOM 2000 OE1 GLUH 6 9.024 -9.769 6.455 1.008.80 ATOM 2001 OE2 GLU H 6 6.969-10.462 6.840 1.004.90 ATOM 2002 C GLUH 6 6.109-14.632 7.730 1.0012.71 ATOM 2003 O GLUH 6 4.908-14.417 7.907 1.0013.94 ATOM 2004 N SERH 7 6.772-15.648 8.266 1.0013.48 ATOM 2006 CA SERH 7 6.122-16.647 9.092 1.0013.96 ATOM 2007 CB SERH 7 5.433-17.672 8.201 1.0015.10 ATOM 2008 OG SERH 7 4.111 -17.308 8.015 1.0023.26 ATOM 2010 C SERH 7 7.122-17.398 9.914 1.0012.29 ATOM 2011 O SERH 7 8.286-17.424 9.582 1.0013.84 ATOM 2012 N GLYH 8 6.633-18.079 10.951 1.0012.53 ATOM 2014 CA GLYH 8 7.470-19.010 11.664 1.0010.51 ATOM 2015 C GLYH 8 8.102-18.466 12.905 1.0012.14 ATOM 2016 O GLYH 8 8.796-19.199 13.565 1.0016.56 ATOM 2017 N GLYH 9 7.891 -17.195 13.244 1.0010.59 ATOM 2019 CA GLYH 9 8.519-16.693 14.462 1.0014.05 ATOM 2020 C GLYH 9 7.917-17.287 15.762 1.0016.57 ATOM 2021 O GLYH 9 6.760-17.790 15.781 1.0017.72 ATOM 2022 N GLYH 10 8.670-17.207 16.848 1.0016.58 ATOM 2024 CA GLYH 10 8.148-17.666 18.134 1.0015.33 ATOM 2025 C GLYH 10 9.138-17.451 19.225 1.0012.28 ATOM 2026 O GLYH 10 10.157-16.779 19.006 1.0011.60 ATOM 2027 N LEUH 11 8.830-18.03920.393 1.0013.95 ATOM 2029 CA LEUH 11 9.698-17.991 21.604 1.0014.48 ATOM 2030 CB LEUH 11 8.808-18.08622.841 1.0014.29 ATOM 2031 CG LEUH 11 9.212-17.43724.171 1.0013.64 ATOM 2032 CD1 LEUH 11 8.438-18.173 25.257 1.0013.85 ATOM 2033 CD2LEUH 11 10.709-17.46424.470 1.004.07 ATOM 2034 C LEUH 11 10.568-19.23021.585 1.0014.46 ATOM 2035 O LEUH 11 10.064-20.28621.346 1.0015.77 ATOM 2036 N VALH 12 11.839-19.10421.907 1.0018.00 ATOM 2038 CA VALH 12 12.751-20.22421.891 1.0015.52 ATOM 2039 CB VALH 12 13.407-20.30620.461 1.0018.43 ATOM 2040 CGI VALH 12 14.920-20.19720.558 1.0013.84 ATOM 2041 CG2VALH 12 13.000-21.593 19.746 1.0016.77 ATOM 2042 C VALH 12 13.825-20.01622.989 1.0015.38 ATOM 2043 O VALH 12 14.178-18.87923.340 1.0013.69 ATOM 2044 N GLNH 13 14.336-21.091 23.567 1.0016.57 ATOM 2046 CA GLNH 13 15.365-20.93624.581 1.0015.98 ATOM 2047 CB GLNH 13 15.307-22.08625.580 1.0019.24 ATOM 2048 CG GLNH 13 14.095-22.08926.528 1.0026.05 ATOM 2049 CD GLNH 13 14.433-22.62627.933 1.0028.25 ATOM 2050 OE1 GLN H 13 15.448-23.31528.141 1.0031.14 ATOM 2051 NE2GLNH 13 13.591-22.29928.915 1.0033.04 ATOM 2054 C GLNH 13 16.710-20.93223.907 1.0014.00 ATOM 2055 O GLNH 13 16.827-21.33622.748 1.0015.42 ATOM 2056 N PROH 14 17.718-20.38424.524 1.0012.23 ATOM 2057 CD PROH 14 17.678-19.54225.718 1.0012.38 ATOM 2058 CA PROH 14 19.033-20.40623.936 1.0012.75 ATOM 2059 CB PROH 14 19.910-19.79925.013 1.0010.09 ATOM 2060 CG PROH 14 18.968-18.78725.569 1.0013.06 ATOM 2061 C PROH 14 19.388-21.84623.592 1.0014.12 ATOM 2062 O PROH 14 19.071 -22.76724.361 1.0016.21 ATOM 2063 N GLYH 15 20.018-22.031 22.424 1.0010.07 ATOM 2065 CA GLYH 15 20.307-23.36721.913 1.007.80 ATOM 2066 C GLYH 15 19.223 -23.801 20.950 1.005.91 ATOM 2067 O GLYH 15 19.386-24.76620.199 1.006.43 ATOM 2068 N GLYH 16 18.140-23.06020.939 1.002.35 ATOM 2070 CA GLYH 16 17.015-23.41920.123 1.006.43 ATOM 2071 C GLYH 16 17.257-23.299 18.610 1.006.38 ATOM 2072 O GLYH 16 18.252-22.759 18.149 1.006.92 ATOM 2073 N SERH 17 16.260-23.700 17.869 1.0012.18 ATOM 2075 CA SERH 17 16.315-23.739 16.416 1.0011.41 ATOM 2076 CB SERH 17 16.721 -25.170 16.065 1.0015.73 ATOM 2077 OG SERH 17 16.994-25.349 14.706 1.0022.31 ATOM 2079 C SERH 17 14.907-23.420 15.869 1.0012.78 ATOM 2080 O SERH 17 13.922-23.816 16.484 1.0016.32 ATOM 2081 N METH 18 14.790-22.664 14.769 1.00 8.79 ATOM 2083 CA METH 18 13.498-22.456 14.119 1.0010.28 ATOM 2084 CB METH 18 12.582-21.425 14.819 1.0013.63 ATOM 2085 CG METH 18 13.212-20.131 15.329 1.0016.88 ATOM 2086 SD METH 18 12.014-19.091 16.241 1.0027.06 ATOM 2087 CE METH 18 10.544-20.141 16.251 1.003.15 ATOM 2088 C METH 18 13.678-22.055 12.669 1.009.07 ATOM 2089 O METH 18 14.753-21.621 12.252 1.0010.49 ATOM 2090 N LYSH 19 12.630-22.199 11.905 1.0010.93 ATOM 2092 CA LYSH 19 12.683-21.822 10.529 1.0011.83 ATOM 2093 CB LYSH 19 12.600-23.061 9.621 1.0014.90 ATOM 2094 CG LYSH 19 12.550-22.781 8.090 1.0017.52 ATOM 2095 CD LYSH 19 13.032-23.996 7.304 1.0020.23 ATOM 2096 CE LYSH 19 12.542-24.031 5.860 1.0019.51 ATOM 2097 NZ LYSH 19 11.259-24.781 5.747 1.0022.58 ATOM 2101 C LYSH 19 11.578-20.848 10.212 1.0013.18 ATOM 2102 O LYSH 19 10.407-21.070 10.524 1.0012.84 ATOM 2103 N LEUH 20 11.994-19.744 9.604 1.0012.76 ATOM 2105 CA LEUH 20 11.101 -18.717 9.170 1.009.79 ATOM 2106 CB LEUH 20 11.715-17.332 9.456 1.0011.85 ATOM 2107 CG LEUH 20 12.256-17.078 10.883 1.009.81 ATOM 2108 CD1 LEUH 20 12.803-15.654 10.965 1.004.16 ATOM 2109 CD2LEUH 20 11.165-17.325 11.928 1.004.65 ATOM 2110 C LEUH 20 10.864-18.860 7.681 1.009.78 ATOM 2111 O LEUH 20 11.728-19.320 6.927 1.008.56 ATOM 2112 N SERH 21 9.704-18.485 7.288 1.009.36 ATOM 2114 CA SERH 21 9.321 -18.533 5.915 1.0013.01 ATOM 2115 CB SERH 21 8.273-19.604 5.717 1.0014.00 ATOM 2116 OG SERH 21 8.807-20.875 6.012 1.0019.15 ATOM 2118 C SERH 21 8.766-17.205 5.473 1.0013.78 ATOM 2119 O SERH 21 8.163-16.482 6.268 1.0018.18 ATOM 2120 N CYSH 22 8.997-16.872 4.199 1.0016.70 ATOM 2122 CA CYS H 22 8.489-15.640 3.604 1.0013.01 ATOM 2123 CB CYSH 22 9.587-14.560 3.529 1.0011.58 ATOM 2124 SG CYSH 22 9.150-13.158 2.425 1.0013.80 ATOM 2125 C CYSH 22 7.995-15.917 2.193 1.0011.47 ATOM 2126 O CYS H 22 8.718-16.418 1.374 1.0013.22 ATOM 2127 N VAL H 23 6.773-15.589 1.935 1.0014.16 ATOM 2129 CA VALH 23 6.195-15.809 0.631 1.0016.31 ATOM 2130 CB VALH 23 4.871-16.609 0.733 1.0017.85 ATOM 2131 CGI VALH 23 5.162-17.918 1.444 1.0021.18 ATOM 2132 CG2 VALH 23 3.811-15.831 1.493 1.0019.36 ATOM 2133 C VALH 23 5.927-14.486 -0.033 1.0016.44 ATOM 21340 VAL H 23 5.313-13.580 0.565 1.0012.06 ATOM 2135 N ALA H 24 6.385-14.400 -1.280 1.0019.48 ATOM 2137 CA ALAH 24 6.247-13.181 -2.088 1.0019.91 ATOM 2138 CB ALAH 24 7.568-12.903 -2.774 1.0018.96 ATOM 2139 C ALA H 24 5.143-13.311 -3.132 1.0021.31 ATOM 2140 O ALAH 24 4.881-14.410 -3.666 1.0024.23 ATOM 2141 N SERH 25 4.488-12.222 -3.434 1.0019.69 ATOM 2143 CA SERH 25 3.474-12.266 -4.447 1.0020.48 ATOM 2144 CB SERH 25 2.151-12.592 -3.804 1.0019.79 ATOM 2145 OG SERH 25 1.844-11.601 -2.853 1.0022.03 ATOM 2147 C SERH 25 3.379-10.931 -5.124 1.0020.75 ATOM 2148 O SERH 25 3.861 -9.929 -4.589 1.0020.32 ATOM 2149 N GLYH 26 2.745-10.910 -6.292 1.0022.48 ATOM 2151 CA GLYH 26 2.518 -9.640 -6.979 1.0024.12 ATOM 2152 C GLYH 26 3.711 -9.128 -7.798 1.0025.02 ATOM 2153 O GLYH 26 3.707 -7.958 -8.219 1.0022.99 ATOM 2154 N PHE H 27 4.720-10.012 -8.005 1.0024.04 ATOM 2156 CA PHEH 27 5.913 -9.716 -8.804 1.0022.13 ATOM 2157 CB PHEH 27 6.808 -8.655 -8.126 1.0023.23 ATOM 2158 CG PHEH 27 7.717 -9.176 -7.022 1.0020.65 ATOM 2159 CD1PHEH 27 9.094 -9.334 -7.249 1.0019.81 ATOM 2160 CD2PHEH 27 7.213 -9.450 -5.750 1.0019.64 ATOM 2161 CE1PHEH 27 9.940 -9.755 -6.225 1.0018.67 ATOM 2162 CE2PHEH 27 8.061 -9.857 -4.730 1.0016.42 ATOM 2163 CZ PHEH 27 9.416-10.009 -4.964 1.0016.29 ATOM 2164 C PHEH 27 6.718-11.005 -9.015 1.0022.10 ATOM 2165 O PHEH 27 6.502-12.018 -8.322 1.0025.47 ATOM 2166 N THRH 28 7.682-10.944 -9.919 1.0017.46 ATOM 2168 CA THRH 28 8.478-12.086-10.239 1.0016.95 ATOM 2169 CB THRH 28 9.042-11.939-11.629 1.0018.84 ATOM 2170 OG1 THRH 28 7.933-11.701-12.512 1.0019.87 ATOM 2172 CG2THRH 28 9.787-13.199-12.039 1.0017.78 ATOM 2173 C THRH 28 9.588-12.303 -9.265 1.0016.32 ATOM 2174 O THRH 28 10.746-11.886 -9.500 1.0013.29 ATOM 2175 N PHEH 29 9.237-13.018 -8.187 1.0017.39 ATOM 2177 CA PHEH 29 10.182-13.315 -7.097 1.0012.65 ATOM 2178 CB PHEH 29 9.507-14.279 -6.097 1.0014.38 ATOM 2179 CG PHEH 29 10.397-14.838 -5.015 1.0013.29 ATOM 2180 CD1PHEH 29 10.551-14.153 -3.797 1.0017.17 ATOM 2181 CD2PHEH 29 11.053-16.054 -5.178 1.0011.79 ATOM 2182 CE1PHEH 29 11.356-14.678 -2.770 1.0016.24 ATOM 2183 CE2PHEH 29 11.856-16.589 -4.162 1.008.50 ATOM 2184 CZ PHEH 29 12.012-15.903 -2.965 1.0014.16 ATOM 2185 C PHEH 29 11.474-13.895 -7.603 1.0011.31 ATOM 2186 O PHEH 29 12.546-13.535 -7.107 1.0011.15 ATOM 2187 N SERH 30 11.384-14.789 -8.634 1.0010.88 ATOM 2189 CA SERH 30 12.574-15.473 -9.198 1.0010.24 ATOM 2190 CB SERH 30 12.135-16.414-10.355 1.0010.59 ATOM 2191 OG SERH 30 10.724-16.474-10.445 1.0020.09 ATOM 2193 C SERH 30 13.663-14.525 -9.728 1.008.21 ATOM 2194 O SERH 30 14.843-14.915 -9.841 1.006.56 ATOM 2195 N ASNH 31 13.251-13.294-10.108 1.0010.86 ATOM 2197 CA ASNH 31 14.160-12.317-10.733 1.0010.45 ATOM 2198 CB ASNH 31 13.370-11.295-11.558 1.0013.88 ATOM 2199 CG ASNH 31 12.872-11.818-12.880 1.0017.90 ATOM 2200 OD1 ASNH 31 13.232-12.928-13.299 1.0017.77 ATOM 2201 ND2ASNH 31 12.031-11.021-13.543 1.0020.48 ATOM 2204 C ASNH 31 15.023-11.519 -9.758 1.0011.11 ATOM 2205 O ASNH 31 15.975-10.849-10.191 1.0011.57 ATOM 2206 N TYRH 32 14.675-11.517 -8.473 1.0010.42 ATOM 2208 CA TYRH 32 15.442-10.727 -7.515 1.007.72 ATOM 2209 CB TYRH 32 14.550 -9.654 -6.923 1.0010.35 ATOM 2210 CG TYRH 32 13.981 -8.740 -7.960 1.0010.12 ATOM 2211 CD1TYRH 32 12.704 -8.983 -8.463 1.0011.35 ATOM 2212 CE1TYRH 32 12.183 -8.238 -9.523 1.0013.96 ATOM 2213 CD2TYRH 32 14.743 -7.719 -8.533 1.0010.05 ATOM 2214 CE2TYRH 32 14.228 -6.955 -9.615 1.0010.42 ATOM 2215 CZ TYRH 32 12.946 -7.222-10.097 1.0013.65 ATOM 2216 OH TYRH 32 12.371 -6.438-11.090 1.0013.93 ATOM 2218 C TYRH 32 16.056-11.540 -6.386 1.008.75 ATOM 2219 O TYRH 32 15.547-12.606 -6.002 1.008.92 ATOM 2220 N TRPH 33 17.167-11.022 -5.866 1.007.78 ATOM 2222 CA TRPH 33 17.751-11.575 -4.714 1.006.34 ATOM 2223 CB TRPH 33 19.104-10.957 -4.367 1.003.32 ATOM 2224 CG TRPH 33 20.137-10.913 -5.428 1.005.31 ATOM 2225 CD2 TRP H 33 21.483-10.438 -5.249 1.002.32 ATOM 2226 CE2TR H 33 22.117-10.500 -6.509 1.003.83 ATOM 2227 CE3TRPH 33 22.201 -9.970 -4.150 1.005.74 ATOM 2228 CDITRPH 33 19.998-11.243 -6.757 1.002.00 ATOM 2229 NE1TRPH 33 21.186-10.988 -7.387 1.003.99 ATOM 2231 CZ2TRPH 33 23.426-10.096 -6.703 1.005.36 ATOM 2232 CZ3TRPH 33 23.503 -9.568 -4.337 1.008.48 ATOM 2233 CH2 TRP H 33 24.101 -9.632 -5.608 1.007.99 ATOM 2234 C TRPH 33 16.821-11.212 -3.557 1.008.26 ATOM 2235 O TRPH 33 16.053-10.225 -3.649 1.006.24 ATOM 2236 N METH 34 16.911-11.997 -2.481 1.007.22 ATOM 2238 CA METH 34 16.133-11.752 -1.269 1.008.81 ATOM 2239 CB METH 34 15.113-12.860 -1.108 1.007.01 ATOM 2240 CG METH 34 13.919-12.749 -2.056 1.0010.07 ATOM 2241 SD METH 34 12.885-11.275 -1.844 1.0017.49 ATOM 2242 CE METH 34 11.928-11.767 -0.412 1.0017.44 ATOM 2243 C METH 34 17.094-11.681 -0.057 1.007.51 ATOM 2244 O METH 34 18.197-12.256 -0.107 1.0010.32 ATOM 2245 N ASNH 35 16.736-10.899 0.981 1.006.44 ATOM 2247 CA ASNH 35 17.586-10.755 2.175 1.004.54 ATOM 2248 CB ASNH 35 18.198 -9.339 2.317 1.005.78 ATOM 2249 CG ASNH 35 18.906 -8.804 1.078 1.003.57 ATOM 2250 ODIASNH 35 20.148 -8.700 1.016 1.002.44 ATOM 2251 ND2ASNH 35 18.121 -8.476 0.102 1.002.00 ATOM 2254 C ASN H 35 16.737-10.941 3.433 1.004.23 ATOM 2255 O ASNH 35 15.499-10.824 3.380 1.002.00 ATOM 2256 N TRPH 36 17.404-11.282 4.532 1.004.82 ATOM 2258 CA TRPH 36 16.755-11.238 5.831 1.006.51 ATOM 2259 CB TRPH 36 16.888-12.554 6.607 1.004.15 ATOM 2260 CG TRPH 36 15.911-13.575 6.121 1.006.17 ATOM 2261 CD2TRPH 36 14.527 -13.755 6.513 1.00 5.59 ATOM 2262 CE2TRPH 36 13.987 -14.743 5.672 1.00 7.68 ATOM 2263 CE3 TRP H 36 13.668 -13.180 7.489 1.00 3.55 ATOM 2264 CD1 TRPH 36 16.138 -14.443 5.102 1.00 7.43 ATOM 2265 NE1 TRP H 36 14.995 -15.119 4.847 1.0011.31 ATOM 2267 CZ2TRPH 36 12.650 -15.189 5.749 1.00 7.42 ATOM 2268 CZ3 TRP H 36 12.315- -13.631 7.564 1.00 2.61 ATOM 2269 CH2TRPH 36 11.829 -14.613 6.706 1.00 5.75 ATOM 2270 C TRPH 36 17.391 -10.102 6.614 1.003.69 ATOM 2271 0 TRPH 36 18.617 -' 9.907 6.585 1.00 3.88 ATOM 2272 N VALH 37 16.565 ■ ■ 9.310 7.251 1.00 8.04 ATOM 2274 CA VALH 37 17.074 -8.206 8.049 1.004.88 ATOM 2275 CB VALH 37 16.856 -6.854 7.314 1.00 7.93 ATOM 2276 CGI VALH 37 17.122 -5.671 8.277 1.005.70 ATOM 2277 CG2 VAL H 37 17.779 -6.772 6.078 1.004.88 ATOM 2278 C VALH 37 16.275 - ■8.201 9.356 1.00 7.96 ATOM 2279 0 VALH 37 15.062 ■ •8.279 9.294 1.0010.89 ATOM 2280 N ARGH 38 16.929 • -8.083 10.499 1.00 4.79 ATOM 2282 CA ARGH 38 16.186 -8.134 11.784 1.00 6.19 ATOM 2283 CB ARG H 38 16.715 -9.294 12.691 1.00 2.00 ATOM 2284 CG ARG H 38 18.083 -9.070 13.402 1.00 5.85 ATOM 2285 CD ARGH 38 18.660 -10.356 14.068 1.00 7.03 ATOM 2286 NE ARG H 38 20.113 -10.243 14.278 1.00 5.02 ATOM 2288 CZ ARGH 38 20.880 -11.237 14.678 1.007.94 ATOM 2289 NH1 ARGH 38 22.163 ι-H.027 14.921 1.00 8.02 ATOM 2292 NH2 ARG H 38 20.378 1-12.448 14.813 1.0010.78 ATOM 2295 C ARGH 38 16.224 • -6.783 12.565 1.00 9.00 ATOM 2296 0 ARG H 38 17.177 -5.984 12.474 1.00 7.20 ATOM 2297 N GLNH 39 15.193 ■ -6.535 13.334 1.0010.07 ATOM 2299 CA GLNH 39 15.146 -5.313 14.106 1.0013.88 ATOM 2300 CB GLNH 39 13.914 -4.517 13.693 1.0012.70 ATOM 2301 CG GLNH 39 13.835 -3.170 14.378 1.0013.88 ATOM 2302 CD GLNH 39 12.562 -2.454 14.079 1.0010.90 ATOM 2303 OE1 GLNH 39 11.554 -3.054 13.637 1.0014.02 ATOM 2304 NE2 GLN H 39 12.580 -1.161 14.311 1.0019.33 ATOM 2307 C GLNH 39 15.092 ■ -5.640 15.634 1.0017.21 ATOM 2308 O GLNH 39 14.153 -6.324 16.086 1.0011.06 ATOM 2309 N SERH 40 16.117 - 5.159 16.390 1.0020.54 ATOM 2311 CA SERH 40 16.190 -5.352 17.844 1.0025.32 ATOM 2312 CB SERH 40 17.407 -6.212 18.210 1.0024.24 ATOM 2313 OG SERH 40 18.567 -5.412 18.281 1.0026.93 ATOM 2315 C SERH 40 16.346 - 3.997 18.533 1.0026.35 ATOM 2316 O SERH 40 16.983 - 3.109 17.969 1.0027.60 ATOM 2317 N PROH 41 15.798 ■ -3.822 19.781 1.0029.80 ATOM 2318 CD PROH 41 15.063 -4.844 20.562 0.5026.67 ATOM 2319 CA PROH 41 15.899 -2.545 20.545 1.0029.86 ATOM 2320 CB PROH 41 15.210 -2.883 21.864 0.5028.55 ATOM 2321 CG PROH 41 15.328 -4.371 21.952 0.5027.83 ATOM 2322 C PROH 41 17.369 ■ ■2.07420.736 1.0033.07 ATOM 2323 O PROH 41 17.754 ■ -0.92420.401 1.0033.27 ATOM 2324 N ALA H 42 18.194 -2.98721.203 1.0034.06 ATOM 2326 CA ALA H 42 19.603 -2.67721.457 1.0037.51 ATOM 2327 CB ALA H 42 20.208 -3.808 22.297 1.0037.30 ATOM 2328 C ALA H 42 20.447 -2.48220.170 1.0037.45 ATOM 2329 O ALA H 42 21.605 -2.039 20.248 1.0038.47 ATOM 2330 N LYS H 43 19.881 -2.791 18.996 1.0036.93 ATOM 2332 CA LYS H 43 20.694 -2.812 17.802 1.0035.11 ATOM 2333 CB LYS H 43 21.032 -4.263 17.457 1.0036.81 ATOM 2334 CG LYS H 43 21.896 -4.979 18.496 1.0040.66 ATOM 2335 CD LYSH 43 22.480 -6.299 17.956 1.0040.17 ATOM 2336 CE LYSH 43 21.507 -7.487 18.083 1.0038.65 ATOM 2337 NZ LYS H 43 22.138 -8.774 17.647 1.0034.06 ATOM 2341 C LYSH 43 20.086 -2.153 16.574 1.0032.32 ATOM 2342 O LYS H 43 20.742 -2.115 15.545 1.0032.74 ATOM 2343 N GLY H 44 18.883 -1.625 16.653 1.0028.07 ATOM 2345 CA GLYH 44 18.269 -1.095 15.433 1.0026.41 ATOM 2346 C GLY H 44 18.252 -2.177 14.336 1.0022.61 ATOM 2347 O GLYH 44 18.077 -3.382 14.667 1.0021.36 ATOM 2348 N LEU H 45 18.484 -1.780 13.056 1.0018.78 ATOM 2350 CA LEUH 45 18.439 -2.758 11.923 1.0014.74 ATOM 2351 CB LEUH 45 17.995 -2.110 10.590 1.0010.90 ATOM 2352 CG LEUH 45 16.506 -1.789 10.431 1.007.35 ATOM 2353 CD1 LEUH 45 16.262 -1.110 9.115 1.008.68 ATOM 2354 CD2 LEU H 45 15.627 -3.031 10.533 1.004.89 ATOM 2355 C LEU H 45 19.759 -3.470 11.715 1.0013.85 ATOM 2356 O LEUH 45 20.859 -2.873 11.722 1.0011.97 ATOM 2357 N GLU H 46 19.676 -4.774 11.523 1.0013.05 ATOM 2359 CA GLUH 46 20.884 -5.550 11.294 1.0010.92 ATOM 2360 CB GLUH 46 21.280 -6.310 12.572 1.0012.86 ATOM 2361 CG GLUH 46 22.748 -6.634 12.653 1.0021.14 ATOM 2362 CD GLU H 46 23.081 -7.707 13.669 1.0024.52 ATOM 2363 OE1 GLUH 46 22.443 -7.735 14.753 1.0028.63 ATOM 2364 OE2 GLU H 46 23.996 -8.514 13.387 1.0025.36 ATOM 2365 C GLU H 46 20.644 -6.543 10.145 1.009.90 ATOM 2366 O GLUH 46 19.712 -7.358 10.197 1.006.95 ATOM 2367 N TRPH 47 21.457 -6.432 9.110 1.007.54 ATOM 2369 CA TRPH 47 21.327 -7.309 7.968 1.007.90 ATOM 2370 CB TRP H 47 22.045 -6.698 6.731 1.0010.76 ATOM 2371 CG TRPH 47 22.145 -7.629 5.553 1.00 5.45 ATOM 2372 CD2TRPH 47 23.284 -8.459 5.230 1.00 3.79 ATOM 2373 CE2TRPH 47 22.977 -9.168 4.069 1.002.00 ATOM 2374 CE3 TRP H 47 24.546 -8.669 5.829 1.003.96 ATOM 2375 CD1 TRPH 47 21.183 -7.863 4.590 1.004.22 ATOM 2376 NE1TRPH 47 21.707 -8.793 3.707 1.005.25 ATOM 2378 CZ2TRPH 47 23.875 -10.060 3.490 1.002.56 AT.OM 2379 CZ3 TRP H 47 25.423 -9.560 5.251 1.002.00 ATOM 2380 CH2TRPH 47 25.079 -10.232 4.094 1.002.00 ATOM 2381 C TRPH 47 21.908 - 8.649 < 8.352 1.002.55 ATOM 2382 O TRPH 47 22.958 - 8.730 18.976 1.005.06 ATOM 2383 N VAL H 48 21.209 -9.667 7.995 1.006.21 ATOM 2385 CA VALH 48 21.538-10.996 8.431 1.007.94 ATOM 2386 CB VALH 48 20.256-11.544 9.165 1.007.86 ATOM 2387 CGI VALH 48 20.190-13.054 9.168 1.0010.48 ATOM 2388 CG2VALH 48 20.234-10.992 10.603 1.004.08 ATOM 2389 C VAL H 48 22.041 -11.928 7.262 1.008.81 ATOM 2390 O VAL H 48 23.086-12.617 7.396 1.005.89 ATOM 2391 N ALA H 49 21.334-11.913 6.123 1.006.18 ATOM 2393 CA ALA H 49 21.687-12.816 5.031 1.004.66 ATOM 2394 CB ALA H 49 21.194-14.210 5.349 1.002.00 ATOM 2395 C ALA H 49 21.046-12.385 3.728 1.005.58 ATOM 2396 O ALA H 49 20.003-11.745 3.740 1.007.99 ATOM 2397 N GLUH 50 21.696-12.784 2.609 1.007.04 ATOM 2399 CA GLUH 50 21.163-12.558 1.264 1.00 8.25 ATOM 2400 CB GLUH 50 21.979-11.510 0.501 1.009.60 ATOM 2401 CG GLUH 50 23.410-11.908 0.258 1.007.83 ATOM 2402 CD GLUH 50 24.060-11.041 -0.762 1.0013.01 ATOM 2403 OE1GLUH 50 24.890-11.555 -1.523 1.009.53 ATOM 2404 OE2GLUH 50 23.733 -9.831 -0.810 1.0013.19 ATOM 2405 C GLUH 50 21.271-13.869 0.479 1.006.87 ATOM 2406 O GLUH 50 22.100-14.697 0.811 1.005.50 ATOM 2407 N ILEH 51 20.411-14.037 -0.511 1.007.46 ATOM 2409 CA ILEH 51 20.504-15.187 -1.426 1.006.66 ATOM 2410 CB ILEH 51 19.517-16.301 -1.071 1.003.45 ATOM 2411 CG2ILEH 51 18.070-15.818 -1.217 1.009.97 ATOM 2412 CGI ILEH 51 19.780-17.539 -1.911 1.002.00 ATOM 2413 CD ILEH 51 18.845-18.675 -1.563 1.002.00 ATOM 2414 C ILEH 51 20.238-14.704 -2.859 1.005.59 ATOM 2415 O ILEH 51 19.284-13.985 -3.134 1.005.07 ATOM 2416 N ARGH 52 21.096-15.107 -3.756 1.006.35 ATOM 2418 CA ARGH 52 20.994-14.629 -5.120 1.00 8.96 ATOM 2419 CB ARGH 52 22.408-14.461 -5.694 1.005.72 ATOM 2420 CG ARGH 52 23.474-14.344 -4.589 1.0012.48 ATOM 2421 CD ARGH 52 24.048-12.970 -4.373 1.0013.83 ATOM 2422 NE ARGH 52 25.246-12.780 -5.134 1.0012.25 ATOM 2424 CZ ARGH 52 26.246-11.933 -4.828 1.0012.96 ATOM 2425 NH1 ARG H 52 27.255-11.857 -5.635 1.0011.49 ATOM 2428 NH2 ARG H 52 26.249-11.156 -3.759 1.0014.67 ATOM 2431 C ARGH 52 20.089-15.503 -5.973 1.0010.32 ATOM 2432 O ARGH 52 19.257-16.224 -5.438 1.008.96 ATOM 2433 N LEUH 52A 20.244-15.437 -7.320 1.009.13 ATOM 2435 CA LEUH 52A 19.300-16.095 -8.199 1.009.35 ATOM 2436 CB LEUH 52A 19.204-15.297 -9.499 1.008.23 ATOM 2437 CG LEUH 52A 19.031-13.765 -9.341 1.004.43 ATOM 2438 CD1LEUH 52A 19.048-13.106-10.712 1.009.87 ATOM 2439 CD2 LEU H 52A 17.727-13.445 -8.645 1.004.72 ATOM 2440 C LEUH 52A 19.657-17.540 -8.504 1.006.27 ATOM 2441 O LEUH 52A 20.750-18.001 -8.220 1.006.95 ATOM 2442 N LYSH 52B 18.723-18.250 -9.074 1.007.45 ATOM 2444 CA LYSH 52B 19.023-19.580 -9.558 1.0011.04 ATOM 2445 CB LYSH 52B 17.873-20.081-10.384 1.0013.40 ATOM 2446 CG LYSH 52B 18.078-21.510-10.825 1.0018.86 ATOM 2447 CD LYSH 52B 16.930-21.989-11.679 1.0021.41 ATOM 2448 CE LYSH 52B 17.323-23.278-12.418 1.0027.85 ATOM 2449 NZ LYSH 52B 16.318-23.616-13.459 1.0034.07 ATOM 2453 C LYSH 52B 20.289-19.578-10.406 1.0011.82 ATOM 2454 O LYS H 52B 21.181-20.376-10.179 1.0010.65 ATOM 2455 N SERH 52C 20.369-18.635-11.381 1.0010.14 ATOM 2457 CA SERH 52C 21.525-18.526-12.237 1.008.75 ATOM 2458 CB SERH 52C 21.282-17.520-13.358 1.0011.63 ATOM 2459 OG SERH 52C 20.885-16.286-12.846 1.0015.43 ATOM 2461 C SERH 52C 22.786-18.177-11.507 1.0011.06 ATOM 2462 O SERH 52C 23.852-18.244-12.093 1.009.23 ATOM 2463 N ASNH 53 22.687-17.797-10.207 1.0010.74 ATOM 2465 CA ASNH 53 23.890-17.552 -9.399 1.0011.27 ATOM 2466 CB ASNH 53 23.664-16.369 -8.474 1.0010.94 ATOM 2467 CG ASNH 53 23.347-15.139 -9.257 1.00 8.42 ATOM 2468 ODI ASNH 53 22.269-14.573 -9.150 1.0012.13 ATOM 2469 ND2 ASN H 53 24.281-14.733-10.056 1.0010.17 ATOM 2472 C ASNH 53 24.200-18.799 -8.559 1.0010.33 ATOM 2473 O ASNH 53 25.123-18.802 -7.711 1.009.92 ATOM 2474 N ASNH 54 23.433-19.867 -8.841 1.0010.20 ATOM 2476 CA ASNH 54 23.553-21.171 -8.120 1.0010.20 ATOM 2477 CB ASNH 54 25.018-21.608 -7.987 1.006.42 ATOM 2478 CG ASNH 54 25.728-21.672 -9.344 1.008.73 ATOM 2479 ODIASNH 54 25.259-22.310-10.276 1.008.04 ATOM 2480 ND2ASNH 54 26.831-20.992 -9.465 1.004.73 ATOM 2483 C ASNH 54 22.954-21.063 -6.718 1.0011.89 ATOM 2484 O ASNH 54 23.310-21.844 -5.837 1.0012.26 ATOM 2485 N TYRH 55 22.027-20.102 -6.536 1.009.38 ATOM 2487 CA TYRH 55 21.467-19.805 -5.191 1.008.46 ATOM 2488 CB TYRH 55 20.675-20.998 -4.712 1.002.42 ATOM 2489 CG TYRH 55 19.506-21.296 -5.592 1.00 8.11 ATOM 2490 CD1TYRH 55 19.493-22.436 -6.421 1.009.49 ATOM 2491 CEl TYRH 55 18.379-22.709 -7.234 1.0012.87 ATOM 2492 CD2TYRH 55 18.408-20.468 -5.600 1.004.03 ATOM 2493 CE2 TYR H 55 17.313-20.726 -6.393 1.0011.68 ATOM 2494 CZ TYRH 55 17.296-21.852 -7.220 1.0015.91 ATOM 2495 OH TYRH 55 16.178-22.098 -8.056 1.0020.99 ATOM 2497 C TYRH 55 22.591-19.439 -4.184 1.00 8.90 ATOM 2498 O TYRH 55 22.558-19.848 -3.000 1.0012.11 ATOM 2499 N ALAH 56 23.578-18.631 -4.656 1.005.77 ATOM 2501 CA ALAH 56 24.694-18.199 -3.833 1.007.06 ATOM 2502 CB ALAH 56 25.723-17.516 -4.733 1.0011.84 ATOM 2503 C ALAH 56 24.214-17.266 -2.667 1.007.10 ATOM 2504 O ALAH 56 23.170-16.606 -2.757 1.005.63 ATOM 2505 N THRH 57 24.963-17.246 -1.571 1.007.85 ATOM 2507 CA THRH 57 24.500-16.552 -0.372 1.006.03 ATOM 2508 CB THRH 57 23.968-17.571 0.680 1.004.33 ATOM 2509 OG1 THRH 57 25.027-18.488 1.036 1.003.89 ATOM 2511 CG2THRH 57 22.767-18.362 0.166 1.003.87 ATOM 2512 C THRH 57 25.616-15.821 0.286 1.004.64 ATOM 2513 O THRH 57 26.803-16.086 0.030 1.007.15 ATOM 2514 N HISH 58 25.259-14.857 1.133 1.005.83 ATOM 2516 CA HISH 58 26.265-14.223 2.005 1.002.00 ATOM 2517 CB HISH 58 26.868-12.919 1.470 1.004.50 ATOM 2518 CG HISH 58 27.547-13.109 0.164 1.004.63 ATOM 2519 CD2HISH 58 28.832-13.271 -0.177 1.007.27 ATOM 2520 ND1HISH 58 26.850-13.173 -0.991 1.005.48 ATOM 2522 CEl HISH 58 27.613-13.361 -2.013 1.008.70 ATOM 2523 NE2 HIS H 58 28.822-13.418 -1.542 1.009.97 ATOM 2525 C HISH 58 25.588-13.987 3.334 1.002.00 ATOM 2526 O HISH 58 24.363-13.904 3.369 1.002.00 ATOM 2527 N TYRH 59 26.384-13.953 4.377 1.003.87 ATOM 2529 CA TYRH 59 25.875-13.909 5.761 1.006.14 ATOM 2530 CB TYRH 59 26.152-15.253 6.442 1.004.65 ATOM 2531 CG TYRH 59 25.309-16.336 5.884 1.002.93 ATOM 2532 CD1 TYRH 59 25.788-17.155 4.883 1.007.71 ATOM 2533 CEl TYRH 59 24.973-18.093 4.290 1.005.29 ATOM 2534 CD2TYRH 59 23.985-16.488 6.289 1.004.20 ATOM 2535 CE2TYRH 59 23.184-17.418 5.699 1.005.04 ATOM 2536 CZ TYRH 59 23.705-18.212 4.689 1.005.90 ATOM 2537 OH TYRH 59 22.942-19.140 4.124 1.009.69 ATOM 2539 C TYRH 59 26.600-12.897 6.559 1.006.82 ATOM 2540 O TYRH 59 27.771-12.697 6.337 1.007.72 ATOM 2541 N ALAH 60 25.925-12.282 7.515 1.008.95 ATOM 2543 CA ALAH 60 26.639-11.382 8.424 1.006.79 ATOM 2544 CB ALA H 60 25.661 -10.580 9.276 1.00 8.53 ATOM 2545 C ALAH 60 27.486-12.224 9.322 1.0010.22 ATOM 2546 O ALA H 60 27.095 -13.356 9.685 1.0011.26 ATOM 2547 N ALAH 61 28.630-11.687 9.731 1.0013.53 ATOM 2549 CA ALAH 61 29.557-12.439 10.577 1.0014.91 ATOM 2550 CB ALAH 61 30.778-11.575 10.917 1.0014.40 ATOM 2551 C ALAH 61 28.899-12.973 1.866 1.0017.24 ATOM 2552 O ALAH 61 29.251 -14.049 12.335 1.0021.67 ATOM 2553 N SERH 62 27.923 -12.257 12.408 1.0018.88 ATOM 2555 CA SERH 62 27.304-12.651 13.691 1.0020.00 ATOM 2556 CB SERH 62 26.493-11.485 14.211 1.0016.39 ATOM 2557 OG SERH 62 25.625-10.986 13.206 1.0018.61 ATOM 2559 C SERH 62 26.378-13.857 13.557 1.0021.12 ATOM 2560 O SERH 62 25.799-14.355 14.542 1.0019.05 ATOM 2561 N VALH 63 26.235-14.324 12.350 1.0018.08 ATOM 2563 CA VALH 63 25.239-15.311 12.066 1.0017.68 ATOM 2564 CB VAL H 63 24.130-14.543 11.334 1.0018.65 ATOM 2565 CGI VALH 63 23.637-15.237 10.092 1.0016.99 ATOM 2566 CG2VALH 63 23.017-14.228 12.333 1.0012.88 ATOM 2567 C VALH 63 25.838-16.474 11.274 1.0015.76 ATOM 2568 O VALH 63 25.290-17.566 11.214 1.0014.97 ATOM 2569 N LYS H 64 27.015-16.239 10.768 1.0018.14 ATOM 2571 CA LYSH 64 27.688-17.213 9.966 1.0020.28 ATOM 2572 CB LYS H 64 29.059-16.666 9.545 1.0022.43 ATOM 2573 CG LYSH 64 29.150-16.132 8.136 1.0020.56 ATOM 2574 CD LYSH 64 30.593-15.735 7.835 1.0023.16 ATOM 2575 CE LYSH 64 30.751 -15.203 6.4250.0121.98 ATOM 2576 NZ LYS H 64 32.163-14.833 6.1290.0123.60 ATOM 2580 C LYSH 64 27.858-18.496 10.756 1.0018.78 ATOM 2581 O LYSH 64 28.225-18.458 11.926 1.0020.26 ATOM 2582 N GLYH 65 27.565-19.618 10.110 1.0017.68 ATOM 2584 CA GLYH 65 27.700-20.919 10.761 1.0016.07 ATOM 2585 C GLY H 65 26.476-21.353 11.581 1.0014.30 ATOM 2586 O GLYH 65 26.364-22.517 11.931 1.0014.97 ATOM 2587 N ARG H 66 25.553-20.432 11.876 1.0014.24 ATOM 2589 CA ARG H 66 24.336-20.780 12.624 1.0010.28 ATOM 2590 CB ARG H 66 24.261 -19.924 13.862 1.007.89 ATOM 2591 CG ARGH 66 25.503 -20.000 14.713 1.007.93 ATOM 2592 CD ARGH 66 25.673-18.695 15.483 1.0014.73 ATOM 2593 NE ARGH 66 24.525-18.448 16.272 1.0017.33 ATOM 2595 CZ ARG H 66 23.913-17.292 16.390 11.0017.22 ATOM 2596 NH1 ARGH 66 22.879-17.258 17.140 1.0018.44 ATOM 2599 NH2 ARG H 66 24.319-16.184 15.800 1.0015.39 ATOM 2602 C ARGH 66 23.090-20.589 11.803 1.009.54 ATOM 2603 O ARGH 66 22.071-21.275 12.011 1.0011.68 ATOM 2604 N PHEH 67 23.106-19.623 10.884 1.009.08 ATOM 2606 CA PHEH 67 21.905-19.393 10.055 1.008.27 ATOM 2607 CB PHEH 67 21.485-17.896 10.062 1.0014.66 ATOM 2608 CG PHEH 67 20.955 -17.333 11.365 1.0011.27 ATOM 2609 CD1 PHEH 67 20.951 -18.096 12.552 1.0016.10 ATOM 2610 CD2PHEH 67 20.441 -16.043 11.410 1.0012.21 ATOM 2611 CEl PHEH 67 20.452-17.567 13.739 1.0015.15 ATOM 2612 CE2PHEH 67 19.943-15.515 12.603 1.0016.05 ATOM 2613 CZ PHEH 67 19.952-16.276 13.758 1.0014.19 ATOM 2614 C PHEH 67 22.151 -19.809 8.590 1.00 8.04 ATOM 2615 O PHEH 67 23.308-19.737 8.107 1.007.14 ATOM 2616 N THRH 68 21.069-20.222 7.902 1.005.55 ATOM 2618 CA THRH 68 21.135-20.635 6.488 1.006.31 ATOM 2619 CB THRH 68 21.138-22.179 6.392 1.0010.66 ATOM 2620 OG1THRH 68 22.268-22.681 7.120 1.00 8.86 ATOM 2622 CG2 THRH 68 21.158-22.667 4.935 1.0010.19 ATOM 2623 C THRH 68 19.909-20.118 5.735 1.006.07 ATOM 2624 O THRH 68 18.761-20.448 6.076 1.009.45 ATOM 2625 N ILEH 69 20.134-19.267 4.742 1.004.87 ATOM 2627 CA ILEH 69 19.048-18.766 3.956 1.002.00 ATOM 2628 CB ILEH 69 19.312-17.255 3.525 1.006.99 ATOM 2629 CG2 ILE H 69 20.551-17.113 2.660 1.007.03 ATOM 2630 CGI ILEH 69 18.099-16.665 2.797 1.002.00 ATOM 2631 CD ILEH 69 18.333-15.229 2.387 1.002.00 ATOM 2632 C ILEH 69 18.896-19.677 2.718 1.002.51 ATOM 2633 O ILEH 69 19.874-20.221 2.257 1.002.38 ATOM 2634 N SER H 70 17.690-19.872 2.253 1.002.57 ATOM 2636 CA SERH 70 17.478-20.679 1.081 1.006.14 ATOM 2637 CB SERH 70 17.375-22.176 1.473 1.009.52 ATOM 2638 OG SERH 70 16.243-22.479 2.291 1.0010.39 ATOM 2640 C SERH 70 16.224-20.206 0.384 1.006.48 ATOM 2641 O SERH 70 15.483-19.433 0.956 1.007.77 ATOM 2642 N ARGH 71 15.977-20.635 -0.859 1.007.82 ATOM 2644 CA ARGH 71 14.771-20.200 -1.545 1.008.16 ATOM 2645 CB ARGH 71 15.013-18.926 -2.433 1.0010.92 ATOM 2646 CG ARGH 71 16.003-19.089 -3.610 1.008.76 ATOM 2647 CD ARGH 71 16.351-17.736 -4.291 1.004.61 ATOM 2648 NE ARGH 71 15.173-17.037 -4.839 1.007.09 ATOM 2650 CZ ARGH 71 15.201-15.734 -5.185 1.007.29 ATOM 2651 NH1ARGH 71 14.129-15.130 -5.657 1.00 8.76 ATOM 2654 NH2 ARG H 71 16.294-15.048 -5.020 1.003.13 ATOM 2657 C ARGH 71 14.170-21.289 -2.385 1.009.04 ATOM 2658 O ARGH 71 14.832-22.200 -2.814 1.0011.10 ATOM 2659 N ASPH 72 12.920-21.167 -2.619 1.008.40 ATOM 2661 CA ASPH 72 12.275-22.064 -3.477 1.0013.86 ATOM 2662 CB ASPH 72 11.461-23.048 -2.660 1.0018.00 ATOM 2663 CG ASPH 72 10.873-24.134 -3.531 1.0022.29 ATOM 2664 OD1ASPH 72 9.993-23.818 -4.333 1.0018.82 ATOM 2665 OD2 ASP H 72 11.286-25.303 -3.392 1.0029.08 ATOM 2666 C ASPH 72 11.402-21.244 -4.397 1.0012.87 ATOM 2667 O ASPH 72 10.324-20.782 -4.036 1.0011.56 ATOM 2668 N ASPH 73 11.894-21.045 -5.587 1.0014.62 ATOM 2670 CA ASPH 73 11.183-20.241 -6.506 1.0012.47 ATOM 2671 CB ASPH 73 12.023-19.903 -7.750 1.0014.32 ATOM 2672 CG ASPH 73 13.316-19.152 -7.394 1.0012.44 ATOM 2673 OD1ASPH 73 13.315-18.402 -6.404 1.0013.98 ATOM 2674 OD2 ASP H 73 14.333-19.334 -8.080 1.0014.38 ATOM 2675 C ASPH 73 9.918-20.906 -6.865 1.0015.39 ATOM 2676 O ASP H 73 8.966-20.160 -7.111 1.0017.19 ATOM 2677 N SERH 74 9.842-22.307 -6.828 1.0016.30 ATOM 2679 CA SERH 74 8.521-22.992 -7.159 1.0017.45 ATOM 2680 CB SERH 74 8.491-24.605 -7.038 1.0015.19 ATOM 2681 OG SERH 74 9.303-25.285 -6.039 1.002.00 ATOM 2683 C SERH 74 7.416-22.405 -6.303 1.0019.15 ATOM 2684 O SER H 74 6.283-22.217 -6.761 1.0016.07 ATOM 2685 N LYSH 75 7.806-22.025 -5.060 1.0020.59 ATOM 2687 CA LYS H 75 6.859-21.536 -4.058 1.0022.07 ATOM 2688 CB LYSH 75 7.170-22.240 -2.730 1.0022.73 ATOM 2689 CG LYS H 75 7.169-23.755 -2.843 1.0030.86 ATOM 2690 CD LYSH 75 8.092-24.404 -1.815 1.0034.56 ATOM 2691 CE LYSH 75 7.990-25.915 -1.886 1.0036.81 ATOM 2692 NZ LYS H 75 6.612-26.394 -1.547 1.0038.63 ATOM 2696 C LYSH 75 6.895-20.023 -3.852 1.0021.01 ATOM 2697 O LYSH 75 6.150-19.485 -3.012 1.0018.31 ATOM 2698 N SERH 76 7.738-19.325 -4.592 1.0018.64 ATOM 2700 CA SERH 76 7.840-17.868 -4.412 1.0016.65 ATOM 2701 CB SERH 76 6.519-17.188 -4.729 1.0018.03 ATOM 2702 OG SERH 76 6.400-16.854 -6.090 1.0023.00 ATOM 2704 C SERH 76 8.150-17.583 -2.961 1.0015.08 ATOM 2705 O SERH 76 7.560-16.691 -2.397 1.0013.71 ATOM 2706 N SERH 77 9.072-18.354 -2.371 1.0012.40 ATOM 2708 CA SERH 77 9.328-18.216 -0.955 1.0011.32 ATOM 2709 CB SERH 77 8.642-19.362 -0.220 1.005.62 ATOM 2710 OG SERH 77 7.217-19.321 -0.359 1.0011.83 ATOM 2712 C SERH 77 10.798-18.213 -0.655 1.0011.23 ATOM 2713 O SERH 77 11.586-18.831 -1.383 1.0010.52 ATOM 2714 N VALH 78 11.174-17.444 0.375 1.0011.36 ATOM 2716 CA VALH 78 12.553-17.452 0.903 1.009.82 ATOM 2717 CB VALH 78 13.271 -16.054 0.775 1.002.05 ATOM 2718 CGI VALH 78 12.610-15.007 1.602 1.008.95 ATOM 2719 CG2VALH 78 14.718-16.159 1.131 1.006.47 ATOM 2720 C VALH 78 12.442-17.927 2.373 1.0010.77 ATOM 2721 O VALH 78 11.348-17.873 2.946 1.0010.22 ATOM 2722 N TYRH 79 13.512-18.464 2.944 1.009.85 ATOM 2724 CA TYRH 79 13.408-19.077 4.283 1.0011.42 ATOM 2725 CB TYRH 79 13.281-20.600 4.156 1.008.95 ATOM 2726 CG TYRH 79 12.220-21.110 3.202 1.009.83 ATOM 2727 CD1 TYRH 79 10.886-21.256 3.590 1.0013.08 ATOM 2728 CEl TYRH 79 9.933-21.792 2.727 1.0013.31 ATOM 2729 CD2TYRH 79 12.565-21.505 1.916 1.0016.54 ATOM 2730 CE2TYRH 79 11.642-22.044 1.053 1.0013.14 ATOM 2731 CZ TYRH 79 10.327-22.200 1.458 1.0015.87 ATOM 2732 OH TYRH 79 9.440-22.907 0.647 1.0021.63 ATOM 2734 C TYRH 79 14.656-18.799 5.072 1.008.87 ATOM 2735 O TYRH 79 15.682-18.508 4.482 1.007.96 ATOM 2736 N LEUH 80 14.563-18.863 6.414 1.007.68 ATOM 2738 CA LEUH 80 15.756-18.731 7.274 1.006.13 ATOM 2739 CB LEUH 80 15.865-17.319 7.926 1.003.75 ATOM 2740 CG LEUH 80 17.161 -17.024 8.774 1.005.89 ATOM 2741 CD1 LEUH 80 18.360-16.785 7.857 1.007.66 ATOM 2742 CD2LEUH 80 16.965-15.789 9.665 1.007.64 ATOM 2743 C LEUH 80 15.717-19.812 8.384 1.006.11 ATOM 2744 O LEUH 80 14.834-19.823 9.212 1.0010.81 ATOM 2745 N GLNH 81 16.636-20.703 8.314 1.009.34 ATOM 2747 CA GLNH 81 16.809-21.750 9.279 1.007.35 ATOM 2748 CB GLNH 81 17.433-22.959 8.585 1.0010.80 ATOM 2749 CG GLNH 81 17.864-24.103 9.486 1.007.67 ATOM 2750 CD GLNH 81 16.700-24.584 10.255 1.0012.30 ATOM 2751 OE1 GLNH 81 15.667-24.853 9.682 1.009.50 ATOM 2752 NE2GLNH 81 16.834-24.650 11.577 1.0014.89 ATOM 2755 C GLNH 81 17.760-21.249 10.279 1.007.63 ATOM 2756 O GLN H 81 18.905-20.980 9.946 .006.37 ATOM 2757 N METH 82 17.330-21.109 11.519 1.008.18 ATOM 2759 CA METH 82 18.239-20.590 12.561 1.008.53 ATOM 2760 CB METH 82 17.585-19.400 13.268 1.0011.01 ATOM 2761 CG METH 82 17.055-18.374 12.312 1.0012.29 ATOM 2762 SD METH 82 15.951 -17.219 13.067 1.0013.74 ATOM 2763 CE METH 82 14.487-18.141 12.822 1.0014.37 ATOM 2764 C METH 82 18.515-21.680 13.589 11.008.43 ATOM 2765 O METH 82 17.572-22.280 14.081 1.005.71 ATOM 2766 N ASNH 82A 19.781 -21.872 13.891 1.008.95 ATOM 2768 CA ASN H 82A 20.234-22.884 14.806 1.0011.83 ATOM 2769 CB ASNH 82A 21.152-23.876 14.109 1.0014.31 ATOM 2770 CG ASNH 82A 20.457-24.638 13.025 1.0014.14 ATOM 2771 OD1 ASNH 82A 19.230-24.729 13.011 1.0020.53 ATOM 2772 ND2ASNH 82A 21.227-25.160 12.091 1.0019.33 ATOM 2775 C ASNH 82A 21.065-22.233 15.867 1.0014.07 ATOM 2776 O ASNH 82A 21.572-21.134 15.663 1.0012.90 ATOM 2777 N ASNH 82B 21.234-22.937 16.970 1.0013.76 ATOM 2779 CA ASN H 82B 22.093-22.461 18.068 1.0017.95 ATOM 2780 CB ASNH 82B 23.592-22.660 17.695 1.0020.73 ATOM 2781 CG ASNH 82B 23.893-24.013 16.977 1.0029.83 ATOM 2782 OD1 ASN H 82B 23.763-25.120 17.540 1.0032.41 ATOM 2783 ND2ASNH 82B 24.310-23.938 15.711 1.0033.10 ATOM 2786 C ASNH 82B 21.755-20.982 18.401 1.0015.91 ATOM 2787 O ASNH 82B 22.626-20.117 18.539 1.0012.49 ATOM 2788 N LEUH 82C 20.438-20.717 18.487 1.0014.84 ATOM 2790 CA LEUH 82C 19.930-19.385 18.761 1.0013.25 ATOM 2791 CB LEUH 82C 18.398-19.413 18.672 1.007.42 ATOM 2792 CG LEUH 82C 17.778-19.383 17.253 1.007.73 ATOM 2793 CD1 LEU H 82C 16.299-19.736 17.262 1.004.66 ATOM 2794 CD2 LEU H 82C 17.929-18.000 16.670 1.002.94 ATOM 2795 C LEUH 82C 20.463-18.841 20.118 1.0016.15 ATOM 2796 O LEUH 82C 20.746-19.59921.059 1.0017.22 ATOM 2797 N ARGH 83 20.662-17.53620.166 1.0016.23 ATOM 2799 CA ARGH 83 21.172-16.85421.323 1.0016.47 ATOM 2800 CB ARGH 83 22.493-16.22820.989 1.0017.57 ATOM 2801 CG ARGH 83 23.517-17.16420.447 1.0023.38 ATOM 2802 CD ARGH 83 24.663-16.327 19.937 1.0029.30 ATOM 2803 NE ARGH 83 25.731-17.110 19.366 1.0030.53 ATOM 2805 CZ ARG H 83 26.727-16.556 18.689 1.0033.66 ATOM 2806 NH1 ARG H 83 27.699-17.323 18.213 1.0037.56 ATOM 2809 NH2 ARG H 83 26.754-15.227 18.483 1.0035.33 ATOM 2812 C ARGH 83 20.209-15.73321.680 1.0017.82 ATOM 2813 O ARGH 83 19.500-15.23720.805 1.0019.55 ATOM 2814 N ALAH 84 20.198-15.271 22.920 1.0014.91 ATOM 2816 CA ALAH 84 19.259-14.191 23.263 1.0016.48 ATOM 2817 CB ALAH 84 19.353-13.84624.737 1.0015.35 ATOM 2818 C ALAH 84 19.489-12.92522.398 1.0014.44 ATOM 2819 O ALAH 84 18.540-12.16622.124 1.0016.17 ATOM 2820 N ALAH 85 20.743-12.72921.953 1.0015.72 ATOM 2822 CA ALA H 85 21.087-11.58821.103 1.0015.91 ATOM 2823 CB ALAH 85 22.610-11.47320.964 1.0011.61 ATOM 2824 C ALAH 85 20.428-11.685 19.703 1.0015.42 ATOM 2825 O ALAH 85 20.460-10.694 18.938 1.0014.28 ATOM 2826 N ASPH 86 19.859-12.870 19.362 1.0012.78 ATOM 2828 CA ASPH 86 19.166-13.055 18.066 1.0010.42 ATOM 2829 CB ASPH 86 19.191 -14.501 17.595 1.004.96 ATOM 2830 CG ASPH 86 20.581 -15.025 17.414 1.0010.01 ATOM 2831 OD1 ASPH 86 20.814-16.181 17.786 1.0012.26 ATOM 2832 OD2ASPH 86 21.440-14.291 16.916 1.00 8.11 ATOM 2833 C ASPH 86 17.735-12.629 18.149 1.008.78 ATOM 2834 O ASPH 86 17.003-12.673 17.172 1.0012.52 ATOM 2835 N THRH 87 17.316-12.239 19.320 1.008.30 ATOM 2837 CA THRH 87 15.948-11.788 19.506 1.008.21 ATOM 2838 CB THRH 87 15.713-11.445 21.041 1.007.33 ATOM 2839 OG1 THRH 87 15.904-12.63421.815 1.006.98 ATOM 2841 CG2THRH 87 14.316-10.935 21.301 1.005.67 ATOM 2842 C THRH 87 15.688-10.568 18.601 1.009.42 ATOM 2843 O THRH 87 16.564 -9.721 18.445 1.0013.23 ATOM 2844 N GLYH 88 14.534-10.520 17.972 1.007.71 ATOM 2846 CA GLYH 88 14.200 -9.359 17.178 1.009.10 ATOM 2847 C GLYH 88 13.112 -9.674 16.231 1.009.84 ATOM 2848 O GLYH 88 12.640-10.813 16.227 1.007.86 ATOM 2849 N ILEH 89 12.641 -8.653 15.476 1.009.11 ATOM 2851 CA ILEH 89 11.638 -8.868 14.444 1.0010.31 ATOM 2852 CB ILEH 89 10.773 -7.624 14.277 1.0011.02 ATOM 2853 CG2ILEH 89 9.706 -7.876 13.226 1.0010.51 ATOM 2854 CGI ILEH 89 10.139 -7.299 15.641 1.0011.28 ATOM 2855 CD ILEH 89 9.326 -6.014 15.674 1.0017.09 ATOM 2856 C ILEH 89 12.393 -9.160 13.141 1.0011.03 ATOM 2857 O ILEH 89 13.338 -8.436 12.810 1.0011.03 ATOM 2858 N TYRH 90 12.054-10.278 12.480 1.0011.24 ATOM 2860 CA TYRH 90 12.766-10.682 11.279 1.009.58 ATOM 2861 CB TYRH 90 13.153-12.144 11.352 1.004.73 ATOM 2862 CG TYRH 90 14.367-12.437 12.228 1.004.17 ATOM 2863 CD1 TYRH 90 14.304-12.317 13.632 1.002.00 ATOM 2864 CEl TYRH 90 15.398-12.607 14.428 1.002.00 ATOM 2865 CD2TYRH 90 15.562-12.865 11.673 1.002.40 ATOM 2866 CE2TYRH 90 16.660-13.156 12.473 1.002.17 ATOM 2867 CZ TYRH 90 16.559-13.011 13.862 1.002.00 ATOM 2868 OH TYRH 90 17.670-13.217 14.659 1.002.45 ATOM 2870 C TYRH 90 11.941-10.411 10.053 1.009.22 ATOM 2871 O TYRH 90 10.768-10.839 9.955 1.0012.19 ATOM 2872 N TYRH 91 12.555 -9.661 9.125 1.008.92 ATOM 2874 CA TYRH 91 11.882 -9.261 7.869 1.006.94 ATOM 2875 CB TYRH 91 11.971 -7.724 7.693 1.008.51 ATOM 2876 CG TYRH 91 11.501 -6.909 8.859 1.007.13 ATOM 2877 CD1TYRH 91 10.187 -6.477 8.923 1.006.14 ATOM 2878 CEl TYRH 91 9.726 -5.715 9.997 1.007.31 ATOM 2879 CD2TYRH 91 12.367 -6.566 9.890 1.004.90 ATOM 2880 CE2TYRH 91 11.904 -5.806 10.978 1.008.04 ATOM 2881 CZ TYRH 91 10.578 -5.389 11.017 1.005.99 ATOM 2882 OH TYRH 91 10.097 -4.640 12.115 1.0013.80 ATOM 2884 C TYRH 91 12.596 -9.868 6.640 1.005.68 ATOM 2885 O TYRH 91 13.819 -9.926 6.618 1.0010.68 ATOM 2886 N CYSH 92 11.858-10.361 5.661 1.005.92 ATOM 2888 CA CYSH 92 12.499-10.597 4.354 1.009.62 ATOM 2889 CB CYSH 92 11.868-11.756 3.624 1.008.20 ATOM 2890 SG CYS H 92 10.125-11.557 3.662 1.0016.35 ATOM 2891 C CYS H 92 12.263 -9.318 3.528 1.007.60 ATOM 2892 O CYS H 92 11.176 -8.703 3.579 1.00 8.00 ATOM 2893 N THRH 93 13.236 -8.917 2.785 1.008.87 ATOM 2895 CA THR H 93 13.120 -7.666 2.031 1.00 9.75 ATOM 2896 CB THR H 93 13.581 -6.438 2.904 1.00 7.13 ATOM 2897 OG 1 THR H 93 13.889 -5.309 2.059 1.00 8.1 1 ATOM 2899 CG2 THR H 93 14.789 -6.775 3.729 1.00 6.38 ATOM 2900 C THR H 93 13.983 -7.740 0.786 1.00 9.01 ATOM 2901 0 THR H 93 15.024 -8.385 0.836 1.00 8.92 ATOM 2902 N GLY H 94 13.559 -7.104 -0.319 1.00 8.19 ATOM 2904 CA GLY H 94 14.395 -7.122 -1.486 1.00 9.97 ATOM 2905 C GLY H 94 13.962 -6.132 -2.539 1.00 1 1.34 ATOM 2906 O GLY H 94 13.054 -5.370 -2.318 1.00 8.22 ATOM 2907 N VAL H 95 14.679 -6.169 -3.673 1.00 13.48 ATOM 2909 CA VAL H 95 14.454 -5.327 -4.858 1.00 10.59 ATOM 2910 CB VAL H 95 13.009 -5.252 -5.284 1.00 9.92 ATOM 291 1 CGI VAL H 95 12.943 -4.469 -6.574 1.00 12.93 ATOM 2912 CG2 VAL H 95 12.412 -6.635 -5.491 1.00 12.57 ATOM 2913 C VAL H 95 14.985 -3.907 -4.740 1.00 12.91 ATOM 2914 O VAL H 95 14.407 -3.047 -4.075 1.00 16.60 ATOM 2915 N GLY H 96 16.1 13 -3.695 -5.364 1.00 14.72 ATOM 2917 CA GLY H 96 16.722 -2.351 -5.505 1.00 17.50 ATOM 2918 C GLY H 96 16.912 -1.389 -4.282 1.00 15.41 ATOM 2919 O GLY H 96 16.467 -0.233 -4.348 1.00 16.20 ATOM 2920 N GLN H 97 17.515 -1.782 -3.162 1.00 13.46 ATOM 2922 CA GLN H 97 17.931 -3.133 -2.860 1.00 13.51 ATOM 2923 CB GLN H 97 19.415 -3.173 -2.470 1.00 11.95 ATOM 2924 CG GLN H 97 20.392 -3.138 -3.645 1.00 15.05 ATOM 2925 CD GLN H 97 20.369 -1.859 -4.476 1.00 16.43 ATOM 2926 OE1 GLN H 97 20.832 -0.809 -4.044 1.00 17.08 ATOM 2927 NE2 GLN H 97 19.846 -1.954 -5.688 1.00 18.31 ATOM 2930 C GLN H 97 17.061 -3.628 -1.680 1.00 10.81 ATOM 2931 O GLN H 97 17.109 -4.795 -1.297 1.00 8.86 ATOM 2932 N PHE H 98 16.237 -2.728 -1.153 1.00 8.60 ATOM 2934 CA PHE H 98 15.365 -3.030 -0.021 1.00 8.66 ATOM 2935 CB PHE H 98 16.024 -2.558 1.275 1.00 11.54 ATOM 2936 CG PHE H 98 17.333 -3.213 1.620 1.00 9.16 ATOM 2937 CD1 PHE H 98 17.356 -4.439 2.271 1.00 6.51 ATOM 2938 CD2 PHE H 98 18.544 -2.603 1.305 1.00 9.14 ATOM 2939 CEl PHE H 98 18.564 -5.059 2.603 1.00 9.69 ATOM 2940 CE2 PHE H 98 19.744 -3.21 1 1.639 1.00 8.35 ATOM 2941 CZ PHE H 98 19.759 -4.454 2.296 1.00 6.22 ATOM 2942 C PHE H 98 14.056 -2.275 -0.180 1.00 10.16 ATOM 2943 O PHE H 98 13.588 -1.638 0.747 1.00 11.80 ATOM 2944 N ALA H 101 13.468 -2.339 -1.351 1.00 9.29 ATOM 2946 CA ALA H 101 12.252 -1.628 -1.609 1.00 8.04 ATOM 2947 CB ALA H 101 11.995 1.543 -3.099 1.00 6.69 ATOM 2948 C ALA H 101 1 1 1..007711 • -2.292 - ■ ■00..995577 1.00 1 1.49 ATOM 2949 O ALA H 101 10 0..113388 -1.589 ■ - -00..553333 1.00 1 1.63 ATOM 2950 N TYR H 102 11 1..110055 -3.644 ■ - •00..991100 1.00 8.89 ATOM 2952 CA TYR H 102 9 9..999988 -4.423 - -00..336666 1.00 13.48 ATOM 2953 CB TYR H 102 9 9..558844 -5.528 -1.335 1.00 17.64 ATOM 2954 CG TYR H 102 9.293 -5.047 -2.725 1.00 19.49 ATOM 2955 CD1 TYR H 102 8.791 -3.766 -2.940 1.00 19.65 ATOM 2956 CEl TYR H 102 8.480 -3.313 -4.208 1.00 19.68 ATOM 2957 CD2 TYR H 102 9.490 -5.879 -3.831 1.0021.83 ATOM 2958 CE2 TYR H 102 9.178 -5.422 -5.1 10 1.00 24.66 ATOM 2959 CZ TYR H 102 8.667 -4.140 -5.282 1.00 21.57 ATOM 2960 OH TYR H 102 8.253 -3.720 -6.536 1.00 29.25 ATOM 2962 C TYRH 102 10.402 -5.063 0.928 1.0010.63 ATOM 2963 O TYRH 102 11.504 -5.604 1.031 1.0010.52 ATOM 2964 N TRPH 103 9.509 -4.971 1.883 1.0012.90 ATOM 2966 CA TRPH 103 9.710 -5.489 3.242 1.0012.06 ATOM 2967 CB TRPH 103 9.957 -4.323 4.251 .0010.97 ATOM 2968 CG TRPH 103 11.277 -3.615 4.121 1.007.64 ATOM 2969 CD2 TRP H 103 12.428 -3.716 5.024 1.007.34 ATOM 2970 CE2 TRP H 103 13.445 -2.949 4.472 1.002.00 ATOM 2971 CE3TRPH 103 12.677 -4.386 6.241 1.002.00 ATOM 2972 CD1 TRP H 103 11.664 -2.792 3.104 1.002.00 ATOM 2973 NE1 TRPH 103 12.945 -2.407 3.329 1.005.49 ATOM 2975 CZ2 TRPH 103 14.706 -2.828 5.070 1.006.14 ATOM 2976 CZ3 TRP H 103 13.905 -4.272 6.837 1.004.72 ATOM 2977 CH2 TRPH 103 14.916 -3.504 6.262 1.004.93 ATOM 2978 C TRP H 103 8.426 -6.189 3.650 1.0010.58 ATOM 2979 O TRPH 103 7.324 -5.684 3.357 1.0012.28 ATOM 2980 N GLYH 104 8.524 -7.363 4.264 1.009.92 ATOM 2982 CA GLYH 104 7.304 -7.969 4.775 1.008.86 ATOM 2983 C GLYH 104 6.887 -7.282 6.081 1.0011.03 ATOM 2984 O GLY H 104 7.519 -6.295 6.494 1.007.62 ATOM 2985 N GLN H 105 5.863 -7.817 6.742 1.0014.11 ATOM 2987 CA GLN H 105 5.373 -7.251 8.007 1.0013.52 ATOM 2988 CB GLN H 105 3.904 -7.694 8.265 1.0016.08 ATOM 2989 CG GLN H 105 3.722 -9.067 8.895 1.0016.34 ATOM 2990 CD GLN H 105 4.141 -10.239 8.024 1.0017.73 ATOM 2991 OE1 GLNH 105 4.224-10.145 6.813 1.0021.14 ATOM 2992 NE2 GLN H 105 4.400-11.364 8.646 1.0022.59 ATOM 2995 C GLN H 105 6.276 -7.602 9.188 1.0013.99 ATOM 2996 O GLN H 105 6.240 -6.925 10.216 1.0012.82 ATOM 2997 N GLYH 106 7.111 -8.648 9.017 1.0013.67 ATOM 2999 CA GLY H 106 8.029 -9.065 10.056 1.0011.11 ATOM 3000 C GLY H 106 7.439-10.154 10.931 1.0012.32 ATOM 3001 O GLYH 106 6.213-10.270 11.084 1.0011.02 ATOM 3002 N THRH 107 8.301 -10.977 11.484 1.0014.65 ATOM 3004 CA THRH 107 7.855-12.055 12.387 1.0012.73 ATOM 3005 CB THRH 107 7.902-13.416 11.638 1.0010.15 ATOM 3006 OG1 THRH 107 7.382-14.453 12.483 1.0015.55 ATOM 3008 CG2 THRH 107 9.304-13.766 11.191 1.004.69 ATOM 3009 C THRH 107 8.745-12.027 13.618 1.0010.17 ATOM 3010 O THRH 107 9.944-11.924 13.479 1.0010.87 ATOM 3011 N THRH 108 8.179-12.063 14.843 1.0012.24 ATOM 3013 CA THRH 108 9.039-11.937 16.025 1.0010.94 ATOM 3014 CB THRH 108 8.360-11.094 17.205 1.0012.32 ATOM 3015 OG1 THRH 108 9.224-10.934 18.347 1.0013.78 ATOM 3017 CG2 THRH 108 7.088-11.693 17.677 1.0015.73 ATOM 3018 C THRH 108 9.605-13.274 16.492 1.009.14 ATOM 3019.0 THRH 108 8.933-14.316 16.539 1.006.78 ATOM 3020 N VAL H 109 10.865-13.225 16.754 1.008.85 ATOM 3022 CA VAL H 109 11.605-14.332 17.261 1.009.39 ATOM 3023 CB VALH 109 12.788-14.662 16.322 1.0011.58 ATOM 3024 CGI VAL HI 09 13.739-15.639 16.980 1.005.51 ATOM 3025 CG2 VAL H 109 12.268-15.232 14.986 1.0010.69 ATOM 3026 C VALH 109 12.174-13.883 18.589 1.0012.15 ATOM 3027 O VALH 109 12.926-12.926 18.623 1.0012.01 ATOM 3028 N THRH 110 11.781 -14.552 19.681 1.0011.46 ATOM 3030 CA THRH 110 12.306-14.23821.009 1.0011.24 ATOM 3031 CB THRH 110 11.175-14.04022.044 1.009.63 ATOM 3032 OG1THRH 110 10.211 -13.10621.552 1.0010.83 ATOM 3034 CG2THRH 110 11.749-13.553 23.348 1.008.99 ATOM 3035 C THRH 110 13.132-15.39921.501 1.007.60 ATOM 3036 O THRH 110 12.632-16.511 21.519 1.0012.38 ATOM 3037 N VAL H ill 14.366-15.15521.840 1.009.00 ATOM 3039 CA VAL Hill 15.217-16.191 22.409 1.0012.99 ATOM 3040 CB VALH 111 16.629-16.27621.720 1.0010.01 ATOM 3041 CGI VALH 111 17.395-17.471 22.276 1.00 8.99 ATOM 3042 CG2 VAL Hill 16.484-16.393 20.188 1.0014.22 ATOM 3043 C VAL Hill 15.450-15.89423.907 1.0013.42 ATOM 3044 O VAL H ill 16.248-15.04624.261 1.0014.03 ATOM 3045 N SERH 112 14.814-16.62824.769 1.0015.10 ATOM 3047 CA SER H 112 15.002-16.38526.179 1.0017.45 ATOM 3048 CB SERH 112 13.877-15.495 26.689 1.0017.57 ATOM 3049 OG SER H 112 14.108-15.15428.028 1.0018.71 ATOM 3051 C SERH 112 14.966-17.67326.950 1.0018.74 ATOM 3052 O SERH 112 14.128-18.52226.691 1.0021.32 ATOM 3053 N SERH 113 15.847-17.80727.923 1.0022.03 ATOM 3055 CA SERH 113 15.786-18.96628.831 1.0026.34 ATOM 3056 CB SERH 113 17.195-19.28729.323 1.0028.00 ATOM 3057 OG SERH 113 17.820-18.12229.857 1.0035.95 ATOM 3059 C SERH 113 14.807-18.75830.055 1.0026.98 ATOM 3060 O SERH 113 14.655-19.66430.898 1.0026.75 ATOM 3061 N ALA H 114 14.139-17.57930.126 1.0025.34 ATOM 3063 CA ALA H 114 13.236-17.25931.225 1.0023.14 ATOM 3064 CB ALA H 114 12.850-15.78231.187 1.0022.38 ATOM 3065 C ALA H 114 11.977-18.11631.207 1.0024.60 ATOM 3066 O ALA H 114 11.432-18.441 30.128 1.0024.23 ATOM 3067 N LYSH 115 11.502-18.45932.429 1.0023.35 ATOM 3069 CA LYS HI 15 10.298-19.26032.595 1.0023.70 ATOM 3070 CB LYSH 115 10.436-20.151 33.818 1.0024.56 ATOM 3071 CG LYSH 115 11.651 -21.03433.784 1.0031.61 ATOM 3072 CD LYSH 115 11.555-22.12434.846 1.0037.03 ATOM 3073 CE LYSH 115 12.681-23.14934.714 1.0036.28 ATOM 3074 NZ LYSH 115 12.625-24.161 35.810 1.0037.66 ATOM 3078 C LYSH 115 9.075-18.37632.767 1.0021.83 ATOM 3079 O LYS HI 15 9.186-17.21933.163 1.0019.35 ATOM 3080 N THRH 116 7.896-18.92432.501 1.0022.54 ATOM 3082 CA THRH 116 6.699-18.13632.650 1.0025.02 ATOM 3083 CB THRH 116 5.433-18.95432.354 1.0028.05 ATOM 3084 OG1 THRH 116 5.489-19.41730.987 1.0031.99 ATOM 3086 CG2THRH 116 4.169-18.11832.551 1.0025.98 ATOM 3087 C THR HI 16 6.669-17.593 34.044 1.0023.95 ATOM 3088 O THRH 116 7.081-18.26434.978 1.0023.92 ATOM 3089 N THRH 117 6.245-16.37234.180 1.0024.46 ATOM 3091 CA THRH 117 6.273-15.69935.474 1.0022.17 ATOM 3092 CB THRH 117 7.625-14.99935.667 1.0022.94 ATOM 3093 OG1THRH 117 8.689-15.96735.507 1.0019.91 ATOM 3095 CG2THRH 117 7.726-14.36037.046 1.0025.03 ATOM 3096 C THRH 117 5.154-14.681 35.507 1.0022.41 ATOM 3097 O THRH 117 5.049-13.81034.631 1.0022.33 ATOM 3098 N PROH 118 4.248-14.801 36.473 1.0021.47 ATOM 3099 CD PROH 118 4.278-15.76637.615 1.0024.37 ATOM 3100 CA PROH 118 3.142-13.87736.594 1.0019.44 ATOM 3101 CB PROH 118 2.234-14.58037.605 1.0021.47 ATOM 3102 CG PROH 118 3.232- -15.199 38.533 1.0023.59 ATOM 3103 C PRO H 118 3.743 -1 12.58737.106 1.0016.22 ATOM 3104 O PROH 118 4.806- 12.611 37.749 1.0013.84 ATOM 3105 N PROH 119 3.163- 11.443 36.804 1.0014.35 ATOM 3106 CD PROH 119 1.953- -11.22735.990 1.0014.96 ATOM 3107 CA PROH 119 3.728- -10.18437.275 1.0014.79 ATOM 3108 CB PROH 119 3.056 -9.164 36.380 1.0013.18 ATOM 3109 CG PROH 119 1.696 -9.745 36.220 1.0013.05 ATOM 3110 C PROH 119 3.377 - 9.95838.716 1.0013.65 ATOM 3111 O PROH 119 2.303- 10.393 39.166 1.0014.64 ATOM 3112 N THRH 120 4.256 - •9.31439.447 1.0013.96 ATOM 3114 CA THRH 120 3.845 -8.83740.761 1.0012.82 ATOM 3115 CB THRH 120 4.977 -8.76541.775 1.005.50 ATOM 3116 OG1 THRH 120 5.844 -7.751 41.415 1.0020.74 ATOM 3118 CG2 THR H 120 5.757 -10.03041.829 1.008.80 ATOM 3119 C THR H 120 3.331 - 7.46940.486 1.00 8.85 ATOM 3120 O THR H 120 4.041 - ■6.675 39.868 1.0010.44 ATOM 3121 N VALH 121 2.070 • -7.221 40.800 1.0011.59 ATOM 3123 CA VALH 121 1.455 -5.91340.491 1.008.52 ATOM 3124 CB VALH 121 0.016 -6.08740.012 1.006.26 ATOM 3125 CGI VALH 121 -0.604 -4.73639.688 1.003.84 ATOM 3126 CG2 VALH 121 0.020 -6.995 38.800 1.009.50 ATOM 3127 C VALH 121 1.505 ■ ■4.97041.692 1.0012.01 ATOM 3128 O VALH 121 1.230 ■ -5.37642.828 1.0010.41 ATOM 3129 N TYRH 122 1.888 - ■3.72641.451 1.0011.35 ATOM 3131 CA TYRH 122 2.097 -2.781 42.546 1.0011.02 ATOM 3132 CB TYR H 122 3.596 -2.47742.719 1.007.81 ATOM 3133 CG TYR H 122 4.435 -3.67643.129 1.0015.44 ATOM 3134 CD1 TYRH 122 4.108 -4.421 44.284 1.0016.70 ATOM 3135 CEl TYRH 122 4.872 -5.51644.695 1.0012.55 ATOM 3136 CD2 TYR H 122 5.555 -4.061 42.394 1.007.91 ATOM 3137 CE2TYRH 122 6.327 -5.14242.788 1.00 8.28 ATOM 3138 CZ TYRH 122 5.989 -5.86843.948 1.0011.52 ATOM 3139 OH TYRH 122 6.829 -6.861 44.411 1.0011.02 ATOM 3141 C TYRH 122 1.367 - ■1.51742.256 1.0012.61 ATOM 3142 O TYR H 122 1.477 ■ -0.95641.204 1.0011.44 ATOM 3143 N PRO H 123 0.615 - •1.02743.196 1.0018.80 ATOM 3144 CD PRO H 123 0.495 -1.53244.586 1.0019.13 ATOM 3145 CA PRO H 123 -0.158 0.19943.018 1.0018.57 ATOM 3146 CB PRO H 123 -1.108 0.14244.202 1.0015.86 ATOM 3147 CG PRO H 123 -0.200 -0.37745.251 1.0019.34 ATOM 3148 C PRO H 123 0.767 1.38743.094 1.0018.37 ATOM 3149 O PRO H 123 1.745 1.37243.851 1.0024.31 ATOM 3150 N LEU H 124 0.492 2.39442.302 1.0017.89 ATOM 3152 CA LEU H 124 1.279 3.60742.355 1.0018.57 ATOM 3153 CB LEU H 124 1.976 3.88441.033 1.0017.71 ATOM 3154 CG LEU H 124 2.958 2.81240.543 1.0020.67 ATOM 3155 CD1 LEUH 124 3.674 3.321 39.317 1.0018.20 ATOM 3156 CD2 LEU H 124 3.932 2.391 41.659 1.0018.24 ATOM 3157 C LEUH 124 0.402 4.78842.763 1.0018.06 ATOM 3158 O LEU H 124 -0.459 5.26341.988 1.0014.26 ATOM 3159 N ALA H 125 0.575 5.193 44.024 1.0018.65 ATOM 3161 CA ALA H 125 -0.181 6.29944.575 1.0016.82 ATOM 3162 CB ALA H 125 -0.606 6.00546.015 1.0013.74 ATOM 3163 C ALA H 125 0.678 7.52844.508 1.0015.68 ATOM 3164 O ALA H 125 1.893 7.43544.519 1.0016.41 ATOM 3165 N PRO H 126 0.066 8.687 44.406 1.00 16.40 ATOM 3166 CD PRO H 126 - 1.408 8.891 44.357 1.00 13.85 ATOM 3167 CA PRO H 126 0.790 9.954 44.329 1.00 16.02 ATOM 3168 CB PRO H 126 -0.346 10.988 44.293 1.00 15.53 ATOM 3169 CG PRO H 126 -1.468 10.210 43.677 1.00 14.07 ATOM 3170 C PRO H 126 1.753 .10.168 45.504 1.00 18.31 ATOM 3171 O PRO H 126 1.470 9.847 46.678 1.00 16.34 ATOM 3172 N GLY H 127 2.898 10.680 45.169 1.00 22.48 ATOM 3174 CA GLY H 127 3.870 10.970 46.171 1.00 30.63 ATOM 3175 C GLY H 127 3.658 1 12.353 46.704 1.00 33.75 ATOM 3176 OT1 GLY H 127 4.436 13.259 46.288 1.00 39.27 ATOM 3177 OT2 GLY H 127 2.699 12.543 47.515 1.00 35.28 ATOM 3178 CB ALA H 134 -7.913 19.970 39.281 1.00 21.74 ATOM 3179 C ALA H 134 -8.371 17.522 : 39.464 1.00 25.40 ATOM 3180 O ALA H 134 -9.444 16.941 39.284 1.00 26.02 ATOM 3183 N ALA H 134 -7.293 18.763 41.334 1.00 24.67 ATOM 3185 CA ALA H 134 -8.300 18.856 40.227 1.00 23.36 ATOM 3186 N MET H 135 -7.220 17.078 38.992 1.00 24.22 ATOM 3188 CA MET H 135 -7.086 15.795 38.331 1.00 26.09 ATOM 3189 CB MET H 135 -6.690 15.998 36.848 1.00 30.45 ATOM 3190 CG MET H 135 -7.856 16.182 35.864 1.00 34.99 ATOM 3191 SD MET H 135 -8.959 14.726 35.832 1.00 46.83 ATOM 3192 CE MET H 135 -8.963 14.248 34.104 1.00 42.78 ATOM 3193 C MET H 135 -5.970 15.087 39.063 1.00 25.74 ATOM 3194 O MET H 135 -5.013 15.747 39.498 1.00 25.90 ATOM 3195 N VAL H 136 -6.072 13.787 39.250 1.00 22.09 ATOM 3197 CA VAL H 136 -5.000 13.075 39.925 1.00 18.97 ATOM 3198 CB VAL H 136 -5.421 12.616 41.358 1.00 16.24 ATOM 3199 CGI VAL H 136 -6.664 1 1.760 41.344 1.00 15.37 ATOM 3200 CG2 VAL H 136 -4.273 1 1.897 42.010 1.00 16.51 ATOM 3201 C VAL H 136 -4.563 1 1.886 39.090 1.00 17.30 ATOM 3202 O VAL H 136 -5.405 1 1.217 38.482 1.00 17.97 ATOM 3203 N THR H 137 -3.256 11.641 39.022 1.00 17.82 ATOM 3205 CA THR H 137 -2.783 10.485 38.267 1.00 18.38 ATOM 3206 CB THR H 137 -1.716 10.872 37.253 1.00 15.72 ATOM 3207 OG1 THR H 137 -2.296 1 1.858 36.377 1.00 16.58 ATOM 3209 CG2 THR H 137 -1.310 9.661 36.419 1.00 13.21 ATOM 3210 C THR H 137 -2.294 9.340 39.158 1.00 16.41 ATOM 3211 O THR H 137 -1.419 9.516 40.024 1.00 14.38 ATOM 3212 N LEU H 138 -2.933 8.188 38.935 1.00 13.46 ATOM 3214 CA LEU H 138 -2.625 6.956 39.639 1.00 11.93 ATOM 3215 CB LEU H 138 -3.906 6.404 40.218 1.00 9.54 ATOM 3216 CG LEU H 138 -4.695 7.398 41.034 1.00 9.64 ATOM 3217 CD1 LEU H 138 -5.924 6.726 41.571 1.00 1 1.85 ATOM 3218 CD2 LEU H 138 -3.824 7.938 42.158 1.00 6.56 ATOM 3219 C LEU H 138 -2.053 5.967 38.641 1.00 12.78 ATOM 3220 O LEU H 138 -2.303 6.091 37.448 1.00 10.57 ATOM 3221 N GLY H 139 -1.309 5.004 39.097 1.00 11.80 ATOM 3223 CA GLY H 139 -0.771 4.050 38.164 1.00 11.77 ATOM 3224 C GLY H 139 -0.576 2.690 38.756 1.00 14.58 ATOM 3225 O GLY H 139 -0.870 2.454 39.927 1.00 14.52 ATOM 3226 N CYS H 140 -0.069 1.797 37.952 1.00 13.05 ATOM 3228 CA CYS H 140 0.194 0.461 38.377 1.00 12.15 ATOM 3229 CB CYS H 140 -0.944 -0.465 37.972 1.00 15.82 ATOM 3230 SG CYS H 140 -1.988 -0.926 39.377 1.00 30.05 ATOM 3231 C CYS H 140 1.443 -0.023 37.760 1.00 9.66 ATOM 3232 O CYS H 140 1.589 0.1 18 36.543 1.00 8.35 ATOM 3233 N LEU H 141 2.338 -0.552 38.590 1.00 6.85 ATOM 3235 CA LEU H 141 3.558 -1.210 38.113 1.00 10.45 ATOM 3236 CB LEU H 141 4.732 - 1.024 39.080 1.00 3.00 ATOM 3237 CG LEU H 141 6.079 - 1.654 38.695 1.00 7.34 ATOM 3238 CD1 LEU H 141 6.582 -1.1 17 37.363 1.00 7.63 ATOM 3239 CD2 LEU H 141 7.1 18 - 1.354 39.745 1.00 2.28 ATOM 3240 C LEU H 141 3.31 1 -2.709 37.952 1.00 9.22 ATOM 3241 O LEU H 141 2.869 -3.368 38.884 1.00 8.85 ATOM 3242 N VAL H 142 3.557 -3.220 36.756 1.00 10.01 ATOM 3244 CA VAL H 142 3.455 -4.640 36.485 1.00 7.47 ATOM 3245 CB VAL H 142 2.615 -4.880 35.208 1.00 10.12 ATOM 3246 CGI VAL H 142 2.384 -6.392 34.957 1.00 8.96 ATOM 3247 CG2 VAL H 142 1.282 -4.149 35.351 1.00 6.58 ATOM 3248 C VAL H 142 4.883 -5.162 36.345 1.00 1 1.16 ATOM 3249 O VAL H 142 5.512 -5.095 35.254 1.00 6.29 ATOM 3250 N LYS H 143 5.398 -5.687 37.452 1.00 9.75 ATOM 3252 CA LYS H 143 6.81 1 -6.007 37.531 1.00 12.16 ATOM 3253 CB LYS H 143 7.354 -5.430 38.840 1.00 9.61 ATOM 3254 CG LYS H 143 8.872 -5.352 38.953 1.00 9.64 ATOM 3255 CD LYS H 143 9.272 -4.908 40.356 1.00 1 1.17 ATOM 3256 CE LYS H 143 10.790 -4.927 40.518 1.00 15.36 ATOM 3257 NZ LYS H 143 1 1.194 -4.987 41.953 1.00 13.08 ATOM 3261 C LYS H 143 7.170 -7.505 37.404 1.00 14.70 ATOM 3262 O LYS H 143 6.468 -8.388 37.894 1.00 17.80 ATOM 3263 N GLY H 144 8.247 -7.741 36.666 1.00 16.56 ATOM 3265 CA GLY H 144 8.889 -9.060 36.589 1.00 18.62 ATOM 3266 C GLY H 144 8.106 -10.220 36.012 1.00 16.58 ATOM 3267 O GLY H 144 8.220 -11.321 36.532 1.00 20.26 ATOM 3268 N TYR H 145 7.371 -10.01 1 34.931 1.00 15.03 ATOM 3270 CA TYR H 145 6.630 -11.1 11 34.294 1.00 12.99 ATOM 3271 CB TYR H 145 5.217 -10.675 33.851 1.00 10.99 ATOM 3272 CG TYR H 145 5.137 -9.598 32.797 1.00 13.14 ATOM 3273 CD1 TYR H 145 5.41 1 -8.278 33.126 1.00 15.73 ATOM 3274 CEl TYR H 145 5.280 -7.269 32.194 1.00 12.07 ATOM 3275 CD2 TYR H 145 4.728 -9.867 31.485 1.00 15.71 ATOM 3276 CE2 TYR H 145 4.598 -8.843 30.532 1.00 9.54 ATOM 3277 CZ TYR H 145 4.879 -7.548 30.902 1.00 10.77 ATOM 3278 OH TYR H 145 4.820 -6.506 29.978 1.00 9.76 ATOM 3280 C TYR H 145 7.389 -1 1.662 33.088 1.00 13.49 ATOM 3281 O TYR H 145 8.389 -1 1.098 32.669 1.00 12.72 ATOM 3282 N PHE H 146 6.931 -12.800 32.589 1.00 16.82 ATOM 3284 CA PHE H 146 7.455 -13.385 31.361 1.00 18.55 ATOM 3285 CB PHE H 146 8.887 -13.880 31.495 1.00 18.86 ATOM 3286 CG PHE H 146 9.385 -14.479 30.188 1.00 23.23 ATOM 3287 CD1 PHE H 146 10.168 -13.728 29.327 1.00 25.00 ATOM 3288 CD2 PHE H 146 8.957 -15.751 29.761 1.00 24.90 ATOM 3289 CEl PHE H 146 10.506 -14.210 28.054 1.00 26.32 ATOM 3290 CE2 PHE H 146 9.282 -16.240 28.506 1.00 26.32 ATOM 3291 CZ PHE H 146 10.054 -15.469 27.644 1.00 25.16 ATOM 3292 C PHE H 146 6.642 -14.565 31.019 1.00 19.54 ATOM 3293 O PHE H 146 6.360 -15.333 31.930 1.00 18.10 ATOM 3294 N PRO H 147 6.211 -14.757 29.720 1.00 21.47 ATOM 3295 CD PRO H 147 4.961 -15.458 29.393 1.00 21.60 ATOM 3296 CA PRO H 147 6.430 -13.882 28.555 1.00 21.86 ATOM 3297 CB PRO H 147 6.205 -14.891 27.401 1.00 21.39 ATOM 3298 CG PRO H 147 5.272-15.93828.004 1.0019.80 ATOM 3299 C PRO H 147 5.429-12.70628.486 1.0018.87 ATOM 3300 O PROH 147 4.621-12.53729.372 1.0015.77 ATOM 3301 N GLU H 148 5.438-11.97727.346 1.0019.05 ATOM 3303 CA GLU H 148 4.421-10.97627.061 1.0019.21 ATOM 3304 CB GLU H 148 4.991 -9.89626.155 1.0017.80 ATOM 3305 CG GLU H 148 6.141 -9.13826.738 1.0015.35 ATOM 3306 CD GLUH 148 6.495 -7.945 25.897 1.0019.90 ATOM 3307 OE1 GLUH 148 7.607 -7.93425.314 1.0023.72 ATOM 3308 OE2 GLUH 148 5.666 -7.00625.812 1.0017.13 ATOM 3309 C GLU H 148 3.306-11.661 26.286 1.0019.80 ATOM 3310 O GLUH 148 3.507-12.75925.820 1.0021.47 ATOM 3311 N PRO H 149 2.099-11.07926.136 1.0019.34 ATOM 3312 CD PRO H 149 0.864-11.83025.967 1.0015.47 ATOM 3313 CA PRO H 149 1.670 -9.80826.680 1.0018.47 ATOM 3314 CB PRO H 149 0.574 -9.44025.693 1.0018.21 ATOM 3315 CG PRO H 149 0.055-10.79725.219 1.0017.16 ATOM 3316 C PRO H 149 1.117 -9.89028.128 1.0018.85 ATOM 3317 O PRO H 149 1.138-10.91228.825 1.0016.35 ATOM 3318 N VALH 150 0.431 -8.81228.426 1.0019.66 ATOM 3320 CA VALH 150 -0.234 -8.56229.666 1.0016.78 ATOM 3321 CB VALH 150 0.808 -7.95230.654 1.0016.55 ATOM 3322 CGI VALH 150 0.424 -6.57431.111 1.0017.59 ATOM 3323 CG2 VALH 150 1.049 -8.87931.803 1.0013.17 ATOM 3324 C VALH 150 -1.328 -7.57829.276 1.0016.49 ATOM 3325 O VALH 150 -1.179 -6.84428.299 1.0018.33 ATOM 3326 N THRH 151 -2.454 -7.63729.908 1.0014.32 ATOM 3328 CA THRH 151 -3.518 -6.69529.627 1.0014.69 ATOM 3329 CB THRH 151 -4.767 -7.41529.063 1.0017.81 ATOM 3330 OG1 THRH 151 -5.363 -8.243 30.083 1.0022.14 ATOM 3332 CG2 THRH 151 -4.366 -8.31827.887 1.0020.30 ATOM 3333 C THRH 151 -3.895 -5.975 30.913 1.0013.72 ATOM 3334 O THRH 151 -4.185 -6.62731.907 1.0013.94 ATOM 3335 N VALH 152 -3.914 -4.65030.867 1.0012.98 ATOM 3337 CA VALH 152 -4.179 -3.83832.043 1.0012.73 ATOM 3338 CB VALH 152 -2.978 -2.93432.366 1.0011.49 ATOM 3339 CGI VALH 152 -3.293 -2.08033.597 1.0011.37 ATOM 3340 CG2 VALH 152 -1.722 -3.76832.599 1.009.03 ATOM 3341 C VALH 152 -5.406 -2.95731.861 1.0015.95 ATOM 3342 O VAL H 152 -5.471 -2.15030.915 1.0019.74 ATOM 3343 N THRH 153 -6.392 -3.13032.752 1.0019.44 ATOM 3345 CA THRH 153 -7.597 -2.315 32.735 1.0019.80 ATOM 3346 CB THRH 153 -8.853 -3.18432.492 1.0021.72 ATOM 3347 OG1 THRH 153 -8.787 -4.32933.329 1.0026.52 ATOM 3349 CG2THRH153 -8.933 -3.64031.043 1.0021.56 ATOM 3350 C THRH 153 -7.761 -1.51634.059 1.0017.98 ATOM 3351 O THRH 153 -7.031 -1.72835.029 1.0017.86 ATOM 3352 N TRPH 154 -8.689 -0.56634.061 1.0018.02 ATOM 3354 CA TRPH 154 -8.952 0.23035.234 1.0016.37 ATOM 3355 CB TRPH 154 -8.433 1.61835.037 1.0015.29 ATOM 3356 CG TRPH 154 -6.952 1.64634.971 1.0014.01 ATOM 3357 CD2 TRPH 154 -6.067 1.82336.081 1.0014.22 ATOM 3358 CE2 TRPH 154 -4.758 1.89635.568 1.0012.55 ATOM 3359 CE3 TRPH 154 -6.266 1.94937.475 1.0013.71 ATOM 3360 CD 1 TRPH 154 -6.177 1.60033.856 1.0013.72 ATOM 3361 NE1 TRPH 154 -4.866 1.751 34.220 1.0014.65 ATOM 3363 CZ2TRPH154 -3.652 2.09636.372 1.0011.60 ATOM 3364 CZ3 TRPH 154 -5.166 2.15738.276 1.0013.74 ATOM 3365 CH2 TRPH 154 -3.873 2.23237.715 1.0015.50 ATOM 3366 C TRPH 154 -10.420 0.22635.491 1.0016.57 ATOM 3367 O TRPH 154 -11.208 0.455 34.582 1.0019.07 ATOM 3368 N ASNH 155 -10.778 -0.068 36.722 1.0018.63 ATOM 3370 CA ASNH155 -12.180 -0.281 37.110 1.0019.34 ATOM 3371 CB ASN H 155 -12.891 1.04837.320 1.0019.07 ATOM 3372 CG ASNH 155 -12.490 1.66838.645 1.0019.37 ATOM 3373 OD1 ASNH 155 -11.779 1.057 39.456 1.0017.72 ATOM 3374 ND2 ASNH 155 -12.921 2.88938.867 1.0021.85 ATOM 3377 C ASN H 155 -12.904 -1.17036.102 1.0020.59 ATOM 3378 O ASN H 155 -13.986 -0.84835.618 1.0019.83 ATOM 3379 N SERH 156 -12.241 -2.298 35.766 1.0022.94 ATOM 3381 CA SERH 156 -12.750 -3.25934.796 1.0023.80 ATOM 3382 CB SERH 156 -14.038 -3.89035.323 1.0024.08 ATOM 3383 OG SERH 156 -13.792 -4.57636.536 1.0023.19 ATOM 3385 C SERH 156 -12.976 -2.65833.389 1.0026.88 ATOM 3386 O SERH 156 -13.725 -3.203 32.568 1.0029.20 ATOM 3387 N GLYH 157 -12.320 -1.55733.089 1.0026.24 ATOM 3389 CA GLY H 157 -12.519 -0.96731.796 1.0028.52 ATOM 3390 C GLY H 157 -13.571 0.13831.791 1.0028.13 ATOM 3391 O GLY H 157 -13.806 0.76030.749 1.0028.70 ATOM 3392 N SERH 158 -14.208 0.38232.944 1.0027.82 ATOM 3394 CA SERH 158 -15.168 1.46033.047 1.0027.17 ATOM 3395 CB SERH 158 -16.060 1.313 34.323 1.0028.51 ATOM 3396 OG SERH 158 -15.374 1.57935.535 1.0025.88 ATOM 3398 C SERH 158 -14.409 2.77633.013 1.0027.55 ATOM 3399 O SERH 158 -14.917 3.781 32.545 1.0028.23 ATOM 3400 N LEUH 159 -13.174 2.75633.524 1.0029.42 ATOM 3402 CA LEUH 159 -12.285 3.89433.378 1.0030.68 ATOM 3403 CB LEUH 159 -11.275 3.96934.519 1.0031.18 ATOM 3404 CG LEUH 159 -11.742 4.64735.816 1.0029.87 ATOM 3405 CD1 LEUH 159 -10.617 4.653 36.846 1.0034.45 ATOM 3406 CD2 LEUH 159 -12.180 6.06235.529 1.0029.03 ATOM 3407 C LEUH 159 -11.562 3.691 32.072 1.0031.97 ATOM 3408 O LEUH 159 -10.552 3.001 32.022 1.0031.21 ATOM 3409 N ALA H 160 -12.155 4.21731.009 1.0034.61 ATOM 3411 CA ALAH 160 -11.612 4.06229.651 1.0035.80 ATOM 3412 CB ALA H 160 -12.774 3.83528.686 1.0034.51 ATOM 3413 C ALA H 160 -10.777 5.29329.237 1.0035.27 ATOM 3414 O ALA H 160 -9.618 5.18528.786 1.0034.38 ATOM 3415 N SERH 161 -11.364 6.45929.407 1.0033.77 ATOM 3417 CA SERH 161 -10.671 7.70429.107 1.0033.98 ATOM 3418 CB SERH 161 -11.692 8.84229.075 1.0033.96 ATOM 3419 OG SERH 161 -12.991 8.335 28.755 1.0038.30 ATOM 3421 C SERH 161 -9.605 7.99630.175 1.0030.88 ATOM 3422 O SERH 161 -9.745 7.60431.345 1.0032.73 ATOM 3423 N GLYH 162 -8.540 8.66429.773 1.0028.58 ATOM 3425 CA GLY H 162 -7.509 9.053 30.740 1.0023.36 ATOM 3426 C GLYH 162 -6.481 7.985 31.068 1.0019.44 ATOM 3427 O GLYH 162 -5.660 8.18231.988 1.0017.19 ATOM 3428 N VAL H 163 -6.484 6.88630.290 1.0016.90 ATOM 3430 CA VALH 163 -5.563 5.79030.522 1.0014.28 ATOM 3431 CB VAL H 163 -6.248 4.44730.286 1.0011.19 ATOM 3432 CGI VALH 163 -5.249 3.311 30.466 1.009.55 ATOM 3433 CG2 VAL H 163 -7.394 4.309 31.280 1.00 8.14 ATOM 3434 C VAL H 163 -4.334 5.883 29.638 1.00 16.70 ATOM 3435 O VAL H 163 -4.426 6.310 28.494 1.00 20.46 ATOM 3436 N HIS H 164 -3.208 5.502 30.172 1.00 12.44 ATOM 3438 CA HIS H 164 - 1.976 5.465 29.432 1.00 12.24 ATOM 3439 CB HIS H 164 -1.063 6.591 29.851 1.00 12.04 ATOM 3440 CG HIS H 164 - 1.358 7.848 29.181 1.00 17.45 ATOM 3441 CD2 HIS H 164 - 1.800 9.033 29.657 1.00 16.45 ATOM 3442 ND1 HIS H 164 - 1.1 1 1 8.037 27.847 1.00 19.78 ATOM 3444 CEl HIS H 164 -1.352 9.251 27.488 .00 18.88 ATOM 3445 NE2 HIS H 164 - 1.763 9.876 28.571 .00 19.92 ATOM 3447 C HIS H 164 -1.262 4.216 29.770 1.00 12.66 ATOM 3448 O HIS H 164 -0.943 4.023 30.924 1.00 12.50 ATOM 3449 N THR H 165 -1.030 3.348 28.825 1.00 12.38 ATOM 3451 CA THR H 165 -0.208 2.196 29.132 1.00 10.10 ATOM 3452 CB THR H 165 -0.949 0.879 28.952 1.00 9.55 ATOM 3453 OG1 THR H 165 -2.152 0.949 29.722 1.00 11.21 ATOM 3455 CG2 THR H 165 -0.1 15 -0.286 29.439 1.00 8.04 ATOM 3456 C THR H 165 1.042 2.239 28.295 1.00 1 1.67 ATOM 3457 O THR H 165 0.977 2.443 27.089 1.00 10.32 ATOM 3458 N PHE H 166 2.174 2.052 28.974 1.00 1 1.57 ATOM 3460 CA PHE H 166 3.499 2.190 28.390 1.00 12.01 ATOM 3461 CB PHE H 166 4.382 2.951 29.407 1.00 9.65 ATOM 3462 CG PHE H 166 3.765 4.283 29.822 1.00 8.07 ATOM 3463 CD1 PHE H 166 2.849 4.351 30.868 1.00 4.17 ATOM 3464 CD2 PHE H 166 4.004 5.456 29.073 1.00 10.68 ATOM 3465 CEl PHE H 166 2.155 5.547 31.155 1.00 8.24 ATOM 3466 CE2 PHE H 166 3.314 6.654 29.355 1.00 11.02 ATOM 3467 CZ PHE H 166 2.386 6.698 30.394 1.00 5.44 ATOM 3468 C PHE H 166 4.1 16 0.815 28.006 1.00 15.40 ATOM 3469 O PHE H 166 3.583 -0.249 28.404 1.00 16.48 ATOM 3470 N PRO H 167 5.210 0.826 27.164 1.00 14.51 ATOM 3471 CD PRO H 167 5.803 2.030 26.521 1.00 14.57 ATOM 3472 CA PRO H 167 5.919 -0.378 26.684 1.00 13.56 ATOM 3473 CB PRO H 167 6.884 0.166 25.595 1.00 15.95 ATOM 3474 CG PRO H 167 6.303 1.479 25.213 1.00 15.19 ATOM 3475 C PRO H 167 6.720 -1.095 27.757 1.00 13.70 ATOM 3476 O PRO H 167 7.321 -0.457 28.630 1.00 8.91 ATOM 3477 N ALA H 168 6.767 -2.424 27.618 1.00 14.48 ATOM 3479 CA ALA H 168 7.506 -3.277 28.526 1.00 13.11 ATOM 3480 CB ALA H 168 7.212 -4.746 28.240 1.00 12.04 ATOM 3481 C ALA H 168 8.982 -3.020 28.403 1.00 15.12 ATOM 3482 O ALA H 168 9.496 -2.687 27.332 1.00 14.20 ATOM 3483 N VAL H 169 9.661 -3.093 29.519 1.00 14.23 ATOM 3485 CA VAL H 169 1 1.077 -2.965 29.524 1.00 11.53 ATOM 3486 CB VAL H 169 1 1.614 -1.828 30.480 1.00 10.77 ATOM 3487 CG I VAL H 169 1 1.381 -0.451 29.880 1.00 5.38 ATOM 3488 CG2 VAL H 169 10.921 -1.887 31.820 1.00 8.65 ATOM 3489 C VAL H 169 11.569 -4.309 29.970 1.00 14.43 ATOM 3490 O VAL H 169 10.861 -4.991 30.697 1.00 13.16 ATOM 3491 N LEU H 170 12.714 -4.721 29.457 1.00 16.49 ATOM 3493 CA LEU H 170 13.336 -5.954 29.891 1.00 20.55 ATOM 3494 CB LEU H 170 13.963 -6.711 28.694 1.00 17.41 ATOM 3495 CG LEU H 170 14.387 -8.182 28.942 1.00 16.89 ATOM 3496 CD1 LEU H 170 13.184 -9.004 29.309 1.00 11.20 ATOM 3497 CD2 LEU H 170 15.058 -8.781 27.707 1.00 13.43 ATOM 3498 C LEUH 170 14.400 -5.625 30.916 1.0021.20 ATOM 3499 O LEUH 170 15.390 -4.963 30.619 1.0023.98 ATOM 3500 N GLNH 171 14.169 -6.02832.146 1.0025.48 ATOM 3502 CA GLNH 171 15.157 -5.823 33.175 1.0027.97 ATOM 3503 CB GLNH 171 14.916 -4.492 33.962 1.0033.14 ATOM 3504 CG GLNH 171 13.467 -4.06834.268 1.0035.78 ATOM 3505 CD GLNH 171 13.319 -2.53034.449 1.0041.72 ATOM 3506 OE1 GLNH 171 14.162 -1.751 33.979 1.0043.19 ATOM 3507 NE2 GLN H 171 12.253 -2.07835.114 1.0039.50 ATOM 3510 C GLNH 171 15.230 -7.04234.083 1.0030.85 ATOM 3511 O GLNH 171 14.312 -7.308 34.873 1.0030.30 ATOM 3512 N ALA H 172 16.307 -7.81733.893 1.0030.98 ATOM 3514 CA ALAH 172 16.568 -9.03934.690 1.0032.89 ATOM 3515 CB ALA H 172 16.053 -8.885 36.145 1.0034.56 ATOM 3516 C ALA H 172 15.964-10.291 34.039 1.0032.42 ATOM 3517 O ALA H 172 15.553-11.23934.741 1.0033.51 ATOM 3518 N ALAH 173 15.982-10.303 32.683 1.0028.84 ATOM 3520 CA ALAH 173 15.370-11.36631.889 1.0024.12 ATOM 3521 CB ALAH 173 15.884-12.75432.279 1.0024.73 ATOM 3522 C ALA H 173 13.860-11.32932.002 1.0022.90 ATOM 3523 O ALAH 173 13.186-12.16931.437 1.0024.63 ATOM 3524 N LEU H 174 13.314-10.34732.714 1.0019.03 ATOM 3526 CA LEUH 174 11.868-10.28432.897 1.0016.09 ATOM 3527 CB LEU H 174 11.502-10.52734.386 1.0013.53 ATOM 3528 CG LEUH 174 11.823-11.921 35.008 1.0013.70 ATOM 3529 CD1 LEUH 174 11.399-11.92736.487 1.0013.19 ATOM 3530 CD2 LEUH 174 11.093-13.033 34.243 1.007.07 ATOM 3531 C LEUH 174 11.366 -8.93432.444 1.0011.64 ATOM 3532 O LEU H 174 12.095 -7.98032.520 1.0013.03 ATOM 3533 N TYRH 175 10.153 -8.88731.980 1.0011.45 ATOM 3535 CA TYRH 175 9.546 -7.64431.500 1.0013.69 ATOM 3536 CB TYRH 175 8.505 -7.91730.412 1.0013.82 ATOM 3537 CG TYRH 175 9.047 -8.55929.178 1.0014.75 ATOM 3538 CD1 TYRH 175 9.965 -7.89028.395 1.0017.41 ATOM 3539 CEl TYRH 175 10.503 -8.45427.241 1.0018.34 ATOM 3540 CD2TYRH 175 8.651 -9.82728.790 1.0018.01 ATOM 3541 CE2 TYRH 175 9.174-10.40827.633 1.0020.37 ATOM 3542 CZ TYRH 175 10.106 -9.71026.864 1.0019.65 ATOM 3543 OH TYRH 175 10.628-10.26525.726 1.0021.14 ATOM 3545 C TYRH 175 8.813 -6.86432.614 1.0016.88 ATOM 3546 O TYRH 175 8.188 -7.44833.534 1.0015.69 ATOM 3547 N THRH 176 8.827 -5.545 32.462 1.0014.27 ATOM 3549 CA THRH 176 8.125 -4.65433.374 1.0013.28 ATOM 3550 CB THRH 176 9.101 -3.93234.349 1.0011.07 ATOM 3551 OG1 THRH 176 9.699 -4.85735.280 1.009.99 ATOM 3553 CG2 THRH 176 8.353 -2.85535.118 1.007.94 ATOM 3554 C THRH 176 7.416 -3.58432.574 1.0011.40 ATOM 3555 O THRH 176 8.015 -2.99931.677 1.0010.96 ATOM 3556 N LEUH 177 6.156 -3.34732.837 1.009.44 ATOM 3558 CA LEU H 177 5.528 -2.19032.216 1.0011.96 ATOM 3559 CB LEUH 177 4.765 -2.521 30.918 1.0012.44 ATOM 3560 CG LEU H 177 3.542 -3.43230.927 1.0013.51 ATOM 3561 CD1 LEUH 177 2.348 -2.76231.611 1.0016.92 ATOM 3562 CD2 LEU H 177 3.176 -3.74829.478 1.0019.97 ATOM 3563 C LEU H 177 4.689 -1.44233.231 1.0011.72 ATOM 3564 O LEUH 177 4.664 -1.831 34.398 1.0012.02 ATOM 3565 N SERH 178 4.091 -0.35632.826 1.009.83 ATOM 3567 CA SERH 178 3.261 0.42933.720 1.0012.66 ATOM 3568 CB SERH 178 3.993 1.66534.273 1.0016.23 ATOM 3569 OG SERH 178 5.061 1.325 35.106 1.0021.15 ATOM 3571 C SERH 178 2.068 0.941 32.983 1.0011.78 ATOM 3572 O SER H 178 2.047 0.97931.760 1.0012.05 ATOM 3573 N SERH 179 1.096 1.333 33.750 1.0010.09 ATOM 3575 CA SERH 179 -0.086 1.95433.244 1.009.78 ATOM 3576 CB SERH 179 -1.225 0.943 33.162 1.007.12 ATOM 3577 OG SERH 179 -2.371 1.44832.486 1.0013.99 ATOM 3579 C SERH 179 -0.437 3.04434.227 1.0011.73 ATOM 3580 O SERH 179 0.004 3.01235.394 1.0010.99 ATOM 3581 N SERH 180 -1.192 3.99933.772 1.0012.62 ATOM 3583 CA SERH 180 -1.629 5.08834.616 1.0011.78 ATOM 3584 CB SERH 180 -0.622 6.24734.486 1.0015.26 ATOM 3585 OG SERH 180 -0.758 6.93833.258 1.0015.98 ATOM 3587 C SERH 180 -3.039 5.53834.206 1.0011.26 ATOM 3588 O SERH 180 -3.413 5.31833.063 1.0012.64 ATOM 3589 N VALH 181 -3.841 6.06835.170 1.0012.70 ATOM 3591 CA VALH 181 -5.143 6.69734.893 1.0012.65 ATOM 3592 CB VALH 181 -6.394 6.14835.602 1.0014.52 ATOM 3593 CGI VALH 181 -7.465 5.80834.616 1.008.51 ATOM 3594 CG2 VALH 181 -6.086 5.07636.606 1.0015.67 ATOM 3595 C VALH 181 -5.126 8.06535.510 1.0013.40 ATOM 3596 O VALH 181 -4.564 8.23836.571 1.0010.66 ATOM 3597 N THRH 182 -5.816 8.99434.864 1.0015.42 ATOM 3599 CA THRH 182 -6.029 10.30035.418 1.0012.05 ATOM 3600 CB THRH 182 -5.483 11.39334.504 1.0012.00 ATOM 3601 OG1THRH 182 -4.068 11.185 34.369 1.0012.34 ATOM 3603 CG2THRH 182 -5.731 12.78635.097 1.0010.88 ATOM 3604 C THRH 182 -7.505 10.45235.623 1.0015.30 ATOM 3605 O THRH 182 -8.310 10.221 34.702 1.0015.69 ATOM 3606 N VALH 183 -7.851 10.74736.872 1.0015.89 ATOM 3608 CA VALH 183 -9.237 10.91237.302 1.0015.70 ATOM 3609 CB VALH 183 -9.692 9.77238.276 1.0013.11 ATOM 3610 CGI VALH 183 -9.861 8.47237.519 1.0016.73 ATOM 3611 CG2 VALH 183 -8.678 9.585 39.374 1.007.49 ATOM 3612 C VALH 183 -9.375 12.221 38.050 1.0014.30 ATOM 3613 O VALH 183 -8.395 12.76038.516 1.0015.26 ATOM 3614 N PROH 184 -10.592 12.76838.177 1.0015.74 ATOM 3615 CD PROH 184 -11.860 12.25537.668 1.0015.39 ATOM 3616 CA PROH 184 -10.784 14.00738.906 1.0016.30 ATOM 3617 CB PROH 184 -12.282 14.28938.757 1.0015.06 ATOM 3618 CG PROH 184 -12.662 13.51637.544 1.0015.56 ATOM 3619 C PROH 184 -10.429 13.70440.341 1.0015.62 ATOM 3620 O PROH 184 -10.859 12.70740.872 1.0017.90 ATOM 3621 N SERH 185 -9.648 14.52740.960 1.0021.17 ATOM 3623 CA SERH 185 -9.288 14.311 42.349 1.0023.69 ATOM 3624 CB SERH 185 -8.371 15.43642.815 1.0026.61 ATOM 3625 OG SERH 185 -8.807 16.68542.271 1.0031.23 ATOM 3627 C SERH 185 -10.533 14.241 43.255 1.0026.32 ATOM 3628 O SERH 185 -10.466 13.73744.376 1.0029.50 ATOM 3629 N SERH 186 -11.681 14.74342.795 1.0025.25 ATOM 3631 CA SERH 186 -12.880 14.64943.614 1.0025.46 ATOM 3632 CB SERH 186 -14.011 15.50443.021 1.0026.27 ATOM 3633 OG SERH 186 -14.531 14.97241.797 1.0029.82 ATOM 3635 C SERH 186 -13.358 13.18543.753 1.0024.07 ATOM 36360 SERH 186 -14.198 12.90444.574 1.0024.17 ATOM 3637 N THRH 187 -12.808 12.26042.950 1.0021.70 ATOM 3639 CA THRH 187 -13.302 10.87042.943 1.0021.99 ATOM 3640 CB THRH 187 -13.701 10.44841.520 1.0020.90 ATOM 3641 OG1 THRH 187 -12.531 10.45540.684 1.0018.99 ATOM 3643 CG2THRH187 -14.724 11.40940.950 1.0018.74 ATOM 3644 C THRH 187 -12.278 9.86443.489 1.0023.01 ATOM 3645 O THRH 187 -12.507 8.64643.487 1.0023.61 ATOM 3646 N TRPH 188 -11.142 10.38043.909 1.0020.48 ATOM 3648 CA TRPH 188 -10.135 9.57544.530 1.0021.24 ATOM 3649 CB TRPH 188 -9.132 8.96843.515 1.0015.29 ATOM 3650 CG TRPH 188 -8.154 8.00744.178 1.0011.67 ATOM 3651 CD2 TRPH 188 -6.858 8.32444.777 1.00 8.04 ATOM 3652 CE2 TRPH 188 -6.335 7.12845.303 1.00 8.99 ATOM 3653 CE3 TRPH 188 -6.099 9.50444.933 1.008.90 ATOM 3654 CD 1 TRPH 188 -8.344 6.65444.375 1.0013.61 ATOM 3655 NE1 TRPH 188 -7.254 6.14745.044 1.0014.95 ATOM 3657 CZ2 TRPH 188 -5.091 7.071 45.959 1.0012.53 ATOM 3658 CZ3 TRPH 188 -4.876 9.44745.589 1.0010.52 ATOM 3659 CH2 TRPH 188 -4.377 8.23346.092 1.0012.29 ATOM 3660 C TRPH 188 -9.392 10.46345.500 1.0020.69 ATOM 3661 O TRPH 188 -8.931 11.541 45.126 1.0020.70 ATOM 3662 N PROH 189 -9.147 9.971 46.705 1.0020.09 ATOM 3663 CD PROH 189 -8.337 10.64347.748 1.0022.74 ATOM 3664 CA PROH 189 -9.526 8.62447.137 1.0020.72 ATOM 3665 CB PROH 189 -8.474 8.32948.184 1.0022.60 ATOM 3666 CG PRO H 189 -8.368 9.64048.878 1.0020.47 ATOM 3667 C PROH 189 -10.918 8.38347.687 1.0021.08 ATOM 3668 O PROH 189 -11.094 7.39448.358 1.0022.85 ATOM 3669 N SERH 190 -11.905 9.21747.423 1.0023.42 ATOM 3671 CA SERH 190 -13.246 8.941 47.944 1.0021.96 ATOM 3672 CB SERH 190 -14.182 10.10247.648 1.0023.31 ATOM 3673 OG SERH 190 -14.424 10.22746.247 1.0023.23 ATOM 3675 C SERH 190 -13.818 7.67647.324 1.0024.54 ATOM 3676 O SERH 190 -14.576 6.93848.002 1.0025.15 ATOM 3677 N GLUH 191 -13.510 7.45645.998 1.0025.58 ATOM 3679 CA GLUH 191 -13.957 6.241 45.283 1.0023.69 ATOM 3680 CB GLUH 191 -14.744 6.55043.995 1.0025.22 ATOM 3681 CG GLUH 191 -15.871 7.57944.161 1.0028.53 ATOM 3682 CD GLUH 191 -16.929 7.22845.217 1.0028.30 ATOM 3683 OE1 GLU H 191 -16.805 6.17545.880 1.0031.06 ATOM 3684 OE2 GLUH 191 -17.893 8.01445.380 1.0026.40 ATOM 3685 C GLUH 191 -12.795 5.36744.946 1.0023.74 ATOM 3686 O GLU H 191 -11.649 5.81744.905 1.0021.49 ATOM 3687 N THRH 192 -13.101 4.12044.702 1.0020.79 ATOM 3689 CA THRH 192 -12.082 3.12844.463 1.0021.97 ATOM 3690 CB THRH 192 -12.627 1.71444.722 1.0023.80 ATOM 3691 OG1 THRH 192 -13.073 1.631 46.085 1.0029.80 ATOM 3693 CG2 THR HI 92 -11.541 0.66644.485 1.0027.22 ATOM 3694 C THRH 192 -11.552 3.16443.062 1.0018.87 ATOM 3695 O THRH 192 -12.316 3.25942.102 1.0015.94 ATOM 3696 N VALH 193 -10.243 3.09842.963 1.0016.81 ATOM 3698 CA VALH 193 -9.596 2.91841.685 1.0016.97 ATOM 3699 CB VAL H 193 -8.801 4.20541.206 1.0016.54 ATOM 3700 CGI VALH 193 -7.941 3.913 39.955 1.0011.61 ATOM 3701 CG2VALH 193 -9.818 5.31940.874 1.0014.87 ATOM 3702 C VALH 193 -8.720 1.64841.779 1.0016.78 ATOM 3703 O VALH 193 -7.864 1.51442.626 1.0014.37 ATOM 3704 N THRH 194 -9.039 0.68940.945 1.0018.51 ATOM 3706 CA THRH 194 -8.348 -0.571 40.933 1.0019.26 ATOM 3707 CB THRH 194 -9.335 -1.67241.312 1.0019.05 ATOM 3708 OG1 THRH 194 -10.070 -1.25542.476 1.0022.10 ATOM 3710 CG2THRH 194 -8.625 -2.98041.603 1.0017.95 ATOM 3711 C THRH 194 -7.871 -0.84239.523 1.0020.35 ATOM 3712 O THRH 194 -8.575 -0.52838.560 1.0018.99 ATOM 3713 N CYS H 195 -6.683 -1.38839.389 1.0022.03 ATOM 3715 CA CYSH 195 -6.241 -1.84238.090 1.0021.55 ATOM 3716 CB CYS H 195 -4.838 -1.37437.790 1.0022.21 ATOM 3717 SG CYS H 195 -3.531 -2.325 38.567 1.0026.24 ATOM 3718 C CYS H 195 -6.320 -3.36038.049 1.0020.83 ATOM 3719 O CYS H 195 -6.051 -4.05839.040 1.0021.96 ATOM 3720 N ASNH 196 -6.712 -3.85036.908 1.0019.29 ATOM 3722 CA ASN H 196 -6.924 -5.28036.675 1.0016.40 ATOM 3723 CB ASNH 196 -8.297 -5.433 36.030 1.0016.17 ATOM 3724 CG ASN H 196 -9.253 -4.39236.544 1.0013.27 ATOM 3725 ODIASNH 196 -9.664 -3.475 35.837 1.0020.19 ATOM 3726 ND2 ASN H 196 -9.596 -4.51037.798 1.0011.17 ATOM 3729 C ASNH 196 -5.879 -5.76235.690 1.0016.19 ATOM 3730 O ASNH 196 -5.901 -5.343 34.545 1.0013.42 ATOM 3731 N VALH 197 -4.956 -6.60236.133 1.0015.57 ATOM 3733 CA VALH 197 -3.897 -7.065 35.269 1.0014.42 ATOM 3734 CB VALH 197 -2.521 -6.83435.890 1.009.60 ATOM 3735 CGI VALH 197 -1.458 -7.38934.966 1.007.11 ATOM 3736 CG2VALH 197 -2.290 -5.35436.125 1.0012.01 ATOM 3737 C VAL H 197 -4.033 -8.54734.954 1.0016.35 ATOM 3738 O VALH 197 -4.129 -9.37635.874 1.0014.56 ATOM 3739 N ALA H 198 -4.033 -8.87433.646 1.0017.13 ATOM 3741 CA ALAH 198 -4.135-10.26733.214 1.0016.34 ATOM 3742 CB ALAH 198 -5.315-10.44432.302 1.0017.48 ATOM 3743 C ALA H 198 -2.881-10.68032.503 1.0018.98 ATOM 3744 O ALA H 198 -2.337 -9.92631.692 1.0018.73 ATOM 3745 N HISH 199 -2.372-11.845 32.860 1.0018.76 ATOM 3747 CA HISH 199 -1.205-12.40032.205 1.0017.07 ATOM 3748 CB HISH 199 -0.048-12.50033.166 1.008.69 ATOM 3749 CG HISH 199 1.206-12.95932.494 1.0013.16 ATOM 3750 CD2 HIS H 199 1.784-12.60531.294 1.0011.24 ATOM 3751 ND1 HISH 199 2.076-13.871 33.056 1.0012.67 ATOM 3753 CEl HIS H 199 3.134-14.07432.278 1.0015.05 ATOM 3754 NE2 HIS H 199 2.957-13.31831.211 1.009.04 ATOM 3756 C HIS H 199 -1.582-13.79031.698 1.0020.77 ATOM 3757 O HISH 199 -1.357-14.80932.404 1.0022.61 ATOM 3758 N PRO H 200 -2.203-13.855 30.485 1.0023.38 ATOM 3759 CD PROH 200 -2.513-12.70529.583 1.0023.82 ATOM 3760 CA PROH 200 -2.640-15.113 29.875 1.0022.74 ATOM 3761 CB PROH 200 -2.769-14.75028.407 1.0023.09 ATOM 3762 CG PROH 200 -3.303-13.35728.477 1.0023.84 ATOM 3763 C PROH 200 -1.671-16.25530.118 1.0022.03 ATOM 3764 O PROH 200 -2.091-17.283 30.570 1.0025.71 ATOM 3765 N ALAH 201 -0.382-16.05429.884 1.0021.74 ATOM 3767 CA ALAH 201 0.601-17.13730.024 1.0022.02 ATOM 3768 CB ALAH 201 1.987-16.61429.751 1.0021.34 ATOM 3769 C ALAH 201 0.582-17.84031.399 1.0025.49 ATOM 3770 O ALAH 201 0.590-19.08731.481 1.0027.00 ATOM 3771 N SERH 202 0.588-17.055 32.476 1.0023.97 ATOM 3773 CA SER H 202 0.534-17.61633.826 1.0023.02 ATOM 3774 CB SER H 202 1.046-16.57034.790 1.0020.89 ATOM 3775 OG SER H 202 0.321-15.37234.570 1.0022.36 ATOM 3777 C SER H 202 -0.908-17.948 34.194 1.0022.44 ATOM 3778 O SER H 202 -1.196-18.41735.282 1.0024.26 ATOM 3779 N ALA H 203 -1.807-17.68633.281 1.0023.52 ATOM 3781 CA ALA H 203 -3.226-17.82033.547 1.0024.82 ATOM 3782 CB ALA H 203 -3.599-19.29933.632 1.0025.98 ATOM 3783 C ALA H 203 -3.628-17.04634.835 1.0028.71 ATOM 3784 O ALAH 203 -4.398-17.533 35.678 1.0033.42 ATOM 3785 N THRH 204 -3.134-15.82034.995 1.0027.17 ATOM 3787 CA THRH204 -3.493-15.05636.184 1.0027.24 ATOM 3788 CB THRH204 -2.281-14.72237.006 1.0026.73 ATOM 3789 OG1 THRH 204 -1.396-13.91736.233 1.0029.32 ATOM 3791 CG2 THRH 204 -1.572-15.997 37.415 1.0030.85 ATOM 3792 C THR H 204 -4.211-13.75635.845 1.0028.10 ATOM 3793 O THRH 204 -4.034-13.185 34.756 1.0027.08 ATOM 3794 N LYS H 205 -5.018-13.30836.796 1.0029.70 ATOM 3796 CA LYS H 205 -5.805-12.08236.664 1.0029.70 ATOM 3797 CB LYSH 205 -7.176-12.423 36.058 1.0026.59 ATOM 3798 CG LYSH 205 -8.106-11.253 35.801 1.0030.12 ATOM 3799 CD LYSH 205 -7.440-10.121 35.041 1.0032.29 ATOM 3800 CE LYS H 205 -8.413 -8.99534.687 1.0028.46 ATOM 3801 NZ LYS H 205 -9.228 -9.29233.456 1.0032.30 ATOM 3805 C LYSH 205 -5.915-11.44338.056 1.0029.50 ATOM 3806 O LYSH 205 -6.683-11.903 38.906 1.0029.82 ATOM 3807 N VAL H 206 -5.087-10.41438.287 1.0027.91 ATOM 3809 CA VALH 206 -5.029 -9.76739.575 1.0027.55 ATOM 3810 CB VALH 206 -3.560 -9.75540.139 1.0027.51 ATOM 3811 CG1VALH206 -2.906-11.11239.930 1.0029.90 ATOM 3812 CG2 VALH 206 -2.727 -8.65439.511 1.0025.31 ATOM 3813 C VALH 206 -5.598 -8.33439.578 1.0026.86 ATOM 3814 O VAL H 206 -5.492 -7.595 38.607 1.0025.39 ATOM 3815 N ASPH 207 -6.229 -7.98240.701 1.0027.63 ATOM 3817 CA ASPH 207 -6.728 -6.63840.940 1.0025.50 ATOM 3818 CB ASPH 207 -8.156 -6.67741.442 1.0028.55 ATOM 3819 CG ASPH 207 -9.132 -6.941 40.337 1.0029.54 ATOM 3820 OD1 ASPH 207 -8.700 -6.97239.168 1.0036.07 ATOM 3821 OD2 ASPH 207 -10.328 -7.11840.628 1.0032.67 ATOM 3822 C ASPH 207 -5.903 -5.99742.008 1.0024.44 ATOM 3823 O ASPH 207 -5.547 -6.68242.978 1.0023.66 ATOM 3824 N ALAH208 -5.581 -4.70641.827 1.0021.43 ATOM 3826 CA ALAH 208 -4.881 -3.94342.848 1.0017.91 ATOM 3827 CB ALAH 208 -3.397 -3.781 42.534 1.0020.11 ATOM 3828 C ALAH 208 -5.530 -2.57443.035 1.0016.62 ATOM 3829 O ALAH208 -5.610 -1.75342.086 1.0010.62 ATOM 3830 N LYS H 209 -6.055 -2.35844.261 1.0016.90 ATOM 3832 CA LYSH 209 -6.683 -1.07944.621 1.0015.48 ATOM 3833 CB LYS H 209 -7.654 -1.22245.812 1.0010.13 ATOM 3834 CG LYSH 209 -8.265 0.10446.1790.5010.96 ATOM 3835 CD LYSH 209 -9.145 -0.02247.3960.5014.26 ATOM 3836 CE LYSH 209 -9.497 1.34647.9380.5012.83 ATOM 3837 NZ LYSH 209 -10.519 1.25549.0080.5014.36 ATOM 3841 C LYSH 209 -5.627 -0.011 44.930 1.0012.92 ATOM 3842 O LYSH 209 -4.648 -0.26845.616 1.0010.83 ATOM 3843 N ILEH 210 -5.801 1.18344.380 1.0012.54 ATOM 3845 CA ILEH 210 -4.850 2.25044.663 1.0014.57 ATOM 3846 CB ILEH 210 -4.682 3.263 43.473 1.0010.03 ATOM 3847 CG2 ILEH 210 -3.430 4.07443.671 1.009.58 ATOM 3848 CGI ILEH 210 -4.643 2.54042.097 1.0011.38 ATOM 3849 CD ILEH 210 -3.468 1.61341.881 1.009.16 ATOM 3850 C ILEH 210 -5.369 2.97645.910 1.0016.98 ATOM 3851 O ILEH 210 -6.514 3.47445.936 1.0018.38 ATOM 3852 N VALH 211 -4.543 2.941 46.931 1.0019.13 ATOM 3854 CA VALH 211 -4.831 3.52848.240 1.0020.34 ATOM 3855 CB VALH 211 -4.688 2.41649.299 1.0021.28 ATOM 3856 CGI VALH 211 -4.837 2.98650.708 1.0025.89 ATOM 3857 CG2 VALH 211 -5.705 1.31649.035 1.0018.88 ATOM 3858 C VALH 211 -3.802 4.63348.528 1.0019.87 ATOM 3859 O VALH 211 -2.617 4.47348.212 1.0020.58 ATOM 3860 N PROH 212 -4.201 5.771 49.134 1.0021.21 ATOM 3861 CD PROH 212 -5.573 6.11549.582 1.0018.81 ATOM 3862 CA PROH 212 -3.258 6.88649.422 1.0020.72 ATOM 3863 CB PROH 212 -4.145 7.92050.099 1.0018.51 ATOM 3864 CG PROH 212 -5.488 7.61549.546 1.0018.18 ATOM 3865 C PROH 212 -2.124 6.45650.338 1.0023.63 ATOM 3866 O PROH 212 -2.326 5.57651.182 1.0027.07 ATOM 3867 N ARGH 213 -0.926 7.043 50.151 1.0024.57 ATOM 3869 CA ARGH 213 0.187 6.76651.053 1.0026.72 ATOM 3870 CB ARGH 213 1.569 6.813 50.343 1.0027.15 ATOM 3871 CG ARGH 213 1.860 7.97849.396 1.0033.85 ATOM 3872 CD ARGH 213 3.273 7.86248.791 1.0033.12 ATOM 3873 NE ARGH 213 3.507 6.52048.248 1.0040.88 ATOM 3875 CZ ARGH 213 4.615 5.771 48.499 1.0040.65 ATOM 3876 NH1 ARGH 213 4.693 4.53548.001 1.0039.58 ATOM 3879 NH2 ARGH 213 5.649 6.26049.206 1.0037.54 ATOM 3882 C ARGH 213 0.158 7.70652.255 1.0027.92 ATOM 3883 OT1 ARGH 213 0.614 7.283 53.341 1.0031.74 ATOM 3884 OT2 ARGH 213 -0.357 8.84052.109 1.0029.09 ATOM 3885 CB ALAP 2 31.237 -7.993 -6.254 1.0023.82 ATOM 3886 C ALAP 2 29.863 -5.868 -6.170 1.0018.78 ATOM 3887 O ALAP 2 29.809 -5.461 -5.015 1.0018.94 ATOM 3890 N ALAP 2 32.338 -5.778 -6.117 1.0024.56 ATOM 3892 CA ALA P 2 31.159 -6.526 -6.677 1.0020.94 ATOM 3893 N ALAP 3 28.844 -5.788 -7.037 1.0015.73 ATOM 3895 CA ALAP 3 27.600 -5.082 -6.736 1.0014.42 ATOM 3896 CB ALAP 3 27.064 -4.460 -8.021 1.0013.90 ATOM 3897 C ALAP 3 26.498 -5.955 -6.132 1.0014.34 ATOM 3898 O ALAP 3 26.523 -7.202 -6.212 1.0012.83 ATOM 3899 N PROP 4 25.531 -5.280 -5.471 1.0012.41 ATOM 3900 CD PROP 4 25.569 -3.841 -5.120 1.0010.70 ATOM 3901 CA PROP 4 24.365 -5.915 -4.878 1.009.09 ATOM 3902 CB PROP 4 23.912 -4.871 -3.871 1.0010.23 ATOM 3903 CG PROP 4 24.158 -3.624 -4.622 1.0010.28 ATOM 3904 C PROP 4 23.350 -6.158 -5.998 1.008.50 ATOM 3905 O PROP 4 23.720 -6.084 -7.147 1.0012.29 ATOM 3906 N ASPP 5 22.110 -6.436 -5.707 1.003.44 ATOM 3908 CA ASPP 5 21.187 -6.699 -6.748 1.006.24 ATOM 3909 CB ASPP 5 19.976 -7.498 -6.231 1.004.87 ATOM 3910 CG ASPP 5 18.947 -7.830 -7.322 1.008.73 ATOM 3911 OD1 ASPP 5 19.286 -7.812 -8.552 1.00 5.17 ATOM 3912 OD2ASPP 5 17.787 -8.099 -6.971 1.006.00 ATOM 3913 C ASPP 5 20.734 -5.385 -7.386 1.0011.49 ATOM 3914 O ASPP 5 19.876 -4.707 -6.867 1.0013.66 ATOM 3915 N THRP 6 21.310 -5.045 -8.542 1.0013.74 ATOM 3917 CA THRP 6 20.984 -3.797 -9.202 1.0013.90 ATOM 3918 CB THRP 6 22.263 -3.137 -9.774 1.0013.32 ATOM 3919 OG1 THRP 6 22.896 -4.001 -10.731 1.0019.82 ATOM 3921 CG2THRP 6 23.263 -2.884 -8.651 1.0017.80 ATOM 3922 C THRP 6 19.944 -3.952-10.296 1.0013.91 ATOM 3923 O THRP 6 19.789 -3.050-11.122 1.0016.59 ATOM 3924 N ARGP 7 19.213 -5.065-10.338 1.0012.22 ATOM 3926 CA ARGP 7 18.204 -5.190-11.372 1.0012.33 ATOM 3927 CB ARGP 7 17.679 -6.625-11.529 1.0011.79 ATOM 3928 CG ARGP 7 16.416 -6.694-12.378 1.0014.75 ATOM 3929 CD ARGP 7 15.741 -8.045-12.383 1.0018.52 ATOM 3930 NE ARGP 7 16.521 -8.985-13.132 1.0027.19 ATOM 3932 CZ ARGP 7 16.062 -9.667-14.164 1.0026.31 ATOM 3933 NH1 ARG P 7 16.877-10.489-14.780 1.0031.37 ATOM 3936 NH2 ARG P 7 14.807 -9.547-14.576 1.0025.93 ATOM 3939 C ARGP 7 17.054 -4.242-11.085 1.0015.83 ATOM 3940 O ARGP 7 16.730 -3.991 -9.908 1.0015.84 ATOM 3941 N PROP 16.445 -3.636-12.151 1.0015.86 ATOM 3942 CD PROP 16.848 -3.723-13.596 1.0015.67 ATOM 3943 CA PROP 15.332 -2.725-11.993 1.0011.60 ATOM 3944 CB PROP 15.082 -2.163-13.418 1.0016.26 ATOM 3945 CG PROP 16.398 -2.372-14.113 1.0012.50 ATOM 3946 C PROP 14.099 -3.443-11.426 1.0015.08 ATOM 3947 O PROP 8 13.731 -4.578-11.824 1.007.39 ATOM 3948 N ALAP 9 13.513 -2.754-10.452 1.0014.65 ATOM 3950 CA ALAP 9 12.318 -3.174 -9.766 1.0016.28 ATOM 3951 CB ALAP 9 12.035 -2.141 -8.639 1.0013.79 ATOM 3952 C ALAP 9 11.143 -3.185-10.727 1.0017.17 ATOM 3953 O ALAP 9 11.197 -2.526-11.760 1.0019.75 ATOM 3954 N PROP 10 10.136 -4.011 -10.481 1.0017.47 ATOM 3955 CD PROP 10 10.149 -5.176 -9.580 1.0017.04 ATOM 3956 CA PROP 10 8.950 -3.999-11.292 1.0020.33 ATOM 3957 CB PROP 10 8.088 -5.104-10.680 1.0014.66 ATOM 3958 CG PROP 10 8.708 -5.384 -9.367 1.0018.16 ATOM 3959 C PROP 10 8.280 -2.585-11.246 1.0023.98 ATOM 3960 OT1 PRO P 10 8.663 -1.761 -10.374 1.0029.12 ATOM 3961 OT2PROP 10 7.407 -2.300-12.100 1.0032.81 ATOM 3962 OH2 WAT W 6.469 14.788 -4.498 1.0014.28 ATOM 3965 OH2 WAT W 17.598-23.808 -4.151 1.0021.81 ATOM 3968 OH2 WAT W 18.632 4.03258.157 1.006.32 ATOM 3971 OH2 WAT W 25.496 3.194 -6.045 1.0013.58 ATOM 3974 OH2 WAT W 16.953 -5.194 -7.526 1.0013.00 ATOM 3977 OH2 WAT W 24.903-22.960 6.237 1.0030.37 ATOM 3980 OH2 WAT W 21.593-21.679 -1.338 1.003.40 ATOM 3983 OH2 WAT W -3.000 -3.33728.274 1.0030.92 ATOM 3986 OH2 WAT W 29.010-11.559 3.896 1.009.44 ATOM 3989 OH2 WAT W -2.022 11.29049.065 1.0032.00 ATOM 3992 OH2 WAT W 8.407-21.513 8.625 1.0013.78 ATOM 3995 OH2 WAT W 13.72827.07930.459 1.0039.32 ATOM 3998 OH2 WAT W 3.495 4.63644.813 1.0013.19 ATOM 4001 OH2 WAT W 14 1.218 15.946 14.314 1.00 22.53 ATOM 4004 OH2 WAT W 15 12.903 ■ -17.138 34.597 1.00 19.15 ATOM 4007 OH2 WAT W 16 10.898 -8.237 -12.633 1.00 21.26 ATOM 4010 OH2 WAT W 17 8.064 - 14.542 21.148 1.00 37.92 ATOM 4013 OH2 WAT W 18 21.359 7.434 14.51 1 1.00 18.86 ATOM 4016 OH2 WAT W 19 -1.648 1.908 47.014 1.00 15.06 ATOM 4019 OH2 WAT W 20 16.737 9.406 27.272 1.00 14.21 ATOM 4022 OH2 WAT W 21 20.693 12.449 -7.122 1.00 16.36 ATOM 4025 OH2 WAT W 22 7.885 - 12.508 25.316 1.00 10.64 ATOM 4028 OH2 WAT W 23 -3.655 16.264 24.900 1.00 33.41 ATOM 4031 OH2 WAT W 24 33.177 3.183 45.356 1.00 8.24 ATOM 4034 OH2 WAT W 25 -1 1.952 -7.879 37.114 1.00 26.57 ATOM 4037 OH2 WAT W 26 25.803 12.531 -5.964 1.00 21.74 ATOM 4040 OH2 WAT W 27 -2.656 4.045 26.085 1.00 17.07 ATOM 4043 OH2 WAT W 28 7.532 17.937 41.724 1.00 22.01 ATOM 4046 OH2 WAT W 29 23.879 -14.777 24.976 1.00 8.54 ATOM 4049 OH2 WAT W 30 31.338 -2.334 -1.810 1.00 19.31 ATOM 4052 OH2 WAT W 31 17.502 7.886 16.158 1.00 28.03 ATOM 4055 OH2 WAT W 32 5.941 - 12.525 39.932 1.00 20.30 ATOM 4058 OH2 WAT W 33 5.404 -1.056 17.882 1.00 34.15 ATOM 4061 OH2 WAT W 34 1 1.009 -16.41 1 36.548 1.00 16.42 ATOM 4064 OH2 WAT W 35 6.478 - 14.860 -8.201 1.00 16.12 ATOM 4067 OH2 WAT W 36 9.172 0.986 -2.279 1 .00 22.74 ATOM 4070 OH2 WAT W 37 4.511 -4.656 10.403 1.00 20.60 ATOM 4073 OH2 WAT W 38 20.413 -25.507 7.708 1.00 26.25 ATOM 4076 OH2 WAT W 39 7.710 -2.607 1.725 1 1.00 13.86 ATOM 4079 OH2 WAT W 40 21.067 -25.174 -8.378 1.00 17.33 ATOM 4082 OH2 WAT W 41 14.047 -12.643 28.831 1.00 15.39 ATOM 4085 OH2 WAT W 42 24.985 -8.571 16.098 1.00 16.92 ATOM 4088 OH2 WAT W 43 18.061 -3.176 49.972 1.00 25.44 ATOM 4091 OH2 WAT W 44 8.725 - 22.350 12.897 1.00 22.95 ATOM 4094 OH2 WAT W 45 12.305 -7.538 37.860 1.00 26.88 ATOM 4097 OH2 WAT W 46 3.222 - 16.789 -4.360 1.00 19.56 ATOM 4100 OH2 WAT W 47 0.557 0.177 50.267 1.00 30.33 ATOM 4103 OH2 WAT W 48 19.082 -24.999 2.779 1.00 5.88 ATOM 4106 OH2 WAT W 49 19.857 5.737 -10.591 1.00 15.25 ATOM 4109 OH2 WAT W 50 27.548 -18.756 1.690 1.00 12.48 ATOM 41 12 OH2 WAT W 51 18.386 -0.621 -10.504 1.00 26.95 ATOM 4115 OH2 WAT W 52 14.332 -24.453 3.096 1.00 21.65 ATOM 4118 OH2 WAT W 53 15.420 -1 1.836 25.521 1.00 19.62 ATOM 4121 OH2 WAT W 54 7.048 -3.604 7.452 1.00 10.22 ATOM 4124 OH2 WAT W 55 8.771 ■ ■20.550 29.022 1.00 24.86 ATOM 4127 OH2 WAT W 56 7.223 14.260 47.625 1.00 38.64 ATOM 4130 OH2 WAT W 57 28.000 -19.890 -6.750 1.00 5.62 ATOM 4133 OH2 WAT W 58 25.854 -19.568 7.742 1.00 10.53 ATOM 4136 OH2 WAT W 59 21.053 -23.375 -10.43? ! 1.00 13.82 ATOM 4139 OH2 WAT W 60 27.634 -1.672 12.546 1.00 16.07 ATOM 4142 OH2 WAT W 61 4.320 ■ -13.192 12.140 1.00 29.58 ATOM 4145 OH2 WAT W 62 10.805 -25.481 15.446 ι 1.00 30.70 ATOM 4148 OH2 WAT W 63 16.133 5.455 14.708 1.00 33.54 ATOM 4151 OH2 WAT W 64 18.557 -2.351 28.596 1.00 29.04 ATOM 4154 OH2 WAT W 65 11.919 1.172 24.227 1.00 27.66 ATOM 4157 OH2 WAT W 66 20.602 0.152 12.952 1.00 13.20 ATOM 4160 OH2 WAT W 67 2.523 2.197 48.994 1.00 25.99 ATOM 4163 OH2 WAT W 68 18.370 -9.737 -9.821 1.00 8.99 ATOM 4166 OH2 WAT W 69 12.339 -2.363 38.736 1.00 18.95 ATOM 4169 OH2 WAT W 70 28.531 -9.198 -6.241 1.00 15.87 ATOM 4172 OH2 WAT W 71 7.1 13 2.252 42.134 1.00 24.77 ATOM 4175 OH2 WAT W 72 5.551 -6.218 1.097 11.00 25.37 ATOM 4178 OH2 WAT W 73 27.031 -2.271 - 10.652 1.00 35.24 ATOM 4181 OH2 WAT W 74 23.700 -4.680 9.160 1.00 10.39 ATOM 4184 OH2 WAT W 75 21.927 -8.069 -10.281 1.00 19.23 ATOM 4187 OH2 WAT W 76 9.255 21.329 27.676 1.00 22.97 ATOM 4190 OH2 WAT W 77 -1.050 9.080 47.795 1.00 17.17 ATOM 4193 OH2 WAT W 78 23.569 -2.863 10.958 1.00 11.39 ATOM 4196 OH2 WAT W 79 14.936 -18.091 -13.265 00 38.75 ATOM 4199 OH2 WAT W 80 18.885 -22.021 -1.608 1.00 16.43 ATOM 4202 OH2 WAT W 81 6.214 9.528 3.424 1.00 10.35 ATOM 4205 OH2 WAT W 82 8.852 -8.980 40.128 1.00 19.41 ATOM 4208 OH2 WAT W 83 13.989 26.590 5.643 1.00 30.50 ATOM 4211 OH2 WAT W 84 14.832 15.962 -3.151 1.00 14.73 ATOM 4214 OH2 WAT W 85 22.345 -12.016 -10.082 1.00 12.02 ATOM 4217 OH2 WAT W 86 1 1.978 -24.989 2.736 1.00 17.04 ATOM 4220 OH2 WAT W 87 14.518 -25.660 19.374 1.00 12.97 ATOM 4223 OH2 WAT W 88 26.181 0.882 12.155 1.00 14.84 ATOM 4226 OH2 WAT W 89 3.965 18.045 34.071 1.00 14.92 ATOM 4229 OH2 WAT W 90 2.944 -12.722 -0.100 1.00 30.35 ATOM 4232 OH2 WAT W 91 21.018 -0.090 -7.931 1.00 1 1.45 ATOM 4235 OH2 WAT W 92 17.704 4.172 55.338 1.00 23.03 ATOM 4238 OH2 WAT W 93 30.887 -19.001 0.180 1.00 18.12 ATOM 4241 OH2 WAT W 94 8.090 0.598 -12.040 1.00 35.87 ATOM 4244 OH2 WAT W 95 -0.137 11.808 40.511 1.00 19.09 ATOM 4247 OH2 WAT W 96 25.436 11.667 49.096 1.00 39.93 ATOM 4250 OH2 WAT W 97 1 133..441188 9.927 61.190 1.00 17.48 ATOM 4253 OH2 WAT W 98 3 311..664488 7.847 -5.602 1.00 19.58 ATOM 4256 OH2 WAT W 99 1 155..224433 0.341 35.899 1.00 11.83 ATOM 4259 OH2 WAT W 100 -5.216 - ■15.339 38.926 1.00 16.58 ATOM 4262 OH2 WAT W 101 1.803 -1.527 48.192 1.00 29.29 ATOM 4265 OH2 WAT W 102 -9.962 4.701 47.615 1.00 27.17 ATOM 4268 OH2 WAT W 103 6.926 1.104 30.51 1 1.00 21.69 ATOM 4271 OH2 WAT W 104 20.040 0.675 43.899 1.00 28.97 ATOM 4274 OH2 WAT W 105 6.476 6.252 15.949 1.00 21.65 ATOM 4277 OH2 WAT W 106 13.134 23.738 -4.232 1.00 9.47 ATOM 4280 OH2 WAT W 107 -9.097 -5.473 44.708 1.00 32.78 ATOM 4283 OH2 WAT W 108 29.597 -16.402 0.794 1.00 23.02 ATOM 4286 OH2 WAT W 109 1.393 12.084 -0.555 1.00 27.33 ATOM 4289 OH2 WAT W 110 32.275 10.498 -1.711 1.00 22.13 ATOM 4292 OH2 WAT W i l l 28.840 -8.588 8.722 1.00 16.73 ATOM 4295 OH2 WAT W 112 24.301 5.966 -10.135 1.00 17.97 ATOM 4298 OH2 WAT W 113 13.047 -12.047 26.295 1.00 17.02 ATOM 4301 OH2 WAT W 1 14 23.665 -12.540 16.941 1.00 18.85 ATOM 4304 OH2 WAT W 115 2 288..334466 2.252 -10.297 1.00 57.76 ATOM 4307 OH2 WAT W 1 16 1 166..557799 -- 26.334 6.701 1.00 14.43 ATOM 4310 OH2 WAT W 117 2 255..880077 11.294 9.613 1.00 20.54 ATOM 4313 OH2 WAT W 1 18 3 322..449944 10.036 -4.577 1.00 28.60 ATOM 4316 OH2 WAT W 1 19 3 322..446600 4.112 -6.893 1.00 45.04 ATOM 4319 OH2 WAT W 120 -11.721 12.136 46.764 1.00 24.53 ATOM 4322 OH2 WAT W 121 2.092 -13.612 -7.710 1.00 34.84 ATOM 4325 OH2 WAT W 122 5.719 -8.608 46.184 1.00 13.18 ATOM 4328 OH2 WAT W 123 15.576 -9.029 24.1 15 1.00 30.63 ATOM 4331 OH2 WAT W 124 27.668 -17.190 14.414 1.00 14.55 ATOM 4334 OH2 WAT W 125 -17.404 6.631 48.404 1.00 17.20 ATOM 4337 OH2 WATW 126 23.431 -13.57922.761 1.0026.67 ATOM 4340 OH2 WATW 127 17.744 1.47026.979 1.0047.02 ATOM 4343 OH2 WATW 128 14.051 5.68021.680 1.0023.91 ATOM 4346 OH2 WATW 129 -9.668 0.53231.275 1.0016.36 ATOM 4349 OH2 WATW 130 5.213 -6.655-15.383 1.0038.16 ATOM 4352 OH2 WATW 131 31.931 8.541 5.215 1.0013.75 ATOM 4355 OH2 WATW 132 14.297 -2.79727.765 1.0027.48 ATOM 4358 OH2 WATW 133 34.060 -3.373 1.190 1.0028.35 ATOM 4361 OH2 WATW 134 8.266 -8.418-11.712 1.0016.01 ATOM 4364 OH2 WATW 135 21.210 -24.74725.495 1.0021.80 ATOM 4367 OH2 WATW 136 38.415 7.827 2.261 1.0018.43 ATOM 4370 OH2 WATW 137 7.104 11.613 49.567 1.0016.91 ATOM 4373 OH2 WATW 138 22.354 8.172 -1.094 1.003.60 ATOM 4376 OH2 WATW 139 -0.649 13.87638.964 1.0053.27 ATOM 4379 OH2 WAT W 140 3.53220.50933.354 1.0025.23 ATOM 4382 OH2 WATW 141 26.020-21.708 3.681 1.008.89 ATOM 4385 OH2 WAT W 142 16.768 19.739 12.715 1.0012.58 ATOM 4388 OH2 WAT W 143 22.933 1.122 -9.255 1.0033.61 ATOM 4391 OH2 WATW 144 13.952-25.966 12.995 1.0018.24 ATOM 4394 OH2 WATW 145 -1.798-13.563 5.388 1.0022.46 ATOM 4397 OH2 WAT W 146 31.947 -3.239 6.296 1.0021.74 ATOM 4400 OH2 WATW 147 -4.303 -0.61428.886 1.0026.69 ATOM 4403 OH2 WAT W 148 21.134-26.91523.907 1.0016.34 ATOM 4406 OH2 WAT W 149 21.965 7.892-11.778 1.0026.06 ATOM 4409 OH2 WATW 150 10.626-24.261 12.603 1.0021.28 ATOM 4412 OH2 WATW 151 4.596 13.855 -6.210 1.007.70 ATOM 4415 OH2 WATW 152 30.277 6.152 11.049 1.0016.94 ATOM 4418 OH2 WATW 153 24.985 -7.067 9.817 1.0017.58 ATOM 4421 OH2 WATW 154 11.329 -3.86236.792 1.0023.50 ATOM 4424 OH2 WATW 155 -15.325 3.49441.706 1.0035.32 ATOM 4427 OH2 WATW 156 15.210-24.587 -4.662 1.0018.53 ATOM 4430 OH2 WATW 157 1.420 -5.547 7.576 1.0023.51 ATOM 4433 OH2 WATW 158 -11.870 17.08541.012 1.0030.42 ATOM 4436 OH2 WATW 159 6.864-18.801 28.608 1.0019.33 ATOM 4439 OH2 WATW 160 12.992 -0.67526.187 1.0021.36 ATOM 4442 OH2 WATW 161 33.462 -5.652 6.209 1.0023.60 ATOM 4445 OH2 WAT W 162 13.931 24.641 31.377 1.0036.78 ATOM 4448 OH2 WATW 163 1.149-14.94626.149 1.0029.62 ATOM 4451 OH2 WATW 164 24.449 -8.330 -9.652 1.0015.70 ATOM 4454 OH2 WATW 165 3.122 11.59842.075 1.0020.46 ATOM 4457 OH2 WAT W 166 10.71322.846 -4.457 1.0013.45 ATOM 4460 OH2 WATW 167 -6.701 -5.19046.412 1.0031.64 ATOM 4463 OH2 WATW 168 5.589 -4.185 17.993 1.0032.66 ATOM 4466 OH2 WATW 169 -20.269 5.84545.392 1.0011.80 ATOM 4469 OH2 WATW 170 18.348 -6.708 -2.520 1.003.86 ATOM 4472 OH2 WATW 171 29.246-15.130 3.788 1.0014.16 ATOM 4475 OH2 WATW 172 15.259 12.22654.789 1.0037.54 ATOM 4478 OH2 WATW 173 17.143 -24.993 -9.493 1.0035.04 ATOM 4481 OH2 WATW 174 8.818 -1.363 19.163 1.0036.48 ATOM 4484 OH2 WAT W 175 32.233 -8.889 4.729 1.0019.69 ATOM 4487 OH2 WATW 176 28.467 -17.015 -2.185 1.005.68 ATOM 4490 OH2 WATW 177 6.024 25.034 11.136 1.0022.81 ATOM 4493 OH2 WATW 178 20.243 3.14540.487 1.0023.82 ATOM 4496 OH2 WATW 179 -0.519- -13.61240.661 1.0030.50 ATOM 4499 OH2 WATW 180 34.547 -2.642 5.862 1.0021.60 ATOM 4502 OH2 WATW 181 7.161 4.60725.463 1.0015.09 ATOM 4505 OH2 WAT W 182 -4.704 1 1.61 1 31.080 1.00 20.86 ATOM 4508 OH2 WAT W 183 21.433 -23.454 9.547 1.00 31.82 ATOM 451 1 OH2 WAT W 184 13.857 17.680 46.003 1.00 21.96 ATOM 4514 OH2 WAT W 185 17.187 -16.883 - 12.460 1.00 20.68 ATOM 4517 OH2 WAT W 186 19.746 -21.300 -14.638 1.00 27.48 ATOM 4520 OH2 WAT W 187 12.148 14.642 15.368 1.0019.96 ATOM 4523 OH2 WAT W 188 5.387 -6.500-12.696 1.0035.66 ATOM 4526 OH2 WAT W 189 4.586 13.697 39.870 1.00 20.33 ATOM 4529 OH2 WAT W 190 21.769 5.215 41.762 1.00 36.13 ATOM 4532 OH2 WAT W 191 29.219 -21.787 7.401 1.00 20.15 ATOM 4535 OH2 WAT W 192 17.974 -9.978 24.596 1.00 36.15 ATOM 4538 OH2 WAT W 193 12.473 -28.071 4.359 1.00 18.19 ATOM 4541 OH2 WAT W 194 13.012 10.112 21.862 1.00 38.97 ATOM 4544 OH2 WAT W 195 25.597 8.673 49.783 1.00 27.52 ATOM 4547 OH2 WAT W 196 24.837 10.769 46.030 1.00 10.14 ATOM 4550 OH2 WAT W 197 27.972 -17.140 -7.933 1.00 47.72 ATOM 4553 OH2 WAT W 198 26.863 3.704 48.558 1.00 27.25 ATOM 4556 OH2 WAT W 199 15.918 0.432 -1.51 1 1.00 13.61 ATOM 4559 OH2 WAT W 200 5.655 -3.768 25.280 1.00 30.04 ATOM 4562 OH2 WAT W 201 23.425 6.240 13.624 1.00 11.98 ATOM 4565 OH2 WAT W 202 4.290 5.208 17.451 1.00 21.77 ATOM 4568 OH2 WAT W 203 0.290 -9.212 42.200 1.00 15.59 ATOM 4571 OH2 WAT W 204 25.007 2.912 -8.754 1.00 19.57 ATOM 4574 OH2 WAT W 205 20.205 1.110 -9.843 1.00 34.32 ATOM 4577 OH2 WAT W 206 -3.217 8.862 32.830 1.00 6.08 ATOM 4580 OH2 WAT W 207 16.144 -17.034 -8.816 1.00 22.31 ATOM 4583 OH2 WAT W 208 19.175 8.807 -10.884 1.00 42.96 ATOM 4586 OH2 WAT W 209 1.655 -6.944 45.357 1.00 37.43 ATOM 4589 OH2 WAT W 210 -8.549 4.472 49.787 1.00 25.82 ATOM 4592 OH2 WAT W 21 1 3.867 -7.430 27.878 1.00 27.19 ATOM 4595 OH2 WAT W 212 23.654 -2.619 -13.589 1.00 28.44 ATOM 4598 OH2 WAT W 213 29.110 12.286 -6.363 1.00 38.04 ATOM 4601 OH2 WAT W 214 23.926 -20.838 2.405 1.00 5.04 ATOM 4604 OH2 WAT W 215 27.197 3.738 37.195 1.00 24.05 ATOM 4607 OH2 WAT W 216 5.195 - -12.115 14.877 1.00 13.79 ATOM 4610 OH2 WAT W 217 7.487 4.063 14.308 1.00 26.14 ATOM 4613 OH2 WAT W 218 20.375 10.379 8.335 1.00 2.00 ATOM 4616 OH2 WAT W 219 17.302 -1.823 -8.469 1.00 18.45 ATOM 4619 OH2 WAT W 220 6.804 18.384 -1.961 1.00 18.17 ATOM 4622 OH2 WAT W 221 30.521 -17.401 -8.988 1.00 9.31 ATOM 4625 OH2 WAT W 222 1.118 - -13.903 28.627 1.0022.20 ATOM 4628 OH2 WAT W 223 4.658 4.61224.950 1.0014.99 ATOM 4631 OH2 WAT W 224 0.009 17.440 18.293 1.0024.15 ATOM 4634 OH2 WAT W 225 9.924 • -27.510 -4.500 1.0024.23 ATOM 4637 OH2 WAT W 226 17.922 7.851 29.078 1.0026.71 ATOM 4640 OH2 WAT W 227 26.329 5.158 -2.190 1.007.58 ATOM 4643 OH2 WAT W 228 16.212 -0.65925.988 1.0051.29 ATOM 4646 OH2 WAT W 229 8.255 -11.625 39.145 1.0024.13 ATOM 4649 OH2 WAT W 230 -0.739 11.893 32.356 1.0014.96 ATOM 4652 OH2 WAT W 231 10.244 -6.61643.601 1.0027.57 ATOM 4655 OH2 WAT W 232 0.924 9.055 32.613 1.0024.54 ATOM 4658 OH2 WAT W 233 2.598 11.74232.894 1.0021.65 ATOM 4661 OH2 WAT W 234 6.719 -0.04443.519 1.0010.20 ATOM 4664 OH2 WAT W 235 18.217 -24.604 5.251 1.0011.95 ATOM 4667 OH2 WAT W 236 8.252 6.201 12.463 1.0021.41 ATOM 4670 OH2 WAT W 237 23.441 13.63549.710 1.0030.08 ATOM 4673 OH2 WAT W 238 17.020 -7.750 -4.400 1.00 15.78 ATOM 4676 OH2 WAT W 239 30.779 - 10.002 6.550 1.00 27.21 ATOM 4679 OH2 WAT W 240 -6.748 -6.499 32.312 1.00 29.81 ATOM 4682 OH2 WAT W 241 16.503 - 12.922 28.084 1.00 36.06 ATOM 4685 OH2 WAT W 242 12.122 -24.490 -7.899 1.00 19.39 ATOM 4688 OH2 WAT W 243 21.099 12.849 35.212 1.00 24.60 ATOM 4691 OH2 WAT W 244 18.243 -8.436 20.387 1.00 23.62 ATOM 4694 OH2 WAT W 245 20.147 10.002 34.434 1.00 11.86 ATOM 4697 OH2 WAT W 246 29.723 9.471 -8.340 1.00 34.43 ATOM 4700 OH2 WAT W 247 13.252 2.121 14.964 1.00 24.74 ATOM 4703 OH2 WAT W 248 23.464 -25.374 4.258 1.00 13.44 ATOM 4706 OH2 WAT W 249 14.000 -22.772 -6.620 1.00 17.30 ATOM 4709 OH2 WAT W 250 10.326 0.557 16.215 1.00 41.70 ATOM 4712 OH2 WAT W 251 13.521 2.393 -9.514 1.00 20.28 ATOM 4715 OH2 WAT W 252 13.615 -26.397 -3.875 1.00 15.20 ATOM 4718 OH2 WAT W 253 24.833 10.111 -7.130 1.00 29.35 ATOM 4721 OH2 WAT W 254 13.064 -15.952 -13.595 1.00 26.25 ATOM 4724 OH2 WAT W 255 -15.057 5.686 39.924 1.00 39.38 ATOM 4727 OH2 WAT W 256 16.336 15.971 31.027 1.00 19.01 ATOM 4730 OH2 WAT W 257 12.624 -9.192 43.712 1.00 20.05 ATOM 4733 OH2 WAT W 258 12.967 -8.262 23.940 1.00 41.00 ATOM 4736 OH2 WAT W 259 14.757 0.585 -10.768 1.00 28.58 ATOM 4739 OH2 WAT W 260 19.819 -1.817 -13.475 1.00 35.1 1 ATOM 4742 OH2 WAT W 261 31.389 -15.656 -0.825 1.00 26.24 ATOM 4745 OH2 WAT W 262 14.395 -13.087 -16.099 1.00 16.37 ATOM 4748 OH2 WAT W 263 22.719 13.037 16.198 1.00 21.47 ATOM 4751 OH2 WAT W 264 16.540 21.557 39.053 1.00 26.03 ATOM 4754 OH2 WAT W 265 -6.562 -9.693 42.850 1.00 26.79 ATOM 4757 OH2 WAT W 266 32.765 6.771 -7.894 1.00 26.76 ATOM 4760 OH2 WAT W 267 7.895 14.072 16.472 1.00 18.53 ATOM 4763 OH2 WAT W 268 35.614 1.144 10.445 1.00 31.99 ATOM 4766 OH2 WAT W 269 13.248 -7.824 41.224 1.00 27.81 ATOM 4769 OH2 WAT W 270 26.612 -16.221 -10.354 1.00 24.35 ATOM 4772 OH2 WAT W 271 9.404 21.743 36.231 1.00 26.21 ATOM 4775 OH2 WAT W 272 2.135 -1.886 26.621 1.00 19.18 ATOM 4778 OH2 WAT W 273 5.029 - -16.489 24.250 1.00 21.38 ATOM 4781 OH2 WAT W 274 -3.689 11.484 26.196 1.00 32.16 ATOM 4784 OH2 WAT W 275 -0.444 20.210 19.609 1.00 28.61 ATOM 4787 OH2 WAT W 276 20.202 13.824 -1.393 1.00 6.13 ATOM 4790 OH2 WAT W 277 8.008 8.335 14.152 1.00 26.36 ATOM 4793 OH2 WAT W 278 -0.089 -4.167 27.283 1.00 22.58 ATOM 4796 OH2 WAT W 279 6.446 ■ ■12.379 22.877 1.00 39.32 ATOM 4799 OH2 WAT W 280 27.976 -9.405 11.870 1.00 21.31 ATOM 4802 OH2 WAT W 281 18.063 -5.600 47.215 1.00 28.13 ATOM 4805 OH2 WAT W 282 27.726 -20.314 5.883 1.00 29.05 ATOM 4808 OH2 WAT W 283 7.306 3.337 5.457 1.00 15.35 ATOM 4811 OH2 WAT W 284 -1.946 14.609 1.577 1.00 30.36 ATOM 4814 OH2 WAT W 285 1 1.677 -3.115 17.818 1.00 19.72 ATOM 4817 OH2 WAT W 286 21.862 -21.678 1.194 1.00 14.10 ATOM 4820 OH2 WAT W 287 21.062 -6.560 -2.887 1.00 10.76 ATOM 4823 OH2 WAT W 288 15.270 0.156 17.566 1.0023.02 ATOM 4826 OH2 WAT W 289 17.300 -6.730 54.194 1.00 23.81 ATOM 4829 OH2 WAT W 290 22.196 -16.787 24.840 1.0026.10 ATOM 4832 OH2 WAT W 291 1 1.450 -1.461 -14.210 1.00 17.37 ATOM 4835 OH2 WAT W 292 9.545 1.106 23.451 1.00 18.75 ATOM 4838 OH2 WAT W 293 13.359 17.520 21.914 1.00 32.59 ATOM 4841 OH2 WAT W 294 26.885 -7.151 7.996 1.00 19.34 ATOM 4844 OH2 WAT W 295 21.756 -13.103 -13.701 1.00 29.49 ATOM 4847 OH2 WAT W 296 1 1.457 -7.218 35.141 1.00 22.34 ATOM 4850 OH2 WAT W 297 18.708 0.544 -7.701 1.00 16.39 ATOM 4853 OH2 WAT W 298 - 15.953 3.350 44.816 1.00 37.24 ATOM 4856 OH2 WAT W 299 8.407 -8.314 42.681 1.00 28.38 ATOM 4859 OH2 WAT W 300 2.540 -9.294 23.041 1.00 35.16 ATOM 4862 OH2 WAT W 301 22.018 -7.958 -0.799 1.00 6.1 1 ATOM 4865 OH2 WAT W 302 21.966 -24.488 2.085 1.00 8.66 ATOM 4868 OH2 WAT W 303 20.076 -25.315 17.635 1.00 9.01 ATOM 4871 OH2 WAT W 304 17.006 -22.056 5.026 1.00 5.97 ATOM 4874 OH2 WAT W 305 6.060 -7.502 14.185 1.00 41.33 ATOM 4877 OH2 WAT W 306 32.819 -13.271 -1.536 1.00 7.51 ATOM 4880 OH2 WAT W 307 -7.134 13.283 28.131 1.00 26.60 ATOM 4883 OH2 WAT W 308 6.093 -19.675 20.689 1.00 34.63 ATOM 4886 OH2 WAT W 309 5.245 8.997 12.387 1.00 19.78 ATOM 4889 OH2 WAT W 310 12.019 2.613 52.929 1.00 21.69 ATOM 4892 OH2 WAT W 31 1 10.010 19.928 41.543 1.00 33.05 ATOM 4895 OH2 WAT W 312 13.142 -23.671 -10.200 1.00 36.76 ATOM 4898 OH2 WAT W 313 8.670 -24.177 7.948 1.00 34.91 ATOM 4901 OH2 WAT W 314 29.062 -9.848 -3.498 1.00 29.41 ATOM 4904 OH2 WAT W 315 14.807 -9.227 46.355 1.00 40.86 ATOM 4907 OH2 WAT W 316 7.251 26.098 3.963 1.00 28.36 ATOM 4910 OH2 WAT W 317 23.961 5.881 39.286 1.00 21.45 ATOM 4913 OH2 WAT W 318 8.771 7.324 16.718 1.00 36.71 ATOM 4916 OH2 WAT W 319 -1.090 -7.807 23.575 1.00 40.27 ATOM 4919 OH2 WAT W 320 22.689 2.991 44.255 1.00 31.90 ATOM 4922 OH2 WAT W 321 11.210 -9.771 22.151 1.00 38.45 ATOM 4925 OH2 WAT W 322 22.311 0.357 -12.1 13 1.00 23.98 ATOM 4928 OH2 WAT W 323 6.735 14.216 -9.674 1.00 45.55 ATOM 4931 OH2 WAT W 324 -8.071 -4.209 27.927 1.00 29.83 ATOM 4934 OH2 WAT W 325 1.445 17.951 34.713 1.00 30.61 ATOM 4937 OH2 WAT W 326 19.684 9.965 25.552 1.00 33.30 ATOM 4940 OH2 WAT W 327 2.120 14.444 12.302 1.00 37.1 1 ATOM 4943 OH2 WAT W 328 15.167 -4.201 25.183 1.00 29.17 ATOM 4946 OH2 WAT W 329 12.976 28.071 24.361 1.00 30.90 ATOM 4949 OH2 WAT W 330 1.965 -6.101 27.052 1.00 18.90 ATOM 4952 OH2 WAT W 331 20.107 17.468 33.762 1.00 41.90 ATOM 4955 CD HET I 1 -3.687 1 1.892 28.658 1.00 34.52 ATOM 4956 CD HET I 2 7.014 -2.547 18.557 1.00 56.55 ATOM 4957 CD HET I 3 -18.910 6.317 46.958 1.00 25.08 ATOM 4958 CD HET I 4 31.181 -13.966 -2.383 1.00 17.70 ATOM 4959 CD HET I 5 7.075 -7.626 -14.342 1.00 57.21 ATOM 4960 CD HET I 6 9.353 21.680 25.019 0.75 48.85 ATOM 4961 CD HET I 7 22.069 5.816 -10.264 0.75 26.79 ATOM 4962 CD HET I 8 17.818 -0.561 27.627 0.75 56.40 ATOM 4963 CL CHL I 9 -19.039 3.937 48.052 1.00 22.14 ATOM 4964 CL CHL I 10 30.927 -12.252 -4.117 1.00 26.88 Table 3 Data statistics of S 3 Fab fragment/MUCl epitope crystal D is the resolution defined as the interplanar spacings d=lambda/2 sintheta corresponding to the maximum observed 2theta values where lambda=1.54 angstroms. 2theta refers to the angle of diffraction. Lower resolutions have higher nos and higher resolutions have lower nos. -I=intensity and sig(i) gives the standard deviation of the intensity for each batch of reflections. This indicates how well measured the data is. Higher values means stronger more intense data lower values mean the data is weakly measured. Note this value drops off as the resolution becomes higher, for example at 1.95 A the angle of diffraction is quite great. Table 4 Summary of the refinement statistics for the SM3-EP1 structure. Statistics for Table 2a Resolution range 8.0 - 1.95 /4 No. of residues 434 Missing residues 16 No. of protein atoms 3193 No. of solvent atoms 335 No. of metal atoms 8 No. of reflections with I > 2.5 σø) (all data) 32197 (27688) Space group P 2, Cell dimensions a=42.2; b = 83.7; c=67.2 A, ?=93.3° R with I > 2.5 σ(I) 20.7 % R free with I > 2.5 σ(I) 27.9 % ^ Average B-factor (Fab, antigen, all atoms) 15.6 A 2 , 15.4 A 2 , 16.4 A 2 Rmsd on bond distances 0.017 A Rmsd on bond angles 1.604° Rmsd on impropers 1.357° Statistics for Table 2b Resolution range 8.0 - 1.95 A No. of residues 434 Missing residues 16 No. of protein atoms 3227 No. of solvent atoms 331 No. of metal atoms 8 No. of reflections with F > 4 s(F) (all data) 32197 (28735) Completness with F > 4 s(F) (all data) 85.6% (96.0%) Space group P 2, Cell dimensions a=42.2; b = 83.7; c=67.2 A, ?=93.3° R with F > 4s(F) (all data) 21.3 % (23.8%) R free with F > 4s(F) (all data) 28.3 % 30.1 %) Average B-factor (Fab, antigen, all atoms) 15.6 A 2 , 15.4 A 2 , 16.4 A 2 Rmsd on bond distances 0.017 A Rmsd on bond angles 1.604° Rmsd on impropers 1.357° Table 5 Antigen - antibody contacts Residues involved in -peptide bond are underlined; SAS - solvent accessible surface of peptide residue; Residue no. 2 is Ser, but was modelled as Ala. Peptide residue % of SAS number Fab residues Location buried of contacts in structure Ala2P 31.6 6 Trρ91L, Ser93L L3 (Ser) 7 waters Ala3P 52.0 8 Tyr32L, Trp91L, Trp33H LI, L3, HI 5 waters Pro4P 94.4 17 Tyr32L, Trp91L, Trp96L LI, L3 8 Trp33H, Gln97H HI, H3 2 waters 1 Thr6P antigen AspSP 89.3 24 Tyr32H, Trp33H HI 4 Gln97H H3 16 waters 1 Arg7P antigen ThrόP 23.6 1 Tyr32L LI 11 waters Arg7P 46.9 12 Asn31H, Tyr32H HI 11 waters Pro8P 7.9 5 Tyr32H HI 5 waters Ala9P 60.8 7 Pro56L, Tyr32H, Val95H L2, HI, H3 5 waters * ProlOP 48.7 7 Pro56L, Phe27H, Tyr32H L2. H1 2 Tyrl02H H3 5 waters Table 6. Nucleotide and amino acid sequences of the light and heavy variable chains of SM3. The numbering in this table is for convenience only and does not correspond to the conventional numbering of these sequences. Light Chain Variable Region GAT ATC GTT GTG ACT CAG GAA TCT GCA CTC ACC ACA TCA CCT GGT GAA 48 Asp H e Val Val Thr Gi n Gl u Ser Al a Leu Thr Thr Ser Pro Gl y Gl u 1 5 10 15 ACA GTC ACA CTC ACT TGT CGC TCA AGT ACT GGG GCT GTT ACA ACT AGT 96 Thr Val Thr Leu Thr Cys Arg Ser Ser Thr Gly Ala Val Thr Thr Ser 20 25 30 AAC TAT GCC AAC TGG GTC CAA GAA AAA CCA GAT CAT TTA TTC ACT GGT 144 Asn Tyr Ala Asn Trp Val Gin Glu Lys Pro Asp His Leu Phe Thr Gly 35 40 45 CTA ATA GGT GGT ACC AAC AAC CGA GCA CCA GGT GTT CCT GCC AGA TTC 192 Leu He Gly Gly Thr Asn Asn Arg Ala Pro Gly Val Pro Ala Arg Phe 50 55 60 TCA GGC TCC CTG Aπ GGA GAC AAG GCT GCC CTC ACC ATC ACA GGG GCA 240 Ser Gly Ser Leu H e Gly Asp Lys Al a Al a Leu Thr H e Thr Gl y Al a 65 70 75 80 CAG ACT GAG GAT GAG GCA ATA TAT TTC TGT GCT CTA TGG TAC AGC AAC 288 Gin Thr Glu Asp Glu Ala lie Tyr Phe Cys Ala Leu Trp Tyr Ser Asn 85 90 95 CAT TGG GTG TTC GGT GGA GGA ACC AAA CTG ACT GTC CTA GGA TCC GAG 336 His Trp Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Ser Glu 100 105 110 Heavy Chain Variable Region CAA GTT CAG CTG CAG GAG TCT GGA GGA GGC TTG GTG CAA CCT GGA GGA 48 Gin Val Gin Leu Gin Glu Ser Gly Gly Gly Leu Val Gin Pro Gly Gly 115 120 125 TCC ATG AAA CTC TCC TGT GTT GCC TCT GGA TTC ACT TTC AGT AAC TAC 96 Ser Met Lys Leu Ser Cys Val Ala Ser Gly Phe Thr Phe Ser Asn Tyr 130 135 140 TGG ATG AAC TGG GTC CGC CAG TCT CCA GAG AAG GGG Cπ GAG TGG Gπ 144 Trp Met Asn Trp Val Arg Gin Ser Pro Glu Lys Gly Leu Glu Trp Val 145 150 155 160 GCT GAA Aπ AGA πG AAA TCT AAT AAT TAT GCA ACA CAT TAT GCG GAG 192 Ala Glu lie Arg Leu Lys Ser Asn Asn Tyr Ala Thr His Tyr Ala Glu 165 170 175 TCT GTG AAA GGG AGG πC ACC ATC TCA AGA GAT GAT TCC AAA AGT AGT 240 Ser Val Lys Gly Arg Phe Thr He Ser Arg Asp Asp Ser Lys Ser Ser 180 185 190 GTC TAC CTG CAA ATG AAC AAC πA AGA GCT GAA GAC ACT GGC Aπ TAT 288 Val Tyr Leu Gin Met Asn Asn Leu Arg Ala Glu Asp Thr Gly He Tyr 195 200 205 TAC TGT ACG GGA GTG GGA CAG Tπ GCT TAC TGG GGC CAA GGG ACC ACG 336 Tyr Cys Thr Gly Val Gly Gin Phe Ala Tyr Trp Gly Gin Gly Thr Thr 210 215 220 GTC ACC GTC TCC TC 350 Val Thr Val Ser 225 Table 7 Phi (φ) and psi (ψ) dihedral angles for the bound MUCl peptide antigen. Residue φ (°) ψ (°) Ala 2P — Ϊ4Ϊ Ala 3P -92 160 Pro 4P -81 -165 Asp 5P -78 101 Thr 6P -97 16 Arg 7P -71 143 Pro 8P -65 135 Ala 9P -66 153 Pro 10P -59 Table 8 SM3 - MUCl van der Waals (vdW) contacts and hydrogen bonds (HB; direct and mediated through water). Residues involved in the cis -peptide bond are underlined. Ser2P was modelled as Ala. Distance cut-off used: 4.θA for vdW contacts, 4.θA for direct HBs (weak HB above 3.5A are marked with an asterisk) and 3.5A for water mediated HBs. MC and SC refer to the main chain and side chain atoms of the SM3 antibody, respectively. Peptide number of Fab residues CDR Hydrogen bond Distance (A) residue vdW contacts peptide - Fab MC SC Ser2P 1 4 W 9,L , S 93L L3 O - Nεl (W" L ) 2.63 (Ala) O - O (S 93L ) 3.46 4 W" L L3 1 W 33H HI R 52H H2 0- water -Nηl(R ϊ2H ) 2.90, 2.98 6 W 91L , W 6L L3 N - Nεl (W lL ) 3.88 * 6 W 33H HI 2 gϋ. H3 Asp5P 3 19 γ32H 33H HI 051 - Nεl (W 33H ) 3.89' HI 052 - N (W 3H ) 3.18 HI 052 - water - O (W 33H ) 2.71, 2.78 N 3.H HI Oδl- water - O (N 31H ) 2.48, 2.66 HI 052- ater -0(N 3,H ) 3.35, 2.66 3 CE H3 0-Nε2(C£Iϋ) 3.01 γ»SH H3 052- water -N(V ϊH ) 2.71, 2.89 G 9 W 6H H H3 052- ater -N(ΩUϋ) 3.08,2.73 H3 O - water - N (G 96H ) 2.96, 2.73 Thr6P γ32L LI N 53L L2 O- water -Oδl (N 53 ) 2.94, 3.25 Arg7P N JIH , Y HI Nε - O (N 3IH ) 3.51 Nη2 - N52 (N 3,H ) 3.34 Nη2 - Oδl (N 3IH ) 3.98 * H3 O - water - N (G 96H ) 2.70, 2.73 Pro8P Λ 32H HI O - Oη (Y 32H ) 2.43 2 γ32H HI N-Oη(Y 32H ) 3.91 * ProlOP 2 p56L L2 4 p27H γ32H HI N-Oη(Y 32H ) 3.36 Total 5 88 LI, L2, L3, HI, H3 Table 9 MSA buried upon SM3 - MUCl peptide antigen complex formation . MSA has been calculated for individual SM3 CDRs and the peptide antigen alone . Residues involved in non- Proline cis -peptide bond are underlined . Residues buried MSA l buried (A 2 ) % total buried MSA A. SM3 light chain LI: Ser30L 2.3 0.4 Tyr32L 48.5 9.5 LI: 26-32 (10 residues) 50.8 9.9 L2: Asn53L 4.1 0.8 Ala55L 3.0 0.6 Pro56L 33.8 6.6 L2: 50-56 (7 residues) 40.9 8.0 L3: Trp91L 44.7 8.7 Ser93L 21.1 4.1 Trp96L 16.8 3.3 L3: 89-96 (7 residues) 82.6 16.1 Total light chain 174.3 34.0 B. SM3 Heavy chain Phe27H 20.7 4.0 Thr28H 3.9 0.8 HI: Asn31H 34.4 6.7 Tyr32H 65.6 12.8 Trp33H 58.4 11.4 Asn35H 2.9 0.6 HI: 31-35 (5 residues) 161.3 31.5 H2: Arg52H 9.6 1.9 Leu52aH 10.7 2.1 H2: 52-65 (17 residues) 20.3 4.0 H3: Val95H 40.8 8.0 Glv96H 19.8 3.8 Gln97H 43.4 8.5 AlalOlH 5.3 1.0 Tyrl02H 23.0 4.5 H3: 95-102 (6 rsidues) 132.3 25.8 Total heavy chain 338.5 66.0 Total SM3 Fab 512.8 C. MUCl peptide Ala2P 38.0 8.8 Ala3P 32.2 7.4 Pro4P 69.7 16.1 Asp5P 82.5 19.0 ThrόP 23.5 5.4 Arg7P 65.2 15.1 ProδP 20.7 4.8 Ala9P 36.7 8.5 ProlOP 64.7 14.9 Total MUCl peptide 433.2 1 MSA calculated according to MS program (Connolly, 1983) using a probe radius of 1.7 A. Table 10 SAA buried upon antibody-peptide complex formation, calculated using PDBAREA 1 . Fab PDB Peptide Fab name code 2 Total SAA hydrophobic polar SAA hydrophobic Total SAA hydrophobic polar SAA hydrophobic buried (A 2 ) SAA (A 2 ) (A 2 ) / polar buried (A 2 ) SAA (A 2 ) (A 2 ) / polar 59.1 lacy 614 462 152 3.04 437 257 180 1.43 O lfpt 626 277 349 0.79 439 245 194 1.26 50.1 W 685 514 171 3.00 456 291 165 1.76 17/9 lhim 626 394 232 1.70 464 232 232 1.00 D n likf likf 3 702 600 102 5.88 557 358 199 1.80 MN12H2 lmpa 4 699 326 373 0.87 561 333 228 1.46 π n TE33 ltet 718 425 293 1.45 512 263 249 1.06 CO 2H 19 589 400 189 2.12 < ι 1 1 2hlp 695 529 166 3. I Fll.2.32 2hrp 657 447 210 2.13 527 310 217 1.43 B13I2 2igf 677 427 250 1.71 485 ' 358 127 2.82 m t SM3 lsm3 606 392 214 1.83 480 318 162 1.96 1 PDBAREA (S. Islam, ICRF) calculates SAA using the algorithm of Lee & Richards (1971). For calculations a probe with a standard 1.4 A radii was used. Hydrophobic SAA includes C and S atoms, polar SAA - all other atoms (only non-hydrogen atoms used for calculations). The SAA is different from the MSA calculated by MS (Connolly, 1983) 2 According to Brookhaven Data Bank (Bernstein et al, 1977) 3 Cyclic peptide with non-standard residues 4 N-terminal residue in peptide is THC - N-methylcarbonyl threonine, and C- termnial is CYF - S-(4-Fluoresceinyl- carbamoyle-methyl)-cysteinyl.

Claims: C AIMS 1. Use of the structure factors obtainable by subjecting a crystal comprising at least an epitope binding fragment of the SM3 antibody, bound to a peptide recognised by the epitope binding site of SM3 to X-ray diffraction measurements to identify, screen, characterise, design or modify a chemical entity. 2. Use of the structural coordinates obtainable by subjecting a crystal comprising at least the epitope binding fragment of the SM3 antibody, bound to a peptide recognised by the epitope binding site of SM3 to X-ray diffraction measurements and deducing the structural coordinates from the diffraction measurements, to identify, screen, characterise, design or modify a chemical entity . 3. Use according to claim 1 or claim 2 in which the fragment of the SM3 antibody is the Fab fragment obtainable by digesting SM3 with papain. 4. Use according to claim 1 or claim 2 in which a moiety substantially similar to a fragment of the SM3 antibody is used instead of the fragment of the SM3 antibody. 5. Use according to any one of the preceding claims in which the peptide comprises the sequence Pro- Asp-Thr-Arg-Pro . 6. Use according to claim 5 in which the sequence is Thr-Ser-Ala-Pro-Asp-Thr-Arg-Pro-Ala-Pro-Gly- Ser-Thr. 7. Use of the structure factors as shown in Table 1 to identify, screen, characterise, design or modify a chemical entity. 8. Use of the structural coordinates as shown in Table 2a or 2b to identify, screen, characterise, design or modify a chemical entity. 9. Use according to any one of the preceding claims of the structure factors or structural coordinates to identify, screen, characterise or design a mimic of SM3. 10. Use according to claim 9 in which the mimic of SM3 has a desired association with aberrantly glycosylated MUCl. 11. Use according to claim 10 in which the desired association is binding affinity with aberrantly glycosylated MUCl which is higher than the binding affinity of SM3 for aberrantly glycosylated MUCl. 12. Use according to any one of claims 9 to 11 in which the mimic of SM3 is obtainable by modification of either whole SM3 or a fragment of SM3. 13. Use according to claim 12 in which the modification is the replacement of Proline 56 of SM3. 14. Use according to any one of the preceding claims of the structure factors or structural coordinates to identify, screen, characterise or design a mimic of the peptide epitope of MUCl recognised by SM3. 15. Use according to claim 14 in which the mimic of the peptide is used to produce a moiety which has a desired association with aberrantly glycosylated MUCl. 16. Use according to claim 15 in which the moiety is an antibody. 17. Use according to claim 16 in which the antibody is produced in a method comprising vaccinating an animal or human with the mimic of the peptide. 18. Use according to claim 14 in which the mimic of the peptide can prevent or decrease an immune response . 19. Use according to any one of claims 14 to 18 in which the mimic of the peptide is obtainable by a chemical modification of a peptide. 20. Use accordingly to any one of claims 14 to 19 ln which the mimic of the peptide is a glycosylated peptide . 21. A chemical entity which s a mimic of the peptide epitope of MUCl recognised by SM3 and not described in any database at the date of filing of the application . 22. A mimic of SM3 not described n any database at the date of filing of the application. 23. An antibody having a conformation comprising an engineered non-proline cis peptide bond. 24. A crystal comprising at least an epitope binding fragment of the SM3 antibody bound to a peptide recognised by the epitope binding site of SM3. 25. A method of producing a crystal of claim 24 which comprises contacting the fragment of SM3 or the peptide with cadmium. 26. A machine readable data storage medium comprising a data storage material encoded with machine readable data which when read by an appropriate machine is capable of displaying a three dimensional representation of a crystal as defined in claim 24. 27. A chemical entity, a mimic of SM3, a mimic of the peptide epitope of MUCl recognised by SM3, a moiety having a desired association with aberrantly glycosylated MUCl or an engineered antibody as defined in any one of "claims 7 to 23 for use in a method for treatment of the human or animal body by surgery or therapy or of diagnosis practised on the human or animal body. 28. Use of a chemical entity, a mimic of SM3, a mimic of the peptide epitope of MUCl recognised by SM3, a moiety having a desired association with aberrantly glycosylated MUCl or an engineered antibody as defined in any one of claims 7 to 23 in the production of a medicament for use m a method for anti-cancer treatment of the human or animal body by surgery or therapy or of cancer diagnosis practised on the human or animal body. 29. A method of cancer diagnosis or anti-cancer therapy comprising administering to a human or non-numan animal in need thereof an effective non-toxic amount of a chemical entity, a mimic of SM3, a mimic of the peptide epitope of MUCl recognised by SM3, a moiety having a desired association with aberrantly glycosylated MUCl or an engineered antibody as defined in any one of claims 7 to 23. 30. A product comprising a mimic of SM3 or a specific binding agent and an anti-tumour agent as a combined preparation for simultaneous, separate or sequential use in anti-cancer therapy. 31. A mimic of the MUCl epitope recognised by SM3 for use in a method of treating a disease caused by an immune response. 32. A method of therapy of a disease caused by an immune response comprising administering to a human or non-human animal m need thereof an effective non-toxic amount of a mimic of the MUCl epitope recognised by SM3. 33. Use of the structure factors and/or structural coordinates as defined m any one of claims 1 to 8 to solve the structural coordinates of a crystal.

Inventors: BATES PAUL ALAN, DOKURNO PAWEL, FREEMONT PAUL SIMON, SNARY DAVID, STERNBERG MICHAEL JOSEPH EZRA, BATES, PAUL, ALAN, DOKURNO, PAWEL, FREEMONT, PAUL, SIMON, SNARY, DAVID, STERNBERG, MICHAEL, JOSEPH, EZRA
Applicants: BATES PAUL ALAN, DOKURNO PAWEL, FREEMONT PAUL SIMON, IMP CANCER RES TECH, SNARY DAVID, STERNBERG MICHAEL JOSEPH EZRA, BATES, PAUL, ALAN, DOKURNO, PAWEL, FREEMONT, PAUL, SIMON, IMPERIAL CANCER RESEARCH TECHNOLOGY LIMITED, SNARY, DAVID, STERNBERG, MICHAEL, JOSEPH, EZRA
Application year: 1998
Main classification: C07K14
IPC codes: A61K38, A61K39, A61P35, C07K7, C07K14, C07K16, G01N33, G06F17