# Patent

## Title
Drug therapy for celiac sprue

## Abstract

Celiac Sprue and/or dermatitis herpetiformis are treated by interfering with HLA binding of immunogenic gluten peptides. The antigenicity of gluten oligopeptides and the ill effects caused by an immune response thereto are decreased by administration of an HLA-binding peptide inhibitor. Such inhibitors are analogs of immunogenic gluten peptides and (i) retain the to bind tightly to HLA molecules; (ii) retain the protcolytic stability of these peptides; but (iii) are unable to T cells.

## Background
CROSS-REFERENCE TO RELATED APPLICATIONS
This application claims priority to U.S. Provisional Application No. 60/380,761 filed May 14, 2002; to U.S. Provisional Application No. 60/392,782 filed Jun. 28, 2002; and to U.S. Provisional application No. 60/422,933, filed Oct. 31, 2002, and to U.S. Provisional Application No. 60/428,033, filed Nov. 20, 2002, each of which are herein specifically incorporated by reference.


This invention was made with Government support under contract 9910949 awarded by the National Science Foundation. The Government has certain rights in this invention.


BACKGROUND OF THE INVENTION
In 1953, it was first recognized that ingestion of gluten, a common dietary protein present in wheat, barley and rye causes a disease called Celiac Sprue in sensitive individuals. Gluten is a complex mixture of glutamine- and proline-rich gliadin and glutenin molecules and is thought to be responsible for induction of Celiac Sprue. Ingestion of such proteins by sensitive individuals produces flattening of the normally luxurious, rug-like, epithelial lining of the small intestine known to be responsible for efficient and extensive terminal digestion of peptides and other nutrients. Other clinical symptoms of Celiac Sprue include fatigue, chronic diarrhea, malabsorption of nutrients, weight loss, abdominal distension, anemia, as well as an enhanced risk for the development of osteoporosis and intestinal malignancies such as lymphoma and carcinoma. The disease has an incidence of approximately 1 in 200 in European populations and is believed to be significantly under diagnosed in other populations.
A related disease is dermatitis herpetiformis, which is a chronic eruption of the skin characterized by clusters of intensely pruritic vesicles, papules, and urticaria-like lesions. IgA deposits occur in almost all normal-appearing and perilesional skin. Asymptomatic gluten-sensitive enteropathy is found in 75 to 90% of patients and in some of their relatives. Onset is usually gradual. Itching and burning are severe, and scratching often obscures the primary lesions with eczematization of nearby skin, leading to an erroneous diagnosis of eczema. Strict adherence to a gluten-free diet for prolonged periods may control the disease in some patients, obviating or reducing the requirement for drug therapy. Dapsone, sulfapyridine, and colchicines are sometimes prescribed for relief of itching.
Celiac Sprue (CS) is generally considered to be an autoimmune disease and the antibodies found in the serum of the patients support the theory that the disease is immunological in nature. Antibodies to tissue transglutaminase (TG2, tTGase or tTG) and gliadin appear in almost 100% of the patients with active CS, and the presence of such antibodies, particularly of the IgA class, has been used in diagnosis of the disease.
The large majority of patients express the HLA-DQ2 [DQ(a1*05, b1*02)] and/or DQ8 [DQ(a1*03, b1*0302)] molecules. It is believed that intestinal damage is caused by interactions between specific gliadin oligopeptides and the HLA-DQ2 or DQ8 antigen, which in turn induce proliferation of T lymphocytes in the sub-epithelial layers. T helper 1 cells and cytokines apparently play a major role in a local inflammatory process leading to villous atrophy of the small intestine.
At the present time, there is no good therapy for the disease, except to avoid completely all foods containing gluten. Although gluten withdrawal has transformed the prognosis for children and substantially improved it for adults, some people still die of the disease, mainly adults who had severe disease at the outset. A leading cause of death is lymphoreticular disease, especially intestinal lymphoma. It is not known whether a gluten-free diet diminishes this risk. Apparent clinical remission is often associated with histologic relapse that is detected only by review biopsies or by increased titers of antibodies to tTGase (also called EMA antibodies).
Gluten is so widely used, for example, in commercial soups, sauces, ice creams, hot dogs, and other foodstuffs, that patients need detailed lists of foodstuffs to avoid and expert advice from a dietitian familiar with celiac disease. Ingesting even small amounts of gluten may prevent remission or induce relapse. Supplementary vitamins, minerals, and hematinics may also be required, depending on deficiency. A few patients respond poorly or not at all to gluten withdrawal, either because the diagnosis is incorrect or because the disease is refractory. In the latter case, oral corticosteroids (e.g., prednisone 10 to 20 mg bid) may induce response.
In view of the serious and widespread nature of Celiac Sprue and the difficulty of removing gluten from the diet, better methods of treatment are of great interest. In particular, there is a need for treatment methods that allow the Celiac Sprue individual to eat gluten-containing foodstuffs without ill effect or at least to tolerate such foodstuffs in small or moderate quantities without inducing relapse. The present invention meets this need for better therapies for Celiac Sprue.
SUMMARY OF THE INVENTION
In one aspect, the present invention provides methods for treating Celiac Sprue and/or dermatitis herpetiformis and the symptoms thereof by administration of an HLA-binding peptide inhibitor to the patient. In one embodiment, the HLA-binding peptide inhibitor employed in the method is an analog of an immunogenic gluten peptide, where an immunogenic gluten peptide is altered by the replacement of one or more amino acids, where the replacement may be another naturally occurring amino acid, non-naturally occurring amino acids, modified amino acids, amino acid mimetics, and the like. Analogs of immunogenic gluten peptides that (i) retain the ability to bind tightly to HLA molecules; (ii) retain the proteolytic stability of these peptides; but (iii) are unable to activate disease-specific or other T cells, are useful agents to treat Celiac Sprue.
In another aspect, the present invention provides novel HLA-binding peptide inhibitors and methods for treating Celiac Sprue and/or dermatitis herpetiformis by administering those compounds.
In another aspect, the invention provides pharmaceutical formulations comprising an HLA-binding peptide inhibitor and a pharmaceutically acceptable carrier. In one embodiment, such formulations comprise an enteric coating that allows delivery of the active agent to the intestine, and the agents are stabilized to resist digestion or acid-catalyzed modification in acidic stomach conditions. In another embodiment, the formulation also comprises one or more glutenases, as described in U.S. Provisional Application No. 60/392,782 filed Jun. 28, 2002; and U.S. Provisional Application No. 60/428,033, filed Nov. 20, 2002, both of which are incorporated herein by reference. The invention also provides methods for the administration of enteric formulations of one or more HLA-binding peptide inhibitors to treat Celiac Sprue.
In another aspect, the invention provides methods for screening candidate compounds to determine their suitability for use in the subject methods, by assessing the ability of a candidate agent for its ability to bind to HLA molecules, and/or to inhibit the activity of T cells reactive against gluten antigens.
Methods and compositions are provided for modeling the structure of a soluble (extracellular) domain of human HLA-DQ2 bound to an immunodominant gluten epitope, and for identifying molecules that will compete with the gluten peptide for MHC binding. In one embodiment, the methods of the invention utilize structural modeling, and the identification and design of molecules having a particular structure. The structural data provided herein is used for the rational design of drugs that affect immune system activation in Celiac Sprue and/or dermatitis herpetiformis. Analysis of the crystal structure in conjunction with sequence data identifies residues in the immunogenic gluten peptide that are important for interaction with the MHC molecule, and those that are accessible for interaction with the T cell antigen receptor. This information provides a basis for rational drug design.
These and other aspects and embodiments of the invention and methods for making and using the invention are described in more detail in the description of the drawings and the invention, the examples, the claims, and the drawings that follow.


DETAILED DESCRIPTION OF THE EMBODIMENTS
Celiac Sprue and/or dermatitis herpetiformis are treated by interfering with HLA binding of immunogenic gluten peptides. Therapeutic benefit can be enhanced in some individuals by increasing the digestion of gluten oligopeptides, whether by pretreatment of foodstuffs to be ingested or by administration of an enzyme capable of digesting the gluten oligopeptides, together with administration of an HLA-binding peptide inhibitor. Gluten oligopeptides are highly resistant to cleavage by gastric and pancreatic peptidases such as pepsin, trypsin, chymotrypsin, and the like, and their prolonged presence in the digestive tract can induce an autoimmune response. The antigenicity of gluten oligopeptides and the ill effects caused by an immune response thereto can be decreased by administration of an HLA-binding peptide inhibitor. Such inhibitors are analogs of immunogenic gluten peptides and (i) retain the ability to bind tightly to HLA molecules; (ii) retain the proteolytic stability of these peptides; but (iii) are unable to activate disease-specific or other T cells.
Methods and compositions are provided for the administration of one or more HLA-binding peptide inhibitors to a patient suffering from Celiac Sprue and/or dermatitis herpetiformis. In some embodiments and for some individuals, the methods of the invention remove the requirement that abstention from ingestion of glutens be maintained to keep the disease in remission. The compositions of the invention include formulations of tTGase inhibitors that comprise an enteric coating that allows delivery of the agents to the intestine in an active form; the agents are stabilized to resist digestion or alternative chemical transformations in acidic stomach conditions. In another embodiment, food is pretreated or combined with glutenase, or a glutenase is co-administered (whether in time or in a formulation of the invention) with an HLA-binding peptide inhibitor of the invention.
The subject methods are useful for both prophylactic and therapeutic purposes. Thus, as used herein, the term “treating” is used to refer to both prevention of disease, and treatment of a pre-existing condition. The treatment of ongoing disease, to stabilize or improve the clinical symptoms of the patient, is a particularly important benefit provided by the present invention. Such treatment is desirably performed prior to loss of function in the affected tissues; consequently, the prophylactic therapeutic benefits provided by the invention are also important. Evidence of therapeutic effect may be any diminution in the severity of disease, particularly diminution of the severity of such symptoms as fatigue, chronic diarrhea, malabsorption of nutrients, weight loss, abdominal distension, and anemia. Other disease indicia include the presence of antibodies specific for glutens, antibodies specific for tissue transglutaminase, the presence of pro-inflammatory T cells and cytokines, and degradation of the villus structure of the small intestine. Application of the methods and compositions of the invention can result in the improvement of any and all of these disease indicia of Celiac Sprue.
Patients that can benefit from the present invention include both adults and children. Children in particular benefit from prophylactic treatment, as prevention of early exposure to toxic gluten peptides can prevent development of the disease into its more severe forms. Children suitable for prophylaxis in accordance with the methods of the invention can be identified by genetic testing for predisposition, e.g. by HLA typing; by family history, and by other methods known in the art. As is known in the art for other medications, and in accordance with the teachings herein, dosages of the HLA-binding peptide inhibitors of the invention can be adjusted for pediatric use.
Because most proteases and peptidases are unable to hydrolyze the amide bonds of proline residues, the abundance of proline residues in gliadins and related proteins from wheat, rye and barley can constitute a major digestive obstacle for the enzymes involved. This leads to an increased concentration of relatively stable gluten derived oligopeptides in the gut. These stable gluten derived oligopeptides, called “immunogenic oligopeptides” herein, bind to MHC molecules, including HLA HLA-DQ2 or DQ8 molecules, to stimulate an immune response that results in the autoimmune disease aspects of Celiac Sprue. In some cases the enzyme tissue transglutaminase selectively deamidates certain glutamine residues in these peptides, thereby enhancing their potency for the DQ2 ligand binding pocket.
HLA-binding peptide inhibitors of the present invention are analogs of immunogenic gluten oligopeptides that (i) retain the ability to bind tightly to HLA molecules; (ii) retain the proteolytic stability of these peptides; but (iii) are unable to activate disease-specific or other T cells. The inhibitor may comprise oligomers of analogs. Multivalent gluten derived epitopes have markedly enhanced immunogenicity. Consequently, multivalent oligopeptides analogs can also be expected to have increased potency for MHC molecules. In addition, these longer peptides can be more resistant toward intestinal brush border proteolysis.
An immunogenic gluten oligopeptide analog is an analog of a peptide that comprises at least about 8 residues, and may comprise at least about 10 residues; at least about 11 residues, at least about 12 residues, at least about 13 residues, at least about 14 residues, or more, where the term “residue” refers to naturally occurring amino acids, non-naturally occurring amino acids, and amino acid mimetics or derivatives; and where the gluten peptide is altered by the replacement of one or more amino acids. The replacement may be another naturally occurring amino acid, non-naturally occurring amino acids, modified amino acids, amino acid mimetics, and the like; and may further be derivitized to further reduce the affinity of these ligands for disease-specific T cell receptors. The sequence of immunogenic gluten oligopeptides can be determined by one of skill in the art. Immunogenic gliadin oligopeptides are peptides derived during normal human digestion of gliadins and related storage proteins as described above, from dietary cereals, e.g. wheat, rye, barley, and the like. Such oligopeptides act as antigens for T cells in Celiac Sprue. For binding to Class II MHC proteins, immunogenic peptides are usually from about 8 to 20 amino acids in length, more usually from about 10 to 18 amino acids. Such peptides may include PXP motifs, such as the motif PQPQLP. Determination of whether an oligopeptide is immunogenic for a particular patient is readily determined by standard T cell activation and other assays known to those of skill in the art.
Among gluten proteins with potential harmful effect to Celiac Sprue patients are included the storage proteins of wheat, species of which include Triticum aestivum; Triticum aethiopicum; Triticum baeoticum; Triticum militinae; Triticum monococcum; Triticum sinskajae; Triticum timopheevii; Triticum turgidum; Triticum urartu, Triticum vavilovii; Triticum zhukovskyi; etc. A review of the genes encoding wheat storage proteins may be found in Colot (1990) Genet Eng (N Y) 12:225–41. Gliadin is the alcohol-soluble protein fraction of wheat gluten. Gliadins are typically rich in glutamine and proline, particularly in the N-terminal part. For example, the first 100 amino acids of α- and γ-gliadins contain  ̃35% and  ̃20% of glutamine and proline residues, respectively. Many wheat gliadins have been characterized, and as there are many strains of wheat and other cereals, it is anticipated that many more sequences will be identified using routine methods of molecular biology. Examples of gliadin sequences include but are not limited to wheat alpha gliadin sequences, for example as provided in Genbank, accession numbers AJ133612; AJ133611; AJ133610; AJ133609; AJ133608; AJ133607; AJ133606; AJ133605; AJ133604; AJ133603; AJ133602; D84341.1; U51307; U51306; U51304; U51303; U50984; and U08287. A sequence of wheat omega gliadin is set forth in Genbank accession number AF280605.
Among the immunogenic gluten oligopeptides that may be modified to generate an HLA-binding peptide inhibitor are included the peptide sequence (SEQ ID NO:2) QLQPFPQPELPYP; the sequence (SEQ ID NO:3) PQPELPY; the sequence (SEQ ID NO:4) PFPQPELPYP, (SEQ ID NO:5 PQPELPYPQPQLP, (SEQ ID NO:6) PQQSFPEQQPP, (SEQ ID NO:7) VQGQGIIQPEQPAQ, (SEQ ID NO:8) FPEQPQQPYPQQP, (SEQ ID NO:9) FPQQPEQPYPQQP, (SEQ ID NO:10) FSQPEQEFPQPQ and longer peptides containing such sequences or multiple copies of such sequences. Gliadins, secalins and hordeins contain several (SEQ ID NO:11) PQPQLPY sequences or sequences similar thereto rich in Pro-Gln residues that are high-affinity substrates for tTGase. The tTGase catalyzed deamidation of such sequences increases their affinity for HLA-DQ2, the class II MHC allele present in >90% Celiac Sprue patients. Presentation of these deamidated sequences by DQ2 positive antigen presenting cells effectively stimulates proliferation of gliadin-specific T cells from intestinal biopsies of most Celiac Sprue patients, providing evidence for the proposed mechanism of disease progression in Celiac Sprue.
Analog oligopeptides of the invention comprise at least one difference in amino acid sequence from a native gluten peptide, by the replacement of an amino acid with a different amino acid; a non-naturally occurring amino acid, a peptidomimetics, substituted amino acid, and the like. An L-amino acid from the native peptide may be altered to any other one of the 20 L-amino acids commonly found in proteins, any one of the corresponding D-amino acids, rare amino acids, such as 4-hydroxyproline, and hydroxylysine, or a non-protein amino acid, such as β-alanine, ornithine and homoserine. Also included with the scope of the present invention are amino acids that have been altered by chemical means such as methylation (e.g., α-methylvaline), deamidation, amidation of the C-terminal amino acid by an alkylamine such as ethylamine, ethanolamine, and ethylene diamine, and acylation or methylation of an amino acid side chain function (e.g., acylation of the epsilon amino group of lysine), deimination of arginine to citrulline, isoaspartylation, or phosphorylation on serine, threonine, tyrosine or histidine residues. Importantly, each of these altered amino acids provide a functional handle, e.g. amine, alcohol, aryl halide, and the like, which can be regioselectively derivatized to further reduce the affinity of these ligands for disease-specific T cell receptors. Peptide analogs may be further derivatized with substitutions, including, without limitation, ethers, amines, esters, amides, carbonates, carbamates, carbazates, ureas and C—C coupled derivatives. Other examples include oxidation of alcohols to ketones, followed by further modifications of the resulting carbonyl group, e.g. via preparation of oximes) or the carbon atom adjacent to the ketone. Such derivatives are encompassed by the term “analog”.
The proteolytic stability of gluten oligopeptides can be attributed, at least in part, to the presence of PXP motifs, which are resistant to enzymatic degradation. Preferred analogs of immunogenic gluten oligopeptides will comprise one or more proline residues, and may comprise one or more PXP motifs.
An immunogenic gluten peptide of particular interest is the 33-mer (SEQ ID NO:1) LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF, which is described in detail in International Patent Application US03/04743, herein specifically incorporated by reference. This peptide is both immunogenic and highly stable to proteases. T cell epitopes present in the 33-mer peptide include, inter alia, (SEQ ID NO:12) PFPQPQLPY, (SEQ ID NO:13) PQPQLPYPQ, (SEQ ID NO:14) PFPQPELPY; (SEQ ID NO:15) PQPELPYPQ; (SEQ ID NO:16) PYPOPELPY and (SEQ ID NO:17) PYPQPQLPY. In one embodiment of the invention, the immunogenic gluten oligopeptide analog is an analog of a peptide that comprises at least one T cell epitope selected from the group consisting of (SEQ ID NO:12) PFPQPQLPY, (SEQ ID NO:13) PQPQLPYPQ, (SEQ ID NO:14) PFPQPELPY; (SEQ ID NO:15) PQPELPYPQ; (SEQ ID NO:16) PYPQPELPY and (SEQ ID NO:17) PYPQPQLPY.
The structure of an immunogenic gluten oligopeptide bound to a presenting molecule, e.g. HLA-DQ2; HLA-DQ8; et6. can be determined, e.g. by crystallography, NMR, etc., and used to identify residues in a peptide that are involved in the binding to the MHC molecule, and that are involved in the binding to a T cell antigen receptor. Residues identified as accessible for interacting with the T cell receptor may be modified to decrease the interaction, e.g. by increasing steric hindrance, altering hydrophilicity or hydrophobicity, etc. Residues identified as involved in interaction with the binding cleft of an MHC molecule may be modified to increase the interaction, e.g. by incorporating amino acids known to interact strongly with the binding cleft.
One inhibitor of interest is an oligopeptide or peptidomimetic that comprises the sequence PXPQPELPY, where X is Gly, Ala, Tyr, Trp, Arg, Lys, p-iodo-Phe, 3-iodo-Tyr, p-amino-Phe, 3-amino-Tyr, hydroxylysine, ornithine, Asp, Glu, or any residue that is substantially bulkier or hydrophilic than Phe. Examples of suitable modifications include ethers, amines, esters, amides, carbonates, carbamates, carbazates, ureas and C—C coupled derivatives. Other examples include oxidation of alcohols to ketones, followed by further modifications of the resulting carbonyl group (e.g. via preparation of oximes) or the carbon atom adjacent to the ketone. The peptide may comprise modifications that increase binding potency to an MHC molecule, by varying residues that facilitate peptide docking into the binding cleft. Examples of such residues include Gln4, Glu-6, Leu-7, and Tyr-9 (numbering based on the epitope PFPQPELPY). Each of these residues interacts closely with several residues in the DQ2 binding pocket. By using structure-based molecular design methods, these interactions can be optimized.
Another inhibitor of interest is a oligopeptide or peptidomimetic that comprises the sequence PFPQX1ELX2Y, where X1 and X2 are independently selected from 4-hydroxy-Pro (either isomer at C-4), 4-amino-Pro (either isomer atC-4), or 3-hydroxy-Pro (either isomer atC-3), and proline, with the proviso that at least one of X1 and X2 is a residue other than proline.
Peptides and peptide analogs may be synthesized by standard chemistry techniques, including synthesis by automated procedure. In general, peptide analogs are prepared by solid-phase peptide synthesis methodology which involves coupling each protected amino acid residue to a resin support, preferably a 4-methylbenzhydrylamine resin, by activation with dicyclohexylcarbodiimide to yield a peptide with a C-terminal amide. Alternatively, a chloromethyl resin (Merrifield resin) may be used to yield a peptide with a free carboxylic acid at the C-terminus. After the last residue has been attached, the protected peptide-resin is treated with hydrogen fluoride to cleave the peptide from the resin, as well as deprotect the side chain functional groups. Crude product can be further purified by gel filtration, HPLC, partition chromatography, or ion-exchange chromatography.
The present invention provides crystals and structures of HLA-DQ2 bound to antigen, where the antigen is an immunogenic gluten peptide QLQPFPQPELPYP, which may be referred to for brevity as an “HLA-DQ2/peptide complex”. The structures and structural coordinates are useful in structural homology deduction, and in developing and screening agents that affect the gluten antigen presentation and immunogenicity. The structure information may be provided in a computer readable form, e.g. as a database of atomic coordinates, or as a three-dimensional model. The structures are useful, for example, in modeling interactions of the HLA molecule with the antigen, effect of inhibitors, etc. The structures are also used to identify molecules that bind to or otherwise interact with structural elements. One aspect of the present invention provides crystals of the HLA-DQ2/peptide complex, which can effectively diffract X-rays for the determination of the atomic coordinates.
The present invention further includes methods of using the structural information provided herein to derive a detailed structure of related peptide binding interactions, particularly other gluten peptides, or analogs and mimetics thereof. Such structural homology determination may utilize modeling, alone or in combination with structure determination.
The present invention provides three-dimensional coordinates for the HLA-DQ2/peptide complex. Such a data set may be provided in computer readable form. Methods of using such coordinates (including in computer readable form) in drug assays and drug screens as exemplified herein, are also part of the present invention. In a particular embodiment of this type, the coordinates contained in the data set can be used to identify potential modulators of the HLA-DQ2/peptide complex, including molecules that mimic the binding of the peptide to the HLA molecule, but which lack, or are substantially diminished in the ability to stimulate a T cell response.
In one embodiment, a potential agent for modulation of HLA-DQ2/peptide complex is selected by performing rational drug design with the three-dimensional coordinates determined for the crystal structures. Preferably the selection is performed in conjunction with computer modeling. Rational design may also be used in the genetic modification of immunogenic peptides by modeling the potential effect of a change in the amino acid sequence.
Computer analysis may be performed with one or more of the computer programs including: GRASP, O (Jones et al. (1991) Acta Cryst. A47:110); QUANTA, CHARMM, INSIGHT, SYBYL, MACROMODEL; ICM, and CNS (Brunger et al. (1998) Acta Cryst. D54:905). In a further embodiment of this aspect of the invention, an initial drug screening assay is performed using the three-dimensional structure so obtained, preferably along with a docking computer program. Such computer modeling can be performed with one or more Docking programs such as DOC, GRAM and AUTO DOCK. See, for example, Dunbrack et al. (1997) Foldinq & Design 2:27–42.
It should be understood that in the drug screening and protein modification assays provided herein, a number of iterative cycles of any or all of the steps may be performed to optimize the selection. For example, assays and drug screens that monitor the activity of the T cells in the presence and/or absence of a potential inhibitor are also included in the present invention and can be employed as an assay or drug screen, usually as a single step in a multi-step protocol.
The structure of the HLA-DQ2/peptide complex is useful in the design of agents that mimic the activity and/or specificity of the binding interaction. The structures encoded by the data may be computationally evaluated for an ability to associate with chemical entities. This provides insight into an element's ability to associate with chemical entities. Chemical entities that are capable of associating with these domains may alter immunogenicity. Such chemical entities are potential drug candidates. Alternatively, the structure encoded by the data may be displayed in a graphical format. This allows visual inspection of the structure, as well as visual inspection of the structure's association with chemical entities.
In one embodiment of the invention, an invention is provided for evaluating the ability of a chemical entity to associate with any of the molecules or molecular complexes set forth above. This method comprises the steps of employing computational means to perform a fitting operation between the chemical entity and the interacting surface of the polypeptide or nucleic acid; and analyzing the results of the fitting operation to quantify the association. The term “chemical entity”, as used herein, refers to chemical compounds, complexes of at least two chemical compounds, and fragments of such compounds or complexes. Molecular design techniques are used to design and select chemical entities, including inhibitory compounds, capable of binding to the HLA molecule, or to the gluten peptide. Such chemical entities may interact directly with certain key features of the structure.
It will be understood by those skilled in the art that not all of the atoms present in a significant contact residue need be present in a competitive binding agent. In fact, it is only those few atoms that shape the loops and actually form important contacts that are likely to be important for activity. Those skilled in the art will be able to identify these important atoms based on the structure model of the invention, which can be constructed using the structural data herein.
The design of compounds that bind to HLA-DQ2 according to this invention generally involves consideration of two factors. First, the compound must be capable of either competing for binding with an immunogenic gluten peptide; or physically and structurally associating with the HLA-DQ2 domains. Non-covalent molecular interactions important in this association include hydrogen bonding, van der Waals interactions, hydrophobic interactions and electrostatic interactions.
The compound must be able to assume a conformation that allows it to interact with the binding pocket. Although certain portions of the compound will not directly participate in these associations, those portions may still influence the overall conformation of the molecule. This, in turn, may have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity in relation to all or a portion of the binding pocket, or the spacing between functional groups of an entity comprising several interacting chemical moieties.
Computer-based methods of analysis fall into two broad classes: database methods and de novo design methods. In database methods the compound of interest is compared to all compounds present in a database of chemical structures and compounds whose structure is in some way similar to the compound of interest are identified. The structures in the database are based on either experimental data, generated by NMR or x-ray crystallography, or modeled three-dimensional structures based on two-dimensional data. In de novo design methods, models of compounds whose structure is in some way similar to the compound of interest are generated by a computer program using information derived from known structures, e.g. data generated by x-ray crystallography and/or theoretical rules. Such design methods can build a compound having a desired structure in either an atom-by-atom manner or by assembling stored small molecular fragments. Selected fragments or chemical entities may then be positioned in a variety of orientations, or docked, within the interacting surface of the RNA. Docking may be accomplished using software such as Quanta (Molecular Simulations, San Diego, Calif.) and Sybyl, followed by energy minimization and molecular dynamics with standard molecular mechanics force fields, such as CHARMM and AMBER.
Specialized computer programs may also assist in the process of selecting fragments or chemical entities. These include: SmoG, GRID (Goodford (1985) J. Med. Chem., 28, pp. 849–857; Oxford University, Oxford, UK; MCSS (Miranker et al. (1991) Proteins: Structure, Function and Genetics, 11, pp. 29–34; Molecular Simulations, San Diego, Calif.); AUTODOCK (Goodsell et al., (1990) Proteins: Structure, Function, and Genetics, 8, pp. 195–202; Scripps Research Institute, La Jolla, Calif.); and DOCK (Kuntz et al. (1982) J. Mol. Biol., 161:269–288; University of California, San Francisco, Calif.)
Once suitable chemical entities or fragments have been selected, they can be assembled into a single compound or complex. Assembly may be preceded by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates. Useful programs to aid one of skill in the art in connecting the individual chemical entities or fragments include: CAVEAT (Bartlett et al., (1989) In Molecular Recognition in Chemical and Biological Problems”, Special Pub., Royal Chem. Soc., 78, pp. 182–196; University of California, Berkeley, Calif.); 3D Database systems such as MACCS-3D (MDL Information Systems, San Leandro, Calif.); and HOOK (available from Molecular Simulations, San Diego, Calif.).
Other molecular modeling techniques may also be employed in accordance with this invention. See, e.g., N. C. Cohen et al., “Molecular Modeling Software and Methods for Medicinal Chemistry, J. Med. Chem., 33, pp. 883–894 (1990). See also, M. A. Navia et al., “The Use of Structural Information in Drug Design”, Current Opinions in Structural Biology, 2, pp. 202–210 (1992).
Once the binding entity has been optimally selected or designed, as described above, substitutions may then be made in some of its atoms or side groups in order to improve or modify its 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 group. It should, of course, be understood that components known in the art to alter conformation should be avoided. Such substituted chemical compounds may then be analyzed for efficiency o f fit by the same computer methods described above.
Another approach made possible and enabled by this invention, is the computational screening of small molecule databases. In this screening, the quality of fit of such entities to the binding site may be judged either by shape complementarity or by estimated interaction energy. Generally the tighter the fit, the lower the steric hindrances, and the greater the attractive forces, the more potent the potential modulator since these properties are consistent with a tighter binding constant. Furthermore, the more specificity in the design of a potential drug the more likely that the drug will not interact as well with other proteins. This will minimize potential side effects due to unwanted interactions with other proteins.
Compounds of interest can be systematically modified by computer modeling programs until one or more promising potential analogs are identified. In addition systematic modification of selected analogs can then be systematically modified by computer modeling programs until one or more potential analogs are identified. Alternatively a potential modulator could be obtained by initially screening a random peptide library, for example one produced by recombinant bacteriophage. A peptide selected in this manner would then be systematically modified by computer modeling programs as described above, and then treated analogously to a structural analog.
Once a potential modulator/inhibitor is identified it can be either selected from a library of chemicals as are commercially available from most large chemical companies including Merck, GlaxoWelcome, Bristol Meyers Squib, Monsanto/Searle, Eli Lilly, Novartis and Pharmacia UpJohn, or alternatively the potential modulator may be synthesized de novo. The de novo synthesis of one or even a relatively small group of specific compounds is reasonable in the art of drug design.
The success of both database and de novo methods in identifying compounds with activities similar to the compound of interest depends on the identification of the functionally relevant portion of the compound of interest. For drugs, the functionally relevant portion may be referred to as a pharmacophore, i.e. an arrangement of structural features and functional groups important for biological activity. Not all identified compounds having the desired pharmacophore will act as a modulator of inflammation. The actual activity can be finally determined only by measuring the activity of the compound in relevant biological assays. However, the methods of the invention are extremely valuable because they can be used to greatly reduce the number of compounds that must be tested to identify an actual inhibitor.
In order to determine the biological activity of a candidate pharmacophore it is preferable to measure biological activity at several concentrations of candidate compound. The activity at a given concentration of candidate compound can be tested in a number of ways.
For example, an HLA molecule can be attached to a solid support. Methods for placing proteins on a solid support are well known in the art and include such steps as linking biotin to the protein, and linking avidin to the solid support. The solid support can be washed to remove unreacted species. A solution of a labeled candidate agent can be contacted with the solid support. The solid support is washed again to remove the potential modulator not bound to the support. The amount of labeled potential modulator remaining with the solid support and thereby bound to the protein can be determined. Alternatively, or in addition, the dissociation constant between the labeled candidate agent and the protein can be determined.
Crystals of the binding complex of the present invention can be grown by a number of techniques including batch crystallization, vapor diffusion (either by sitting drop or hanging drop) and by microdialysis. Seeding of the crystals in some instances is required to obtain X-ray quality crystals. Standard micro and/or macro seeding of crystals may therefore be used. The crystals may be shrunk by transfer into solutions of different composition, e.g. by the addition of metal ions such as Mn2+, Pb2+, etc. Crystals may also be generated that include cofactors, substrates, candidate inhibitors, and the like, that interact with the protein, e.g. by cocrystallization of soaking protein crystals in a solution comprising an inhibitor or other agent.
Alternative methods may also be used. For example, crystals can be characterized by using X-rays produced in a conventional source (such as a sealed tube or a rotating anode) or using a synchrotron source. Methods of characterization include, but are not limited to, precision photography, oscillation photography and diffractometer data collection. Selenium-methionine may be used as described in the examples provided herein, or alternatively a heavy metal derivative data set (e.g., using PCMB) may be used in place of the selenium-methionine derivatization.
Electron density maps may be built from crystals using phase information from multiple isomorphous heavy-atom derivatives, molecular replacement or selenomethionine incorporated multiwavelength anomalous disperson technique. Model building is facilitated by the use of sequence markers, especially selenomethionine residues. Anomalous difference Fourier maps may be calculated with data from selenomethionine-substituted HLA-DQ2/GLUTEN EPITOPE and with experimental multiple isomorphous replacement with anomalous scattering (MIRAS) phases (Hemming and Edwards (2000) J. Biol. Chem. 275:2288). Maps are improved by phase combination, where MIRAS phases are combined by the program SIGMAA (Jones et al., supra.) Phase combination may be followed by solvent flattening with DM (Carson (1997) Methods Enzymol. 277:493). Improved maps may be obtained by combination of the MIRAS phases with improved phases from combined polyalanine and atomic models in an iterative process. The model can be refined by classical positional and B-factor minimization, and with manual rebuilding.
HLA-DQ2/peptide complex structure models and databases of structure information are provided. The structural models find use in determining the structure of related and/or analogous peptide complexes. In some cases, modeling will be based on the provided structure. In other embodiments, modeling will utilize the provided structure in combination with features present in homologous and/or related structures, where relationship may be defined by protein sequence similarity, or structural similarity, e.g. in the presence of specific features as described above.
The structure model may be implemented in hardware or software, or a combination of both. For most purposes, in order to use the structure coordinates generated for the structure, it is necessary to convert them into a three-dimensional shape. This is achieved through the use of free or commercially available software that is capable of generating three-dimensional graphical representations of molecules or portions thereof from a set of structure coordinates.
In one embodiment of the invention, a machine-readable storage medium is provided, the medium comprising a data storage material encoded with machine readable data which, when using a machine programmed with instructions for using said data, is capable of displaying a graphical three-dimensional representation of any of the structures of this invention that have been described above. Specifically, the computer-readable storage medium is capable of displaying a graphical three-dimensional representation of the HLA-DQ2/peptide complex.
Thus, in accordance with the present invention, data providing structural coordinates, alone or in combination with software capable of displaying the resulting three dimensional structure of the complex, portions thereof, and their structurally similar analogs, is stored in a machine-readable storage medium. Such data may be used for a variety of purposes, such as drug discovery, analysis of interactions between cellular components during translation, modeling of vaccines, and the like.
Preferably, the invention is implemented in computer programs executing on programmable computers, comprising a processor, a data storage system (including volatile and non-volatile memory and/or storage elements), at least one input device, and at least one output device. Program code is applied to input data to perform the functions described above and generate output information. The output information is applied to one or more output devices, in known fashion. The computer may be, for example, a personal computer, microcomputer, or workstation of conventional design.
Each program is preferably implemented in a high level procedural or object oriented programming language to communicate with a computer system. However, the programs can be implemented in assembly or machine language, if desired. In any case, the language may be a compiled or interpreted language.
Each such computer program is preferably stored on a storage media or device (e.g., ROM or magnetic diskette) readable by a general or special purpose programmable computer, for configuring and operating the computer when the storage media or device is read by the computer to perform the procedures described herein. The system may also be considered to be implemented as a computer-readable storage medium, configured with a computer program, where the storage medium so configured causes a computer to operate in a specific and predefined manner to perform the functions described herein.
The HLA-binding peptide inhibitors are incorporated into a variety of formulations for therapeutic administration. In one aspect, the agents are formulated into pharmaceutical compositions by combination with appropriate, pharmaceutically acceptable carriers or diluents, and may be formulated into preparations in solid, semi-solid, liquid or gaseous forms, such as tablets, capsules, powders, granules, ointments, solutions, suppositories, injections, inhalants, gels, microspheres, and aerosols. As such, administration can be achieved in various ways, usually by oral administration. The HLA-binding peptide inhibitors may be systemic after administration or may be localized by virtue of the formulation, or by the use of an implant that acts to retain the active dose at the site of implantation.
In pharmaceutical dosage forms, the HLA-binding peptide inhibitors may be administered in the form of their pharmaceutically acceptable salts, or they may also be used alone or in appropriate association, as well as in combination with other pharmaceutically active compounds. The agents may be combined, as previously described, to provide a cocktail of activities. The following methods and excipients are merely exemplary and are in no way limiting.
For oral preparations, the agents can be used alone or in combination with appropriate additives to make tablets, powders, granules or capsules, for example, with conventional additives, such as lactose, mannitol, corn starch or potato starch; with binders, such as crystalline cellulose, cellulose derivatives, acacia, corn starch or gelatins; with disintegrators, such as corn starch, potato starch or sodium carboxymethylcellulose; with lubricants, such as talc or magnesium stearate; and if desired, with diluents, buffering agents, moistening agents, preservatives and flavoring agents.
In one embodiment of the invention, the oral formulations comprise enteric coatings, so that the active agent is delivered to the intestinal tract. Enteric formulations are often used to protect an active ingredient from the strongly acid contents of the stomach. Such formulations are created by coating a solid dosage form with a film of a polymer that is insoluble in acid environments, and soluble in basic environments. Exemplary films are cellulose acetate phthalate, polyvinyl acetate phthalate, hydroxypropyl methylcellulose phthalate and hydroxypropyl methylcellulose acetate succinate, methacrylate copolymers, and cellulose acetate phthalate.
Other enteric formulation comprise engineered polymer microspheres made of biologically erodable polymers, which display strong adhesive interactions with gastrointestinal mucus and cellular linings, can traverse both the mucosal absorptive epithelium and the follicle-associated epithelium covering the lymphoid tissue of Peyer's patches. The polymers maintain contact with intestinal epithelium for extended periods of time and actually penetrate it, through and between cells. See, for example, Mathiowitz et al., (1997) Nature 386 (6623): 410–414. Drug delivery systems can also utilize a core of superporous hydrogels (SPH) and SPH composite (SPHC), as described by Dorkoosh et al. (2001) J Control Release 71(3):307–18.
Formulations are typically provided in a unit dosage form, where the term “unit dosage form,” refers to physically discrete units suitable as unitary dosages for human subjects, each unit containing a predetermined quantity of glutenase calculated in an amount sufficient to produce the desired effect in association with a pharmaceutically acceptable diluent, carrier or vehicle. The specifications for the unit dosage forms of the present invention depend on the particular complex employed and the effect to be achieved, and the pharmacodynamics associated with each complex in the host.
The pharmaceutically acceptable excipients, such as vehicles, adjuvants, carriers or diluents, are readily available to the public. Moreover, pharmaceutically acceptable auxiliary substances, such as pH adjusting and buffering agents, tonicity adjusting agents, stabilizers, wetting agents and the like, are readily available to the public.
Methods of Treatment
The subject methods are used to treat individuals suffering from Celiac Sprue and/or dermatitis herpetiformis, by administering an effective dose through a pharmaceutical formulation. Diagnosis of suitable patients may utilize a variety of criteria known to those of skill in the art. A quantitative increase in antibodies specific for gliadin, and/or tissue transglutaminase is indicative of the disease. Family histories and the presence of the HLA alleles HLA-DQ2 [DQ(a1*05, b1*02)] and/or DQ8 [DQ(a1*03, b1*0302)] are indicative of a susceptibility to the disease. Specific peptide analogs may be administered therapeutically to decrease inflammation, and/or to induce antigen-specific tolerance to treat autoimmunity. Methods for the delivery of peptides that are altered from a native peptide are known in the art. Alteration of native peptides with selective changes of crucial residues can induce unresponsiveness or change the responsiveness of antigen-specific autoreactive T cells.
The therapeutic effect may be measured in terms of clinical outcome, or may rely on immunological or biochemical tests. Suppression of the deleterious T-cell activity can be measured by enumeration of reactive Th1 cells, by quantitating the release of cytokines at the sites of lesions, or using other assays for the presence of autoimmune T cells known in the art. Alternatively, one may look for a reduction in symptoms of a disease.
Various methods for administration may be employed. The dosage of the therapeutic formulation will vary widely, depending upon the nature of the disease, the frequency of administration, the manner of administration, the clearance of the agent from the host, and the like. Such treatment could either be before meals or on a once-a-day basis or on a once-a-week basis, depending on the half-life of the inhibitor. A typical dose is at least about 1 μg, usually at least about 10 μg, more usually at least about 0.1 mg, and not more than about 10 mg, usually not more than about 1 mg. Enteric coating of these peptides may also enhance their lifetimes in the gut, thereby permitting delivery to the proximal and distal small intestinal tissue. Treatment of other autoimmune disorders such as Type I diabetes with such ligands may involve oral, intravenous or intramuscular administration. The initial dose may be larger, followed by smaller maintenance doses. The dose may be administered as infrequently as weekly or biweekly, or more often fractionated into smaller doses and administered daily, with meals, semi-weekly, etc. to maintain an effective dosage level.
The HLA-binding peptide inhibitors of the invention may be administered in the treatment of Type 1 diabetes (IDDM). IDDM and celiac disease are both immunologic disorders where specific HLA alleles are associated with disease risk. Transglutaminase autoantibodies can be found in some patients with IDDM. The prevalence of transglutaminase autoantibodies is higher in diabetic patients with HLA DQ2 or DQ8.
Human type I or insulin-dependent diabetes mellitus (IDDM) is characterized by autoimmune destruction of the β cells in the pancreatic islets of Langerhans. The depletion of β cells results in an inability to regulate levels of glucose in the blood. Overt diabetes occurs when the level of glucose in the blood rises above a specific level, usually about 250 mg/dl. In humans a long presymptomatic period precedes the onset of diabetes. During this period there is a gradual loss of pancreatic beta cell function. IDDM is currently treated by monitoring blood glucose levels to guide injection, or pump-based delivery, of recombinant insulin. Diet and exercise regimens contribute to achieving adequate blood glucose control. The inhibitors of the invention may be administered alone, or in combination with other therapies. The route of administration may be oral, as described for treatment of Celiac Sprue, or may be injected, e.g. i.v., i.m., etc. Administration may be performed during the pre-symptomatic phase, or in overt diabetes.
EXPERIMENTAL
EXAMPLE
It has long been known that the principal toxic components of wheat gluten are a family of closely related Pro-Gln rich proteins called gliadins. Recent reports have suggested that peptides from a short segment of α-gliadin appear to account for most of the gluten-specific recognition by CD4+ T cells from Celiac Sprue patients. These peptides are substrates of tissue transglutaminase (tTGase), the primary auto-antigen in Celiac Sprue, and the products of this enzymatic reaction bind to the class II HLA DQ2 molecule. This “immunodominant” region of α-gliadin is part of an unusually long proteolytic product generated by the digestive process that: (a) is exceptionally resistant to further breakdown by gastric, pancreatic and intestinal brush border proteases; (b) is the highest specificity substrate of human tissue transglutaminase (tTGase) discovered to date; (c) contains at least six overlapping copies of epitopes known to be recognized by patient derived T cells; (d) stimulates representative T cell clones that recognize these epitopes with sub-micromolar efficacy; and (e) has homologs in proteins from all toxic foodgrains but no homologs in non-toxic foodgrain proteins.
Identification of stable peptides from gastric protease, pancreatic protease and brush border membrane peptidase catalyzed digestion of recombinant α2-gliadin: α2-gliadin, a representative α-gliadin (Arentz-Hansen et al. (2000) Gut 46:46), was expressed in recombinant form and purified from E. coli. The α2-gliadin gene was cloned in pET28a plasmid (Novagen) and transformed into the expression host BL21(DE3) (Novagen). The transformed cells were grown in 1-liter cultures of LB media containing 50 μg/ml of kanamycin at 37° C. until the OD600 0.6–1 was achieved. The expression of α2-gliadin protein was induced with the addition of 0.4 mM isopropyl α-D-thiogalactoside (Sigma) and the cultures were further incubated at 37° C. for 20 hours. The cells expressing the recombinant α2-gliadin were centrifuged at 3600 rpm for 30 minutes. The pellet was resuspended in 15 ml of disruption buffer (200 mM sodium phosphate; 200 mM NaCl; 2.5 mM DTT; 1.5 mM benzamidine; 2.5 mM EDTA; 2 mg/L pepstatin; 2 mg/L leupeptin; 30% v/v glycerol) and lysed by sonication (1 minute; output control set to 6). After centrifugation at 45000 g for 45 min, the supernatant was discarded and the pellet containing gliadin protein was resuspended in 50 ml of 7M urea in 50 mM Tris (pH=8.0). The suspension was again centrifuged at 45000 g for 45 min and the supernatant was harvested for purification. The supernatant containing α2-gliadin was incubated with 1 ml of nickel-nitrilotriacetic acid resin (Ni-NTA; Qiagen) overnight and then batch-loaded on a column with 2 ml of Ni-NTA. The column was washed with 7M urea in 50 mM Tris (pH=8.0) and α2-gliadin was eluted with 200 mM imidazole, 7 M urea in 50 mM Tris (pH=4.5). The fractions containing α2-gliadin were pooled into a final concentration of 70% ethanol solution and two volumes of 1.5M NaCl were added to precipitate the protein. The solution was incubated at 4° C. overnight and the final precipitate was collected by centrifugation at 45000 g for 30 min, rinsed in water, and re-centrifuged to remove the urea. The final purification step of the α-2 gliadin was developed with reverse-phase HPLC. The Ni-NTA purified protein fractions were pooled in 7 M urea buffer and injected to a Vydac (Hesperia, Calif.) polystyrene reverse-phase column (i.d. 4.6 mm×25 cm) with the starting solvent (30% of solvent B: 1:1 HPLC-grade acetonitrile/isopropanol: 0.1% TFA). Solvent A was an aqueous solution with 0.1% TFA. The separation gradient extended from 30–100% of solvent B over 120 min at a flow rate of 0.8 ml/min.







TABLE 1







Amount of Peptides Digested after 15 hours













33-mer
Control A
Control B







H1P0
<20%
>90%
>90%



H2P0
<20%
>61%
>85%



H3P0
<20%
>87%
>95%



H4P0
<20%
>96%
>95%



H5P0
<20%
>96%
>95%










The purity of the recombinant gliadin was >95%, which allowed for facile identification and assignment of proteolytic products by LC-MS/MS/UV. Although many previous studies utilized pepsin/trypsin treated gliadins, it was found that, among gastric and pancreatic proteases, chymotrypsin played a major role in the breakdown of α2-gliadin, resulting in many small peptides from the C-terminal half of the protein and a few longer (>8 residues) peptides from the N-terminal half, the most noteworthy being a relatively large fragment, the 33-mer (SEQ ID NO: 1) LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF (residues 57–89). This peptide was of particular interest for two reasons: (a) Whereas most other relatively stable proteolytic fragments were cleaved to smaller fragments when the reaction times were extended, the 33-mer peptide remained intact despite prolonged exposure to proteases; and (b) three distinct patient-specific T cell epitopes identified previously are present in this peptide, namely, (SEQ ID NO:12) PFPQPQLPY, (SEQ ID NO:13) PQPQLPYPQ (3 copies), and (SEQ ID NO:17) PYPQPQLPY (2 copies).
To establish the physiological relevance of this peptide, composite gastric/pancreatic enzymatic digestion of α2 gliadin was then examined. As expected, enzymatic digestion with pepsin (1:100 w/w ratio), trypsin (1:100), chymotrypsin (1:100), elastase (1:500) and carboxypeptidase (1:100) was quite efficient, leaving behind only a few peptides longer than 9 residues (the minimum size for a peptide to show class II MHC mediated antigenicity). In addition to the above-mentioned 33-mer, the peptide WQIPEQSR was also identified, and was used as a control in many of the following studies.
The small intestinal brush-border membrane (BBM) enzymes are known to be vital for breaking down any remaining peptides from gastric/pancreatic digestion into amino acids, dipeptides or tripeptides for nutritional uptake. Therefore a comprehensive analysis of gliadin metabolism also required investigations into BBM processing of gliadin peptides of reasonable length derived from gastric and pancreatic protease treatment. BBM fractions were prepared from rat small intestinal mucosa. The specific activities of known BBM peptidases were verified to be within the previously reported range. Whereas the half-life of disappearance of (SEQ ID NO:18) WQIPEQSR was  ̃60 mm in the presence of 12 ng/μl BBM protein, the half-life of (SEQ ID NO:1) LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF digestion was >20 h. Therefore, the latter peptide remains intact throughout the digestive process in the stomach and upper small intestine, and is poised to act as a potential antigen for T cell proliferation and intestinal toxicity in genetically susceptible individuals.
The 33-mer gliadin peptide is an excellent substrate for tTGase, and the resulting product is a highly potent activator of patient-derived T cells: A number of recent studies have demonstrated that regiospecific deamidation of immunogenic gliadin peptides by tTGase increases their affinity for HLA-DQ2 as well as the potency with which they activate patient-derived gluten-specific T cells. It has been shown the specificity of tTGase for certain short antigenic peptides derived from gliadin is higher than its specificity toward its physiological target site in fibronectin, for example, the specificity of tTGase for the α-gliadin derived peptide (SEQ ID NO:19) PQPQLPYPQPQLPY is 5-fold higher than that for its target peptide sequence in fibrinogen, its natural substrate. The kinetics and regiospecificity of deamidation of the 33-mer α-gliadin peptide identified as above were therefore measured. The kcat/KM was higher than that reported for any peptide studied thus far: kcat/KM=440 min−1 mM−1 for (SEQ ID NO:1) LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF compared to kcat/KM=82 mm−1 mM−1 for (SEQ ID NO:11) PQPQLPY and kcat/KM=350 min−1 mM−1 for (SEQ ID NO:19) PQPQLPYPQPQLPY.
Moreover, LC-MS-MS analysis revealed that (SEQ ID NO:1) LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF was selectively deamidated by tTGase at the underlined residues. Since tTGase activity is associated with the brush border membrane of intestinal enterocytes, it is likely that dietary uptake of even small quantities of wheat gluten will lead to the build-up of sufficient quantities of this 33-mer gliadin peptide in the intestinal lumen so as to be recognized and processed by tTGase.
Structural characteristics of the 33-mer gliadin peptide and its naturally occurring homologs: Sequence alignment searches using BLASTP in all non-redundant protein databases revealed several homologs (E-value >0.001) of the 33-mer gliadin peptide. Interestingly, foodgrain derived homologs were only found in gliadins (from wheat), hordeins (from barley) and secalins (from rye), all of which have been proven to be toxic to Celiac patients (FIG. 7). Nontoxic foodgrain proteins, such as avenins (in oats), rice and maize, do not contain homologous sequences to the 33-mer gliadin. In contrast, a BLASTP search with the entire α2-gliadin sequence identified foodgrain protein homologs from both toxic and nontoxic proteins. Based on available information regarding the substrate specificities of gastric, pancreatic and BBM proteases and peptidases, it is predicted that, although most gluten homologs to the 33-mer gliadin peptide contained multiple proteolytic sites and are therefore unlikely to be completely stable toward digestion, several sequences from wheat, rye and barley are expected to be comparably resistant to gastric and intestinal proteolysis. The stable peptide homologs to the 33-mer α2-gliadin peptide are (SEQ ID NO:20) QPQPFPPQLPYPQTQPFPPQQPYPQP QPQ YPQPQ (from α1- and α6-gliadins); (SEQ ID NO:21) QQQPFPQQPIPQQPQPYPQQP QPYPQQPFPPQQPF (from B1 hordein SEQ ID NO:22) QPFPQPQQTFPQQPQLPFPQQPQQPFPQPQ (from y-gliadin); (SEQ ID NO:23) VQWPQQQPVPQPHQPF (from γ-gliadin), (SEQ ID NO:24) VQGQGIIQPQQPAQ (from γ-gliadin), (SEQ ID NO:25) FLQPQQPFPQQPQQPYPQQPQQPFPQ (from γ-gliadin), (SEQ ID NO:26) FSQPQQQFPQPQQPQQSFPQQQPP (from γ-gliadin), (SEQ ID NO:27) QPFPQPQQPTPIQPQQPFPQRPQQPFPQPQ (from ω-secalin). These stable peptides are all located at the N-terminal region of the corresponding proteins. The presence of proline residues after otherwise cleavable residues in these peptides would contribute to their proteolytic stability.
The unique primary sequence of the 33-mer gliadin peptide also had homologs among a few non-gluten proteins. Among the strongest homologs were internal sequences from pertactin (a highly immunogenic protein from Bordetella pertussis) and a mammalian inositol-polyphosphate 5-phosphatase of unknown function. In both cases available information suggested that the homology could have biologically relevance. For example, the region of pertactin that is homologous to the 33-mer gliadin peptide is known to be part of the immunodominant segment of the protein. In the case of the homologous phosphatase, the corresponding peptide region of the phosphatase is known to be responsible for vesicular trafficking of the phosphatase to the cytoplasmic Golgi. In analogy with the current picture of how gliadin peptides are presented to HLA-DQ2 via a tTGase mediated pathway, these Pro-Gln-rich segments of both pertactin and the phosphatase are likely to be good tTGase substrates.
Example 3
X-ray Crystallographic Analysis of soluble HLA-DQ2. The soluble extracellular domains of the α- and β-chains of HLA-DQ2 were co-expressed in insect cells using a baculovirus expression system (pAcAB3 vector, BD Biosciences). The β-chain is fused to a sequence encoding the epitope (SEQ ID NO:28) QLQPFPQPELPY at its N-terminal end, and to a biotin recognition sequence at its C-terminal end. Both subunits are also fused to complementary leucine zipper sequences at their C-terminal ends. Since a Factor Xa proteolysis site is engineered between the leucine zipper sequences and the DQ2 subunits, prior to crystallization the leucine zippers were removed from DQ2 by Factor Xa digestion.
Initial purification of the DQ2 heterodimer from the culture medium was performed on an immunoaffinity column containing an anti-DQ2 monoclonal antibody (2.12.E11) bound to a Protein A Sepharose CL-4B column. Subsequently DQ2 was treated with Factor Xa, and purified from the digestion mixture by anion-exchange chromatography followed by size-exclusion chromatography, and concentrated to 4 mg/ml in 25 mM Tris-HCl, pH 8.0. Crystals of the DQ2-epitope complex were obtained using the hanging drop method. Typically, 2 μL of protein solution (2 ̃4 mg/ml DQ2, 25 mM Tris-HCl, pH 8.0) and 2 μL of precipitant buffer (200 mM ammonium acetate, 40 mM ammonium sulfate, 4% ethylene glycol, 22 ̃26% PEG 3350) were combined in a single drop hanging over 1 mL of precipitant buffer at room temperature. Small crystals appeared within three days and grew to full size in two weeks.
For data collection, crystals were transferred to a cryoprotectant solution (mother liquor containing 28% ethylene glycol) for 2 hours, and then flash cooled at. 100K in liquid nitrogen. X-ray diffraction data were collected from a single crystal to 2.22 Å resolution at beamline 11-1 of the Stanford Synchrotron Radiation Laboratory using a Quantum 315 CCD detector. Oscillation images were processed with DENZO and data reduction was carried out with SCALEPACK.
The structure of DQ2-epitope complex was determined by molecular replacement using the program AMoRe in the CCP4 suite of programs. The 2.4 Å resolution structure of insulin peptide-HLA-DQ8 complex (RCSB accession code: 1JK8) minus the insulin peptide and solvent molecules was used as the search model. After initial refinement with the maximum likelihood function of program REFMAC, iterative cycles of refinement including simulated annealing, temperature factor refinement, and energy minimization were made with the program CNS. Model building and correction were performed using σA-weighted Fo–Fc and 2Fo–Fc electron density maps with the program O. The current model has R-factor of 0.2209 with a Rfree of 0.2793 at 2.22 Å resolution. Analysis of the Ramachandran plot generated using the program PROCHECK shows that 91.2% of residues are in most favored regions, 7.9% are in additional allowed regions, 0.5% are in generously allowed regions, and 0.5% are in disallowed regions.
There are two molecules of DQ2-epitope in the asymmetric unit. In the first complex, α-chain of DQ2, β-chain of DQ2, and the alpha-I epitope peptide (sequence QLQPFPQPELPY) are designated A, B, and C respectively. In the second complex, α-chain, β-chain, and epitope peptide are designated D, E, and F respectively. The model includes 354 water molecules (name: HOH) and 4 ethylene glycol molecules (name: EDO).
Thr-106—His-112 region in chain B and Arg-105—His-112 region in chain E are disordered and thus absent from the model. Superposition of the DQ8 structure suggests that these regions form an extended loop. Side chain conformation of the following residues are undefined due to weak electron density in the corresponding region and therefore only their backbone atoms are included in the model. Asp-135 (in chain B), Leu-2, Gln-3, Tyr-12 (in chain C), Asp-135, Gln-136 (in chain E), and Leu-2, Gln-3 (in chain F).
Structure-based design of DQ2 binding peptide inhibitors. The crystal structure of the DQ2-epitope complex reveals precisely which atoms in the peptide (SEQ ID NO:2) QLQPFPQPELPYP point outward (by inference into the T cell receptor binding pocket). Substitutions at these atoms can yield altered peptide ligands that retain the ability to bind tightly to DQ2 but are no longer able to allow docking of the DQ2-peptide complex into disease specific T cell receptors.
The coordinate of the structure are as follows:







TABLE 2





Coordinates















REMARK peptide link removed (applied DPEP): from B  105 to B  113


REMARK peptide link removed (applied DPEP): from E  104 to E  113


REMARK disulphide added: from A  107 to A  163


REMARK disulphide added: from B  15  to B  79


REMARK disulphide added: from B  117 to B  173


REMARK disulphide added: from D  107 to D  163


REMARK disulphide added: from E  15  to E  79


REMARK disulphide added: from E  117 to E  173


REMARK DATE: 25-Apr-03 13:00:06    created by user: kim


REMARK VERSION: 1.0


















ATOM
1
CB
VAL
A
2
31.060
3.851
4.095
1.00
39.43
A


ATOM
2
CG1
VAL
A
2
30.078
2.835
3.531
1.00
40.06
A


ATOM
3
CG2
VAL
A
2
30.370
5.185
4.344
1.00
39.97
A


ATOM
4
C
VAL
A
2
30.653
3.406
6.542
1.00
36.80
A


ATOM
5
O
VAL
A
2
29.644
2.702
6.527
1.00
38.25
A


ATOM
6
N
VAL
A
2
32.189
1.926
5.235
1.00
36.80
A


ATOM
7
CA
VAL
A
2
31.684
3.321
5.414
1.00
37.95
A


ATOM
8
N
ALA
A
3
30.910
4.267
7.523
1.00
34.99
A


ATOM
9
CA
ALA
A
3
30.003
4.416
8.658
1.00
32.94
A


ATOM
10
CB
ALA
A
3
30.325
3.368
9.721
1.00
33.34
A


ATOM
11
C
ALA
A
3
30.094
5.805
9.263
1.00
30.81
A


ATOM
12
O
ALA
A
3
30.980
6.583
8.914
1.00
29.57
A


ATOM
13
N
ASP
A
4
29.172
6.115
10.170
1.00
28.70
A


ATOM
14
CA
ASP
A
4
29.173
7.416
10.822
1.00
26.95
A


ATOM
15
CB
ASP
A
4
27.812
7.722
11.456
1.00
28.65
A


ATOM
16
CG
ASP
A
4
26.687
7.845
10.431
1.00
31.67
A


ATOM
17
OD1
ASP
A
4
26.904
8.417
9.339
1.00
33.31
A


ATOM
18
OD2
ASP
A
4
25.568
7.381
10.735
1.00
33.31
A


ATOM
19
C
ASP
A
4
30.254
7.432
11.898
1.00
26.51
A


ATOM
20
O
ASP
A
4
30.857
8.469
12.170
1.00
25.25
A


ATOM
21
N
HIS
A
5
30.493
6.277
12.515
1.00
26.22
A


ATOM
22
CA
HIS
A
5
31.527
6.164
13.544
1.00
26.52
A


ATOM
23
CB
HIS
A
5
30.939
6.339
14.950
1.00
25.34
A


ATOM
24
CG
HIS
A
5
30.240
7.647
15.156
1.00
28.69
A


ATOM
25
CD2
HIS
A
5
30.716
8.870
15.492
1.00
29.15
A


ATOM
26
ND1
HIS
A
5
28.881
7.801
14.979
1.00
28.23
A


ATOM
27
CE1
HIS
A
5
28.550
9.062
15.198
1.00
29.92
A


ATOM
28
NE2
HIS
A
5
29.645
9.732
15.511
1.00
29.84
A


ATOM
29
C
HIS
A
5
32.246
4.826
13.465
1.00
25.79
A


ATOM
30
O
HIS
A
5
31.630
3.785
13.227
1.00
25.68
A


ATOM
31
N
VAL
A
6
33.559
4.866
13.659
1.00
24.52
A


ATOM
32
CA
VAL
A
6
34.385
3.667
13.628
1.00
23.27
A


ATOM
33
CB
VAL
A
6
35.311
3.657
12.407
1.00
25.22
A


ATOM
34
CG1
VAL
A
6
36.187
2.414
12.440
1.00
24.31
A


ATOM
35
CG2
VAL
A
6
34.489
3.708
11.127
1.00
27.15
A


ATOM
36
C
VAL
A
6
35.256
3.633
14.876
1.00
22.15
A


ATOM
37
O
VAL
A
6
35.937
4.606
15.185
1.00
21.49
A


ATOM
38
N
ALA
A
7
35.239
2.513
15.586
1.00
19.90
A


ATOM
39
CA
ALA
A
7
36.038
2.382
16.799
1.00
19.70
A


ATOM
40
CB
ALA
A
7
35.132
2.394
18.034
1.00
14.59
A


ATOM
41
C
ALA
A
7
36.867
1.111
16.791
1.00
18.62
A


ATOM
42
O
ALA
A
7
36.548
0.153
16.088
1.00
20.78
A


ATOM
43
N
SER
A
8
37.947
1.120
17.560
1.00
16.95
A


ATOM
44
CA
SER
A
8
38.807
−0.048
17.700
1.00
18.62
A


ATOM
45
CB
SER
A
8
40.211
0.215
17.153
1.00
17.69
A


ATOM
46
OG
SER
A
8
40.209
0.271
15.738
1.00
19.81
A


ATOM
47
C
SER
A
8
38.868
−0.310
19.199
1.00
18.76
A


ATOM
48
O
SER
A
8
39.570
0.376
19.943
1.00
19.35
A


ATOM
49
N
TYR
A
9
38.070
−1.268
19.645
1.00
19.38
A


ATOM
50
CA
TYR
A
9
38.038
−1.608
21.048
1.00
19.44
A


ATOM
51
CB
TYR
A
9
36.628
−1.980
21.471
1.00
19.18
A


ATOM
52
CG
TYR
A
9
35.714
−0.785
21.375
1.00
18.65
A


ATOM
53
CD1
TYR
A
9
36.073
0.435
21.962
1.00
16.57
A


ATOM
54
CE1
TYR
A
9
35.237
1.537
21.897
1.00
17.39
A


ATOM
55
CD2
TYR
A
9
34.493
−0.865
20.716
1.00
17.15
A


ATOM
56
CE2
TYR
A
9
33.641
0.235
20.647
1.00
16.82
A


ATOM
57
CZ
TYR
A
9
34.020
1.431
21.243
1.00
18.07
A


ATOM
58
OH
TYR
A
9
33.169
2.509
21.210
1.00
19.77
A


ATOM
59
C
TYR
A
9
38.993
−2.751
21.106
1.00
20.21
A


ATOM
60
O
TYR
A
9
38.652
−3.911
21.344
1.00
15.05
A


ATOM
61
N
GLY
A
10
40.225
−2.357
20.831
1.00
21.69
A


ATOM
62
CA
GLY
A
10
41.311
−3.275
20.808
1.00
22.54
A


ATOM
63
C
GLY
A
10
42.276
−3.080
19.655
1.00
21.74
A


ATOM
64
O
GLY
A
10
42.248
−3.863
18.713
1.00
22.02
A


ATOM
65
N
VAL
A
11
43.083
−2.023
19.674
1.00
18.91
A


ATOM
66
CA
VAL
A
11
44.119
−1.949
18.651
1.00
17.39
A


ATOM
67
CB
VAL
A
11
44.554
−0.506
18.277
1.00
18.75
A


ATOM
68
CG1
VAL
A
11
45.845
−0.558
17.455
1.00
16.18
A


ATOM
69
CG2
VAL
A
11
43.481
0.165
17.432
1.00
15.25
A


ATOM
70
C
VAL
A
11
45.228
−2.644
19.447
1.00
17.05
A


ATOM
71
O
VAL
A
11
45.679
−2.145
20.481
1.00
19.34
A


ATOM
72
N
ASN
A
12
45.616
−3.828
19.005
1.00
17.39
A


ATOM
73
CA
ASN
A
12
46.643
−4.597
19.693
1.00
17.18
A


ATOM
74
CB
ASN
A
12
46.113
−5.994
20.052
1.00
15.04
A


ATOM
75
CG
ASN
A
12
44.834
−5.947
20.882
1.00
15.96
A


ATOM
76
OD1
ASN
A
12
43.780
−5.490
20.417
1.00
18.20
A


ATOM
77
ND2
ASN
A
12
44.921
−6.420
22.114
1.00
10.46
A


ATOM
78
C
ASN
A
12
47.863
−4.739
18.797
1.00
18.90
A


ATOM
79
O
ASN
A
12
47.752
−5.162
17.641
1.00
18.80
A


ATOM
80
N
LEU
A
13
49.026
−4.403
19.343
1.00
18.60
A


ATOM
81
CA
LEU
A
13
50.264
−4.478
18.599
1.00
19.90
A


ATOM
82
CB
LEU
A
13
50.695
−3.064
18.217
1.00
23.26
A


ATOM
83
CG
LEU
A
13
52.077
−2.881
17.594
1.00
24.86
A


ATOM
84
CD1
LEU
A
13
52.085
−3.494
16.201
1.00
26.92
A


ATOM
85
CD2
LEU
A
13
52.417
−1.402
17.534
1.00
24.75
A


ATOM
86
C
LEU
A
13
51.391
−5.165
19.370
1.00
20.37
A


ATOM
87
O
LEU
A
13
51.559
−4.953
20.566
1.00
21.11
A


ATOM
88
N
TYR
A
14
52.145
−6.004
18.673
1.00
21.04
A


ATOM
89
CA
TYR
A
14
53.291
−6.691
19.255
1.00
24.07
A


ATOM
90
CB
TYR
A
14
52.909
−8.050
19.844
1.00
27.05
A


ATOM
91
CG
TYR
A
14
54.091
−8.729
20.489
1.00
29.27
A


ATOM
92
CD1
TYR
A
14
54.569
−8.304
21.723
1.00
30.07
A


ATOM
93
CE1
TYR
A
14
55.709
−8.867
22.285
1.00
31.38
A


ATOM
94
CD2
TYR
A
14
54.783
−9.744
19.830
1.00
31.63
A


ATOM
95
CE2
TYR
A
14
55.923
−10.314
20.383
1.00
30.29
A


ATOM
96
CZ
TYR
A
14
56.381
−9.868
21.609
1.00
31.37
A


ATOM
97
OH
TYR
A
14
57.515
−10.413
22.160
1.00
34.48
A


ATOM
98
C
TYR
A
14
54.291
−6.900
18.128
1.00
25.30
A


ATOM
99
O
TYR
A
14
53.907
−7.206
16.994
1.00
25.51
A


ATOM
100
N
GLN
A
15
55.571
−6.725
18.429
1.00
24.61
A


ATOM
101
CA
GLN
A
15
56.603
−6.891
17.414
1.00
25.19
A


ATOM
102
CB
GLN
A
15
56.932
−5.549
16.754
1.00
23.54
A


ATOM
103
CG
GLN
A
15
57.278
−4.443
17.738
1.00
23.98
A


ATOM
104
CD
GLN
A
15
57.567
−3.116
17.056
1.00
26.32
A


ATOM
105
OE1
GLN
A
15
57.575
−2.062
17.702
1.00
28.26
A


ATOM
106
NE2
GLN
A
15
57.810
−3.159
15.749
1.00
24.64
A


ATOM
107
C
GLN
A
15
57.848
−7.487
18.036
1.00
26.16
A


ATOM
108
O
GLN
A
15
58.134
−7.263
19.211
1.00
24.31
A


ATOM
109
N
SER
A
16
58.583
−8.252
17.236
1.00
28.72
A


ATOM
110
CA
SER
A
16
59.801
−8.912
17.698
1.00
30.37
A


ATOM
111
CB
SER
A
16
60.341
−9.830
16.603
1.00
28.35
A


ATOM
112
OG
SER
A
16
60.569
−9.100
15.407
1.00
31.43
A


ATOM
113
C
SER
A
16
60.883
−7.918
18.111
1.00
32.37
A


ATOM
114
O
SER
A
16
61.538
−8.104
19.134
1.00
33.91
A


ATOM
115
N
TYR
A
17
61.073
−6.863
17.325
1.00
32.49
A


ATOM
116
CA
TYR
A
17
62.096
−5.890
17.664
1.00
34.27
A


ATOM
117
CB
TYR
A
17
62.172
−4.788
16.620
1.00
35.41
A


ATOM
118
CG
TYR
A
17
63.371
−3.911
16.837
1.00
37.77
A


ATOM
119
CD1
TYR
A
17
64.646
−4.347
16.470
1.00
39.38
A


ATOM
120
CE1
TYR
A
17
65.769
−3.569
16.715
1.00
40.15
A


ATOM
121
CD2
TYR
A
17
63.247
−2.671
17.456
1.00
36.31
A


ATOM
122
CE2
TYR
A
17
64.360
−1.886
17.707
1.00
39.40
A


ATOM
123
CZ
TYR
A
17
65.621
−2.338
17.335
1.00
41.42
A


ATOM
124
OH
TYR
A
17
66.732
−1.562
17.580
1.00
43.02
A


ATOM
125
C
TYR
A
17
61.821
−5.270
19.027
1.00
34.43
A


ATOM
126
O
TYR
A
17
60.765
−4.682
19.248
1.00
35.58
A


ATOM
127
N
GLY
A
18
62.783
−5.390
19.935
1.00
34.98
A


ATOM
128
CA
GLY
A
18
62.609
−4.854
21.270
1.00
35.78
A


ATOM
129
C
GLY
A
18
62.730
−5.968
22.292
1.00
36.87
A


ATOM
130
O
GLY
A
18
63.761
−6.082
22.952
1.00
38.48
A


ATOM
131
N
PRO
A
19
61.692
−6.807
22.459
1.00
37.06
A


ATOM
132
CD
PRO
A
19
61.745
−7.967
23.368
1.00
35.58
A


ATOM
133
CA
PRO
A
19
60.409
−6.769
21.747
1.00
34.79
A


ATOM
134
CB
PRO
A
19
59.853
−8.166
21.981
1.00
35.91
A


ATOM
135
CG
PRO
A
19
60.300
−8.437
23.394
1.00
36.88
A


ATOM
136
C
PRO
A
19
59.531
−5.706
22.379
1.00
33.10
A


ATOM
137
O
PRO
A
19
59.844
−5.209
23.456
1.00
33.71
A


ATOM
138
N
SER
A
20
58.435
−5.349
21.722
1.00
31.83
A


ATOM
139
CA
SER
A
20
57.548
−4.341
22.290
1.00
30.25
A


ATOM
140
CB
SER
A
20
58.060
−2.932
21.965
1.00
29.00
A


ATOM
141
OG
SER
A
20
58.072
−2.689
20.567
1.00
32.27
A


ATOM
142
C
SER
A
20
56.108
−4.497
21.820
1.00
27.93
A


ATOM
143
O
SER
A
20
55.829
−5.129
20.805
1.00
28.23
A


ATOM
144
N
GLY
A
21
55.191
−3.911
22.576
1.00
25.87
A


ATOM
145
CA
GLY
A
21
53.797
−4.001
22.222
1.00
23.78
A


ATOM
146
C
GLY
A
21
53.076
−2.732
22.598
1.00
23.94
A


ATOM
147
O
GLY
A
21
53.638
−1.840
23.247
1.00
24.81
A


ATOM
148
N
GLN
A
22
51.821
−2.641
22.187
1.00
20.60
A


ATOM
149
CA
GLN
A
22
51.033
−1.470
22.495
1.00
19.67
A


ATOM
150
CB
GLN
A
22
51.239
−0.400
21.415
1.00
19.28
A


ATOM
151
CG
GLN
A
22
50.584
0.943
21.736
1.00
18.12
A


ATOM
152
CD
GLN
A
22
50.732
1.971
20.613
1.00
18.84
A


ATOM
153
OE1
GLN
A
22
51.694
2.749
20.576
1.00
19.77
A


ATOM
154
NE2
GLN
A
22
49.777
1.968
19.688
1.00
16.83
A


ATOM
155
C
GLN
A
22
49.573
−1.873
22.566
1.00
18.66
A


ATOM
156
O
GLN
A
22
49.128
−2.747
21.826
1.00
18.45
A


ATOM
157
N
TYR
A
23
48.842
−1.257
23.484
1.00
17.25
A


ATOM
158
CA
TYR
A
23
47.423
−1.529
23.615
1.00
16.53
A


ATOM
159
CB
TYR
A
23
47.127
−2.497
24.752
1.00
14.51
A


ATOM
160
CG
TYR
A
23
45.674
−2.904
24.760
1.00
12.67
A


ATOM
161
CD1
TYR
A
23
45.251
−4.070
24.121
1.00
13.38
A


ATOM
162
CE1
TYR
A
23
43.904
−4.415
24.070
1.00
13.23
A


ATOM
163
CD2
TYR
A
23
44.713
−2.093
25.346
1.00
11.07
A


ATOM
164
CE2
TYR
A
23
43.365
−2.425
25.299
1.00
12.99
A


ATOM
165
CZ
TYR
A
23
42.964
−3.583
24.664
1.00
13.72
A


ATOM
166
OH
TYR
A
23
41.624
−3.907
24.611
1.00
17.15
A


ATOM
167
C
TYR
A
23
46.694
−0.220
23.860
1.00
16.88
A


ATOM
168
O
TYR
A
23
46.975
0.491
24.824
1.00
16.57
A


ATOM
169
N
THR
A
24
45.757
0.085
22.969
1.00
16.16
A


ATOM
170
CA
THR
A
24
44.975
1.311
23.038
1.00
16.43
A


ATOM
171
CB
THR
A
24
45.594
2.405
22.136
1.00
18.41
A


ATOM
172
OG1
THR
A
24
45.581
1.954
20.771
1.00
17.20
A


ATOM
173
CG2
THR
A
24
47.029
2.692
22.537
1.00
18.64
A


ATOM
174
C
THR
A
24
43.570
1.058
22.499
1.00
15.15
A


ATOM
175
O
THR
A
24
43.314
0.037
21.879
1.00
15.70
A


ATOM
176
N
HIS
A
25
42.667
1.993
22.754
1.00
15.66
A


ATOM
177
CA
HIS
A
25
41.320
1.924
22.210
1.00
15.79
A


ATOM
178
CB
HIS
A
25
40.243
1.834
23.297
1.00
13.55
A


ATOM
179
CG
HIS
A
25
39.956
0.430
23.734
1.00
15.91
A


ATOM
180
CD2
HIS
A
25
40.688
−0.704
23.624
1.00
13.86
A


ATOM
181
ND1
HIS
A
25
38.790
0.071
24.374
1.00
15.91
A


ATOM
182
CE1
HIS
A
25
38.815
−1.222
24.639
1.00
14.38
A


ATOM
183
NE2
HIS
A
25
39.956
−1.715
24.193
1.00
16.99
A


ATOM
184
C
HIS
A
25
41.176
3.212
21.437
1.00
14.18
A


ATOM
185
O
HIS
A
25
41.677
4.241
21.865
1.00
13.52
A


ATOM
186
N
GLU
A
26
40.510
3.150
20.292
1.00
14.81
A


ATOM
187
CA
GLU
A
26
40.333
4.329
19.462
1.00
16.96
A


ATOM
188
CB
GLU
A
26
41.132
4.188
18.164
1.00
16.34
A


ATOM
189
CG
GLU
A
26
42.644
4.158
18.311
1.00
18.80
A


ATOM
190
CD
GLU
A
26
43.345
4.036
16.958
1.00
22.68
A


ATOM
191
OE1
GLU
A
26
42.744
4.456
15.946
1.00
26.77
A


ATOM
192
OE2
GLU
A
26
44.490
3.539
16.901
1.00
20.46
A


ATOM
193
C
GLU
A
26
38.875
4.543
19.101
1.00
17.22
A


ATOM
194
O
GLU
A
26
38.104
3.597
18.996
1.00
18.66
A


ATOM
195
N
PHE
A
27
38.503
5.802
18.917
1.00
18.91
A


ATOM
196
CA
PHE
A
27
37.150
6.135
18.509
1.00
19.32
A


ATOM
197
CB
PHE
A
27
36.290
6.546
19.698
1.00
20.19
A


ATOM
198
CG
PHE
A
27
34.834
6.653
19.357
1.00
23.33
A


ATOM
199
CD1
PHE
A
27
34.024
5.524
19.360
1.00
22.07
A


ATOM
200
CD2
PHE
A
27
34.289
7.868
18.971
1.00
23.24
A


ATOM
201
CE1
PHE
A
27
32.692
5.606
18.980
1.00
26.16
A


ATOM
202
CE2
PHE
A
27
32.954
7.962
18.587
1.00
25.99
A


ATOM
203
CZ
PHE
A
27
32.155
6.828
18.592
1.00
25.46
A


ATOM
204
C
PHE
A
27
37.260
7.291
17.522
1.00
19.10
A


ATOM
205
O
PHE
A
27
37.733
8.375
17.871
1.00
19.83
A


ATOM
206
N
ASP
A
28
36.831
7.052
16.288
1.00
19.17
A


ATOM
207
CA
ASP
A
28
36.901
8.060
15.227
1.00
18.94
A


ATOM
208
CB
ASP
A
28
35.910
9.203
15.473
1.00
21.33
A


ATOM
209
CG
ASP
A
28
34.472
8.787
15.223
1.00
24.96
A


ATOM
210
OD1
ASP
A
28
34.266
7.801
14.484
1.00
25.18
A


ATOM
211
OD2
ASP
A
28
33.552
9.448
15.749
1.00
27.42
A


ATOM
212
C
ASP
A
28
38.297
8.640
15.043
1.00
17.57
A


ATOM
213
O
ASP
A
28
38.467
9.853
14.955
1.00
17.04
A


ATOM
214
N
GLY
A
29
39.292
7.760
15.002
1.00
17.53
A


ATOM
215
CA
GLY
A
29
40.658
8.189
14.779
1.00
17.51
A


ATOM
216
C
GLY
A
29
41.437
8.738
15.953
1.00
16.95
A


ATOM
217
O
GLY
A
29
42.621
9.010
15.814
1.00
19.26
A


ATOM
218
N
ASP
A
30
40.797
8.922
17.098
1.00
16.92
A


ATOM
219
CA
ASP
A
30
41.511
9.438
18.254
1.00
16.83
A


ATOM
220
CB
ASP
A
30
40.816
10.678
18.796
1.00
18.99
A


ATOM
221
CG
ASP
A
30
40.988
11.864
17.888
1.00
21.09
A


ATOM
222
OD1
ASP
A
30
42.145
12.177
17.538
1.00
22.94
A


ATOM
223
OD2
ASP
A
30
39.971
12.478
17.525
1.00
21.68
A


ATOM
224
C
ASP
A
30
41.656
8.392
19.345
1.00
17.25
A


ATOM
225
O
ASP
A
30
40.777
7.553
19.543
1.00
15.40
A


ATOM
226
N
GLU
A
31
42.784
8.453
20.041
1.00
16.77
A


ATOM
227
CA
GLU
A
31
43.111
7.514
21.107
1.00
18.43
A


ATOM
228
CB
GLU
A
31
44.620
7.607
21.392
1.00
20.90
A


ATOM
229
CG
GLU
A
31
45.147
6.853
22.608
1.00
24.68
A


ATOM
230
CD
GLU
A
31
46.678
6.924
22.702
1.00
27.25
A


ATOM
231
OE1
GLU
A
31
47.258
7.931
22.239
1.00
26.93
A


ATOM
232
OE2
GLU
A
31
47.302
5.985
23.242
1.00
27.21
A


ATOM
233
C
GLU
A
31
42.296
7.777
22.375
1.00
17.51
A


ATOM
234
O
GLU
A
31
42.361
8.863
22.952
1.00
17.13
A


ATOM
235
N
GLN
A
32
41.525
6.784
22.807
1.00
15.52
A


ATOM
236
CA
GLN
A
32
40.726
6.942
24.020
1.00
16.47
A


ATOM
237
CB
GLN
A
32
39.542
5.980
24.009
1.00
15.91
A


ATOM
238
CG
GLN
A
32
38.439
6.399
23.065
1.00
15.97
A


ATOM
239
CD
GLN
A
32
37.292
5.419
23.071
1.00
20.20
A


ATOM
240
OE1
GLN
A
32
37.478
4.228
22.808
1.00
18.09
A


ATOM
241
NE2
GLN
A
32
36.091
5.912
23.374
1.00
20.57
A


ATOM
242
C
GLN
A
32
41.584
6.701
25.255
1.00
16.61
A


ATOM
243
O
GLN
A
32
41.448
7.387
26.272
1.00
15.51
A


ATOM
244
N
PHE
A
33
42.470
5.720
25.151
1.00
15.59
A


ATOM
245
CA
PHE
A
33
43.370
5.389
26.239
1.00
16.34
A


ATOM
246
CB
PHE
A
33
42.583
4.854
27.443
1.00
17.21
A


ATOM
247
CG
PHE
A
33
41.951
3.502
27.222
1.00
16.68
A


ATOM
248
CD1
PHE
A
33
42.686
2.333
27.406
1.00
15.57
A


ATOM
249
CD2
PHE
A
33
40.598
3.397
26.903
1.00
18.54
A


ATOM
250
CE1
PHE
A
33
42.083
1.076
27.288
1.00
16.34
A


ATOM
251
CE2
PHE
A
33
39.983
2.147
26.782
1.00
17.35
A


ATOM
252
CZ
PHE
A
33
40.729
0.983
26.978
1.00
16.56
A


ATOM
253
C
PHE
A
33
44.363
4.343
25.776
1.00
16.66
A


ATOM
254
O
PHE
A
33
44.209
3.746
24.712
1.00
16.85
A


ATOM
255
N
TYR
A
34
45.398
4.139
26.572
1.00
16.03
A


ATOM
256
CA
TYR
A
34
46.377
3.125
26.264
1.00
16.93
A


ATOM
257
CB
TYR
A
34
47.636
3.730
25.621
1.00
16.33
A


ATOM
258
CG
TYR
A
34
48.528
4.541
26.523
1.00
17.31
A


ATOM
259
CD1
TYR
A
34
49.519
3.930
27.291
1.00
17.48
A


ATOM
260
CE1
TYR
A
34
50.367
4.683
28.097
1.00
19.16
A


ATOM
261
CD2
TYR
A
34
48.404
5.928
26.586
1.00
17.68
A


ATOM
262
CE2
TYR
A
34
49.244
6.690
27.388
1.00
19.73
A


ATOM
263
CZ
TYR
A
34
50.224
6.060
28.141
1.00
20.10
A


ATOM
264
OH
TYR
A
34
51.044
6.815
28.941
1.00
23.02
A


ATOM
265
C
TYR
A
34
46.692
2.473
27.588
1.00
17.88
A


ATOM
266
O
TYR
A
34
46.429
3.042
28.646
1.00
21.13
A


ATOM
267
N
VAL
A
35
47.213
1.261
27.535
1.00
17.31
A


ATOM
268
CA
VAL
A
35
47.571
0.570
28.749
1.00
18.89
A


ATOM
269
CB
VAL
A
35
46.950
−0.848
28.804
1.00
19.12
A


ATOM
270
CG1
VAL
A
35
47.589
−1.660
29.912
1.00
17.56
A


ATOM
271
CG2
VAL
A
35
45.454
−0.742
29.048
1.00
19.75
A


ATOM
272
C
VAL
A
35
49.084
0.478
28.786
1.00
18.84
A


ATOM
273
O
VAL
A
35
49.701
−0.050
27.877
1.00
16.51
A


ATOM
274
N
ASP
A
36
49.676
1.039
29.830
1.00
22.55
A


ATOM
275
CA
ASP
A
36
51.121
0.984
29.996
1.00
25.86
A


ATOM
276
CB
ASP
A
36
51.542
1.872
31.172
1.00
26.89
A


ATOM
277
CG
ASP
A
36
53.033
2.108
31.221
1.00
26.55
A


ATOM
278
OD1
ASP
A
36
53.796
1.125
31.270
1.00
29.78
A


ATOM
279
OD2
ASP
A
36
53.441
3.285
31.213
1.00
30.03
A


ATOM
280
C
ASP
A
36
51.393
−0.484
30.314
1.00
26.39
A


ATOM
281
O
ASP
A
36
51.016
−0.976
31.378
1.00
27.38
A


ATOM
282
N
LEU
A
37
52.024
−1.187
29.387
1.00
27.51
A


ATOM
283
CA
LEU
A
37
52.305
−2.600
29.588
1.00
29.51
A


ATOM
284
CB
LEU
A
37
52.754
−3.231
28.270
1.00
26.29
A


ATOM
285
CG
LEU
A
37
51.704
−3.111
27.160
1.00
25.10
A


ATOM
286
CD1
LEU
A
37
52.265
−3.630
25.852
1.00
21.32
A


ATOM
287
CD2
LEU
A
37
50.455
−3.876
27.557
1.00
22.51
A


ATOM
288
C
LEU
A
37
53.348
−2.838
30.674
1.00
30.95
A


ATOM
289
O
LEU
A
37
53.222
−3.774
31.457
1.00
31.43
A


ATOM
290
N
GLY
A
38
54.362
−1.980
30.734
1.00
33.46
A


ATOM
291
CA
GLY
A
38
55.403
−2.140
31.737
1.00
35.44
A


ATOM
292
C
GLY
A
38
54.956
−1.863
33.162
1.00
37.63
A


ATOM
293
O
GLY
A
38
55.369
−2.549
34.098
1.00
38.42
A


ATOM
294
N
ARG
A
39
54.101
−0.861
33.334
1.00
38.93
A


ATOM
295
CA
ARG
A
39
53.625
−0.499
34.660
1.00
40.81
A


ATOM
296
CB
ARG
A
39
53.645
1.029
34.803
1.00
42.41
A


ATOM
297
CG
ARG
A
39
54.968
1.627
34.339
1.00
44.76
A


ATOM
298
CD
ARG
A
39
55.113
3.118
34.619
1.00
47.83
A


ATOM
299
NE
ARG
A
39
56.318
3.644
33.976
1.00
50.52
A


ATOM
300
CZ
ARG
A
39
56.902
4.799
34.281
1.00
53.40
A


ATOM
301
NH1
ARG
A
39
56.399
5.575
35.235
1.00
54.01
A


ATOM
302
NH2
ARG
A
39
57.998
5.179
33.633
1.00
54.18
A


ATOM
303
C
ARG
A
39
52.229
−1.057
34.936
1.00
41.12
A


ATOM
304
O
ARG
A
39
51.664
−0.847
36.014
1.00
39.71
A


ATOM
305
N
LYS
A
40
51.687
−1.779
33.955
1.00
40.65
A


ATOM
306
CA
LYS
A
40
50.365
−2.380
34.070
1.00
39.55
A


ATOM
307
CB
LYS
A
40
50.415
−3.554
35.053
1.00
42.42
A


ATOM
308
CG
LYS
A
40
49.196
−4.467
34.996
1.00
46.46
A


ATOM
309
CD
LYS
A
40
49.266
−5.563
36.054
1.00
50.42
A


ATOM
310
CE
LYS
A
40
48.077
−6.513
35.947
1.00
51.25
A


ATOM
311
NZ
LYS
A
40
46.781
−5.779
35.970
1.00
52.15
A


ATOM
312
C
LYS
A
40
49.338
−1.348
34.540
1.00
37.45
A


ATOM
313
O
LYS
A
40
48.647
−1.560
35.533
1.00
35.78
A


ATOM
314
N
GLU
A
41
49.245
−0.237
33.812
1.00
35.81
A


ATOM
315
CA
GLU
A
41
48.317
0.847
34.142
1.00
33.83
A


ATOM
316
CB
GLU
A
41
49.077
2.079
34.655
1.00
36.46
A


ATOM
317
CG
GLU
A
41
49.660
1.997
36.049
1.00
41.33
A


ATOM
318
CD
GLU
A
41
50.500
3.224
36.374
1.00
44.23
A


ATOM
319
OE1
GLU
A
41
50.067
4.343
36.022
1.00
46.67
A


ATOM
320
OE2
GLU
A
41
51.585
3.076
36.981
1.00
45.55
A


ATOM
321
C
GLU
A
41
47.492
1.301
32.937
1.00
30.89
A


ATOM
322
O
GLU
A
41
47.995
1.373
31.816
1.00
27.89
A


ATOM
323
N
THR
A
42
46.227
1.623
33.182
1.00
28.11
A


ATOM
324
CA
THR
A
42
45.354
2.127
32.135
1.00
26.58
A


ATOM
325
CB
THR
A
42
43.882
1.773
32.406
1.00
27.67
A


ATOM
326
OG1
THR
A
42
43.716
0.349
32.394
1.00
25.55
A


ATOM
327
CG2
THR
A
42
42.979
2.419
31.357
1.00
25.33
A


ATOM
328
C
THR
A
42
45.506
3.642
32.212
1.00
26.90
A


ATOM
329
O
THR
A
42
45.305
4.232
33.269
1.00
25.79
A


ATOM
330
N
VAL
A
43
45.881
4.273
31.108
1.00
25.87
A


ATOM
331
CA
VAL
A
43
46.045
5.720
31.106
1.00
24.36
A


ATOM
332
CB
VAL
A
43
47.474
6.119
30.670
1.00
24.45
A


ATOM
333
CG1
VAL
A
43
47.698
7.606
30.906
1.00
24.38
A


ATOM
334
CG2
VAL
A
43
48.504
5.289
31.433
1.00
22.82
A


ATOM
335
C
VAL
A
43
45.039
6.331
30.141
1.00
24.94
A


ATOM
336
O
VAL
A
43
45.143
6.133
28.930
1.00
24.72
A


ATOM
337
N
TRP
A
44
44.063
7.065
30.672
1.00
24.50
A


ATOM
338
CA
TRP
A
44
43.050
7.681
29.824
1.00
25.64
A


ATOM
339
CB
TRP
A
44
41.804
8.033
30.642
1.00
25.03
A


ATOM
340
CG
TRP
A
44
41.224
6.859
31.370
1.00
25.96
A


ATOM
341
CD2
TRP
A
44
40.281
5.906
30.858
1.00
25.77
A


ATOM
342
CE2
TRP
A
44
40.067
4.946
31.870
1.00
26.64
A


ATOM
343
CE3
TRP
A
44
39.599
5.766
29.641
1.00
24.94
A


ATOM
344
CD1
TRP
A
44
41.529
6.450
32.634
1.00
26.43
A


ATOM
345
NE1
TRP
A
44
40.840
5.305
32.942
1.00
26.28
A


ATOM
346
CZ2
TRP
A
44
39.197
3.860
31.704
1.00
25.00
A


ATOM
347
CZ3
TRP
A
44
38.734
4.688
29.476
1.00
22.40
A


ATOM
348
CH2
TRP
A
44
38.542
3.749
30.501
1.00
24.18
A


ATOM
349
C
TRP
A
44
43.578
8.925
29.116
1.00
26.30
A


ATOM
350
O
TRP
A
44
44.321
9.713
29.700
1.00
24.42
A


ATOM
351
N
CYS
A
45
43.193
9.090
27.853
1.00
28.01
A


ATOM
352
CA
CYS
A
45
43.635
10.234
27.062
1.00
30.22
A


ATOM
353
CB
CYS
A
45
44.069
9.777
25.666
1.00
29.51
A


ATOM
354
SG
CYS
A
45
45.547
8.727
25.680
1.00
30.66
A


ATOM
355
C
CYS
A
45
42.574
11.317
26.951
1.00
31.06
A


ATOM
356
O
CYS
A
45
42.836
12.399
26.428
1.00
34.14
A


ATOM
357
N
LEU
A
46
41.375
11.016
27.439
1.00
31.99
A


ATOM
358
CA
LEU
A
46
40.261
11.965
27.436
1.00
32.61
A


ATOM
359
CB
LEU
A
46
39.137
11.493
26.506
1.00
31.72
A


ATOM
360
CG
LEU
A
46
38.810
12.325
25.263
1.00
32.47
A


ATOM
361
CD1
LEU
A
46
37.492
11.830
24.674
1.00
28.87
A


ATOM
362
CD2
LEU
A
46
38.710
13.810
25.617
1.00
29.99
A


ATOM
363
C
LEU
A
46
39.734
12.042
28.869
1.00
32.81
A


ATOM
364
O
LEU
A
46
39.195
11.066
29.395
1.00
33.99
A


ATOM
365
N
PRO
A
47
39.893
13.201
29.521
1.00
32.52
A


ATOM
366
CD
PRO
A
47
40.488
14.442
28.986
1.00
32.23
A


ATOM
367
CA
PRO
A
47
39.437
13.392
30.901
1.00
32.18
A


ATOM
368
CB
PRO
A
47
39.487
14.908
31.063
1.00
32.11
A


ATOM
369
CG
PRO
A
47
40.690
15.270
30.236
1.00
31.60
A


ATOM
370
C
PRO
A
47
38.066
12.800
31.245
1.00
30.96
A


ATOM
371
O
PRO
A
47
37.927
12.103
32.243
1.00
30.17
A


ATOM
372
N
VAL
A
48
37.064
13.068
30.418
1.00
30.75
A


ATOM
373
CA
VAL
A
48
35.715
12.563
30.663
1.00
32.56
A


ATOM
374
CB
VAL
A
48
34.748
13.040
29.560
1.00
34.04
A


ATOM
375
CG1
VAL
A
48
33.320
12.683
29.932
1.00
34.16
A


ATOM
376
CG2
VAL
A
48
34.881
14.556
29.368
1.00
38.02
A


ATOM
377
C
VAL
A
48
35.633
11.033
30.765
1.00
33.13
A


ATOM
378
O
VAL
A
48
34.698
10.485
31.355
1.00
33.55
A


ATOM
379
N
LEU
A
49
36.615
10.350
30.192
1.00
33.30
A


ATOM
380
CA
LEU
A
49
36.661
8.892
30.208
1.00
32.44
A


ATOM
381
CB
LEU
A
49
37.498
8.391
29.023
1.00
30.62
A


ATOM
382
CG
LEU
A
49
36.792
8.027
27.702
1.00
31.64
A


ATOM
383
CD1
LEU
A
49
35.578
8.888
27.464
1.00
29.12
A


ATOM
384
CD2
LEU
A
49
37.783
8.157
26.551
1.00
31.05
A


ATOM
385
C
LEU
A
49
37.226
8.343
31.519
1.00
33.77
A


ATOM
386
O
LEU
A
49
37.138
7.142
31.787
1.00
34.14
A


ATOM
387
N
ARG
A
50
37.794
9.221
32.339
1.00
34.56
A


ATOM
388
CA
ARG
A
50
38.367
8.810
33.618
1.00
35.58
A


ATOM
389
CB
ARG
A
50
38.987
10.009
34.345
1.00
37.99
A


ATOM
390
CG
ARG
A
50
40.137
10.720
33.636
1.00
40.65
A


ATOM
391
CD
ARG
A
50
40.657
11.846
34.529
1.00
43.05
A


ATOM
392
NE
ARG
A
50
41.603
12.748
33.872
1.00
44.85
A


ATOM
393
CZ
ARG
A
50
42.815
12.403
33.444
1.00
46.08
A


ATOM
394
NH1
ARG
A
50
43.254
11.159
33.592
1.00
46.76
A


ATOM
395
NH2
ARG
A
50
43.599
13.314
32.880
1.00
46.08
A


ATOM
396
C
ARG
A
50
37.334
8.168
34.547
1.00
35.55
A


ATOM
397
O
ARG
A
50
37.693
7.475
35.495
1.00
35.21
A


ATOM
398
N
GLN
A
51
36.054
8.412
34.284
1.00
36.77
A


ATOM
399
CA
GLN
A
51
34.987
7.859
35.116
1.00
37.34
A


ATOM
400
CB
GLN
A
51
33.658
8.558
34.821
1.00
39.02
A


ATOM
401
CG
GLN
A
51
33.123
8.306
33.418
1.00
41.24
A


ATOM
402
CD
GLN
A
51
31.765
8.947
33.189
1.00
43.49
A


ATOM
403
OE1
GLN
A
51
30.781
8.597
33.843
1.00
43.80
A


ATOM
404
NE2
GLN
A
51
31.706
9.895
32.260
1.00
44.01
A


ATOM
405
C
GLN
A
51
34.821
6.362
34.896
1.00
36.85
A


ATOM
406
O
GLN
A
51
34.250
5.665
35.734
1.00
37.06
A


ATOM
407
N
PHE
A
52
35.316
5.871
33.764
1.00
35.13
A


ATOM
408
CA
PHE
A
52
35.218
4.454
33.446
1.00
32.82
A


ATOM
409
CB
PHE
A
52
35.143
4.258
31.931
1.00
31.28
A


ATOM
410
CG
PHE
A
52
33.902
4.838
31.301
1.00
29.86
A


ATOM
411
CD1
PHE
A
52
32.640
4.549
31.821
1.00
27.82
A


ATOM
412
CD2
PHE
A
52
33.992
5.652
30.177
1.00
27.71
A


ATOM
413
CE1
PHE
A
52
31.490
5.060
31.234
1.00
25.58
A


ATOM
414
CE2
PHE
A
52
32.847
6.171
29.580
1.00
28.10
A


ATOM
415
CZ
PHE
A
52
31.592
5.873
30.111
1.00
28.21
A


ATOM
416
C
PHE
A
52
36.405
3.675
34.004
1.00
32.57
A


ATOM
417
O
PHE
A
52
37.370
4.256
34.494
1.00
32.22
A


ATOM
418
N
ARG
A
53
36.327
2.353
33.927
1.00
32.80
A


ATOM
419
CA
ARG
A
53
37.397
1.498
34.419
1.00
32.77
A


ATOM
420
CB
ARG
A
53
37.005
0.862
35.760
1.00
36.56
A


ATOM
421
CG
ARG
A
53
36.741
1.867
36.881
1.00
42.83
A


ATOM
422
CD
ARG
A
53
36.523
1.168
38.214
1.00
49.04
A


ATOM
423
NE
ARG
A
53
36.308
2.111
39.312
1.00
53.82
A


ATOM
424
CZ
ARG
A
53
36.195
1.758
40.589
1.00
54.70
A


ATOM
425
NH1
ARG
A
53
36.277
0.478
40.937
1.00
55.50
A


ATOM
426
NH2
ARG
A
53
36.004
2.683
41.520
1.00
55.64
A


ATOM
427
C
ARG
A
53
37.706
0.404
33.405
1.00
29.88
A


ATOM
428
O
ARG
A
53
36.806
−0.117
32.743
1.00
28.71
A


ATOM
429
N
PHE
A
54
38.986
0.066
33.293
1.00
26.44
A


ATOM
430
CA
PHE
A
54
39.440
−0.960
32.371
1.00
22.47
A


ATOM
431
CB
PHE
A
54
39.905
−0.325
31.060
1.00
21.88
A


ATOM
432
CG
PHE
A
54
40.181
−1.320
29.974
1.00
20.69
A


ATOM
433
CD1
PHE
A
54
39.150
−1.801
29.180
1.00
19.52
A


ATOM
434
CD2
PHE
A
54
41.471
−1.782
29.750
1.00
18.68
A


ATOM
435
CE1
PHE
A
54
39.399
−2.734
28.170
1.00
22.81
A


ATOM
436
CE2
PHE
A
54
41.733
−2.714
28.746
1.00
20.58
A


ATOM
437
CZ
PHE
A
54
40.697
−3.190
27.954
1.00
20.86
A


ATOM
438
C
PHE
A
54
40.597
−1.711
33.017
1.00
23.43
A


ATOM
439
O
PHE
A
54
41.631
−1.122
33.351
1.00
23.53
A


ATOM
440
N
ASP
A
55
40.408
−3.011
33.198
1.00
22.82
A


ATOM
441
CA
ASP
A
55
41.411
−3.874
33.805
1.00
24.70
A


ATOM
442
CB
ASP
A
55
40.785
−5.246
34.083
1.00
23.26
A


ATOM
443
CG
ASP
A
55
41.729
−6.190
34.789
1.00
26.24
A


ATOM
444
OD1
ASP
A
55
42.924
−5.853
34.933
1.00
28.75
A


ATOM
445
OD2
ASP
A
55
41.274
−7.279
35.192
1.00
26.38
A


ATOM
446
C
ASP
A
55
42.613
−4.011
32.861
1.00
24.24
A


ATOM
447
O
ASP
A
55
42.510
−4.629
31.802
1.00
23.91
A


ATOM
448
N
PRO
A
56
43.770
−3.437
33.238
1.00
23.69
A


ATOM
449
CD
PRO
A
56
44.084
−2.761
34.509
1.00
23.79
A


ATOM
450
CA
PRO
A
56
44.961
−3.522
32.387
1.00
23.45
A


ATOM
451
CB
PRO
A
56
46.002
−2.707
33.162
1.00
23.35
A


ATOM
452
CG
PRO
A
56
45.592
−2.897
34.580
1.00
23.31
A


ATOM
453
C
PRO
A
56
45.413
−4.952
32.114
1.00
23.66
A


ATOM
454
O
PRO
A
56
46.099
−5.220
31.125
1.00
23.15
A


ATOM
455
N
GLN
A
57
45.025
−5.871
32.991
1.00
21.84
A


ATOM
456
CA
GLN
A
57
45.397
−7.261
32.818
1.00
22.47
A


ATOM
457
CB
GLN
A
57
44.834
−8.108
33.965
1.00
23.11
A


ATOM
458
CG
GLN
A
57
45.226
−9.568
33.873
1.00
20.82
A


ATOM
459
CD
GLN
A
57
46.722
−9.745
33.733
1.00
22.23
A


ATOM
460
OE1
GLN
A
57
47.497
−9.227
34.539
1.00
21.88
A


ATOM
461
NE2
GLN
A
57
47.138
−10.475
32.707
1.00
23.15
A


ATOM
462
C
GLN
A
57
44.882
−7.792
31.482
1.00
22.21
A


ATOM
463
O
GLN
A
57
45.452
−8.723
30.913
1.00
23.00
A


ATOM
464
N
PHE
A
58
43.801
−7.203
30.980
1.00
22.42
A


ATOM
465
CA
PHE
A
58
43.254
−7.640
29.704
1.00
21.07
A


ATOM
466
CB
PHE
A
58
42.004
−6.857
29.338
1.00
20.45
A


ATOM
467
CG
PHE
A
58
41.411
−7.287
28.031
1.00
21.03
A


ATOM
468
CD1
PHE
A
58
40.472
−8.312
27.988
1.00
18.42
A


ATOM
469
CD2
PHE
A
58
41.864
−6.736
26.835
1.00
18.79
A


ATOM
470
CE1
PHE
A
58
39.992
−8.792
26.765
1.00
21.25
A


ATOM
471
CE2
PHE
A
58
41.393
−7.207
25.610
1.00
20.28
A


ATOM
472
CZ
PHE
A
58
40.457
−8.238
25.578
1.00
21.18
A


ATOM
473
C
PHE
A
58
44.278
−7.401
28.612
1.00
21.79
A


ATOM
474
O
PHE
A
58
44.529
−8.260
27.763
1.00
21.84
A


ATOM
475
N
ALA
A
59
44.849
−6.202
28.637
1.00
21.80
A


ATOM
476
CA
ALA
A
59
45.840
−5.801
27.657
1.00
21.67
A


ATOM
477
CB
ALA
A
59
46.254
−4.346
27.892
1.00
21.11
A


ATOM
478
C
ALA
A
59
47.053
−6.711
27.732
1.00
22.06
A


ATOM
479
O
ALA
A
59
47.518
−7.213
26.706
1.00
22.53
A


ATOM
480
N
LEU
A
60
47.561
−6.925
28.945
1.00
19.83
A


ATOM
481
CA
LEU
A
60
48.729
−7.777
29.116
1.00
20.88
A


ATOM
482
CB
LEU
A
60
49.163
−7.815
30.585
1.00
20.57
A


ATOM
483
CG
LEU
A
60
50.060
−6.657
31.053
1.00
24.17
A


ATOM
484
CD1
LEU
A
60
49.239
−5.392
31.205
1.00
24.16
A


ATOM
485
CD2
LEU
A
60
50.717
−7.012
32.382
1.00
24.31
A


ATOM
486
C
LEU
A
60
48.496
−9.193
28.598
1.00
20.44
A


ATOM
487
O
LEU
A
60
49.367
−9.770
27.955
1.00
21.97
A


ATOM
488
N
THR
A
61
47.319
−9.749
28.871
1.00
20.69
A


ATOM
489
CA
THR
A
61
46.997
−11.101
28.418
1.00
19.49
A


ATOM
490
CB
THR
A
61
45.697
−11.629
29.084
1.00
18.59
A


ATOM
491
OG1
THR
A
61
45.919
−11.830
30.489
1.00
21.12
A


ATOM
492
CG2
THR
A
61
45.274
−12.942
28.453
1.00
17.61
A


ATOM
493
C
THR
A
61
46.834
−11.140
26.903
1.00
19.22
A


ATOM
494
O
THR
A
61
47.325
−12.059
26.242
1.00
21.19
A


ATOM
495
N
ASN
A
62
46.152
−10.142
26.351
1.00
18.05
A


ATOM
496
CA
ASN
A
62
45.934
−10.092
24.910
1.00
19.26
A


ATOM
497
CB
ASN
A
62
45.020
−8.910
24.552
1.00
20.51
A


ATOM
498
CG
ASN
A
62
43.835
−9.324
23.680
1.00
22.06
A


ATOM
499
OD1
ASN
A
62
43.406
−10.482
23.693
1.00
21.71
A


ATOM
500
ND2
ASN
A
62
43.294
−8.371
22.930
1.00
20.64
A


ATOM
501
C
ASN
A
62
47.270
−9.975
24.188
1.00
18.14
A


ATOM
502
O
ASN
A
62
47.517
−10.681
23.217
1.00
19.73
A


ATOM
503
N
ILE
A
63
48.146
−9.108
24.684
1.00
18.98
A


ATOM
504
CA
ILE
A
63
49.448
−8.921
24.061
1.00
19.88
A


ATOM
505
CB
ILE
A
63
50.229
−7.757
24.725
1.00
21.31
A


ATOM
506
CG2
ILE
A
63
51.601
−7.590
24.064
1.00
20.11
A


ATOM
507
CG1
ILE
A
63
49.425
−6.457
24.599
1.00
20.91
A


ATOM
508
CD1
ILE
A
63
49.037
−6.092
23.171
1.00
16.67
A


ATOM
509
C
ILE
A
63
50.247
−10.212
24.169
1.00
20.35
A


ATOM
510
O
ILE
A
63
51.048
−10.538
23.297
1.00
21.37
A


ATOM
511
N
ALA
A
64
50.028
−10.949
25.247
1.00
22.48
A


ATOM
512
CA
ALA
A
64
50.713
−12.222
25.423
1.00
23.35
A


ATOM
513
CB
ALA
A
64
50.373
−12.816
26.785
1.00
22.29
A


ATOM
514
C
ALA
A
64
50.252
−13.158
24.301
1.00
23.03
A


ATOM
515
O
ALA
A
64
51.032
−13.939
23.766
1.00
25.08
A


ATOM
516
N
VAL
A
65
48.976
−13.072
23.948
1.00
23.28
A


ATOM
517
CA
VAL
A
65
48.437
−13.905
22.888
1.00
22.97
A


ATOM
518
CB
VAL
A
65
46.887
−13.840
22.859
1.00
24.28
A


ATOM
519
CG1
VAL
A
65
46.338
−14.722
21.729
1.00
22.40
A


ATOM
520
CG2
VAL
A
65
46.325
−14.296
24.209
1.00
19.61
A


ATOM
521
C
VAL
A
65
49.013
−13.471
21.538
1.00
23.88
A


ATOM
522
O
VAL
A
65
49.313
−14.314
20.692
1.00
22.01
A


ATOM
523
N
LEU
A
66
49.179
−12.164
21.332
1.00
24.00
A


ATOM
524
CA
LEU
A
66
49.747
−11.692
20.064
1.00
24.66
A


ATOM
525
CB
LEU
A
66
49.872
−10.171
20.011
1.00
22.13
A


ATOM
526
CG
LEU
A
66
48.679
−9.228
20.117
1.00
23.81
A


ATOM
527
CD1
LEU
A
66
49.014
−8.001
19.277
1.00
20.24
A


ATOM
528
CD2
LEU
A
66
47.407
−9.866
19.627
1.00
20.49
A


ATOM
529
C
LEU
A
66
51.143
−12.267
19.906
1.00
23.53
A


ATOM
530
O
LEU
A
66
51.548
−12.644
18.813
1.00
22.08
A


ATOM
531
N
LYS
A
67
51.879
−12.303
21.011
1.00
26.17
A


ATOM
532
CA
LYS
A
67
53.237
−12.832
21.019
1.00
28.99
A


ATOM
533
CB
LYS
A
67
53.839
−12.698
22.421
1.00
29.27
A


ATOM
534
CG
LYS
A
67
55.278
−13.174
22.548
1.00
30.64
A


ATOM
535
CD
LYS
A
67
55.779
−13.001
23.976
1.00
32.41
A


ATOM
536
CE
LYS
A
67
57.159
−13.609
24.157
1.00
35.25
A


ATOM
537
NZ
LYS
A
67
58.144
−13.036
23.199
1.00
38.78
A


ATOM
538
C
LYS
A
67
53.200
−14.299
20.598
1.00
29.87
A


ATOM
539
O
LYS
A
67
53.952
−14.719
19.716
1.00
30.35
A


ATOM
540
N
HIS
A
68
52.313
−15.066
21.230
1.00
30.48
A


ATOM
541
CA
HIS
A
68
52.163
−16.483
20.922
1.00
31.95
A


ATOM
542
CB
HIS
A
68
51.051
−17.097
21.775
1.00
34.42
A


ATOM
543
CG
HIS
A
68
50.827
−18.557
21.520
1.00
38.63
A


ATOM
544
CD2
HIS
A
68
49.859
−19.203
20.826
1.00
40.18
A


ATOM
545
ND1
HIS
A
68
51.676
−19.536
21.992
1.00
41.00
A


ATOM
546
CE1
HIS
A
68
51.241
−20.721
21.601
1.00
39.93
A


ATOM
547
NE2
HIS
A
68
50.141
−20.547
20.891
1.00
39.69
A


ATOM
548
C
HIS
A
68
51.828
−16.660
19.448
1.00
31.53
A


ATOM
549
O
HIS
A
68
52.463
−17.447
18.746
1.00
32.07
A


ATOM
550
N
ASN
A
69
50.826
−15.928
18.977
1.00
29.53
A


ATOM
551
CA
ASN
A
69
50.427
−16.024
17.583
1.00
29.99
A


ATOM
552
CB
ASN
A
69
49.180
−15.173
17.332
1.00
30.27
A


ATOM
553
CG
ASN
A
69
47.918
−15.814
17.885
1.00
31.83
A


ATOM
554
OD1
ASN
A
69
47.986
−16.728
18.703
1.00
32.19
A


ATOM
555
ND2
ASN
A
69
46.759
−15.328
17.447
1.00
31.41
A


ATOM
556
C
ASN
A
69
51.552
−15.602
16.638
1.00
30.37
A


ATOM
557
O
ASN
A
69
51.722
−16.186
15.571
1.00
29.41
A


ATOM
558
N
LEU
A
70
52.324
−14.593
17.026
1.00
29.86
A


ATOM
559
CA
LEU
A
70
53.413
−14.131
16.175
1.00
31.35
A


ATOM
560
CB
LEU
A
70
54.039
−12.857
16.751
1.00
28.55
A


ATOM
561
CG
LEU
A
70
55.190
−12.237
15.950
1.00
28.77
A


ATOM
562
CD1
LEU
A
70
54.745
−11.949
14.519
1.00
28.48
A


ATOM
563
CD2
LEU
A
70
55.651
−10.957
16.627
1.00
27.89
A


ATOM
564
C
LEU
A
70
54.479
−15.214
16.009
1.00
31.92
A


ATOM
565
O
LEU
A
70
54.994
−15.422
14.914
1.00
31.72
A


ATOM
566
N
ASN
A
71
54.798
−15.905
17.097
1.00
34.09
A


ATOM
567
CA
ASN
A
71
55.801
−16.968
17.060
1.00
38.27
A


ATOM
568
CB
ASN
A
71
55.884
−17.651
18.427
1.00
39.70
A


ATOM
569
CG
ASN
A
71
56.490
−16.748
19.490
1.00
44.05
A


ATOM
570
OD1
ASN
A
71
56.290
−16.955
20.693
1.00
44.98
A


ATOM
571
ND2
ASN
A
71
57.247
−15.746
19.049
1.00
44.44
A


ATOM
572
C
ASN
A
71
55.484
−18.003
15.983
1.00
38.32
A


ATOM
573
O
ASN
A
71
56.358
−18.417
15.224
1.00
37.91
A


ATOM
574
N
SER
A
72
54.221
−18.407
15.919
1.00
39.49
A


ATOM
575
CA
SER
A
72
53.780
−19.390
14.944
1.00
40.10
A


ATOM
576
CB
SER
A
72
52.341
−19.816
15.256
1.00
41.05
A


ATOM
577
OG
SER
A
72
51.867
−20.763
14.311
1.00
42.44
A


ATOM
578
C
SER
A
72
53.860
−18.838
13.523
1.00
40.66
A


ATOM
579
O
SER
A
72
54.336
−19.516
12.608
1.00
40.90
A


ATOM
580
N
LEU
A
73
53.391
−17.608
13.341
1.00
39.86
A


ATOM
581
CA
LEU
A
73
53.408
−16.973
12.030
1.00
39.32
A


ATOM
582
CB
LEU
A
73
52.676
−15.632
12.082
1.00
38.99
A


ATOM
583
CG
LEU
A
73
51.221
−15.651
11.598
1.00
40.31
A


ATOM
584
CD1
LEU
A
73
50.482
−16.860
12.152
1.00
39.79
A


ATOM
585
CD2
LEU
A
73
50.539
−14.363
12.024
1.00
40.04
A


ATOM
586
C
LEU
A
73
54.816
−16.778
11.492
1.00
38.55
A


ATOM
587
O
LEU
A
73
55.028
−16.806
10.280
1.00
36.83
A


ATOM
588
N
ILE
A
74
55.780
−16.576
12.383
1.00
39.70
A


ATOM
589
CA
ILE
A
74
57.158
−16.402
11.942
1.00
41.87
A


ATOM
590
CB
ILE
A
74
58.104
−16.084
13.123
1.00
41.88
A


ATOM
591
CG2
ILE
A
74
59.552
−16.054
12.640
1.00
41.29
A


ATOM
592
CG1
ILE
A
74
57.729
−14.734
13.738
1.00
41.53
A


ATOM
593
CD1
ILE
A
74
58.519
−14.380
14.990
1.00
40.94
A


ATOM
594
C
ILE
A
74
57.599
−17.699
11.273
1.00
42.04
A


ATOM
595
O
ILE
A
74
58.119
−17.689
10.157
1.00
41.12
A


ATOM
596
N
LYS
A
75
57.364
−18.816
11.954
1.00
43.51
A


ATOM
597
CA
LYS
A
75
57.730
−20.125
11.423
1.00
46.61
A


ATOM
598
CB
LYS
A
75
57.470
−21.217
12.466
1.00
47.84
A


ATOM
599
CG
LYS
A
75
58.096
−20.964
13.828
1.00
50.82
A


ATOM
600
CD
LYS
A
75
57.661
−22.029
14.828
1.00
53.97
A


ATOM
601
CE
LYS
A
75
58.005
−21.646
16.269
1.00
55.95
A


ATOM
602
NZ
LYS
A
75
59.472
−21.572
16.531
1.00
56.31
A


ATOM
603
C
LYS
A
75
56.944
−20.452
10.151
1.00
47.99
A


ATOM
604
O
LYS
A
75
57.530
−20.720
9.106
1.00
48.11
A


ATOM
605
N
ARG
A
76
55.617
−20.419
10.242
1.00
49.31
A


ATOM
606
CA
ARG
A
76
54.763
−20.742
9.103
1.00
50.89
A


ATOM
607
CB
ARG
A
76
53.287
−20.744
9.530
1.00
53.08
A


ATOM
608
CG
ARG
A
76
52.960
−21.847
10.538
1.00
56.83
A


ATOM
609
CD
ARG
A
76
51.478
−22.247
10.574
1.00
58.85
A


ATOM
610
NE
ARG
A
76
50.620
−21.253
11.212
1.00
60.24
A


ATOM
611
CZ
ARG
A
76
49.786
−20.452
10.557
1.00
61.29
A


ATOM
612
NH1
ARG
A
76
49.692
−20.526
9.234
1.00
60.08
A


ATOM
613
NH2
ARG
A
76
49.044
−19.578
11.226
1.00
61.97
A


ATOM
614
C
ARG
A
76
54.947
−19.871
7.864
1.00
50.93
A


ATOM
615
O
ARG
A
76
54.705
−20.324
6.747
1.00
51.19
A


ATOM
616
N
SER
A
77
55.380
−18.630
8.046
1.00
50.61
A


ATOM
617
CA
SER
A
77
55.574
−17.745
6.900
1.00
50.08
A


ATOM
618
CB
SER
A
77
55.262
−16.295
7.282
1.00
50.05
A


ATOM
619
OG
SER
A
77
56.223
−15.787
8.193
1.00
49.23
A


ATOM
620
C
SER
A
77
57.006
−17.827
6.386
1.00
49.56
A


ATOM
621
O
SER
A
77
57.420
−17.015
5.558
1.00
49.40
A


ATOM
622
N
ASN
A
78
57.752
−18.817
6.866
1.00
49.24
A


ATOM
623
CA
ASN
A
78
59.148
−18.982
6.472
1.00
49.14
A


ATOM
624
CB
ASN
A
78
59.256
−19.307
4.976
1.00
48.86
A


ATOM
625
CG
ASN
A
78
60.668
−19.689
4.558
1.00
48.09
A


ATOM
626
OD1
ASN
A
78
61.347
−20.442
5.254
1.00
46.05
A


ATOM
627
ND2
ASN
A
78
61.109
−19.182
3.409
1.00
47.78
A


ATOM
628
C
ASN
A
78
59.857
−17.667
6.803
1.00
49.08
A


ATOM
629
O
ASN
A
78
60.614
−17.114
6.001
1.00
48.39
A


ATOM
630
N
SER
A
79
59.571
−17.177
8.006
1.00
48.58
A


ATOM
631
CA
SER
A
79
60.139
−15.945
8.538
1.00
48.38
A


ATOM
632
CB
SER
A
79
61.549
−16.208
9.071
1.00
48.53
A


ATOM
633
OG
SER
A
79
62.415
−16.612
8.027
1.00
50.05
A


ATOM
634
C
SER
A
79
60.176
−14.768
7.573
1.00
47.13
A


ATOM
635
O
SER
A
79
61.197
−14.098
7.444
1.00
47.66
A


ATOM
636
N
THR
A
80
59.069
−14.516
6.887
1.00
45.82
A


ATOM
637
CA
THR
A
80
59.008
−13.379
5.982
1.00
45.51
A


ATOM
638
CB
THR
A
80
57.814
−13.501
5.016
1.00
47.03
A


ATOM
639
OG1
THR
A
80
56.663
−13.963
5.731
1.00
47.95
A


ATOM
640
CG2
THR
A
80
58.134
−14.487
3.909
1.00
47.59
A


ATOM
641
C
THR
A
80
58.855
−12.147
6.882
1.00
44.25
A


ATOM
642
O
THR
A
80
57.835
−11.976
7.556
1.00
43.69
A


ATOM
643
N
ALA
A
81
59.889
−11.311
6.903
1.00
41.47
A


ATOM
644
CA
ALA
A
81
59.916
−10.119
7.740
1.00
38.59
A


ATOM
645
CB
ALA
A
81
61.363
−9.734
8.039
1.00
38.61
A


ATOM
646
C
ALA
A
81
59.168
−8.915
7.185
1.00
36.89
A


ATOM
647
O
ALA
A
81
58.766
−8.884
6.018
1.00
35.83
A


ATOM
648
N
ALA
A
82
58.993
−7.920
8.050
1.00
34.86
A


ATOM
649
CA
ALA
A
82
58.300
−6.690
7.698
1.00
33.41
A


ATOM
650
CB
ALA
A
82
57.957
−5.912
8.961
1.00
34.17
A


ATOM
651
C
ALA
A
82
59.141
−5.824
6.770
1.00
32.28
A


ATOM
652
O
ALA
A
82
60.372
−5.807
6.859
1.00
28.62
A


ATOM
653
N
THR
A
83
58.457
−5.113
5.878
1.00
31.60
A


ATOM
654
CA
THR
A
83
59.100
−4.217
4.931
1.00
32.87
A


ATOM
655
CB
THR
A
83
58.377
−4.224
3.575
1.00
34.31
A


ATOM
656
OG1
THR
A
83
58.347
−5.562
3.058
1.00
36.90
A


ATOM
657
CG2
THR
A
83
59.098
−3.309
2.578
1.00
34.35
A


ATOM
658
C
THR
A
83
59.041
−2.808
5.500
1.00
32.84
A


ATOM
659
O
THR
A
83
58.029
−2.406
6.067
1.00
33.97
A


ATOM
660
N
ASN
A
84
60.130
−2.062
5.356
1.00
34.76
A


ATOM
661
CA
ASN
A
84
60.188
−0.697
5.858
1.00
34.66
A


ATOM
662
CB
ASN
A
84
61.634
−0.252
6.069
1.00
36.13
A


ATOM
663
CG
ASN
A
84
62.337
−1.045
7.132
1.00
37.22
A


ATOM
664
OD1
ASN
A
84
61.809
−1.241
8.220
1.00
39.34
A


ATOM
665
ND2
ASN
A
84
63.548
−1.497
6.830
1.00
38.89
A


ATOM
666
C
ASN
A
84
59.549
0.267
4.881
1.00
35.51
A


ATOM
667
O
ASN
A
84
59.961
0.343
3.724
1.00
38.89
A


ATOM
668
N
GLU
A
85
58.546
1.004
5.344
1.00
34.17
A


ATOM
669
CA
GLU
A
85
57.890
2.001
4.507
1.00
32.82
A


ATOM
670
CB
GLU
A
85
56.427
2.183
4.921
1.00
36.55
A


ATOM
671
CG
GLU
A
85
55.523
0.993
4.645
1.00
42.74
A


ATOM
672
CD
GLU
A
85
55.271
0.782
3.167
1.00
46.65
A


ATOM
673
OE1
GLU
A
85
54.829
1.741
2.494
1.00
49.22
A


ATOM
674
OE2
GLU
A
85
55.508
−0.345
2.679
1.00
48.74
A


ATOM
675
C
GLU
A
85
58.624
3.328
4.701
1.00
30.10
A


ATOM
676
O
GLU
A
85
59.489
3.453
5.571
1.00
27.29
A


ATOM
677
N
VAL
A
86
58.274
4.308
3.878
1.00
28.67
A


ATOM
678
CA
VAL
A
86
58.849
5.641
3.951
1.00
27.33
A


ATOM
679
CB
VAL
A
86
59.146
6.202
2.539
1.00
27.74
A


ATOM
680
CG1
VAL
A
86
59.688
7.637
2.640
1.00
22.06
A


ATOM
681
CG2
VAL
A
86
60.139
5.289
1.815
1.00
25.30
A


ATOM
682
C
VAL
A
86
57.786
6.519
4.614
1.00
27.98
A


ATOM
683
O
VAL
A
86
56.685
6.671
4.086
1.00
28.76
A


ATOM
684
N
PRO
A
87
58.095
7.098
5.784
1.00
27.39
A


ATOM
685
CD
PRO
A
87
59.268
6.861
6.644
1.00
26.00
A


ATOM
686
CA
PRO
A
87
57.106
7.949
6.458
1.00
28.38
A


ATOM
687
CB
PRO
A
87
57.611
7.989
7.899
1.00
26.97
A


ATOM
688
CG
PRO
A
87
59.099
7.915
7.727
1.00
27.97
A


ATOM
689
C
PRO
A
87
56.963
9.341
5.848
1.00
30.15
A


ATOM
690
O
PRO
A
87
57.902
9.871
5.245
1.00
31.62
A


ATOM
691
N
GLU
A
88
55.778
9.922
6.004
1.00
29.70
A


ATOM
692
CA
GLU
A
88
55.489
11.252
5.481
1.00
29.65
A


ATOM
693
CB
GLU
A
88
54.173
11.229
4.699
1.00
32.09
A


ATOM
694
CG
GLU
A
88
54.038
12.330
3.655
1.00
38.40
A


ATOM
695
CD
GLU
A
88
52.790
12.172
2.792
1.00
41.07
A


ATOM
696
OE1
GLU
A
88
51.675
12.411
3.303
1.00
42.35
A


ATOM
697
OE2
GLU
A
88
52.925
11.800
1.604
1.00
43.46
A


ATOM
698
C
GLU
A
88
55.385
12.191
6.680
1.00
27.98
A


ATOM
699
O
GLU
A
88
54.588
11.954
7.597
1.00
26.16
A


ATOM
700
N
VAL
A
89
56.187
13.253
6.672
1.00
23.90
A


ATOM
701
CA
VAL
A
89
56.201
14.194
7.788
1.00
21.62
A


ATOM
702
CB
VAL
A
89
57.637
14.358
8.333
1.00
18.36
A


ATOM
703
CG1
VAL
A
89
57.639
15.295
9.534
1.00
17.11
A


ATOM
704
CG2
VAL
A
89
58.204
12.990
8.719
1.00
16.77
A


ATOM
705
C
VAL
A
89
55.626
15.575
7.483
1.00
21.60
A


ATOM
706
O
VAL
A
89
55.859
16.143
6.420
1.00
21.72
A


ATOM
707
N
THR
A
90
54.886
16.115
8.444
1.00
21.28
A


ATOM
708
CA
THR
A
90
54.269
17.425
8.301
1.00
20.62
A


ATOM
709
CB
THR
A
90
52.813
17.303
7.823
1.00
21.90
A


ATOM
710
OG1
THR
A
90
52.770
16.537
6.613
1.00
26.43
A


ATOM
711
CG2
THR
A
90
52.220
18.678
7.558
1.00
23.70
A


ATOM
712
C
THR
A
90
54.264
18.153
9.639
1.00
21.08
A


ATOM
713
O
THR
A
90
53.887
17.578
10.667
1.00
20.41
A


ATOM
714
N
VAL
A
91
54.670
19.423
9.618
1.00
19.24
A


ATOM
715
CA
VAL
A
91
54.712
20.243
10.822
1.00
19.55
A


ATOM
716
CB
VAL
A
91
56.149
20.739
11.102
1.00
19.97
A


ATOM
717
CG1
VAL
A
91
56.167
21.629
12.338
1.00
16.82
A


ATOM
718
CG2
VAL
A
91
57.072
19.547
11.280
1.00
17.43
A


ATOM
719
C
VAL
A
91
53.789
21.452
10.703
1.00
19.10
A


ATOM
720
O
VAL
A
91
53.735
22.108
9.666
1.00
20.59
A


ATOM
721
N
PHE
A
92
53.059
21.739
11.772
1.00
18.65
A


ATOM
722
CA
PHE
A
92
52.146
22.870
11.785
1.00
19.10
A


ATOM
723
CB
PHE
A
92
50.853
22.516
11.030
1.00
18.89
A


ATOM
724
CG
PHE
A
92
50.176
21.264
11.525
1.00
16.16
A


ATOM
725
CD1
PHE
A
92
49.165
21.331
12.480
1.00
16.77
A


ATOM
726
CD2
PHE
A
92
50.561
20.017
11.047
1.00
16.62
A


ATOM
727
CE1
PHE
A
92
48.543
20.168
12.955
1.00
18.06
A


ATOM
728
CE2
PHE
A
92
49.954
18.848
11.511
1.00
18.17
A


ATOM
729
CZ
PHE
A
92
48.936
18.922
12.471
1.00
17.05
A


ATOM
730
C
PHE
A
92
51.844
23.236
13.229
1.00
19.48
A


ATOM
731
O
PHE
A
92
52.055
22.430
14.134
1.00
19.64
A


ATOM
732
N
SER
A
93
51.365
24.453
13.445
1.00
18.69
A


ATOM
733
CA
SER
A
93
51.052
24.896
14.792
1.00
19.26
A


ATOM
734
CB
SER
A
93
51.275
26.408
14.921
1.00
17.24
A


ATOM
735
OG
SER
A
93
50.435
27.132
14.043
1.00
20.17
A


ATOM
736
C
SER
A
93
49.618
24.554
15.172
1.00
19.04
A


ATOM
737
O
SER
A
93
48.748
24.417
14.316
1.00
17.44
A


ATOM
738
N
LYS
A
94
49.390
24.418
16.472
1.00
20.26
A


ATOM
739
CA
LYS
A
94
48.077
24.108
17.010
1.00
21.70
A


ATOM
740
CB
LYS
A
94
48.227
23.670
18.464
1.00
22.45
A


ATOM
741
CG
LYS
A
94
46.938
23.273
19.139
1.00
24.42
A


ATOM
742
CD
LYS
A
94
47.189
22.867
20.587
1.00
25.48
A


ATOM
743
CE
LYS
A
94
45.881
22.548
21.297
1.00
25.73
A


ATOM
744
NZ
LYS
A
94
45.122
21.533
20.517
1.00
26.34
A


ATOM
745
C
LYS
A
94
47.169
25.340
16.921
1.00
23.44
A


ATOM
746
O
LYS
A
94
45.984
25.235
16.598
1.00
20.95
A


ATOM
747
N
SER
A
95
47.742
26.505
17.212
1.00
24.82
A


ATOM
748
CA
SER
A
95
47.013
27.769
17.172
1.00
27.69
A


ATOM
749
CB
SER
A
95
46.969
28.408
18.565
1.00
26.33
A


ATOM
750
OG
SER
A
95
46.202
27.635
19.468
1.00
32.56
A


ATOM
751
C
SER
A
95
47.688
28.747
16.219
1.00
27.36
A


ATOM
752
O
SER
A
95
48.824
28.529
15.797
1.00
27.94
A


ATOM
753
N
PRO
A
96
46.985
29.830
15.849
1.00
27.27
A


ATOM
754
CD
PRO
A
96
45.611
30.232
16.193
1.00
28.85
A


ATOM
755
CA
PRO
A
96
47.606
30.801
14.946
1.00
26.90
A


ATOM
756
CB
PRO
A
96
46.471
31.788
14.663
1.00
28.13
A


ATOM
757
CG
PRO
A
96
45.634
31.719
15.907
1.00
28.36
A


ATOM
758
C
PRO
A
96
48.786
31.421
15.700
1.00
24.92
A


ATOM
759
O
PRO
A
96
48.757
31.556
16.925
1.00
24.65
A


ATOM
760
N
VAL
A
97
49.828
31.786
14.973
1.00
24.24
A


ATOM
761
CA
VAL
A
97
51.016
32.332
15.601
1.00
25.15
A


ATOM
762
CB
VAL
A
97
52.261
32.087
14.715
1.00
26.78
A


ATOM
763
CG1
VAL
A
97
53.531
32.372
15.508
1.00
26.15
A


ATOM
764
CG2
VAL
A
97
52.255
30.659
14.198
1.00
26.15
A


ATOM
765
C
VAL
A
97
50.935
33.820
15.920
1.00
25.62
A


ATOM
766
O
VAL
A
97
50.624
34.638
15.054
1.00
25.01
A


ATOM
767
N
THR
A
98
51.207
34.157
17.175
1.00
24.46
A


ATOM
768
CA
THR
A
98
51.212
35.542
17.627
1.00
25.36
A


ATOM
769
CB
THR
A
98
49.835
35.941
18.283
1.00
25.29
A


ATOM
770
OG1
THR
A
98
50.030
37.008
19.217
1.00
30.50
A


ATOM
771
CG2
THR
A
98
49.196
34.771
18.985
1.00
29.80
A


ATOM
772
C
THR
A
98
52.382
35.678
18.605
1.00
24.87
A


ATOM
773
O
THR
A
98
52.499
34.902
19.554
1.00
23.01
A


ATOM
774
N
LEU
A
99
53.273
36.634
18.344
1.00
25.94
A


ATOM
775
CA
LEU
A
99
54.445
36.843
19.198
1.00
28.02
A


ATOM
776
CB
LEU
A
99
55.194
38.114
18.797
1.00
31.12
A


ATOM
777
CG
LEU
A
99
55.950
38.211
17.469
1.00
35.44
A


ATOM
778
CD1
LEU
A
99
56.650
39.577
17.416
1.00
35.45
A


ATOM
779
CD2
LEU
A
99
56.970
37.087
17.341
1.00
35.62
A


ATOM
780
C
LEU
A
99
54.135
36.932
20.689
1.00
27.10
A


ATOM
781
O
LEU
A
99
53.201
37.616
21.097
1.00
25.34
A


ATOM
782
N
GLY
A
100
54.935
36.233
21.492
1.00
26.71
A


ATOM
783
CA
GLY
A
100
54.762
36.253
22.935
1.00
26.48
A


ATOM
784
C
GLY
A
100
53.635
35.398
23.479
1.00
26.32
A


ATOM
785
O
GLY
A
100
53.428
35.323
24.695
1.00
25.37
A


ATOM
786
N
GLN
A
101
52.913
34.734
22.585
1.00
25.16
A


ATOM
787
CA
GLN
A
101
51.796
33.896
22.999
1.00
25.74
A


ATOM
788
CB
GLN
A
101
50.573
34.219
22.143
1.00
28.06
A


ATOM
789
CG
GLN
A
101
49.258
33.911
22.814
1.00
30.50
A


ATOM
790
CD
GLN
A
101
49.123
34.599
24.162
1.00
32.88
A


ATOM
791
OE1
GLN
A
101
48.953
35.820
24.251
1.00
30.83
A


ATOM
792
NE2
GLN
A
101
49.202
33.813
25.221
1.00
33.04
A


ATOM
793
C
GLN
A
101
52.117
32.409
22.901
1.00
24.01
A


ATOM
794
O
GLN
A
101
52.280
31.881
21.807
1.00
24.25
A


ATOM
795
N
PRO
A
102
52.199
31.715
24.051
1.00
22.08
A


ATOM
796
CD
PRO
A
102
51.959
32.244
25.410
1.00
22.41
A


ATOM
797
CA
PRO
A
102
52.500
30.278
24.096
1.00
21.37
A


ATOM
798
CB
PRO
A
102
52.136
29.898
25.526
1.00
21.61
A


ATOM
799
CG
PRO
A
102
52.521
31.147
26.297
1.00
21.90
A


ATOM
800
C
PRO
A
102
51.706
29.480
23.068
1.00
21.30
A


ATOM
801
O
PRO
A
102
50.496
29.644
22.947
1.00
21.93
A


ATOM
802
N
ASN
A
103
52.396
28.618
22.327
1.00
18.86
A


ATOM
803
CA
ASN
A
103
51.749
27.802
21.305
1.00
17.69
A


ATOM
804
CB
ASN
A
103
52.040
28.379
19.913
1.00
17.99
A


ATOM
805
CG
ASN
A
103
50.899
28.162
18.929
1.00
18.28
A


ATOM
806
OD1
ASN
A
103
50.348
27.060
18.808
1.00
17.82
A


ATOM
807
ND2
ASN
A
103
50.549
29.223
18.204
1.00
17.71
A


ATOM
808
C
ASN
A
103
52.281
26.370
21.385
1.00
15.57
A


ATOM
809
O
ASN
A
103
53.000
26.012
22.310
1.00
14.67
A


ATOM
810
N
ILE
A
104
51.918
25.565
20.397
1.00
15.80
A


ATOM
811
CA
ILE
A
104
52.335
24.177
20.328
1.00
13.66
A


ATOM
812
CB
ILE
A
104
51.255
23.235
20.888
1.00
15.40
A


ATOM
813
CG2
ILE
A
104
51.589
21.792
20.539
1.00
13.82
A


ATOM
814
CG1
ILE
A
104
51.132
23.421
22.400
1.00
17.40
A


ATOM
815
CD1
ILE
A
104
50.129
22.494
23.047
1.00
18.65
A


ATOM
816
C
ILE
A
104
52.588
23.775
18.896
1.00
14.36
A


ATOM
817
O
ILE
A
104
51.716
23.924
18.052
1.00
16.86
A


ATOM
818
N
LEU
A
105
53.785
23.272
18.616
1.00
15.67
A


ATOM
819
CA
LEU
A
105
54.090
22.822
17.272
1.00
15.52
A


ATOM
820
CB
LEU
A
105
55.568
22.978
16.940
1.00
15.73
A


ATOM
821
CG
LEU
A
105
56.058
24.391
16.649
1.00
20.75
A


ATOM
822
CD1
LEU
A
105
57.400
24.298
15.919
1.00
20.19
A


ATOM
823
CD2
LEU
A
105
55.030
25.141
15.791
1.00
21.31
A


ATOM
824
C
LEU
A
105
53.709
21.362
17.202
1.00
15.97
A


ATOM
825
O
LEU
A
105
53.968
20.589
18.133
1.00
14.11
A


ATOM
826
N
ILE
A
106
53.078
20.993
16.099
1.00
14.18
A


ATOM
827
CA
ILE
A
106
52.643
19.630
15.903
1.00
15.40
A


ATOM
828
CB
ILE
A
106
51.122
19.576
15.636
1.00
15.11
A


ATOM
829
CG2
ILE
A
106
50.661
18.135
15.592
1.00
12.46
A


ATOM
830
CG1
ILE
A
106
50.380
20.354
16.734
1.00
15.51
A


ATOM
831
CD1
ILE
A
106
48.862
20.413
16.565
1.00
12.83
A


ATOM
832
C
ILE
A
106
53.381
19.011
14.725
1.00
16.48
A


ATOM
833
O
ILE
A
106
53.484
19.607
13.651
1.00
17.37
A


ATOM
834
N
CYS
A
107
53.900
17.811
14.944
1.00
17.86
A


ATOM
835
CA
CYS
A
107
54.621
17.083
13.917
1.00
18.32
A


ATOM
836
C
CYS
A
107
53.886
15.776
13.663
1.00
18.29
A


ATOM
837
O
CYS
A
107
53.846
14.909
14.533
1.00
18.13
A


ATOM
838
CB
CYS
A
107
56.041
16.792
14.382
1.00
19.33
A


ATOM
839
SG
CYS
A
107
57.029
15.889
13.158
1.00
25.82
A


ATOM
840
N
LEU
A
108
53.304
15.649
12.472
1.00
17.89
A


ATOM
841
CA
LEU
A
108
52.556
14.456
12.088
1.00
18.82
A


ATOM
842
CB
LEU
A
108
51.330
14.850
11.252
1.00
20.17
A


ATOM
843
CG
LEU
A
108
50.129
13.900
11.053
1.00
21.48
A


ATOM
844
CD1
LEU
A
108
49.623
14.049
9.624
1.00
20.62
A


ATOM
845
CD2
LEU
A
108
50.493
12.458
11.316
1.00
18.40
A


ATOM
846
C
LEU
A
108
53.445
13.538
11.252
1.00
19.49
A


ATOM
847
O
LEU
A
108
53.841
13.892
10.144
1.00
20.39
A


ATOM
848
N
VAL
A
109
53.760
12.368
11.789
1.00
18.45
A


ATOM
849
CA
VAL
A
109
54.586
11.398
11.087
1.00
19.04
A


ATOM
850
CB
VAL
A
109
55.665
10.805
12.042
1.00
18.71
A


ATOM
851
CG1
VAL
A
109
56.626
9.923
11.279
1.00
15.16
A


ATOM
852
CG2
VAL
A
109
56.431
11.949
12.729
1.00
17.68
A


ATOM
853
C
VAL
A
109
53.611
10.322
10.606
1.00
20.50
A


ATOM
854
O
VAL
A
109
53.115
9.516
11.393
1.00
21.55
A


ATOM
855
N
ASP
A
110
53.326
10.337
9.308
1.00
21.50
A


ATOM
856
CA
ASP
A
110
52.376
9.407
8.700
1.00
21.95
A


ATOM
857
CB
ASP
A
110
51.493
10.165
7.701
1.00
22.25
A


ATOM
858
CG
ASP
A
110
50.084
9.612
7.622
1.00
24.20
A


ATOM
859
OD1
ASP
A
110
49.874
8.435
7.989
1.00
23.87
A


ATOM
860
OD2
ASP
A
110
49.182
10.356
7.182
1.00
25.94
A


ATOM
861
C
ASP
A
110
53.059
8.240
7.985
1.00
21.53
A


ATOM
862
O
ASP
A
110
54.273
8.254
7.782
1.00
18.80
A


ATOM
863
N
ASN
A
111
52.254
7.245
7.603
1.00
23.78
A


ATOM
864
CA
ASN
A
111
52.706
6.037
6.900
1.00
23.32
A


ATOM
865
CB
ASN
A
111
53.046
6.360
5.437
1.00
24.67
A


ATOM
866
CG
ASN
A
111
53.181
5.102
4.575
1.00
31.76
A


ATOM
867
OD1
ASN
A
111
52.291
4.240
4.567
1.00
31.05
A


ATOM
868
ND2
ASN
A
111
54.292
4.994
3.842
1.00
29.09
A


ATOM
869
C
ASN
A
111
53.905
5.389
7.587
1.00
23.68
A


ATOM
870
O
ASN
A
111
54.953
5.156
6.976
1.00
22.88
A


ATOM
871
N
ILE
A
112
53.738
5.090
8.868
1.00
22.97
A


ATOM
872
CA
ILE
A
112
54.797
4.473
9.646
1.00
20.73
A


ATOM
873
CB
ILE
A
112
54.791
4.967
11.108
1.00
20.13
A


ATOM
874
CG2
ILE
A
112
55.979
4.363
11.864
1.00
15.53
A


ATOM
875
CG1
ILE
A
112
54.833
6.495
11.158
1.00
19.14
A


ATOM
876
CD1
ILE
A
112
54.671
7.058
12.575
1.00
20.42
A


ATOM
877
C
ILE
A
112
54.658
2.960
9.699
1.00
22.54
A


ATOM
878
O
ILE
A
112
53.605
2.436
10.054
1.00
22.65
A


ATOM
879
N
PHE
A
113
55.732
2.266
9.343
1.00
21.37
A


ATOM
880
CA
PHE
A
113
55.769
0.819
9.412
1.00
21.74
A


ATOM
881
CB
PHE
A
113
54.742
0.167
8.483
1.00
21.64
A


ATOM
882
CG
PHE
A
113
54.451
−1.252
8.850
1.00
21.22
A


ATOM
883
CD1
PHE
A
113
53.528
−1.543
9.856
1.00
20.25
A


ATOM
884
CD2
PHE
A
113
55.183
−2.296
8.285
1.00
20.76
A


ATOM
885
CE1
PHE
A
113
53.341
−2.848
10.302
1.00
19.85
A


ATOM
886
CE2
PHE
A
113
55.008
−3.607
8.721
1.00
20.75
A


ATOM
887
CZ
PHE
A
113
54.086
−3.887
9.735
1.00
21.24
A


ATOM
888
C
PHE
A
113
57.157
0.329
9.042
1.00
21.21
A


ATOM
889
O
PHE
A
113
57.700
0.719
8.011
1.00
19.97
A


ATOM
890
N
PRO
A
114
57.765
−0.509
9.893
1.00
22.22
A


ATOM
891
CD
PRO
A
114
59.118
−1.018
9.614
1.00
22.88
A


ATOM
892
CA
PRO
A
114
57.263
−1.040
11.170
1.00
23.38
A


ATOM
893
CB
PRO
A
114
58.340
−2.045
11.571
1.00
23.68
A


ATOM
894
CG
PRO
A
114
59.592
−1.435
10.984
1.00
23.26
A


ATOM
895
C
PRO
A
114
57.078
0.059
12.221
1.00
24.33
A


ATOM
896
O
PRO
A
114
57.571
1.174
12.054
1.00
24.35
A


ATOM
897
N
PRO
A
115
56.363
−0.247
13.319
1.00
24.59
A


ATOM
898
CD
PRO
A
115
55.579
−1.472
13.567
1.00
22.60
A


ATOM
899
CA
PRO
A
115
56.135
0.751
14.372
1.00
23.79
A


ATOM
900
CB
PRO
A
115
54.923
0.194
15.107
1.00
23.96
A


ATOM
901
CG
PRO
A
115
55.129
−1.291
14.998
1.00
23.45
A


ATOM
902
C
PRO
A
115
57.337
0.996
15.289
1.00
24.97
A


ATOM
903
O
PRO
A
115
57.322
0.670
16.482
1.00
23.11
A


ATOM
904
N
VAL
A
116
58.380
1.573
14.705
1.00
24.77
A


ATOM
905
CA
VAL
A
116
59.607
1.902
15.423
1.00
24.05
A


ATOM
906
CB
VAL
A
116
60.733
0.881
15.135
1.00
26.45
A


ATOM
907
CG1
VAL
A
116
61.977
1.250
15.933
1.00
24.89
A


ATOM
908
CG2
VAL
A
116
60.267
−0.539
15.470
1.00
26.43
A


ATOM
909
C
VAL
A
116
60.043
3.254
14.875
1.00
24.47
A


ATOM
910
O
VAL
A
116
60.340
3.381
13.684
1.00
23.94
A


ATOM
911
N
VAL
A
117
60.088
4.269
15.728
1.00
22.43
A


ATOM
912
CA
VAL
A
117
60.472
5.577
15.239
1.00
22.18
A


ATOM
913
CB
VAL
A
117
59.247
6.277
14.565
1.00
21.24
A


ATOM
914
CG1
VAL
A
117
58.276
6.807
15.631
1.00
17.87
A


ATOM
915
CG2
VAL
A
117
59.710
7.387
13.653
1.00
19.98
A


ATOM
916
C
VAL
A
117
61.035
6.484
16.326
1.00
23.40
A


ATOM
917
O
VAL
A
117
60.743
6.323
17.512
1.00
22.77
A


ATOM
918
N
ASN
A
118
61.868
7.427
15.909
1.00
24.87
A


ATOM
919
CA
ASN
A
118
62.434
8.398
16.833
1.00
25.96
A


ATOM
920
CB
ASN
A
118
63.970
8.341
16.858
1.00
29.36
A


ATOM
921
CG
ASN
A
118
64.506
7.213
17.728
1.00
31.24
A


ATOM
922
OD1
ASN
A
118
63.885
6.833
18.722
1.00
34.20
A


ATOM
923
ND2
ASN
A
118
65.679
6.694
17.374
1.00
34.04
A


ATOM
924
C
ASN
A
118
61.989
9.746
16.312
1.00
24.87
A


ATOM
925
O
ASN
A
118
62.298
10.112
15.177
1.00
26.17
A


ATOM
926
N
ILE
A
119
61.229
10.468
17.122
1.00
23.82
A


ATOM
927
CA
ILE
A
119
60.774
11.793
16.727
1.00
23.07
A


ATOM
928
CB
ILE
A
119
59.231
11.892
16.711
1.00
22.65
A


ATOM
929
CG2
ILE
A
119
58.797
13.197
16.051
1.00
18.01
A


ATOM
930
CG1
ILE
A
119
58.642
10.716
15.936
1.00
21.02
A


ATOM
931
CD1
ILE
A
119
57.135
10.714
15.921
1.00
21.88
A


ATOM
932
C
ILE
A
119
61.323
12.771
17.754
1.00
22.76
A


ATOM
933
O
ILE
A
119
61.013
12.680
18.940
1.00
22.92
A


ATOM
934
N
THR
A
120
62.162
13.691
17.303
1.00
23.11
A


ATOM
935
CA
THR
A
120
62.737
14.673
18.205
1.00
23.65
A


ATOM
936
CB
THR
A
120
64.216
14.363
18.495
1.00
25.23
A


ATOM
937
OG1
THR
A
120
64.921
14.199
17.258
1.00
26.55
A


ATOM
938
CG2
THR
A
120
64.335
13.081
19.331
1.00
23.93
A


ATOM
939
C
THR
A
120
62.622
16.064
17.616
1.00
23.20
A


ATOM
940
O
THR
A
120
62.437
16.232
16.412
1.00
23.15
A


ATOM
941
N
TRP
A
121
62.725
17.069
18.470
1.00
22.54
A


ATOM
942
CA
TRP
A
121
62.619
18.432
17.998
1.00
21.37
A


ATOM
943
CB
TRP
A
121
61.563
19.196
18.791
1.00
19.43
A


ATOM
944
CG
TRP
A
121
60.173
18.679
18.616
1.00
18.76
A


ATOM
945
CD2
TRP
A
121
59.191
19.179
17.703
1.00
19.96
A


ATOM
946
CE2
TRP
A
121
58.002
18.454
17.931
1.00
18.06
A


ATOM
947
CE3
TRP
A
121
59.200
20.178
16.715
1.00
16.07
A


ATOM
948
CD1
TRP
A
121
59.567
17.694
19.330
1.00
18.18
A


ATOM
949
NE1
TRP
A
121
58.261
17.553
18.929
1.00
19.21
A


ATOM
950
CZ2
TRP
A
121
56.827
18.694
17.210
1.00
16.20
A


ATOM
951
CZ3
TRP
A
121
58.036
20.419
16.000
1.00
16.43
A


ATOM
952
CH2
TRP
A
121
56.864
19.679
16.252
1.00
17.37
A


ATOM
953
C
TRP
A
121
63.927
19.178
18.097
1.00
22.88
A


ATOM
954
O
TRP
A
121
64.743
18.937
18.992
1.00
22.75
A


ATOM
955
N
LEU
A
122
64.109
20.100
17.164
1.00
23.24
A


ATOM
956
CA
LEU
A
122
65.291
20.930
17.136
1.00
22.66
A


ATOM
957
CB
LEU
A
122
66.094
20.699
15.850
1.00
23.05
A


ATOM
958
CG
LEU
A
122
66.638
19.293
15.563
1.00
22.23
A


ATOM
959
CD1
LEU
A
122
67.404
19.326
14.253
1.00
20.93
A


ATOM
960
CD2
LEU
A
122
67.542
18.830
16.700
1.00
20.21
A


ATOM
961
C
LEU
A
122
64.837
22.376
17.186
1.00
23.52
A


ATOM
962
O
LEU
A
122
63.830
22.752
16.572
1.00
21.74
A


ATOM
963
N
SER
A
123
65.579
23.174
17.945
1.00
23.69
A


ATOM
964
CA
SER
A
123
65.330
24.597
18.063
1.00
24.10
A


ATOM
965
CB
SER
A
123
64.998
24.983
19.504
1.00
25.22
A


ATOM
966
OG
SER
A
123
64.735
26.373
19.591
1.00
25.55
A


ATOM
967
C
SER
A
123
66.664
25.200
17.650
1.00
24.79
A


ATOM
968
O
SER
A
123
67.670
25.014
18.335
1.00
23.07
A


ATOM
969
N
ASN
A
124
66.666
25.903
16.521
1.00
25.02
A


ATOM
970
CA
ASN
A
124
67.880
26.513
15.986
1.00
25.63
A


ATOM
971
CB
ASN
A
124
68.351
27.676
16.868
1.00
24.46
A


ATOM
972
CG
ASN
A
124
67.376
28.839
16.873
1.00
25.33
A


ATOM
973
OD1
ASN
A
124
66.636
29.056
15.907
1.00
26.04
A


ATOM
974
ND2
ASN
A
124
67.381
29.606
17.956
1.00
21.77
A


ATOM
975
C
ASN
A
124
69.006
25.487
15.838
1.00
26.53
A


ATOM
976
O
ASN
A
124
70.132
25.706
16.301
1.00
26.36
A


ATOM
977
N
GLY
A
125
68.684
24.361
15.205
1.00
24.78
A


ATOM
978
CA
GLY
A
125
69.669
23.326
14.964
1.00
26.09
A


ATOM
979
C
GLY
A
125
70.030
22.377
16.089
1.00
27.35
A


ATOM
980
O
GLY
A
125
70.728
21.395
15.846
1.00
28.21
A


ATOM
981
N
HIS
A
126
69.566
22.645
17.307
1.00
28.65
A


ATOM
982
CA
HIS
A
126
69.889
21.774
18.430
1.00
30.12
A


ATOM
983
CB
HIS
A
126
70.816
22.507
19.408
1.00
32.68
A


ATOM
984
CG
HIS
A
126
70.226
23.750
19.996
1.00
35.25
A


ATOM
985
CD2
HIS
A
126
70.296
25.044
19.601
1.00
36.90
A


ATOM
986
ND1
HIS
A
126
69.475
23.743
21.151
1.00
35.93
A


ATOM
987
CE1
HIS
A
126
69.110
24.979
21.445
1.00
36.88
A


ATOM
988
NE2
HIS
A
126
69.595
25.788
20.520
1.00
36.73
A


ATOM
989
C
HIS
A
126
68.661
21.220
19.149
1.00
30.87
A


ATOM
990
O
HIS
A
126
67.634
21.889
19.270
1.00
31.49
A


ATOM
991
N
SER
A
127
68.789
19.990
19.635
1.00
30.93
A


ATOM
992
CA
SER
A
127
67.697
19.286
20.302
1.00
33.08
A


ATOM
993
CB
SER
A
127
68.165
17.889
20.714
1.00
33.91
A


ATOM
994
OG
SER
A
127
69.231
17.979
21.645
1.00
38.34
A


ATOM
995
C
SER
A
127
67.050
19.971
21.501
1.00
32.98
A


ATOM
996
O
SER
A
127
67.708
20.654
22.288
1.00
34.83
A


ATOM
997
N
VAL
A
128
65.743
19.770
21.624
1.00
32.42
A


ATOM
998
CA
VAL
A
128
64.960
20.325
22.716
1.00
31.29
A


ATOM
999
CB
VAL
A
128
63.645
20.921
22.202
1.00
30.48
A


ATOM
1000
CG1
VAL
A
128
62.856
21.520
23.358
1.00
27.06
A


ATOM
1001
CG2
VAL
A
128
63.937
21.970
21.142
1.00
28.52
A


ATOM
1002
C
VAL
A
128
64.645
19.183
23.669
1.00
32.28
A


ATOM
1003
O
VAL
A
128
64.275
18.093
23.237
1.00
32.80
A


ATOM
1004
N
THR
A
129
64.786
19.437
24.965
1.00
33.30
A


ATOM
1005
CA
THR
A
129
64.546
18.411
25.981
1.00
33.70
A


ATOM
1006
CB
THR
A
129
65.740
18.344
26.966
1.00
34.52
A


ATOM
1007
OG1
THR
A
129
65.969
19.643
27.528
1.00
38.18
A


ATOM
1008
CG2
THR
A
129
67.006
17.898
26.245
1.00
34.60
A


ATOM
1009
C
THR
A
129
63.257
18.591
26.791
1.00
32.08
A


ATOM
1010
O
THR
A
129
62.645
17.615
27.220
1.00
34.04
A


ATOM
1011
N
GLU
A
130
62.843
19.835
26.993
1.00
28.85
A


ATOM
1012
CA
GLU
A
130
61.639
20.119
27.762
1.00
26.09
A


ATOM
1013
CB
GLU
A
130
61.926
21.236
28.770
1.00
28.58
A


ATOM
1014
CG
GLU
A
130
62.962
20.894
29.822
1.00
32.87
A


ATOM
1015
CD
GLU
A
130
62.592
19.654
30.609
1.00
35.34
A


ATOM
1016
OE1
GLU
A
130
61.392
19.475
30.907
1.00
37.85
A


ATOM
1017
OE2
GLU
A
130
63.501
18.865
30.941
1.00
36.29
A


ATOM
1018
C
GLU
A
130
60.451
20.534
26.893
1.00
23.53
A


ATOM
1019
O
GLU
A
130
60.629
21.166
25.859
1.00
19.76
A


ATOM
1020
N
GLY
A
131
59.243
20.188
27.334
1.00
21.13
A


ATOM
1021
CA
GLY
A
131
58.046
20.563
26.601
1.00
20.14
A


ATOM
1022
C
GLY
A
131
57.693
19.684
25.421
1.00
20.64
A


ATOM
1023
O
GLY
A
131
56.989
20.109
24.507
1.00
20.11
A


ATOM
1024
N
VAL
A
132
58.164
18.447
25.444
1.00
18.28
A


ATOM
1025
CA
VAL
A
132
57.899
17.527
24.355
1.00
20.08
A


ATOM
1026
CB
VAL
A
132
59.230
16.985
23.767
1.00
20.35
A


ATOM
1027
CG1
VAL
A
132
58.946
15.874
22.772
1.00
22.11
A


ATOM
1028
CG2
VAL
A
132
60.006
18.114
23.093
1.00
20.17
A


ATOM
1029
C
VAL
A
132
57.027
16.340
24.786
1.00
20.06
A


ATOM
1030
O
VAL
A
132
57.194
15.794
25.875
1.00
18.65
A


ATOM
1031
N
SER
A
133
56.094
15.948
23.925
1.00
17.90
A


ATOM
1032
CA
SER
A
133
55.238
14.802
24.215
1.00
18.16
A


ATOM
1033
CB
SER
A
133
54.045
15.206
25.094
1.00
18.24
A


ATOM
1034
OG
SER
A
133
53.202
16.143
24.440
1.00
24.24
A


ATOM
1035
C
SER
A
133
54.738
14.200
22.914
1.00
16.52
A


ATOM
1036
O
SER
A
133
54.876
14.794
21.843
1.00
16.18
A


ATOM
1037
N
GLU
A
134
54.166
13.009
22.996
1.00
17.45
A


ATOM
1038
CA
GLU
A
134
53.653
12.369
21.800
1.00
18.50
A


ATOM
1039
CB
GLU
A
134
54.797
11.661
21.050
1.00
22.31
A


ATOM
1040
CG
GLU
A
134
55.475
10.513
21.801
1.00
24.62
A


ATOM
1041
CD
GLU
A
134
56.610
9.859
20.992
1.00
28.65
A


ATOM
1042
OE1
GLU
A
134
56.932
8.680
21.254
1.00
29.58
A


ATOM
1043
OE2
GLU
A
134
57.188
10.521
20.099
1.00
27.96
A


ATOM
1044
C
GLU
A
134
52.523
11.389
22.087
1.00
18.44
A


ATOM
1045
O
GLU
A
134
52.279
11.003
23.234
1.00
17.30
A


ATOM
1046
N
THR
A
135
51.824
11.008
21.027
1.00
16.71
A


ATOM
1047
CA
THR
A
135
50.733
10.059
21.119
1.00
15.49
A


ATOM
1048
CB
THR
A
135
49.738
10.246
19.967
1.00
16.16
A


ATOM
1049
OG1
THR
A
135
50.369
9.867
18.731
1.00
16.02
A


ATOM
1050
CG2
THR
A
135
49.280
11.697
19.879
1.00
14.19
A


ATOM
1051
C
THR
A
135
51.346
8.682
20.946
1.00
17.19
A


ATOM
1052
O
THR
A
135
52.551
8.554
20.733
1.00
17.26
A


ATOM
1053
N
SER
A
136
50.519
7.650
21.047
1.00
17.53
A


ATOM
1054
CA
SER
A
136
51.001
6.297
20.818
1.00
15.92
A


ATOM
1055
CB
SER
A
136
50.035
5.266
21.416
1.00
16.85
A


ATOM
1056
OG
SER
A
136
49.756
5.532
22.781
1.00
18.22
A


ATOM
1057
C
SER
A
136
50.967
6.187
19.294
1.00
15.84
A


ATOM
1058
O
SER
A
136
50.715
7.169
18.596
1.00
17.25
A


ATOM
1059
N
PHE
A
137
51.236
5.003
18.767
1.00
17.08
A


ATOM
1060
CA
PHE
A
137
51.155
4.806
17.333
1.00
15.67
A


ATOM
1061
CB
PHE
A
137
51.874
3.519
16.936
1.00
13.47
A


ATOM
1062
CG
PHE
A
137
53.363
3.628
16.951
1.00
14.48
A


ATOM
1063
CD1
PHE
A
137
54.037
4.255
15.907
1.00
15.82
A


ATOM
1064
CD2
PHE
A
137
54.100
3.112
18.010
1.00
15.21
A


ATOM
1065
CE1
PHE
A
137
55.427
4.367
15.918
1.00
15.72
A


ATOM
1066
CE2
PHE
A
137
55.490
3.220
18.031
1.00
15.14
A


ATOM
1067
CZ
PHE
A
137
56.152
3.848
16.983
1.00
14.35
A


ATOM
1068
C
PHE
A
137
49.659
4.657
17.067
1.00
16.21
A


ATOM
1069
O
PHE
A
137
49.037
3.767
17.622
1.00
18.05
A


ATOM
1070
N
LEU
A
138
49.074
5.534
16.259
1.00
17.51
A


ATOM
1071
CA
LEU
A
138
47.648
5.433
15.953
1.00
19.20
A


ATOM
1072
CB
LEU
A
138
47.017
6.822
15.800
1.00
20.80
A


ATOM
1073
CG
LEU
A
138
46.809
7.688
17.044
1.00
23.47
A


ATOM
1074
CD1
LEU
A
138
46.141
6.879
18.144
1.00
24.75
A


ATOM
1075
CD2
LEU
A
138
48.140
8.212
17.529
1.00
27.62
A


ATOM
1076
C
LEU
A
138
47.490
4.637
14.658
1.00
18.41
A


ATOM
1077
O
LEU
A
138
48.218
4.862
13.698
1.00
16.16
A


ATOM
1078
N
SER
A
139
46.530
3.716
14.630
1.00
18.51
A


ATOM
1079
CA
SER
A
139
46.333
2.863
13.460
1.00
17.61
A


ATOM
1080
CB
SER
A
139
45.481
1.656
13.836
1.00
18.17
A


ATOM
1081
OG
SER
A
139
44.134
2.036
14.040
1.00
20.80
A


ATOM
1082
C
SER
A
139
45.729
3.510
12.216
1.00
17.44
A


ATOM
1083
O
SER
A
139
45.122
4.578
12.276
1.00
16.41
A


ATOM
1084
N
LYS
A
140
45.908
2.822
11.088
1.00
18.56
A


ATOM
1085
CA
LYS
A
140
45.402
3.237
9.778
1.00
18.37
A


ATOM
1086
CB
LYS
A
140
46.543
3.751
8.895
1.00
21.60
A


ATOM
1087
CG
LYS
A
140
47.149
5.085
9.326
1.00
24.86
A


ATOM
1088
CD
LYS
A
140
46.513
6.267
8.602
1.00
30.27
A


ATOM
1089
CE
LYS
A
140
46.961
6.345
7.150
1.00
29.93
A


ATOM
1090
NZ
LYS
A
140
48.440
6.349
7.038
1.00
30.14
A


ATOM
1091
C
LYS
A
140
44.773
2.012
9.118
1.00
17.79
A


ATOM
1092
O
LYS
A
140
45.106
0.878
9.458
1.00
17.76
A


ATOM
1093
N
SER
A
141
43.882
2.234
8.160
1.00
18.54
A


ATOM
1094
CA
SER
A
141
43.220
1.124
7.481
1.00
21.55
A


ATOM
1095
CB
SER
A
141
42.047
1.634
6.630
1.00
21.05
A


ATOM
1096
OG
SER
A
141
42.490
2.482
5.588
1.00
28.41
A


ATOM
1097
C
SER
A
141
44.154
0.263
6.625
1.00
21.42
A


ATOM
1098
O
SER
A
141
43.828
−0.885
6.332
1.00
21.49
A


ATOM
1099
N
ASP
A
142
45.311
0.793
6.226
1.00
20.12
A


ATOM
1100
CA
ASP
A
142
46.234
−0.016
5.430
1.00
19.88
A


ATOM
1101
CB
ASP
A
142
47.008
0.843
4.420
1.00
22.82
A


ATOM
1102
CG
ASP
A
142
47.949
1.834
5.076
1.00
24.81
A


ATOM
1103
OD1
ASP
A
142
47.837
2.061
6.298
1.00
25.33
A


ATOM
1104
OD2
ASP
A
142
48.799
2.395
4.354
1.00
28.43
A


ATOM
1105
C
ASP
A
142
47.176
−0.752
6.368
1.00
20.11
A


ATOM
1106
O
ASP
A
142
48.127
−1.416
5.946
1.00
19.21
A


ATOM
1107
N
HIS
A
143
46.885
−0.626
7.659
1.00
18.99
A


ATOM
1108
CA
HIS
A
143
47.637
−1.295
8.706
1.00
17.27
A


ATOM
1109
CB
HIS
A
143
47.686
−2.792
8.409
1.00
16.45
A


ATOM
1110
CG
HIS
A
143
46.329
−3.396
8.190
1.00
18.33
A


ATOM
1111
CD2
HIS
A
143
45.860
−4.211
7.213
1.00
17.59
A


ATOM
1112
ND1
HIS
A
143
45.262
−3.151
9.032
1.00
15.97
A


ATOM
1113
CE1
HIS
A
143
44.194
−3.786
8.580
1.00
19.46
A


ATOM
1114
NE2
HIS
A
143
44.529
−4.436
7.478
1.00
18.06
A


ATOM
1115
C
HIS
A
143
49.019
−0.749
9.030
1.00
19.46
A


ATOM
1116
O
HIS
A
143
49.812
−1.401
9.715
1.00
19.95
A


ATOM
1117
N
SER
A
144
49.301
0.454
8.536
1.00
19.70
A


ATOM
1118
CA
SER
A
144
50.542
1.141
8.852
1.00
20.18
A


ATOM
1119
CB
SER
A
144
51.018
2.011
7.678
1.00
19.91
A


ATOM
1120
OG
SER
A
144
50.099
3.044
7.364
1.00
23.64
A


ATOM
1121
C
SER
A
144
50.109
2.018
10.034
1.00
19.40
A


ATOM
1122
O
SER
A
144
48.970
1.906
10.499
1.00
19.70
A


ATOM
1123
N
PHE
A
145
50.986
2.883
10.525
1.00
16.99
A


ATOM
1124
CA
PHE
A
145
50.614
3.728
11.649
1.00
16.06
A


ATOM
1125
CB
PHE
A
145
51.325
3.274
12.929
1.00
16.25
A


ATOM
1126
CG
PHE
A
145
51.062
1.841
13.297
1.00
19.53
A


ATOM
1127
CD1
PHE
A
145
51.754
0.807
12.672
1.00
20.17
A


ATOM
1128
CD2
PHE
A
145
50.114
1.522
14.263
1.00
18.18
A


ATOM
1129
CE1
PHE
A
145
51.505
−0.525
13.005
1.00
21.33
A


ATOM
1130
CE2
PHE
A
145
49.856
0.193
14.606
1.00
19.50
A


ATOM
1131
CZ
PHE
A
145
50.553
−0.831
13.975
1.00
20.23
A


ATOM
1132
C
PHE
A
145
50.955
5.182
11.419
1.00
15.69
A


ATOM
1133
O
PHE
A
145
51.548
5.538
10.404
1.00
16.69
A


ATOM
1134
N
PHE
A
146
50.530
6.021
12.357
1.00
14.53
A


ATOM
1135
CA
PHE
A
146
50.869
7.429
12.332
1.00
16.67
A


ATOM
1136
CB
PHE
A
146
49.841
8.279
11.552
1.00
16.59
A


ATOM
1137
CG
PHE
A
146
48.535
8.528
12.259
1.00
15.25
A


ATOM
1138
CD1
PHE
A
146
48.370
9.644
13.071
1.00
15.42
A


ATOM
1139
CD2
PHE
A
146
47.433
7.708
12.019
1.00
16.06
A


ATOM
1140
CE1
PHE
A
146
47.123
9.952
13.629
1.00
17.50
A


ATOM
1141
CE2
PHE
A
146
46.180
8.003
12.571
1.00
16.80
A


ATOM
1142
CZ
PHE
A
146
46.023
9.126
13.375
1.00
17.47
A


ATOM
1143
C
PHE
A
146
51.017
7.841
13.783
1.00
17.00
A


ATOM
1144
O
PHE
A
146
50.345
7.308
14.661
1.00
19.50
A


ATOM
1145
N
LYS
A
147
51.950
8.747
14.032
1.00
17.82
A


ATOM
1146
CA
LYS
A
147
52.224
9.221
15.377
1.00
18.67
A


ATOM
1147
CB
LYS
A
147
53.540
8.604
15.863
1.00
20.48
A


ATOM
1148
CG
LYS
A
147
53.771
8.668
17.359
1.00
25.54
A


ATOM
1149
CD
LYS
A
147
54.822
7.645
17.774
1.00
29.96
A


ATOM
1150
CE
LYS
A
147
54.835
7.417
19.282
1.00
30.05
A


ATOM
1151
NZ
LYS
A
147
55.740
6.291
19.643
1.00
33.05
A


ATOM
1152
C
LYS
A
147
52.315
10.743
15.338
1.00
17.25
A


ATOM
1153
O
LYS
A
147
52.716
11.320
14.329
1.00
19.15
A


ATOM
1154
N
ILE
A
148
51.932
11.391
16.428
1.00
15.47
A


ATOM
1155
CA
ILE
A
148
51.969
12.846
16.494
1.00
14.99
A


ATOM
1156
CB
ILE
A
148
50.529
13.424
16.642
1.00
15.37
A


ATOM
1157
CG2
ILE
A
148
50.566
14.932
16.740
1.00
14.06
A


ATOM
1158
CG1
ILE
A
148
49.689
13.025
15.426
1.00
16.41
A


ATOM
1159
CD1
ILE
A
148
48.223
13.325
15.550
1.00
18.61
A


ATOM
1160
C
ILE
A
148
52.829
13.271
17.682
1.00
17.07
A


ATOM
1161
O
ILE
A
148
52.721
12.702
18.772
1.00
15.61
A


ATOM
1162
N
SER
A
149
53.696
14.255
17.458
1.00
16.79
A


ATOM
1163
CA
SER
A
149
54.570
14.757
18.514
1.00
17.66
A


ATOM
1164
CB
SER
A
149
56.042
14.612
18.116
1.00
15.95
A


ATOM
1165
OG
SER
A
149
56.900
14.956
19.190
1.00
17.31
A


ATOM
1166
C
SER
A
149
54.239
16.225
18.763
1.00
18.34
A


ATOM
1167
O
SER
A
149
53.854
16.949
17.842
1.00
18.33
A


ATOM
1168
N
TYR
A
150
54.401
16.665
20.005
1.00
16.95
A


ATOM
1169
CA
TYR
A
150
54.085
18.040
20.362
1.00
17.59
A


ATOM
1170
CB
TYR
A
150
52.893
18.057
21.310
1.00
17.57
A


ATOM
1171
CG
TYR
A
150
51.679
17.314
20.797
1.00
18.52
A


ATOM
1172
CD1
TYR
A
150
50.879
17.851
19.789
1.00
17.12
A


ATOM
1173
CE1
TYR
A
150
49.733
17.182
19.340
1.00
18.32
A


ATOM
1174
CD2
TYR
A
150
51.313
16.078
21.345
1.00
18.89
A


ATOM
1175
CE2
TYR
A
150
50.176
15.399
20.901
1.00
17.65
A


ATOM
1176
CZ
TYR
A
150
49.391
15.957
19.900
1.00
17.92
A


ATOM
1177
OH
TYR
A
150
48.275
15.285
19.457
1.00
19.69
A


ATOM
1178
C
TYR
A
150
55.237
18.768
21.021
1.00
17.16
A


ATOM
1179
O
TYR
A
150
55.953
18.207
21.847
1.00
19.65
A


ATOM
1180
N
LEU
A
151
55.409
20.029
20.649
1.00
17.01
A


ATOM
1181
CA
LEU
A
151
56.449
20.868
21.224
1.00
15.24
A


ATOM
1182
CB
LEU
A
151
57.540
21.182
20.197
1.00
16.33
A


ATOM
1183
CG
LEU
A
151
58.487
22.335
20.575
1.00
16.27
A


ATOM
1184
CD1
LEU
A
151
59.402
21.906
21.706
1.00
17.13
A


ATOM
1185
CD2
LEU
A
151
59.315
22.755
19.359
1.00
19.34
A


ATOM
1186
C
LEU
A
151
55.825
22.174
21.666
1.00
16.08
A


ATOM
1187
O
LEU
A
151
55.221
22.881
20.860
1.00
16.22
A


ATOM
1188
N
THR
A
152
55.952
22.497
22.945
1.00
16.84
A


ATOM
1189
CA
THR
A
152
55.428
23.765
23.424
1.00
18.70
A


ATOM
1190
CB
THR
A
152
55.283
23.799
24.946
1.00
20.14
A


ATOM
1191
OG1
THR
A
152
56.576
23.633
25.544
1.00
23.32
A


ATOM
1192
CG2
THR
A
152
54.355
22.694
25.419
1.00
18.36
A


ATOM
1193
C
THR
A
152
56.498
24.772
23.050
1.00
20.04
A


ATOM
1194
O
THR
A
152
57.689
24.448
23.034
1.00
20.72
A


ATOM
1195
N
LEU
A
153
56.085
25.986
22.735
1.00
20.63
A


ATOM
1196
CA
LEU
A
153
57.043
27.014
22.389
1.00
24.69
A


ATOM
1197
CB
LEU
A
153
57.579
26.794
20.960
1.00
24.19
A


ATOM
1198
CG
LEU
A
153
56.716
26.942
19.694
1.00
26.72
A


ATOM
1199
CD1
LEU
A
153
55.303
26.451
19.959
1.00
27.32
A


ATOM
1200
CD2
LEU
A
153
56.686
28.393
19.249
1.00
26.15
A


ATOM
1201
C
LEU
A
153
56.410
28.385
22.531
1.00
26.36
A


ATOM
1202
O
LEU
A
153
55.180
28.511
22.597
1.00
29.59
A


ATOM
1203
N
LEU
A
154
57.262
29.401
22.620
1.00
26.29
A


ATOM
1204
CA
LEU
A
154
56.830
30.787
22.729
1.00
26.89
A


ATOM
1205
CB
LEU
A
154
57.459
31.444
23.965
1.00
26.94
A


ATOM
1206
CG
LEU
A
154
56.966
32.833
24.407
1.00
28.58
A


ATOM
1207
CD1
LEU
A
154
55.507
32.755
24.864
1.00
24.43
A


ATOM
1208
CD2
LEU
A
154
57.845
33.342
25.549
1.00
27.14
A


ATOM
1209
C
LEU
A
154
57.337
31.458
21.456
1.00
28.94
A


ATOM
1210
O
LEU
A
154
58.538
31.689
21.304
1.00
30.73
A


ATOM
1211
N
PRO
A
155
56.428
31.773
20.518
1.00
30.57
A


ATOM
1212
CD
PRO
A
155
54.975
31.534
20.559
1.00
29.60
A


ATOM
1213
CA
PRO
A
155
56.806
32.412
19.254
1.00
31.63
A


ATOM
1214
CB
PRO
A
155
55.460
32.668
18.581
1.00
30.63
A


ATOM
1215
CG
PRO
A
155
54.612
31.552
19.087
1.00
28.73
A


ATOM
1216
C
PRO
A
155
57.639
33.688
19.370
1.00
33.58
A


ATOM
1217
O
PRO
A
155
57.322
34.593
20.136
1.00
33.98
A


ATOM
1218
N
SER
A
156
58.706
33.741
18.586
1.00
35.79
A


ATOM
1219
CA
SER
A
156
59.595
34.888
18.546
1.00
37.77
A


ATOM
1220
CB
SER
A
156
60.604
34.839
19.694
1.00
38.66
A


ATOM
1221
OG
SER
A
156
59.955
34.966
20.949
1.00
44.00
A


ATOM
1222
C
SER
A
156
60.332
34.841
17.222
1.00
38.83
A


ATOM
1223
O
SER
A
156
60.257
33.849
16.492
1.00
38.36
A


ATOM
1224
N
ALA
A
157
61.042
35.915
16.909
1.00
40.38
A


ATOM
1225
CA
ALA
A
157
61.796
35.972
15.670
1.00
39.93
A


ATOM
1226
CB
ALA
A
157
61.822
37.401
15.148
1.00
40.36
A


ATOM
1227
C
ALA
A
157
63.214
35.466
15.918
1.00
39.65
A


ATOM
1228
O
ALA
A
157
64.058
35.504
15.021
1.00
39.72
A


ATOM
1229
N
GLU
A
158
63.463
34.984
17.135
1.00
39.12
A


ATOM
1230
CA
GLU
A
158
64.784
34.480
17.517
1.00
40.24
A


ATOM
1231
CB
GLU
A
158
65.082
34.808
18.988
1.00
44.21
A


ATOM
1232
CG
GLU
A
158
65.426
36.268
19.287
1.00
50.31
A


ATOM
1233
CD
GLU
A
158
64.204
37.174
19.356
1.00
55.36
A


ATOM
1234
OE1
GLU
A
158
64.353
38.351
19.765
1.00
55.75
A


ATOM
1235
OE2
GLU
A
158
63.095
36.712
19.002
1.00
58.12
A


ATOM
1236
C
GLU
A
158
65.005
32.979
17.303
1.00
38.02
A


ATOM
1237
O
GLU
A
158
66.130
32.493
17.419
1.00
36.30
A


ATOM
1238
N
GLU
A
159
63.950
32.234
17.002
1.00
35.79
A


ATOM
1239
CA
GLU
A
159
64.136
30.807
16.805
1.00
35.02
A


ATOM
1240
CB
GLU
A
159
63.949
30.066
18.135
1.00
36.97
A


ATOM
1241
CG
GLU
A
159
62.699
30.439
18.891
1.00
41.68
A


ATOM
1242
CD
GLU
A
159
62.717
29.933
20.323
1.00
44.82
A


ATOM
1243
OE1
GLU
A
159
62.819
28.705
20.527
1.00
46.62
A


ATOM
1244
OE2
GLU
A
159
62.631
30.767
21.248
1.00
47.25
A


ATOM
1245
C
GLU
A
159
63.277
30.162
15.735
1.00
32.21
A


ATOM
1246
O
GLU
A
159
62.147
30.574
15.473
1.00
32.05
A


ATOM
1247
N
SER
A
160
63.849
29.147
15.107
1.00
29.55
A


ATOM
1248
CA
SER
A
160
63.167
28.394
14.076
1.00
28.89
A


ATOM
1249
CB
SER
A
160
63.885
28.551
12.734
1.00
27.34
A


ATOM
1250
OG
SER
A
160
65.206
28.053
12.807
1.00
29.49
A


ATOM
1251
C
SER
A
160
63.241
26.957
14.565
1.00
27.42
A


ATOM
1252
O
SER
A
160
64.092
26.628
15.392
1.00
25.45
A


ATOM
1253
N
TYR
A
161
62.359
26.101
14.066
1.00
24.73
A


ATOM
1254
CA
TYR
A
161
62.359
24.725
14.517
1.00
24.26
A


ATOM
1255
CB
TYR
A
161
61.172
24.480
15.451
1.00
23.50
A


ATOM
1256
CG
TYR
A
161
60.935
25.593
16.434
1.00
24.01
A


ATOM
1257
CD1
TYR
A
161
60.255
26.748
16.052
1.00
26.02
A


ATOM
1258
CE1
TYR
A
161
60.009
27.774
16.959
1.00
27.93
A


ATOM
1259
CD2
TYR
A
161
61.374
25.491
17.753
1.00
24.78
A


ATOM
1260
CE2
TYR
A
161
61.136
26.514
18.674
1.00
25.93
A


ATOM
1261
CZ
TYR
A
161
60.450
27.650
18.270
1.00
27.56
A


ATOM
1262
OH
TYR
A
161
60.182
28.650
19.173
1.00
29.78
A


ATOM
1263
C
TYR
A
161
62.330
23.700
13.397
1.00
25.15
A


ATOM
1264
O
TYR
A
161
62.082
24.021
12.239
1.00
24.96
A


ATOM
1265
N
ASP
A
162
62.600
22.455
13.775
1.00
26.26
A


ATOM
1266
CA
ASP
A
162
62.598
21.331
12.858
1.00
26.94
A


ATOM
1267
CB
ASP
A
162
64.007
21.014
12.356
1.00
30.11
A


ATOM
1268
CG
ASP
A
162
64.548
22.067
11.434
1.00
32.85
A


ATOM
1269
OD1
ASP
A
162
64.075
22.138
10.277
1.00
33.31
A


ATOM
1270
OD2
ASP
A
162
65.443
22.819
11.874
1.00
33.08
A


ATOM
1271
C
ASP
A
162
62.122
20.117
13.613
1.00
25.87
A


ATOM
1272
O
ASP
A
162
62.449
19.947
14.789
1.00
24.38
A


ATOM
1273
N
CYS
A
163
61.352
19.277
12.935
1.00
23.95
A


ATOM
1274
CA
CYS
A
163
60.914
18.027
13.530
1.00
24.46
A


ATOM
1275
C
CYS
A
163
61.916
17.043
12.938
1.00
22.46
A


ATOM
1276
O
CYS
A
163
62.110
17.021
11.726
1.00
24.01
A


ATOM
1277
CB
CYS
A
163
59.497
17.658
13.083
1.00
24.14
A


ATOM
1278
SG
CYS
A
163
58.931
16.101
13.836
1.00
30.35
A


ATOM
1279
N
LYS
A
164
62.571
16.259
13.782
1.00
22.96
A


ATOM
1280
CA
LYS
A
164
63.559
15.292
13.307
1.00
24.69
A


ATOM
1281
CB
LYS
A
164
64.867
15.450
14.089
1.00
27.54
A


ATOM
1282
CG
LYS
A
164
65.977
14.490
13.689
1.00
28.93
A


ATOM
1283
CD
LYS
A
164
67.179
14.643
14.622
1.00
32.03
A


ATOM
1284
CE
LYS
A
164
68.254
13.596
14.350
1.00
33.85
A


ATOM
1285
NZ
LYS
A
164
69.319
13.607
15.398
1.00
36.46
A


ATOM
1286
C
LYS
A
164
63.023
13.875
13.463
1.00
24.25
A


ATOM
1287
O
LYS
A
164
62.697
13.443
14.570
1.00
23.52
A


ATOM
1288
N
VAL
A
165
62.931
13.160
12.345
1.00
23.37
A


ATOM
1289
CA
VAL
A
165
62.415
11.797
12.344
1.00
24.06
A


ATOM
1290
CB
VAL
A
165
61.174
11.682
11.408
1.00
23.45
A


ATOM
1291
CG1
VAL
A
165
60.657
10.248
11.382
1.00
18.80
A


ATOM
1292
CG2
VAL
A
165
60.078
12.632
11.878
1.00
22.37
A


ATOM
1293
C
VAL
A
165
63.457
10.772
11.903
1.00
25.04
A


ATOM
1294
O
VAL
A
165
64.103
10.931
10.869
1.00
25.12
A


ATOM
1295
N
GLU
A
166
63.621
9.725
12.703
1.00
26.91
A


ATOM
1296
CA
GLU
A
166
64.556
8.648
12.383
1.00
28.84
A


ATOM
1297
CB
GLU
A
166
65.554
8.424
13.523
1.00
30.71
A


ATOM
1298
CG
GLU
A
166
66.382
9.634
13.922
1.00
36.90
A


ATOM
1299
CD
GLU
A
166
67.247
9.356
15.147
1.00
39.97
A


ATOM
1300
OE1
GLU
A
166
67.466
10.286
15.954
1.00
43.02
A


ATOM
1301
OE2
GLU
A
166
67.714
8.206
15.301
1.00
43.24
A


ATOM
1302
C
GLU
A
166
63.739
7.369
12.183
1.00
28.96
A


ATOM
1303
O
GLU
A
166
62.975
6.971
13.067
1.00
27.40
A


ATOM
1304
N
HIS
A
167
63.910
6.728
11.029
1.00
29.87
A


ATOM
1305
CA
HIS
A
167
63.189
5.496
10.713
1.00
30.70
A


ATOM
1306
CB
HIS
A
167
61.838
5.833
10.084
1.00
30.90
A


ATOM
1307
CG
HIS
A
167
60.932
4.655
9.933
1.00
34.01
A


ATOM
1308
CD2
HIS
A
167
60.698
3.842
8.876
1.00
33.60
A


ATOM
1309
ND1
HIS
A
167
60.159
4.172
10.967
1.00
36.69
A


ATOM
1310
CE1
HIS
A
167
59.488
3.112
10.554
1.00
34.84
A


ATOM
1311
NE2
HIS
A
167
59.798
2.890
9.290
1.00
34.90
A


ATOM
1312
C
HIS
A
167
63.999
4.639
9.739
1.00
31.21
A


ATOM
1313
O
HIS
A
167
64.696
5.167
8.866
1.00
29.44
A


ATOM
1314
N
TRP
A
168
63.895
3.320
9.879
1.00
31.70
A


ATOM
1315
CA
TRP
A
168
64.625
2.402
9.006
1.00
31.76
A


ATOM
1316
CB
TRP
A
168
64.344
0.954
9.396
1.00
30.39
A


ATOM
1317
CG
TRP
A
168
64.735
0.650
10.797
1.00
28.49
A


ATOM
1318
CD2
TRP
A
168
64.115
−0.297
11.666
1.00
28.31
A


ATOM
1319
CE2
TRP
A
168
64.837
−0.288
12.878
1.00
28.31
A


ATOM
1320
CE3
TRP
A
168
63.017
−1.157
11.538
1.00
26.47
A


ATOM
1321
CD1
TRP
A
168
65.778
1.184
11.491
1.00
28.32
A


ATOM
1322
NE1
TRP
A
168
65.849
0.627
12.744
1.00
28.98
A


ATOM
1323
CZ2
TRP
A
168
64.498
−1.107
13.958
1.00
28.85
A


ATOM
1324
CZ3
TRP
A
168
62.678
−1.970
12.608
1.00
27.57
A


ATOM
1325
CH2
TRP
A
168
63.418
−1.940
13.805
1.00
29.20
A


ATOM
1326
C
TRP
A
168
64.332
2.588
7.523
1.00
33.06
A


ATOM
1327
O
TRP
A
168
65.190
2.314
6.682
1.00
32.28
A


ATOM
1328
N
GLY
A
169
63.126
3.049
7.202
1.00
34.81
A


ATOM
1329
CA
GLY
A
169
62.760
3.263
5.810
1.00
35.23
A


ATOM
1330
C
GLY
A
169
63.267
4.588
5.266
1.00
37.25
A


ATOM
1331
O
GLY
A
169
62.907
4.992
4.162
1.00
37.65
A


ATOM
1332
N
LEU
A
170
64.100
5.268
6.049
1.00
39.27
A


ATOM
1333
CA
LEU
A
170
64.673
6.555
5.660
1.00
41.10
A


ATOM
1334
CB
LEU
A
170
64.354
7.626
6.706
1.00
38.47
A


ATOM
1335
CG
LEU
A
170
62.923
8.143
6.843
1.00
38.66
A


ATOM
1336
CD1
LEU
A
170
62.790
8.919
8.142
1.00
37.48
A


ATOM
1337
CD2
LEU
A
170
62.572
9.017
5.653
1.00
37.65
A


ATOM
1338
C
LEU
A
170
66.183
6.425
5.556
1.00
43.62
A


ATOM
1339
O
LEU
A
170
66.809
5.762
6.382
1.00
44.45
A


ATOM
1340
N
ASP
A
171
66.764
7.066
4.545
1.00
46.98
A


ATOM
1341
CA
ASP
A
171
68.211
7.036
4.350
1.00
48.99
A


ATOM
1342
CB
ASP
A
171
68.602
7.810
3.086
1.00
51.12
A


ATOM
1343
CG
ASP
A
171
67.735
7.466
1.895
1.00
53.30
A


ATOM
1344
OD1
ASP
A
171
66.520
7.761
1.936
1.00
54.82
A


ATOM
1345
OD2
ASP
A
171
68.271
6.903
0.917
1.00
54.86
A


ATOM
1346
C
ASP
A
171
68.836
7.726
5.554
1.00
48.82
A


ATOM
1347
O
ASP
A
171
69.437
7.093
6.420
1.00
48.88
A


ATOM
1348
N
LYS
A
172
68.673
9.044
5.585
1.00
48.96
A


ATOM
1349
CA
LYS
A
172
69.192
9.877
6.659
1.00
48.79
A


ATOM
1350
CB
LYS
A
172
69.986
11.059
6.084
1.00
51.32
A


ATOM
1351
CG
LYS
A
172
71.074
10.698
5.075
1.00
55.53
A


ATOM
1352
CD
LYS
A
172
71.799
11.952
4.571
1.00
57.81
A


ATOM
1353
CE
LYS
A
172
72.859
11.621
3.518
1.00
59.22
A


ATOM
1354
NZ
LYS
A
172
73.912
10.702
4.038
1.00
58.32
A


ATOM
1355
C
LYS
A
172
67.990
10.419
7.420
1.00
46.36
A


ATOM
1356
O
LYS
A
172
66.862
10.381
6.919
1.00
44.39
A


ATOM
1357
N
PRO
A
173
68.211
10.920
8.645
1.00
44.20
A


ATOM
1358
CD
PRO
A
173
69.432
10.866
9.469
1.00
44.15
A


ATOM
1359
CA
PRO
A
173
67.089
11.462
9.410
1.00
42.74
A


ATOM
1360
CB
PRO
A
173
67.768
12.050
10.637
1.00
42.02
A


ATOM
1361
CG
PRO
A
173
68.887
11.080
10.872
1.00
44.25
A


ATOM
1362
C
PRO
A
173
66.369
12.517
8.578
1.00
41.09
A


ATOM
1363
O
PRO
A
173
67.002
13.309
7.877
1.00
39.67
A


ATOM
1364
N
LEU
A
174
65.044
12.502
8.636
1.00
39.80
A


ATOM
1365
CA
LEU
A
174
64.241
13.457
7.888
1.00
38.58
A


ATOM
1366
CB
LEU
A
174
62.894
12.838
7.522
1.00
38.73
A


ATOM
1367
CG
LEU
A
174
62.202
13.329
6.251
1.00
39.18
A


ATOM
1368
CD1
LEU
A
174
60.826
12.691
6.170
1.00
39.20
A


ATOM
1369
CD2
LEU
A
174
62.093
14.836
6.245
1.00
40.87
A


ATOM
1370
C
LEU
A
174
64.019
14.662
8.785
1.00
37.43
A


ATOM
1371
O
LEU
A
174
63.630
14.514
9.943
1.00
37.68
A


ATOM
1372
N
LEU
A
175
64.284
15.849
8.255
1.00
35.85
A


ATOM
1373
CA
LEU
A
175
64.098
17.077
9.012
1.00
34.38
A


ATOM
1374
CB
LEU
A
175
65.400
17.882
9.074
1.00
33.21
A


ATOM
1375
CG
LEU
A
175
66.425
17.502
10.147
1.00
34.82
A


ATOM
1376
CD1
LEU
A
175
65.838
17.768
11.526
1.00
34.32
A


ATOM
1377
CD2
LEU
A
175
66.819
16.038
10.008
1.00
35.37
A


ATOM
1378
C
LEU
A
175
63.020
17.898
8.337
1.00
33.09
A


ATOM
1379
O
LEU
A
175
63.080
18.137
7.132
1.00
33.84
A


ATOM
1380
N
LYS
A
176
62.023
18.312
9.108
1.00
30.14
A


ATOM
1381
CA
LYS
A
176
60.943
19.119
8.566
1.00
30.03
A


ATOM
1382
CB
LYS
A
176
59.598
18.416
8.772
1.00
30.60
A


ATOM
1383
CG
LYS
A
176
58.463
19.049
8.010
1.00
33.60
A


ATOM
1384
CD
LYS
A
176
58.742
19.054
6.508
1.00
37.73
A


ATOM
1385
CE
LYS
A
176
58.869
17.642
5.960
1.00
37.37
A


ATOM
1386
NZ
LYS
A
176
59.075
17.629
4.484
1.00
41.15
A


ATOM
1387
C
LYS
A
176
60.976
20.457
9.292
1.00
28.62
A


ATOM
1388
O
LYS
A
176
60.764
20.524
10.501
1.00
27.68
A


ATOM
1389
N
HIS
A
177
61.238
21.520
8.539
1.00
28.72
A


ATOM
1390
CA
HIS
A
177
61.353
22.868
9.088
1.00
29.54
A


ATOM
1391
CB
HIS
A
177
62.284
23.691
8.195
1.00
29.51
A


ATOM
1392
CG
HIS
A
177
62.485
25.097
8.663
1.00
30.53
A


ATOM
1393
CD2
HIS
A
177
62.124
26.282
8.114
1.00
31.99
A


ATOM
1394
ND1
HIS
A
177
63.117
25.401
9.849
1.00
32.09
A


ATOM
1395
CE1
HIS
A
177
63.138
26.713
10.010
1.00
32.65
A


ATOM
1396
NE2
HIS
A
177
62.542
27.271
8.971
1.00
32.04
A


ATOM
1397
C
HIS
A
177
60.059
23.654
9.304
1.00
29.24
A


ATOM
1398
O
HIS
A
177
59.100
23.519
8.549
1.00
27.66
A


ATOM
1399
N
TRP
A
178
60.062
24.492
10.340
1.00
30.09
A


ATOM
1400
CA
TRP
A
178
58.926
25.350
10.674
1.00
33.43
A


ATOM
1401
CB
TRP
A
178
57.959
24.647
11.632
1.00
28.07
A


ATOM
1402
CG
TRP
A
178
56.681
25.422
11.851
1.00
25.25
A


ATOM
1403
CD2
TRP
A
178
56.476
26.518
12.761
1.00
21.68
A


ATOM
1404
CE2
TRP
A
178
55.138
26.942
12.611
1.00
20.86
A


ATOM
1405
CE3
TRP
A
178
57.292
27.178
13.688
1.00
20.72
A


ATOM
1406
CD1
TRP
A
178
55.489
25.239
11.206
1.00
24.81
A


ATOM
1407
NE1
TRP
A
178
54.559
26.146
11.657
1.00
21.51
A


ATOM
1408
CZ2
TRP
A
178
54.598
27.999
13.354
1.00
21.11
A


ATOM
1409
CZ3
TRP
A
178
56.754
28.229
14.428
1.00
21.58
A


ATOM
1410
CH2
TRP
A
178
55.419
28.627
14.255
1.00
20.94
A


ATOM
1411
C
TRP
A
178
59.425
26.628
11.348
1.00
36.30
A


ATOM
1412
O
TRP
A
178
60.314
26.591
12.195
1.00
36.91
A


ATOM
1413
N
GLU
A
179
58.852
27.761
10.975
1.00
40.65
A


ATOM
1414
CA
GLU
A
179
59.240
29.029
11.587
1.00
45.62
A


ATOM
1415
CB
GLU
A
179
60.481
29.622
10.899
1.00
47.42
A


ATOM
1416
CG
GLU
A
179
60.323
29.868
9.404
1.00
52.77
A


ATOM
1417
CD
GLU
A
179
61.498
30.624
8.806
1.00
55.17
A


ATOM
1418
OE1
GLU
A
179
62.653
30.179
8.987
1.00
57.20
A


ATOM
1419
OE2
GLU
A
179
61.265
31.663
8.149
1.00
57.21
A


ATOM
1420
C
GLU
A
179
58.074
30.001
11.489
1.00
46.47
A


ATOM
1421
O
GLU
A
179
57.322
29.983
10.513
1.00
45.49
A


ATOM
1422
N
PRO
A
180
57.898
30.855
12.509
1.00
47.97
A


ATOM
1423
CD
PRO
A
180
58.679
31.008
13.752
1.00
48.35
A


ATOM
1424
CA
PRO
A
180
56.789
31.810
12.460
1.00
49.45
A


ATOM
1425
CB
PRO
A
180
56.763
32.372
13.880
1.00
49.39
A


ATOM
1426
CG
PRO
A
180
58.214
32.358
14.266
1.00
48.65
A


ATOM
1427
C
PRO
A
180
57.014
32.891
11.401
1.00
50.21
A


ATOM
1428
O
PRO
A
180
58.174
33.041
10.950
1.00
49.95
A


ATOM
1429
OXT
PRO
A
180
56.030
33.578
11.043
1.00
50.90
A


ATOM
1430
CB
SER
B
3
67.953
−2.426
7.203
1.00
59.72
B


ATOM
1431
OG
SER
B
3
68.517
−3.384
6.321
1.00
60.71
B


ATOM
1432
C
SER
B
3
68.164
−3.822
9.277
1.00
57.49
B


ATOM
1433
O
SER
B
3
68.117
−4.879
8.642
1.00
57.32
B


ATOM
1434
N
SER
B
3
70.072
−2.418
8.486
1.00
59.35
B


ATOM
1435
CA
SER
B
3
68.586
−2.517
8.597
1.00
58.84
B


ATOM
1436
N
PRO
B
4
67.855
−3.763
10.585
1.00
55.71
B


ATOM
1437
CD
PRO
B
4
67.914
−2.580
11.463
1.00
54.97
B


ATOM
1438
CA
PRO
B
4
67.438
−4.952
11.338
1.00
53.72
B


ATOM
1439
CB
PRO
B
4
67.457
−4.467
12.787
1.00
54.71
B


ATOM
1440
CG
PRO
B
4
67.095
−3.021
12.660
1.00
54.93
B


ATOM
1441
C
PRO
B
4
66.069
−5.487
10.918
1.00
51.05
B


ATOM
1442
O
PRO
B
4
65.240
−4.753
10.379
1.00
50.96
B


ATOM
1443
N
GLU
B
5
65.843
−6.773
11.165
1.00
47.90
B


ATOM
1444
CA
GLU
B
5
64.581
−7.410
10.810
1.00
45.24
B


ATOM
1445
CB
GLU
B
5
64.811
−8.893
10.489
1.00
48.23
B


ATOM
1446
CG
GLU
B
5
65.603
−9.656
11.545
1.00
54.54
B


ATOM
1447
CD
GLU
B
5
65.896
−11.102
11.140
1.00
57.83
B


ATOM
1448
OE1
GLU
B
5
66.421
−11.317
10.024
1.00
59.67
B


ATOM
1449
OE2
GLU
B
5
65.609
−12.020
11.941
1.00
59.33
B


ATOM
1450
C
GLU
B
5
63.548
−7.269
11.920
1.00
40.85
B


ATOM
1451
O
GLU
B
5
63.876
−7.328
13.105
1.00
40.81
B


ATOM
1452
N
ASP
B
6
62.294
−7.083
11.532
1.00
36.03
B


ATOM
1453
CA
ASP
B
6
61.223
−6.936
12.508
1.00
32.11
B


ATOM
1454
CB
ASP
B
6
60.833
−5.460
12.616
1.00
29.96
B


ATOM
1455
CG
ASP
B
6
59.933
−5.171
13.798
1.00
27.91
B


ATOM
1456
OD1
ASP
B
6
59.280
−4.110
13.785
1.00
29.62
B


ATOM
1457
OD2
ASP
B
6
59.884
−5.982
14.745
1.00
29.86
B


ATOM
1458
C
ASP
B
6
60.014
−7.766
12.077
1.00
29.68
B


ATOM
1459
O
ASP
B
6
59.676
−7.802
10.899
1.00
29.14
B


ATOM
1460
N
PHE
B
7
59.380
−8.438
13.032
1.00
27.77
B


ATOM
1461
CA
PHE
B
7
58.193
−9.249
12.765
1.00
28.11
B


ATOM
1462
CB
PHE
B
7
58.453
−10.704
13.161
1.00
29.55
B


ATOM
1463
CG
PHE
B
7
59.461
−11.385
12.282
1.00
31.06
B


ATOM
1464
CD1
PHE
B
7
59.126
−11.766
10.989
1.00
29.85
B


ATOM
1465
CD2
PHE
B
7
60.761
−11.603
12.730
1.00
32.21
B


ATOM
1466
CE1
PHE
B
7
60.073
−12.355
10.145
1.00
33.75
B


ATOM
1467
CE2
PHE
B
7
61.719
−12.190
11.897
1.00
34.27
B


ATOM
1468
CZ
PHE
B
7
61.373
−12.568
10.599
1.00
33.07
B


ATOM
1469
C
PHE
B
7
57.032
−8.657
13.562
1.00
26.58
B


ATOM
1470
O
PHE
B
7
57.046
−8.645
14.794
1.00
25.72
B


ATOM
1471
N
VAL
B
8
56.023
−8.174
12.849
1.00
25.17
B


ATOM
1472
CA
VAL
B
8
54.891
−7.520
13.493
1.00
23.46
B


ATOM
1473
CB
VAL
B
8
54.670
−6.132
12.871
1.00
21.55
B


ATOM
1474
CG1
VAL
B
8
53.573
−5.394
13.612
1.00
21.83
B


ATOM
1475
CG2
VAL
B
8
55.975
−5.342
12.895
1.00
21.30
B


ATOM
1476
C
VAL
B
8
53.556
−8.255
13.467
1.00
24.08
B


ATOM
1477
O
VAL
B
8
53.204
−8.912
12.491
1.00
23.46
B


ATOM
1478
N
TYR
B
9
52.804
−8.127
14.554
1.00
23.26
B


ATOM
1479
CA
TYR
B
9
51.493
−8.747
14.619
1.00
23.18
B


ATOM
1480
CB
TYR
B
9
51.510
−9.978
15.520
1.00
23.12
B


ATOM
1481
CG
TYR
B
9
50.231
−10.786
15.465
1.00
24.54
B


ATOM
1482
CD1
TYR
B
9
50.158
−11.962
14.722
1.00
26.50
B


ATOM
1483
CE1
TYR
B
9
49.000
−12.743
14.716
1.00
25.08
B


ATOM
1484
CD2
TYR
B
9
49.108
−10.399
16.190
1.00
22.88
B


ATOM
1485
CE2
TYR
B
9
47.948
−11.165
16.188
1.00
23.91
B


ATOM
1486
CZ
TYR
B
9
47.902
−12.342
15.455
1.00
24.87
B


ATOM
1487
C
TYR
B
9
46.780
−13.140
15.501
1.00
25.45
B


ATOM
1488
C
TYR
B
9
50.509
−7.723
15.163
1.00
21.33
B


ATOM
1489
O
TYR
B
9
50.798
−7.028
16.133
1.00
22.92
B


ATOM
1490
N
GLN
B
10
49.353
−7.622
14.521
1.00
19.98
B


ATOM
1491
CA
GLN
B
10
48.326
−6.687
14.952
1.00
19.52
B


ATOM
1492
CB
GLN
B
10
48.171
−5.523
13.962
1.00
19.13
B


ATOM
1493
CG
GLN
B
10
49.433
−4.810
13.509
1.00
19.33
B


ATOM
1494
CD
GLN
B
10
49.117
−3.708
12.499
1.00
17.96
B


ATOM
1495
OE1
GLN
B
10
48.336
−2.802
12.783
1.00
18.49
B


ATOM
1496
NE2
GLN
B
10
49.715
−3.790
11.316
1.00
19.41
B


ATOM
1497
C
GLN
B
10
46.967
−7.375
15.029
1.00
19.74
B


ATOM
1498
O
GLN
B
10
46.626
−8.227
14.192
1.00
18.98
B


ATOM
1499
N
PHE
B
11
46.195
−6.996
16.040
1.00
19.06
B


ATOM
1500
CA
PHE
B
11
44.842
−7.487
16.182
1.00
16.54
B


ATOM
1501
CB
PHE
B
11
44.668
−8.454
17.336
1.00
17.48
B


ATOM
1502
CG
PHE
B
11
43.237
−8.847
17.544
1.00
16.17
B


ATOM
1503
CD1
PHE
B
11
42.570
−9.604
16.582
1.00
17.49
B


ATOM
1504
CD2
PHE
B
11
42.536
−8.406
18.656
1.00
14.41
B


ATOM
1505
CE1
PHE
B
11
41.219
−9.913
16.725
1.00
18.03
B


ATOM
1506
CE2
PHE
B
11
41.191
−8.708
18.814
1.00
16.34
B


ATOM
1507
CZ
PHE
B
11
40.528
−9.463
17.845
1.00
17.60
B


ATOM
1508
C
PHE
B
11
43.984
−6.271
16.450
1.00
18.14
B


ATOM
1509
O
PHE
B
11
44.241
−5.506
17.386
1.00
15.63
B


ATOM
1510
N
LYS
B
12
42.961
−6.094
15.625
1.00
17.33
B


ATOM
1511
CA
LYS
B
12
42.082
−4.958
15.770
1.00
17.63
B


ATOM
1512
CB
LYS
B
12
42.188
−4.067
14.536
1.00
18.71
B


ATOM
1513
CG
LYS
B
12
43.599
−3.642
14.192
1.00
15.90
B


ATOM
1514
CD
LYS
B
12
43.602
−2.909
12.871
1.00
17.33
B


ATOM
1515
CE
LYS
B
12
44.946
−2.297
12.570
1.00
18.72
B


ATOM
1516
NZ
LYS
B
12
44.838
−1.450
11.340
1.00
20.93
B


ATOM
1517
C
LYS
B
12
40.632
−5.387
15.968
1.00
18.92
B


ATOM
1518
O
LYS
B
12
40.041
−6.050
15.109
1.00
17.25
B


ATOM
1519
N
GLY
B
13
40.076
−5.002
17.114
1.00
17.59
B


ATOM
1520
CA
GLY
B
13
38.701
−5.322
17.430
1.00
19.88
B


ATOM
1521
C
GLY
B
13
37.874
−4.113
17.064
1.00
20.12
B


ATOM
1522
O
GLY
B
13
37.515
−3.309
17.923
1.00
21.08
B


ATOM
1523
N
MET
B
14
37.561
−4.000
15.779
1.00
20.42
B


ATOM
1524
CA
MET
B
14
36.817
−2.866
15.262
1.00
22.96
B


ATOM
1525
CB
MET
B
14
37.334
−2.554
13.866
1.00
23.02
B


ATOM
1526
CG
MET
B
14
38.846
−2.485
13.820
1.00
23.58
B


ATOM
1527
SD
MET
B
14
39.449
−2.095
12.191
1.00
26.23
B


ATOM
1528
CE
MET
B
14
39.260
−0.318
12.182
1.00
25.78
B


ATOM
1529
C
MET
B
14
35.295
−2.997
15.242
1.00
23.12
B


ATOM
1530
O
MET
B
14
34.751
−4.089
15.081
1.00
24.36
B


ATOM
1531
N
CYS
B
15
34.628
−1.860
15.427
1.00
24.04
B


ATOM
1532
CA
CYS
B
15
33.173
−1.768
15.433
1.00
24.91
B


ATOM
1533
C
CYS
B
15
32.808
−0.587
14.547
1.00
25.49
B


ATOM
1534
O
CYS
B
15
33.369
0.504
14.700
1.00
23.97
B


ATOM
1535
CB
CYS
B
15
32.630
−1.489
16.847
1.00
26.02
B


ATOM
1536
SG
CYS
B
15
32.691
−2.831
18.084
1.00
33.69
B


ATOM
1537
N
TYR
B
16
31.871
−0.805
13.630
1.00
25.87
B


ATOM
1538
CA
TYR
B
16
31.413
0.244
12.724
1.00
25.59
B


ATOM
1539
CB
TYR
B
16
31.539
−0.223
11.274
1.00
24.73
B


ATOM
1540
CG
TYR
B
16
32.958
−0.575
10.879
1.00
26.05
B


ATOM
1541
CD1
TYR
B
16
33.523
−1.795
11.239
1.00
22.96
B


ATOM
1542
CE1
TYR
B
16
34.843
−2.102
10.904
1.00
25.81
B


ATOM
1543
CD2
TYR
B
16
33.748
0.334
10.171
1.00
25.30
B


ATOM
1544
CE2
TYR
B
16
35.066
0.041
9.835
1.00
25.12
B


ATOM
1545
CZ
TYR
B
16
35.607
−1.176
10.202
1.00
26.66
B


ATOM
1546
OH
TYR
B
16
36.908
−1.463
9.868
1.00
29.22
B


ATOM
1547
C
TYR
B
16
29.960
0.575
13.045
1.00
26.48
B


ATOM
1548
O
TYR
B
16
29.113
−0.315
13.091
1.00
26.41
B


ATOM
1549
N
PHE
B
17
29.684
1.859
13.266
1.00
27.76
B


ATOM
1550
CA
PHE
B
17
28.346
2.338
13.613
1.00
29.09
B


ATOM
1551
CB
PHE
B
17
28.382
3.047
14.967
1.00
28.08
B


ATOM
1552
CG
PHE
B
17
28.885
2.194
16.091
1.00
28.21
B


ATOM
1553
CD1
PHE
B
17
28.056
1.253
16.693
1.00
27.20
B


ATOM
1554
CD2
PHE
B
17
30.188
2.340
16.558
1.00
26.60
B


ATOM
1555
CE1
PHE
B
17
28.519
0.470
17.752
1.00
28.13
B


ATOM
1556
CE2
PHE
B
17
30.662
1.565
17.610
1.00
25.62
B


ATOM
1557
CZ
PHE
B
17
29.828
0.629
18.210
1.00
26.17
B


ATOM
1558
C
PHE
B
17
27.772
3.318
12.592
1.00
30.71
B


ATOM
1559
O
PHE
B
17
28.452
4.239
12.155
1.00
31.05
B


ATOM
1560
N
THR
B
18
26.506
3.125
12.237
1.00
33.51
B


ATOM
1561
CA
THR
B
18
25.831
4.005
11.291
1.00
36.95
B


ATOM
1562
CB
THR
B
18
25.797
3.395
9.875
1.00
37.23
B


ATOM
1563
OG1
THR
B
18
27.133
3.105
9.447
1.00
40.77
B


ATOM
1564
CG2
THR
B
18
25.171
4.369
8.891
1.00
38.43
B


ATOM
1565
C
THR
B
18
24.398
4.273
11.753
1.00
38.56
B


ATOM
1566
O
THR
B
18
23.671
3.351
12.131
1.00
38.36
B


ATOM
1567
N
ASN
B
19
24.007
5.544
11.726
1.00
39.80
B


ATOM
1568
CA
ASN
B
19
22.668
5.961
12.132
1.00
41.35
B


ATOM
1569
CB
ASN
B
19
21.638
5.465
11.110
1.00
41.21
B


ATOM
1570
CG
ASN
B
19
20.311
6.190
11.223
1.00
42.85
B


ATOM
1571
OD1
ASN
B
19
20.271
7.378
11.548
1.00
42.24
B


ATOM
1572
ND2
ASN
B
19
19.219
5.485
10.937
1.00
42.57
B


ATOM
1573
C
ASN
B
19
22.352
5.416
13.521
1.00
42.37
B


ATOM
1574
O
ASN
B
19
21.540
4.503
13.673
1.00
43.36
B


ATOM
1575
N
GLY
B
20
22.997
5.989
14.533
1.00
42.56
B


ATOM
1576
CA
GLY
B
20
22.790
5.535
15.894
1.00
43.89
B


ATOM
1577
C
GLY
B
20
23.293
4.110
16.031
1.00
45.10
B


ATOM
1578
O
GLY
B
20
24.421
3.807
15.646
1.00
44.28
B


ATOM
1579
N
THR
B
21
22.458
3.232
16.575
1.00
46.37
B


ATOM
1580
CA
THR
B
21
22.824
1.832
16.738
1.00
47.42
B


ATOM
1581
CB
THR
B
21
22.667
1.373
18.199
1.00
48.57
B


ATOM
1582
OG1
THR
B
21
21.438
1.885
18.731
1.00
49.14
B


ATOM
1583
CG2
THR
B
21
23.843
1.856
19.043
1.00
47.59
B


ATOM
1584
C
THR
B
21
21.958
0.947
15.846
1.00
48.74
B


ATOM
1585
O
THR
B
21
21.925
−0.276
16.016
1.00
48.04
B


ATOM
1586
N
GLU
B
22
21.253
1.570
14.902
1.00
48.57
B


ATOM
1587
CA
GLU
B
22
20.405
0.822
13.979
1.00
48.90
B


ATOM
1588
CB
GLU
B
22
19.741
1.745
12.957
1.00
52.60
B


ATOM
1589
CG
GLU
B
22
18.669
2.667
13.493
1.00
58.06
B


ATOM
1590
CD
GLU
B
22
17.862
3.297
12.368
1.00
62.27
B


ATOM
1591
OE1
GLU
B
22
17.027
4.185
12.648
1.00
63.99
B


ATOM
1592
OE2
GLU
B
22
18.065
2.894
11.199
1.00
64.70
B


ATOM
1593
C
GLU
B
22
21.285
−0.156
13.229
1.00
46.38
B


ATOM
1594
O
GLU
B
22
21.029
−1.356
13.209
1.00
45.52
B


ATOM
1595
N
ARG
B
23
22.324
0.379
12.601
1.00
45.42
B


ATOM
1596
CA
ARG
B
23
23.260
−0.438
11.844
1.00
44.59
B


ATOM
1597
CB
ARG
B
23
23.423
0.127
10.422
1.00
45.69
B


ATOM
1598
CG
ARG
B
23
22.169
−0.062
9.554
1.00
49.95
B


ATOM
1599
CD
ARG
B
23
22.406
0.237
8.074
1.00
53.34
B


ATOM
1600
NE
ARG
B
23
22.153
1.632
7.708
1.00
55.57
B


ATOM
1601
CZ
ARG
B
23
20.949
2.200
7.700
1.00
57.20
B


ATOM
1602
NH1
ARG
B
23
19.878
1.495
8.042
1.00
58.09
B


ATOM
1603
NH2
ARG
B
23
20.813
3.471
7.340
1.00
56.82
B


ATOM
1604
C
ARG
B
23
24.606
−0.534
12.567
1.00
40.56
B


ATOM
1605
O
ARG
B
23
25.306
0.459
12.748
1.00
41.15
B


ATOM
1606
N
VAL
B
24
24.944
−1.743
12.995
1.00
38.17
B


ATOM
1607
CA
VAL
B
24
26.191
−1.996
13.708
1.00
34.88
B


ATOM
1608
CB
VAL
B
24
25.931
−2.314
15.200
1.00
34.41
B


ATOM
1609
CG1
VAL
B
24
27.251
−2.526
15.918
1.00
35.28
B


ATOM
1610
CG2
VAL
B
24
25.146
−1.190
15.852
1.00
34.70
B


ATOM
1611
C
VAL
B
24
26.909
−3.194
13.100
1.00
32.34
B


ATOM
1612
O
VAL
B
24
26.287
−4.214
12.812
1.00
33.23
B


ATOM
1613
N
ARG
B
25
28.217
−3.076
12.898
1.00
30.18
B


ATOM
1614
CA
ARG
B
25
28.970
−4.194
12.354
1.00
26.97
B


ATOM
1615
CB
ARG
B
25
29.225
−4.022
10.852
1.00
27.67
B


ATOM
1616
CG
ARG
B
25
29.400
−5.362
10.170
1.00
29.58
B


ATOM
1617
CD
ARG
B
25
30.406
−5.363
9.052
1.00
31.26
B


ATOM
1618
NE
ARG
B
25
30.058
−4.454
7.974
1.00
33.12
B


ATOM
1619
CZ
ARG
B
25
30.415
−4.631
6.705
1.00
32.27
B


ATOM
1620
NH1
ARG
B
25
31.124
−5.695
6.346
1.00
31.13
B


ATOM
1621
NH2
ARG
B
25
30.087
−3.726
5.799
1.00
30.62
B


ATOM
1622
C
ARG
B
25
30.305
−4.402
13.065
1.00
24.10
B


ATOM
1623
O
ARG
B
25
31.095
−3.477
13.225
1.00
22.56
B


ATOM
1624
N
LEU
B
26
30.551
−5.630
13.495
1.00
22.65
B


ATOM
1625
CA
LEU
B
26
31.801
−5.942
14.163
1.00
22.38
B


ATOM
1626
CB
LEU
B
26
31.558
−6.888
15.345
1.00
20.25
B


ATOM
1627
CG
LEU
B
26
32.795
−7.389
16.100
1.00
19.86
B


ATOM
1628
CD1
LEU
B
26
32.452
−7.613
17.568
1.00
22.49
B


ATOM
1629
CD2
LEU
B
26
33.304
−8.665
15.464
1.00
18.43
B


ATOM
1630
C
LEU
B
26
32.726
−6.591
13.150
1.00
21.50
B


ATOM
1631
O
LEU
B
26
32.289
−7.402
12.342
1.00
22.83
B


ATOM
1632
N
VAL
B
27
33.998
−6.208
13.177
1.00
21.29
B


ATOM
1633
CA
VAL
B
27
34.984
−6.780
12.270
1.00
20.66
B


ATOM
1634
CB
VAL
B
27
35.178
−5.911
11.004
1.00
20.59
B


ATOM
1635
CG1
VAL
B
27
36.169
−6.576
10.069
1.00
19.45
B


ATOM
1636
CG2
VAL
B
27
33.849
−5.696
10.297
1.00
22.37
B


ATOM
1637
C
VAL
B
27
36.330
−6.885
12.988
1.00
22.39
B


ATOM
1638
O
VAL
B
27
37.046
−5.889
13.135
1.00
22.63
B


ATOM
1639
N
SER
B
28
36.673
−8.083
13.450
1.00
21.32
B


ATOM
1640
CA
SER
B
28
37.947
−8.259
14.130
1.00
21.51
B


ATOM
1641
CB
SER
B
28
37.831
−9.284
15.275
1.00
19.72
B


ATOM
1642
OG
SER
B
28
37.542
−10.581
14.819
1.00
24.33
B


ATOM
1643
C
SER
B
28
38.954
−8.693
13.074
1.00
21.25
B


ATOM
1644
O
SER
B
28
38.661
−9.537
12.229
1.00
19.44
B


ATOM
1645
N
ARG
B
29
40.137
−8.089
13.106
1.00
20.61
B


ATOM
1646
CA
ARG
B
29
41.158
−8.402
12.115
1.00
19.66
B


ATOM
1647
CB
ARG
B
29
41.418
−7.169
11.230
1.00
19.91
B


ATOM
1648
CG
ARG
B
29
40.178
−6.407
10.754
1.00
16.79
B


ATOM
1649
CD
ARG
B
29
40.608
−5.121
10.031
1.00
18.10
B


ATOM
1650
NE
ARG
B
29
39.487
−4.318
9.553
1.00
19.38
B


ATOM
1651
CZ
ARG
B
29
38.738
−4.619
8.497
1.00
20.62
B


ATOM
1652
NH1
ARG
B
29
38.983
−5.714
7.789
1.00
19.50
B


ATOM
1653
NH2
ARG
B
29
37.736
−3.822
8.149
1.00
21.90
B


ATOM
1654
C
ARG
B
29
42.482
−8.833
12.738
1.00
18.57
B


ATOM
1655
O
ARG
B
29
43.024
−8.121
13.584
1.00
19.40
B


ATOM
1656
N
SER
B
30
42.991
−9.995
12.326
1.00
18.99
B


ATOM
1657
CA
SER
B
30
44.284
−10.501
12.797
1.00
21.66
B


ATOM
1658
CB
SER
B
30
44.241
−12.015
13.023
1.00
22.77
B


ATOM
1659
OG
SER
B
30
43.390
−12.352
14.106
1.00
26.81
B


ATOM
1660
C
SER
B
30
45.265
−10.163
11.673
1.00
23.37
B


ATOM
1661
O
SER
B
30
45.055
−10.553
10.522
1.00
21.31
B


ATOM
1662
N
ILE
B
31
46.338
−9.450
12.009
1.00
24.76
B


ATOM
1663
CA
ILE
B
31
47.298
−8.998
10.999
1.00
24.33
B


ATOM
1664
CB
ILE
B
31
47.341
−7.440
10.958
1.00
25.20
B


ATOM
1665
CG2
ILE
B
31
47.982
−6.964
9.672
1.00
23.24
B


ATOM
1666
CG1
ILE
B
31
45.934
−6.857
11.106
1.00
26.96
B


ATOM
1667
CD1
ILE
B
31
45.032
−7.136
9.947
1.00
31.25
B


ATOM
1668
C
ILE
B
31
48.741
−9.460
11.187
1.00
23.98
B


ATOM
1669
O
ILE
B
31
49.298
−9.318
12.272
1.00
22.29
B


ATOM
1670
N
TYR
B
32
49.345
−9.993
10.123
1.00
25.50
B


ATOM
1671
CA
TYR
B
32
50.750
−10.405
10.162
1.00
26.21
B


ATOM
1672
CB
TYR
B
32
50.965
−11.764
9.492
1.00
28.46
B


ATOM
1673
CG
TYR
B
32
52.406
−12.224
9.544
1.00
31.10
B


ATOM
1674
CD1
TYR
B
32
53.050
−12.412
10.765
1.00
32.47
B


ATOM
1675
CE1
TYR
B
32
54.393
−12.780
10.827
1.00
34.69
B


ATOM
1676
CD2
TYR
B
32
53.140
−12.424
8.375
1.00
33.60
B


ATOM
1677
CE2
TYR
B
32
54.484
−12.795
8.422
1.00
34.50
B


ATOM
1678
CZ
TYR
B
32
55.103
−12.965
9.654
1.00
35.65
B


ATOM
1679
OH
TYR
B
32
56.438
−13.281
9.717
1.00
37.73
B


ATOM
1680
C
TYR
B
32
51.478
−9.307
9.384
1.00
25.67
B


ATOM
1681
O
TYR
B
32
51.273
−9.140
8.174
1.00
24.75
B


ATOM
1682
N
ASN
B
33
52.319
−8.559
10.094
1.00
25.63
B


ATOM
1683
CA
ASN
B
33
53.036
−7.416
9.526
1.00
24.95
B


ATOM
1684
CB
ASN
B
33
53.955
−7.848
8.379
1.00
23.75
B


ATOM
1685
CG
ASN
B
33
55.171
−8.615
8.878
1.00
24.11
B


ATOM
1686
OD1
ASN
B
33
55.803
−8.223
9.861
1.00
25.42
B


ATOM
1687
ND2
ASN
B
33
55.506
−9.708
8.204
1.00
25.18
B


ATOM
1688
C
ASN
B
33
51.990
−6.392
9.070
1.00
25.11
B


ATOM
1689
O
ASN
B
33
51.491
−5.618
9.893
1.00
26.06
B


ATOM
1690
N
ARG
B
34
51.652
−6.375
7.786
1.00
25.75
B


ATOM
1691
CA
ARG
B
34
50.631
−5.449
7.296
1.00
27.64
B


ATOM
1692
CB
ARG
B
34
51.244
−4.362
6.408
1.00
27.74
B


ATOM
1693
CG
ARG
B
34
51.972
−3.257
7.158
1.00
29.94
B


ATOM
1694
CD
ARG
B
34
51.664
−1.888
6.541
1.00
32.95
B


ATOM
1695
NE
ARG
B
34
51.897
−1.875
5.101
1.00
35.17
B


ATOM
1696
CZ
ARG
B
34
51.392
−0.973
4.267
1.00
37.51
B


ATOM
1697
NH1
ARG
B
34
50.622
0.003
4.729
1.00
39.45
B


ATOM
1698
NH2
ARG
B
34
51.642
−1.058
2.967
1.00
36.90
B


ATOM
1699
C
ARG
B
34
49.587
−6.218
6.498
1.00
26.48
B


ATOM
1700
O
ARG
B
34
48.740
−5.639
5.825
1.00
27.17
B


ATOM
1701
N
GLU
B
35
49.647
−7.534
6.602
1.00
25.66
B


ATOM
1702
CA
GLU
B
35
48.746
−8.394
5.867
1.00
26.99
B


ATOM
1703
CB
GLU
B
35
49.570
−9.483
5.175
1.00
31.53
B


ATOM
1704
CG
GLU
B
35
48.814
−10.396
4.235
1.00
36.29
B


ATOM
1705
CD
GLU
B
35
49.695
−11.530
3.731
1.00
40.61
B


ATOM
1706
OE1
GLU
B
35
50.825
−11.240
3.276
1.00
45.20
B


ATOM
1707
OE2
GLU
B
35
49.266
−12.705
3.791
1.00
41.13
B


ATOM
1708
C
GLU
B
35
47.699
−9.031
6.764
1.00
25.09
B


ATOM
1709
O
GLU
B
35
48.028
−9.807
7.663
1.00
23.31
B


ATOM
1710
N
GLU
B
36
46.439
−8.689
6.522
1.00
24.53
B


ATOM
1711
CA
GLU
B
36
45.332
−9.263
7.275
1.00
25.73
B


ATOM
1712
CB
GLU
B
36
44.023
−8.519
6.958
1.00
26.62
B


ATOM
1713
CG
GLU
B
36
42.783
−9.095
7.636
1.00
28.26
B


ATOM
1714
CD
GLU
B
36
41.545
−8.232
7.442
1.00
31.08
B


ATOM
1715
OE1
GLU
B
36
41.420
−7.590
6.377
1.00
32.56
B


ATOM
1716
OE2
GLU
B
36
40.685
−8.206
8.349
1.00
32.83
B


ATOM
1717
C
GLU
B
36
45.238
−10.717
6.822
1.00
24.67
B


ATOM
1718
O
GLU
B
36
45.141
−10.992
5.626
1.00
23.91
B


ATOM
1719
N
ILE
B
37
45.282
−11.647
7.771
1.00
26.11
B


ATOM
1720
CA
ILE
B
37
45.219
−13.067
7.433
1.00
27.80
B


ATOM
1721
CB
ILE
B
37
46.444
−13.822
8.013
1.00
27.27
B


ATOM
1722
CG2
ILE
B
37
47.728
−13.174
7.516
1.00
27.41
B


ATOM
1723
CG1
ILE
B
37
46.440
−13.767
9.537
1.00
29.35
B


ATOM
1724
CD1
ILE
B
37
47.596
−14.509
10.175
1.00
30.27
B


ATOM
1725
C
ILE
B
37
43.922
−13.750
7.879
1.00
27.86
B


ATOM
1726
O
ILE
B
37
43.445
−14.674
7.221
1.00
28.29
B


ATOM
1727
N
VAL
B
38
43.348
−13.296
8.989
1.00
28.78
B


ATOM
1728
CA
VAL
B
38
42.097
−13.870
9.487
1.00
29.29
B


ATOM
1729
CB
VAL
B
38
42.294
−14.751
10.741
1.00
30.18
B


ATOM
1730
CG1
VAL
B
38
40.983
−15.452
11.071
1.00
33.17
B


ATOM
1731
CG2
VAL
B
38
43.399
−15.764
10.520
1.00
31.09
B


ATOM
1732
C
VAL
B
38
41.161
−12.745
9.882
1.00
28.75
B


ATOM
1733
O
VAL
B
38
41.585
−11.758
10.480
1.00
29.70
B


ATOM
1734
N
ARG
B
39
39.881
−12.911
9.581
1.00
27.05
B


ATOM
1735
CA
ARG
B
39
38.895
−11.890
9.892
1.00
25.46
B


ATOM
1736
CB
ARG
B
39
38.627
−11.064
8.632
1.00
27.23
B


ATOM
1737
CG
ARG
B
39
37.544
−10.011
8.765
1.00
30.84
B


ATOM
1738
CD
ARG
B
39
37.111
−9.476
7.398
1.00
29.34
B


ATOM
1739
NE
ARG
B
39
38.218
−8.861
6.673
1.00
30.83
B


ATOM
1740
CZ
ARG
B
39
38.116
−8.328
5.459
1.00
31.23
B


ATOM
1741
NH1
ARG
B
39
36.951
−8.333
4.823
1.00
31.08
B


ATOM
1742
NH2
ARG
B
39
39.178
−7.779
4.883
1.00
30.81
B


ATOM
1743
C
ARG
B
39
37.573
−12.476
10.381
1.00
25.41
B


ATOM
1744
O
ARG
B
39
37.192
−13.587
9.996
1.00
25.06
B


ATOM
1745
N
PHE
B
40
36.890
−11.742
11.252
1.00
23.72
B


ATOM
1746
CA
PHE
B
40
35.569
−12.164
11.696
1.00
24.04
B


ATOM
1747
CB
PHE
B
40
35.498
−12.554
13.171
1.00
22.69
B


ATOM
1748
CG
PHE
B
40
34.133
−13.036
13.573
1.00
20.75
B


ATOM
1749
CD1
PHE
B
40
33.777
−14.370
13.413
1.00
21.07
B


ATOM
1750
CD2
PHE
B
40
33.162
−12.135
14.003
1.00
21.00
B


ATOM
1751
CE1
PHE
B
40
32.475
−14.800
13.670
1.00
20.86
B


ATOM
1752
CE2
PHE
B
40
31.858
−12.553
14.261
1.00
19.95
B


ATOM
1753
CZ
PHE
B
40
31.517
−13.890
14.092
1.00
19.78
B


ATOM
1754
C
PHE
B
40
34.662
−10.969
11.474
1.00
24.27
B


ATOM
1755
O
PHE
B
40
34.755
−9.970
12.183
1.00
22.94
B


ATOM
1756
N
ASP
B
41
33.800
−11.088
10.471
1.00
24.75
B


ATOM
1757
CA
ASP
B
41
32.857
−10.040
10.101
1.00
24.98
B


ATOM
1758
CB
ASP
B
41
32.863
−9.881
8.578
1.00
25.64
B


ATOM
1759
CG
ASP
B
41
32.162
−8.626
8.116
1.00
27.70
B


ATOM
1760
OD1
ASP
B
41
31.163
−8.227
8.749
1.00
26.21
B


ATOM
1761
OD2
ASP
B
41
32.607
−8.045
7.102
1.00
30.42
B


ATOM
1762
C
ASP
B
41
31.477
−10.497
10.560
1.00
24.50
B


ATOM
1763
O
ASP
B
41
31.011
−11.558
10.151
1.00
24.95
B


ATOM
1764
N
SER
B
42
30.822
−9.710
11.404
1.00
24.16
B


ATOM
1765
CA
SER
B
42
29.501
−10.096
11.882
1.00
26.13
B


ATOM
1766
CB
SER
B
42
29.013
−9.133
12.972
1.00
24.53
B


ATOM
1767
OG
SER
B
42
28.932
−7.806
12.497
1.00
23.39
B


ATOM
1768
C
SER
B
42
28.497
−10.149
10.729
1.00
27.68
B


ATOM
1769
O
SER
B
42
27.474
−10.833
10.818
1.00
27.31
B


ATOM
1770
N
ASP
B
43
28.789
−9.419
9.654
1.00
28.17
B


ATOM
1771
CA
ASP
B
43
27.924
−9.413
8.477
1.00
29.40
B


ATOM
1772
CB
ASP
B
43
28.332
−8.298
7.508
1.00
29.57
B


ATOM
1773
CG
ASP
B
43
27.587
−7.006
7.766
1.00
32.71
B


ATOM
1774
OD1
ASP
B
43
26.999
−6.868
8.862
1.00
33.94
B


ATOM
1775
OD2
ASP
B
43
27.593
−6.120
6.881
1.00
33.98
B


ATOM
1776
C
ASP
B
43
28.036
−10.762
7.782
1.00
29.46
B


ATOM
1777
O
ASP
B
43
27.162
−11.150
7.009
1.00
30.77
B


ATOM
1778
N
VAL
B
44
29.123
−11.471
8.068
1.00
27.98
B


ATOM
1779
CA
VAL
B
44
29.365
−12.780
7.486
1.00
27.16
B


ATOM
1780
CB
VAL
B
44
30.846
−12.939
7.075
1.00
27.32
B


ATOM
1781
CG1
VAL
B
44
31.083
−14.323
6.488
1.00
24.09
B


ATOM
1782
CG2
VAL
B
44
31.218
−11.857
6.073
1.00
24.66
B


ATOM
1783
C
VAL
B
44
28.990
−13.867
8.490
1.00
28.43
B


ATOM
1784
O
VAL
B
44
28.558
−14.948
8.108
1.00
29.45
B


ATOM
1785
N
GLY
B
45
29.177
−13.590
9.774
1.00
28.05
B


ATOM
1786
CA
GLY
B
45
28.794
−14.561
10.780
1.00
28.67
B


ATOM
1787
C
GLY
B
45
29.758
−15.679
11.125
1.00
28.25
B


ATOM
1788
O
GLY
B
45
29.458
−16.486
12.002
1.00
29.67
B


ATOM
1789
N
GLU
B
46
30.895
−15.755
10.443
1.00
27.03
B


ATOM
1790
CA
GLU
B
46
31.873
−16.787
10.757
1.00
29.26
B


ATOM
1791
CB
GLU
B
46
31.571
−18.087
10.000
1.00
32.16
B


ATOM
1792
CG
GLU
B
46
32.039
−18.121
8.554
1.00
37.36
B


ATOM
1793
CD
GLU
B
46
31.752
−19.458
7.885
1.00
41.59
B


ATOM
1794
OE1
GLU
B
46
32.163
−20.505
8.433
1.00
43.30
B


ATOM
1795
OE2
GLU
B
46
31.116
−19.463
6.810
1.00
43.54
B


ATOM
1796
C
GLU
B
46
33.272
−16.295
10.413
1.00
29.29
B


ATOM
1797
O
GLU
B
46
33.432
−15.288
9.722
1.00
30.45
B


ATOM
1798
N
PHE
B
47
34.281
−17.005
10.904
1.00
28.00
B


ATOM
1799
CA
PHE
B
47
35.670
−16.650
10.651
1.00
28.10
B


ATOM
1800
CB
PHE
B
47
36.594
−17.445
11.566
1.00
28.74
B


ATOM
1801
CG
PHE
B
47
36.487
−17.067
13.016
1.00
30.23
B


ATOM
1802
CD1
PHE
B
47
37.248
−16.023
13.535
1.00
28.96
B


ATOM
1803
CD2
PHE
B
47
35.636
−17.768
13.870
1.00
30.80
B


ATOM
1804
CE1
PHE
B
47
37.166
−15.683
14.888
1.00
31.59
B


ATOM
1805
CE2
PHE
B
47
35.544
−17.435
15.229
1.00
31.97
B


ATOM
1806
CZ
PHE
B
47
36.311
−16.392
15.737
1.00
30.36
B


ATOM
1807
C
PHE
B
47
36.034
−16.948
9.211
1.00
28.71
B


ATOM
1808
O
PHE
B
47
35.576
−17.937
8.640
1.00
28.03
B


ATOM
1809
N
ARG
B
48
36.872
−16.091
8.637
1.00
27.96
B


ATOM
1810
CA
ARG
B
48
37.327
−16.242
7.261
1.00
26.41
B


ATOM
1811
CB
ARG
B
48
36.513
−15.341
6.326
1.00
26.57
B


ATOM
1812
CG
ARG
B
48
35.068
−15.755
6.108
1.00
26.19
B


ATOM
1813
CD
ARG
B
48
34.971
−17.079
5.352
1.00
24.98
B


ATOM
1814
NE
ARG
B
48
33.579
−17.465
5.146
1.00
26.01
B


ATOM
1815
CZ
ARG
B
48
32.755
−16.867
4.294
1.00
26.84
B


ATOM
1816
NH1
ARG
B
48
33.181
−15.857
3.554
1.00
26.92
B


ATOM
1817
NH2
ARG
B
48
31.492
−17.260
4.204
1.00
30.22
B


ATOM
1818
C
ARG
B
48
38.799
−15.861
7.140
1.00
26.95
B


ATOM
1819
O
ARG
B
48
39.255
−14.878
7.737
1.00
24.36
B


ATOM
1820
N
ALA
B
49
39.542
−16.647
6.373
1.00
24.93
B


ATOM
1821
CA
ALA
B
49
40.943
−16.349
6.143
1.00
26.58
B


ATOM
1822
CB
ALA
B
49
41.709
−17.619
5.792
1.00
27.05
B


ATOM
1823
C
ALA
B
49
40.927
−15.397
4.956
1.00
26.47
B


ATOM
1824
O
ALA
B
49
40.210
−15.635
3.983
1.00
26.12
B


ATOM
1825
N
VAL
B
50
41.674
−14.302
5.044
1.00
27.06
B


ATOM
1826
CA
VAL
B
50
41.720
−13.357
3.936
1.00
26.50
B


ATOM
1827
CB
VAL
B
50
41.790
−11.876
4.439
1.00
27.14
B


ATOM
1828
CG1
VAL
B
50
42.327
−11.827
5.846
1.00
29.89
B


ATOM
1829
CG2
VAL
B
50
42.628
−11.020
3.501
1.00
27.33
B


ATOM
1830
C
VAL
B
50
42.891
−13.742
3.037
1.00
26.58
B


ATOM
1831
O
VAL
B
50
42.914
−13.390
1.860
1.00
27.84
B


ATOM
1832
N
THR
B
51
43.842
−14.489
3.598
1.00
26.61
B


ATOM
1833
CA
THR
B
51
44.992
−15.011
2.846
1.00
28.59
B


ATOM
1834
CB
THR
B
51
46.295
−14.193
3.056
1.00
28.25
B


ATOM
1835
OG1
THR
B
51
46.828
−14.464
4.356
1.00
28.56
B


ATOM
1836
CG2
THR
B
51
46.033
−12.699
2.899
1.00
27.40
B


ATOM
1837
C
THR
B
51
45.256
−16.435
3.344
1.00
29.29
B


ATOM
1838
O
THR
B
51
44.787
−16.818
4.418
1.00
30.16
B


ATOM
1839
N
LEU
B
52
46.005
−17.217
2.575
1.00
30.64
B


ATOM
1840
CA
LEU
B
52
46.309
−18.596
2.959
1.00
31.32
B


ATOM
1841
CB
LEU
B
52
47.277
−19.237
1.963
1.00
32.19
B


ATOM
1842
CG
LEU
B
52
46.706
−19.724
0.624
1.00
36.90
B


ATOM
1843
CD1
LEU
B
52
47.836
−20.306
−0.216
1.00
35.68
B


ATOM
1844
CD2
LEU
B
52
45.620
−20.775
0.861
1.00
35.34
B


ATOM
1845
C
LEU
B
52
46.892
−18.724
4.359
1.00
31.57
B


ATOM
1846
O
LEU
B
52
46.570
−19.656
5.097
1.00
31.50
B


ATOM
1847
N
LEU
B
53
47.753
−17.786
4.723
1.00
31.09
B


ATOM
1848
CA
LEU
B
53
48.388
−17.815
6.029
1.00
30.93
B


ATOM
1849
CB
LEU
B
53
49.160
−16.511
6.246
1.00
31.99
B


ATOM
1850
CG
LEU
B
53
50.338
−16.532
7.221
1.00
35.20
B


ATOM
1851
CD1
LEU
B
53
51.364
−17.559
6.763
1.00
35.92
B


ATOM
1852
CD2
LEU
B
53
50.975
−15.148
7.284
1.00
34.96
B


ATOM
1853
C
LEU
B
53
47.377
−18.017
7.160
1.00
29.90
B


ATOM
1854
O
LEU
B
53
47.663
−18.709
8.138
1.00
30.68
B


ATOM
1855
N
GLY
B
54
46.192
−17.430
7.015
1.00
28.63
B


ATOM
1856
CA
GLY
B
54
45.181
−17.537
8.057
1.00
29.75
B


ATOM
1857
C
GLY
B
54
44.140
−18.635
7.901
1.00
30.44
B


ATOM
1858
O
GLY
B
54
43.146
−18.664
8.630
1.00
28.02
B


ATOM
1859
N
LEU
B
55
44.364
−19.547
6.964
1.00
30.54
B


ATOM
1860
CA
LEU
B
55
43.417
−20.630
6.732
1.00
32.59
B


ATOM
1861
CB
LEU
B
55
43.765
−21.344
5.422
1.00
35.94
B


ATOM
1862
CG
LEU
B
55
42.776
−22.383
4.889
1.00
38.88
B


ATOM
1863
CD1
LEU
B
55
41.355
−21.831
4.927
1.00
38.23
B


ATOM
1864
CD2
LEU
B
55
43.173
−22.766
3.467
1.00
39.03
B


ATOM
1865
C
LEU
B
55
43.330
−21.631
7.892
1.00
32.20
B


ATOM
1866
O
LEU
B
55
42.235
−22.026
8.291
1.00
33.32
B


ATOM
1867
N
PRO
B
56
44.478
−22.058
8.447
1.00
31.03
B


ATOM
1868
CD
PRO
B
56
45.862
−21.802
8.009
1.00
30.17
B


ATOM
1869
CA
PRO
B
56
44.451
−23.013
9.561
1.00
30.23
B


ATOM
1870
CB
PRO
B
56
45.925
−23.148
9.931
1.00
30.27
B


ATOM
1871
CG
PRO
B
56
46.609
−22.967
8.610
1.00
28.92
B


ATOM
1872
C
PRO
B
56
43.613
−22.525
10.740
1.00
31.42
B


ATOM
1873
O
PRO
B
56
42.730
−23.237
11.222
1.00
33.17
B


ATOM
1874
N
ALA
B
57
43.893
−21.305
11.196
1.00
30.04
B


ATOM
1875
CA
ALA
B
57
43.181
−20.719
12.322
1.00
28.60
B


ATOM
1876
CB
ALA
B
57
43.818
−19.389
12.697
1.00
26.81
B


ATOM
1877
C
ALA
B
57
41.695
−20.528
12.021
1.00
29.08
B


ATOM
1878
O
ALA
B
57
40.847
−20.737
12.887
1.00
28.22
B


ATOM
1879
N
ALA
B
58
41.385
−20.135
10.791
1.00
28.84
B


ATOM
1880
CA
ALA
B
58
40.002
−19.922
10.386
1.00
31.06
B


ATOM
1881
CB
ALA
B
58
39.955
−19.426
8.947
1.00
29.79
B


ATOM
1882
C
ALA
B
58
39.169
−21.199
10.529
1.00
32.38
B


ATOM
1883
O
ALA
B
58
38.113
−21.197
11.170
1.00
31.57
B


ATOM
1884
N
GLU
B
59
39.647
−22.285
9.929
1.00
33.50
B


ATOM
1885
CA
GLU
B
59
38.949
−23.565
9.993
1.00
33.91
B


ATOM
1886
CB
GLU
B
59
39.706
−24.622
9.195
1.00
35.67
B


ATOM
1887
CG
GLU
B
59
39.619
−24.457
7.696
1.00
39.73
B


ATOM
1888
CD
GLU
B
59
40.327
−25.583
6.957
1.00
43.58
B


ATOM
1889
OE1
GLU
B
59
41.561
−25.715
7.119
1.00
44.52
B


ATOM
1890
OE2
GLU
B
59
39.648
−26.337
6.222
1.00
44.30
B


ATOM
1891
C
GLU
B
59
38.771
−24.063
11.425
1.00
33.56
B


ATOM
1892
O
GLU
B
59
37.708
−24.570
11.790
1.00
34.40
B


ATOM
1893
N
TYR
B
60
39.815
−23.923
12.233
1.00
31.99
B


ATOM
1894
CA
TYR
B
60
39.754
−24.369
13.611
1.00
31.01
B


ATOM
1895
CB
TYR
B
60
41.112
−24.202
14.292
1.00
31.13
B


ATOM
1896
CG
TYR
B
60
41.051
−24.548
15.750
1.00
30.99
B


ATOM
1897
CD1
TYR
B
60
40.919
−25.871
16.162
1.00
32.55
B


ATOM
1898
CE1
TYR
B
60
40.770
−26.192
17.508
1.00
35.39
B


ATOM
1899
CD2
TYR
B
60
41.039
−23.550
16.716
1.00
32.67
B


ATOM
1900
CE2
TYR
B
60
40.890
−23.853
18.064
1.00
35.14
B


ATOM
1901
CZ
TYR
B
60
40.756
−25.177
18.455
1.00
36.91
B


ATOM
1902
OH
TYR
B
60
40.606
−25.483
19.791
1.00
40.06
B


ATOM
1903
C
TYR
B
60
38.695
−23.631
14.426
1.00
31.72
B


ATOM
1904
O
TYR
B
60
37.840
−24.258
15.050
1.00
31.72
B


ATOM
1905
N
TRP
B
61
38.752
−22.303
14.428
1.00
30.37
B


ATOM
1906
CA
TRP
B
61
37.790
−21.525
15.194
1.00
31.57
B


ATOM
1907
CB
TRP
B
61
38.129
−20.024
15.140
1.00
32.14
B


ATOM
1908
CG
TRP
B
61
39.430
−19.666
15.824
1.00
33.73
B


ATOM
1909
CD2
TRP
B
61
40.359
−18.648
15.429
1.00
35.16
B


ATOM
1910
CE2
TRP
B
61
41.418
−18.662
16.362
1.00
35.99
B


ATOM
1911
CE3
TRP
B
61
40.397
−17.719
14.378
1.00
38.30
B


ATOM
1912
CD1
TRP
B
61
39.949
−20.236
16.949
1.00
33.63
B


ATOM
1913
NE1
TRP
B
61
41.142
−19.642
17.278
1.00
33.97
B


ATOM
1914
CZ2
TRP
B
61
42.512
−17.782
16.277
1.00
38.13
B


ATOM
1915
CZ3
TRP
B
61
41.487
−16.836
14.293
1.00
39.26
B


ATOM
1916
CH2
TRP
B
61
42.527
−16.879
15.240
1.00
38.22
B


ATOM
1917
C
TRP
B
61
36.349
−21.758
14.739
1.00
31.22
B


ATOM
1918
O
TRP
B
61
35.436
−21.758
15.559
1.00
29.98
B


ATOM
1919
N
ASN
B
62
36.137
−21.955
13.440
1.00
31.63
B


ATOM
1920
CA
ASN
B
62
34.781
−22.191
12.950
1.00
32.57
B


ATOM
1921
CB
ASN
B
62
34.701
−22.021
11.434
1.00
30.37
B


ATOM
1922
CG
ASN
B
62
34.575
−20.574
11.025
1.00
29.69
B


ATOM
1923
OD1
ASN
B
62
33.889
−19.794
11.680
1.00
29.42
B


ATOM
1924
ND2
ASN
B
62
35.222
−20.209
9.926
1.00
31.50
B


ATOM
1925
C
ASN
B
62
34.238
−23.561
13.339
1.00
32.87
B


ATOM
1926
O
ASN
B
62
33.028
−23.789
13.292
1.00
34.70
B


ATOM
1927
N
SER
B
63
35.128
−24.469
13.725
1.00
32.43
B


ATOM
1928
CA
SER
B
63
34.705
−25.797
14.140
1.00
32.38
B


ATOM
1929
CB
SER
B
63
35.818
−26.819
13.879
1.00
32.20
B


ATOM
1930
OG
SER
B
63
36.905
−26.626
14.760
1.00
33.33
B


ATOM
1931
C
SER
B
63
34.348
−25.768
15.630
1.00
32.14
B


ATOM
1932
O
SER
B
63
33.677
−26.667
16.138
1.00
32.86
B


ATOM
1933
N
GLN
B
64
34.794
−24.724
16.325
1.00
31.10
B


ATOM
1934
CA
GLN
B
64
34.513
−24.569
17.752
1.00
30.99
B


ATOM
1935
CB
GLN
B
64
35.661
−23.837
18.446
1.00
32.54
B


ATOM
1936
CG
GLN
B
64
36.988
−24.557
18.383
1.00
34.49
B


ATOM
1937
CD
GLN
B
64
36.870
−25.998
18.810
1.00
38.20
B


ATOM
1938
OE1
GLN
B
64
36.629
−26.884
17.984
1.00
40.82
B


ATOM
1939
NE2
GLN
B
64
37.022
−26.245
20.108
1.00
38.34
B


ATOM
1940
C
GLN
B
64
33.226
−23.775
17.944
1.00
29.88
B


ATOM
1941
O
GLN
B
64
33.252
−22.549
18.064
1.00
29.28
B


ATOM
1942
N
LYS
B
65
32.101
−24.476
17.979
1.00
28.74
B


ATOM
1943
CA
LYS
B
65
30.815
−23.812
18.123
1.00
29.18
B


ATOM
1944
CB
LYS
B
65
29.688
−24.851
18.132
1.00
30.63
B


ATOM
1945
CG
LYS
B
65
29.575
−25.612
16.812
1.00
32.20
B


ATOM
1946
CD
LYS
B
65
29.371
−24.654
15.629
1.00
34.44
B


ATOM
1947
CE
LYS
B
65
29.688
−25.327
14.284
1.00
37.24
B


ATOM
1948
NZ
LYS
B
65
29.430
−24.427
13.109
1.00
37.89
B


ATOM
1949
C
LYS
B
65
30.745
−22.919
19.352
1.00
28.19
B


ATOM
1950
O
LYS
B
65
30.075
−21.891
19.333
1.00
28.16
B


ATOM
1951
N
ASP
B
66
31.440
−23.304
20.417
1.00
27.58
B


ATOM
1952
CA
ASP
B
66
31.460
−22.504
21.636
1.00
27.41
B


ATOM
1953
CB
ASP
B
66
32.283
−23.208
22.727
1.00
28.45
B


ATOM
1954
CG
ASP
B
66
33.559
−23.847
22.184
1.00
32.24
B


ATOM
1955
OD1
ASP
B
66
33.478
−24.591
21.183
1.00
33.17
B


ATOM
1956
OD2
ASP
B
66
34.642
−23.623
22.765
1.00
33.25
B


ATOM
1957
C
ASP
B
66
32.050
−21.131
21.316
1.00
26.63
B


ATOM
1958
O
ASP
B
66
31.468
−20.102
21.662
1.00
24.32
B


ATOM
1959
N
ILE
B
67
33.198
−21.116
20.640
1.00
26.12
B


ATOM
1960
CA
ILE
B
67
33.840
−19.855
20.273
1.00
26.42
B


ATOM
1961
CB
ILE
B
67
35.206
−20.088
19.613
1.00
28.29
B


ATOM
1962
CG2
ILE
B
67
35.859
−18.753
19.290
1.00
28.54
B


ATOM
1963
CG1
ILE
B
67
36.094
−20.925
20.535
1.00
28.25
B


ATOM
1964
CD1
ILE
B
67
36.319
−20.321
21.906
1.00
32.66
B


ATOM
1965
C
ILE
B
67
32.968
−19.061
19.300
1.00
26.36
B


ATOM
1966
O
ILE
B
67
32.747
−17.869
19.491
1.00
25.33
B


ATOM
1967
N
LEU
B
68
32.472
−19.730
18.261
1.00
26.11
B


ATOM
1968
CA
LEU
B
68
31.617
−19.086
17.267
1.00
26.66
B


ATOM
1969
CB
LEU
B
68
31.132
−20.102
16.235
1.00
27.61
B


ATOM
1970
CG
LEU
B
68
31.807
−20.171
14.872
1.00
30.12
B


ATOM
1971
CD1
LEU
B
68
31.081
−21.216
14.031
1.00
33.09
B


ATOM
1972
CD2
LEU
B
68
31.766
−18.812
14.190
1.00
30.01
B


ATOM
1973
C
LEU
B
68
30.394
−18.415
17.878
1.00
26.81
B


ATOM
1974
O
LEU
B
68
30.067
−17.280
17.541
1.00
26.19
B


ATOM
1975
N
GLU
B
69
29.706
−19.135
18.756
1.00
28.87
B


ATOM
1976
CA
GLU
B
69
28.509
−18.614
19.404
1.00
31.55
B


ATOM
1977
CB
GLU
B
69
27.945
−19.654
20.382
1.00
35.75
B


ATOM
1978
CG
GLU
B
69
27.304
−20.862
19.695
1.00
43.71
B


ATOM
1979
CD
GLU
B
69
26.883
−21.954
20.673
1.00
47.92
B


ATOM
1980
OE1
GLU
B
69
27.756
−22.454
21.418
1.00
49.27
B


ATOM
1981
OE2
GLU
B
69
25.683
−22.316
20.694
1.00
50.44
B


ATOM
1982
C
GLU
B
69
28.773
−17.295
20.130
1.00
29.82
B


ATOM
1983
O
GLU
B
69
27.986
−16.356
20.027
1.00
27.91
B


ATOM
1984
N
ARG
B
70
29.886
−17.226
20.855
1.00
29.32
B


ATOM
1985
CA
ARG
B
70
30.239
−16.016
21.597
1.00
28.97
B


ATOM
1986
CB
ARG
B
70
31.347
−16.315
22.606
1.00
28.94
B


ATOM
1987
CG
ARG
B
70
30.982
−17.344
23.673
1.00
30.55
B


ATOM
1988
CD
ARG
B
70
32.251
−17.810
24.371
1.00
32.35
B


ATOM
1989
NE
ARG
B
70
32.040
−19.037
25.117
1.00
34.83
B


ATOM
1990
CZ
ARG
B
70
32.946
−19.997
25.232
1.00
34.98
B


ATOM
1991
NH1
ARG
B
70
34.131
−19.875
24.647
1.00
35.03
B


ATOM
1992
NH2
ARG
B
70
32.662
−21.083
25.930
1.00
39.48
B


ATOM
1993
C
ARG
B
70
30.691
−14.888
20.682
1.00
26.77
B


ATOM
1994
O
ARG
B
70
30.412
−13.725
20.951
1.00
26.95
B


ATOM
1995
N
LYS
B
71
31.395
−15.235
19.608
1.00
25.97
B


ATOM
1996
CA
LYS
B
71
31.885
−14.236
18.670
1.00
25.98
B


ATOM
1997
CB
LYS
B
71
32.830
−14.877
17.652
1.00
27.62
B


ATOM
1998
CG
LYS
B
71
33.728
−13.873
16.924
1.00
29.24
B


ATOM
1999
CD
LYS
B
71
34.628
−13.137
17.909
1.00
32.14
B


ATOM
2000
CE
LYS
B
71
35.430
−12.035
17.236
1.00
33.13
B


ATOM
2001
NZ
LYS
B
71
36.093
−11.164
18.245
1.00
34.18
B


ATOM
2002
C
LYS
B
71
30.710
−13.591
17.952
1.00
25.22
B


ATOM
2003
O
LYS
B
71
30.719
−12.395
17.671
1.00
24.39
B


ATOM
2004
N
ARG
B
72
29.701
−14.399
17.657
1.00
25.08
B


ATOM
2005
CA
ARG
B
72
28.500
−13.922
16.989
1.00
26.32
B


ATOM
2006
CB
ARG
B
72
27.628
−15.101
16.561
1.00
28.02
B


ATOM
2007
CG
ARG
B
72
28.116
−15.830
15.340
1.00
28.10
B


ATOM
2008
CD
ARG
B
72
27.225
−17.013
15.083
1.00
32.02
B


ATOM
2009
NE
ARG
B
72
27.451
−17.583
13.766
1.00
36.46
B


ATOM
2010
CZ
ARG
B
72
27.014
−18.779
13.389
1.00
38.62
B


ATOM
2011
NH1
ARG
B
72
26.324
−19.538
14.238
1.00
37.88
B


ATOM
2012
NH2
ARG
B
72
27.270
−19.212
12.163
1.00
38.55
B


ATOM
2013
C
ARG
B
72
27.687
−13.017
17.898
1.00
24.31
B


ATOM
2014
O
ARG
B
72
26.792
−12.326
17.439
1.00
24.84
B


ATOM
2015
N
ALA
B
73
27.990
−13.028
19.189
1.00
26.18
B


ATOM
2016
CA
ALA
B
73
27.267
−12.185
20.140
1.00
28.18
B


ATOM
2017
CB
ALA
B
73
26.973
−12.974
21.418
1.00
28.97
B


ATOM
2018
C
ALA
B
73
28.056
−10.916
20.472
1.00
28.97
B


ATOM
2019
O
ALA
B
73
27.528
−9.977
21.066
1.00
30.50
B


ATOM
2020
N
ALA
B
74
29.320
−10.882
20.070
1.00
29.65
B


ATOM
2021
CA
ALA
B
74
30.170
−9.732
20.347
1.00
30.77
B


ATOM
2022
CB
ALA
B
74
31.558
−9.966
19.764
1.00
30.77
B


ATOM
2023
C
ALA
B
74
29.594
−8.414
19.827
1.00
31.78
B


ATOM
2024
O
ALA
B
74
29.789
−7.359
20.438
1.00
32.74
B


ATOM
2025
N
VAL
B
75
28.886
−8.465
18.704
1.00
31.60
B


ATOM
2026
CA
VAL
B
75
28.308
−7.248
18.145
1.00
32.38
B


ATOM
2027
CB
VAL
B
75
27.397
−7.539
16.929
1.00
30.51
B


ATOM
2028
CG1
VAL
B
75
27.291
−6.295
16.062
1.00
31.44
B


ATOM
2029
CG2
VAL
B
75
27.931
−8.696
16.137
1.00
33.08
B


ATOM
2030
C
VAL
B
75
27.465
−6.529
19.201
1.00
33.07
B


ATOM
2031
O
VAL
B
75
27.402
−5.302
19.218
1.00
33.54
B


ATOM
2032
N
ASP
B
76
26.811
−7.302
20.065
1.00
34.70
B


ATOM
2033
CA
ASP
B
76
25.971
−6.748
21.130
1.00
36.27
B


ATOM
2034
CB
ASP
B
76
24.780
−7.670
21.420
1.00
38.57
B


ATOM
2035
CG
ASP
B
76
23.889
−7.881
20.215
1.00
41.48
B


ATOM
2036
OD1
ASP
B
76
23.335
−6.887
19.694
1.00
43.46
B


ATOM
2037
OD2
ASP
B
76
23.739
−9.048
19.792
1.00
43.76
B


ATOM
2038
C
ASP
B
76
26.780
−6.600
22.411
1.00
35.56
B


ATOM
2039
O
ASP
B
76
26.731
−5.569
23.081
1.00
34.13
B


ATOM
2040
N
ARG
B
77
27.508
−7.661
22.744
1.00
35.22
B


ATOM
2041
CA
ARG
B
77
28.343
−7.708
23.937
1.00
34.49
B


ATOM
2042
CB
ARG
B
77
29.071
−9.052
23.991
1.00
37.16
B


ATOM
2043
CG
ARG
B
77
29.841
−9.328
25.271
1.00
40.90
B


ATOM
2044
CD
ARG
B
77
30.735
−10.553
25.102
1.00
43.79
B


ATOM
2045
NE
ARG
B
77
30.004
−11.743
24.665
1.00
48.65
B


ATOM
2046
CZ
ARG
B
77
29.103
−12.385
25.406
1.00
51.36
B


ATOM
2047
NH1
ARG
B
77
28.816
−11.949
26.626
1.00
52.34
B


ATOM
2048
NH2
ARG
B
77
28.499
−13.470
24.935
1.00
50.76
B


ATOM
2049
C
ARG
B
77
29.362
−6.576
23.927
1.00
32.18
B


ATOM
2050
O
ARG
B
77
29.499
−5.835
24.896
1.00
32.49
B


ATOM
2051
N
VAL
B
78
30.073
−6.442
22.818
1.00
30.66
B


ATOM
2052
CA
VAL
B
78
31.086
−5.414
22.707
1.00
29.00
B


ATOM
2053
CB
VAL
B
78
32.276
−5.917
21.867
1.00
27.82
B


ATOM
2054
CG1
VAL
B
78
33.327
−4.815
21.740
1.00
25.08
B


ATOM
2055
CG2
VAL
B
78
32.870
−7.160
22.504
1.00
23.27
B


ATOM
2056
C
VAL
B
78
30.594
−4.093
22.113
1.00
29.33
B


ATOM
2057
O
VAL
B
78
30.435
−3.104
22.831
1.00
29.83
B


ATOM
2058
N
CYS
B
79
30.354
−4.091
20.804
1.00
28.42
B


ATOM
2059
CA
CYS
B
79
29.927
−2.891
20.083
1.00
29.14
B


ATOM
2060
C
CYS
B
79
28.724
−2.107
20.629
1.00
28.59
B


ATOM
2061
O
CYS
B
79
28.883
−0.961
21.062
1.00
26.06
B


ATOM
2062
CB
CYS
B
79
29.675
−3.219
18.604
1.00
29.19
B


ATOM
2063
SG
CYS
B
79
31.052
−3.983
17.680
1.00
31.71
B


ATOM
2064
N
ARG
B
80
27.527
−2.693
20.586
1.00
28.34
B


ATOM
2065
CA
ARG
B
80
26.347
−1.980
21.071
1.00
30.77
B


ATOM
2066
CB
ARG
B
80
25.079
−2.828
20.915
1.00
32.82
B


ATOM
2067
CG
ARG
B
80
24.612
−2.973
19.474
1.00
35.65
B


ATOM
2068
CD
ARG
B
80
23.120
−3.273
19.387
1.00
36.01
B


ATOM
2069
NE
ARG
B
80
22.649
−3.243
18.005
1.00
35.49
B


ATOM
2070
CZ
ARG
B
80
22.913
−4.188
17.108
1.00
37.80
B


ATOM
2071
NH1
ARG
B
80
23.640
−5.242
17.449
1.00
40.57
B


ATOM
2072
NH2
ARG
B
80
22.467
−4.075
15.864
1.00
38.86
B


ATOM
2073
C
ARG
B
80
26.507
−1.552
22.524
1.00
31.24
B


ATOM
2074
O
ARG
B
80
25.975
−0.525
22.944
1.00
32.07
B


ATOM
2075
N
HIS
B
81
27.257
−2.337
23.283
1.00
31.40
B


ATOM
2076
CA
HIS
B
81
27.492
−2.028
24.683
1.00
32.20
B


ATOM
2077
CB
HIS
B
81
28.220
−3.185
25.366
1.00
33.00
B


ATOM
2078
CG
HIS
B
81
28.595
−2.899
26.787
1.00
37.24
B


ATOM
2079
CD2
HIS
B
81
29.764
−2.490
27.335
1.00
38.05
B


ATOM
2080
ND1
HIS
B
81
27.692
−2.981
27.826
1.00
39.11
B


ATOM
2081
CE1
HIS
B
81
28.290
−2.635
28.952
1.00
40.49
B


ATOM
2082
NE2
HIS
B
81
29.548
−2.332
28.682
1.00
39.16
B


ATOM
2083
C
HIS
B
81
28.326
−0.762
24.831
1.00
30.87
B


ATOM
2084
O
HIS
B
81
27.906
0.206
25.470
1.00
31.38
B


ATOM
2085
N
ASN
B
82
29.511
−0.770
24.233
1.00
29.77
B


ATOM
2086
CA
ASN
B
82
30.403
0.375
24.332
1.00
28.02
B


ATOM
2087
CB
ASN
B
82
31.755
0.056
23.683
1.00
26.64
B


ATOM
2088
CG
ASN
B
82
32.470
−1.092
24.373
1.00
25.02
B


ATOM
2089
OD1
ASN
B
82
32.305
−1.305
25.572
1.00
24.06
B


ATOM
2090
ND2
ASN
B
82
33.278
−1.829
23.619
1.00
26.38
B


ATOM
2091
C
ASN
B
82
29.819
1.648
23.741
1.00
26.04
B


ATOM
2092
O
ASN
B
82
30.163
2.747
24.174
1.00
25.71
B


ATOM
2093
N
TYR
B
83
28.930
1.512
22.765
1.00
25.90
B


ATOM
2094
CA
TYR
B
83
28.324
2.693
22.156
1.00
25.91
B


ATOM
2095
CB
TYR
B
83
27.462
2.297
20.946
1.00
25.69
B


ATOM
2096
CG
TYR
B
83
27.102
3.462
20.056
1.00
25.95
B


ATOM
2097
CD1
TYR
B
83
26.022
4.294
20.353
1.00
27.11
B


ATOM
2098
CE1
TYR
B
83
25.712
5.403
19.545
1.00
25.98
B


ATOM
2099
CD2
TYR
B
83
27.865
3.759
18.933
1.00
27.72
B


ATOM
2100
CE2
TYR
B
83
27.567
4.862
18.121
1.00
28.05
B


ATOM
2101
CZ
TYR
B
83
26.493
5.680
18.434
1.00
27.73
B


ATOM
2102
OH
TYR
B
83
26.225
6.781
17.645
1.00
27.55
B


ATOM
2103
C
TYR
B
83
27.485
3.458
23.181
1.00
25.87
B


ATOM
2104
O
TYR
B
83
27.315
4.673
23.070
1.00
26.05
B


ATOM
2105
N
GLN
B
84
26.975
2.750
24.186
1.00
28.25
B


ATOM
2106
CA
GLN
B
84
26.159
3.375
25.229
1.00
30.44
B


ATOM
2107
CB
GLN
B
84
25.467
2.310
26.093
1.00
34.30
B


ATOM
2108
CG
GLN
B
84
24.595
1.343
25.301
1.00
40.52
B


ATOM
2109
CD
GLN
B
84
23.515
2.047
24.496
1.00
43.21
B


ATOM
2110
OE1
GLN
B
84
23.023
1.516
23.499
1.00
46.12
B


ATOM
2111
NE2
GLN
B
84
23.133
3.244
24.932
1.00
45.41
B


ATOM
2112
C
GLN
B
84
27.030
4.254
26.111
1.00
29.01
B


ATOM
2113
O
GLN
B
84
26.633
5.353
26.494
1.00
27.82
B


ATOM
2114
N
LEU
B
85
28.219
3.757
26.436
1.00
28.32
B


ATOM
2115
CA
LEU
B
85
29.150
4.505
27.263
1.00
28.76
B


ATOM
2116
CB
LEU
B
85
30.355
3.631
27.631
1.00
28.92
B


ATOM
2117
CG
LEU
B
85
30.065
2.226
28.184
1.00
30.98
B


ATOM
2118
CD1
LEU
B
85
31.343
1.631
28.758
1.00
30.59
B


ATOM
2119
CD2
LEU
B
85
29.006
2.291
29.265
1.00
31.87
B


ATOM
2120
C
LEU
B
85
29.609
5.719
26.461
1.00
29.95
B


ATOM
2121
O
LEU
B
85
29.836
6.798
27.010
1.00
30.93
B


ATOM
2122
N
GLU
B
86
29.724
5.529
25.150
1.00
30.31
B


ATOM
2123
CA
GLU
B
86
30.160
6.577
24.245
1.00
31.41
B


ATOM
2124
CB
GLU
B
86
30.426
5.981
22.861
1.00
32.60
B


ATOM
2125
CG
GLU
B
86
31.741
6.420
22.236
1.00
39.25
B


ATOM
2126
CD
GLU
B
86
32.962
5.854
22.953
1.00
41.02
B


ATOM
2127
OE1
GLU
B
86
33.379
4.714
22.636
1.00
40.75
B


ATOM
2128
OE2
GLU
B
86
33.497
6.553
23.843
1.00
41.96
B


ATOM
2129
C
GLU
B
86
29.113
7.684
24.146
1.00
32.44
B


ATOM
2130
O
GLU
B
86
29.454
8.865
24.109
1.00
30.73
B


ATOM
2131
N
LEU
B
87
27.838
7.303
24.103
1.00
33.77
B


ATOM
2132
CA
LEU
B
87
26.755
8.282
24.015
1.00
34.65
B


ATOM
2133
CB
LEU
B
87
25.398
7.583
23.899
1.00
34.69
B


ATOM
2134
CG
LEU
B
87
24.916
7.169
22.508
1.00
36.86
B


ATOM
2135
CD1
LEU
B
87
23.655
6.326
22.642
1.00
35.43
B


ATOM
2136
CD2
LEU
B
87
24.645
8.411
21.660
1.00
35.76
B


ATOM
2137
C
LEU
B
87
26.740
9.199
25.231
1.00
35.16
B


ATOM
2138
O
LEU
B
87
26.250
10.326
25.164
1.00
34.29
B


ATOM
2139
N
ARG
B
88
27.280
8.711
26.343
1.00
36.69
B


ATOM
2140
CA
ARG
B
88
27.317
9.493
27.573
1.00
37.64
B


ATOM
2141
CB
ARG
B
88
27.173
8.575
28.791
1.00
39.79
B


ATOM
2142
CG
ARG
B
88
25.827
7.878
28.908
1.00
45.19
B


ATOM
2143
CD
ARG
B
88
25.704
7.173
30.253
1.00
49.04
B


ATOM
2144
NE
ARG
B
88
26.657
6.074
30.388
1.00
54.57
B


ATOM
2145
CZ
ARG
B
88
27.101
5.603
31.552
1.00
55.76
B


ATOM
2146
NH1
ARG
B
88
26.683
6.137
32.694
1.00
55.56
B


ATOM
2147
NH2
ARG
B
88
27.963
4.595
31.574
1.00
56.11
B


ATOM
2148
C
ARG
B
88
28.601
10.299
27.714
1.00
36.93
B


ATOM
2149
O
ARG
B
88
28.702
11.160
28.589
1.00
37.24
B


ATOM
2150
N
THR
B
89
29.571
10.035
26.842
1.00
35.19
B


ATOM
2151
CA
THR
B
89
30.860
10.712
26.914
1.00
31.71
B


ATOM
2152
CB
THR
B
89
31.916
9.767
27.529
1.00
31.61
B


ATOM
2153
OG1
THR
B
89
31.980
8.554
26.762
1.00
29.72
B


ATOM
2154
CG2
THR
B
89
31.557
9.436
28.963
1.00
25.87
B


ATOM
2155
C
THR
B
89
31.420
11.254
25.600
1.00
31.31
B


ATOM
2156
O
THR
B
89
31.214
12.415
25.249
1.00
32.41
B


ATOM
2157
N
THR
B
90
32.139
10.403
24.880
1.00
30.72
B


ATOM
2158
CA
THR
B
90
32.766
10.786
23.623
1.00
30.43
B


ATOM
2159
CB
THR
B
90
33.368
9.558
22.925
1.00
30.54
B


ATOM
2160
OG1
THR
B
90
34.297
8.919
23.808
1.00
33.70
B


ATOM
2161
CG2
THR
B
90
34.099
9.970
21.666
1.00
31.65
B


ATOM
2162
C
THR
B
90
31.874
11.512
22.625
1.00
30.61
B


ATOM
2163
O
THR
B
90
32.267
12.543
22.070
1.00
30.24
B


ATOM
2164
N
LEU
B
91
30.683
10.977
22.385
1.00
30.30
B


ATOM
2165
CA
LEU
B
91
29.767
11.581
21.425
1.00
31.93
B


ATOM
2166
CB
LEU
B
91
28.709
10.554
21.007
1.00
32.55
B


ATOM
2167
CG
LEU
B
91
29.268
9.315
20.292
1.00
33.01
B


ATOM
2168
CD1
LEU
B
91
28.201
8.233
20.205
1.00
33.73
B


ATOM
2169
CD2
LEU
B
91
29.761
9.700
18.902
1.00
31.26
B


ATOM
2170
C
LEU
B
91
29.096
12.872
21.907
1.00
32.38
B


ATOM
2171
O
LEU
B
91
28.402
13.534
21.139
1.00
32.08
B


ATOM
2172
N
GLN
B
92
29.303
13.229
23.173
1.00
32.44
B


ATOM
2173
CA
GLN
B
92
28.725
14.454
23.713
1.00
34.54
B


ATOM
2174
CB
GLN
B
92
28.138
14.217
25.110
1.00
38.48
B


ATOM
2175
CG
GLN
B
92
26.836
13.419
25.121
1.00
44.66
B


ATOM
2176
CD
GLN
B
92
26.233
13.291
26.516
1.00
49.27
B


ATOM
2177
OE1
GLN
B
92
25.239
12.588
26.712
1.00
51.65
B


ATOM
2178
NE2
GLN
B
92
26.832
13.975
27.491
1.00
49.93
B


ATOM
2179
C
GLN
B
92
29.779
15.557
23.777
1.00
32.86
B


ATOM
2180
O
GLN
B
92
29.457
16.721
24.019
1.00
32.19
B


ATOM
2181
N
ARG
B
93
31.038
15.187
23.555
1.00
31.53
B


ATOM
2182
CA
ARG
B
93
32.132
16.157
23.576
1.00
29.87
B


ATOM
2183
CB
ARG
B
93
33.477
15.472
23.302
1.00
28.14
B


ATOM
2184
CG
ARG
B
93
34.681
16.433
23.217
1.00
23.56
B


ATOM
2185
CD
ARG
B
93
35.953
15.656
22.925
1.00
22.53
B


ATOM
2186
NE
ARG
B
93
37.128
16.486
22.662
1.00
19.19
B


ATOM
2187
CZ
ARG
B
93
37.769
17.205
23.581
1.00
18.66
B


ATOM
2188
NH1
ARG
B
93
37.352
17.214
24.843
1.00
17.45
B


ATOM
2189
NH2
ARG
B
93
38.847
17.898
23.242
1.00
16.56
B


ATOM
2190
C
ARG
B
93
31.921
17.245
22.535
1.00
29.02
B


ATOM
2191
O
ARG
B
93
31.755
16.965
21.349
1.00
29.55
B


ATOM
2192
N
ARG
B
94
31.933
18.490
22.987
1.00
28.71
B


ATOM
2193
CA
ARG
B
94
31.767
19.613
22.087
1.00
29.63
B


ATOM
2194
CB
ARG
B
94
30.299
20.046
22.041
1.00
32.44
B


ATOM
2195
CG
ARG
B
94
29.506
19.196
21.060
1.00
37.10
B


ATOM
2196
CD
ARG
B
94
28.016
19.414
21.124
1.00
39.80
B


ATOM
2197
NE
ARG
B
94
27.350
18.742
20.008
1.00
44.04
B


ATOM
2198
CZ
ARG
B
94
27.372
17.428
19.791
1.00
44.11
B


ATOM
2199
NH1
ARG
B
94
28.026
16.625
20.617
1.00
45.60
B


ATOM
2200
NH2
ARG
B
94
26.747
16.916
18.739
1.00
44.45
B


ATOM
2201
C
ARG
B
94
32.656
20.760
22.498
1.00
28.84
B


ATOM
2202
O
ARG
B
94
32.464
21.363
23.550
1.00
29.13
B


ATOM
2203
N
VAL
B
95
33.650
21.038
21.663
1.00
27.49
B


ATOM
2204
CA
VAL
B
95
34.592
22.117
21.916
1.00
26.47
B


ATOM
2205
CB
VAL
B
95
36.047
21.605
21.890
1.00
25.65
B


ATOM
2206
CG1
VAL
B
95
37.004
22.734
22.260
1.00
22.82
B


ATOM
2207
CG2
VAL
B
95
36.202
20.423
22.849
1.00
26.01
B


ATOM
2208
C
VAL
B
95
34.415
23.180
20.840
1.00
27.00
B


ATOM
2209
O
VAL
B
95
34.721
22.945
19.665
1.00
27.00
B


ATOM
2210
N
GLU
B
96
33.912
24.340
21.253
1.00
26.94
B


ATOM
2211
CA
GLU
B
96
33.673
25.462
20.348
1.00
26.50
B


ATOM
2212
CB
GLU
B
96
33.072
26.649
21.107
1.00
29.19
B


ATOM
2213
CG
GLU
B
96
31.736
26.372
21.775
1.00
36.47
B


ATOM
2214
CD
GLU
B
96
31.211
27.582
22.537
1.00
40.45
B


ATOM
2215
OE1
GLU
B
96
30.121
27.477
23.144
1.00
42.85
B


ATOM
2216
OE2
GLU
B
96
31.891
28.634
22.526
1.00
40.11
B


ATOM
2217
C
GLU
B
96
34.960
25.916
19.689
1.00
25.02
B


ATOM
2218
O
GLU
B
96
35.999
26.022
20.338
1.00
24.73
B


ATOM
2219
N
PRO
B
97
34.900
26.204
18.383
1.00
24.54
B


ATOM
2220
CD
PRO
B
97
33.744
26.011
17.493
1.00
22.89
B


ATOM
2221
CA
PRO
B
97
36.069
26.655
17.626
1.00
23.87
B


ATOM
2222
CB
PRO
B
97
35.580
26.633
16.175
1.00
22.81
B


ATOM
2223
CG
PRO
B
97
34.411
25.663
16.202
1.00
25.55
B


ATOM
2224
C
PRO
B
97
36.498
28.061
18.021
1.00
23.80
B


ATOM
2225
O
PRO
B
97
35.665
28.905
18.353
1.00
24.40
B


ATOM
2226
N
THR
B
98
37.799
28.307
17.990
1.00
22.02
B


ATOM
2227
CA
THR
B
98
38.306
29.634
18.266
1.00
24.00
B


ATOM
2228
CB
THR
B
98
39.569
29.592
19.150
1.00
27.31
B


ATOM
2229
OG1
THR
B
98
40.626
28.929
18.449
1.00
35.69
B


ATOM
2230
CG2
THR
B
98
39.282
28.839
20.439
1.00
26.76
B


ATOM
2231
C
THR
B
98
38.631
30.143
16.860
1.00
22.38
B


ATOM
2232
O
THR
B
98
39.376
29.504
16.116
1.00
19.48
B


ATOM
2233
N
VAL
B
99
38.041
31.274
16.487
1.00
21.55
B


ATOM
2234
CA
VAL
B
99
38.242
31.824
15.152
1.00
21.20
B


ATOM
2235
CB
VAL
B
99
36.871
32.153
14.509
1.00
21.09
B


ATOM
2236
CG1
VAL
B
99
37.043
32.541
13.050
1.00
19.62
B


ATOM
2237
CG2
VAL
B
99
35.950
30.944
14.625
1.00
18.29
B


ATOM
2238
C
VAL
B
99
39.140
33.059
15.167
1.00
21.59
B


ATOM
2239
O
VAL
B
99
38.970
33.962
15.982
1.00
21.57
B


ATOM
2240
N
THR
B
100
40.099
33.084
14.252
1.00
22.65
B


ATOM
2241
CA
THR
B
100
41.056
34.179
14.168
1.00
24.95
B


ATOM
2242
CB
THR
B
100
42.399
33.770
14.820
1.00
26.31
B


ATOM
2243
OG1
THR
B
100
42.162
33.321
16.160
1.00
30.10
B


ATOM
2244
CG2
THR
B
100
43.359
34.942
14.854
1.00
29.07
B


ATOM
2245
C
THR
B
100
41.329
34.556
12.717
1.00
24.61
B


ATOM
2246
O
THR
B
100
41.514
33.689
11.869
1.00
23.89
B


ATOM
2247
N
ILE
B
101
41.363
35.852
12.435
1.00
26.18
B


ATOM
2248
CA
ILE
B
101
41.638
36.315
11.080
1.00
29.32
B


ATOM
2249
CB
ILE
B
101
40.572
37.327
10.582
1.00
29.37
B


ATOM
2250
CG2
ILE
B
101
40.986
37.885
9.231
1.00
29.49
B


ATOM
2251
CG1
ILE
B
101
39.198
36.664
10.492
1.00
30.11
B


ATOM
2252
CD1
ILE
B
101
38.110
37.605
10.002
1.00
29.81
B


ATOM
2253
C
ILE
B
101
42.988
37.015
11.040
1.00
31.04
B


ATOM
2254
O
ILE
B
101
43.270
37.868
11.877
1.00
31.24
B


ATOM
2255
N
SER
B
102
43.820
36.664
10.066
1.00
34.47
B


ATOM
2256
CA
SER
B
102
45.124
37.303
9.940
1.00
39.17
B


ATOM
2257
CB
SER
B
102
46.143
36.617
10.844
1.00
37.33
B


ATOM
2258
OG
SER
B
102
46.326
35.265
10.462
1.00
41.93
B


ATOM
2259
C
SER
B
102
45.632
37.289
8.501
1.00
42.45
B


ATOM
2260
O
SER
B
102
45.641
36.248
7.845
1.00
42.45
B


ATOM
2261
N
PRO
B
103
46.052
38.455
7.988
1.00
45.38
B


ATOM
2262
CD
PRO
B
103
45.938
39.793
8.596
1.00
45.47
B


ATOM
2263
CA
PRO
B
103
46.564
38.545
6.617
1.00
48.91
B


ATOM
2264
CB
PRO
B
103
46.446
40.032
6.312
1.00
47.74
B


ATOM
2265
CG
PRO
B
103
46.739
40.652
7.642
1.00
47.08
B


ATOM
2266
C
PRO
B
103
48.010
38.042
6.545
1.00
51.96
B


ATOM
2267
O
PRO
B
103
48.688
37.957
7.568
1.00
52.51
B


ATOM
2268
N
SER
B
104
48.475
37.699
5.346
1.00
55.84
B


ATOM
2269
CA
SER
B
104
49.843
37.209
5.177
1.00
60.00
B


ATOM
2270
CB
SER
B
104
50.018
36.578
3.791
1.00
59.60
B


ATOM
2271
OG
SER
B
104
49.778
37.520
2.759
1.00
59.05
B


ATOM
2272
C
SER
B
104
50.842
38.353
5.368
1.00
63.75
B


ATOM
2273
O
SER
B
104
50.853
39.325
4.605
1.00
64.64
B


ATOM
2274
N
ARG
B
105
51.677
38.228
6.398
1.00
66.99
B


ATOM
2275
CA
ARG
B
105
52.674
39.242
6.736
1.00
69.17
B


ATOM
2276
CB
ARG
B
105
53.631
38.700
7.808
1.00
70.33
B


ATOM
2277
CG
ARG
B
105
54.672
37.690
7.318
1.00
72.24
B


ATOM
2278
CD
ARG
B
105
54.073
36.586
6.449
1.00
73.51
B


ATOM
2279
NE
ARG
B
105
52.981
35.859
7.095
1.00
75.02
B


ATOM
2280
CZ
ARG
B
105
53.120
35.051
8.142
1.00
76.07
B


ATOM
2281
NH1
ARG
B
105
54.314
34.852
8.684
1.00
77.38
B


ATOM
2282
NH2
ARG
B
105
52.059
34.431
8.644
1.00
76.05
B


ATOM
2283
C
ARG
B
105
53.464
39.720
5.523
1.00
70.38
B


ATOM
2284
O
ARG
B
105
53.134
40.746
4.923
1.00
71.56
B


ATOM
2285
N
ASN
B
113
46.629
40.478
−1.867
1.00
49.25
B


ATOM
2286
CA
ASN
B
113
46.963
40.039
−0.515
1.00
48.42
B


ATOM
2287
CB
ASN
B
113
46.726
41.181
0.477
1.00
51.23
B


ATOM
2288
CG
ASN
B
113
47.268
40.875
1.863
1.00
53.89
B


ATOM
2289
OD1
ASN
B
113
48.429
40.498
2.019
1.00
55.14
B


ATOM
2290
ND2
ASN
B
113
46.428
41.048
2.880
1.00
55.30
B


ATOM
2291
C
ASN
B
113
46.143
38.808
−0.118
1.00
45.78
B


ATOM
2292
O
ASN
B
113
45.155
38.471
−0.774
1.00
44.99
B


ATOM
2293
N
LEU
B
114
46.550
38.146
0.961
1.00
42.27
B


ATOM
2294
CA
LEU
B
114
45.862
36.944
1.415
1.00
38.77
B


ATOM
2295
CB
LEU
B
114
46.770
35.739
1.182
1.00
39.10
B


ATOM
2296
CG
LEU
B
114
46.238
34.330
1.421
1.00
40.81
B


ATOM
2297
CD1
LEU
B
114
45.097
34.023
0.459
1.00
41.59
B


ATOM
2298
CD2
LEU
B
114
47.379
33.341
1.222
1.00
41.03
B


ATOM
2299
C
LEU
B
114
45.424
36.986
2.883
1.00
36.39
B


ATOM
2300
O
LEU
B
114
46.237
37.204
3.783
1.00
35.98
B


ATOM
2301
N
LEU
B
115
44.130
36.777
3.112
1.00
31.79
B


ATOM
2302
CA
LEU
B
115
43.576
36.766
4.460
1.00
28.77
B


ATOM
2303
CB
LEU
B
115
42.231
37.496
4.493
1.00
29.52
B


ATOM
2304
CG
LEU
B
115
42.156
38.843
5.218
1.00
30.12
B


ATOM
2305
CD1
LEU
B
115
43.281
39.751
4.764
1.00
30.28
B


ATOM
2306
CD2
LEU
B
115
40.799
39.479
4.951
1.00
28.39
B


ATOM
2307
C
LEU
B
115
43.374
35.323
4.896
1.00
27.23
B


ATOM
2308
O
LEU
B
115
42.815
34.513
4.154
1.00
25.72
B


ATOM
2309
N
VAL
B
116
43.825
35.002
6.103
1.00
24.13
B


ATOM
2310
CA
VAL
B
116
43.695
33.651
6.618
1.00
20.76
B


ATOM
2311
CB
VAL
B
116
45.078
33.098
7.078
1.00
20.02
B


ATOM
2312
CG1
VAL
B
116
44.915
31.757
7.777
1.00
17.46
B


ATOM
2313
CG2
VAL
B
116
45.996
32.944
5.880
1.00
19.44
B


ATOM
2314
C
VAL
B
116
42.723
33.568
7.784
1.00
20.38
B


ATOM
2315
O
VAL
B
116
42.860
34.293
8.766
1.00
19.54
B


ATOM
2316
N
CYS
B
117
41.724
32.701
7.669
1.00
20.87
B


ATOM
2317
CA
CYS
B
117
40.793
32.523
8.774
1.00
22.57
B


ATOM
2318
C
CYS
B
117
41.132
31.196
9.444
1.00
21.84
B


ATOM
2319
O
CYS
B
117
40.867
30.123
8.892
1.00
22.98
B


ATOM
2320
CB
CYS
B
117
39.332
32.486
8.315
1.00
23.53
B


ATOM
2321
SG
CYS
B
117
38.217
32.222
9.734
1.00
29.76
B


ATOM
2322
N
SER
B
118
41.728
31.277
10.627
1.00
19.87
B


ATOM
2323
CA
SER
B
118
42.094
30.092
11.381
1.00
18.65
B


ATOM
2324
CB
SER
B
118
43.345
30.356
12.226
1.00
19.67
B


ATOM
2325
OG
SER
B
118
44.463
30.672
11.421
1.00
22.97
B


ATOM
2326
C
SER
B
118
40.962
29.656
12.300
1.00
18.03
B


ATOM
2327
O
SER
B
118
40.579
30.389
13.209
1.00
19.82
B


ATOM
2328
N
VAL
B
119
40.426
28.463
12.050
1.00
17.57
B


ATOM
2329
CA
VAL
B
119
39.365
27.889
12.874
1.00
15.30
B


ATOM
2330
CB
VAL
B
119
38.202
27.364
12.006
1.00
15.69
B


ATOM
2331
CG1
VAL
B
119
37.091
26.852
12.892
1.00
11.64
B


ATOM
2332
CG2
VAL
B
119
37.695
28.484
11.076
1.00
13.82
B


ATOM
2333
C
VAL
B
119
40.073
26.739
13.579
1.00
15.38
B


ATOM
2334
O
VAL
B
119
40.318
25.680
12.992
1.00
16.76
B


ATOM
2335
N
THR
B
120
40.404
26.958
14.844
1.00
16.03
B


ATOM
2336
CA
THR
B
120
41.165
25.988
15.615
1.00
15.04
B


ATOM
2337
CB
THR
B
120
42.487
26.613
16.031
1.00
13.75
B


ATOM
2338
OG1
THR
B
120
42.221
27.713
16.915
1.00
17.84
B


ATOM
2339
CG2
THR
B
120
43.230
27.144
14.815
1.00
12.18
B


ATOM
2340
C
THR
B
120
40.533
25.405
16.872
1.00
17.87
B


ATOM
2341
O
THR
B
120
39.571
25.944
17.425
1.00
17.71
B


ATOM
2342
N
ASP
B
121
41.132
24.303
17.317
1.00
19.07
B


ATOM
2343
CA
ASP
B
121
40.738
23.576
18.511
1.00
20.97
B


ATOM
2344
CB
ASP
B
121
41.268
24.291
19.766
1.00
24.82
B


ATOM
2345
CG
ASP
B
121
42.797
24.330
19.831
1.00
31.04
B


ATOM
2346
OD1
ASP
B
121
43.460
23.360
19.397
1.00
30.81
B


ATOM
2347
OD2
ASP
B
121
43.339
25.333
20.346
1.00
34.38
B


ATOM
2348
C
ASP
B
121
39.238
23.293
18.679
1.00
21.27
B


ATOM
2349
O
ASP
B
121
38.629
23.671
19.683
1.00
23.00
B


ATOM
2350
N
PHE
B
122
38.641
22.613
17.710
1.00
20.38
B


ATOM
2351
CA
PHE
B
122
37.233
22.280
17.818
1.00
18.51
B


ATOM
2352
CB
PHE
B
122
36.414
22.988
16.732
1.00
16.18
B


ATOM
2353
CG
PHE
B
122
36.817
22.644
15.319
1.00
13.31
B


ATOM
2354
CD1
PHE
B
122
37.695
23.463
14.615
1.00
11.43
B


ATOM
2355
CD2
PHE
B
122
36.247
21.547
14.664
1.00
10.93
B


ATOM
2356
CE1
PHE
B
122
37.998
23.210
13.272
1.00
10.91
B


ATOM
2357
CE2
PHE
B
122
36.541
21.280
13.317
1.00
12.31
B


ATOM
2358
CZ
PHE
B
122
37.419
22.118
12.618
1.00
8.92
B


ATOM
2359
C
PHE
B
122
37.011
20.778
17.739
1.00
19.55
B


ATOM
2360
O
PHE
B
122
37.889
20.029
17.301
1.00
18.45
B


ATOM
2361
N
TYR
B
123
35.829
20.357
18.182
1.00
20.50
B


ATOM
2362
CA
TYR
B
123
35.412
18.959
18.180
1.00
21.08
B


ATOM
2363
CB
TYR
B
123
36.067
18.201
19.340
1.00
19.11
B


ATOM
2364
CG
TYR
B
123
35.919
16.702
19.228
1.00
18.56
B


ATOM
2365
CD1
TYR
B
123
34.746
16.062
19.629
1.00
19.13
B


ATOM
2366
CE1
TYR
B
123
34.572
14.695
19.446
1.00
17.75
B


ATOM
2367
CD2
TYR
B
123
36.920
15.932
18.647
1.00
17.20
B


ATOM
2368
CE2
TYR
B
123
36.762
14.566
18.455
1.00
17.38
B


ATOM
2369
CZ
TYR
B
123
35.584
13.953
18.853
1.00
19.59
B


ATOM
2370
OH
TYR
B
123
35.412
12.608
18.631
1.00
22.32
B


ATOM
2371
C
TYR
B
123
33.896
18.957
18.351
1.00
21.83
B


ATOM
2372
O
TYR
B
123
33.365
19.708
19.165
1.00
23.26
B


ATOM
2373
N
PRO
B
124
33.175
18.126
17.584
1.00
21.65
B


ATOM
2374
CD
PRO
B
124
31.725
17.996
17.808
1.00
23.81
B


ATOM
2375
CA
PRO
B
124
33.627
17.177
16.562
1.00
22.30
B


ATOM
2376
CB
PRO
B
124
32.398
16.290
16.353
1.00
21.95
B


ATOM
2377
CG
PRO
B
124
31.270
17.237
16.586
1.00
23.07
B


ATOM
2378
C
PRO
B
124
34.128
17.813
15.266
1.00
22.20
B


ATOM
2379
O
PRO
B
124
34.204
19.035
15.149
1.00
24.43
B


ATOM
2380
N
ALA
B
125
34.457
16.971
14.291
1.00
20.63
B


ATOM
2381
CA
ALA
B
125
34.987
17.428
13.007
1.00
22.13
B


ATOM
2382
CB
ALA
B
125
35.571
16.236
12.244
1.00
20.20
B


ATOM
2383
C
ALA
B
125
34.057
18.222
12.078
1.00
22.42
B


ATOM
2384
O
ALA
B
125
34.512
19.129
11.400
1.00
24.48
B


ATOM
2385
N
GLN
B
126
32.772
17.893
12.036
1.00
25.59
B


ATOM
2386
CA
GLN
B
126
31.845
18.598
11.147
1.00
27.46
B


ATOM
2387
CB
GLN
B
126
30.414
18.101
11.357
1.00
29.99
B


ATOM
2388
CG
GLN
B
126
30.283
16.595
11.480
1.00
36.21
B


ATOM
2389
CD
GLN
B
126
30.625
16.102
12.870
1.00
38.28
B


ATOM
2390
OE1
GLN
B
126
30.558
14.905
13.158
1.00
40.46
B


ATOM
2391
NE2
GLN
B
126
30.989
17.030
13.745
1.00
40.92
B


ATOM
2392
C
GLN
B
126
31.876
20.112
11.333
1.00
28.28
B


ATOM
2393
O
GLN
B
126
31.571
20.627
12.410
1.00
29.36
B


ATOM
2394
N
ILE
B
127
32.221
20.831
10.273
1.00
27.17
B


ATOM
2395
CA
ILE
B
127
32.292
22.279
10.353
1.00
27.02
B


ATOM
2396
CB
ILE
B
127
33.656
22.716
10.931
1.00
27.21
B


ATOM
2397
CG2
ILE
B
127
34.767
22.453
9.898
1.00
21.63
B


ATOM
2398
CG1
ILE
B
127
33.612
24.195
11.316
1.00
24.63
B


ATOM
2399
CD1
ILE
B
127
34.760
24.633
12.198
1.00
25.86
B


ATOM
2400
C
ILE
B
127
32.117
22.903
8.969
1.00
27.10
B


ATOM
2401
O
ILE
B
127
32.393
22.258
7.956
1.00
26.58
B


ATOM
2402
N
LYS
B
128
31.666
24.155
8.940
1.00
25.41
B


ATOM
2403
CA
LYS
B
128
31.457
24.884
7.689
1.00
27.45
B


ATOM
2404
CB
LYS
B
128
29.964
24.927
7.334
1.00
29.68
B


ATOM
2405
CG
LYS
B
128
29.633
25.685
6.046
1.00
34.69
B


ATOM
2406
CD
LYS
B
128
30.129
24.954
4.793
1.00
38.25
B


ATOM
2407
CE
LYS
B
128
29.802
25.742
3.517
1.00
40.20
B


ATOM
2408
NZ
LYS
B
128
30.281
25.071
2.271
1.00
39.87
B


ATOM
2409
C
LYS
B
128
31.983
26.301
7.861
1.00
25.41
B


ATOM
2410
O
LYS
B
128
31.559
27.019
8.759
1.00
26.68
B


ATOM
2411
N
VAL
B
129
32.911
26.700
7.002
1.00
25.70
B


ATOM
2412
CA
VAL
B
129
33.493
28.034
7.078
1.00
24.82
B


ATOM
2413
CB
VAL
B
129
35.013
27.956
7.329
1.00
24.17
B


ATOM
2414
CG1
VAL
B
129
35.592
29.351
7.452
1.00
22.14
B


ATOM
2415
CG2
VAL
B
129
35.295
27.136
8.583
1.00
22.44
B


ATOM
2416
C
VAL
B
129
33.248
28.791
5.778
1.00
25.17
B


ATOM
2417
O
VAL
B
129
33.532
28.283
4.701
1.00
25.50
B


ATOM
2418
N
ARG
B
130
32.724
30.007
5.884
1.00
27.21
B


ATOM
2419
CA
ARG
B
130
32.445
30.814
4.701
1.00
28.49
B


ATOM
2420
CB
ARG
B
130
30.931
30.920
4.470
1.00
31.77
B


ATOM
2421
CG
ARG
B
130
30.239
29.591
4.183
1.00
34.92
B


ATOM
2422
CD
ARG
B
130
28.927
29.813
3.432
1.00
41.30
B


ATOM
2423
NE
ARG
B
130
27.834
30.254
4.291
1.00
42.15
B


ATOM
2424
CZ
ARG
B
130
27.032
29.426
4.953
1.00
46.05
B


ATOM
2425
NH1
ARG
B
130
27.200
28.112
4.849
1.00
45.50
B


ATOM
2426
NH2
ARG
B
130
26.061
29.910
5.718
1.00
48.30
B


ATOM
2427
C
ARG
B
130
33.036
32.211
4.792
1.00
27.57
B


ATOM
2428
O
ARG
B
130
33.130
32.789
5.874
1.00
26.00
B


ATOM
2429
N
TRP
B
131
33.440
32.744
3.645
1.00
27.37
B


ATOM
2430
CA
TRP
B
131
34.004
34.085
3.571
1.00
30.27
B


ATOM
2431
CB
TRP
B
131
35.281
34.083
2.737
1.00
30.21
B


ATOM
2432
CG
TRP
B
131
36.532
33.844
3.521
1.00
32.32
B


ATOM
2433
CD2
TRP
B
131
37.155
34.757
4.432
1.00
32.41
B


ATOM
2434
CE2
TRP
B
131
38.334
34.142
4.900
1.00
33.07
B


ATOM
2435
CE3
TRP
B
131
36.831
36.039
4.897
1.00
31.75
B


ATOM
2436
CD1
TRP
B
131
37.333
32.741
3.478
1.00
32.80
B


ATOM
2437
NE1
TRP
B
131
38.420
32.913
4.300
1.00
31.53
B


ATOM
2438
CZ2
TRP
B
131
39.193
34.764
5.812
1.00
32.82
B


ATOM
2439
CZ3
TRP
B
131
37.680
36.656
5.800
1.00
32.08
B


ATOM
2440
CH2
TRP
B
131
38.849
36.017
6.249
1.00
33.40
B


ATOM
2441
C
TRP
B
131
33.003
35.064
2.949
1.00
32.99
B


ATOM
2442
O
TRP
B
131
32.367
34.759
1.940
1.00
32.18
B


ATOM
2443
N
PHE
B
132
32.879
36.242
3.550
1.00
35.48
B


ATOM
2444
CA
PHE
B
132
31.962
37.263
3.058
1.00
39.35
B


ATOM
2445
CB
PHE
B
132
30.856
37.501
4.077
1.00
38.14
B


ATOM
2446
CG
PHE
B
132
29.843
36.407
4.123
1.00
38.39
B


ATOM
2447
CD1
PHE
B
132
28.804
36.373
3.202
1.00
38.31
B


ATOM
2448
CD2
PHE
B
132
29.930
35.399
5.075
1.00
38.21
B


ATOM
2449
CE1
PHE
B
132
27.860
35.348
3.229
1.00
39.26
B


ATOM
2450
CE2
PHE
B
132
28.992
34.369
5.111
1.00
38.83
B


ATOM
2451
CZ
PHE
B
132
27.954
34.345
4.184
1.00
37.91
B


ATOM
2452
C
PHE
B
132
32.650
38.583
2.755
1.00
41.59
B


ATOM
2453
O
PHE
B
132
33.515
39.025
3.508
1.00
42.72
B


ATOM
2454
N
ARG
B
133
32.267
39.203
1.640
1.00
45.04
B


ATOM
2455
CA
ARG
B
133
32.829
40.490
1.242
1.00
48.28
B


ATOM
2456
CB
ARG
B
133
32.510
40.787
−0.227
1.00
51.68
B


ATOM
2457
CG
ARG
B
133
33.293
41.958
−0.829
1.00
55.78
B


ATOM
2458
CD
ARG
B
133
34.787
41.655
−0.867
1.00
57.07
B


ATOM
2459
NE
ARG
B
133
35.580
42.741
−1.440
1.00
59.30
B


ATOM
2460
CZ
ARG
B
133
35.523
43.135
−2.710
1.00
60.93
B


ATOM
2461
NH1
ARG
B
133
34.702
42.536
−3.564
1.00
61.44
B


ATOM
2462
NH2
ARG
B
133
36.295
44.132
−3.128
1.00
61.77
B


ATOM
2463
C
ARG
B
133
32.129
41.492
2.145
1.00
49.07
B


ATOM
2464
O
ARG
B
133
32.299
41.460
3.358
1.00
51.26
B


ATOM
2465
N
ASN
B
134
31.331
42.376
1.572
1.00
49.23
B


ATOM
2466
CA
ASN
B
134
30.614
43.336
2.393
1.00
48.83
B


ATOM
2467
CB
ASN
B
134
30.582
44.702
1.710
1.00
45.93
B


ATOM
2468
CG
ASN
B
134
31.973
45.290
1.523
1.00
45.10
B


ATOM
2469
OD1
ASN
B
134
32.450
45.440
0.397
1.00
41.81
B


ATOM
2470
ND2
ASN
B
134
32.634
45.618
2.634
1.00
41.82
B


ATOM
2471
C
ASN
B
134
29.203
42.795
2.594
1.00
50.25
B


ATOM
2472
O
ASN
B
134
28.222
43.529
2.508
1.00
52.28
B


ATOM
2473
N
ASP
B
135
29.122
41.496
2.868
1.00
50.15
B


ATOM
2474
CA
ASP
B
135
27.847
40.819
3.072
1.00
51.07
B


ATOM
2475
C
ASP
B
135
27.590
39.855
1.910
1.00
51.76
B


ATOM
2476
O
ASP
B
135
26.586
39.136
1.893
1.00
51.82
B


ATOM
2477
N
GLN
B
136
28.507
39.856
0.944
1.00
50.97
B


ATOM
2478
CA
GLN
B
136
28.421
38.999
−0.240
1.00
51.24
B


ATOM
2479
CB
GLN
B
136
28.766
39.805
−1.493
1.00
53.78
B


ATOM
2480
CG
GLN
B
136
28.736
39.000
−2.783
1.00
58.16
B


ATOM
2481
CD
GLN
B
136
29.675
39.559
−3.839
1.00
59.39
B


ATOM
2482
OE1
GLN
B
136
30.895
39.527
−3.675
1.00
60.12
B


ATOM
2483
NE2
GLN
B
136
29.110
40.078
−4.926
1.00
59.45
B


ATOM
2484
C
GLN
B
136
29.395
37.825
−0.124
1.00
49.46
B


ATOM
2485
O
GLN
B
136
30.607
38.026
−0.035
1.00
48.29
B


ATOM
2486
N
GLU
B
137
28.873
36.603
−0.144
1.00
47.64
B


ATOM
2487
CA
GLU
B
137
29.730
35.432
−0.027
1.00
46.85
B


ATOM
2488
CB
GLU
B
137
28.899
34.152
0.022
1.00
47.17
B


ATOM
2489
CG
GLU
B
137
29.695
32.975
0.556
1.00
50.22
B


ATOM
2490
CD
GLU
B
137
28.866
31.726
0.743
1.00
52.65
B


ATOM
2491
OE1
GLU
B
137
27.699
31.842
1.171
1.00
55.57
B


ATOM
2492
OE2
GLU
B
137
29.391
30.623
0.478
1.00
54.41
B


ATOM
2493
C
GLU
B
137
30.755
35.320
−1.149
1.00
45.23
B


ATOM
2494
O
GLU
B
137
30.445
35.544
−2.314
1.00
45.04
B


ATOM
2495
N
GLU
B
138
31.983
34.977
−0.776
1.00
44.63
B


ATOM
2496
CA
GLU
B
138
33.078
34.808
−1.724
1.00
44.36
B


ATOM
2497
CB
GLU
B
138
34.284
35.658
−1.307
1.00
45.65
B


ATOM
2498
CG
GLU
B
138
34.076
37.166
−1.320
1.00
48.42
B


ATOM
2499
CD
GLU
B
138
34.144
37.761
−2.717
1.00
50.71
B


ATOM
2500
OE1
GLU
B
138
35.120
37.471
−3.442
1.00
51.60
B


ATOM
2501
OE2
GLU
B
138
33.227
38.526
−3.086
1.00
50.99
B


ATOM
2502
C
GLU
B
138
33.498
33.335
−1.740
1.00
43.68
B


ATOM
2503
O
GLU
B
138
33.831
32.769
−0.697
1.00
43.53
B


ATOM
2504
N
THR
B
139
33.468
32.711
−2.914
1.00
42.58
B


ATOM
2505
CA
THR
B
139
33.881
31.313
−3.044
1.00
41.76
B


ATOM
2506
CB
THR
B
139
32.739
30.415
−3.543
1.00
41.04
B


ATOM
2507
OG1
THR
B
139
32.207
30.948
−4.759
1.00
40.71
B


ATOM
2508
CG2
THR
B
139
31.641
30.325
−2.492
1.00
41.89
B


ATOM
2509
C
THR
B
139
35.038
31.245
−4.026
1.00
40.93
B


ATOM
2510
O
THR
B
139
35.855
30.326
−3.981
1.00
40.04
B


ATOM
2511
N
ALA
B
140
35.096
32.224
−4.920
1.00
40.67
B


ATOM
2512
CA
ALA
B
140
36.179
32.305
−5.887
1.00
41.22
B


ATOM
2513
CB
ALA
B
140
35.714
33.016
−7.158
1.00
41.13
B


ATOM
2514
C
ALA
B
140
37.247
33.126
−5.177
1.00
41.09
B


ATOM
2515
O
ALA
B
140
36.976
34.232
−4.693
1.00
43.11
B


ATOM
2516
N
GLY
B
141
38.455
32.582
−5.102
1.00
39.60
B


ATOM
2517
CA
GLY
B
141
39.526
33.278
−4.418
1.00
35.11
B


ATOM
2518
C
GLY
B
141
39.739
32.651
−3.051
1.00
33.42
B


ATOM
2519
O
GLY
B
141
40.605
33.076
−2.287
1.00
31.24
B


ATOM
2520
N
VAL
B
142
38.945
31.628
−2.750
1.00
31.89
B


ATOM
2521
CA
VAL
B
142
39.033
30.937
−1.470
1.00
32.27
B


ATOM
2522
CB
VAL
B
142
37.645
30.790
−0.813
1.00
31.90
B


ATOM
2523
CG1
VAL
B
142
37.733
29.861
0.400
1.00
32.37
B


ATOM
2524
CG2
VAL
B
142
37.125
32.161
−0.402
1.00
32.53
B


ATOM
2525
C
VAL
B
142
39.652
29.552
−1.564
1.00
31.26
B


ATOM
2526
O
VAL
B
142
39.211
28.712
−2.343
1.00
32.44
B


ATOM
2527
N
VAL
B
143
40.676
29.326
−0.752
1.00
30.76
B


ATOM
2528
CA
VAL
B
143
41.357
28.045
−0.702
1.00
29.79
B


ATOM
2529
CB
VAL
B
143
42.815
28.154
−1.162
1.00
29.63
B


ATOM
2530
CG1
VAL
B
143
43.439
26.768
−1.212
1.00
31.60
B


ATOM
2531
CG2
VAL
B
143
42.885
28.819
−2.514
1.00
33.43
B


ATOM
2532
C
VAL
B
143
41.357
27.575
0.749
1.00
30.61
B


ATOM
2533
O
VAL
B
143
41.665
28.338
1.667
1.00
28.64
B


ATOM
2534
N
SER
B
144
41.017
26.313
0.950
1.00
29.65
B


ATOM
2535
CA
SER
B
144
40.970
25.756
2.282
1.00
28.42
B


ATOM
2536
CB
SER
B
144
39.541
25.325
2.605
1.00
29.23
B


ATOM
2537
OG
SER
B
144
39.457
24.705
3.875
1.00
33.81
B


ATOM
2538
C
SER
B
144
41.900
24.562
2.373
1.00
27.32
B


ATOM
2539
O
SER
B
144
42.101
23.840
1.397
1.00
27.40
B


ATOM
2540
N
THR
B
145
42.492
24.372
3.542
1.00
25.70
B


ATOM
2541
CA
THR
B
145
43.364
23.227
3.755
1.00
24.82
B


ATOM
2542
CB
THR
B
145
44.272
23.418
4.995
1.00
25.01
B


ATOM
2543
OG1
THR
B
145
43.467
23.399
6.186
1.00
25.18
B


ATOM
2544
CG2
THR
B
145
45.022
24.743
4.923
1.00
23.27
B


ATOM
2545
C
THR
B
145
42.392
22.100
4.071
1.00
24.16
B


ATOM
2546
O
THR
B
145
41.200
22.335
4.272
1.00
23.86
B


ATOM
2547
N
PRO
B
146
42.865
20.854
4.081
1.00
23.17
B


ATOM
2548
CD
PRO
B
146
44.116
20.231
3.618
1.00
22.29
B


ATOM
2549
CA
PRO
B
146
41.854
19.852
4.419
1.00
23.18
B


ATOM
2550
CB
PRO
B
146
42.521
18.536
4.008
1.00
24.20
B


ATOM
2551
CG
PRO
B
146
43.998
18.833
4.162
1.00
22.82
B


ATOM
2552
C
PRO
B
146
41.597
19.945
5.933
1.00
22.63
B


ATOM
2553
O
PRO
B
146
42.213
20.766
6.625
1.00
21.32
B


ATOM
2554
N
LEU
B
147
40.667
19.146
6.445
1.00
22.60
B


ATOM
2555
CA
LEU
B
147
40.414
19.142
7.883
1.00
22.34
B


ATOM
2556
CB
LEU
B
147
39.241
18.216
8.213
1.00
22.17
B


ATOM
2557
CG
LEU
B
147
38.934
17.973
9.691
1.00
24.53
B


ATOM
2558
CD1
LEU
B
147
38.629
19.288
10.368
1.00
25.95
B


ATOM
2559
CD2
LEU
B
147
37.746
17.026
9.826
1.00
25.55
B


ATOM
2560
C
LEU
B
147
41.710
18.609
8.515
1.00
21.99
B


ATOM
2561
O
LEU
B
147
42.290
17.640
8.024
1.00
21.35
B


ATOM
2562
N
ILE
B
148
42.175
19.246
9.581
1.00
20.48
B


ATOM
2563
CA
ILE
B
148
43.406
18.813
10.228
1.00
19.15
B


ATOM
2564
CB
ILE
B
148
44.392
19.990
10.403
1.00
21.68
B


ATOM
2565
CG2
ILE
B
148
45.666
19.505
11.065
1.00
20.10
B


ATOM
2566
CG1
ILE
B
148
44.728
20.609
9.041
1.00
25.04
B


ATOM
2567
CD1
ILE
B
148
45.416
19.649
8.090
1.00
29.06
B


ATOM
2568
C
ILE
B
148
43.160
18.208
11.603
1.00
17.56
B


ATOM
2569
O
ILE
B
148
42.566
18.852
12.467
1.00
14.88
B


ATOM
2570
N
ARG
B
149
43.625
16.973
11.795
1.00
15.95
B


ATOM
2571
CA
ARG
B
149
43.492
16.273
13.077
1.00
17.47
B


ATOM
2572
CB
ARG
B
149
43.420
14.763
12.852
1.00
16.94
B


ATOM
2573
CG
ARG
B
149
43.202
13.941
14.128
1.00
20.29
B


ATOM
2574
CD
ARG
B
149
43.252
12.448
13.821
1.00
21.64
B


ATOM
2575
NE
ARG
B
149
42.168
12.028
12.938
1.00
21.97
B


ATOM
2576
CZ
ARG
B
149
40.934
11.742
13.348
1.00
23.22
B


ATOM
2577
NH1
ARG
B
149
40.015
11.374
12.471
1.00
23.89
B


ATOM
2578
NH2
ARG
B
149
40.623
11.803
14.636
1.00
23.11
B


ATOM
2579
C
ARG
B
149
44.720
16.603
13.937
1.00
17.66
B


ATOM
2580
O
ARG
B
149
45.850
16.311
13.549
1.00
17.51
B


ATOM
2581
N
ASN
B
150
44.496
17.210
15.098
1.00
16.67
B


ATOM
2582
CA
ASN
B
150
45.592
17.593
15.980
1.00
16.94
B


ATOM
2583
CB
ASN
B
150
45.174
18.756
16.890
1.00
15.38
B


ATOM
2584
CG
ASN
B
150
44.899
20.034
16.118
1.00
18.41
B


ATOM
2585
OD1
ASN
B
150
45.685
20.436
15.249
1.00
19.05
B


ATOM
2586
ND2
ASN
B
150
43.790
20.691
16.440
1.00
17.88
B


ATOM
2587
C
ASN
B
150
46.116
16.452
16.841
1.00
18.47
B


ATOM
2588
O
ASN
B
150
47.220
16.540
17.384
1.00
17.03
B


ATOM
2589
N
GLY
B
151
45.324
15.391
16.968
1.00
17.77
B


ATOM
2590
CA
GLY
B
151
45.734
14.251
17.770
1.00
19.16
B


ATOM
2591
C
GLY
B
151
45.258
14.293
19.213
1.00
20.44
B


ATOM
2592
O
GLY
B
151
45.198
13.264
19.877
1.00
22.31
B


ATOM
2593
N
ASP
B
152
44.906
15.475
19.701
1.00
20.79
B


ATOM
2594
CA
ASP
B
152
44.450
15.624
21.077
1.00
21.97
B


ATOM
2595
CB
ASP
B
152
45.192
16.790
21.748
1.00
21.95
B


ATOM
2596
CG
ASP
B
152
45.027
18.101
20.992
1.00
28.05
B


ATOM
2597
OD1
ASP
B
152
45.764
19.060
21.300
1.00
30.94
B


ATOM
2598
OD2
ASP
B
152
44.158
18.181
20.090
1.00
28.02
B


ATOM
2599
C
ASP
B
152
42.939
15.847
21.175
1.00
20.51
B


ATOM
2600
O
ASP
B
152
42.474
16.619
22.010
1.00
21.63
B


ATOM
2601
N
TRP
B
153
42.183
15.166
20.322
1.00
19.19
B


ATOM
2602
CA
TRP
B
153
40.724
15.278
20.300
1.00
16.82
B


ATOM
2603
CB
TRP
B
153
40.121
14.865
21.657
1.00
15.80
B


ATOM
2604
CG
TRP
B
153
40.326
13.408
22.005
1.00
16.21
B


ATOM
2605
CD2
TRP
B
153
39.415
12.322
21.756
1.00
16.58
B


ATOM
2606
CE2
TRP
B
153
40.047
11.134
22.188
1.00
15.08
B


ATOM
2607
CE3
TRP
B
153
38.125
12.238
21.211
1.00
15.69
B


ATOM
2608
CD1
TRP
B
153
41.435
12.848
22.564
1.00
14.68
B


ATOM
2609
NE1
TRP
B
153
41.278
11.483
22.677
1.00
15.53
B


ATOM
2610
CZ2
TRP
B
153
39.438
9.879
22.087
1.00
15.60
B


ATOM
2611
CZ3
TRP
B
153
37.518
10.987
21.112
1.00
14.22
B


ATOM
2612
CH2
TRP
B
153
38.176
9.827
21.549
1.00
13.89
B


ATOM
2613
C
TRP
B
153
40.194
16.660
19.890
1.00
16.09
B


ATOM
2614
O
TRP
B
153
39.159
17.110
20.379
1.00
14.28
B


ATOM
2615
N
THR
B
154
40.929
17.342
19.020
1.00
15.11
B


ATOM
2616
CA
THR
B
154
40.499
18.627
18.483
1.00
16.19
B


ATOM
2617
CB
THR
B
154
41.176
19.877
19.150
1.00
18.02
B


ATOM
2618
OG1
THR
B
154
42.602
19.804
19.008
1.00
19.50
B


ATOM
2619
CG2
THR
B
154
40.788
20.000
20.608
1.00
15.03
B


ATOM
2620
C
THR
B
154
40.908
18.602
17.024
1.00
15.24
B


ATOM
2621
O
THR
B
154
41.773
17.832
16.635
1.00
15.24
B


ATOM
2622
N
PHE
B
155
40.269
19.437
16.220
1.00
18.04
B


ATOM
2623
CA
PHE
B
155
40.577
19.538
14.801
1.00
16.03
B


ATOM
2624
CB
PHE
B
155
39.404
19.042
13.938
1.00
16.98
B


ATOM
2625
CG
PHE
B
155
39.069
17.579
14.118
1.00
17.58
B


ATOM
2626
CD1
PHE
B
155
38.133
17.170
15.074
1.00
18.20
B


ATOM
2627
CD2
PHE
B
155
39.670
16.611
13.312
1.00
17.71
B


ATOM
2628
CE1
PHE
B
155
37.799
15.810
15.223
1.00
17.81
B


ATOM
2629
CE2
PHE
B
155
39.346
15.250
13.451
1.00
17.57
B


ATOM
2630
CZ
PHE
B
155
38.407
14.849
14.409
1.00
16.39
B


ATOM
2631
C
PHE
B
155
40.793
21.015
14.503
1.00
16.67
B


ATOM
2632
O
PHE
B
155
40.532
21.870
15.352
1.00
16.84
B


ATOM
2633
N
GLN
B
156
41.281
21.312
13.304
1.00
14.72
B


ATOM
2634
CA
GLN
B
156
41.467
22.689
12.886
1.00
14.66
B


ATOM
2635
CB
GLN
B
156
42.811
23.264
13.357
1.00
16.69
B


ATOM
2636
CG
GLN
B
156
44.039
22.698
12.669
1.00
15.65
B


ATOM
2637
CD
GLN
B
156
45.292
23.486
13.011
1.00
17.87
B


ATOM
2638
OE1
GLN
B
156
45.477
24.617
12.555
1.00
17.56
B


ATOM
2639
NE2
GLN
B
156
46.153
22.897
13.830
1.00
15.40
B


ATOM
2640
C
GLN
B
156
41.398
22.722
11.371
1.00
14.00
B


ATOM
2641
O
GLN
B
156
41.477
21.691
10.716
1.00
15.17
B


ATOM
2642
N
ILE
B
157
41.241
23.911
10.818
1.00
15.34
B


ATOM
2643
CA
ILE
B
157
41.165
24.057
9.383
1.00
17.26
B


ATOM
2644
CB
ILE
B
157
39.791
23.585
8.856
1.00
16.56
B


ATOM
2645
CG2
ILE
B
157
38.675
24.429
9.474
1.00
13.07
B


ATOM
2646
CG1
ILE
B
157
39.765
23.649
7.326
1.00
17.72
B


ATOM
2647
CD1
ILE
B
157
38.583
22.913
6.712
1.00
14.50
B


ATOM
2648
C
ILE
B
157
41.379
25.523
9.074
1.00
18.67
B


ATOM
2649
O
ILE
B
157
40.823
26.391
9.745
1.00
22.28
B


ATOM
2650
N
LEU
B
158
42.217
25.795
8.083
1.00
18.98
B


ATOM
2651
CA
LEU
B
158
42.508
27.162
7.690
1.00
20.77
B


ATOM
2652
CB
LEU
B
158
44.022
27.368
7.555
1.00
22.23
B


ATOM
2653
CG
LEU
B
158
44.851
27.525
8.838
1.00
26.12
B


ATOM
2654
CD1
LEU
B
158
44.689
26.320
9.740
1.00
29.01
B


ATOM
2655
CD2
LEU
B
158
46.311
27.701
8.465
1.00
28.46
B


ATOM
2656
C
LEU
B
158
41.817
27.484
6.371
1.00
20.61
B


ATOM
2657
O
LEU
B
158
41.934
26.734
5.401
1.00
19.39
B


ATOM
2658
N
VAL
B
159
41.088
28.596
6.346
1.00
21.67
B


ATOM
2659
CA
VAL
B
159
40.380
29.011
5.141
1.00
21.90
B


ATOM
2660
CB
VAL
B
159
38.855
29.061
5.365
1.00
22.06
B


ATOM
2661
CG1
VAL
B
159
38.147
29.252
4.043
1.00
20.55
B


ATOM
2662
CG2
VAL
B
159
38.381
27.766
6.009
1.00
20.83
B


ATOM
2663
C
VAL
B
159
40.899
30.379
4.749
1.00
21.80
B


ATOM
2664
O
VAL
B
159
40.721
31.357
5.473
1.00
20.82
B


ATOM
2665
N
MET
B
160
41.555
30.416
3.592
1.00
23.56
B


ATOM
2666
CA
MET
B
160
42.179
31.613
3.055
1.00
25.12
B


ATOM
2667
CB
MET
B
160
43.580
31.257
2.559
1.00
26.80
B


ATOM
2668
CG
MET
B
160
44.479
30.736
3.678
1.00
32.00
B


ATOM
2669
SD
MET
B
160
45.850
29.700
3.145
1.00
38.02
B


ATOM
2670
CE
MET
B
160
45.094
28.065
3.307
1.00
35.43
B


ATOM
2671
C
MET
B
160
41.387
32.269
1.941
1.00
28.27
B


ATOM
2672
O
MET
B
160
40.684
31.602
1.177
1.00
28.76
B


ATOM
2673
N
LEU
B
161
41.518
33.588
1.854
1.00
29.59
B


ATOM
2674
CA
LEU
B
161
40.820
34.366
0.845
1.00
32.69
B


ATOM
2675
CB
LEU
B
161
39.669
35.142
1.487
1.00
30.80
B


ATOM
2676
CG
LEU
B
161
39.031
36.199
0.586
1.00
31.56
B


ATOM
2677
CD1
LEU
B
161
38.156
35.516
−0.460
1.00
29.64
B


ATOM
2678
CD2
LEU
B
161
38.213
37.167
1.423
1.00
29.89
B


ATOM
2679
C
LEU
B
161
41.755
35.349
0.154
1.00
35.59
B


ATOM
2680
O
LEU
B
161
42.350
36.216
0.801
1.00
35.54
B


ATOM
2681
N
GLU
B
162
41.895
35.203
−1.158
1.00
39.87
B


ATOM
2682
CA
GLU
B
162
42.728
36.118
−1.927
1.00
44.05
B


ATOM
2683
CB
GLU
B
162
42.995
35.565
−3.331
1.00
46.86
B


ATOM
2684
CG
GLU
B
162
43.795
36.497
−4.239
1.00
50.98
B


ATOM
2685
CD
GLU
B
162
45.274
36.537
−3.891
1.00
54.75
B


ATOM
2686
OE1
GLU
B
162
45.604
36.802
−2.715
1.00
56.53
B


ATOM
2687
OE2
GLU
B
162
46.108
36.308
−4.796
1.00
55.16
B


ATOM
2688
C
GLU
B
162
41.879
37.372
−2.029
1.00
44.69
B


ATOM
2689
O
GLU
B
162
40.719
37.302
−2.434
1.00
44.39
B


ATOM
2690
N
MET
B
163
42.436
38.514
−1.648
1.00
46.67
B


ATOM
2691
CA
MET
B
163
41.670
39.746
−1.716
1.00
49.56
B


ATOM
2692
CB
MET
B
163
40.881
39.949
−0.412
1.00
51.22
B


ATOM
2693
CG
MET
B
163
41.652
39.675
0.876
1.00
51.58
B


ATOM
2694
SD
MET
B
163
42.910
40.901
1.274
1.00
56.87
B


ATOM
2695
CE
MET
B
163
41.915
42.187
2.029
1.00
54.89
B


ATOM
2696
C
MET
B
163
42.487
40.986
−2.028
1.00
51.43
B


ATOM
2697
O
MET
B
163
43.717
40.988
−1.942
1.00
51.02
B


ATOM
2698
N
THR
B
164
41.777
42.038
−2.412
1.00
53.70
B


ATOM
2699
CA
THR
B
164
42.385
43.316
−2.738
1.00
56.61
B


ATOM
2700
CB
THR
B
164
41.889
43.820
−4.116
1.00
57.48
B


ATOM
2701
OG1
THR
B
164
40.457
43.744
−4.172
1.00
57.81
B


ATOM
2702
CG2
THR
B
164
42.480
42.967
−5.234
1.00
57.23
B


ATOM
2703
C
THR
B
164
42.012
44.318
−1.642
1.00
57.80
B


ATOM
2704
O
THR
B
164
40.866
44.766
−1.555
1.00
57.08
B


ATOM
2705
N
PRO
B
165
42.976
44.658
−0.770
1.00
58.98
B


ATOM
2706
CD
PRO
B
165
44.315
44.055
−0.647
1.00
59.54
B


ATOM
2707
CA
PRO
B
165
42.734
45.605
0.322
1.00
60.52
B


ATOM
2708
CB
PRO
B
165
44.063
45.608
1.078
1.00
60.33
B


ATOM
2709
CG
PRO
B
165
44.604
44.236
0.822
1.00
60.42
B


ATOM
2710
C
PRO
B
165
42.347
47.002
−0.163
1.00
61.65
B


ATOM
2711
O
PRO
B
165
43.149
47.698
−0.790
1.00
61.24
B


ATOM
2712
N
GLN
B
166
41.110
47.395
0.126
1.00
62.45
B


ATOM
2713
CA
GLN
B
166
40.598
48.709
−0.250
1.00
63.32
B


ATOM
2714
CB
GLN
B
166
39.605
48.590
−1.410
1.00
65.46
B


ATOM
2715
CG
GLN
B
166
40.177
47.945
−2.661
1.00
69.00
B


ATOM
2716
CD
GLN
B
166
39.195
47.942
−3.819
1.00
71.19
B


ATOM
2717
OE1
GLN
B
166
38.071
47.448
−3.697
1.00
72.48
B


ATOM
2718
NE2
GLN
B
166
39.617
48.492
−4.954
1.00
72.65
B


ATOM
2719
C
GLN
B
166
39.893
49.287
0.970
1.00
62.65
B


ATOM
2720
O
GLN
B
166
39.021
48.635
1.550
1.00
62.16
B


ATOM
2721
N
ARG
B
167
40.266
50.501
1.366
1.00
61.62
B


ATOM
2722
CA
ARG
B
167
39.645
51.111
2.535
1.00
60.86
B


ATOM
2723
CB
ARG
B
167
40.190
52.525
2.777
1.00
62.57
B


ATOM
2724
CG
ARG
B
167
39.953
53.029
4.204
1.00
64.82
B


ATOM
2725
CD
ARG
B
167
40.742
52.198
5.227
1.00
67.31
B


ATOM
2726
NE
ARG
B
167
40.094
52.143
6.539
1.00
69.03
B


ATOM
2727
CZ
ARG
B
167
40.570
51.477
7.591
1.00
69.14
B


ATOM
2728
NH1
ARG
B
167
41.710
50.804
7.499
1.00
69.34
B


ATOM
2729
NH2
ARG
B
167
39.897
51.471
8.735
1.00
69.52
B


ATOM
2730
C
ARG
B
167
38.136
51.154
2.333
1.00
59.19
B


ATOM
2731
O
ARG
B
167
37.647
51.615
1.303
1.00
58.60
B


ATOM
2732
N
GLY
B
168
37.404
50.656
3.320
1.00
58.18
B


ATOM
2733
CA
GLY
B
168
35.959
50.632
3.226
1.00
56.57
B


ATOM
2734
C
GLY
B
168
35.466
49.200
3.191
1.00
55.42
B


ATOM
2735
O
GLY
B
168
34.306
48.924
3.495
1.00
55.98
B


ATOM
2736
N
ASP
B
169
36.350
48.280
2.814
1.00
53.44
B


ATOM
2737
CA
ASP
B
169
35.979
46.871
2.757
1.00
51.76
B


ATOM
2738
CB
ASP
B
169
36.841
46.115
1.740
1.00
50.49
B


ATOM
2739
CG
ASP
B
169
36.428
46.392
0.311
1.00
50.57
B


ATOM
2740
OD1
ASP
B
169
35.207
46.479
0.060
1.00
49.92
B


ATOM
2741
OD2
ASP
B
169
37.318
46.507
−0.559
1.00
49.84
B


ATOM
2742
C
ASP
B
169
36.083
46.181
4.110
1.00
49.36
B


ATOM
2743
O
ASP
B
169
37.066
46.343
4.836
1.00
48.92
B


ATOM
2744
N
VAL
B
170
35.047
45.418
4.436
1.00
47.48
B


ATOM
2745
CA
VAL
B
170
34.981
44.667
5.680
1.00
45.10
B


ATOM
2746
CB
VAL
B
170
33.800
45.130
6.543
1.00
45.86
B


ATOM
2747
CG1
VAL
B
170
33.702
44.268
7.795
1.00
46.26
B


ATOM
2748
CG2
VAL
B
170
33.974
46.598
6.906
1.00
46.23
B


ATOM
2749
C
VAL
B
170
34.787
43.191
5.342
1.00
43.62
B


ATOM
2750
O
VAL
B
170
33.774
42.807
4.762
1.00
42.86
B


ATOM
2751
N
TYR
B
171
35.762
42.367
5.704
1.00
41.69
B


ATOM
2752
CA
TYR
B
171
35.694
40.935
5.425
1.00
38.95
B


ATOM
2753
CB
TYR
B
171
37.044
40.455
4.899
1.00
37.52
B


ATOM
2754
CG
TYR
B
171
37.405
41.031
3.553
1.00
38.12
B


ATOM
2755
CD1
TYR
B
171
37.023
40.391
2.376
1.00
37.52
B


ATOM
2756
CE1
TYR
B
171
37.342
40.923
1.131
1.00
38.06
B


ATOM
2757
CD2
TYR
B
171
38.118
42.224
3.454
1.00
37.54
B


ATOM
2758
CE2
TYR
B
171
38.442
42.767
2.216
1.00
38.45
B


ATOM
2759
CZ
TYR
B
171
38.052
42.110
1.056
1.00
39.25
B


ATOM
2760
OH
TYR
B
171
38.372
42.641
−0.172
1.00
38.84
B


ATOM
2761
C
TYR
B
171
35.314
40.139
6.671
1.00
37.46
B


ATOM
2762
O
TYR
B
171
35.791
40.428
7.773
1.00
34.85
B


ATOM
2763
N
THR
B
172
34.452
39.140
6.501
1.00
35.06
B


ATOM
2764
CA
THR
B
172
34.049
38.328
7.638
1.00
35.81
B


ATOM
2765
CB
THR
B
172
32.589
38.622
8.064
1.00
38.37
B


ATOM
2766
OG1
THR
B
172
31.688
38.177
7.043
1.00
42.02
B


ATOM
2767
CG2
THR
B
172
32.390
40.119
8.292
1.00
39.83
B


ATOM
2768
C
THR
B
172
34.182
36.830
7.406
1.00
33.71
B


ATOM
2769
O
THR
B
172
33.953
36.335
6.300
1.00
32.99
B


ATOM
2770
N
CYS
B
173
34.578
36.123
8.463
1.00
32.09
B


ATOM
2771
CA
CYS
B
173
34.714
34.670
8.438
1.00
31.08
B


ATOM
2772
C
CYS
B
173
33.497
34.183
9.200
1.00
30.92
B


ATOM
2773
O
CYS
B
173
33.240
34.614
10.326
1.00
32.70
B


ATOM
2774
CB
CYS
B
173
35.988
34.214
9.155
1.00
31.48
B


ATOM
2775
SG
CYS
B
173
36.338
32.436
8.983
1.00
31.85
B


ATOM
2776
N
HIS
B
174
32.748
33.288
8.578
1.00
30.26
B


ATOM
2777
CA
HIS
B
174
31.524
32.754
9.152
1.00
29.72
B


ATOM
2778
CB
HIS
B
174
30.401
32.977
8.128
1.00
30.80
B


ATOM
2779
CG
HIS
B
174
29.030
32.625
8.615
1.00
32.90
B


ATOM
2780
CD2
HIS
B
174
28.016
33.405
9.058
1.00
33.11
B


ATOM
2781
ND1
HIS
B
174
28.551
31.332
8.621
1.00
34.85
B


ATOM
2782
CE1
HIS
B
174
27.299
31.332
9.044
1.00
37.21
B


ATOM
2783
NE2
HIS
B
174
26.950
32.577
9.316
1.00
34.95
B


ATOM
2784
C
HIS
B
174
31.751
31.271
9.449
1.00
28.49
B


ATOM
2785
O
HIS
B
174
32.080
30.494
8.554
1.00
27.69
B


ATOM
2786
N
VAL
B
175
31.584
30.888
10.710
1.00
27.48
B


ATOM
2787
CA
VAL
B
175
31.810
29.508
11.121
1.00
25.94
B


ATOM
2788
CB
VAL
B
175
32.988
29.418
12.126
1.00
25.31
B


ATOM
2789
CG1
VAL
B
175
33.147
27.982
12.629
1.00
21.10
B


ATOM
2790
CG2
VAL
B
175
34.271
29.896
11.462
1.00
22.12
B


ATOM
2791
C
VAL
B
175
30.606
28.821
11.748
1.00
26.58
B


ATOM
2792
O
VAL
B
175
30.004
29.328
12.694
1.00
27.01
B


ATOM
2793
N
GLU
B
176
30.274
27.652
11.212
1.00
27.17
B


ATOM
2794
CA
GLU
B
176
29.168
26.846
11.712
1.00
28.51
B


ATOM
2795
CB
GLU
B
176
28.166
26.573
10.588
1.00
32.35
B


ATOM
2796
CG
GLU
B
176
27.454
27.827
10.082
1.00
38.87
B


ATOM
2797
CD
GLU
B
176
26.776
27.616
8.735
1.00
42.45
B


ATOM
2798
OE1
GLU
B
176
25.947
26.684
8.618
1.00
43.07
B


ATOM
2799
OE2
GLU
B
176
27.075
28.386
7.794
1.00
42.94
B


ATOM
2800
C
GLU
B
176
29.750
25.536
12.235
1.00
27.34
B


ATOM
2801
O
GLU
B
176
30.576
24.900
11.574
1.00
26.12
B


ATOM
2802
N
HIS
B
177
29.308
25.134
13.420
1.00
26.08
B


ATOM
2803
CA
HIS
B
177
29.800
23.921
14.049
1.00
26.30
B


ATOM
2804
CB
HIS
B
177
31.132
24.244
14.738
1.00
24.58
B


ATOM
2805
CG
HIS
B
177
31.759
23.076
15.422
1.00
22.32
B


ATOM
2806
CD2
HIS
B
177
32.646
22.156
14.977
1.00
21.05
B


ATOM
2807
ND1
HIS
B
177
31.437
22.711
16.710
1.00
21.01
B


ATOM
2808
CE1
HIS
B
177
32.097
21.613
17.030
1.00
23.72
B


ATOM
2809
NE2
HIS
B
177
32.838
21.255
15.995
1.00
23.87
B


ATOM
2810
C
HIS
B
177
28.762
23.413
15.057
1.00
27.87
B


ATOM
2811
O
HIS
B
177
28.059
24.205
15.672
1.00
29.54
B


ATOM
2812
N
PRO
B
178
28.654
22.085
15.237
1.00
29.57
B


ATOM
2813
CD
PRO
B
178
29.365
21.025
14.501
1.00
28.96
B


ATOM
2814
CA
PRO
B
178
27.687
21.497
16.175
1.00
31.71
B


ATOM
2815
CB
PRO
B
178
28.062
20.019
16.166
1.00
30.49
B


ATOM
2816
CG
PRO
B
178
28.503
19.810
14.769
1.00
30.01
B


ATOM
2817
C
PRO
B
178
27.649
22.071
17.595
1.00
33.29
B


ATOM
2818
O
PRO
B
178
26.619
22.020
18.256
1.00
35.00
B


ATOM
2819
N
SER
B
179
28.762
22.615
18.067
1.00
34.96
B


ATOM
2820
CA
SER
B
179
28.813
23.168
19.418
1.00
36.85
B


ATOM
2821
CB
SER
B
179
30.261
23.228
19.896
1.00
35.35
B


ATOM
2822
OG
SER
B
179
31.023
24.053
19.034
1.00
35.14
B


ATOM
2823
C
SER
B
179
28.206
24.564
19.522
1.00
38.40
B


ATOM
2824
O
SER
B
179
27.953
25.056
20.619
1.00
37.27
B


ATOM
2825
N
LEU
B
180
27.971
25.192
18.377
1.00
40.10
B


ATOM
2826
CA
LEU
B
180
27.434
26.545
18.340
1.00
41.36
B


ATOM
2827
CB
LEU
B
180
28.162
27.352
17.269
1.00
39.74
B


ATOM
2828
CG
LEU
B
180
29.677
27.432
17.422
1.00
39.93
B


ATOM
2829
CD1
LEU
B
180
30.286
28.013
16.157
1.00
39.41
B


ATOM
2830
CD2
LEU
B
180
30.021
28.279
18.636
1.00
39.61
B


ATOM
2831
C
LEU
B
180
25.944
26.633
18.078
1.00
43.85
B


ATOM
2832
O
LEU
B
180
25.449
26.125
17.072
1.00
44.25
B


ATOM
2833
N
GLN
B
181
25.230
27.289
18.984
1.00
47.20
B


ATOM
2834
CA
GLN
B
181
23.794
27.475
18.814
1.00
49.93
B


ATOM
2835
CB
GLN
B
181
23.158
27.956
20.121
1.00
52.00
B


ATOM
2836
CG
GLN
B
181
23.873
29.134
20.758
1.00
56.40
B


ATOM
2837
CD
GLN
B
181
23.263
29.538
22.084
1.00
59.03
B


ATOM
2838
OE1
GLN
B
181
22.087
29.908
22.153
1.00
60.55
B


ATOM
2839
NE2
GLN
B
181
24.059
29.468
23.149
1.00
58.44
B


ATOM
2840
C
GLN
B
181
23.635
28.522
17.715
1.00
49.23
B


ATOM
2841
O
GLN
B
181
22.712
28.465
16.906
1.00
49.91
B


ATOM
2842
N
SER
B
182
24.560
29.474
17.688
1.00
48.48
B


ATOM
2843
CA
SER
B
182
24.555
30.523
16.679
1.00
47.89
B


ATOM
2844
CB
SER
B
182
24.241
31.879
17.314
1.00
48.68
B


ATOM
2845
OG
SER
B
182
25.211
32.223
18.286
1.00
50.58
B


ATOM
2846
C
SER
B
182
25.938
30.550
16.038
1.00
45.93
B


ATOM
2847
O
SER
B
182
26.945
30.354
16.714
1.00
45.13
B


ATOM
2848
N
PRO
B
183
26.004
30.783
14.721
1.00
45.12
B


ATOM
2849
CD
PRO
B
183
24.911
31.096
13.784
1.00
44.93
B


ATOM
2850
CA
PRO
B
183
27.302
30.819
14.042
1.00
43.29
B


ATOM
2851
CB
PRO
B
183
26.923
31.070
12.581
1.00
43.70
B


ATOM
2852
CG
PRO
B
183
25.642
31.833
12.688
1.00
44.70
B


ATOM
2853
C
PRO
B
183
28.254
31.876
14.593
1.00
40.67
B


ATOM
2854
O
PRO
B
183
27.828
32.851
15.209
1.00
40.46
B


ATOM
2855
N
ILE
B
184
29.547
31.664
14.382
1.00
37.76
B


ATOM
2856
CA
ILE
B
184
30.550
32.607
14.842
1.00
35.88
B


ATOM
2857
CB
ILE
B
184
31.759
31.889
15.468
1.00
35.92
B


ATOM
2858
CG2
ILE
B
184
32.907
32.867
15.657
1.00
35.57
B


ATOM
2859
CG1
ILE
B
184
31.362
31.270
16.806
1.00
36.74
B


ATOM
2860
CD1
ILE
B
184
32.475
30.477
17.458
1.00
36.59
B


ATOM
2861
C
ILE
B
184
31.040
33.453
13.680
1.00
34.88
B


ATOM
2862
O
ILE
B
184
31.412
32.932
12.630
1.00
35.06
B


ATOM
2863
N
THR
B
185
31.043
34.764
13.876
1.00
34.50
B


ATOM
2864
CA
THR
B
185
31.500
35.675
12.845
1.00
34.32
B


ATOM
2865
CB
THR
B
185
30.356
36.592
12.341
1.00
35.40
B


ATOM
2866
OG1
THR
B
185
29.770
37.285
13.450
1.00
37.01
B


ATOM
2867
CG2
THR
B
185
29.286
35.774
11.631
1.00
35.73
B


ATOM
2868
C
THR
B
185
32.622
36.548
13.375
1.00
33.38
B


ATOM
2869
O
THR
B
185
32.559
37.050
14.494
1.00
32.86
B


ATOM
2870
N
VAL
B
186
33.652
36.713
12.560
1.00
32.69
B


ATOM
2871
CA
VAL
B
186
34.791
37.538
12.911
1.00
33.21
B


ATOM
2872
CB
VAL
B
186
36.041
36.683
13.155
1.00
33.39
B


ATOM
2873
CG1
VAL
B
186
37.212
37.570
13.516
1.00
33.93
B


ATOM
2874
CG2
VAL
B
186
35.766
35.674
14.262
1.00
33.67
B


ATOM
2875
C
VAL
B
186
35.023
38.454
11.721
1.00
34.68
B


ATOM
2876
O
VAL
B
186
35.060
37.997
10.579
1.00
32.50
B


ATOM
2877
N
GLU
B
187
35.172
39.746
11.988
1.00
36.30
B


ATOM
2878
CA
GLU
B
187
35.373
40.713
10.922
1.00
38.96
B


ATOM
2879
CB
GLU
B
187
34.484
41.937
11.154
1.00
40.90
B


ATOM
2880
CG
GLU
B
187
33.008
41.623
11.333
1.00
46.09
B


ATOM
2881
CD
GLU
B
187
32.146
42.876
11.421
1.00
48.81
B


ATOM
2882
OE1
GLU
B
187
30.909
42.739
11.545
1.00
51.77
B


ATOM
2883
OE2
GLU
B
187
32.701
43.997
11.363
1.00
49.79
B


ATOM
2884
C
GLU
B
187
36.816
41.175
10.784
1.00
39.59
B


ATOM
2885
O
GLU
B
187
37.637
40.998
11.684
1.00
39.84
B


ATOM
2886
N
TRP
B
188
37.113
41.765
9.635
1.00
39.59
B


ATOM
2887
CA
TRP
B
188
38.430
42.302
9.360
1.00
40.86
B


ATOM
2888
CB
TRP
B
188
39.339
41.252
8.736
1.00
38.70
B


ATOM
2889
CG
TRP
B
188
40.769
41.704
8.693
1.00
37.82
B


ATOM
2890
CD2
TRP
B
188
41.421
42.383
7.615
1.00
36.62
B


ATOM
2891
CE2
TRP
B
188
42.748
42.640
8.023
1.00
36.31
B


ATOM
2892
CE3
TRP
B
188
41.013
42.799
6.340
1.00
36.14
B


ATOM
2893
CD1
TRP
B
188
41.698
41.583
9.686
1.00
37.31
B


ATOM
2894
NE1
TRP
B
188
42.890
42.141
9.291
1.00
37.27
B


ATOM
2895
CZ2
TRP
B
188
43.673
43.296
7.204
1.00
37.17
B


ATOM
2896
CZ3
TRP
B
188
41.932
43.452
5.522
1.00
38.70
B


ATOM
2897
CH2
TRP
B
188
43.249
43.694
5.960
1.00
37.13
B


ATOM
2898
C
TRP
B
188
38.258
43.455
8.383
1.00
42.97
B


ATOM
2899
O
TRP
B
188
37.946
43.240
7.211
1.00
42.37
B


ATOM
2900
N
ARG
B
189
38.442
44.678
8.864
1.00
46.69
B


ATOM
2901
CA
ARG
B
189
38.303
45.842
7.999
1.00
50.32
B


ATOM
2902
CB
ARG
B
189
37.731
47.040
8.776
1.00
52.18
B


ATOM
2903
CG
ARG
B
189
38.615
47.590
9.893
1.00
56.00
B


ATOM
2904
CD
ARG
B
189
38.234
47.041
11.270
1.00
59.95
B


ATOM
2905
NE
ARG
B
189
38.639
45.650
11.479
1.00
63.62
B


ATOM
2906
CZ
ARG
B
189
39.903
45.236
11.559
1.00
64.33
B


ATOM
2907
NH1
ARG
B
189
40.899
46.105
11.447
1.00
65.45
B


ATOM
2908
NH2
ARG
B
189
40.172
43.951
11.760
1.00
64.46
B


ATOM
2909
C
ARG
B
189
39.664
46.192
7.412
1.00
50.56
B


ATOM
2910
O
ARG
B
189
40.680
46.119
8.100
1.00
50.34
B


ATOM
2911
N
ALA
B
190
39.684
46.554
6.135
1.00
52.30
B


ATOM
2912
CA
ALA
B
190
40.933
46.911
5.476
1.00
54.16
B


ATOM
2913
CB
ALA
B
190
40.846
46.592
3.987
1.00
55.33
B


ATOM
2914
C
ALA
B
190
41.238
48.392
5.679
1.00
55.19
B


ATOM
2915
O
ALA
B
190
40.300
49.147
6.023
1.00
54.90
B


ATOM
2916
OXT
ALA
B
190
42.408
48.782
5.481
1.00
56.19
B


ATOM
2917
C
LEU
C
1
32.073
1.033
33.225
1.00
35.70
C


ATOM
2918
O
LEU
C
1
33.091
1.607
33.619
1.00
35.87
C


ATOM
2919
N
LEU
C
1
29.791
1.906
32.702
1.00
36.17
C


ATOM
2920
CA
LEU
C
1
30.699
1.409
33.777
1.00
34.35
C


ATOM
2921
N
GLN
C
2
32.105
0.072
32.307
1.00
34.64
C


ATOM
2922
CA
GLN
C
2
33.374
−0.359
31.737
1.00
34.20
C


ATOM
2923
C
GLN
C
2
33.250
−0.823
30.294
1.00
33.55
C


ATOM
2924
O
GLN
C
2
32.373
−1.610
29.955
1.00
33.68
C


ATOM
2925
N
PRO
C
3
34.130
−0.329
29.418
1.00
33.74
C


ATOM
2926
CD
PRO
C
3
35.226
0.632
29.639
1.00
33.81
C


ATOM
2927
CA
PRO
C
3
34.064
−0.742
28.015
1.00
34.77
C


ATOM
2928
CB
PRO
C
3
35.027
0.222
27.329
1.00
34.33
C


ATOM
2929
CG
PRO
C
3
36.070
0.449
28.393
1.00
34.78
C


ATOM
2930
C
PRO
C
3
34.508
−2.195
27.890
1.00
34.42
C


ATOM
2931
O
PRO
C
3
35.435
−2.626
28.579
1.00
34.76
C


ATOM
2932
N
PHE
C
4
33.837
−2.947
27.024
1.00
31.97
C


ATOM
2933
CA
PHE
C
4
34.173
−4.355
26.812
1.00
32.26
C


ATOM
2934
CB
PHE
C
4
32.897
−5.193
26.632
1.00
34.22
C


ATOM
2935
CG
PHE
C
4
32.006
−5.235
27.852
1.00
37.02
C


ATOM
2936
CD1
PHE
C
4
32.481
−4.835
29.103
1.00
38.53
C


ATOM
2937
CD2
PHE
C
4
30.701
−5.726
27.756
1.00
40.29
C


ATOM
2938
CE1
PHE
C
4
31.673
−4.925
30.248
1.00
40.80
C


ATOM
2939
CE2
PHE
C
4
29.878
−5.824
28.891
1.00
41.19
C


ATOM
2940
CZ
PHE
C
4
30.369
−5.421
30.142
1.00
40.74
C


ATOM
2941
C
PHE
C
4
35.052
−4.483
25.571
1.00
29.17
C


ATOM
2942
O
PHE
C
4
34.655
−4.072
24.482
1.00
30.93
C


ATOM
2943
N
PRO
C
5
36.257
−5.059
25.715
1.00
26.63
C


ATOM
2944
CD
PRO
C
5
36.936
−5.421
26.974
1.00
24.97
C


ATOM
2945
CA
PRO
C
5
37.168
−5.217
24.577
1.00
23.69
C


ATOM
2946
CB
PRO
C
5
38.527
−5.052
25.227
1.00
23.66
C


ATOM
2947
CG
PRO
C
5
38.335
−5.832
26.504
1.00
23.13
C


ATOM
2948
C
PRO
C
5
37.043
−6.569
23.887
1.00
22.95
C


ATOM
2949
O
PRO
C
5
36.403
−7.475
24.404
1.00
22.96
C


ATOM
2950
N
GLN
C
6
37.666
−6.696
22.719
1.00
23.53
C


ATOM
2951
CA
GLN
C
6
37.659
−7.945
21.967
1.00
21.10
C


ATOM
2952
CB
GLN
C
6
37.506
−7.670
20.475
1.00
20.90
C


ATOM
2953
CG
GLN
C
6
36.170
−7.105
20.063
1.00
21.10
C


ATOM
2954
CD
GLN
C
6
36.074
−6.901
18.557
1.00
22.85
C


ATOM
2955
OE1
GLN
C
6
36.483
−7.760
17.773
1.00
23.94
C


ATOM
2956
NE2
GLN
C
6
35.525
−5.766
18.149
1.00
20.70
C


ATOM
2957
C
GLN
C
6
38.996
−8.637
22.204
1.00
20.71
C


ATOM
2958
O
GLN
C
6
40.046
−8.008
22.105
1.00
19.85
C


ATOM
2959
N
PRO
C
7
38.974
−9.932
22.548
1.00
21.37
C


ATOM
2960
CD
PRO
C
7
37.810
−10.710
23.017
1.00
21.21
C


ATOM
2961
CA
PRO
C
7
40.215
−10.673
22.790
1.00
21.62
C


ATOM
2962
CB
PRO
C
7
39.783
−11.730
23.795
1.00
21.96
C


ATOM
2963
CG
PRO
C
7
38.416
−12.085
23.297
1.00
20.65
C


ATOM
2964
C
PRO
C
7
40.741
−11.316
21.511
1.00
24.05
C


ATOM
2965
O
PRO
C
7
39.972
−11.577
20.588
1.00
22.84
C


ATOM
2966
N
GLU
C
8
42.051
−11.550
21.448
1.00
26.22
C


ATOM
2967
CA
GLU
C
8
42.631
−12.215
20.292
1.00
27.00
C


ATOM
2968
CB
GLU
C
8
44.038
−11.687
19.988
1.00
27.94
C


ATOM
2969
CG
GLU
C
8
44.803
−12.494
18.915
1.00
28.38
C


ATOM
2970
CD
GLU
C
8
44.043
−12.649
17.589
1.00
31.32
C


ATOM
2971
OE1
GLU
C
8
42.980
−13.309
17.564
1.00
31.69
C


ATOM
2972
OE2
GLU
C
8
44.514
−12.112
16.563
1.00
29.86
C


ATOM
2973
C
GLU
C
8
42.678
−13.691
20.676
1.00
28.48
C


ATOM
2974
O
GLU
C
8
42.937
−14.029
21.829
1.00
28.74
C


ATOM
2975
N
LEU
C
9
42.407
−14.571
19.721
1.00
30.08
C


ATOM
2976
CA
LEU
C
9
42.404
−15.998
20.002
1.00
31.21
C


ATOM
2977
CB
LEU
C
9
41.313
−16.688
19.183
1.00
32.12
C


ATOM
2978
CG
LEU
C
9
39.918
−16.072
19.302
1.00
33.78
C


ATOM
2979
CD1
LEU
C
9
38.941
−16.866
18.457
1.00
35.00
C


ATOM
2980
CD2
LEU
C
9
39.481
−16.061
20.761
1.00
35.59
C


ATOM
2981
C
LEU
C
9
43.748
−16.641
19.712
1.00
31.83
C


ATOM
2982
O
LEU
C
9
44.342
−16.415
18.658
1.00
30.94
C


ATOM
2983
N
PRO
C
10
44.256
−17.442
20.657
1.00
33.31
C


ATOM
2984
CD
PRO
C
10
43.774
−17.661
22.032
1.00
33.12
C


ATOM
2985
CA
PRO
C
10
45.545
−18.097
20.439
1.00
36.08
C


ATOM
2986
CB
PRO
C
10
45.926
−18.590
21.836
1.00
36.62
C


ATOM
2987
CG
PRO
C
10
44.598
−18.846
22.476
1.00
35.26
C


ATOM
2988
C
PRO
C
10
45.428
−19.229
19.430
1.00
37.51
C


ATOM
2989
O
PRO
C
10
44.495
−20.030
19.491
1.00
39.49
C


ATOM
2990
N
TYR
C
11
46.365
−19.269
18.488
1.00
38.68
C


ATOM
2991
CA
TYR
C
11
46.392
−20.305
17.463
1.00
40.24
C


ATOM
2992
C
TYR
C
11
47.834
−20.782
17.290
1.00
42.03
C


ATOM
2993
O
TYR
C
11
48.121
−21.967
17.586
1.00
42.72
C


ATOM
2994
OXT
TYR
C
11
48.665
−19.949
16.870
1.00
42.75
C


ATOM
2995
CB
VAL
D
2
76.722
40.050
4.030
1.00
35.81
D


ATOM
2996
CG1
VAL
D
2
77.537
40.465
2.823
1.00
36.64
D


ATOM
2997
CG2
VAL
D
2
76.313
38.577
3.893
1.00
37.71
D


ATOM
2998
C
VAL
D
2
76.622
40.298
6.537
1.00
31.61
D


ATOM
2999
O
VAL
D
2
75.696
39.494
6.653
1.00
31.96
D


ATOM
3000
N
VAL
D
2
78.625
39.207
5.418
1.00
32.12
D


ATOM
3001
CA
VAL
D
2
77.560
40.255
5.317
1.00
33.74
D


ATOM
3002
N
ALA
D
3
76.864
41.246
7.441
1.00
29.52
D


ATOM
3003
CA
ALA
D
3
76.053
41.379
8.653
1.00
27.92
D


ATOM
3004
CB
ALA
D
3
76.480
40.321
9.684
1.00
27.11
D


ATOM
3005
C
ALA
D
3
76.128
42.767
9.286
1.00
25.71
D


ATOM
3006
O
ALA
D
3
77.050
43.540
9.016
1.00
23.11
D


ATOM
3007
N
ASP
D
4
75.152
43.070
10.137
1.00
24.26
D


ATOM
3008
CA
ASP
D
4
75.109
44.354
10.825
1.00
24.77
D


ATOM
3009
CB
ASP
D
4
73.774
44.533
11.555
1.00
25.88
D


ATOM
3010
CG
ASP
D
4
72.595
44.668
10.611
1.00
26.24
D


ATOM
3011
OD1
ASP
D
4
71.449
44.489
11.080
1.00
24.74
D


ATOM
3012
OD2
ASP
D
4
72.811
44.961
9.416
1.00
28.25
D


ATOM
3013
C
ASP
D
4
76.230
44.407
11.857
1.00
25.96
D


ATOM
3014
O
ASP
D
4
76.882
45.437
12.027
1.00
26.40
D


ATOM
3015
N
HIS
D
5
76.440
43.290
12.549
1.00
24.52
D


ATOM
3016
CA
HIS
D
5
77.469
43.204
13.582
1.00
24.25
D


ATOM
3017
CB
HIS
D
5
76.836
43.302
14.972
1.00
23.42
D


ATOM
3018
CG
HIS
D
5
76.138
44.599
15.231
1.00
26.12
D


ATOM
3019
CD2
HIS
D
5
76.567
45.879
15.126
1.00
26.16
D


ATOM
3020
ND1
HIS
D
5
74.830
44.667
15.657
1.00
25.67
D


ATOM
3021
CE1
HIS
D
5
74.481
45.932
15.799
1.00
26.53
D


ATOM
3022
NE2
HIS
D
5
75.516
46.688
15.484
1.00
25.96
D


ATOM
3023
C
HIS
D
5
78.241
41.895
13.492
1.00
22.88
D


ATOM
3024
O
HIS
D
5
77.657
40.835
13.258
1.00
22.31
D


ATOM
3025
N
VAL
D
6
79.552
41.980
13.691
1.00
20.27
D


ATOM
3026
CA
VAL
D
6
80.421
40.815
13.657
1.00
19.49
D


ATOM
3027
CB
VAL
D
6
81.419
40.866
12.486
1.00
20.45
D


ATOM
3028
CG1
VAL
D
6
82.357
39.674
12.564
1.00
19.85
D


ATOM
3029
CG2
VAL
D
6
80.674
40.869
11.161
1.00
25.29
D


ATOM
3030
C
VAL
D
6
81.223
40.792
14.944
1.00
18.77
D


ATOM
3031
O
VAL
D
6
81.767
41.812
15.352
1.00
17.70
D


ATOM
3032
N
ALA
D
7
81.304
39.626
15.575
1.00
18.23
D


ATOM
3033
CA
ALA
D
7
82.046
39.489
16.821
1.00
18.01
D


ATOM
3034
CB
ALA
D
7
81.080
39.452
18.006
1.00
17.61
D


ATOM
3035
C
ALA
D
7
82.899
38.239
16.838
1.00
17.37
D


ATOM
3036
O
ALA
D
7
82.568
37.242
16.208
1.00
19.56
D


ATOM
3037
N
SER
D
8
84.008
38.306
17.562
1.00
17.07
D


ATOM
3038
CA
SER
D
8
84.892
37.158
17.712
1.00
15.46
D


ATOM
3039
CB
SER
D
8
86.297
37.455
17.202
1.00
12.56
D


ATOM
3040
OG
SER
D
8
86.324
37.492
15.789
1.00
18.97
D


ATOM
3041
C
SER
D
8
84.932
36.904
19.201
1.00
16.39
D


ATOM
3042
O
SER
D
8
85.613
37.614
19.951
1.00
15.61
D


ATOM
3043
N
TYR
D
9
84.144
35.930
19.637
1.00
17.58
D


ATOM
3044
CA
TYR
D
9
84.096
35.587
21.044
1.00
18.51
D


ATOM
3045
CB
TYR
D
9
82.698
35.133
21.444
1.00
17.92
D


ATOM
3046
CG
TYR
D
9
81.730
36.290
21.362
1.00
17.41
D


ATOM
3047
CD1
TYR
D
9
82.056
37.523
21.928
1.00
16.27
D


ATOM
3048
CE1
TYR
D
9
81.208
38.603
21.840
1.00
15.18
D


ATOM
3049
CD2
TYR
D
9
80.515
36.169
20.701
1.00
17.05
D


ATOM
3050
CE2
TYR
D
9
79.649
37.252
20.608
1.00
18.01
D


ATOM
3051
CZ
TYR
D
9
80.005
38.466
21.181
1.00
16.67
D


ATOM
3052
OH
TYR
D
9
79.157
39.543
21.104
1.00
20.30
D


ATOM
3053
C
TYR
D
9
85.120
34.508
21.115
1.00
19.92
D


ATOM
3054
O
TYR
D
9
84.856
33.323
21.337
1.00
17.21
D


ATOM
3055
N
GLY
D
10
86.321
34.989
20.843
1.00
22.61
D


ATOM
3056
CA
GLY
D
10
87.478
34.160
20.836
1.00
20.96
D


ATOM
3057
C
GLY
D
10
88.358
34.354
19.624
1.00
18.79
D


ATOM
3058
O
GLY
D
10
88.170
33.693
18.618
1.00
16.79
D


ATOM
3059
N
VAL
D
11
89.275
35.307
19.683
1.00
17.75
D


ATOM
3060
CA
VAL
D
11
90.256
35.394
18.616
1.00
16.92
D


ATOM
3061
CB
VAL
D
11
90.666
36.829
18.242
1.00
17.76
D


ATOM
3062
CG1
VAL
D
11
91.873
36.778
17.313
1.00
15.46
D


ATOM
3063
CG2
VAL
D
11
89.522
37.544
17.544
1.00
13.00
D


ATOM
3064
C
VAL
D
11
91.391
34.728
19.395
1.00
17.46
D


ATOM
3065
O
VAL
D
11
91.865
35.266
20.405
1.00
18.93
D


ATOM
3066
N
ASN
D
12
91.773
33.531
18.973
1.00
17.46
D


ATOM
3067
CA
ASN
D
12
92.831
32.779
19.644
1.00
18.01
D


ATOM
3068
CB
ASN
D
12
92.339
31.360
19.969
1.00
16.68
D


ATOM
3069
CG
ASN
D
12
91.179
31.356
20.955
1.00
16.27
D


ATOM
3070
OD1
ASN
D
12
91.346
30.989
22.115
1.00
14.97
D


ATOM
3071
ND2
ASN
D
12
90.000
31.779
20.497
1.00
14.97
D


ATOM
3072
C
ASN
D
12
94.061
32.699
18.759
1.00
18.74
D


ATOM
3073
O
ASN
D
12
93.963
32.373
17.578
1.00
19.66
D


ATOM
3074
N
LEU
D
13
95.221
32.969
19.344
1.00
20.75
D


ATOM
3075
CA
LEU
D
13
96.471
32.949
18.600
1.00
22.59
D


ATOM
3076
CB
LEU
D
13
96.841
34.387
18.234
1.00
24.32
D


ATOM
3077
CG
LEU
D
13
98.215
34.672
17.632
1.00
25.29
D


ATOM
3078
CD1
LEU
D
13
98.355
33.966
16.289
1.00
24.58
D


ATOM
3079
CD2
LEU
D
13
98.380
36.177
17.475
1.00
23.52
D


ATOM
3080
C
LEU
D
13
97.646
32.290
19.330
1.00
22.44
D


ATOM
3081
O
LEU
D
13
97.900
32.578
20.494
1.00
24.67
D


ATOM
3082
N
TYR
D
14
98.350
31.397
18.641
1.00
23.69
D


ATOM
3083
CA
TYR
D
14
99.535
30.740
19.196
1.00
25.57
D


ATOM
3084
CB
TYR
D
14
99.223
29.360
19.765
1.00
26.53
D


ATOM
3085
CG
TYR
D
14
100.445
28.712
20.383
1.00
28.87
D


ATOM
3086
CD1
TYR
D
14
100.872
29.057
21.668
1.00
28.57
D


ATOM
3087
CE1
TYR
D
14
102.032
28.500
22.218
1.00
27.29
D


ATOM
3088
CD2
TYR
D
14
101.209
27.793
19.664
1.00
29.65
D


ATOM
3089
CE2
TYR
D
14
102.369
27.235
20.204
1.00
26.94
D


ATOM
3090
CZ
TYR
D
14
102.773
27.592
21.477
1.00
27.22
D


ATOM
3091
OH
TYR
D
14
103.914
27.039
22.008
1.00
29.69
D


ATOM
3092
C
TYR
D
14
100.553
30.574
18.074
1.00
26.73
D


ATOM
3093
O
TYR
D
14
100.210
30.128
16.980
1.00
27.22
D


ATOM
3094
N
GLN
D
15
101.800
30.945
18.338
1.00
26.92
D


ATOM
3095
CA
GLN
D
15
102.847
30.820
17.332
1.00
27.70
D


ATOM
3096
CB
GLN
D
15
103.164
32.179
16.710
1.00
27.39
D


ATOM
3097
CG
GLN
D
15
103.534
33.251
17.704
1.00
27.78
D


ATOM
3098
CD
GLN
D
15
103.806
34.590
17.044
1.00
27.70
D


ATOM
3099
OE1
GLN
D
15
103.723
35.638
17.685
1.00
31.07
D


ATOM
3100
NE2
GLN
D
15
104.142
34.562
15.763
1.00
25.83
D


ATOM
3101
C
GLN
D
15
104.097
30.222
17.952
1.00
28.40
D


ATOM
3102
O
GLN
D
15
104.368
30.416
19.141
1.00
28.81
D


ATOM
3103
N
SER
D
16
104.852
29.488
17.143
1.00
27.95
D


ATOM
3104
CA
SER
D
16
106.070
28.834
17.611
1.00
28.04
D


ATOM
3105
CB
SER
D
16
106.613
27.887
16.534
1.00
25.04
D


ATOM
3106
OG
SER
D
16
106.879
28.581
15.330
1.00
26.28
D


ATOM
3107
C
SER
D
16
107.155
29.824
18.024
1.00
27.77
D


ATOM
3108
O
SER
D
16
107.922
29.558
18.946
1.00
26.81
D


ATOM
3109
N
TYR
D
17
107.221
30.965
17.351
1.00
29.70
D


ATOM
3110
CA
TYR
D
17
108.228
31.953
17.694
1.00
32.41
D


ATOM
3111
CB
TYR
D
17
108.248
33.086
16.672
1.00
35.15
D


ATOM
3112
CG
TYR
D
17
109.440
33.986
16.864
1.00
40.80
D


ATOM
3113
CD1
TYR
D
17
110.719
33.556
16.508
1.00
43.28
D


ATOM
3114
CE1
TYR
D
17
111.836
34.345
16.743
1.00
44.62
D


ATOM
3115
CD2
TYR
D
17
109.308
35.235
17.460
1.00
40.97
D


ATOM
3116
CE2
TYR
D
17
110.419
36.032
17.702
1.00
44.83
D


ATOM
3117
CZ
TYR
D
17
111.679
35.580
17.341
1.00
45.74
D


ATOM
3118
OH
TYR
D
17
112.788
36.353
17.590
1.00
49.39
D


ATOM
3119
C
TYR
D
17
107.954
32.525
19.084
1.00
33.13
D


ATOM
3120
O
TYR
D
17
106.888
33.092
19.332
1.00
32.77
D


ATOM
3121
N
GLY
D
18
108.930
32.383
19.981
1.00
32.74
D


ATOM
3122
CA
GLY
D
18
108.780
32.867
21.341
1.00
31.76
D


ATOM
3123
C
GLY
D
18
108.958
31.716
22.311
1.00
32.63
D


ATOM
3124
O
GLY
D
18
110.005
31.600
22.948
1.00
34.20
D


ATOM
3125
N
PRO
D
19
107.946
30.840
22.452
1.00
33.13
D


ATOM
3126
CD
PRO
D
19
108.029
29.606
23.256
1.00
31.73
D


ATOM
3127
CA
PRO
D
19
106.663
30.906
21.741
1.00
32.71
D


ATOM
3128
CB
PRO
D
19
106.115
29.492
21.903
1.00
33.20
D


ATOM
3129
CG
PRO
D
19
106.591
29.128
23.280
1.00
31.76
D


ATOM
3130
C
PRO
D
19
105.768
31.948
22.406
1.00
32.52
D


ATOM
3131
O
PRO
D
19
105.970
32.282
23.568
1.00
33.11
D


ATOM
3132
N
SER
D
20
104.786
32.463
21.676
1.00
31.92
D


ATOM
3133
CA
SER
D
20
103.886
33.455
22.246
1.00
30.99
D


ATOM
3134
CB
SER
D
20
104.287
34.867
21.795
1.00
30.92
D


ATOM
3135
OG
SER
D
20
104.263
34.988
20.381
1.00
33.16
D


ATOM
3136
C
SER
D
20
102.441
33.172
21.852
1.00
30.01
D


ATOM
3137
O
SER
D
20
102.179
32.428
20.902
1.00
29.42
D


ATOM
3138
N
GLY
D
21
101.512
33.763
22.598
1.00
27.60
D


ATOM
3139
CA
GLY
D
21
100.101
33.580
22.318
1.00
25.70
D


ATOM
3140
C
GLY
D
21
99.309
34.836
22.632
1.00
24.66
D


ATOM
3141
O
GLY
D
21
99.848
35.798
23.187
1.00
23.84
D


ATOM
3142
N
GLN
D
22
98.030
34.834
22.268
1.00
22.55
D


ATOM
3143
CA
GLN
D
22
97.149
35.974
22.527
1.00
20.16
D


ATOM
3144
CB
GLN
D
22
97.301
37.049
21.445
1.00
18.28
D


ATOM
3145
CG
GLN
D
22
96.416
38.284
21.672
1.00
18.60
D


ATOM
3146
CD
GLN
D
22
96.513
39.327
20.562
1.00
18.36
D


ATOM
3147
OE1
GLN
D
22
97.379
40.207
20.587
1.00
19.82
D


ATOM
3148
NE2
GLN
D
22
95.617
39.232
19.582
1.00
17.69
D


ATOM
3149
C
GLN
D
22
95.699
35.517
22.561
1.00
18.61
D


ATOM
3150
O
GLN
D
22
95.301
34.638
21.790
1.00
17.26
D


ATOM
3151
N
TYR
D
23
94.926
36.097
23.475
1.00
16.42
D


ATOM
3152
CA
TYR
D
23
93.507
35.785
23.592
1.00
16.21
D


ATOM
3153
CB
TYR
D
23
93.212
34.839
24.762
1.00
14.97
D


ATOM
3154
CG
TYR
D
23
91.750
34.438
24.798
1.00
14.24
D


ATOM
3155
CD1
TYR
D
23
91.309
33.318
24.109
1.00
14.49
D


ATOM
3156
CE1
TYR
D
23
89.969
33.004
24.029
1.00
14.23
D


ATOM
3157
CD2
TYR
D
23
90.795
35.240
25.421
1.00
13.21
D


ATOM
3158
CE2
TYR
D
23
89.443
34.934
25.344
1.00
13.08
D


ATOM
3159
CZ
TYR
D
23
89.039
33.814
24.647
1.00
12.88
D


ATOM
3160
OH
TYR
D
23
87.710
33.471
24.566
1.00
16.44
D


ATOM
3161
C
TYR
D
23
92.751
37.089
23.806
1.00
15.56
D


ATOM
3162
O
TYR
D
23
93.014
37.817
24.763
1.00
16.57
D


ATOM
3163
N
THR
D
24
91.811
37.377
22.914
1.00
14.11
D


ATOM
3164
CA
THR
D
24
91.026
38.598
22.995
1.00
13.31
D


ATOM
3165
CB
THR
D
24
91.606
39.692
22.071
1.00
16.07
D


ATOM
3166
OG1
THR
D
24
91.682
39.176
20.734
1.00
17.94
D


ATOM
3167
CG2
THR
D
24
92.992
40.116
22.514
1.00
13.19
D


ATOM
3168
C
THR
D
24
89.604
38.342
22.519
1.00
12.68
D


ATOM
3169
O
THR
D
24
89.306
37.287
21.994
1.00
15.13
D


ATOM
3170
N
HIS
D
25
88.726
39.312
22.727
1.00
13.47
D


ATOM
3171
CA
HIS
D
25
87.360
39.224
22.229
1.00
13.83
D


ATOM
3172
CB
HIS
D
25
86.326
39.132
23.346
1.00
11.26
D


ATOM
3173
CG
HIS
D
25
86.053
37.727
23.785
1.00
14.42
D


ATOM
3174
CD2
HIS
D
25
86.815
36.610
23.723
1.00
12.09
D


ATOM
3175
ND1
HIS
D
25
84.876
37.351
24.392
1.00
15.93
D


ATOM
3176
CE1
HIS
D
25
84.922
36.064
24.685
1.00
14.24
D


ATOM
3177
NE2
HIS
D
25
86.089
35.591
24.289
1.00
13.67
D


ATOM
3178
C
HIS
D
25
87.158
40.495
21.436
1.00
13.30
D


ATOM
3179
O
HIS
D
25
87.573
41.563
21.859
1.00
13.77
D


ATOM
3180
N
GLU
D
26
86.544
40.376
20.271
1.00
15.40
D


ATOM
3181
CA
GLU
D
26
86.318
41.540
19.434
1.00
16.53
D


ATOM
3182
CB
GLU
D
26
87.109
41.396
18.133
1.00
14.47
D


ATOM
3183
CG
GLU
D
26
88.627
41.460
18.277
1.00
14.81
D


ATOM
3184
CD
GLU
D
26
89.341
41.205
16.947
1.00
19.22
D


ATOM
3185
OE1
GLU
D
26
88.726
41.429
15.884
1.00
22.84
D


ATOM
3186
OE2
GLU
D
26
90.512
40.792
16.953
1.00
17.41
D


ATOM
3187
C
GLU
D
26
84.841
41.721
19.111
1.00
17.28
D


ATOM
3188
O
GLU
D
26
84.073
40.760
19.100
1.00
16.62
D


ATOM
3189
N
PHE
D
27
84.455
42.971
18.879
1.00
19.63
D


ATOM
3190
CA
PHE
D
27
83.092
43.313
18.494
1.00
19.71
D


ATOM
3191
CB
PHE
D
27
82.231
43.722
19.684
1.00
21.05
D


ATOM
3192
CG
PHE
D
27
80.758
43.816
19.348
1.00
24.29
D


ATOM
3193
CD1
PHE
D
27
79.971
42.668
19.278
1.00
23.22
D


ATOM
3194
CD2
PHE
D
27
80.169
45.047
19.073
1.00
22.47
D


ATOM
3195
CE1
PHE
D
27
78.617
42.744
18.940
1.00
24.89
D


ATOM
3196
CE2
PHE
D
27
78.818
45.132
18.733
1.00
24.72
D


ATOM
3197
CZ
PHE
D
27
78.041
43.980
18.667
1.00
22.80
D


ATOM
3198
C
PHE
D
27
83.182
44.482
17.532
1.00
18.41
D


ATOM
3199
O
PHE
D
27
83.700
45.545
17.879
1.00
19.21
D


ATOM
3200
N
ASP
D
28
82.680
44.272
16.321
1.00
18.46
D


ATOM
3201
CA
ASP
D
28
82.700
45.284
15.272
1.00
18.63
D


ATOM
3202
CB
ASP
D
28
81.702
46.404
15.568
1.00
19.29
D


ATOM
3203
CG
ASP
D
28
80.268
45.981
15.305
1.00
22.52
D


ATOM
3204
OD1
ASP
D
28
80.076
44.885
14.738
1.00
23.13
D


ATOM
3205
OD2
ASP
D
28
79.333
46.736
15.651
1.00
24.61
D


ATOM
3206
C
ASP
D
28
84.075
45.865
15.037
1.00
17.83
D


ATOM
3207
O
ASP
D
28
84.225
47.069
14.860
1.00
20.60
D


ATOM
3208
N
GLY
D
29
85.079
44.997
15.042
1.00
18.44
D


ATOM
3209
CA
GLY
D
29
86.439
45.431
14.788
1.00
19.49
D


ATOM
3210
C
GLY
D
29
87.218
46.011
15.949
1.00
18.93
D


ATOM
3211
O
GLY
D
29
88.382
46.359
15.784
1.00
19.51
D


ATOM
3212
N
ASP
D
30
86.595
46.122
17.117
1.00
17.91
D


ATOM
3213
CA
ASP
D
30
87.279
46.667
18.288
1.00
17.21
D


ATOM
3214
CB
ASP
D
30
86.499
47.858
18.831
1.00
15.85
D


ATOM
3215
CG
ASP
D
30
86.594
49.060
17.924
1.00
18.96
D


ATOM
3216
OD1
ASP
D
30
87.731
49.515
17.668
1.00
18.56
D


ATOM
3217
OD2
ASP
D
30
85.541
49.544
17.466
1.00
19.00
D


ATOM
3218
C
ASP
D
30
87.491
45.629
19.389
1.00
17.20
D


ATOM
3219
O
ASP
D
30
86.651
44.763
19.621
1.00
15.68
D


ATOM
3220
N
GLU
D
31
88.629
45.739
20.062
1.00
18.79
D


ATOM
3221
CA
GLU
D
31
89.015
44.829
21.131
1.00
17.52
D


ATOM
3222
CB
GLU
D
31
90.531
44.947
21.363
1.00
19.03
D


ATOM
3223
CG
GLU
D
31
91.074
44.215
22.579
1.00
22.08
D


ATOM
3224
CD
GLU
D
31
92.596
44.254
22.653
1.00
25.29
D


ATOM
3225
OE1
GLU
D
31
93.198
45.159
22.041
1.00
26.54
D


ATOM
3226
OE2
GLU
D
31
93.193
43.387
23.331
1.00
25.19
D


ATOM
3227
C
GLU
D
31
88.248
45.109
22.421
1.00
17.80
D


ATOM
3228
O
GLU
D
31
88.360
46.195
23.004
1.00
16.81
D


ATOM
3229
N
GLN
D
32
87.478
44.118
22.862
1.00
15.25
D


ATOM
3230
CA
GLN
D
32
86.685
44.230
24.085
1.00
15.53
D


ATOM
3231
CB
GLN
D
32
85.502
43.260
24.044
1.00
12.86
D


ATOM
3232
CG
GLN
D
32
84.391
43.680
23.101
1.00
13.72
D


ATOM
3233
CD
GLN
D
32
83.233
42.708
23.111
1.00
16.53
D


ATOM
3234
OE1
GLN
D
32
83.407
41.526
22.838
1.00
20.27
D


ATOM
3235
NE2
GLN
D
32
82.044
43.203
23.423
1.00
17.48
D


ATOM
3236
C
GLN
D
32
87.528
43.956
25.329
1.00
16.00
D


ATOM
3237
O
GLN
D
32
87.356
44.603
26.366
1.00
15.18
D


ATOM
3238
N
PHE
D
33
88.423
42.981
25.222
1.00
16.17
D


ATOM
3239
CA
PHE
D
33
89.315
42.638
26.321
1.00
15.74
D


ATOM
3240
CB
PHE
D
33
88.520
42.083
27.515
1.00
15.40
D


ATOM
3241
CG
PHE
D
33
87.969
40.693
27.307
1.00
15.83
D


ATOM
3242
CD1
PHE
D
33
88.781
39.572
27.480
1.00
16.23
D


ATOM
3243
CD2
PHE
D
33
86.625
40.503
26.977
1.00
17.27
D


ATOM
3244
CE1
PHE
D
33
88.262
38.282
27.332
1.00
15.79
D


ATOM
3245
CE2
PHE
D
33
86.088
39.218
26.827
1.00
15.20
D


ATOM
3246
CZ
PHE
D
33
86.909
38.108
27.006
1.00
17.77
D


ATOM
3247
C
PHE
D
33
90.330
41.614
25.860
1.00
15.28
D


ATOM
3248
O
PHE
D
33
90.157
40.979
24.825
1.00
15.16
D


ATOM
3249
N
TYR
D
34
91.405
41.476
26.620
1.00
15.54
D


ATOM
3250
CA
TYR
D
34
92.414
40.480
26.314
1.00
16.00
D


ATOM
3251
CB
TYR
D
34
93.649
41.124
25.670
1.00
17.46
D


ATOM
3252
CG
TYR
D
34
94.508
41.970
26.588
1.00
20.90
D


ATOM
3253
CD1
TYR
D
34
95.488
41.390
27.391
1.00
21.91
D


ATOM
3254
CE1
TYR
D
34
96.295
42.174
28.221
1.00
24.17
D


ATOM
3255
CD2
TYR
D
34
94.351
43.354
26.638
1.00
20.26
D


ATOM
3256
CE2
TYR
D
34
95.147
44.141
27.463
1.00
24.97
D


ATOM
3257
CZ
TYR
D
34
96.117
43.546
28.251
1.00
23.87
D


ATOM
3258
OH
TYR
D
34
96.904
44.326
29.065
1.00
26.29
D


ATOM
3259
C
TYR
D
34
92.766
39.836
27.642
1.00
16.56
D


ATOM
3260
O
TYR
D
34
92.476
40.386
28.699
1.00
15.36
D


ATOM
3261
N
VAL
D
35
93.354
38.653
27.586
1.00
18.29
D


ATOM
3262
CA
VAL
D
35
93.768
37.971
28.795
1.00
19.11
D


ATOM
3263
CB
VAL
D
35
93.257
36.514
28.842
1.00
17.61
D


ATOM
3264
CG1
VAL
D
35
93.910
35.780
29.992
1.00
17.99
D


ATOM
3265
CG2
VAL
D
35
91.744
36.493
29.003
1.00
17.82
D


ATOM
3266
C
VAL
D
35
95.290
37.950
28.813
1.00
19.96
D


ATOM
3267
O
VAL
D
35
95.914
37.492
27.866
1.00
17.73
D


ATOM
3268
N
ASP
D
36
95.883
38.473
29.880
1.00
22.63
D


ATOM
3269
CA
ASP
D
36
97.333
38.456
30.005
1.00
24.79
D


ATOM
3270
CB
ASP
D
36
97.795
39.409
31.106
1.00
26.41
D


ATOM
3271
CG
ASP
D
36
99.298
39.574
31.131
1.00
30.12
D


ATOM
3272
OD1
ASP
D
36
100.002
38.547
31.252
1.00
32.04
D


ATOM
3273
OD2
ASP
D
36
99.776
40.726
31.028
1.00
32.20
D


ATOM
3274
C
ASP
D
36
97.650
37.011
30.389
1.00
25.23
D


ATOM
3275
O
ASP
D
36
97.349
36.575
31.502
1.00
25.21
D


ATOM
3276
N
LEU
D
37
98.236
36.272
29.455
1.00
23.64
D


ATOM
3277
CA
LEU
D
37
98.549
34.870
29.676
1.00
25.25
D


ATOM
3278
CB
LEU
D
37
98.992
34.232
28.355
1.00
21.08
D


ATOM
3279
CG
LEU
D
37
97.955
34.360
27.225
1.00
20.24
D


ATOM
3280
CD1
LEU
D
37
98.568
33.934
25.899
1.00
17.23
D


ATOM
3281
CD2
LEU
D
37
96.730
33.516
27.541
1.00
19.11
D


ATOM
3282
C
LEU
D
37
99.590
34.626
30.770
1.00
27.73
D


ATOM
3283
O
LEU
D
37
99.464
33.682
31.554
1.00
27.92
D


ATOM
3284
N
GLY
D
38
100.608
35.474
30.837
1.00
29.31
D


ATOM
3285
CA
GLY
D
38
101.629
35.292
31.851
1.00
30.44
D


ATOM
3286
C
GLY
D
38
101.141
35.640
33.242
1.00
32.52
D


ATOM
3287
O
GLY
D
38
101.502
34.986
34.220
1.00
34.37
D


ATOM
3288
N
ARG
D
39
100.309
36.669
33.335
1.00
35.10
D


ATOM
3289
CA
ARG
D
39
99.786
37.103
34.623
1.00
36.92
D


ATOM
3290
CB
ARG
D
39
99.693
38.632
34.653
1.00
39.96
D


ATOM
3291
CG
ARG
D
39
101.011
39.318
34.301
1.00
44.57
D


ATOM
3292
CD
ARG
D
39
101.006
40.798
34.667
1.00
49.71
D


ATOM
3293
NE
ARG
D
39
102.240
41.484
34.270
1.00
53.08
D


ATOM
3294
CZ
ARG
D
39
103.460
41.164
34.698
1.00
55.33
D


ATOM
3295
NH1
ARG
D
39
103.635
40.158
35.546
1.00
56.98
D


ATOM
3296
NH2
ARG
D
39
104.512
41.859
34.282
1.00
56.80
D


ATOM
3297
C
ARG
D
39
98.429
36.476
34.924
1.00
35.86
D


ATOM
3298
O
ARG
D
39
97.886
36.630
36.022
1.00
35.27
D


ATOM
3299
N
LYS
D
40
97.893
35.757
33.944
1.00
34.51
D


ATOM
3300
CA
LYS
D
40
96.602
35.095
34.090
1.00
33.49
D


ATOM
3301
CB
LYS
D
40
96.714
33.939
35.088
1.00
34.77
D


ATOM
3302
CG
LYS
D
40
95.482
33.040
35.133
1.00
41.38
D


ATOM
3303
CD
LYS
D
40
95.703
31.839
36.046
1.00
45.02
D


ATOM
3304
CE
LYS
D
40
94.443
31.001
36.185
1.00
46.54
D


ATOM
3305
NZ
LYS
D
40
94.652
29.853
37.112
1.00
48.98
D


ATOM
3306
C
LYS
D
40
95.511
36.064
34.542
1.00
30.95
D


ATOM
3307
O
LYS
D
40
94.780
35.794
35.492
1.00
28.23
D


ATOM
3308
N
GLU
D
41
95.401
37.197
33.858
1.00
30.54
D


ATOM
3309
CA
GLU
D
41
94.384
38.175
34.210
1.00
30.41
D


ATOM
3310
CB
GLU
D
41
94.980
39.302
35.078
1.00
34.10
D


ATOM
3311
CG
GLU
D
41
96.180
40.034
34.488
1.00
41.52
D


ATOM
3312
CD
GLU
D
41
96.834
40.997
35.482
1.00
45.72
D


ATOM
3313
OE1
GLU
D
41
97.826
41.665
35.108
1.00
48.68
D


ATOM
3314
OE2
GLU
D
41
96.362
41.086
36.638
1.00
47.60
D


ATOM
3315
C
GLU
D
41
93.651
38.766
33.014
1.00
28.03
D


ATOM
3316
O
GLU
D
41
94.220
38.981
31.940
1.00
25.49
D


ATOM
3317
N
THR
D
42
92.364
39.006
33.226
1.00
25.48
D


ATOM
3318
CA
THR
D
42
91.488
39.582
32.224
1.00
23.42
D


ATOM
3319
CB
THR
D
42
90.035
39.187
32.511
1.00
22.07
D


ATOM
3320
OG1
THR
D
42
89.927
37.761
32.468
1.00
18.54
D


ATOM
3321
CG2
THR
D
42
89.087
39.817
31.497
1.00
20.32
D


ATOM
3322
C
THR
D
42
91.615
41.098
32.301
1.00
22.29
D


ATOM
3323
O
THR
D
42
91.492
41.680
33.373
1.00
21.54
D


ATOM
3324
N
VAL
D
43
91.874
41.736
31.167
1.00
21.50
D


ATOM
3325
CA
VAL
D
43
92.004
43.183
31.136
1.00
19.88
D


ATOM
3326
CB
VAL
D
43
93.428
43.584
30.697
1.00
21.56
D


ATOM
3327
CG1
VAL
D
43
93.620
45.091
30.828
1.00
20.99
D


ATOM
3328
CG2
VAL
D
43
94.456
42.827
31.539
1.00
19.79
D


ATOM
3329
C
VAL
D
43
90.968
43.744
30.164
1.00
20.50
D


ATOM
3330
O
VAL
D
43
91.045
43.513
28.959
1.00
19.49
D


ATOM
3331
N
TRP
D
44
89.987
44.466
30.690
1.00
21.49
D


ATOM
3332
CA
TRP
D
44
88.946
45.028
29.836
1.00
22.88
D


ATOM
3333
CB
TRP
D
44
87.685
45.326
30.649
1.00
21.57
D


ATOM
3334
CG
TRP
D
44
87.167
44.129
31.372
1.00
21.99
D


ATOM
3335
CD2
TRP
D
44
86.280
43.125
30.854
1.00
22.20
D


ATOM
3336
CE2
TRP
D
44
86.119
42.150
31.862
1.00
22.19
D


ATOM
3337
CE3
TRP
D
44
85.611
42.951
29.634
1.00
20.96
D


ATOM
3338
CD1
TRP
D
44
87.492
43.736
32.633
1.00
23.17
D


ATOM
3339
NE1
TRP
D
44
86.868
42.548
32.937
1.00
23.70
D


ATOM
3340
CZ2
TRP
D
44
85.311
41.016
31.693
1.00
24.30
D


ATOM
3341
CZ3
TRP
D
44
84.807
41.824
29.461
1.00
22.81
D


ATOM
3342
CH2
TRP
D
44
84.666
40.870
30.487
1.00
24.05
D


ATOM
3343
C
TRP
D
44
89.425
46.291
29.143
1.00
23.92
D


ATOM
3344
O
TRP
D
44
90.081
47.131
29.759
1.00
24.50
D


ATOM
3345
N
CYS
D
45
89.098
46.417
27.859
1.00
24.24
D


ATOM
3346
CA
CYS
D
45
89.498
47.580
27.069
1.00
26.23
D


ATOM
3347
CB
CYS
D
45
89.951
47.141
25.672
1.00
25.96
D


ATOM
3348
SG
CYS
D
45
91.422
46.098
25.665
1.00
25.42
D


ATOM
3349
C
CYS
D
45
88.377
48.608
26.950
1.00
27.07
D


ATOM
3350
O
CYS
D
45
88.612
49.749
26.549
1.00
28.23
D


ATOM
3351
N
LEU
D
46
87.157
48.193
27.273
1.00
27.18
D


ATOM
3352
CA
LEU
D
46
86.002
49.087
27.232
1.00
28.16
D


ATOM
3353
CB
LEU
D
46
84.907
48.525
26.320
1.00
27.82
D


ATOM
3354
CG
LEU
D
46
84.142
49.460
25.372
1.00
30.22
D


ATOM
3355
CD1
LEU
D
46
82.792
48.827
25.040
1.00
29.72
D


ATOM
3356
CD2
LEU
D
46
83.928
50.827
25.994
1.00
31.10
D


ATOM
3357
C
LEU
D
46
85.504
49.138
28.675
1.00
28.73
D


ATOM
3358
O
LEU
D
46
85.049
48.133
29.216
1.00
28.92
D


ATOM
3359
N
PRO
D
47
85.601
50.309
29.318
1.00
29.35
D


ATOM
3360
CD
PRO
D
47
86.116
51.554
28.717
1.00
28.33
D


ATOM
3361
CA
PRO
D
47
85.182
50.533
30.709
1.00
29.01
D


ATOM
3362
CB
PRO
D
47
85.139
52.051
30.806
1.00
29.32
D


ATOM
3363
CG
PRO
D
47
86.307
52.447
29.929
1.00
30.61
D


ATOM
3364
C
PRO
D
47
83.879
49.875
31.169
1.00
28.51
D


ATOM
3365
O
PRO
D
47
83.867
49.151
32.163
1.00
28.22
D


ATOM
3366
N
VAL
D
48
82.784
50.126
30.458
1.00
28.05
D


ATOM
3367
CA
VAL
D
48
81.492
49.545
30.826
1.00
27.41
D


ATOM
3368
CB
VAL
D
48
80.406
49.918
29.810
1.00
26.31
D


ATOM
3369
CG1
VAL
D
48
79.955
51.345
30.027
1.00
30.25
D


ATOM
3370
CG2
VAL
D
48
80.949
49.744
28.398
1.00
26.11
D


ATOM
3371
C
VAL
D
48
81.490
48.022
30.961
1.00
26.77
D


ATOM
3372
O
VAL
D
48
80.622
47.462
31.627
1.00
27.43
D


ATOM
3373
N
LEU
D
49
82.449
47.353
30.332
1.00
25.75
D


ATOM
3374
CA
LEU
D
49
82.517
45.898
30.395
1.00
27.21
D


ATOM
3375
CB
LEU
D
49
83.237
45.354
29.153
1.00
27.47
D


ATOM
3376
CG
LEU
D
49
82.405
44.886
27.944
1.00
29.74
D


ATOM
3377
CD1
LEU
D
49
81.361
45.898
27.578
1.00
29.28
D


ATOM
3378
CD2
LEU
D
49
83.329
44.627
26.753
1.00
29.72
D


ATOM
3379
C
LEU
D
49
83.185
45.374
31.674
1.00
27.86
D


ATOM
3380
O
LEU
D
49
83.246
44.163
31.900
1.00
25.45
D


ATOM
3381
N
ARG
D
50
83.680
46.283
32.508
1.00
29.82
D


ATOM
3382
CA
ARG
D
50
84.319
45.892
33.768
1.00
32.18
D


ATOM
3383
CB
ARG
D
50
84.900
47.105
34.509
1.00
35.49
D


ATOM
3384
CG
ARG
D
50
86.010
47.890
33.824
1.00
40.53
D


ATOM
3385
CD
ARG
D
50
86.524
48.968
34.786
1.00
42.89
D


ATOM
3386
NE
ARG
D
50
87.297
50.017
34.125
1.00
46.26
D


ATOM
3387
CZ
ARG
D
50
88.484
49.836
33.555
1.00
46.43
D


ATOM
3388
NH1
ARG
D
50
89.049
48.636
33.564
1.00
46.42
D


ATOM
3389
NH2
ARG
D
50
89.100
50.857
32.968
1.00
43.78
D


ATOM
3390
C
ARG
D
50
83.283
45.247
34.690
1.00
31.58
D


ATOM
3391
O
ARG
D
50
83.631
44.577
35.664
1.00
31.56
D


ATOM
3392
N
GLN
D
51
82.009
45.476
34.397
1.00
30.22
D


ATOM
3393
CA
GLN
D
51
80.942
44.921
35.221
1.00
30.10
D


ATOM
3394
CB
GLN
D
51
79.610
45.592
34.880
1.00
31.37
D


ATOM
3395
CG
GLN
D
51
79.194
45.469
33.426
1.00
33.44
D


ATOM
3396
CD
GLN
D
51
77.888
46.188
33.144
1.00
37.07
D


ATOM
3397
OE1
GLN
D
51
76.835
45.824
33.678
1.00
36.72
D


ATOM
3398
NE2
GLN
D
51
77.951
47.222
32.309
1.00
34.55
D


ATOM
3399
C
GLN
D
51
80.830
43.411
35.049
1.00
29.51
D


ATOM
3400
O
GLN
D
51
80.291
42.721
35.911
1.00
29.09
D


ATOM
3401
N
PHE
D
52
81.342
42.899
33.935
1.00
28.19
D


ATOM
3402
CA
PHE
D
52
81.300
41.468
33.676
1.00
26.27
D


ATOM
3403
CB
PHE
D
52
81.218
41.188
32.178
1.00
25.00
D


ATOM
3404
CG
PHE
D
52
80.030
41.801
31.513
1.00
23.07
D


ATOM
3405
CD1
PHE
D
52
78.744
41.569
31.999
1.00
22.75
D


ATOM
3406
CD2
PHE
D
52
80.188
42.594
30.380
1.00
23.46
D


ATOM
3407
CE1
PHE
D
52
77.627
42.122
31.364
1.00
21.26
D


ATOM
3408
CE2
PHE
D
52
79.079
43.151
29.735
1.00
21.92
D


ATOM
3409
CZ
PHE
D
52
77.799
42.913
30.231
1.00
21.69
D


ATOM
3410
C
PHE
D
52
82.547
40.797
34.217
1.00
27.11
D


ATOM
3411
O
PHE
D
52
83.477
41.461
34.669
1.00
27.64
D


ATOM
3412
N
ARG
D
53
82.556
39.471
34.152
1.00
27.25
D


ATOM
3413
CA
ARG
D
53
83.683
38.672
34.609
1.00
28.31
D


ATOM
3414
CB
ARG
D
53
83.347
37.976
35.939
1.00
32.75
D


ATOM
3415
CG
ARG
D
53
83.263
38.921
37.143
1.00
40.59
D


ATOM
3416
CD
ARG
D
53
82.418
38.325
38.269
1.00
45.99
D


ATOM
3417
NE
ARG
D
53
81.007
38.229
37.892
1.00
52.14
D


ATOM
3418
CZ
ARG
D
53
80.172
39.265
37.808
1.00
53.70
D


ATOM
3419
NH1
ARG
D
53
80.597
40.493
38.080
1.00
53.85
D


ATOM
3420
NH2
ARG
D
53
78.910
39.071
37.440
1.00
54.61
D


ATOM
3421
C
ARG
D
53
84.007
37.624
33.548
1.00
25.73
D


ATOM
3422
O
ARG
D
53
83.120
37.103
32.875
1.00
23.84
D


ATOM
3423
N
PHE
D
54
85.290
37.335
33.387
1.00
23.47
D


ATOM
3424
CA
PHE
D
54
85.716
36.336
32.425
1.00
19.92
D


ATOM
3425
CB
PHE
D
54
86.159
36.980
31.113
1.00
15.46
D


ATOM
3426
CG
PHE
D
54
86.346
35.994
30.007
1.00
17.29
D


ATOM
3427
CD1
PHE
D
54
85.249
35.506
29.303
1.00
15.32
D


ATOM
3428
CD2
PHE
D
54
87.615
35.503
29.701
1.00
15.07
D


ATOM
3429
CE1
PHE
D
54
85.415
34.539
28.309
1.00
16.04
D


ATOM
3430
CE2
PHE
D
54
87.788
34.535
28.709
1.00
13.99
D


ATOM
3431
CZ
PHE
D
54
86.688
34.055
28.014
1.00
14.35
D


ATOM
3432
C
PHE
D
54
86.879
35.598
33.055
1.00
18.63
D


ATOM
3433
O
PHE
D
54
87.922
36.188
33.329
1.00
19.50
D


ATOM
3434
N
ASP
D
55
86.676
34.312
33.309
1.00
19.05
D


ATOM
3435
CA
ASP
D
55
87.689
33.466
33.921
1.00
19.33
D


ATOM
3436
CB
ASP
D
55
87.084
32.100
34.237
1.00
21.38
D


ATOM
3437
CG
ASP
D
55
88.090
31.138
34.832
1.00
24.95
D


ATOM
3438
OD1
ASP
D
55
89.264
31.528
35.021
1.00
27.01
D


ATOM
3439
OD2
ASP
D
55
87.703
29.985
35.112
1.00
27.48
D


ATOM
3440
C
ASP
D
55
88.863
33.323
32.955
1.00
19.84
D


ATOM
3441
O
ASP
D
55
88.741
32.691
31.904
1.00
18.07
D


ATOM
3442
N
PRO
D
56
90.024
33.909
33.311
1.00
19.36
D


ATOM
3443
CD
PRO
D
56
90.285
34.584
34.593
1.00
16.09
D


ATOM
3444
CA
PRO
D
56
91.240
33.867
32.486
1.00
18.34
D


ATOM
3445
CB
PRO
D
56
92.228
34.729
33.278
1.00
19.78
D


ATOM
3446
CG
PRO
D
56
91.792
34.517
34.692
1.00
18.66
D


ATOM
3447
C
PRO
D
56
91.770
32.468
32.206
1.00
18.30
D


ATOM
3448
O
PRO
D
56
92.583
32.277
31.299
1.00
17.41
D


ATOM
3449
N
GLN
D
57
91.304
31.489
32.977
1.00
18.31
D


ATOM
3450
CA
GLN
D
57
91.744
30.114
32.781
1.00
18.39
D


ATOM
3451
CB
GLN
D
57
91.314
29.233
33.963
1.00
19.94
D


ATOM
3452
CG
GLN
D
57
91.738
27.773
33.856
1.00
18.50
D


ATOM
3453
CD
GLN
D
57
93.252
27.603
33.765
1.00
23.86
D


ATOM
3454
OE1
GLN
D
57
94.000
28.110
34.612
1.00
23.68
D


ATOM
3455
NE2
GLN
D
57
93.709
26.885
32.739
1.00
19.56
D


ATOM
3456
C
GLN
D
57
91.174
29.555
31.480
1.00
20.01
D


ATOM
3457
O
GLN
D
57
91.733
28.618
30.903
1.00
19.26
D


ATOM
3458
N
PHE
D
58
90.059
30.113
31.016
1.00
19.19
D


ATOM
3459
CA
PHE
D
58
89.490
29.629
29.765
1.00
20.37
D


ATOM
3460
CB
PHE
D
58
88.178
30.347
29.427
1.00
18.69
D


ATOM
3461
CG
PHE
D
58
87.587
29.912
28.114
1.00
20.67
D


ATOM
3462
CD1
PHE
D
58
88.040
30.456
26.912
1.00
19.84
D


ATOM
3463
CD2
PHE
D
58
86.640
28.891
28.070
1.00
19.87
D


ATOM
3464
CE1
PHE
D
58
87.562
29.984
25.682
1.00
19.25
D


ATOM
3465
CE2
PHE
D
58
86.156
28.411
26.844
1.00
20.67
D


ATOM
3466
CZ
PHE
D
58
86.623
28.961
25.652
1.00
19.50
D


ATOM
3467
C
PHE
D
58
90.508
29.892
28.659
1.00
20.46
D


ATOM
3468
O
PHE
D
58
90.745
29.049
27.790
1.00
20.36
D


ATOM
3469
N
ALA
D
59
91.115
31.070
28.716
1.00
20.85
D


ATOM
3470
CA
ALA
D
59
92.111
31.477
27.736
1.00
21.87
D


ATOM
3471
CB
ALA
D
59
92.458
32.959
27.937
1.00
20.20
D


ATOM
3472
C
ALA
D
59
93.374
30.618
27.819
1.00
22.41
D


ATOM
3473
O
ALA
D
59
93.877
30.151
26.796
1.00
22.54
D


ATOM
3474
N
LEU
D
60
93.890
30.409
29.030
1.00
21.24
D


ATOM
3475
CA
LEU
D
60
95.101
29.601
29.188
1.00
22.31
D


ATOM
3476
CB
LEU
D
60
95.501
29.474
30.663
1.00
22.79
D


ATOM
3477
CG
LEU
D
60
96.063
30.698
31.393
1.00
25.87
D


ATOM
3478
CD1
LEU
D
60
96.455
30.303
32.805
1.00
28.75
D


ATOM
3479
CD2
LEU
D
60
97.270
31.223
30.670
1.00
28.42
D


ATOM
3480
C
LEU
D
60
94.891
28.207
28.617
1.00
21.85
D


ATOM
3481
O
LEU
D
60
95.731
27.691
27.875
1.00
22.48
D


ATOM
3482
N
THR
D
61
93.763
27.600
28.966
1.00
19.32
D


ATOM
3483
CA
THR
D
61
93.457
26.259
28.489
1.00
20.67
D


ATOM
3484
CB
THR
D
61
92.175
25.721
29.158
1.00
20.04
D


ATOM
3485
OG1
THR
D
61
92.419
25.539
30.558
1.00
23.09
D


ATOM
3486
CG2
THR
D
61
91.759
24.393
28.546
1.00
21.15
D


ATOM
3487
C
THR
D
61
93.283
26.240
26.974
1.00
19.50
D


ATOM
3488
O
THR
D
61
93.805
25.363
26.288
1.00
18.76
D


ATOM
3489
N
ASN
D
62
92.565
27.229
26.456
1.00
19.66
D


ATOM
3490
CA
ASN
D
62
92.310
27.300
25.032
1.00
19.00
D


ATOM
3491
CB
ASN
D
62
91.356
28.453
24.729
1.00
18.52
D


ATOM
3492
CG
ASN
D
62
90.262
28.052
23.760
1.00
20.31
D


ATOM
3493
OD1
ASN
D
62
89.726
26.942
23.833
1.00
19.27
D


ATOM
3494
ND2
ASN
D
62
89.917
28.952
22.854
1.00
22.25
D


ATOM
3495
C
ASN
D
62
93.599
27.445
24.244
1.00
19.63
D


ATOM
3496
O
ASN
D
62
93.774
26.788
23.221
1.00
21.16
D


ATOM
3497
N
ILE
D
63
94.509
28.290
24.724
1.00
19.68
D


ATOM
3498
CA
ILE
D
63
95.779
28.481
24.033
1.00
18.76
D


ATOM
3499
CB
ILE
D
63
96.587
29.660
24.645
1.00
18.72
D


ATOM
3500
CG2
ILE
D
63
97.946
29.780
23.966
1.00
17.99
D


ATOM
3501
CG1
ILE
D
63
95.813
30.968
24.471
1.00
17.09
D


ATOM
3502
CD1
ILE
D
63
95.507
31.313
23.017
1.00
17.47
D


ATOM
3503
C
ILE
D
63
96.613
27.195
24.094
1.00
18.86
D


ATOM
3504
O
ILE
D
63
97.354
26.885
23.164
1.00
20.67
D


ATOM
3505
N
ALA
D
64
96.497
26.448
25.188
1.00
18.22
D


ATOM
3506
CA
ALA
D
64
97.244
25.193
25.316
1.00
20.33
D


ATOM
3507
CB
ALA
D
64
97.039
24.574
26.708
1.00
17.30
D


ATOM
3508
C
ALA
D
64
96.756
24.232
24.233
1.00
21.38
D


ATOM
3509
O
ALA
D
64
97.536
23.459
23.677
1.00
23.44
D


ATOM
3510
N
VAL
D
65
95.459
24.290
23.940
1.00
21.97
D


ATOM
3511
CA
VAL
D
65
94.872
23.444
22.910
1.00
22.59
D


ATOM
3512
CB
VAL
D
65
93.324
23.570
22.890
1.00
22.30
D


ATOM
3513
CG1
VAL
D
65
92.744
22.781
21.728
1.00
17.73
D


ATOM
3514
CG2
VAL
D
65
92.747
23.053
24.204
1.00
19.10
D


ATOM
3515
C
VAL
D
65
95.441
23.832
21.541
1.00
23.65
D


ATOM
3516
O
VAL
D
65
95.783
22.961
20.746
1.00
23.24
D


ATOM
3517
N
LEU
D
66
95.552
25.133
21.271
1.00
25.03
D


ATOM
3518
CA
LEU
D
66
96.102
25.580
19.991
1.00
26.10
D


ATOM
3519
CB
LEU
D
66
96.104
27.111
19.870
1.00
23.98
D


ATOM
3520
CG
LEU
D
66
94.826
27.953
19.969
1.00
25.20
D


ATOM
3521
CD1
LEU
D
66
95.030
29.233
19.169
1.00
21.70
D


ATOM
3522
CD2
LEU
D
66
93.629
27.211
19.435
1.00
26.16
D


ATOM
3523
C
LEU
D
66
97.533
25.078
19.880
1.00
26.24
D


ATOM
3524
O
LEU
D
66
97.971
24.667
18.816
1.00
27.10
D


ATOM
3525
N
LYS
D
67
98.262
25.131
20.989
1.00
27.93
D


ATOM
3526
CA
LYS
D
67
99.642
24.658
21.024
1.00
28.00
D


ATOM
3527
CB
LYS
D
67
100.215
24.827
22.437
1.00
27.69
D


ATOM
3528
CG
LYS
D
67
101.633
24.316
22.625
1.00
28.46
D


ATOM
3529
CD
LYS
D
67
102.086
24.504
24.069
1.00
30.94
D


ATOM
3530
CE
LYS
D
67
103.401
23.791
24.356
1.00
32.95
D


ATOM
3531
NZ
LYS
D
67
104.517
24.279
23.503
1.00
35.64
D


ATOM
3532
C
LYS
D
67
99.642
23.182
20.629
1.00
27.56
D


ATOM
3533
O
LYS
D
67
100.414
22.759
19.767
1.00
27.65
D


ATOM
3534
N
HIS
D
68
98.761
22.405
21.254
1.00
27.05
D


ATOM
3535
CA
HIS
D
68
98.665
20.982
20.956
1.00
26.31
D


ATOM
3536
CB
HIS
D
68
97.600
20.324
21.844
1.00
27.74
D


ATOM
3537
CG
HIS
D
68
97.356
18.879
21.531
1.00
31.20
D


ATOM
3538
CD2
HIS
D
68
97.801
17.748
22.130
1.00
31.26
D


ATOM
3539
ND1
HIS
D
68
96.582
18.466
20.465
1.00
32.71
D


ATOM
3540
CE1
HIS
D
68
96.560
17.146
20.423
1.00
31.32
D


ATOM
3541
NE2
HIS
D
68
97.292
16.686
21.421
1.00
31.58
D


ATOM
3542
C
HIS
D
68
98.341
20.757
19.483
1.00
25.27
D


ATOM
3543
O
HIS
D
68
98.958
19.914
18.830
1.00
25.67
D


ATOM
3544
N
ASN
D
69
97.386
21.521
18.959
1.00
22.00
D


ATOM
3545
CA
ASN
D
69
96.986
21.398
17.561
1.00
23.20
D


ATOM
3546
CB
ASN
D
69
95.706
22.210
17.307
1.00
23.27
D


ATOM
3547
CG
ASN
D
69
94.447
21.504
17.805
1.00
24.20
D


ATOM
3548
OD1
ASN
D
69
94.521
20.536
18.562
1.00
26.69
D


ATOM
3549
ND2
ASN
D
69
93.283
21.994
17.381
1.00
21.03
D


ATOM
3550
C
ASN
D
69
98.091
21.855
16.601
1.00
24.52
D


ATOM
3551
O
ASN
D
69
98.329
21.223
15.570
1.00
22.82
D


ATOM
3552
N
LEU
D
70
98.763
22.954
16.934
1.00
24.56
D


ATOM
3553
CA
LEU
D
70
99.831
23.459
16.078
1.00
26.89
D


ATOM
3554
CB
LEU
D
70
100.478
24.707
16.690
1.00
23.85
D


ATOM
3555
CG
LEU
D
70
101.619
25.306
15.857
1.00
22.71
D


ATOM
3556
CD1
LEU
D
70
101.082
25.776
14.519
1.00
19.18
D


ATOM
3557
CD2
LEU
D
70
102.254
26.472
16.592
1.00
23.62
D


ATOM
3558
C
LEU
D
70
100.900
22.388
15.882
1.00
28.63
D


ATOM
3559
O
LEU
D
70
101.413
22.210
14.780
1.00
27.56
D


ATOM
3560
N
ASN
D
71
101.224
21.687
16.967
1.00
31.13
D


ATOM
3561
CA
ASN
D
71
102.238
20.637
16.962
1.00
35.25
D


ATOM
3562
CB
ASN
D
71
102.393
20.052
18.370
1.00
35.30
D


ATOM
3563
CG
ASN
D
71
103.149
20.978
19.307
1.00
38.03
D


ATOM
3564
OD1
ASN
D
71
103.197
20.751
20.518
1.00
40.05
D


ATOM
3565
ND2
ASN
D
71
103.752
22.026
18.748
1.00
38.78
D


ATOM
3566
C
ASN
D
71
101.931
19.521
15.975
1.00
36.85
D


ATOM
3567
O
ASN
D
71
102.829
18.997
15.316
1.00
36.91
D


ATOM
3568
N
SER
D
72
100.660
19.157
15.876
1.00
38.08
D


ATOM
3569
CA
SER
D
72
100.261
18.104
14.961
1.00
39.44
D


ATOM
3570
CB
SER
D
72
98.847
17.623
15.306
1.00
40.69
D


ATOM
3571
OG
SER
D
72
98.529
16.427
14.611
1.00
44.84
D


ATOM
3572
C
SER
D
72
100.320
18.614
13.520
1.00
39.55
D


ATOM
3573
O
SER
D
72
100.798
17.915
12.625
1.00
38.61
D


ATOM
3574
N
LEU
D
73
99.846
19.839
13.305
1.00
40.64
D


ATOM
3575
CA
LEU
D
73
99.844
20.443
11.974
1.00
42.19
D


ATOM
3576
CB
LEU
D
73
99.085
21.768
11.990
1.00
42.17
D


ATOM
3577
CG
LEU
D
73
97.608
21.700
11.608
1.00
43.12
D


ATOM
3578
CD1
LEU
D
73
96.891
20.664
12.443
1.00
44.19
D


ATOM
3579
CD2
LEU
D
73
96.988
23.072
11.801
1.00
44.59
D


ATOM
3580
C
LEU
D
73
101.237
20.678
11.407
1.00
43.27
D


ATOM
3581
O
LEU
D
73
101.466
20.479
10.215
1.00
43.00
D


ATOM
3582
N
ILE
D
74
102.162
21.116
12.253
1.00
44.60
D


ATOM
3583
CA
ILE
D
74
103.529
21.364
11.812
1.00
46.44
D


ATOM
3584
CB
ILE
D
74
104.431
21.770
13.000
1.00
46.31
D


ATOM
3585
CG2
ILE
D
74
105.893
21.792
12.571
1.00
46.14
D


ATOM
3586
CG1
ILE
D
74
103.996
23.140
13.529
1.00
45.97
D


ATOM
3587
CD1
ILE
D
74
104.683
23.561
14.812
1.00
43.97
D


ATOM
3588
C
ILE
D
74
104.077
20.095
11.166
1.00
48.14
D


ATOM
3589
O
ILE
D
74
104.724
20.147
10.119
1.00
48.28
D


ATOM
3590
N
LYS
D
75
103.800
18.957
11.795
1.00
49.68
D


ATOM
3591
CA
LYS
D
75
104.252
17.669
11.290
1.00
51.82
D


ATOM
3592
CB
LYS
D
75
104.060
16.589
12.356
1.00
52.85
D


ATOM
3593
CG
LYS
D
75
104.856
16.839
13.621
1.00
54.78
D


ATOM
3594
CD
LYS
D
75
104.517
15.831
14.704
1.00
57.28
D


ATOM
3595
CE
LYS
D
75
105.222
16.170
16.010
1.00
58.75
D


ATOM
3596
NZ
LYS
D
75
104.803
15.266
17.116
1.00
59.97
D


ATOM
3597
C
LYS
D
75
103.499
17.276
10.023
1.00
52.37
D


ATOM
3598
O
LYS
D
75
104.106
17.086
8.972
1.00
52.78
D


ATOM
3599
N
ARG
D
76
102.177
17.171
10.124
1.00
52.67
D


ATOM
3600
CA
ARG
D
76
101.353
16.783
8.986
1.00
52.67
D


ATOM
3601
CB
ARG
D
76
99.911
16.546
9.439
1.00
53.54
D


ATOM
3602
CG
ARG
D
76
99.764
15.339
10.346
1.00
55.62
D


ATOM
3603
CD
ARG
D
76
98.310
15.011
10.639
1.00
58.29
D


ATOM
3604
NE
ARG
D
76
97.628
16.107
11.319
1.00
61.07
D


ATOM
3605
CZ
ARG
D
76
96.437
16.000
11.900
1.00
62.21
D


ATOM
3606
NH1
ARG
D
76
95.793
14.840
11.885
1.00
62.71
D


ATOM
3607
NH2
ARG
D
76
95.889
17.055
12.492
1.00
61.94
D


ATOM
3608
C
ARG
D
76
101.375
17.761
7.816
1.00
52.35
D


ATOM
3609
O
ARG
D
76
100.691
17.550
6.817
1.00
52.65
D


ATOM
3610
N
SER
D
77
102.160
18.824
7.932
1.00
52.02
D


ATOM
3611
CA
SER
D
77
102.255
19.807
6.856
1.00
51.87
D


ATOM
3612
CB
SER
D
77
101.945
21.212
7.379
1.00
50.95
D


ATOM
3613
OG
SER
D
77
102.975
21.668
8.239
1.00
48.11
D


ATOM
3614
C
SER
D
77
103.667
19.789
6.287
1.00
52.25
D


ATOM
3615
O
SER
D
77
104.028
20.633
5.464
1.00
51.67
D


ATOM
3616
N
ASN
D
78
104.455
18.814
6.731
1.00
52.79
D


ATOM
3617
CA
ASN
D
78
105.841
18.675
6.301
1.00
53.67
D


ATOM
3618
CB
ASN
D
78
105.912
18.364
4.797
1.00
55.53
D


ATOM
3619
CG
ASN
D
78
107.298
17.901
4.355
1.00
57.31
D


ATOM
3620
OD1
ASN
D
78
107.959
17.129
5.051
1.00
56.41
D


ATOM
3621
ND2
ASN
D
78
107.732
18.360
3.184
1.00
58.05
D


ATOM
3622
C
ASN
D
78
106.549
19.985
6.632
1.00
52.90
D


ATOM
3623
O
ASN
D
78
107.300
20.536
5.826
1.00
53.98
D


ATOM
3624
N
SER
D
79
106.275
20.479
7.835
1.00
51.25
D


ATOM
3625
CA
SER
D
79
106.856
21.715
8.341
1.00
49.59
D


ATOM
3626
CB
SER
D
79
108.333
21.498
8.664
1.00
49.69
D


ATOM
3627
OG
SER
D
79
108.472
20.604
9.753
1.00
52.23
D


ATOM
3628
C
SER
D
79
106.711
22.931
7.437
1.00
47.21
D


ATOM
3629
O
SER
D
79
107.699
23.588
7.111
1.00
47.49
D


ATOM
3630
N
THR
D
80
105.483
23.235
7.032
1.00
44.68
D


ATOM
3631
CA
THR
D
80
105.245
24.401
6.189
1.00
43.69
D


ATOM
3632
CB
THR
D
80
103.928
24.274
5.407
1.00
45.12
D


ATOM
3633
OG1
THR
D
80
103.976
23.112
4.570
1.00
47.94
D


ATOM
3634
CG2
THR
D
80
103.706
25.505
4.541
1.00
44.11
D


ATOM
3635
C
THR
D
80
105.166
25.634
7.094
1.00
42.94
D


ATOM
3636
O
THR
D
80
104.225
25.783
7.874
1.00
41.60
D


ATOM
3637
N
ALA
D
81
106.162
26.510
6.988
1.00
40.39
D


ATOM
3638
CA
ALA
D
81
106.215
27.715
7.804
1.00
37.86
D


ATOM
3639
CB
ALA
D
81
107.657
28.171
7.958
1.00
39.23
D


ATOM
3640
C
ALA
D
81
105.372
28.846
7.234
1.00
36.29
D


ATOM
3641
O
ALA
D
81
104.988
28.829
6.065
1.00
35.21
D


ATOM
3642
N
ALA
D
82
105.087
29.829
8.079
1.00
34.40
D


ATOM
3643
CA
ALA
D
82
104.294
30.984
7.685
1.00
32.51
D


ATOM
3644
CB
ALA
D
82
103.915
31.789
8.920
1.00
32.45
D


ATOM
3645
C
ALA
D
82
105.064
31.866
6.707
1.00
32.78
D


ATOM
3646
O
ALA
D
82
106.294
31.913
6.740
1.00
30.87
D


ATOM
3647
N
THR
D
83
104.333
32.561
5.839
1.00
32.79
D


ATOM
3648
CA
THR
D
83
104.940
33.459
4.867
1.00
34.48
D


ATOM
3649
CB
THR
D
83
104.195
33.429
3.521
1.00
35.64
D


ATOM
3650
OG1
THR
D
83
104.179
32.094
3.006
1.00
38.88
D


ATOM
3651
CG2
THR
D
83
104.880
34.342
2.521
1.00
35.33
D


ATOM
3652
C
THR
D
83
104.886
34.887
5.401
1.00
35.30
D


ATOM
3653
O
THR
D
83
103.827
35.355
5.824
1.00
36.88
D


ATOM
3654
N
ASN
D
84
106.025
35.575
5.379
1.00
35.07
D


ATOM
3655
CA
ASN
D
84
106.095
36.949
5.855
1.00
33.90
D


ATOM
3656
CB
ASN
D
84
107.548
37.413
6.010
1.00
34.23
D


ATOM
3657
CG
ASN
D
84
108.351
36.545
6.954
1.00
36.16
D


ATOM
3658
OD1
ASN
D
84
107.895
36.195
8.043
1.00
34.99
D


ATOM
3659
ND2
ASN
D
84
109.572
36.205
6.545
1.00
37.40
D


ATOM
3660
C
ASN
D
84
105.419
37.879
4.865
1.00
34.74
D


ATOM
3661
O
ASN
D
84
105.814
37.940
3.699
1.00
35.59
D


ATOM
3662
N
GLU
D
85
104.401
38.599
5.327
1.00
34.09
D


ATOM
3663
CA
GLU
D
85
103.695
39.561
4.489
1.00
32.99
D


ATOM
3664
CB
GLU
D
85
102.239
39.714
4.939
1.00
35.56
D


ATOM
3665
CG
GLU
D
85
101.370
38.475
4.746
1.00
40.80
D


ATOM
3666
CD
GLU
D
85
101.019
38.215
3.291
1.00
43.32
D


ATOM
3667
OE1
GLU
D
85
100.409
39.104
2.658
1.00
46.21
D


ATOM
3668
OE2
GLU
D
85
101.345
37.119
2.782
1.00
44.58
D


ATOM
3669
C
GLU
D
85
104.418
40.886
4.681
1.00
31.21
D


ATOM
3670
O
GLU
D
85
105.220
41.024
5.602
1.00
32.36
D


ATOM
3671
N
VAL
D
86
104.140
41.848
3.808
1.00
29.71
D


ATOM
3672
CA
VAL
D
86
104.749
43.170
3.882
1.00
27.94
D


ATOM
3673
CB
VAL
D
86
105.079
43.712
2.467
1.00
26.90
D


ATOM
3674
CG1
VAL
D
86
105.569
45.166
2.543
1.00
23.11
D


ATOM
3675
CG2
VAL
D
86
106.134
42.829
1.821
1.00
24.31
D


ATOM
3676
C
VAL
D
86
103.767
44.114
4.574
1.00
29.81
D


ATOM
3677
O
VAL
D
86
102.658
44.343
4.088
1.00
30.28
D


ATOM
3678
N
PRO
D
87
104.162
44.666
5.729
1.00
29.08
D


ATOM
3679
CD
PRO
D
87
105.356
44.310
6.509
1.00
29.37
D


ATOM
3680
CA
PRO
D
87
103.306
45.583
6.485
1.00
30.85
D


ATOM
3681
CB
PRO
D
87
104.083
45.791
7.786
1.00
30.80
D


ATOM
3682
CG
PRO
D
87
104.878
44.551
7.920
1.00
30.83
D


ATOM
3683
C
PRO
D
87
103.049
46.907
5.772
1.00
31.43
D


ATOM
3684
O
PRO
D
87
103.863
47.357
4.968
1.00
31.78
D


ATOM
3685
N
GLU
D
88
101.907
47.517
6.081
1.00
31.85
D


ATOM
3686
CA
GLU
D
88
101.516
48.808
5.521
1.00
32.77
D


ATOM
3687
CB
GLU
D
88
100.195
48.687
4.744
1.00
35.18
D


ATOM
3688
CG
GLU
D
88
99.814
49.960
3.987
1.00
43.00
D


ATOM
3689
CD
GLU
D
88
98.512
49.839
3.205
1.00
46.30
D


ATOM
3690
OE1
GLU
D
88
97.439
49.745
3.837
1.00
47.40
D


ATOM
3691
OE2
GLU
D
88
98.564
49.840
1.954
1.00
48.25
D


ATOM
3692
C
GLU
D
88
101.338
49.748
6.721
1.00
31.26
D


ATOM
3693
O
GLU
D
88
100.556
49.457
7.630
1.00
31.21
D


ATOM
3694
N
VAL
D
89
102.060
50.864
6.728
1.00
28.43
D


ATOM
3695
CA
VAL
D
89
101.988
51.806
7.842
1.00
26.87
D


ATOM
3696
CB
VAL
D
89
103.385
52.024
8.454
1.00
26.58
D


ATOM
3697
CG1
VAL
D
89
103.277
52.886
9.699
1.00
26.80
D


ATOM
3698
CG2
VAL
D
89
104.021
50.679
8.787
1.00
24.58
D


ATOM
3699
C
VAL
D
89
101.389
53.174
7.505
1.00
27.02
D


ATOM
3700
O
VAL
D
89
101.698
53.772
6.473
1.00
26.22
D


ATOM
3701
N
THR
D
90
100.530
53.662
8.394
1.00
26.33
D


ATOM
3102
CA
THR
D
90
99.881
54.955
8.219
1.00
26.05
D


ATOM
3703
CB
THR
D
90
98.414
54.802
7.769
1.00
27.24
D


ATOM
3704
OG1
THR
D
90
98.359
54.063
6.543
1.00
31.41
D


ATOM
3705
CG2
THR
D
90
97.786
56.163
7.545
1.00
28.57
D


ATOM
3706
C
THR
D
90
99.883
55.698
9.546
1.00
24.83
D


ATOM
3707
O
THR
D
90
99.542
55.120
10.581
1.00
25.45
D


ATOM
3708
N
VAL
D
91
100.266
56.972
9.512
1.00
22.04
D


ATOM
3709
CA
VAL
D
91
100.300
57.791
10.716
1.00
21.50
D


ATOM
3710
CB
VAL
D
91
101.749
58.280
11.031
1.00
23.04
D


ATOM
3711
CG1
VAL
D
91
101.737
59.245
12.225
1.00
22.74
D


ATOM
3712
CG2
VAL
D
91
102.650
57.082
11.340
1.00
20.38
D


ATOM
3713
C
VAL
D
91
99.369
58.993
10.553
1.00
21.65
D


ATOM
3714
O
VAL
D
91
99.357
59.653
9.509
1.00
21.70
D


ATOM
3715
N
PHE
D
92
98.573
59.252
11.586
1.00
21.34
D


ATOM
3716
CA
PHE
D
92
97.633
60.363
11.580
1.00
21.48
D


ATOM
3717
CB
PHE
D
92
96.370
59.985
10.788
1.00
21.60
D


ATOM
3718
CG
PHE
D
92
95.652
58.771
11.314
1.00
22.22
D


ATOM
3719
CD1
PHE
D
92
94.601
58.902
12.215
1.00
24.10
D


ATOM
3720
CD2
PHE
D
92
96.038
57.495
10.925
1.00
24.53
D


ATOM
3721
CE1
PHE
D
92
93.940
57.774
12.724
1.00
22.72
D


ATOM
3722
CE2
PHE
D
92
95.386
56.355
11.428
1.00
23.87
D


ATOM
3723
CZ
PHE
D
92
94.335
56.501
12.329
1.00
21.18
D


ATOM
3724
C
PHE
D
92
97.303
60.700
13.030
1.00
22.72
D


ATOM
3725
O
PHE
D
92
97.607
59.921
13.933
1.00
22.31
D


ATOM
3726
N
SER
D
93
96.696
61.859
13.261
1.00
22.45
D


ATOM
3727
CA
SER
D
93
96.366
62.262
14.623
1.00
21.69
D


ATOM
3728
CB
SER
D
93
96.599
63.764
14.799
1.00
20.96
D


ATOM
3729
OG
SER
D
93
95.696
64.508
14.010
1.00
25.08
D


ATOM
3730
C
SER
D
93
94.931
61.913
14.990
1.00
21.02
D


ATOM
3731
O
SER
D
93
94.078
61.755
14.127
1.00
20.62
D


ATOM
3732
N
LYS
D
94
94.676
61.791
16.283
1.00
20.66
D


ATOM
3733
CA
LYS
D
94
93.350
61.453
16.768
1.00
24.11
D


ATOM
3734
CB
LYS
D
94
93.444
60.985
18.223
1.00
24.91
D


ATOM
3735
CG
LYS
D
94
92.121
60.605
18.865
1.00
29.49
D


ATOM
3736
CD
LYS
D
94
92.353
60.101
20.293
1.00
32.97
D


ATOM
3737
CE
LYS
D
94
91.050
59.909
21.052
1.00
33.37
D


ATOM
3738
NZ
LYS
D
94
90.175
58.897
20.399
1.00
34.08
D


ATOM
3739
C
LYS
D
94
92.406
62.646
16.654
1.00
24.40
D


ATOM
3740
O
LYS
D
94
91.224
62.495
16.356
1.00
24.55
D


ATOM
3741
N
SER
D
95
92.935
63.834
16.894
1.00
25.54
D


ATOM
3742
CA
SER
D
95
92.133
65.040
16.815
1.00
29.22
D


ATOM
3743
CB
SER
D
95
91.932
65.643
18.208
1.00
30.47
D


ATOM
3744
OG
SER
D
95
91.236
64.746
19.060
1.00
36.11
D


ATOM
3745
C
SER
D
95
92.843
66.046
15.932
1.00
29.71
D


ATOM
3746
O
SER
D
95
93.993
65.834
15.531
1.00
29.68
D


ATOM
3747
N
PRO
D
96
92.159
67.146
15.588
1.00
29.93
D


ATOM
3748
CD
PRO
D
96
90.760
67.532
15.843
1.00
31.14
D


ATOM
3749
CA
PRO
D
96
92.836
68.129
14.747
1.00
29.29
D


ATOM
3750
CB
PRO
D
96
91.714
69.097
14.369
1.00
31.65
D


ATOM
3751
CG
PRO
D
96
90.777
69.010
15.545
1.00
30.66
D


ATOM
3752
C
PRO
D
96
93.939
68.765
15.587
1.00
27.35
D


ATOM
3753
O
PRO
D
96
93.818
68.904
16.806
1.00
24.86
D


ATOM
3754
N
VAL
D
97
95.025
69.127
14.929
1.00
26.81
D


ATOM
3755
CA
VAL
D
97
96.158
69.706
15.615
1.00
29.25
D


ATOM
3756
CB
VAL
D
97
97.438
69.501
14.783
1.00
31.49
D


ATOM
3757
CG1
VAL
D
97
98.652
69.998
15.556
1.00
33.50
D


ATOM
3758
CG2
VAL
D
97
97.583
68.029
14.415
1.00
34.03
D


ATOM
3759
C
VAL
D
97
96.007
71.196
15.910
1.00
28.80
D


ATOM
3760
O
VAL
D
97
95.749
71.998
15.012
1.00
28.78
D


ATOM
3761
N
THR
D
98
96.144
71.559
17.178
1.00
27.47
D


ATOM
3762
CA
THR
D
98
96.091
72.960
17.572
1.00
26.55
D


ATOM
3763
CB
THR
D
98
94.723
73.365
18.209
1.00
26.16
D


ATOM
3764
OG1
THR
D
98
94.684
72.961
19.575
1.00
31.83
D


ATOM
3765
CG2
THR
D
98
93.567
72.717
17.469
1.00
23.66
D


ATOM
3766
C
THR
D
98
97.220
73.114
18.581
1.00
25.73
D


ATOM
3767
O
THR
D
98
97.260
72.412
19.591
1.00
27.12
D


ATOM
3768
N
LEU
D
99
98.159
74.005
18.285
1.00
26.12
D


ATOM
3769
CA
LEU
D
99
99.307
74.236
19.156
1.00
27.47
D


ATOM
3770
CB
LEU
D
99
100.089
75.459
18.675
1.00
31.04
D


ATOM
3771
CG
LEU
D
99
100.758
75.309
17.310
1.00
33.09
D


ATOM
3772
CD1
LEU
D
99
101.458
76.607
16.940
1.00
36.20
D


ATOM
3773
CD2
LEU
D
99
101.754
74.165
17.361
1.00
35.56
D


ATOM
3774
C
LEU
D
99
98.935
74.416
20.621
1.00
26.08
D


ATOM
3775
O
LEU
D
99
98.077
75.222
20.946
1.00
25.97
D


ATOM
3776
N
GLY
D
100
99.585
73.654
21.500
1.00
26.97
D


ATOM
3777
CA
GLY
D
100
99.310
73.749
22.924
1.00
26.03
D


ATOM
3778
C
GLY
D
100
98.233
72.798
23.422
1.00
26.02
D


ATOM
3779
O
GLY
D
100
98.020
72.662
24.629
1.00
25.51
D


ATOM
3780
N
GLN
D
101
97.553
72.143
22.491
1.00
25.73
D


ATOM
3781
CA
GLN
D
101
96.490
71.199
22.820
1.00
28.13
D


ATOM
3782
CB
GLN
D
101
95.372
71.297
21.776
1.00
32.24
D


ATOM
3783
CG
GLN
D
101
94.617
69.981
21.560
1.00
38.65
D


ATOM
3784
CD
GLN
D
101
94.680
69.459
20.115
1.00
41.08
D


ATOM
3785
OE1
GLN
D
101
95.760
69.348
19.511
1.00
38.18
D


ATOM
3786
NE2
GLN
D
101
93.515
69.119
19.566
1.00
40.87
D


ATOM
3787
C
GLN
D
101
96.994
69.756
22.861
1.00
25.22
D


ATOM
3788
O
GLN
D
101
97.477
69.245
21.857
1.00
24.55
D


ATOM
3789
N
PRO
D
102
96.885
69.078
24.019
1.00
24.18
D


ATOM
3790
CD
PRO
D
102
96.436
69.544
25.343
1.00
22.22
D


ATOM
3791
CA
PRO
D
102
97.359
67.683
24.080
1.00
22.76
D


ATOM
3792
CB
PRO
D
102
96.983
67.253
25.494
1.00
22.02
D


ATOM
3793
CG
PRO
D
102
97.088
68.542
26.274
1.00
22.44
D


ATOM
3794
C
PRO
D
102
96.649
66.845
23.015
1.00
21.72
D


ATOM
3795
O
PRO
D
102
95.429
66.922
22.876
1.00
22.65
D


ATOM
3796
N
ASN
D
103
97.409
66.055
22.264
1.00
19.84
D


ATOM
3797
CA
ASN
D
103
96.833
65.225
21.209
1.00
17.89
D


ATOM
3798
CB
ASN
D
103
97.112
65.856
19.838
1.00
16.30
D


ATOM
3799
CG
ASN
D
103
96.005
65.587
18.824
1.00
16.50
D


ATOM
3800
OD1
ASN
D
103
95.552
64.446
18.636
1.00
16.80
D


ATOM
3801
ND2
ASN
D
103
95.569
66.643
18.160
1.00
14.61
D


ATOM
3802
C
ASN
D
103
97.410
63.805
21.248
1.00
17.24
D


ATOM
3803
O
ASN
D
103
98.199
63.473
22.129
1.00
15.74
D


ATOM
3804
N
ILE
D
104
97.010
62.977
20.284
1.00
17.39
D


ATOM
3805
CA
ILE
D
104
97.465
61.595
20.198
1.00
15.30
D


ATOM
3806
CB
ILE
D
104
96.402
60.627
20.755
1.00
17.89
D


ATOM
3807
CG2
ILE
D
104
96.818
59.175
20.498
1.00
13.27
D


ATOM
3808
CG1
ILE
D
104
96.202
60.886
22.253
1.00
18.46
D


ATOM
3809
CD1
ILE
D
104
95.179
59.965
22.895
1.00
17.98
D


ATOM
3810
C
ILE
D
104
97.760
61.185
18.763
1.00
17.15
D


ATOM
3811
O
ILE
D
104
96.887
61.283
17.902
1.00
18.07
D


ATOM
3812
N
LEU
D
105
98.987
60.727
18.509
1.00
16.66
D


ATOM
3813
CA
LEU
D
105
99.370
60.272
17.177
1.00
16.59
D


ATOM
3814
CB
LEU
D
105
100.864
60.482
16.895
1.00
17.56
D


ATOM
3815
CG
LEU
D
105
101.375
61.926
16.842
1.00
21.66
D


ATOM
3816
CD1
LEU
D
105
102.811
61.943
16.302
1.00
21.26
D


ATOM
3817
CD2
LEU
D
105
100.460
62.771
15.951
1.00
21.56
D


ATOM
3818
C
LEU
D
105
99.061
58.804
17.128
1.00
17.13
D


ATOM
3819
O
LEU
D
105
99.368
58.056
18.056
1.00
18.35
D


ATOM
3820
N
ILE
D
106
98.432
58.399
16.039
1.00
17.88
D


ATOM
3821
CA
ILE
D
106
98.045
57.016
15.839
1.00
17.14
D


ATOM
3822
CB
ILE
D
106
96.525
56.939
15.492
1.00
16.99
D


ATOM
3823
CG2
ILE
D
106
96.093
55.496
15.318
1.00
15.63
D


ATOM
3824
CG1
ILE
D
106
95.711
57.619
16.604
1.00
19.04
D


ATOM
3825
CD1
ILE
D
106
94.238
57.877
16.260
1.00
16.48
D


ATOM
3826
C
ILE
D
106
98.876
56.431
14.700
1.00
17.19
D


ATOM
3827
O
ILE
D
106
98.941
57.004
13.618
1.00
16.06
D


ATOM
3828
N
CYS
D
107
99.540
55.312
14.966
1.00
18.84
D


ATOM
3829
CA
CYS
D
107
100.339
54.637
13.954
1.00
19.74
D


ATOM
3830
C
CYS
D
107
99.634
53.323
13.670
1.00
20.17
D


ATOM
3831
O
CYS
D
107
99.632
52.421
14.507
1.00
20.08
D


ATOM
3832
CB
CYS
D
107
101.755
54.349
14.453
1.00
22.00
D


ATOM
3833
SG
CYS
D
107
102.800
53.514
13.211
1.00
28.61
D


ATOM
3834
N
LEU
D
108
99.027
53.221
12.493
1.00
19.48
D


ATOM
3835
CA
LEU
D
108
98.313
52.015
12.113
1.00
19.67
D


ATOM
3836
CB
LEU
D
108
97.024
52.391
11.369
1.00
19.98
D


ATOM
3837
CG
LEU
D
108
95.977
51.358
10.925
1.00
20.40
D


ATOM
3838
CD1
LEU
D
108
95.883
51.366
9.412
1.00
20.15
D


ATOM
3839
CD2
LEU
D
108
96.301
49.971
11.454
1.00
19.44
D


ATOM
3840
C
LEU
D
108
99.207
51.145
11.237
1.00
19.84
D


ATOM
3841
O
LEU
D
108
99.657
51.563
10.170
1.00
20.11
D


ATOM
3842
N
VAL
D
109
99.473
49.940
11.721
1.00
19.32
D


ATOM
3843
CA
VAL
D
109
100.289
48.972
11.016
1.00
19.64
D


ATOM
3844
CB
VAL
D
109
101.368
48.402
11.958
1.00
19.40
D


ATOM
3845
CG1
VAL
D
109
102.290
47.474
11.202
1.00
18.01
D


ATOM
3846
CG2
VAL
D
109
102.155
49.560
12.590
1.00
17.30
D


ATOM
3847
C
VAL
D
109
99.321
47.876
10.568
1.00
21.45
D


ATOM
3848
O
VAL
D
109
98.845
47.079
11.382
1.00
22.65
D


ATOM
3849
N
ASP
D
110
99.022
47.861
9.274
1.00
22.00
D


ATOM
3850
CA
ASP
D
110
98.086
46.901
8.689
1.00
23.80
D


ATOM
3851
CB
ASP
D
110
97.156
47.648
7.728
1.00
24.68
D


ATOM
3852
CG
ASP
D
110
95.790
47.002
7.603
1.00
26.64
D


ATOM
3853
OD1
ASP
D
110
95.582
45.915
8.177
1.00
28.80
D


ATOM
3854
OD2
ASP
D
110
94.920
47.591
6.926
1.00
27.99
D


ATOM
3855
C
ASP
D
110
98.802
45.756
7.944
1.00
23.77
D


ATOM
3856
O
ASP
D
110
100.005
45.831
7.684
1.00
22.82
D


ATOM
3857
N
ASN
D
111
98.044
44.711
7.604
1.00
23.55
D


ATOM
3858
CA
ASN
D
111
98.548
43.530
6.889
1.00
23.79
D


ATOM
3859
CB
ASN
D
111
98.880
43.867
5.425
1.00
25.36
D


ATOM
3860
CG
ASN
D
111
99.079
42.610
4.562
1.00
29.95
D


ATOM
3861
OD1
ASN
D
111
99.981
42.547
3.724
1.00
29.58
D


ATOM
3862
ND2
ASN
D
111
98.220
41.611
4.761
1.00
30.51
D


ATOM
3863
C
ASN
D
111
99.786
42.941
7.556
1.00
22.70
0


ATOM
3864
O
ASN
D
111
100.834
42.784
6.929
1.00
22.97
D


ATOM
3865
N
ILE
D
112
99.656
42.612
8.835
1.00
22.14
D


ATOM
3866
CA
ILE
D
112
100.754
42.038
9.598
1.00
20.20
D


ATOM
3867
CB
ILE
D
112
100.746
42.536
11.055
1.00
18.82
D


ATOM
3868
CG2
ILE
D
112
101.926
41.950
11.808
1.00
15.77
D


ATOM
3869
CG1
ILE
D
112
100.770
44.058
11.103
1.00
19.09
D


ATOM
3870
CD1
ILE
D
112
100.630
44.602
12.514
1.00
21.18
D


ATOM
3871
C
ILE
D
112
100.666
40.512
9.659
1.00
21.41
D


ATOM
3872
O
ILE
D
112
99.626
39.960
10.002
1.00
22.04
D


ATOM
3873
N
PHE
D
113
101.765
39.838
9.338
1.00
21.35
D


ATOM
3874
CA
PHE
D
113
101.818
38.386
9.409
1.00
19.93
D


ATOM
3875
CB
PHE
D
113
100.822
37.726
8.462
1.00
21.28
D


ATOM
3876
CG
PHE
D
113
100.537
36.306
8.825
1.00
20.91
D


ATOM
3877
CD1
PHE
D
113
99.630
36.012
9.838
1.00
19.85
D


ATOM
3878
CD2
PHE
0
113
101.244
35.261
8.230
1.00
22.61
D


ATOM
3879
CE1
PHE
D
113
99.430
34.698
10.264
1.00
20.63
D


ATOM
3880
CE2
PHE
D
113
101.054
33.942
8.646
1.00
21.21
D


ATOM
3881
CZ
PHE
D
113
100.144
33.660
9.669
1.00
20.87
D


ATOM
3882
C
PHE
D
113
103.201
37.871
9.071
1.00
19.98
D


ATOM
3883
O
PHE
D
113
103.762
38.238
8.044
1.00
20.80
D


ATOM
3884
N
PRO
D
114
103.765
37.005
9.925
1.00
21.26
D


ATOM
3885
CD
PRO
D
114
105.101
36.414
9.732
1.00
21.94
D


ATOM
3886
CA
PRO
D
114
103.150
36.518
11.166
1.00
21.41
D


ATOM
3887
CB
PRO
D
114
104.117
35.424
11.625
1.00
21.03
D


ATOM
3888
CG
PRO
D
114
105.441
35.912
11.115
1.00
22.98
D


ATOM
3889
C
PRO
D
114
103.002
37.648
12.185
1.00
21.84
D


ATOM
3890
O
PRO
D
114
103.621
38.711
12.034
1.00
20.41
D


ATOM
3891
N
PRO
D
115
102.167
37.441
13.222
1.00
22.52
D


ATOM
3892
CD
PRO
D
115
101.314
36.256
13.445
1.00
22.08
D


ATOM
3893
CA
PRO
D
115
101.937
38.448
14.266
1.00
21.19
D


ATOM
3894
CB
PRO
D
115
100.730
37.895
15.025
1.00
20.92
D


ATOM
3895
CG
PRO
D
115
100.917
36.410
14.902
1.00
19.88
D


ATOM
3896
C
PRO
D
115
103.139
38.683
15.171
1.00
21.62
D


ATOM
3897
O
PRO
D
115
103.127
38.336
16.356
1.00
22.92
D


ATOM
3898
N
VAL
D
116
104.179
39.263
14.588
1.00
21.58
D


ATOM
3899
CA
VAL
D
116
105.405
39.598
15.300
1.00
22.53
D


ATOM
3900
CB
VAL
D
116
106.520
38.554
15.067
1.00
24.90
D


ATOM
3901
CG1
VAL
D
116
107.817
39.035
15.713
1.00
24.06
D


ATOM
3902
CG2
VAL
D
116
106.104
37.195
15.641
1.00
24.88
D


ATOM
3903
C
VAL
D
116
105.855
40.929
14.708
1.00
21.86
D


ATOM
3904
O
VAL
D
116
106.114
41.027
13.509
1.00
20.87
D


ATOM
3905
N
VAL
D
117
105.935
41.962
15.534
1.00
20.65
D


ATOM
3906
CA
VAL
D
117
106.338
43.255
15.007
1.00
21.60
D


ATOM
3907
CB
VAL
D
117
105.126
43.978
14.345
1.00
18.11
D


ATOM
3908
CG1
VAL
D
117
104.156
44.473
15.403
1.00
16.63
D


ATOM
3909
CG2
VAL
D
117
105.599
45.101
13.469
1.00
17.02
D


ATOM
3910
C
VAL
D
117
106.928
44.137
16.092
1.00
23.84
D


ATOM
3911
O
VAL
D
117
106.677
43.936
17.280
1.00
24.78
D


ATOM
3912
N
ASN
D
118
107.719
45.113
15.670
1.00
27.93
D


ATOM
3913
CA
ASN
D
118
108.348
46.051
16.593
1.00
30.45
D


ATOM
3914
CB
ASN
D
118
109.866
45.898
16.538
1.00
33.93
D


ATOM
3915
CG
ASN
D
118
110.564
46.644
17.650
1.00
39.88
D


ATOM
3916
OD1
ASN
D
118
110.327
47.834
17.856
1.00
42.45
D


ATOM
3917
ND2
ASN
D
118
111.438
45.946
18.375
1.00
43.14
D


ATOM
3918
C
ASN
D
118
107.960
47.465
16.181
1.00
27.72
D


ATOM
3919
O
ASN
D
118
108.398
47.952
15.140
1.00
26.88
D


ATOM
3920
N
ILE
D
119
107.126
48.113
16.988
1.00
27.59
D


ATOM
3921
CA
ILE
D
119
106.680
49.476
16.700
1.00
27.12
D


ATOM
3922
CB
ILE
D
119
105.133
49.580
16.719
1.00
27.17
D


ATOM
3923
CG2
ILE
D
119
104.698
50.994
16.346
1.00
26.16
D


ATOM
3924
CG1
ILE
D
119
104.528
48.572
15.741
1.00
24.63
D


ATOM
3925
CD1
ILE
D
119
103.026
48.423
15.877
1.00
24.19
D


ATOM
3926
C
ILE
D
119
107.243
50.436
17.746
1.00
27.72
D


ATOM
3927
O
ILE
D
119
107.050
50.248
18.946
1.00
26.86
D


ATOM
3928
N
THR
D
120
107.951
51.460
17.291
1.00
27.54
D


ATOM
3929
CA
THR
D
120
108.524
52.423
18.214
1.00
29.37
D


ATOM
3930
CB
THR
D
120
110.022
52.131
18.477
1.00
32.22
D


ATOM
3931
OG1
THR
D
120
110.722
52.034
17.229
1.00
35.14
D


ATOM
3932
CG2
THR
D
120
110.176
50.817
19.247
1.00
35.67
D


ATOM
3933
C
THR
D
120
108.369
53.826
17.668
1.00
27.95
D


ATOM
3934
O
THR
D
120
108.398
54.035
16.459
1.00
29.89
D


ATOM
3935
N
TRP
D
121
108.187
54.789
18.560
1.00
26.28
D


ATOM
3936
CA
TRP
D
121
108.031
56.171
18.135
1.00
26.93
D


ATOM
3937
CB
TRP
D
121
106.935
56.866
18.940
1.00
24.20
D


ATOM
3938
CG
TRP
D
121
105.568
56.343
18.687
1.00
22.03
D


ATOM
3939
CD2
TRP
D
121
104.643
56.826
17.707
1.00
20.30
D


ATOM
3940
CE2
TRP
D
121
103.454
56.085
17.856
1.00
20.70
D


ATOM
3941
CE3
TRP
D
121
104.705
57.817
16.717
1.00
17.15
D


ATOM
3942
CD1
TRP
D
121
104.929
55.351
19.365
1.00
21.06
D


ATOM
3943
NE1
TRP
D
121
103.655
55.190
18.875
1.00
22.39
D


ATOM
3944
CZ2
TRP
D
121
102.332
56.305
17.057
1.00
17.25
D


ATOM
3945
CZ3
TRP
D
121
103.593
58.036
15.924
1.00
17.92
D


ATOM
3946
CH2
TRP
D
121
102.419
57.282
16.099
1.00
19.11
D


ATOM
3947
C
TRP
D
121
109.319
56.957
18.284
1.00
26.88
D


ATOM
3948
O
TRP
D
121
110.059
56.789
19.251
1.00
27.48
D


ATOM
3949
N
LEU
D
122
109.572
57.830
17.321
1.00
29.82
D


ATOM
3950
CA
LEU
D
122
110.764
58.658
17.343
1.00
31.91
D


ATOM
3951
CB
LEU
D
122
111.664
58.331
16.144
1.00
34.65
D


ATOM
3952
CG
LEU
D
122
112.391
56.977
16.112
1.00
37.28
D


ATOM
3953
CD1
LEU
D
122
113.247
56.828
17.360
1.00
37.11
D


ATOM
3954
CD2
LEU
D
122
111.394
55.840
16.025
1.00
39.41
D


ATOM
3955
C
LEU
D
122
110.416
60.142
17.324
1.00
31.97
D


ATOM
3956
O
LEU
D
122
109.619
60.593
16.503
1.00
31.46
D


ATOM
3957
N
SER
D
123
111.010
60.889
18.250
1.00
31.03
D


ATOM
3958
CA
SER
D
123
110.813
62.331
18.326
1.00
33.04
D


ATOM
3959
CB
SER
D
123
110.312
62.745
19.712
1.00
32.42
D


ATOM
3960
OG
SER
D
123
110.169
64.154
19.793
1.00
32.43
D


ATOM
3961
C
SER
D
123
112.184
62.948
18.062
1.00
33.10
D


ATOM
3962
O
SER
D
123
113.108
62.784
18.860
1.00
33.57
D


ATOM
3963
N
ASN
D
124
112.309
63.646
16.941
1.00
33.51
D


ATOM
3964
CA
ASN
D
124
113.575
64.258
16.553
1.00
36.20
D


ATOM
3965
CB
ASN
D
124
113.963
65.392
17.510
1.00
34.61
D


ATOM
3966
CG
ASN
D
124
112.946
66.512
17.531
1.00
34.17
D


ATOM
3967
OD1
ASN
D
124
112.262
66.764
16.539
1.00
34.73
D


ATOM
3968
ND2
ASN
D
124
112.850
67.202
18.660
1.00
35.34
D


ATOM
3969
C
ASN
D
124
114.664
63.191
16.561
1.00
37.34
D


ATOM
3970
O
ASN
D
124
115.747
63.401
17.104
1.00
37.93
D


ATOM
3971
N
GLY
D
125
114.358
62.039
15.970
1.00
38.73
D


ATOM
3972
CA
GLY
D
125
115.317
60.951
15.910
1.00
39.56
D


ATOM
3973
C
GLY
D
125
115.457
60.131
17.183
1.00
40.55
D


ATOM
3974
O
GLY
D
125
116.051
59.054
17.157
1.00
42.52
D


ATOM
3975
N
HIS
D
126
114.911
60.622
18.291
1.00
40.35
D


ATOM
3976
CA
HIS
D
126
115.009
59.918
19.569
1.00
41.15
D


ATOM
3977
CB
HIS
D
126
115.234
60.923
20.702
1.00
43.51
D


ATOM
3978
CG
HIS
D
126
116.525
61.678
20.599
1.00
47.67
D


ATOM
3979
CD2
HIS
D
126
116.775
62.997
20.422
1.00
47.36
D


ATOM
3980
ND1
HIS
D
126
117.757
61.064
20.694
1.00
49.39
D


ATOM
3981
CE1
HIS
D
126
118.709
61.973
20.581
1.00
48.59
D


ATOM
3982
NE2
HIS
D
126
118.140
63.154
20.415
1.00
48.17
D


ATOM
3983
C
HIS
D
126
113.794
59.053
19.907
1.00
40.38
D


ATOM
3984
O
HIS
D
126
112.648
59.458
19.706
1.00
39.87
D


ATOM
3985
N
SER
D
127
114.056
57.863
20.438
1.00
39.11
D


ATOM
3986
CA
SER
D
127
112.995
56.939
20.821
1.00
39.54
D


ATOM
3987
CB
SER
D
127
113.592
55.592
21.232
1.00
40.04
D


ATOM
3988
OG
SER
D
127
114.299
55.001
20.159
1.00
45.08
D


ATOM
3989
C
SER
D
127
112.167
57.492
21.979
1.00
38.18
D


ATOM
3990
O
SER
D
127
112.707
58.054
22.930
1.00
38.52
D


ATOM
3991
N
VAL
D
128
110.854
57.326
21.894
1.00
36.40
D


ATOM
3992
CA
VAL
D
128
109.967
57.800
22.942
1.00
35.00
D


ATOM
3993
CB
VAL
D
128
108.699
58.444
22.358
1.00
33.68
D


ATOM
3994
CG1
VAL
D
128
107.834
59.001
23.479
1.00
32.31
D


ATOM
3995
CG2
VAL
D
128
109.081
59.543
21.383
1.00
32.69
D


ATOM
3996
C
VAL
D
128
109.574
56.608
23.790
1.00
34.62
D


ATOM
3997
O
VAL
D
128
109.150
55.584
23.268
1.00
35.98
D


ATOM
3998
N
THR
D
129
109.715
56.743
25.100
1.00
35.57
D


ATOM
3999
CA
THR
D
129
109.393
55.653
26.007
1.00
38.21
D


ATOM
4000
CB
THR
D
129
110.562
55.410
26.992
1.00
40.63
D


ATOM
4001
OG1
THR
D
129
110.184
54.413
27.949
1.00
44.78
D


ATOM
4002
CG2
THR
D
129
110.929
56.700
27.715
1.00
42.66
D


ATOM
4003
C
THR
D
129
108.103
55.862
26.799
1.00
36.54
D


ATOM
4004
O
THR
D
129
107.359
54.911
27.042
1.00
38.87
D


ATOM
4005
N
GLU
D
130
107.833
57.101
27.195
1.00
33.00
D


ATOM
4006
CA
GLU
D
130
106.631
57.401
27.963
1.00
31.03
D


ATOM
4007
CB
GLU
D
130
106.935
58.453
29.039
1.00
33.90
D


ATOM
4008
CG
GLU
D
130
108.067
58.089
29.987
1.00
38.08
D


ATOM
4009
CD
GLU
D
130
107.809
56.788
30.731
1.00
43.43
D


ATOM
4010
OE1
GLU
D
130
106.744
56.672
31.375
1.00
45.61
D


ATOM
4011
OE2
GLU
D
130
108.671
55.879
30.675
1.00
45.67
D


ATOM
4012
C
GLU
D
130
105.521
57.922
27.058
1.00
27.87
D


ATOM
4013
O
GLU
D
130
105.795
58.527
26.029
1.00
24.56
D


ATOM
4014
N
GLY
D
131
104.272
57.692
27.457
1.00
26.29
D


ATOM
4015
CA
GLY
D
131
103.140
58.166
26.679
1.00
25.19
D


ATOM
4016
C
GLY
D
131
102.826
57.304
25.474
1.00
24.46
D


ATOM
4017
O
GLY
D
131
102.130
57.725
24.559
1.00
23.65
D


ATOM
4018
N
VAL
D
132
103.349
56.089
25.476
1.00
22.83
D


ATOM
4019
CA
VAL
D
132
103.117
55.169
24.379
1.00
23.04
D


ATOM
4020
CB
VAL
D
132
104.448
54.674
23.784
1.00
22.91
D


ATOM
4021
CG1
VAL
D
132
104.182
53.538
22.821
1.00
24.12
D


ATOM
4022
CG2
VAL
D
132
105.164
55.816
23.076
1.00
22.85
D


ATOM
4023
C
VAL
D
132
102.326
53.943
24.829
1.00
21.91
D


ATOM
4024
O
VAL
D
132
102.535
53.416
25.917
1.00
21.27
D


ATOM
4025
N
SER
D
133
101.412
53.499
23.979
1.00
22.08
D


ATOM
4026
CA
SER
D
133
100.622
52.307
24.251
1.00
21.07
D


ATOM
4027
CB
SER
D
133
99.405
52.637
25.119
1.00
21.95
D


ATOM
4028
OG
SER
D
133
98.567
53.595
24.498
1.00
27.01
D


ATOM
4029
C
SER
D
133
100.178
51.738
22.908
1.00
21.27
D


ATOM
4030
O
SER
D
133
100.344
52.369
21.864
1.00
19.82
D


ATOM
4031
N
GLU
D
134
99.627
50.538
22.926
1.00
20.29
D


ATOM
4032
CA
GLU
D
134
99.182
49.938
21.689
1.00
24.12
D


ATOM
4033
CB
GLU
D
134
100.370
49.323
20.932
1.00
26.01
D


ATOM
4034
CG
GLU
D
134
100.932
48.045
21.532
1.00
30.80
D


ATOM
4035
CD
GLU
D
134
102.080
47.480
20.704
1.00
35.43
D


ATOM
4036
OE1
GLU
D
134
102.273
46.243
20.702
1.00
36.93
D


ATOM
4037
OE2
GLU
D
134
102.793
48.278
20.057
1.00
37.66
D


ATOM
4038
C
GLU
D
134
98.127
48.882
21.955
1.00
22.81
D


ATOM
4039
O
GLU
D
134
97.968
48.416
23.081
1.00
22.94
D


ATOM
4040
N
THR
D
135
97.400
48.522
20.908
1.00
21.95
D


ATOM
4041
CA
THR
D
135
96.361
47.519
21.009
1.00
20.78
D


ATOM
4042
CB
THR
D
135
95.368
47.625
19.843
1.00
20.82
D


ATOM
4043
OG1
THR
D
135
96.032
47.262
18.623
1.00
22.24
D


ATOM
4044
CG2
THR
D
135
94.833
49.046
19.721
1.00
18.01
D


ATOM
4045
C
THR
D
135
97.037
46.168
20.890
1.00
20.80
D


ATOM
4046
O
THR
D
135
98.259
46.084
20.742
1.00
21.08
D


ATOM
4047
N
SER
D
136
96.234
45.116
20.972
1.00
19.11
D


ATOM
4048
CA
SER
D
136
96.728
43.764
20.790
1.00
16.93
D


ATOM
4049
CB
SER
D
136
95.769
42.755
21.428
1.00
19.17
D


ATOM
4050
OG
SER
D
136
95.656
42.951
22.831
1.00
23.01
D


ATOM
4051
C
SER
D
136
96.665
43.635
19.267
1.00
15.30
D


ATOM
4052
O
SER
D
136
96.325
44.592
18.580
1.00
13.19
D


ATOM
4053
N
PHE
D
137
97.002
42.472
18.733
1.00
16.43
D


ATOM
4054
CA
PHE
D
137
96.896
42.267
17.294
1.00
16.20
D


ATOM
4055
CB
PHE
D
137
97.652
41.001
16.874
1.00
15.86
D


ATOM
4056
CG
PHE
D
137
99.138
41.146
16.879
1.00
17.29
D


ATOM
4057
CD1
PHE
D
137
99.792
41.775
15.823
1.00
20.23
D


ATOM
4058
CD2
PHE
D
137
99.894
40.644
17.932
1.00
17.79
D


ATOM
4059
CE1
PHE
D
137
101.187
41.900
15.815
1.00
21.20
D


ATOM
4060
CE2
PHE
D
137
101.291
40.762
17.936
1.00
19.39
D


ATOM
4061
CZ
PHE
D
137
101.935
41.392
16.874
1.00
19.70
D


ATOM
4062
C
PHE
D
137
95.402
42.056
17.025
1.00
16.08
D


ATOM
4063
O
PHE
D
137
94.823
41.121
17.556
1.00
15.19
D


ATOM
4064
N
LEU
D
138
94.786
42.925
16.227
1.00
19.23
D


ATOM
4065
CA
LEU
D
138
93.367
42.797
15.882
1.00
21.12
D


ATOM
4066
CB
LEU
D
138
92.722
44.175
15.678
1.00
21.40
D


ATOM
4067
CG
LEU
D
138
92.452
45.087
16.881
1.00
22.42
D


ATOM
4068
CD1
LEU
D
138
91.889
44.277
18.032
1.00
23.38
D


ATOM
4069
CD2
LEU
D
138
93.732
45.164
17.301
1.00
28.68
D


ATOM
4070
C
LEU
D
138
93.230
41.982
14.593
1.00
20.56
D


ATOM
4071
O
LEU
D
138
93.919
42.244
13.615
1.00
22.27
D


ATOM
4072
N
SER
D
139
92.326
41.013
14.586
1.00
20.44
D


ATOM
4073
CA
SER
D
139
92.143
40.142
13.427
1.00
19.23
D


ATOM
4074
CB
SER
D
139
91.222
38.986
13.788
1.00
19.74
D


ATOM
4075
OG
SER
D
139
89.888
39.443
13.861
1.00
21.32
D


ATOM
4076
C
SER
D
139
91.594
40.802
12.168
1.00
19.43
D


ATOM
4077
O
SER
D
139
91.028
41.893
12.210
1.00
19.49
D


ATOM
4078
N
LYS
D
140
91.755
40.102
11.050
1.00
18.62
D


ATOM
4079
CA
LYS
D
140
91.276
40.553
9.749
1.00
19.20
D


ATOM
4080
CB
LYS
D
140
92.437
41.058
8.895
1.00
18.92
D


ATOM
4081
CG
LYS
D
140
93.286
42.126
9.554
1.00
19.38
D


ATOM
4082
CD
LYS
D
140
93.254
43.393
8.758
1.00
20.95
D


ATOM
4083
CE
LYS
D
140
93.833
43.195
7.377
1.00
18.23
D


ATOM
4084
NZ
LYS
D
140
93.743
44.457
6.617
1.00
20.40
D


ATOM
4085
C
LYS
D
140
90.660
39.339
9.068
1.00
19.16
D


ATOM
4086
O
LYS
D
140
91.091
38.217
9.312
1.00
19.77
D


ATOM
4087
N
SER
D
141
89.670
39.552
8.207
1.00
21.60
D


ATOM
4088
CA
SER
D
141
89.030
38.438
7.507
1.00
23.19
D


ATOM
4089
CB
SER
D
141
87.859
38.948
6.653
1.00
24.88
D


ATOM
4090
OG
SER
D
141
88.288
39.858
5.655
1.00
28.69
D


ATOM
4091
C
SER
D
141
89.989
37.605
6.636
1.00
23.26
D


ATOM
4092
O
SER
D
141
89.692
36.454
6.327
1.00
23.33
D


ATOM
4093
N
ASP
D
142
91.137
38.159
6.251
1.00
21.38
D


ATOM
4094
CA
ASP
D
142
92.075
37.387
5.429
1.00
22.54
D


ATOM
4095
CB
ASP
D
142
92.834
38.303
4.466
1.00
25.84
D


ATOM
4096
CG
ASP
D
142
93.943
39.064
5.143
1.00
29.78
D


ATOM
4097
OD1
ASP
D
142
93.760
39.486
6.309
1.00
31.16
D


ATOM
4098
OD2
ASP
D
142
94.997
39.246
4.500
1.00
34.64
D


ATOM
4099
C
ASP
D
142
93.045
36.637
6.336
1.00
22.89
D


ATOM
4100
O
ASP
D
142
94.027
36.037
5.883
1.00
20.54
D


ATOM
4101
N
HIS
D
143
92.753
36.700
7.632
1.00
21.06
D


ATOM
4102
CA
HIS
D
143
93.522
36.020
8.659
1.00
19.58
D


ATOM
4103
CB
HIS
D
143
93.628
34.534
8.317
1.00
19.03
D


ATOM
4104
CG
HIS
D
143
92.295
33.892
8.104
1.00
23.00
D


ATOM
4105
CD2
HIS
D
143
91.827
33.108
7.104
1.00
24.78
D


ATOM
4106
ND1
HIS
D
143
91.237
34.087
8.967
1.00
21.97
D


ATOM
4107
CE1
HIS
D
143
90.174
33.455
8.505
1.00
24.67
D


ATOM
4108
NE2
HIS
D
143
90.504
32.853
7.375
1.00
24.72
D


ATOM
4109
C
HIS
D
143
94.878
36.602
8.986
1.00
20.11
D


ATOM
4110
O
HIS
D
143
95.691
35.962
9.654
1.00
21.09
D


ATOM
4111
N
SER
D
144
95.118
37.820
8.514
1.00
21.24
D


ATOM
4112
CA
SER
D
144
96.352
38.525
8.826
1.00
21.79
D


ATOM
4113
CB
SER
D
144
96.834
39.353
7.627
1.00
20.33
D


ATOM
4114
OG
SER
D
144
96.047
40.511
7.434
1.00
24.32
D


ATOM
4115
C
SER
D
144
95.940
39.440
9.990
1.00
21.43
D


ATOM
4116
O
SER
D
144
94.830
39.317
10.504
1.00
20.74
D


ATOM
4117
N
PHE
D
145
96.809
40.352
10.412
1.00
21.56
D


ATOM
4118
CA
PHE
D
145
96.463
41.235
11.523
1.00
22.54
D


ATOM
4119
CB
PHE
D
145
97.156
40.791
12.817
1.00
22.63
D


ATOM
4120
CG
PHE
D
145
96.896
39.368
13.200
1.00
25.73
D


ATOM
4121
CD1
PHE
D
145
97.565
38.329
12.562
1.00
26.67
D


ATOM
4122
CD2
PHE
D
145
95.987
39.063
14.207
1.00
23.65
D


ATOM
4123
CE1
PHE
D
145
97.333
37.004
12.921
1.00
27.30
D


ATOM
4124
CE2
PHE
D
145
95.750
37.746
14.572
1.00
25.43
D


ATOM
4125
CZ
PHE
D
145
96.426
36.713
13.926
1.00
24.90
D


ATOM
4126
C
PHE
D
145
96.850
42.687
11.299
1.00
22.51
D


ATOM
4127
O
PHE
D
145
97.540
43.028
10.339
1.00
23.97
D


ATOM
4128
N
PHE
D
146
96.371
43.540
12.198
1.00
20.96
D


ATOM
4129
CA
PHE
D
146
96.729
44.946
12.190
1.00
19.68
D


ATOM
4130
CB
PHE
D
146
95.696
45.817
11.439
1.00
17.70
D


ATOM
4131
CG
PHE
D
146
94.392
46.041
12.159
1.00
15.76
D


ATOM
4132
CD1
PHE
D
146
94.201
47.173
12.948
1.00
16.08
D


ATOM
4133
CD2
PHE
D
146
93.321
45.170
11.976
1.00
14.70
D


ATOM
4134
CE1
PHE
D
146
92.961
47.442
13.543
1.00
13.47
D


ATOM
4135
CE2
PHE
D
146
92.080
45.426
12.563
1.00
15.43
D


ATOM
4136
CZ
PHE
D
146
91.900
46.567
13.350
1.00
14.68
D


ATOM
4137
C
PHE
D
146
96.893
45.335
13.654
1.00
19.66
D


ATOM
4138
O
PHE
D
146
96.373
44.672
14.551
1.00
19.92
D


ATOM
4139
N
LYS
D
147
97.666
46.379
13.901
1.00
20.23
D


ATOM
4140
CA
LYS
D
147
97.910
46.817
15.260
1.00
19.84
D


ATOM
4141
CB
LYS
D
147
99.184
46.148
15.796
1.00
21.50
D


ATOM
4142
CG
LYS
D
147
99.651
46.679
17.134
1.00
24.87
D


ATOM
4143
CD
LYS
D
147
100.764
45.832
17.724
1.00
27.18
D


ATOM
4144
CE
LYS
D
147
100.220
44.515
18.253
1.00
31.41
D


ATOM
4145
NZ
LYS
D
147
101.086
43.984
19.341
1.00
32.97
D


ATOM
4146
C
LYS
D
147
98.038
48.324
15.274
1.00
18.69
D


ATOM
4147
O
LYS
D
147
98.603
48.914
14.352
1.00
20.14
D


ATOM
4148
N
ILE
D
148
97.497
48.944
16.314
1.00
18.22
D


ATOM
4149
CA
ILE
D
148
97.530
50.387
16.446
1.00
18.25
D


ATOM
4150
CB
ILE
D
148
96.092
50.942
16.548
1.00
20.80
D


ATOM
4151
CG2
ILE
D
148
96.113
52.459
16.659
1.00
22.44
D


ATOM
4152
CG1
ILE
D
148
95.308
50.533
15.292
1.00
23.89
D


ATOM
4153
CD1
ILE
D
148
93.840
50.858
15.314
1.00
24.42
D


ATOM
4154
C
ILE
D
148
98.369
50.816
17.646
1.00
19.71
D


ATOM
4155
O
ILE
D
148
98.213
50.294
18.757
1.00
17.77
D


ATOM
4156
N
SER
D
149
99.284
51.753
17.395
1.00
19.08
D


ATOM
4157
CA
SER
D
149
100.173
52.278
18.424
1.00
18.19
D


ATOM
4158
CB
SER
D
149
101.633
52.137
17.991
1.00
18.51
D


ATOM
4159
OG
SER
D
149
102.518
52.492
19.040
1.00
19.49
D


ATOM
4160
C
SER
D
149
99.839
53.744
18.646
1.00
18.14
D


ATOM
4161
O
SER
D
149
99.591
54.490
17.693
1.00
18.17
D


ATOM
4162
N
TYR
D
150
99.843
54.155
19.905
1.00
16.95
D


ATOM
4163
CA
TYR
D
150
99.503
55.524
20.261
1.00
16.12
D


ATOM
4164
CB
TYR
D
150
98.310
55.524
21.213
1.00
15.57
D


ATOM
4165
CG
TYR
D
150
97.116
54.750
20.701
1.00
16.81
D


ATOM
4166
CD1
TYR
D
150
96.291
55.276
19.709
1.00
14.33
D


ATOM
4167
CE1
TYR
D
150
95.197
54.554
19.222
1.00
17.50
D


ATOM
4168
CD2
TYR
D
150
96.819
53.486
21.199
1.00
15.90
D


ATOM
4169
CE2
TYR
D
150
95.731
52.760
20.719
1.00
18.41
D


ATOM
4170
CZ
TYR
D
150
94.928
53.297
19.732
1.00
16.27
D


ATOM
4171
OH
TYR
D
150
93.868
52.574
19.244
1.00
20.03
D


ATOM
4172
C
TYR
D
150
100.650
56.266
20.922
1.00
16.35
D


ATOM
4173
O
TYR
D
150
101.438
55.690
21.669
1.00
16.95
D


ATOM
4174
N
LEU
D
151
100.732
57.558
20.643
1.00
16.64
D


ATOM
4175
CA
LEU
D
151
101.760
58.396
21.227
1.00
16.50
D


ATOM
4176
CB
LEU
D
151
102.849
58.705
20.203
1.00
15.48
D


ATOM
4177
CG
LEU
D
151
103.806
59.825
20.639
1.00
17.55
D


ATOM
4178
CD1
LEU
D
151
104.641
59.374
21.834
1.00
16.60
D


ATOM
4179
CD2
LEU
D
151
104.702
60.213
19.476
1.00
16.11
D


ATOM
4180
C
LEU
D
151
101.140
59.701
21.693
1.00
17.56
D


ATOM
4181
O
LEU
D
151
100.577
60.440
20.888
1.00
17.18
D


ATOM
4182
N
THR
D
152
101.233
59.997
22.983
1.00
16.14
D


ATOM
4183
CA
THR
D
152
100.690
61.259
23.448
1.00
19.47
D


ATOM
4184
CB
THR
D
152
100.359
61.248
24.966
1.00
21.24
D


ATOM
4185
OG1
THR
D
152
101.517
60.871
25.725
1.00
25.03
D


ATOM
4186
CG2
THR
D
152
99.214
60.281
25.247
1.00
20.79
D


ATOM
4187
C
THR
D
152
101.717
62.345
23.151
1.00
19.82
D


ATOM
4188
O
THR
D
152
102.921
62.113
23.218
1.00
21.31
D


ATOM
4189
N
LEU
D
153
101.241
63.523
22.781
1.00
20.76
D


ATOM
4190
CA
LEU
D
153
102.143
64.617
22.488
1.00
24.15
D


ATOM
4191
CB
LEU
D
153
102.760
64.450
21.089
1.00
25.45
D


ATOM
4192
CG
LEU
D
153
101.959
64.575
19.785
1.00
27.17
D


ATOM
4193
CD1
LEU
D
153
100.520
64.101
19.986
1.00
27.83
D


ATOM
4194
CD2
LEU
D
153
101.982
66.015
19.319
1.00
27.38
D


ATOM
4195
C
LEU
D
153
101.440
65.952
22.601
1.00
25.73
D


ATOM
4196
O
LEU
D
153
100.208
66.028
22.681
1.00
26.55
D


ATOM
4197
N
LEU
D
154
102.251
67.000
22.640
1.00
26.77
D


ATOM
4198
CA
LEU
D
154
101.781
68.369
22.734
1.00
26.34
D


ATOM
4199
CB
LEU
D
154
102.298
69.027
24.019
1.00
25.08
D


ATOM
4200
CG
LEU
D
154
101.877
70.478
24.288
1.00
26.28
D


ATOM
4201
CD1
LEU
D
154
100.377
70.531
24.570
1.00
24.44
D


ATOM
4202
CD2
LEU
D
154
102.667
71.031
25.477
1.00
23.08
D


ATOM
4203
C
LEU
D
154
102.374
69.063
21.522
1.00
28.41
D


ATOM
4204
O
LEU
D
154
103.577
69.327
21.468
1.00
27.19
D


ATOM
4205
N
PRO
D
155
101.534
69.351
20.523
1.00
30.32
D


ATOM
4206
CD
PRO
D
155
100.109
68.979
20.453
1.00
30.25
D


ATOM
4207
CA
PRO
D
155
101.965
70.014
19.294
1.00
31.71
D


ATOM
4208
CB
PRO
D
155
100.667
70.160
18.510
1.00
31.92
D


ATOM
4209
CG
PRO
D
155
99.861
68.968
18.963
1.00
31.51
D


ATOM
4210
C
PRO
D
155
102.663
71.354
19.508
1.00
35.12
D


ATOM
4211
O
PRO
D
155
102.110
72.275
20.112
1.00
35.64
D


ATOM
4212
N
SER
D
156
103.893
71.436
19.014
1.00
39.00
D


ATOM
4213
CA
SER
D
156
104.706
72.643
19.083
1.00
42.94
D


ATOM
4214
CB
SER
D
156
105.819
72.492
20.121
1.00
43.03
D


ATOM
4215
OG
SER
D
156
105.288
72.385
21.430
1.00
45.30
D


ATOM
4216
C
SER
D
156
105.311
72.763
17.694
1.00
46.03
D


ATOM
4217
O
SER
D
156
104.875
72.084
16.770
1.00
47.06
D


ATOM
4218
N
ALA
D
157
106.316
73.609
17.534
1.00
49.61
D


ATOM
4219
CA
ALA
D
157
106.931
73.756
16.222
1.00
51.03
D


ATOM
4220
CB
ALA
D
157
106.977
75.231
15.828
1.00
51.20
D


ATOM
4221
C
ALA
D
157
108.334
73.163
16.195
1.00
51.50
D


ATOM
4222
O
ALA
D
157
108.985
73.147
15.150
1.00
52.20
D


ATOM
4223
N
GLU
D
158
108.797
72.669
17.339
1.00
52.37
D


ATOM
4224
CA
GLU
D
158
110.141
72.103
17.411
1.00
53.43
D


ATOM
4225
CB
GLU
D
158
110.946
72.785
18.524
1.00
57.17
D


ATOM
4226
CG
GLU
D
158
110.401
72.570
19.934
1.00
61.50
D


ATOM
4227
CD
GLU
D
158
109.278
73.529
20.291
1.00
63.75
D


ATOM
4228
OE1
GLU
D
158
108.757
73.431
21.425
1.00
63.56
D


ATOM
4229
OE2
GLU
D
158
108.922
74.381
19.445
1.00
65.17
D


ATOM
4230
C
GLU
D
158
110.190
70.592
17.614
1.00
51.03
D


ATOM
4231
O
GLU
D
158
111.103
70.084
18.265
1.00
51.07
D


ATOM
4232
N
GLU
D
159
109.219
69.876
17.057
1.00
47.47
D


ATOM
4233
CA
GLU
D
159
109.185
68.425
17.193
1.00
46.22
D


ATOM
4234
CB
GLU
D
159
108.337
68.013
18.406
1.00
47.11
D


ATOM
4235
CG
GLU
D
159
109.127
67.692
19.671
1.00
48.53
D


ATOM
4236
CD
GLU
D
159
108.268
67.042
20.751
1.00
50.37
D


ATOM
4237
OE1
GLU
D
159
107.319
67.694
21.238
1.00
50.39
D


ATOM
4238
OE2
GLU
D
159
108.537
65.873
21.112
1.00
50.03
D


ATOM
4239
C
GLU
D
159
108.641
67.714
15.960
1.00
43.84
D


ATOM
4240
O
GLU
D
159
107.515
67.974
15.535
1.00
44.12
D


ATOM
4241
N
SER
D
160
109.443
66.825
15.380
1.00
39.56
D


ATOM
4242
CA
SER
D
160
108.993
66.054
14.229
1.00
37.29
D


ATOM
4243
CB
SER
D
160
109.971
66.172
13.055
1.00
37.41
D


ATOM
4244
OG
SER
D
160
111.070
65.298
13.206
1.00
41.72
D


ATOM
4245
C
SER
D
160
108.933
64.615
14.734
1.00
35.08
D


ATOM
4246
O
SER
D
160
109.754
64.207
15.557
1.00
33.66
D


ATOM
4247
N
TYR
D
161
107.961
63.846
14.260
1.00
32.11
D


ATOM
4248
CA
TYR
D
161
107.828
62.478
14.728
1.00
29.69
D


ATOM
4249
CB
TYR
D
161
106.550
62.315
15.547
1.00
29.62
D


ATOM
4250
CG
TYR
D
161
106.347
63.349
16.620
1.00
29.33
D


ATOM
4251
CD1
TYR
D
161
105.761
64.577
16.327
1.00
31.31
D


ATOM
4252
CE1
TYR
D
161
105.513
65.515
17.329
1.00
32.70
D


ATOM
4253
CD2
TYR
D
161
106.695
63.085
17.937
1.00
30.13
D


ATOM
4254
CE2
TYR
D
161
106.457
64.013
18.947
1.00
30.43
D


ATOM
4255
CZ
TYR
D
161
105.863
65.223
18.638
1.00
31.92
D


ATOM
4256
OH
TYR
D
161
105.592
66.128
19.643
1.00
35.12
D


ATOM
4257
C
TYR
D
161
107.820
61.441
13.627
1.00
29.60
D


ATOM
4258
O
TYR
D
161
107.493
61.728
12.473
1.00
29.45
D


ATOM
4259
N
ASP
D
162
108.172
60.221
14.005
1.00
29.35
D


ATOM
4260
CA
ASP
D
162
108.201
59.109
13.075
1.00
30.15
D


ATOM
4261
CB
ASP
D
162
109.618
58.863
12.548
1.00
34.90
D


ATOM
4262
CG
ASP
D
162
110.154
60.016
11.733
1.00
37.70
D


ATOM
4263
OD1
ASP
D
162
109.669
60.218
10.597
1.00
40.13
D


ATOM
4264
OD2
ASP
D
162
111.061
60.716
12.235
1.00
38.68
D


ATOM
4265
C
ASP
D
162
107.759
57.851
13.784
1.00
29.84
D


ATOM
4266
O
ASP
D
162
108.010
57.672
14.978
1.00
26.72
D


ATOM
4267
N
CYS
D
163
107.088
56.984
13.039
1.00
29.31
D


ATOM
4268
CA
CYS
D
163
106.684
55.700
13.569
1.00
29.59
D


ATOM
4269
C
CYS
D
163
107.689
54.769
12.902
1.00
28.04
D


ATOM
4270
O
CYS
D
163
107.822
54.772
11.685
1.00
26.22
D


ATOM
4271
CB
CYS
D
163
105.265
55.326
13.134
1.00
29.11
D


ATOM
4272
SG
CYS
D
163
104.703
53.760
13.878
1.00
34.32
D


ATOM
4273
N
LYS
D
164
108.417
54.001
13.699
1.00
29.03
D


ATOM
4274
CA
LYS
D
164
109.404
53.072
13.161
1.00
29.67
D


ATOM
4275
CB
LYS
D
164
110.730
53.238
13.911
1.00
32.54
D


ATOM
4276
CG
LYS
D
164
111.874
52.352
13.416
1.00
34.76
D


ATOM
4277
CD
LYS
D
164
113.109
52.528
14.297
1.00
34.79
D


ATOM
4278
CE
LYS
D
164
114.254
51.630
13.850
1.00
38.29
D


ATOM
4279
NZ
LYS
D
164
115.425
51.702
14.775
1.00
36.58
D


ATOM
4280
C
LYS
D
164
108.863
51.651
13.322
1.00
28.94
D


ATOM
4281
O
LYS
D
164
108.642
51.189
14.443
1.00
29.32
D


ATOM
4282
N
VAL
D
165
108.632
50.974
12.197
1.00
27.33
D


ATOM
4283
CA
VAL
D
165
108.100
49.618
12.212
1.00
26.58
D


ATOM
4284
CB
VAL
D
165
106.797
49.516
11.359
1.00
27.12
D


ATOM
4285
CG1
VAL
D
165
106.199
48.122
11.462
1.00
25.56
D


ATOM
4286
CG2
VAL
D
165
105.787
50.544
11.827
1.00
27.97
D


ATOM
4287
C
VAL
D
165
109.113
48.600
11.690
1.00
26.91
D


ATOM
4288
O
VAL
D
165
109.621
48.720
10.583
1.00
25.56
D


ATOM
4289
N
GLU
D
166
109.414
47.606
12.513
1.00
28.75
D


ATOM
4290
CA
GLU
D
166
110.338
46.544
12.139
1.00
30.67
D


ATOM
4291
CB
GLU
D
166
111.445
46.410
13.194
1.00
33.57
D


ATOM
4292
CG
GLU
D
166
112.452
47.565
13.142
1.00
41.68
D


ATOM
4293
CD
GLU
D
166
113.506
47.526
14.244
1.00
46.12
D


ATOM
4294
OE1
GLU
D
166
114.482
48.304
14.146
1.00
49.01
D


ATOM
4295
OE2
GLU
D
166
113.363
46.736
15.206
1.00
49.40
D


ATOM
4296
C
GLU
D
166
109.543
45.243
12.008
1.00
30.18
D


ATOM
4297
O
GLU
D
166
108.737
44.900
12.878
1.00
28.51
D


ATOM
4298
N
HIS
D
167
109.759
44.535
10.907
1.00
29.48
D


ATOM
4299
CA
HIS
D
167
109.056
43.281
10.648
1.00
30.29
D


ATOM
4300
CB
HIS
D
167
107.686
43.569
10.025
1.00
29.56
D


ATOM
4301
CG
HIS
D
167
106.808
42.363
9.903
1.00
30.02
D


ATOM
4302
CD2
HIS
D
167
106.562
41.541
8.856
1.00
29.91
D


ATOM
4303
ND1
HIS
D
167
106.068
41.871
10.957
1.00
31.27
D


ATOM
4304
CE1
HIS
D
167
105.404
40.798
10.564
1.00
28.43
D


ATOM
4305
NE2
HIS
D
167
105.687
40.576
9.293
1.00
28.97
D


ATOM
4306
C
HIS
D
167
109.886
42.440
9.684
1.00
30.36
D


ATOM
4307
O
HIS
D
167
110.607
42.976
8.842
1.00
30.66
D


ATOM
4308
N
TRP
D
168
109.775
41.122
9.801
1.00
31.13
D


ATOM
4309
CA
TRP
D
168
110.521
40.219
8.930
1.00
32.08
D


ATOM
4310
CB
TRP
D
168
110.270
38.765
9.336
1.00
28.28
D


ATOM
4311
CG
TRP
D
168
110.665
38.475
10.739
1.00
26.36
D


ATOM
4312
CD2
TRP
D
168
110.031
37.556
11.635
1.00
25.51
D


ATOM
4313
CE2
TRP
D
168
110.759
37.578
12.842
1.00
26.35
D


ATOM
4314
CE3
TRP
D
168
108.916
36.715
11.534
1.00
24.88
D


ATOM
4315
CD1
TRP
D
168
111.721
39.004
11.416
1.00
27.27
D


ATOM
4316
NE1
TRP
D
168
111.786
38.471
12.682
1.00
28.25
D


ATOM
4317
CZ2
TRP
D
168
110.412
36.791
13.943
1.00
27.00
D


ATOM
4318
CZ3
TRP
D
168
108.568
35.932
12.628
1.00
25.90
D


ATOM
4319
CH2
TRP
D
168
109.315
35.976
13.817
1.00
26.65
D


ATOM
4320
C
TRP
D
168
110.180
40.403
7.452
1.00
33.22
D


ATOM
4321
O
TRP
D
168
111.011
40.139
6.582
1.00
33.90
D


ATOM
4322
N
GLY
D
169
108.959
40.853
7.174
1.00
34.75
D


ATOM
4323
CA
GLY
D
169
108.533
41.060
5.797
1.00
36.14
D


ATOM
4324
C
GLY
D
169
109.056
42.359
5.215
1.00
37.80
D


ATOM
4325
O
GLY
D
169
108.635
42.796
4.139
1.00
36.95
D


ATOM
4326
N
LEU
D
170
109.979
42.981
5.938
1.00
38.89
D


ATOM
4327
CA
LEU
D
170
110.578
44.234
5.509
1.00
40.79
D


ATOM
4328
CB
LEU
D
170
110.212
45.356
6.480
1.00
39.77
D


ATOM
4329
CG
LEU
D
170
108.745
45.765
6.581
1.00
39.57
D


ATOM
4330
CD1
LEU
D
170
108.592
46.809
7.671
1.00
38.10
D


ATOM
4331
CD2
LEU
D
170
108.267
46.308
5.243
1.00
39.58
D


ATOM
4332
C
LEU
D
170
112.092
44.085
5.465
1.00
42.12
D


ATOM
4333
O
LEU
D
170
112.688
43.506
6.370
1.00
41.54
D


ATOM
4334
N
ASP
D
171
112.706
44.613
4.411
1.00
45.36
D


ATOM
4335
CA
ASP
D
171
114.158
44.559
4.252
1.00
48.35
D


ATOM
4336
CB
ASP
D
171
114.539
44.947
2.820
1.00
50.69
D


ATOM
4337
CG
ASP
D
171
113.467
45.775
2.137
1.00
52.75
D


ATOM
4338
OD1
ASP
D
171
113.076
46.827
2.689
1.00
54.19
D


ATOM
4339
OD2
ASP
D
171
113.012
45.372
1.046
1.00
54.32
D


ATOM
4340
C
ASP
D
171
114.849
45.485
5.255
1.00
48.43
D


ATOM
4341
O
ASP
D
171
115.816
45.090
5.910
1.00
48.29
D


ATOM
4342
N
LYS
D
172
114.348
46.715
5.364
1.00
48.92
D


ATOM
4343
CA
LYS
D
172
114.883
47.707
6.299
1.00
49.86
D


ATOM
4344
CB
LYS
D
172
115.502
48.898
5.552
1.00
51.58
D


ATOM
4345
CG
LYS
D
172
116.667
48.566
4.637
1.00
55.86
D


ATOM
4346
CD
LYS
D
172
116.203
47.963
3.316
1.00
58.23
D


ATOM
4347
CE
LYS
D
172
115.408
48.966
2.493
1.00
59.62
D


ATOM
4348
NZ
LYS
D
172
114.946
48.368
1.211
1.00
59.53
D


ATOM
4349
C
LYS
D
172
113.734
48.224
7.165
1.00
48.46
D


ATOM
4350
O
LYS
D
172
112.564
48.026
6.833
1.00
48.43
D


ATOM
4351
N
PRO
D
173
114.050
48.885
8.291
1.00
46.54
D


ATOM
4352
CD
PRO
D
173
115.355
49.048
8.954
1.00
46.03
D


ATOM
4353
CA
PRO
D
173
112.974
49.400
9.137
1.00
44.41
D


ATOM
4354
CB
PRO
D
173
113.722
50.029
10.305
1.00
44.19
D


ATOM
4355
CG
PRO
D
173
114.950
49.197
10.399
1.00
45.63
D


ATOM
4356
C
PRO
D
173
112.180
50.430
8.348
1.00
43.26
D


ATOM
4357
O
PRO
D
173
112.746
51.197
7.570
1.00
43.42
D


ATOM
4358
N
LEU
D
174
110.869
50.434
8.532
1.00
41.53
D


ATOM
4359
CA
LEU
D
174
110.023
51.381
7.829
1.00
39.96
D


ATOM
4360
CB
LEU
D
174
108.675
50.730
7.523
1.00
40.30
D


ATOM
4361
CG
LEU
D
174
107.900
51.223
6.303
1.00
40.55
D


ATOM
4362
CD1
LEU
D
174
106.637
50.397
6.151
1.00
42.25
D


ATOM
4363
CD2
LEU
D
174
107.568
52.698
6.448
1.00
42.67
D


ATOM
4364
C
LEU
D
174
109.845
52.586
8.753
1.00
39.80
D


ATOM
4365
O
LEU
D
174
109.645
52.420
9.955
1.00
39.99
D


ATOM
4366
N
LEU
D
175
109.947
53.792
8.200
1.00
38.49
D


ATOM
4367
CA
LEU
D
175
109.787
55.016
8.983
1.00
38.04
D


ATOM
4368
CB
LEU
D
175
111.095
55.812
9.045
1.00
38.62
D


ATOM
4369
CG
LEU
D
175
112.127
55.442
10.113
1.00
38.70
D


ATOM
4370
CD1
LEU
D
175
111.518
55.648
11.489
1.00
39.24
D


ATOM
4371
CD2
LEU
D
175
112.577
54.001
9.936
1.00
40.07
D


ATOM
4372
C
LEU
D
175
108.712
55.892
8.372
1.00
37.31
D


ATOM
4373
O
LEU
D
175
108.885
56.432
7.282
1.00
38.54
D


ATOM
4374
N
LYS
D
176
107.599
56.033
9.076
1.00
35.14
D


ATOM
4375
CA
LYS
D
176
106.511
56.850
8.577
1.00
34.26
D


ATOM
4376
CB
LYS
D
176
105.175
56.124
8.768
1.00
33.88
D


ATOM
4377
CG
LYS
D
176
104.204
56.325
7.620
1.00
36.72
D


ATOM
4378
CD
LYS
0
176
104.829
55.887
6.295
1.00
37.68
D


ATOM
4379
CE
LYS
D
176
103.820
55.913
5.155
1.00
39.32
D


ATOM
4380
NZ
LYS
D
176
103.195
57.254
4.974
1.00
40.75
D


ATOM
4381
C
LYS
D
176
106.523
58.166
9.335
1.00
32.22
D


ATOM
4382
O
LYS
D
176
106.272
58.204
10.537
1.00
32.35
D


ATOM
4383
N
HIS
D
177
106.825
59.243
8.625
1.00
29.85
D


ATOM
4384
CA
HIS
D
177
106.897
60.563
9.229
1.00
29.87
D


ATOM
4385
CB
HIS
D
177
107.836
61.456
8.411
1.00
30.84
D


ATOM
4386
CG
HIS
0
177
108.014
62.830
8.979
1.00
31.41
D


ATOM
4387
CD2
HIS
D
177
107.607
64.042
8.529
1.00
32.01
D


ATOM
4388
ND1
HIS
D
177
108.695
63.067
10.155
1.00
32.16
D


ATOM
4389
CE1
HIS
D
177
108.704
64.365
10.402
1.00
30.49
D


ATOM
4390
NE2
HIS
D
177
108.051
64.979
9.431
1.00
31.08
D


ATOM
4391
C
HIS
D
177
105.532
61.228
9.332
1.00
29.28
D


ATOM
4392
O
HIS
D
177
104.709
61.121
8.429
1.00
27.97
D


ATOM
4393
N
TRP
D
178
105.295
61.922
10.439
1.00
29.05
D


ATOM
4394
CA
TRP
D
178
104.031
62.617
10.619
1.00
29.38
D


ATOM
4395
CB
TRP
D
178
103.518
62.464
12.048
1.00
26.73
D


ATOM
4396
CG
TRP
D
178
102.205
63.165
12.243
1.00
27.32
D


ATOM
4397
CD2
TRP
D
178
101.939
64.262
13.122
1.00
24.87
D


ATOM
4398
CE2
TRP
D
178
100.580
64.608
12.959
1.00
26.97
D


ATOM
4399
CE3
TRP
D
178
102.714
64.986
14.033
1.00
26.15
D


ATOM
4400
CD1
TRP
D
178
101.028
62.898
11.599
1.00
26.41
D


ATOM
4401
NE1
TRP
D
178
100.050
63.759
12.023
1.00
25.31
D


ATOM
4402
CZ2
TRP
D
178
99.980
65.649
13.675
1.00
25.60
D


ATOM
4403
CZ3
TRP
D
178
102.118
66.021
14.746
1.00
27.98
D


ATOM
4404
CH2
TRP
D
178
100.763
66.340
14.562
1.00
27.02
D


ATOM
4405
C
TRP
D
178
104.185
64.100
10.294
1.00
30.33
D


ATOM
4406
O
TRP
D
178
104.756
64.824
11.143
1.00
29.85
D


ATOM
4407
OXT
TRP
D
178
103.745
64.512
9.193
1.00
32.23
D


ATOM
4408
CB
SER
E
3
113.641
35.776
8.019
1.00
59.19
E


ATOM
4409
OG
SER
E
3
112.349
35.748
8.608
1.00
59.65
E


ATOM
4410
C
SER
E
3
114.352
33.977
9.601
1.00
57.92
E


ATOM
4411
O
SER
E
3
114.571
32.945
8.970
1.00
57.45
E


ATOM
4412
N
SER
E
3
116.055
35.305
8.352
1.00
59.31
E


ATOM
4413
CA
SER
E
3
114.719
35.342
9.020
1.00
58.85
E


ATOM
4414
N
PRO
E
4
113.799
33.958
10.824
1.00
56.65
E


ATOM
4415
CD
PRO
E
4
113.679
35.092
11.759
1.00
56.20
E


ATOM
4416
CA
PRO
E
4
113.403
32.704
11.472
1.00
55.50
E


ATOM
4417
CB
PRO
E
4
113.362
33.086
12.946
1.00
56.49
E


ATOM
4418
CG
PRO
E
4
112.870
34.493
12.893
1.00
56.56
E


ATOM
4419
C
PRO
E
4
112.046
32.217
10.957
1.00
53.68
E


ATOM
4420
O
PRO
E
4
111.168
33.024
10.648
1.00
54.06
E


ATOM
4421
N
GLU
E
5
111.875
30.903
10.855
1.00
51.52
E


ATOM
4422
CA
GLU
E
5
110.610
30.360
10.373
1.00
49.69
E


ATOM
4423
CB
GLU
E
5
110.831
29.007
9.676
1.00
53.42
E


ATOM
4424
CG
GLU
E
5
111.305
27.867
10.561
1.00
57.99
E


ATOM
4425
CD
GLU
E
5
111.671
26.626
9.758
1.00
60.86
E


ATOM
4426
OE1
GLU
E
5
110.857
26.196
8.908
1.00
62.41
E


ATOM
4427
OE2
GLU
E
5
112.772
26.077
9.979
1.00
63.42
E


ATOM
4428
C
GLU
E
5
109.619
30.231
11.525
1.00
45.48
E


ATOM
4429
O
GLU
E
5
109.919
29.644
12.564
1.00
46.07
E


ATOM
4430
N
ASP
E
6
108.436
30.800
11.337
1.00
40.87
E


ATOM
4431
CA
ASP
E
6
107.403
30.782
12.363
1.00
36.20
E


ATOM
4432
CB
ASP
E
6
106.911
32.214
12.617
1.00
35.53
E


ATOM
4433
CG
ASP
E
6
105.995
32.323
13.827
1.00
33.60
E


ATOM
4434
OD1
ASP
E
6
105.185
33.268
13.864
1.00
34.88
E


ATOM
4435
OD2
ASP
E
6
106.089
31.487
14.748
1.00
33.84
E


ATOM
4436
C
ASP
E
6
106.229
29.915
11.938
1.00
33.07
E


ATOM
4437
O
ASP
E
6
105.882
29.867
10.762
1.00
32.95
E


ATOM
4438
N
PHE
E
7
105.632
29.228
12.906
1.00
31.08
E


ATOM
4439
CA
PHE
E
7
104.466
28.380
12.669
1.00
29.18
E


ATOM
4440
CB
PHE
E
7
104.760
26.950
13.116
1.00
31.11
E


ATOM
4441
CG
PHE
E
7
105.833
26.278
12.305
1.00
31.97
E


ATOM
4442
CD1
PHE
E
7
105.544
25.745
11.053
1.00
31.67
E


ATOM
4443
CD2
PHE
E
7
107.141
26.200
12.782
1.00
32.49
E


ATOM
4444
CE1
PHE
E
7
106.546
25.141
10.282
1.00
33.41
E


ATOM
4445
CE2
PHE
E
7
108.148
25.602
12.023
1.00
32.29
E


ATOM
4446
CZ
PHE
E
7
107.850
25.071
10.770
1.00
31.62
E


ATOM
4447
C
PHE
E
7
103.345
28.994
13.504
1.00
27.19
E


ATOM
4448
O
PHE
E
7
103.483
29.151
14.715
1.00
25.77
E


ATOM
4449
N
VAL
E
8
102.238
29.340
12.855
1.00
25.52
E


ATOM
4450
CA
VAL
E
8
101.127
29.998
13.538
1.00
23.97
E


ATOM
4451
CB
VAL
E
8
100.903
31.411
12.949
1.00
22.51
E


ATOM
4452
CG1
VAL
E
8
99.789
32.130
13.703
1.00
20.58
E


ATOM
4453
CG2
VAL
E
8
102.205
32.211
13.002
1.00
22.51
E


ATOM
4454
C
VAL
E
8
99.785
29.275
13.510
1.00
24.21
E


ATOM
4455
O
VAL
E
8
99.369
28.736
12.485
1.00
25.26
E


ATOM
4456
N
TYR
E
9
99.096
29.288
14.643
1.00
23.98
E


ATOM
4457
CA
TYR
E
9
97.786
28.663
14.724
1.00
23.53
E


ATOM
4458
CB
TYR
E
9
97.796
27.505
15.718
1.00
24.07
E


ATOM
4459
CG
TYR
E
9
96.562
26.640
15.627
1.00
25.27
E


ATOM
4460
CD1
TYR
E
9
96.570
25.460
14.889
1.00
27.68
E


ATOM
4461
CE1
TYR
E
9
95.435
24.658
14.801
1.00
27.67
E


ATOM
4462
CD2
TYR
E
9
95.384
27.002
16.272
1.00
24.82
E


ATOM
4463
CE2
TYR
E
9
94.245
26.211
16.191
1.00
25.29
E


ATOM
4464
CZ
TYR
E
9
94.277
25.040
15.458
1.00
26.82
E


ATOM
4465
OH
TYR
E
9
93.163
24.240
15.403
1.00
27.65
E


ATOM
4466
C
TYR
E
9
96.775
29.707
15.179
1.00
23.14
E


ATOM
4467
O
TYR
E
9
97.037
30.476
16.106
1.00
23.66
E


ATOM
4468
N
GLN
E
10
95.622
29.739
14.523
1.00
21.64
E


ATOM
4469
CA
GLN
E
10
94.582
30.686
14.892
1.00
21.14
E


ATOM
4470
CB
GLN
E
10
94.438
31.793
13.843
1.00
20.35
E


ATOM
4471
CG
GLN
E
10
95.677
32.598
13.529
1.00
19.58
E


ATOM
4472
CD
GLN
E
10
95.410
33.655
12.461
1.00
18.44
E


ATOM
4473
OE1
GLN
E
10
94.498
34.474
12.593
1.00
19.00
E


ATOM
4474
NE2
GLN
E
10
96.206
33.640
11.400
1.00
18.89
E


ATOM
4475
C
GLN
E
10
93.232
29.997
15.006
1.00
19.74
E


ATOM
4476
O
GLN
E
10
92.904
29.113
14.223
1.00
21.71
E


ATOM
4477
N
PHE
E
11
92.450
30.408
15.991
1.00
19.13
E


ATOM
4478
CA
PHE
E
11
91.108
29.887
16.145
1.00
16.86
E


ATOM
4479
CB
PHE
E
11
90.981
28.881
17.271
1.00
16.74
E


ATOM
4480
CG
PHE
E
11
89.562
28.466
17.517
1.00
18.71
E


ATOM
4481
CD1
PHE
E
11
88.910
27.615
16.626
1.00
21.10
E


ATOM
4482
CD2
PHE
E
11
88.849
28.985
18.595
1.00
18.11
E


ATOM
4483
CE1
PHE
E
11
87.559
27.290
16.807
1.00
22.40
E


ATOM
4484
CE2
PHE
E
11
87.499
28.671
18.789
1.00
15.75
E


ATOM
4485
CZ
PHE
E
11
86.854
27.826
17.898
1.00
21.25
E


ATOM
4486
C
PHE
E
11
90.218
31.069
16.451
1.00
17.10
E


ATOM
4487
O
PHE
E
11
90.461
31.819
17.406
1.00
13.97
E


ATOM
4488
N
LYS
E
12
89.197
31.241
15.622
1.00
16.07
E


ATOM
4489
CA
LYS
E
12
88.266
32.338
15.789
1.00
16.96
E


ATOM
4490
CB
LYS
E
12
88.308
33.246
14.564
1.00
17.05
E


ATOM
4491
CG
LYS
E
12
89.703
33.748
14.200
1.00
17.57
E


ATOM
4492
CD
LYS
E
12
89.663
34.535
12.888
1.00
18.92
E


ATOM
4493
CE
LYS
E
12
91.018
35.136
12.532
1.00
17.07
E


ATOM
4494
NZ
LYS
E
12
90.920
36.063
11.362
1.00
14.26
E


ATOM
4495
C
LYS
E
12
86.856
31.803
15.987
1.00
17.87
E


ATOM
4496
O
LYS
E
12
86.354
31.039
15.165
1.00
16.82
E


ATOM
4497
N
GLY
E
13
86.235
32.195
17.098
1.00
18.19
E


ATOM
4498
CA
GLY
E
13
84.875
31.776
17.391
1.00
19.62
E


ATOM
4499
C
GLY
E
13
83.991
32.939
17.010
1.00
19.93
E


ATOM
4500
O
GLY
E
13
83.539
33.695
17.868
1.00
21.65
E


ATOM
4501
N
MET
E
14
83.728
33.070
15.715
1.00
19.89
E


ATOM
4502
CA
MET
E
14
82.947
34.184
15.197
1.00
20.54
E


ATOM
4503
CB
MET
E
14
83.430
34.490
13.785
1.00
21.02
E


ATOM
4504
CG
MET
E
14
84.937
34.657
13.751
1.00
23.04
E


ATOM
4505
SD
MET
E
14
85.587
35.218
12.190
1.00
25.32
E


ATOM
4506
CE
MET
E
14
85.218
36.938
12.284
1.00
20.32
E


ATOM
4507
C
MET
E
14
81.429
34.078
15.219
1.00
20.83
E


ATOM
4508
O
MET
E
14
80.859
32.999
15.101
1.00
20.77
E


ATOM
4509
N
CYS
E
15
80.789
35.232
15.377
1.00
20.66
E


ATOM
4510
CA
CYS
E
15
79.332
35.336
15.418
1.00
22.09
E


ATOM
4511
C
CYS
E
15
78.882
36.495
14.524
1.00
21.39
E


ATOM
4512
O
CYS
E
15
79.393
37.614
14.644
1.00
19.38
E


ATOM
4513
CB
CYS
E
15
78.841
35.616
16.848
1.00
22.10
E


ATOM
4514
SG
CYS
E
15
78.970
34.281
18.094
1.00
26.75
E


ATOM
4515
N
TYR
E
16
77.931
36.229
13.633
1.00
20.94
E


ATOM
4516
CA
TYR
E
16
77.408
37.270
12.752
1.00
21.23
E


ATOM
4517
CB
TYR
E
16
77.548
36.858
11.287
1.00
18.37
E


ATOM
4518
CG
TYR
E
16
78.972
36.574
10.876
1.00
19.23
E


ATOM
4519
CD1
TYR
E
16
79.576
35.354
11.178
1.00
18.71
E


ATOM
4520
CE1
TYR
E
16
80.875
35.084
10.789
1.00
18.69
E


ATOM
4521
CD2
TYR
E
16
79.715
37.524
10.178
1.00
20.25
E


ATOM
4522
CE2
TYR
E
16
81.022
37.270
9.785
1.00
17.18
E


ATOM
4523
CZ
TYR
E
16
81.595
36.047
10.088
1.00
21.03
E


ATOM
4524
OH
TYR
E
16
82.872
35.775
9.662
1.00
22.99
E


ATOM
4525
C
TYR
E
16
75.938
37.543
13.085
1.00
22.17
E


ATOM
4526
O
TYR
E
16
75.132
36.612
13.199
1.00
21.71
E


ATOM
4527
N
PHE
E
17
75.607
38.825
13.247
1.00
23.05
E


ATOM
4528
CA
PHE
E
17
74.254
39.263
13.591
1.00
23.67
E


ATOM
4529
CB
PHE
E
17
74.261
39.988
14.942
1.00
22.49
E


ATOM
4530
CG
PHE
E
17
74.813
39.172
16.084
1.00
25.10
E


ATOM
4531
CD1
PHE
E
17
74.007
38.270
16.772
1.00
24.22
E


ATOM
4532
CD2
PHE
E
17
76.140
39.318
16.482
1.00
24.67
E


ATOM
4533
CE1
PHE
E
17
74.516
37.526
17.844
1.00
24.68
E


ATOM
4534
CE2
PHE
E
17
76.656
38.579
17.548
1.00
24.45
E


ATOM
4535
CZ
PHE
E
17
75.843
37.684
18.228
1.00
24.13
E


ATOM
4536
C
PHE
E
17
73.673
40.223
12.549
1.00
25.10
E


ATOM
4537
O
PHE
E
17
74.390
41.034
11.971
1.00
24.65
E


ATOM
4538
N
THR
E
18
72.365
40.122
12.333
1.00
27.15
E


ATOM
4539
CA
THR
E
18
71.638
40.983
11.405
1.00
29.69
E


ATOM
4540
CB
THR
E
18
71.609
40.397
9.978
1.00
29.46
E


ATOM
4541
OG1
THR
E
18
72.949
40.252
9.500
1.00
32.31
E


ATOM
4542
CG2
THR
E
18
70.863
41.321
9.032
1.00
28.09
E


ATOM
4543
C
THR
E
18
70.217
41.080
11.950
1.00
31.56
E


ATOM
4544
O
THR
E
18
69.638
40.071
12.355
1.00
32.09
E


ATOM
4545
N
ASN
E
19
69.661
42.290
11.969
1.00
33.38
E


ATOM
4546
CA
ASN
E
19
68.316
42.495
12.497
1.00
35.02
E


ATOM
4547
CB
ASN
E
19
67.279
41.755
11.647
1.00
37.99
E


ATOM
4548
CG
ASN
E
19
66.779
42.587
10.489
1.00
42.21
E


ATOM
4549
OD1
ASN
E
19
66.271
43.695
10.687
1.00
47.70
E


ATOM
4550
ND2
ASN
E
19
66.910
42.063
9.273
1.00
43.13
E


ATOM
4551
C
ASN
E
19
68.264
41.977
13.924
1.00
34.10
E


ATOM
4552
O
ASN
E
19
67.487
41.077
14.233
1.00
34.27
E


ATOM
4553
N
GLY
E
20
69.088
42.553
14.795
1.00
33.50
E


ATOM
4554
CA
GLY
E
20
69.120
42.106
16.175
1.00
33.61
E


ATOM
4555
C
GLY
E
20
69.575
40.663
16.175
1.00
33.98
E


ATOM
4556
O
GLY
E
20
70.580
40.343
15.541
1.00
34.56
E


ATOM
4557
N
THR
E
21
68.847
39.789
16.866
1.00
34.08
E


ATOM
4558
CA
THR
E
21
69.198
38.372
16.897
1.00
35.71
E


ATOM
4559
CB
THR
E
21
69.193
37.809
18.335
1.00
37.69
E


ATOM
4560
OG1
THR
E
21
67.907
38.026
18.930
1.00
39.78
E


ATOM
4561
CG2
THR
E
21
70.268
38.480
19.174
1.00
38.05
E


ATOM
4562
C
THR
E
21
68.251
37.517
16.050
1.00
35.19
E


ATOM
4563
O
THR
E
21
68.092
36.324
16.303
1.00
36.08
E


ATOM
4564
N
GLU
E
22
67.619
38.129
15.052
1.00
34.15
E


ATOM
4565
CA
GLU
E
22
66.705
37.405
14.176
1.00
34.08
E


ATOM
4566
CB
GLU
E
22
65.868
38.388
13.354
1.00
33.12
E


ATOM
4567
CG
GLU
E
22
64.781
39.073
14.164
1.00
33.66
E


ATOM
4568
CD
GLU
E
22
64.173
40.266
13.451
1.00
35.85
E


ATOM
4569
OE1
GLU
E
22
63.865
40.151
12.244
1.00
35.10
E


ATOM
4570
OE2
GLU
E
22
63.995
41.317
14.105
1.00
38.34
E


ATOM
4571
C
GLU
E
22
67.523
36.503
13.265
1.00
33.80
E


ATOM
4572
O
GLU
E
22
67.205
35.329
13.092
1.00
34.50
E


ATOM
4573
N
ARG
E
23
68.574
37.065
12.678
1.00
33.59
E


ATOM
4574
CA
ARG
E
23
69.467
36.298
11.818
1.00
33.75
E


ATOM
4575
CB
ARG
E
23
69.703
36.996
10.470
1.00
36.33
E


ATOM
4576
CG
ARG
E
23
68.599
36.815
9.434
1.00
42.06
E


ATOM
4577
CD
ARG
E
23
67.342
37.577
9.813
1.00
47.83
E


ATOM
4578
NE
ARG
E
23
66.408
37.696
8.695
1.00
51.02
E


ATOM
4579
CZ
ARG
E
23
65.349
38.502
8.690
1.00
52.66
E


ATOM
4580
NH1
ARG
E
23
65.087
39.263
9.747
1.00
50.82
E


ATOM
4581
NH2
ARG
E
23
64.555
38.555
7.626
1.00
53.53
E


ATOM
4582
C
ARG
E
23
70.788
36.177
12.560
1.00
30.98
E


ATOM
4583
O
ARG
E
23
71.465
37.172
12.827
1.00
30.90
E


ATOM
4584
N
VAL
E
24
71.149
34.955
12.909
1.00
28.33
E


ATOM
4585
CA
VAL
E
24
72.394
34.735
13.621
1.00
25.06
E


ATOM
4586
CB
VAL
E
24
72.148
34.500
15.129
1.00
22.98
E


ATOM
4587
CG1
VAL
E
24
73.456
34.106
15.817
1.00
21.05
E


ATOM
4588
CG2
VAL
E
24
71.582
35.762
15.763
1.00
21.04
E


ATOM
4589
C
VAL
E
24
73.144
33.550
13.049
1.00
23.08
E


ATOM
4590
O
VAL
E
24
72.600
32.458
12.914
1.00
24.17
E


ATOM
4591
N
ARG
E
25
74.398
33.778
12.694
1.00
23.02
E


ATOM
4592
CA
ARG
E
25
75.223
32.718
12.156
1.00
23.30
E


ATOM
4593
CB
ARG
E
25
75.511
32.930
10.659
1.00
24.06
E


ATOM
4594
CG
ARG
E
25
76.653
32.044
10.176
1.00
25.99
E


ATOM
4595
CD
ARG
E
25
76.470
31.478
8.774
1.00
28.29
E


ATOM
4596
NE
ARG
E
25
76.468
32.502
7.743
1.00
29.69
E


ATOM
4597
CZ
ARG
E
25
76.786
32.287
6.466
1.00
29.57
E


ATOM
4598
NH1
ARG
E
25
77.145
31.075
6.047
1.00
27.28
E


ATOM
4599
NH2
ARG
E
25
76.733
33.293
5.604
1.00
26.98
E


ATOM
4600
C
ARG
E
25
76.535
32.631
12.916
1.00
22.65
E


ATOM
4601
O
ARG
E
25
77.261
33.620
13.041
1.00
22.47
E


ATOM
4602
N
LEU
E
26
76.828
31.444
13.433
1.00
21.04
E


ATOM
4603
CA
LEU
E
26
78.069
31.227
14.152
1.00
21.94
E


ATOM
4604
CB
LEU
E
26
77.834
30.338
15.383
1.00
21.37
E


ATOM
4605
CG
LEU
E
26
79.054
29.778
16.128
1.00
22.89
E


ATOM
4606
CD1
LEU
E
26
78.723
29.567
17.602
1.00
25.16
E


ATOM
4607
CD2
LEU
E
26
79.483
28.466
15.493
1.00
23.51
E


ATOM
4608
C
LEU
E
26
79.032
30.552
13.193
1.00
21.17
E


ATOM
4609
O
LEU
E
26
78.637
29.674
12.432
1.00
21.77
E


ATOM
4610
N
VAL
E
27
80.285
30.983
13.201
1.00
19.92
E


ATOM
4611
CA
VAL
E
27
81.278
30.358
12.345
1.00
21.31
E


ATOM
4612
CB
VAL
E
27
81.530
31.166
11.039
1.00
20.44
E


ATOM
4613
CG1
VAL
E
27
82.524
30.420
10.156
1.00
21.63
E


ATOM
4614
CG2
VAL
E
27
80.221
31.366
10.275
1.00
20.48
E


ATOM
4615
C
VAL
E
27
82.581
30.231
13.112
1.00
21.74
E


ATOM
4616
O
VAL
E
27
83.189
31.228
13.487
1.00
24.11
E


ATOM
4617
N
SER
E
28
82.994
29.001
13.383
1.00
20.88
E


ATOM
4618
CA
SER
E
28
84.249
28.799
14.084
1.00
21.53
E


ATOM
4619
CB
SER
E
28
84.113
27.702
15.152
1.00
20.62
E


ATOM
4620
OG
SER
E
28
83.693
26.475
14.598
1.00
29.22
E


ATOM
4621
C
SER
E
28
85.274
28.433
13.006
1.00
21.41
E


ATOM
4622
O
SER
E
28
84.992
27.631
12.105
1.00
19.11
E


ATOM
4623
N
ARG
E
29
86.450
29.051
13.090
1.00
18.23
E


ATOM
4624
CA
ARG
E
29
87.496
28.838
12.105
1.00
18.45
E


ATOM
4625
CB
ARG
E
29
87.701
30.124
11.287
1.00
16.91
E


ATOM
4626
CG
ARG
E
29
86.433
30.817
10.810
1.00
17.70
E


ATOM
4627
CD
ARG
E
29
86.791
32.117
10.109
1.00
18.98
E


ATOM
4628
NE
ARG
E
29
85.631
32.902
9.705
1.00
20.82
E


ATOM
4629
CZ
ARG
E
29
84.939
32.704
8.586
1.00
22.76
E


ATOM
4630
NH1
ARG
E
29
85.285
31.739
7.743
1.00
21.05
E


ATOM
4631
NH2
ARG
E
29
83.904
33.482
8.309
1.00
20.13
E


ATOM
4632
C
ARG
E
29
88.842
28.435
12.710
1.00
18.44
E


ATOM
4633
O
ARG
E
29
89.401
29.171
13.520
1.00
19.35
E


ATOM
4634
N
SER
E
30
89.351
27.269
12.315
1.00
18.98
E


ATOM
4635
CA
SER
E
30
90.657
26.788
12.774
1.00
21.70
E


ATOM
4636
CB
SER
E
30
90.619
25.284
13.028
1.00
22.10
E


ATOM
4637
OG
SER
E
30
89.718
24.969
14.072
1.00
27.24
E


ATOM
4638
C
SER
E
30
91.637
27.119
11.639
1.00
23.03
E


ATOM
4639
O
SER
E
30
91.509
26.604
10.528
1.00
23.56
E


ATOM
4640
N
ILE
E
31
92.611
27.978
11.927
1.00
23.05
E


ATOM
4641
CA
ILE
E
31
93.560
28.439
10.923
1.00
22.24
E


ATOM
4642
CB
ILE
E
31
93.563
29.997
10.856
1.00
22.84
E


ATOM
4643
CG2
ILE
E
31
94.163
30.470
9.545
1.00
19.19
E


ATOM
4644
CG1
ILE
E
31
92.143
30.546
11.043
1.00
24.76
E


ATOM
4645
CD1
ILE
E
31
91.144
30.032
10.047
1.00
29.25
E


ATOM
4646
C
ILE
E
31
95.013
28.014
11.134
1.00
24.53
E


ATOM
4647
O
ILE
E
31
95.566
28.187
12.225
1.00
22.94
E


ATOM
4648
N
TYR
E
32
95.625
27.468
10.081
1.00
24.41
E


ATOM
4649
CA
TYR
E
32
97.030
27.089
10.120
1.00
24.27
E


ATOM
4650
CB
TYR
E
32
97.277
25.755
9.417
1.00
26.61
E


ATOM
4651
CG
TYR
E
32
98.733
25.338
9.444
1.00
29.24
E


ATOM
4652
CD1
TYR
E
32
99.423
25.231
10.649
1.00
30.69
E


ATOM
4653
CE1
TYR
E
32
100.770
24.880
10.683
1.00
32.83
E


ATOM
4654
CD2
TYR
E
32
99.426
25.078
8.267
1.00
31.46
E


ATOM
4655
CE2
TYR
E
32
100.774
24.721
8.288
1.00
32.58
E


ATOM
4656
CZ
TYR
E
32
101.438
24.625
9.497
1.00
32.80
E


ATOM
4657
OH
TYR
E
32
102.768
24.280
9.522
1.00
33.44
E


ATOM
4658
C
TYR
E
32
97.700
28.225
9.353
1.00
24.83
E


ATOM
4659
O
TYR
E
32
97.444
28.415
8.164
1.00
25.49
E


ATOM
4660
N
ASN
E
33
98.543
28.985
10.045
1.00
24.28
E


ATOM
4661
CA
ASN
E
33
99.202
30.146
9.461
1.00
24.25
E


ATOM
4662
CB
ASN
E
33
100.144
29.740
8.324
1.00
23.93
E


ATOM
4663
CG
ASN
E
33
101.379
29.014
8.834
1.00
25.26
E


ATOM
4664
OD1
ASN
E
33
102.003
29.439
9.808
1.00
26.40
E


ATOM
4665
ND2
ASN
E
33
101.737
27.918
8.181
1.00
25.47
E


ATOM
4666
C
ASN
E
33
98.114
31.099
8.980
1.00
24.88
E


ATOM
4667
O
ASN
E
33
97.494
31.780
9.799
1.00
25.88
E


ATOM
4668
N
ARG
E
34
97.864
31.163
7.677
1.00
24.52
E


ATOM
4669
CA
ARG
E
34
96.815
32.055
7.194
1.00
26.32
E


ATOM
4670
CB
ARG
E
34
97.385
33.175
6.317
1.00
26.61
E


ATOM
4671
CG
ARG
E
34
97.999
34.346
7.072
1.00
26.37
E


ATOM
4672
CD
ARG
E
34
97.776
35.646
6.304
1.00
28.18
E


ATOM
4673
NE
ARG
E
34
97.886
35.429
4.865
1.00
31.86
E


ATOM
4674
CZ
ARG
E
34
97.607
36.332
3.931
1.00
33.42
E


ATOM
4675
NH1
ARG
E
34
97.197
37.550
4.265
1.00
35.40
E


ATOM
4676
NH2
ARG
E
34
97.722
36.003
2.653
1.00
35.29
E


ATOM
4677
C
ARG
E
34
95.728
31.333
6.417
1.00
26.98
E


ATOM
4678
O
ARG
E
34
94.896
31.968
5.763
1.00
28.88
E


ATOM
4679
N
GLU
E
35
95.719
30.010
6.481
1.00
26.13
E


ATOM
4680
CA
GLU
E
35
94.698
29.279
5.759
1.00
27.02
E


ATOM
4681
CB
GLU
E
35
95.350
28.359
4.720
1.00
31.96
E


ATOM
4682
CG
GLU
E
35
96.284
27.301
5.278
1.00
38.52
E


ATOM
4683
CD
GLU
E
35
97.116
26.633
4.192
1.00
42.24
E


ATOM
4684
OE1
GLU
E
35
98.180
27.187
3.832
1.00
44.86
E


ATOM
4685
OE2
GLU
E
35
96.699
25.565
3.690
1.00
43.70
E


ATOM
4686
C
GLU
E
35
93.754
28.498
6.671
1.00
25.31
E


ATOM
4687
O
GLU
E
35
94.175
27.709
7.522
1.00
22.18
E


ATOM
4688
N
GLU
E
36
92.464
28.756
6.498
1.00
24.46
E


ATOM
4689
CA
GLU
E
36
91.438
28.085
7.272
1.00
24.13
E


ATOM
4690
CB
GLU
E
36
90.085
28.731
7.001
1.00
24.37
E


ATOM
4691
CG
GLU
E
36
88.975
28.295
7.928
1.00
25.26
E


ATOM
4692
CD
GLU
E
36
87.669
28.991
7.604
1.00
26.01
E


ATOM
4693
OE1
GLU
E
36
87.672
29.847
6.694
1.00
27.25
E


ATOM
4694
OE2
GLU
E
36
86.646
28.689
8.253
1.00
27.12
E


ATOM
4695
C
GLU
E
36
91.413
26.630
6.826
1.00
23.40
E


ATOM
4696
O
GLU
E
36
91.252
26.347
5.645
1.00
23.72
E


ATOM
4697
N
ILE
E
37
91.576
25.707
7.767
1.00
23.97
E


ATOM
4698
CA
ILE
E
37
91.579
24.294
7.419
1.00
24.33
E


ATOM
4699
CB
ILE
E
37
92.818
23.578
8.019
1.00
24.98
E


ATOM
4700
CG2
ILE
E
37
94.096
24.255
7.532
1.00
24.26
E


ATOM
4701
CG1
ILE
E
37
92.771
23.616
9.544
1.00
25.10
E


ATOM
4702
CD1
ILE
E
37
93.822
22.742
10.204
1.00
26.49
E


ATOM
4703
C
ILE
E
37
90.301
23.555
7.836
1.00
23.49
E


ATOM
4704
O
ILE
E
37
89.871
22.627
7.162
1.00
23.62
E


ATOM
4705
N
VAL
E
38
89.690
23.975
8.936
1.00
25.16
E


ATOM
4706
CA
VAL
E
38
88.465
23.342
9.415
1.00
25.85
E


ATOM
4707
CB
VAL
E
38
88.715
22.489
10.667
1.00
26.44
E


ATOM
4708
CG1
VAL
E
38
87.516
21.610
10.932
1.00
27.10
E


ATOM
4709
CG2
VAL
E
38
89.980
21.671
10.495
1.00
29.59
E


ATOM
4710
C
VAL
E
38
87.481
24.428
9.792
1.00
24.45
E


ATOM
4711
O
VAL
E
38
87.885
25.471
10.288
1.00
24.36
E


ATOM
4712
N
ARG
E
39
86.193
24.168
9.594
1.00
24.90
E


ATOM
4713
CA
ARG
E
39
85.175
25.161
9.904
1.00
23.66
E


ATOM
4714
CB
ARG
E
39
84.975
26.055
8.678
1.00
25.55
E


ATOM
4715
CG
ARG
E
39
83.956
27.174
8.857
1.00
29.11
E


ATOM
4716
CD
ARG
E
39
83.514
27.755
7.515
1.00
29.37
E


ATOM
4717
NE
ARG
E
39
84.626
28.289
6.739
1.00
29.70
E


ATOM
4718
CZ
ARG
E
39
84.505
28.798
5.516
1.00
31.37
E


ATOM
4719
NH1
ARG
E
39
83.314
28.842
4.930
1.00
33.54
E


ATOM
4720
NH2
ARG
E
39
85.572
29.266
4.879
1.00
27.78
E


ATOM
4721
C
ARG
E
39
83.813
24.594
10.328
1.00
23.51
E


ATOM
4722
O
ARG
E
39
83.385
23.539
9.853
1.00
23.83
E


ATOM
4723
N
PHE
E
40
83.147
25.295
11.242
1.00
22.04
E


ATOM
4724
CA
PHE
E
40
81.799
24.918
11.655
1.00
21.92
E


ATOM
4725
CB
PHE
E
40
81.682
24.551
13.137
1.00
21.36
E


ATOM
4726
CG
PHE
E
40
80.296
24.088
13.514
1.00
17.04
E


ATOM
4727
CD1
PHE
E
40
79.944
22.748
13.407
1.00
19.76
E


ATOM
4728
CD2
PHE
E
40
79.315
25.004
13.875
1.00
16.82
E


ATOM
4729
CE1
PHE
E
40
78.628
22.324
13.649
1.00
17.84
E


ATOM
4730
CE2
PHE
E
40
78.001
24.594
14.119
1.00
18.10
E


ATOM
4731
CZ
PHE
E
40
77.661
23.248
14.003
1.00
16.61
E


ATOM
4732
C
PHE
E
40
80.938
26.148
11.395
1.00
21.77
E


ATOM
4733
O
PHE
E
40
81.064
27.167
12.071
1.00
20.81
E


ATOM
4734
N
ASP
E
41
80.067
26.033
10.404
1.00
21.82
E


ATOM
4735
CA
ASP
E
41
79.181
27.110
9.995
1.00
21.76
E


ATOM
4736
CB
ASP
E
41
79.190
27.182
8.470
1.00
22.62
E


ATOM
4737
CG
ASP
E
41
78.492
28.400
7.929
1.00
23.09
E


ATOM
4738
OD1
ASP
E
41
77.507
28.864
8.546
1.00
22.57
E


ATOM
4739
OD2
ASP
E
41
78.929
28.881
6.861
1.00
25.40
E


ATOM
4740
C
ASP
E
41
77.801
26.713
10.493
1.00
21.43
E


ATOM
4741
O
ASP
E
41
77.277
25.672
10.085
1.00
22.83
E


ATOM
4742
N
SER
E
42
77.210
27.520
11.369
1.00
19.04
E


ATOM
4743
CA
SER
E
42
75.896
27.173
11.895
1.00
20.39
E


ATOM
4744
CB
SER
E
42
75.399
28.220
12.907
1.00
19.13
E


ATOM
4745
OG
SER
E
42
75.271
29.505
12.323
1.00
24.30
E


ATOM
4746
C
SER
E
42
74.891
27.000
10.762
1.00
20.23
E


ATOM
4747
O
SER
E
42
73.916
26.267
10.910
1.00
18.97
E


ATOM
4748
N
ASP
E
43
75.145
27.660
9.631
1.00
21.77
E


ATOM
4749
CA
ASP
E
43
74.261
27.556
8.470
1.00
24.99
E


ATOM
4750
CB
ASP
E
43
74.561
28.651
7.439
1.00
26.10
E


ATOM
4751
CG
ASP
E
43
73.819
29.947
7.727
1.00
28.71
E


ATOM
4752
OD1
ASP
E
43
73.078
30.013
8.737
1.00
28.83
E


ATOM
4753
OD2
ASP
E
43
73.976
30.902
6.939
1.00
31.35
E


ATOM
4754
C
ASP
E
43
74.378
26.193
7.809
1.00
25.68
E


ATOM
4755
O
ASP
E
43
73.424
25.727
7.190
1.00
28.27
E


ATOM
4756
N
VAL
E
44
75.544
25.558
7.937
1.00
25.47
E


ATOM
4757
CA
VAL
E
44
75.764
24.229
1.362
1.00
23.51
E


ATOM
4758
CB
VAL
E
44
77.251
24.007
6.964
1.00
24.39
E


ATOM
4759
CG1
VAL
E
44
77.456
22.579
6.491
1.00
19.52
E


ATOM
4760
CG2
VAL
E
44
77.655
24.984
5.867
1.00
23.79
E


ATOM
4761
C
VAL
E
44
75.356
23.154
8.373
1.00
23.25
E


ATOM
4762
O
VAL
E
44
74.774
22.136
8.005
1.00
22.01
E


ATOM
4763
N
GLY
E
45
75.683
23.370
9.644
1.00
22.52
E


ATOM
4764
CA
GLY
E
45
75.292
22.411
10.664
1.00
21.82
E


ATOM
4765
C
GLY
E
45
76.275
21.311
11.001
1.00
22.07
E


ATOM
4766
O
GLY
E
45
75.982
20.442
11.818
1.00
22.49
E


ATOM
4767
N
GLU
E
46
77.439
21.317
10.373
1.00
22.18
E


ATOM
4768
CA
GLU
E
46
78.421
20.295
10.691
1.00
23.77
E


ATOM
4769
CB
GLU
E
46
78.147
19.017
9.891
1.00
26.29
E


ATOM
4770
CG
GLU
E
46
78.455
19.112
8.411
1.00
28.23
E


ATOM
4771
CD
GLU
E
46
78.214
17.795
7.677
1.00
32.67
E


ATOM
4772
OE1
GLU
E
46
78.575
17.706
6.482
1.00
33.19
E


ATOM
4773
OE2
GLU
E
46
77.661
16.855
8.290
1.00
33.19
E


ATOM
4774
C
GLU
E
46
79.807
20.839
10.383
1.00
23.15
E


ATOM
4775
O
GLU
E
46
79.943
21.880
9.747
1.00
23.06
E


ATOM
4776
N
PHE
E
47
80.835
20.153
10.857
1.00
21.79
E


ATOM
4777
CA
PHE
E
47
82.192
20.595
10.599
1.00
22.22
E


ATOM
4778
CB
PHE
E
47
83.175
19.864
11.515
1.00
22.30
E


ATOM
4779
CG
PHE
E
47
83.058
20.249
12.968
1.00
22.20
E


ATOM
4780
CD1
PHE
E
47
83.867
21.246
13.508
1.00
19.80
E


ATOM
4781
CD2
PHE
E
47
82.151
19.598
13.802
1.00
23.06
E


ATOM
4782
CE1
PHE
E
47
83.781
21.585
14.858
1.00
18.93
E


ATOM
4783
CE2
PHE
E
47
82.055
19.931
15.157
1.00
22.63
E


ATOM
4784
CZ
PHE
E
47
82.872
20.925
15.684
1.00
20.81
E


ATOM
4785
C
PHE
E
47
82.513
20.278
9.147
1.00
24.14
E


ATOM
4786
O
PHE
E
47
82.064
19.258
8.609
1.00
23.25
E


ATOM
4787
N
ARG
E
48
83.272
21.164
8.511
1.00
22.66
E


ATOM
4788
CA
ARG
E
48
83.672
20.966
7.131
1.00
23.86
E


ATOM
4789
CB
ARG
E
48
82.801
21.795
6.181
1.00
23.48
E


ATOM
4790
CG
ARG
E
48
81.339
21.375
6.091
1.00
25.01
E


ATOM
4791
CD
ARG
E
48
81.155
20.061
5.348
1.00
25.08
E


ATOM
4792
NE
ARG
E
48
79.747
19.811
5.044
1.00
27.17
E


ATOM
4793
CZ
ARG
E
48
79.038
20.515
4.164
1.00
29.38
E


ATOM
4794
NH1
ARG
E
48
79.604
21.513
3.498
1.00
31.36
E


ATOM
4795
NH2
ARG
E
48
77.763
20.226
3.946
1.00
30.50
E


ATOM
4796
C
ARG
E
48
85.119
21.395
6.972
1.00
24.13
E


ATOM
4797
O
ARG
E
48
85.507
22.480
7.416
1.00
25.58
E


ATOM
4798
N
ALA
E
49
85.924
20.537
6.360
1.00
22.26
E


ATOM
4799
CA
ALA
E
49
87.316
20.875
6.122
1.00
23.11
E


ATOM
4800
CB
ALA
E
49
88.102
19.630
5.711
1.00
22.46
E


ATOM
4801
C
ALA
E
49
87.290
21.875
4.980
1.00
22.04
E


ATOM
4802
O
ALA
E
49
86.507
21.722
4.048
1.00
23.16
E


ATOM
4803
N
VAL
E
50
88.108
22.916
5.050
1.00
23.56
E


ATOM
4804
CA
VAL
E
50
88.135
23.875
3.953
1.00
23.79
E


ATOM
4805
CB
VAL
E
50
88.059
25.360
4.478
1.00
24.14
E


ATOM
4806
CG1
VAL
E
50
88.341
25.408
5.959
1.00
24.71
E


ATOM
4807
CG2
VAL
E
50
89.010
26.268
3.704
1.00
22.47
E


ATOM
4808
C
VAL
E
50
89.374
23.578
3.098
1.00
23.50
E


ATOM
4809
O
VAL
E
50
89.485
24.041
1.963
1.00
24.92
E


ATOM
4810
N
THR
E
51
90.281
22.770
3.650
1.00
24.49
E


ATOM
4811
CA
THR
E
51
91.492
22.317
2.951
1.00
25.50
E


ATOM
4812
CB
THR
E
51
92.742
23.198
3.234
1.00
25.69
E


ATOM
4813
OG1
THR
E
51
93.171
23.007
4.586
1.00
27.89
E


ATOM
4814
CG2
THR
E
51
92.443
24.670
2.985
1.00
23.29
E


ATOM
4815
C
THR
E
51
91.817
20.895
3.420
1.00
26.59
E


ATOM
4816
O
THR
E
51
91.387
20.477
4.496
1.00
27.35
E


ATOM
4817
N
LEU
E
52
92.576
20.154
2.617
1.00
28.03
E


ATOM
4818
CA
LEU
E
52
92.949
18.783
2.956
1.00
28.49
E


ATOM
4819
CB
LEU
E
52
93.995
18.259
1.969
1.00
30.33
E


ATOM
4820
CG
LEU
E
52
93.536
17.892
0.556
1.00
34.17
E


ATOM
4821
CD1
LEU
E
52
94.749
17.628
−0.334
1.00
34.41
E


ATOM
4822
CD2
LEU
E
52
92.644
16.668
0.620
1.00
34.30
E


ATOM
4823
C
LEU
E
52
93.494
18.645
4.374
1.00
28.20
E


ATOM
4824
O
LEU
E
52
93.304
17.624
5.027
1.00
29.17
E


ATOM
4825
N
LEU
E
53
94.179
19.677
4.839
1.00
28.30
E


ATOM
4826
CA
LEU
E
53
94.766
19.682
6.171
1.00
28.75
E


ATOM
4827
CB
LEU
E
53
95.490
21.015
6.387
1.00
30.37
E


ATOM
4828
CG
LEU
E
53
96.939
21.010
6.882
1.00
32.74
E


ATOM
4829
CD1
LEU
E
53
97.777
20.085
6.008
1.00
31.60
E


ATOM
4830
CD2
LEU
E
53
97.498
22.444
6.854
1.00
30.06
E


ATOM
4831
C
LEU
E
53
93.727
19.464
7.278
1.00
27.82
E


ATOM
4832
O
LEU
E
53
94.027
18.858
8.312
1.00
25.47
E


ATOM
4833
N
GLY
E
54
92.508
19.957
7.059
1.00
27.39
E


ATOM
4834
CA
GLY
E
54
91.466
19.813
8.062
1.00
26.92
E


ATOM
4835
C
GLY
E
54
90.569
18.589
7.949
1.00
28.33
E


ATOM
4836
O
GLY
E
54
89.725
18.348
8.813
1.00
28.02
E


ATOM
4837
N
LEU
E
55
90.755
17.801
6.898
1.00
29.28
E


ATOM
4838
CA
LEU
E
55
89.930
16.620
6.675
1.00
31.43
E


ATOM
4839
CB
LEU
E
55
90.410
15.885
5.419
1.00
32.39
E


ATOM
4840
CG
LEU
E
55
89.426
14.934
4.731
1.00
35.68
E


ATOM
4841
CD1
LEU
E
55
88.086
15.627
4.504
1.00
34.41
E


ATOM
4842
CD2
LEU
E
55
90.018
14.473
3.406
1.00
35.99
E


ATOM
4843
C
LEU
E
55
89.865
15.659
7.867
1.00
32.09
E


ATOM
4844
O
LEU
E
55
88.778
15.294
8.312
1.00
32.58
E


ATOM
4845
N
PRO
E
56
91.023
15.235
8.402
1.00
31.67
E


ATOM
4846
CD
PRO
E
56
92.411
15.520
8.000
1.00
31.37
E


ATOM
4847
CA
PRO
E
56
90.986
14.316
9.546
1.00
31.17
E


ATOM
4848
CB
PRO
E
56
92.459
14.163
9.919
1.00
30.50
E


ATOM
4849
CG
PRO
E
56
93.161
14.352
8.611
1.00
31.19
E


ATOM
4850
C
PRO
E
56
90.158
14.865
10.708
1.00
31.43
E


ATOM
4851
O
PRO
E
56
89.250
14.195
11.205
1.00
32.17
E


ATOM
4852
N
ALA
E
57
90.473
16.086
11.138
1.00
29.94
E


ATOM
4853
CA
ALA
E
57
89.748
16.709
12.244
1.00
28.45
E


ATOM
4854
CB
ALA
E
57
90.314
18.098
12.532
1.00
27.09
E


ATOM
4855
C
ALA
E
57
88.249
16.807
11.960
1.00
27.57
E


ATOM
4856
O
ALA
E
57
87.436
16.466
12.812
1.00
26.57
E


ATOM
4857
N
ALA
E
58
87.899
17.270
10.761
1.00
27.40
E


ATOM
4858
CA
ALA
E
58
86.505
17.422
10.349
1.00
28.85
E


ATOM
4859
CB
ALA
E
58
86.439
18.007
8.939
1.00
27.80
E


ATOM
4860
C
ALA
E
58
85.726
16.110
10.406
1.00
30.37
E


ATOM
4861
O
ALA
E
58
84.624
16.058
10.954
1.00
29.58
E


ATOM
4862
N
GLU
E
59
86.292
15.052
9.837
1.00
32.24
E


ATOM
4863
CA
GLU
E
59
85.632
13.750
9.845
1.00
35.22
E


ATOM
4864
CB
GLU
E
59
86.441
12.724
9.049
1.00
36.81
E


ATOM
4865
CG
GLU
E
59
86.392
12.917
7.549
1.00
40.89
E


ATOM
4866
CD
GLU
E
59
87.057
11.775
6.805
1.00
44.28
E


ATOM
4867
OE1
GLU
E
59
88.291
11.597
6.955
1.00
45.76
E


ATOM
4868
OE2
GLU
E
59
86.342
11.052
6.075
1.00
45.12
E


ATOM
4869
C
GLU
E
59
85.441
13.231
11.260
1.00
34.08
E


ATOM
4870
O
GLU
E
59
84.384
12.697
11.596
1.00
34.48
E


ATOM
4871
N
TYR
E
60
86.466
13.387
12.090
1.00
33.21
E


ATOM
4872
CA
TYR
E
60
86.390
12.919
13.463
1.00
32.36
E


ATOM
4873
CB
TYR
E
60
87.724
13.101
14.177
1.00
33.78
E


ATOM
4874
CG
TYR
E
60
87.657
12.617
15.594
1.00
35.68
E


ATOM
4875
CD1
TYR
E
60
87.543
11.259
15.872
1.00
37.48
E


ATOM
4876
CE1
TYR
E
60
87.394
10.802
17.173
1.00
41.14
E


ATOM
4877
CD2
TYR
E
60
87.628
13.514
16.655
1.00
37.26
E


ATOM
4878
CE2
TYR
E
60
87.478
13.073
17.965
1.00
40.26
E


ATOM
4879
CZ
TYR
E
60
87.360
11.714
18.218
1.00
41.88
E


ATOM
4880
OH
TYR
E
60
87.198
11.262
19.508
1.00
44.51
E


ATOM
4881
C
TYR
E
60
85.312
13.623
14.275
1.00
32.30
E


ATOM
4882
O
TYR
E
60
84.430
12.976
14.839
1.00
30.56
E


ATOM
4883
N
TRP
E
61
85.391
14.950
14.347
1.00
31.42
E


ATOM
4884
CA
TRP
E
61
84.412
15.715
15.112
1.00
31.35
E


ATOM
4885
CB
TRP
E
61
84.744
17.219
15.071
1.00
32.78
E


ATOM
4886
CG
TRP
E
61
86.051
17.584
15.748
1.00
35.14
E


ATOM
4887
CD2
TRP
E
61
86.909
18.687
15.425
1.00
37.07
E


ATOM
4888
CE2
TRP
E
61
87.994
18.655
16.331
1.00
37.15
E


ATOM
4889
CE3
TRP
E
61
86.864
19.706
14.458
1.00
39.50
E


ATOM
4890
CD1
TRP
E
61
86.635
16.947
16.809
1.00
35.82
E


ATOM
4891
NE1
TRP
E
61
87.800
17.582
17.163
1.00
35.66
E


ATOM
4892
CZ2
TRP
E
61
89.034
19.602
16.300
1.00
38.95
E


ATOM
4893
CZ3
TRP
E
61
87.902
20.656
14.427
1.00
41.16
E


ATOM
4894
CH2
TRP
E
61
88.971
20.591
15.346
1.00
40.81
E


ATOM
4895
C
TRP
E
61
82.968
15.472
14.653
1.00
29.29
E


ATOM
4896
O
TRP
E
61
82.045
15.563
15.458
1.00
29.20
E


ATOM
4897
N
ASN
E
62
82.772
15.162
13.373
1.00
27.86
E


ATOM
4898
CA
ASN
E
62
81.428
14.902
12.853
1.00
29.09
E


ATOM
4899
CB
ASN
E
62
81.379
15.051
11.331
1.00
29.42
E


ATOM
4900
CG
ASN
E
62
81.241
16.492
10.893
1.00
31.22
E


ATOM
4901
OD1
ASN
E
62
80.563
17.288
11.545
1.00
29.56
E


ATOM
4902
ND2
ASN
E
62
81.870
16.834
9.772
1.00
31.73
E


ATOM
4903
C
ASN
E
62
80.906
13.519
13.220
1.00
28.26
E


ATOM
4904
O
ASN
E
62
79.716
13.242
13.086
1.00
27.48
E


ATOM
4905
N
SER
E
63
81.795
12.647
13.672
1.00
27.47
E


ATOM
4906
CA
SER
E
63
81.381
11.311
14.056
1.00
29.39
E


ATOM
4907
CB
SER
E
63
82.511
10.310
13.803
1.00
28.56
E


ATOM
4908
OG
SER
E
63
83.607
10.545
14.671
1.00
32.72
E


ATOM
4909
C
SER
E
63
80.987
11.310
15.534
1.00
30.11
E


ATOM
4910
O
SER
E
63
80.515
10.297
16.055
1.00
31.52
E


ATOM
4911
N
GLN
E
64
81.173
12.453
16.196
1.00
28.86
E


ATOM
4912
CA
GLN
E
64
80.834
12.604
17.612
1.00
28.28
E


ATOM
4913
CB
GLN
E
64
81.929
13.379
18.350
1.00
29.50
E


ATOM
4914
CG
GLN
E
64
83.330
12.787
18.266
1.00
29.72
E


ATOM
4915
CD
GLN
E
64
83.418
11.412
18.888
1.00
32.69
E


ATOM
4916
OE1
GLN
E
64
83.055
10.405
18.267
1.00
35.22
E


ATOM
4917
NE2
GLN
E
64
83.887
11.358
20.128
1.00
31.92
E


ATOM
4918
C
GLN
E
64
79.522
13.366
17.783
1.00
28.42
E


ATOM
4919
O
GLN
E
64
79.525
14.599
17.800
1.00
27.68
E


ATOM
4920
N
LYS
E
65
78.410
12.648
17.926
1.00
27.17
E


ATOM
4921
CA
LYS
E
65
77.111
13.300
18.097
1.00
29.82
E


ATOM
4922
CB
LYS
E
65
75.994
12.258
18.253
1.00
31.43
E


ATOM
4923
CG
LYS
E
65
75.479
11.692
16.936
1.00
37.61
E


ATOM
4924
CD
LYS
E
65
74.801
12.766
16.072
1.00
41.12
E


ATOM
4925
CE
LYS
E
65
73.489
13.267
16.696
1.00
44.25
E


ATOM
4926
NZ
LYS
E
65
72.832
14.322
15.861
1.00
44.10
E


ATOM
4927
C
LYS
E
65
77.067
14.273
19.278
1.00
28.07
E


ATOM
4928
O
LYS
E
65
76.406
15.308
19.211
1.00
27.46
E


ATOM
4929
N
ASP
E
66
77.758
13.938
20.361
1.00
27.40
E


ATOM
4930
CA
ASP
E
66
77.783
14.809
21.532
1.00
26.85
E


ATOM
4931
CB
ASP
E
66
78.566
14.142
22.670
1.00
26.10
E


ATOM
4932
CG
ASP
E
66
79.899
13.576
22.212
1.00
29.25
E


ATOM
4933
OD1
ASP
E
66
79.915
12.836
21.205
1.00
28.95
E


ATOM
4934
OD2
ASP
E
66
80.929
13.858
22.864
1.00
31.03
E


ATOM
4935
C
ASP
E
66
78.390
16.174
21.193
1.00
26.21
E


ATOM
4936
O
ASP
E
66
77.844
17.215
21.559
1.00
26.58
E


ATOM
4937
N
ILE
E
67
79.510
16.170
20.478
1.00
26.25
E


ATOM
4938
CA
ILE
E
67
80.164
17.414
20.100
1.00
25.76
E


ATOM
4939
CB
ILE
E
67
81.551
17.153
19.477
1.00
27.31
E


ATOM
4940
CG2
ILE
E
67
82.261
18.467
19.210
1.00
25.90
E


ATOM
4941
CG1
ILE
E
67
82.396
16.304
20.429
1.00
28.85
E


ATOM
4942
CD1
ILE
E
67
82.494
16.871
21.844
1.00
32.35
E


ATOM
4943
C
ILE
E
67
79.307
18.189
19.108
1.00
25.95
E


ATOM
4944
O
ILE
E
67
79.125
19.392
19.255
1.00
26.97
E


ATOM
4945
N
LEU
E
68
78.775
17.504
18.100
1.00
26.05
E


ATOM
4946
CA
LEU
E
68
77.927
18.172
17.113
1.00
26.36
E


ATOM
4947
CB
LEU
E
68
77.382
17.169
16.094
1.00
26.91
E


ATOM
4948
CG
LEU
E
68
78.154
16.987
14.790
1.00
27.01
E


ATOM
4949
CD1
LEU
E
68
77.389
16.002
13.913
1.00
26.26
E


ATOM
4950
CD2
LEU
E
68
78.311
18.342
14.076
1.00
24.04
E


ATOM
4951
C
LEU
E
68
76.760
18.870
17.792
1.00
26.03
E


ATOM
4952
O
LEU
E
68
76.433
20.011
17.465
1.00
25.76
E


ATOM
4953
N
GLU
E
69
76.134
18.175
18.737
1.00
27.50
E


ATOM
4954
CA
GLU
E
69
75.000
18.726
19.471
1.00
30.38
E


ATOM
4955
CB
GLU
E
69
74.481
17.720
20.508
1.00
34.06
E


ATOM
4956
CG
GLU
E
69
73.426
16.742
19.989
1.00
40.55
E


ATOM
4957
CD
GLU
E
69
72.211
17.444
19.392
1.00
44.43
E


ATOM
4958
OE1
GLU
E
69
71.802
18.505
19.922
1.00
43.73
E


ATOM
4959
OE2
GLU
E
69
71.656
16.926
18.397
1.00
48.15
E


ATOM
4960
C
GLU
E
69
75.335
20.034
20.178
1.00
29.17
E


ATOM
4961
O
GLU
E
69
74.587
21.009
20.071
1.00
29.71
E


ATOM
4962
N
ARG
E
70
76.453
20.059
20.899
1.00
26.65
E


ATOM
4963
CA
ARG
E
70
76.844
21.262
21.620
1.00
25.51
E


ATOM
4964
CB
ARG
E
70
78.001
20.965
22.572
1.00
27.14
E


ATOM
4965
CG
ARG
E
70
77.711
19.855
23.563
1.00
31.22
E


ATOM
4966
CD
ARG
E
70
78.637
19.934
24.769
1.00
35.11
E


ATOM
4967
NE
ARG
E
70
78.758
18.647
25.440
1.00
39.19
E


ATOM
4968
CZ
ARG
E
70
79.456
17.628
24.956
1.00
41.08
E


ATOM
4969
NH1
ARG
E
70
80.096
17.752
23.802
1.00
45.32
E


ATOM
4970
NH2
ARG
E
70
79.511
16.486
25.618
1.00
44.01
E


ATOM
4971
C
ARG
E
70
77.230
22.395
20.677
1.00
24.57
E


ATOM
4972
O
ARG
E
70
76.927
23.557
20.941
1.00
21.44
E


ATOM
4973
N
LYS
E
71
77.897
22.057
19.576
1.00
24.56
E


ATOM
4974
CA
LYS
E
71
78.309
23.071
18.612
1.00
24.08
E


ATOM
4975
CB
LYS
E
71
79.202
22.452
17.534
1.00
25.39
E


ATOM
4976
CG
LYS
E
71
80.100
23.474
16.852
1.00
29.73
E


ATOM
4977
CD
LYS
E
71
81.067
24.095
17.862
1.00
30.94
E


ATOM
4978
CE
LYS
E
71
81.905
25.205
17.256
1.00
31.82
E


ATOM
4979
NZ
LYS
E
71
82.774
25.849
18.290
1.00
33.45
E


ATOM
4980
C
LYS
E
71
77.087
23.732
17.960
1.00
22.42
E


ATOM
4981
O
LYS
E
71
77.045
24.951
17.780
1.00
18.65
E


ATOM
4982
N
ARG
E
72
76.092
22.919
17.620
1.00
22.31
E


ATOM
4983
CA
ARG
E
72
74.867
23.419
17.002
1.00
21.44
E


ATOM
4984
CB
ARG
E
72
73.984
22.250
16.578
1.00
19.93
E


ATOM
4985
CG
ARG
E
72
74.534
21.497
15.407
1.00
21.45
E


ATOM
4986
CD
ARG
E
72
73.779
20.223
15.141
1.00
23.34
E


ATOM
4987
NE
ARG
E
72
74.211
19.643
13.877
1.00
24.99
E


ATOM
4988
CZ
ARG
E
72
74.028
18.377
13.522
1.00
27.42
E


ATOM
4989
NH1
ARG
E
72
73.411
17.533
14.344
1.00
25.90
E


ATOM
4990
NH2
ARG
E
72
74.475
17.955
12.341
1.00
25.41
E


ATOM
4991
C
ARG
E
72
74.093
24.315
17.961
1.00
21.34
E


ATOM
4992
O
ARG
E
72
73.336
25.182
17.535
1.00
23.67
E


ATOM
4993
N
ALA
E
73
74.293
24.105
19.256
1.00
21.13
E


ATOM
4994
CA
ALA
E
73
73.610
24.887
20.281
1.00
22.11
E


ATOM
4995
CB
ALA
E
73
73.476
24.052
21.568
1.00
21.20
E


ATOM
4996
C
ALA
E
73
74.347
26.189
20.576
1.00
22.67
E


ATOM
4997
O
ALA
E
73
73.773
27.133
21.125
1.00
25.58
E


ATOM
4998
N
ALA
E
74
75.614
26.248
20.195
1.00
22.52
E


ATOM
4999
CA
ALA
E
74
76.420
27.432
20.448
1.00
22.20
E


ATOM
5000
CB
ALA
E
74
77.830
27.219
19.910
1.00
24.81
E


ATOM
5001
C
ALA
E
74
75.828
28.722
19.882
1.00
22.28
E


ATOM
5002
O
ALA
E
74
76.027
29.796
20.452
1.00
20.24
E


ATOM
5003
N
VAL
E
75
75.102
28.634
18.770
1.00
21.92
E


ATOM
5004
CA
VAL
E
75
74.519
29.841
18.185
1.00
21.69
E


ATOM
5005
CB
VAL
E
75
73.700
29.517
16.890
1.00
22.61
E


ATOM
5006
CG1
VAL
E
75
72.488
28.657
17.219
1.00
24.39
E


ATOM
5007
CG2
VAL
E
75
73.270
30.798
16.218
1.00
24.00
E


ATOM
5008
C
VAL
E
75
73.639
30.558
19.219
1.00
21.26
E


ATOM
5009
O
VAL
E
75
73.464
31.777
19.164
1.00
20.64
E


ATOM
5010
N
ASP
E
76
73.106
29.802
20.171
1.00
20.84
E


ATOM
5011
CA
ASP
E
76
72.273
30.385
21.220
1.00
23.98
E


ATOM
5012
CB
ASP
E
76
71.022
29.532
21.471
1.00
25.33
E


ATOM
5013
CG
ASP
E
76
70.010
29.605
20.331
1.00
27.46
E


ATOM
5014
OD1
ASP
E
76
69.807
30.697
19.763
1.00
29.45
E


ATOM
5015
OD2
ASP
E
76
69.398
28.566
20.020
1.00
31.17
E


ATOM
5016
C
ASP
E
76
73.044
30.525
22.538
1.00
24.46
E


ATOM
5017
O
ASP
E
76
72.910
31.524
23.247
1.00
25.64
E


ATOM
5018
N
ARG
E
77
73.846
29.515
22.855
1.00
23.56
E


ATOM
5019
CA
ARG
E
77
74.627
29.486
24.085
1.00
22.99
E


ATOM
5020
CB
ARG
E
77
75.176
28.077
24.279
1.00
26.55
E


ATOM
5021
CG
ARG
E
77
75.848
27.806
25.607
1.00
33.45
E


ATOM
5022
CD
ARG
E
77
75.961
26.295
25.825
1.00
37.66
E


ATOM
5023
NE
ARG
E
77
74.639
25.666
25.883
1.00
40.99
E


ATOM
5024
CZ
ARG
E
77
74.423
24.352
25.862
1.00
43.13
E


ATOM
5025
NH1
ARG
E
77
75.438
23.503
25.782
1.00
43.11
E


ATOM
5026
NH2
ARG
E
77
73.183
23.885
25.914
1.00
44.93
E


ATOM
5027
C
ARG
E
77
75.763
30.509
24.078
1.00
23.23
E


ATOM
5028
O
ARG
E
77
76.162
31.022
25.129
1.00
23.14
E


ATOM
5029
N
VAL
E
78
76.275
30.808
22.889
1.00
20.54
E


ATOM
5030
CA
VAL
E
78
77.354
31.767
22.741
1.00
19.56
E


ATOM
5031
CB
VAL
E
78
78.500
31.181
21.891
1.00
19.17
E


ATOM
5032
CG1
VAL
E
78
79.612
32.208
21.724
1.00
17.69
E


ATOM
5033
CG2
VAL
E
78
79.032
29.921
22.541
1.00
19.40
E


ATOM
5034
C
VAL
E
78
76.888
33.075
22.093
1.00
19.95
E


ATOM
5035
O
VAL
E
78
76.786
34.110
22.756
1.00
21.57
E


ATOM
5036
N
CYS
E
79
76.595
33.021
20.799
1.00
17.88
E


ATOM
5037
CA
CYS
E
79
76.181
34.205
20.059
1.00
17.48
E


ATOM
5038
C
CYS
E
79
74.967
34.966
20.620
1.00
18.40
E


ATOM
5039
O
CYS
E
79
75.087
36.146
20.967
1.00
16.69
E


ATOM
5040
CB
CYS
E
79
75.946
33.847
18.592
1.00
17.30
E


ATOM
5041
SG
CYS
E
79
77.361
33.071
17.722
1.00
27.04
E


ATOM
5042
N
ARG
E
80
73.802
34.326
20.717
1.00
17.59
E


ATOM
5043
CA
ARG
E
80
72.641
35.050
21.240
1.00
20.01
E


ATOM
5044
CB
ARG
E
80
71.340
34.256
21.032
1.00
20.22
E


ATOM
5045
CG
ARG
E
80
70.886
34.213
19.584
1.00
22.92
E


ATOM
5046
CD
ARG
E
80
69.423
33.811
19.439
1.00
23.91
E


ATOM
5047
NE
ARG
E
80
68.972
33.965
18.057
1.00
23.49
E


ATOM
5048
CZ
ARG
E
80
69.206
33.089
17.082
1.00
25.16
E


ATOM
5049
NH1
ARG
E
80
69.884
31.975
17.326
1.00
24.15
E


ATOM
5050
NH2
ARG
E
80
68.778
33.336
15.851
1.00
25.51
E


ATOM
5051
C
ARG
E
80
72.804
35.423
22.716
1.00
20.35
E


ATOM
5052
O
ARG
E
80
72.317
36.464
23.153
1.00
17.98
E


ATOM
5053
N
HIS
E
81
73.495
34.581
23.479
1.00
21.22
E


ATOM
5054
CA
HIS
E
81
73.717
34.867
24.895
1.00
22.79
E


ATOM
5055
CB
HIS
E
81
74.467
33.717
25.572
1.00
24.38
E


ATOM
5056
CG
HIS
E
81
74.955
34.046
26.950
1.00
26.42
E


ATOM
5057
CD2
HIS
E
81
76.188
34.381
27.404
1.00
26.61
E


ATOM
5058
ND1
HIS
E
81
74.122
34.080
28.048
1.00
26.60
E


ATOM
5059
CE1
HIS
E
81
74.819
34.420
29.117
1.00
25.75
E


ATOM
5060
NE2
HIS
E
81
76.075
34.609
28.754
1.00
26.16
E


ATOM
5061
C
HIS
E
81
74.531
36.146
25.060
1.00
21.41
E


ATOM
5062
O
HIS
E
81
74.109
37.076
25.742
1.00
19.84
E


ATOM
5063
N
ASN
E
82
75.700
36.188
24.426
1.00
22.13
E


ATOM
5064
CA
ASN
E
82
76.568
37.361
24.535
1.00
21.51
E


ATOM
5065
CB
ASN
E
82
77.927
37.111
23.864
1.00
18.47
E


ATOM
5066
CG
ASN
E
82
78.702
35.982
24.515
1.00
18.09
E


ATOM
5067
OD1
ASN
E
82
78.453
35.632
25.669
1.00
19.05
E


ATOM
5068
ND2
ASN
E
82
79.656
35.409
23.777
1.00
15.06
E


ATOM
5069
C
ASN
E
82
75.936
38.612
23.949
1.00
20.33
E


ATOM
5070
O
ASN
E
82
76.212
39.716
24.412
1.00
22.84
E


ATOM
5071
N
TYR
E
83
75.089
38.454
22.940
1.00
19.71
E


ATOM
5072
CA
TYR
E
83
74.454
39.620
22.336
1.00
20.96
E


ATOM
5073
CB
TYR
E
83
73.619
39.211
21.114
1.00
21.58
E


ATOM
5074
CG
TYR
E
83
73.223
40.368
20.218
1.00
22.56
E


ATOM
5075
CD1
TYR
E
83
72.047
41.090
20.439
1.00
23.70
E


ATOM
5076
CE1
TYR
E
83
71.682
42.152
19.593
1.00
25.46
E


ATOM
5077
CD2
TYR
E
83
74.027
40.736
19.140
1.00
22.35
E


ATOM
5078
CE2
TYR
E
83
73.675
41.788
18.297
1.00
24.48
E


ATOM
5079
CZ
TYR
E
83
72.508
42.491
18.523
1.00
26.06
E


ATOM
5080
OH
TYR
E
83
72.185
43.524
17.671
1.00
28.63
E


ATOM
5081
C
TYR
E
83
73.583
40.345
23.363
1.00
21.22
E


ATOM
5082
O
TYR
E
83
73.399
41.557
23.276
1.00
21.25
E


ATOM
5083
N
GLN
E
84
73.046
39.606
24.333
1.00
22.94
E


ATOM
5084
CA
GLN
E
84
72.234
40.226
25.377
1.00
25.07
E


ATOM
5085
CB
GLN
E
84
71.631
39.180
26.324
1.00
25.76
E


ATOM
5086
CG
GLN
E
84
70.863
38.047
25.653
1.00
30.97
E


ATOM
5087
CD
GLN
E
84
69.889
38.525
24.594
1.00
33.95
E


ATOM
5088
OE1
GLN
E
84
69.055
39.401
24.840
1.00
36.35
E


ATOM
5089
NE2
GLN
E
84
69.986
37.940
23.401
1.00
36.25
E


ATOM
5090
C
GLN
E
84
73.158
41.145
26.174
1.00
25.41
E


ATOM
5091
O
GLN
E
84
72.804
42.290
26.473
1.00
27.11
E


ATOM
5092
N
LEU
E
85
74.344
40.637
26.510
1.00
24.17
E


ATOM
5093
CA
LEU
E
85
75.330
41.413
27.256
1.00
26.47
E


ATOM
5094
CB
LEU
E
85
76.601
40.590
27.515
1.00
26.91
E


ATOM
5095
CG
LEU
E
85
76.485
39.202
28.161
1.00
29.65
E


ATOM
5096
CD1
LEU
E
85
77.872
38.735
28.587
1.00
31.29
E


ATOM
5097
CD2
LEU
E
85
75.564
39.247
29.365
1.00
32.27
E


ATOM
5098
C
LEU
E
85
75.698
42.661
26.459
1.00
26.89
E


ATOM
5099
O
LEU
E
85
75.762
43.757
27.004
1.00
28.24
E


ATOM
5100
N
GLU
E
86
75.941
42.484
25.162
1.00
27.39
E


ATOM
5101
CA
GLU
E
86
76.293
43.603
24.295
1.00
28.02
E


ATOM
5102
CB
GLU
E
86
76.492
43.126
22.852
1.00
26.60
E


ATOM
5103
CG
GLU
E
86
77.524
42.026
22.672
1.00
30.65
E


ATOM
5104
CD
GLU
E
86
78.942
42.457
23.024
1.00
31.17
E


ATOM
5105
OE1
GLU
E
86
79.860
41.612
22.919
1.00
31.68
E


ATOM
5106
OE2
GLU
E
86
79.139
43.631
23.402
1.00
31.77
E


ATOM
5107
C
GLU
E
86
75.165
44.630
24.327
1.00
27.95
E


ATOM
5108
O
GLU
E
86
75.407
45.834
24.257
1.00
24.30
E


ATOM
5109
N
LEU
E
87
73.935
44.130
24.442
1.00
28.96
E


ATOM
5110
CA
LEU
E
87
72.736
44.962
24.468
1.00
32.20
E


ATOM
5111
CB
LEU
E
87
71.496
44.062
24.423
1.00
32.64
E


ATOM
5112
CG
LEU
E
87
70.506
44.100
23.248
1.00
35.59
E


ATOM
5113
CD1
LEU
E
87
71.101
44.734
21.997
1.00
35.24
E


ATOM
5114
CD2
LEU
E
87
70.071
42.675
22.965
1.00
34.35
E


ATOM
5115
C
LEU
E
87
72.669
45.893
25.686
1.00
33.33
E


ATOM
5116
O
LEU
E
87
71.967
46.902
25.663
1.00
32.52
E


ATOM
5117
N
ARG
E
88
73.401
45.560
26.745
1.00
35.06
E


ATOM
5118
CA
ARG
E
88
73.399
46.389
27.948
1.00
37.29
E


ATOM
5119
CB
ARG
E
88
73.348
45.524
29.215
1.00
39.69
E


ATOM
5120
CG
ARG
E
88
72.471
44.275
29.158
1.00
43.37
E


ATOM
5121
CD
ARG
E
88
72.441
43.592
30.529
1.00
45.38
E


ATOM
5122
NE
ARG
E
88
71.846
42.257
30.499
1.00
48.76
E


ATOM
5123
CZ
ARG
E
88
70.625
41.985
30.047
1.00
50.95
E


ATOM
5124
NH1
ARG
E
88
69.854
42.958
29.579
1.00
52.23
E


ATOM
5125
NH2
ARG
E
88
70.171
40.738
30.064
1.00
51.26
E


ATOM
5126
C
ARG
E
88
74.670
47.225
28.010
1.00
37.36
E


ATOM
5127
O
ARG
E
88
74.842
48.044
28.913
1.00
37.55
E


ATOM
5128
N
THR
E
89
75.564
47.019
27.049
1.00
36.40
E


ATOM
5129
CA
THR
E
89
76.834
47.731
27.055
1.00
34.93
E


ATOM
5130
CB
THR
E
89
77.951
46.807
27.590
1.00
36.26
E


ATOM
5131
OG1
THR
E
89
77.973
45.590
26.825
1.00
34.21
E


ATOM
5132
CG2
THR
E
89
77.708
46.478
29.056
1.00
33.95
E


ATOM
5133
C
THR
E
89
77.294
48.304
25.718
1.00
33.37
E


ATOM
5134
O
THR
E
89
76.958
49.431
25.356
1.00
33.30
E


ATOM
5135
N
THR
E
90
78.080
47.510
25.000
1.00
32.11
E


ATOM
5136
CA
THR
E
90
78.639
47.895
23.712
1.00
30.45
E


ATOM
5137
CB
THR
E
90
79.313
46.681
23.041
1.00
31.20
E


ATOM
5138
OG1
THR
E
90
80.238
46.086
23.958
1.00
32.67
E


ATOM
5139
CG2
THR
E
90
80.076
47.109
21.811
1.00
32.64
E


ATOM
5140
C
THR
E
90
77.639
48.504
22.738
1.00
28.40
E


ATOM
5141
O
THR
E
90
77.903
49.538
22.133
1.00
27.20
E


ATOM
5142
N
LEU
E
91
76.489
47.864
22.582
1.00
29.83
E


ATOM
5143
CA
LEU
E
91
75.482
48.361
21.655
1.00
29.52
E


ATOM
5144
CB
LEU
E
91
74.474
47.252
21.354
1.00
27.50
E


ATOM
5145
CG
LEU
E
91
75.091
46.101
20.550
1.00
26.15
E


ATOM
5146
CD1
LEU
E
91
74.102
44.959
20.457
1.00
24.51
E


ATOM
5147
CD2
LEU
E
91
75.487
46.593
19.157
1.00
23.04
E


ATOM
5148
C
LEU
E
91
74.770
49.629
22.129
1.00
30.74
E


ATOM
5149
O
LEU
E
91
73.994
50.228
21.382
1.00
31.46
E


ATOM
5150
N
GLN
E
92
75.035
50.043
23.366
1.00
29.33
E


ATOM
5151
CA
GLN
E
92
74.427
51.259
23.884
1.00
30.04
E


ATOM
5152
CB
GLN
E
92
73.869
51.044
25.294
1.00
31.55
E


ATOM
5153
CG
GLN
E
92
72.500
50.381
25.327
1.00
36.90
E


ATOM
5154
CD
GLN
E
92
71.865
50.426
26.706
1.00
41.59
E


ATOM
5155
OE1
GLN
E
92
70.760
49.920
26.911
1.00
43.76
E


ATOM
5156
NE2
GLN
E
92
72.563
51.037
27.662
1.00
43.75
E


ATOM
5157
C
GLN
E
92
75.430
52.409
23.898
1.00
28.45
E


ATOM
5158
O
GLN
E
92
75.059
53.558
24.125
1.00
28.57
E


ATOM
5159
N
ARG
E
93
76.699
52.098
23.650
1.00
26.37
E


ATOM
5160
CA
ARG
E
93
77.737
53.127
23.633
1.00
26.74
E


ATOM
5161
CB
ARG
E
93
79.112
52.513
23.340
1.00
24.84
E


ATOM
5162
CG
ARG
E
93
80.260
53.525
23.217
1.00
20.15
E


ATOM
5163
CD
ARG
E
93
81.569
52.801
22.894
1.00
20.06
E


ATOM
5164
NE
ARG
E
93
82.718
53.685
22.729
1.00
15.27
E


ATOM
5165
CZ
ARG
E
93
83.316
54.330
23.729
1.00
16.93
E


ATOM
5166
NH1
ARG
E
93
82.875
54.197
24.973
1.00
17.82
E


ATOM
5167
NH2
ARG
E
93
84.367
55.101
23.492
1.00
16.28
E


ATOM
5168
C
ARG
E
93
77.428
54.173
22.576
1.00
28.26
E


ATOM
5169
O
ARG
E
93
77.202
53.847
21.407
1.00
29.80
E


ATOM
5170
N
ARG
E
94
77.411
55.431
22.995
1.00
28.24
E


ATOM
5171
CA
ARG
E
94
77.159
56.529
22.084
1.00
29.74
E


ATOM
5172
CB
ARG
E
94
75.661
56.855
22.053
1.00
32.88
E


ATOM
5173
CG
ARG
E
94
74.912
55.941
21.086
1.00
36.76
E


ATOM
5174
CD
ARG
E
94
73.402
56.055
21.163
1.00
40.38
E


ATOM
5175
NE
ARG
E
94
72.758
55.304
20.080
1.00
44.16
E


ATOM
5176
CZ
ARG
E
94
72.871
53.991
19.894
1.00
43.57
E


ATOM
5177
NH1
ARG
E
94
73.602
53.259
20.720
1.00
45.04
E


ATOM
5178
NH2
ARG
E
94
72.262
53.408
18.869
1.00
45.75
E


ATOM
5179
C
ARG
E
94
77.992
57.734
22.497
1.00
29.26
E


ATOM
5180
O
ARG
E
94
77.773
58.331
23.546
1.00
30.32
E


ATOM
5181
N
VAL
E
95
78.974
58.063
21.667
1.00
26.76
E


ATOM
5182
CA
VAL
E
95
79.859
59.188
21.936
1.00
25.75
E


ATOM
5183
CB
VAL
E
95
81.340
58.763
21.855
1.00
22.33
E


ATOM
5184
CG1
VAL
E
95
82.244
59.914
22.287
1.00
19.80
E


ATOM
5185
CG2
VAL
E
95
81.565
57.534
22.717
1.00
19.11
E


ATOM
5186
C
VAL
E
95
79.600
60.266
20.902
1.00
26.51
E


ATOM
5187
O
VAL
E
95
79.787
60.042
19.703
1.00
27.04
E


ATOM
5188
N
GLU
E
96
79.160
61.430
21.366
1.00
27.28
E


ATOM
5189
CA
GLU
E
96
78.870
62.536
20.466
1.00
28.16
E


ATOM
5190
CB
GLU
E
96
78.260
63.716
21.227
1.00
30.40
E


ATOM
5191
CG
GLU
E
96
76.965
63.396
21.952
1.00
34.36
E


ATOM
5192
CD
GLU
E
96
76.348
64.625
22.609
1.00
36.84
E


ATOM
5193
OE1
GLU
E
96
75.295
64.478
23.272
1.00
38.81
E


ATOM
5194
OE2
GLU
E
96
76.914
65.734
22.460
1.00
35.73
E


ATOM
5195
C
GLU
E
96
80.148
62.987
19.793
1.00
25.65
E


ATOM
5196
O
GLU
E
96
81.176
63.171
20.440
1.00
24.93
E


ATOM
5197
N
PRO
E
97
80.101
63.168
18.473
1.00
25.41
E


ATOM
5198
CD
PRO
E
97
78.977
62.979
17.539
1.00
24.36
E


ATOM
5199
CA
PRO
E
97
81.304
63.603
17.770
1.00
24.81
E


ATOM
5200
CB
PRO
E
97
80.927
63.416
16.306
1.00
24.85
E


ATOM
5201
CG
PRO
E
97
79.456
63.717
16.309
1.00
25.36
E


ATOM
5202
C
PRO
E
97
81.643
65.048
18.089
1.00
24.48
E


ATOM
5203
O
PRO
E
97
80.761
65.844
18.419
1.00
23.85
E


ATOM
5204
N
THR
E
98
82.927
65.377
18.025
1.00
22.82
E


ATOM
5205
CA
THR
E
98
83.340
66.748
18.244
1.00
24.12
E


ATOM
5206
CB
THR
E
98
84.679
66.852
19.019
1.00
26.31
E


ATOM
5207
OG1
THR
E
98
85.744
66.355
18.205
1.00
34.47
E


ATOM
5208
CG2
THR
E
98
84.623
66.049
20.302
1.00
23.83
E


ATOM
5209
C
THR
E
98
83.519
67.254
16.817
1.00
22.12
E


ATOM
5210
O
THR
E
98
84.162
66.601
15.993
1.00
21.35
E


ATOM
5211
N
VAL
E
99
82.923
68.400
16.516
1.00
21.99
E


ATOM
5212
CA
VAL
E
99
83.001
68.957
15.177
1.00
20.67
E


ATOM
5213
CB
VAL
E
99
81.585
69.217
14.619
1.00
19.57
E


ATOM
5214
CG1
VAL
E
99
81.667
69.645
13.154
1.00
14.62
E


ATOM
5215
CG2
VAL
E
99
80.732
67.944
14.766
1.00
15.20
E


ATOM
5216
C
VAL
E
99
83.814
70.240
15.158
1.00
22.05
E


ATOM
5217
O
VAL
E
99
83.524
71.194
15.884
1.00
22.27
E


ATOM
5218
N
THR
E
100
84.827
70.250
14.304
1.00
21.34
E


ATOM
5219
CA
THR
E
100
85.728
71.376
14.176
1.00
23.10
E


ATOM
5220
CB
THR
E
100
87.104
71.024
14.786
1.00
24.55
E


ATOM
5221
OG1
THR
E
100
86.941
70.728
16.180
1.00
30.47
E


ATOM
5222
CG2
THR
E
100
88.079
72.183
14.634
1.00
27.79
E


ATOM
5223
C
THR
E
100
85.934
71.777
12.722
1.00
23.36
E


ATOM
5224
O
THR
E
100
86.024
70.926
11.842
1.00
21.77
E


ATOM
5225
N
ILE
E
101
86.009
73.082
12.473
1.00
24.40
E


ATOM
5226
CA
ILE
E
101
86.236
73.584
11.124
1.00
25.31
E


ATOM
5227
CB
ILE
E
101
85.092
74.518
10.645
1.00
24.21
E


ATOM
5228
CG2
ILE
E
101
85.398
75.044
9.245
1.00
22.51
E


ATOM
5229
CG1
ILE
E
101
83.760
73.768
10.636
1.00
24.86
E


ATOM
5230
CD1
ILE
E
101
82.584
74.635
10.197
1.00
25.22
E


ATOM
5231
C
ILE
E
101
87.538
74.372
11.116
1.00
26.66
E


ATOM
5232
O
ILE
E
101
87.859
75.065
12.074
1.00
26.18
E


ATOM
5233
N
SER
E
102
88.287
74.262
10.029
1.00
31.17
E


ATOM
5234
CA
SER
E
102
89.547
74.977
9.902
1.00
35.36
E


ATOM
5235
CB
SER
E
102
90.619
74.306
10.755
1.00
34.20
E


ATOM
5236
OG
SER
E
102
90.777
72.953
10.374
1.00
40.09
E


ATOM
5237
C
SER
E
102
89.976
74.979
8.448
1.00
36.82
E


ATOM
5238
O
SER
E
102
89.913
73.953
7.777
1.00
36.68
E


ATOM
5239
N
PRO
E
103
90.404
76.139
7.932
1.00
39.96
E


ATOM
5240
CD
PRO
E
103
90.458
77.473
8.553
1.00
40.07
E


ATOM
5241
CA
PRO
E
103
90.831
76.190
6.532
1.00
42.01
E


ATOM
5242
CB
PRO
E
103
90.856
77.682
6.237
1.00
41.76
E


ATOM
5243
CG
PRO
E
103
91.282
78.258
7.556
1.00
42.86
E


ATOM
5244
C
PRO
E
103
92.196
75.534
6.390
1.00
44.62
E


ATOM
5245
O
PRO
E
103
92.943
75.430
7.365
1.00
44.53
E


ATOM
5246
N
SER
E
104
92.514
75.086
5.181
1.00
47.92
E


ATOM
5247
CA
SER
E
104
93.789
74.426
4.920
1.00
50.83
E


ATOM
5248
CB
SER
E
104
93.712
73.637
3.612
1.00
52.33
E


ATOM
5249
OG
SER
E
104
94.904
72.901
3.396
1.00
55.60
E


ATOM
5250
C
SER
E
104
94.941
75.422
4.845
1.00
52.18
E


ATOM
5251
O
SER
E
104
96.080
75.093
5.186
1.00
53.53
E


ATOM
5252
N
ASN
E
113
90.669
78.112
−1.692
1.00
48.40
E


ATOM
5253
CA
ASN
E
113
90.651
77.795
−0.269
1.00
47.57
E


ATOM
5254
CB
ASN
E
113
89.863
78.854
0.496
1.00
51.34
E


ATOM
5255
CG
ASN
E
113
90.504
80.219
0.417
1.00
52.99
E


ATOM
5256
OD1
ASN
E
113
90.693
80.765
−0.670
1.00
55.11
E


ATOM
5257
ND2
ASN
E
113
90.845
80.781
1.572
1.00
55.09
E


ATOM
5258
C
ASN
E
113
90.045
76.424
−0.001
1.00
44.87
E


ATOM
5259
O
ASN
E
113
89.374
75.852
−0.860
1.00
44.99
E


ATOM
5260
N
LEU
E
114
90.282
75.904
1.197
1.00
41.65
E


ATOM
5261
CA
LEU
E
114
89.765
74.592
1.568
1.00
38.53
E


ATOM
5262
CB
LEU
E
114
90.823
73.521
1.287
1.00
38.84
E


ATOM
5263
CG
LEU
E
114
90.383
72.060
1.441
1.00
40.32
E


ATOM
5264
CD1
LEU
E
114
89.314
71.726
0.400
1.00
39.94
E


ATOM
5265
CD2
LEU
E
114
91.586
71.145
1.266
1.00
40.52
E


ATOM
5266
C
LEU
E
114
89.349
74.523
3.036
1.00
34.78
E


ATOM
5267
O
LEU
E
114
90.173
74.684
3.929
1.00
33.51
E


ATOM
5268
N
LEU
E
115
88.063
74.293
3.278
1.00
32.05
E


ATOM
5269
CA
LEU
E
115
87.550
74.181
4.641
1.00
29.68
E


ATOM
5270
CB
LEU
E
115
86.158
74.809
4.754
1.00
29.84
E


ATOM
5271
CG
LEU
E
115
86.046
76.257
5.241
1.00
31.52
E


ATOM
5272
CD1
LEU
E
115
87.101
77.140
4.574
1.00
32.51
E


ATOM
5273
CD2
LEU
E
115
84.636
76.762
4.948
1.00
30.75
E


ATOM
5274
C
LEU
E
115
87.472
72.712
5.034
1.00
27.57
E


ATOM
5275
O
LEU
E
115
86.871
71.900
4.331
1.00
25.33
E


ATOM
5276
N
VAL
E
116
88.089
72.381
6.161
1.00
26.32
E


ATOM
5277
CA
VAL
E
116
88.099
71.014
6.651
1.00
24.42
E


ATOM
5278
CB
VAL
E
116
89.513
70.572
7.075
1.00
24.51
E


ATOM
5279
CG1
VAL
E
116
89.467
69.160
7.641
1.00
22.66
E


ATOM
5280
CG2
VAL
E
116
90.458
70.643
5.879
1.00
26.70
E


ATOM
5281
C
VAL
E
116
87.195
70.842
7.846
1.00
22.77
E


ATOM
5282
O
VAL
E
116
87.376
71.496
8.868
1.00
23.04
E


ATOM
5283
N
CYS
E
117
86.208
69.968
7.717
1.00
22.34
E


ATOM
5284
CA
CYS
E
117
85.326
69.711
8.840
1.00
21.65
E


ATOM
5285
C
CYS
E
117
85.769
68.391
9.466
1.00
19.44
E


ATOM
5286
O
CYS
E
117
85.607
67.319
8.877
1.00
18.95
E


ATOM
5287
CB
CYS
E
117
83.863
69.626
8.401
1.00
22.57
E


ATOM
5288
SG
CYS
E
117
82.771
69.420
9.844
1.00
25.79
E


ATOM
5289
N
SER
E
118
86.355
68.488
10.654
1.00
19.92
E


ATOM
5290
CA
SER
E
118
86.837
67.330
11.387
1.00
17.98
E


ATOM
5291
CB
SER
E
118
88.115
67.671
12.146
1.00
18.33
E


ATOM
5292
OG
SER
E
118
89.121
68.117
11.260
1.00
24.58
E


ATOM
5293
C
SER
E
118
85.798
66.860
12.377
1.00
17.01
E


ATOM
5294
O
SER
E
118
85.507
67.543
13.354
1.00
16.69
E


ATOM
5295
N
VAL
E
119
85.240
65.688
12.112
1.00
16.58
E


ATOM
5296
CA
VAL
E
119
84.242
65.095
12.985
1.00
16.03
E


ATOM
5297
CB
VAL
E
119
83.040
64.582
12.160
1.00
15.47
E


ATOM
5298
CG1
VAL
E
119
81.918
64.147
13.077
1.00
13.75
E


ATOM
5299
CG2
VAL
E
119
82.559
65.686
11.216
1.00
10.95
E


ATOM
5300
C
VAL
E
119
85.018
63.960
13.638
1.00
17.51
E


ATOM
5301
O
VAL
E
119
85.238
62.906
13.042
1.00
19.30
E


ATOM
5302
N
THR
E
120
85.442
64.203
14.871
1.00
18.44
E


ATOM
5303
CA
THR
E
120
86.265
63.266
15.616
1.00
18.41
E


ATOM
5304
CB
THR
E
120
87.562
63.962
16.042
1.00
18.11
E


ATOM
5305
OG1
THR
E
120
87.242
65.078
16.887
1.00
17.18
E


ATOM
5306
CG2
THR
E
120
88.304
64.481
14.835
1.00
16.77
E


ATOM
5307
C
TER
E
120
85.655
62.656
16.875
1.00
20.11
E


ATOM
5308
O
THR
E
120
84.665
63.148
17.417
1.00
21.96
E


ATOM
5309
N
ASP
E
121
86.272
61.566
17.319
1.00
19.96
E


ATOM
5310
CA
ASP
E
121
85.882
60.864
18.529
1.00
21.06
E


ATOM
5311
CB
ASP
E
121
86.313
61.686
19.745
1.00
25.93
E


ATOM
5312
CG
ASP
E
121
87.814
61.765
19.882
1.00
30.02
E


ATOM
5313
OD1
ASP
E
121
88.291
62.524
20.756
1.00
34.97
E


ATOM
5314
OD2
ASP
E
121
88.513
61.063
19.114
1.00
31.15
E


ATOM
5315
C
ASP
E
121
84.431
60.463
18.709
1.00
20.39
E


ATOM
5316
O
ASP
E
121
83.857
60.698
19.766
1.00
22.05
E


ATOM
5317
N
PHE
E
122
83.827
59.841
17.708
1.00
19.69
E


ATOM
5318
CA
PHE
E
122
82.443
59.429
17.873
1.00
18.28
E


ATOM
5319
CB
PHE
E
122
81.538
60.108
16.843
1.00
16.99
E


ATOM
5320
CG
PHE
E
122
81.905
59.821
15.417
1.00
16.67
E


ATOM
5321
CD1
PHE
E
122
82.770
60.661
14.725
1.00
16.72
E


ATOM
5322
CD2
PHE
E
122
81.370
58.717
14.756
1.00
17.17
E


ATOM
5323
CE1
PHE
E
122
83.096
60.410
13.384
1.00
17.00
E


ATOM
5324
CE2
PHE
E
122
81.686
58.456
13.419
1.00
16.82
E


ATOM
5325
CZ
PHE
E
122
82.549
59.305
12.733
1.00
15.81
E


ATOM
5326
C
PHE
E
122
82.287
57.925
17.774
1.00
18.35
E


ATOM
5327
O
PHE
E
122
83.168
57.231
17.272
1.00
15.90
E


ATOM
5328
N
TYR
E
123
81.157
57.436
18.276
1.00
19.49
E


ATOM
5329
CA
TYR
E
123
80.818
56.021
18.243
1.00
20.92
E


ATOM
5330
CB
TYR
E
123
81.523
55.261
19.374
1.00
21.02
E


ATOM
5331
CG
TYR
E
123
81.387
53.762
19.247
1.00
20.05
E


ATOM
5332
CD1
TYR
E
123
80.242
53.103
19.688
1.00
21.66
E


ATOM
5333
CE1
TYR
E
123
80.095
51.726
19.516
1.00
21.85
E


ATOM
5334
CD2
TYR
E
123
82.383
53.009
18.633
1.00
20.08
E


ATOM
5335
CE2
TYR
E
123
82.250
51.643
18.455
1.00
19.20
E


ATOM
5336
CZ
TYR
E
123
81.105
51.002
18.896
1.00
22.24
E


ATOM
5337
OH
TYR
E
123
80.970
49.640
18.712
1.00
25.26
E


ATOM
5338
C
TYR
E
123
79.311
55.957
18.440
1.00
21.42
E


ATOM
5339
O
TYR
E
123
78.778
56.647
19.305
1.00
23.90
E


ATOM
5340
N
PRO
E
124
78.609
55.100
17.676
1.00
20.39
E


ATOM
5341
CD
PRO
E
124
77.155
54.937
17.844
1.00
21.24
E


ATOM
5342
CA
PRO
E
124
79.113
54.177
16.655
1.00
21.61
E


ATOM
5343
CB
PRO
E
124
77.956
53.188
16.500
1.00
19.35
E


ATOM
5344
CG
PRO
E
124
76.776
54.056
16.670
1.00
19.34
E


ATOM
5345
C
PRO
E
124
79.549
54.802
15.325
1.00
20.84
E


ATOM
5346
O
PRO
E
124
79.602
56.024
15.184
1.00
22.13
E


ATOM
5347
N
ALA
E
125
79.862
53.940
14.361
1.00
22.61
E


ATOM
5348
CA
ALA
E
125
80.329
54.341
13.027
1.00
25.48
E


ATOM
5349
CB
ALA
E
125
80.860
53.121
12.288
1.00
26.06
E


ATOM
5350
C
ALA
E
125
79.311
55.058
12.137
1.00
27.38
E


ATOM
5351
O
ALA
E
125
79.681
55.906
11.332
1.00
29.08
E


ATOM
5352
N
GLN
E
126
78.039
54.706
12.268
1.00
29.18
E


ATOM
5353
CA
GLN
E
126
76.990
55.312
11.455
1.00
29.94
E


ATOM
5354
CB
GLN
E
126
75.625
54.737
11.848
1.00
33.48
E


ATOM
5355
CG
GLN
E
126
75.536
53.200
11.840
1.00
39.27
E


ATOM
5356
CD
GLN
E
126
76.067
52.537
13.117
1.00
41.92
E


ATOM
5357
OE1
GLN
E
126
77.271
52.523
13.379
1.00
44.02
E


ATOM
5358
NE2
GLN
E
126
75.159
51.981
13.913
1.00
43.83
E


ATOM
5359
C
GLN
E
126
76.977
56.829
11.621
1.00
28.88
E


ATOM
5360
O
GLN
E
126
76.739
57.331
12.719
1.00
28.83
E


ATOM
5361
N
ILE
E
127
77.221
57.558
10.532
1.00
27.90
E


ATOM
5362
CA
ILE
E
127
77.245
59.018
10.591
1.00
25.67
E


ATOM
5363
CB
ILE
E
127
78.611
59.514
11.150
1.00
25.23
E


ATOM
5364
CG2
ILE
E
127
79.693
59.398
10.084
1.00
21.16
E


ATOM
5365
CG1
ILE
E
127
78.504
60.965
11.610
1.00
22.40
E


ATOM
5366
CD1
ILE
E
127
79.610
61.376
12.546
1.00
25.35
E


ATOM
5367
C
ILE
E
127
76.985
59.673
9.230
1.00
26.38
E


ATOM
5368
O
ILE
E
127
77.196
59.065
8.182
1.00
26.20
E


ATOM
5369
N
LYS
E
128
76.521
60.916
9.252
1.00
25.64
E


ATOM
5370
CA
LYS
E
128
76.248
61.635
8.016
1.00
29.02
E


ATOM
5371
CB
LYS
E
128
74.754
61.566
7.671
1.00
29.97
E


ATOM
5372
CG
LYS
E
128
74.408
62.178
6.317
1.00
35.17
E


ATOM
5373
CD
LYS
E
128
75.175
61.487
5.183
1.00
39.63
E


ATOM
5374
CE
LYS
E
128
74.936
62.163
3.836
1.00
41.20
E


ATOM
5375
NZ
LYS
E
128
75.685
61.492
2.731
1.00
44.74
E


ATOM
5376
C
LYS
E
128
76.683
63.090
8.154
1.00
28.40
E


ATOM
5377
O
LYS
E
128
76.203
63.812
9.028
1.00
27.15
E


ATOM
5378
N
VAL
E
129
77.600
63.506
7.287
1.00
28.99
E


ATOM
5379
CA
VAL
E
129
78.119
64.866
7.304
1.00
29.32
E


ATOM
5380
CB
VAL
E
129
79.651
64.860
7.502
1.00
30.69
E


ATOM
5381
CG1
VAL
E
129
80.171
66.282
7.654
1.00
27.54
E


ATOM
5382
CG2
VAL
E
129
80.014
64.012
8.721
1.00
30.82
E


ATOM
5383
C
VAL
E
129
77.788
65.574
5.992
1.00
30.45
E


ATOM
5384
O
VAL
E
129
78.042
65.039
4.915
1.00
30.36
E


ATOM
5385
N
ARG
E
130
77.221
66.775
6.090
1.00
31.17
E


ATOM
5386
CA
ARG
E
130
76.851
67.562
4.914
1.00
32.17
E


ATOM
5387
CB
ARG
E
130
75.330
67.626
4.764
1.00
34.73
E


ATOM
5388
CG
ARG
E
130
74.632
66.335
4.400
1.00
40.85
E


ATOM
5389
CD
ARG
E
130
73.121
66.527
4.511
1.00
46.16
E


ATOM
5390
NE
ARG
E
130
72.365
65.456
3.864
1.00
51.33
E


ATOM
5391
CZ
ARG
E
130
71.046
65.308
3.959
1.00
53.45
E


ATOM
5392
NH1
ARG
E
130
70.327
66.162
4.680
1.00
54.21
E


ATOM
5393
NH2
ARG
E
130
70.444
64.307
3.329
1.00
53.97
E


ATOM
5394
C
ARG
E
130
77.359
68.994
5.017
1.00
30.88
E


ATOM
5395
O
ARG
E
130
77.321
69.590
6.093
1.00
30.84
E


ATOM
5396
N
TRP
E
131
77.831
69.542
3.900
1.00
29.14
E


ATOM
5397
CA
TRP
E
131
78.291
70.928
3.865
1.00
29.57
E


ATOM
5398
CB
TRP
E
131
79.538
71.086
2.996
1.00
27.97
E


ATOM
5399
CG
TRP
E
131
80.809
70.979
3.760
1.00
29.37
E


ATOM
5400
CD2
TRP
E
131
81.342
71.949
4.671
1.00
29.95
E


ATOM
5401
CE2
TRP
E
131
82.551
71.427
5.174
1.00
29.75
E


ATOM
5402
CE3
TRP
E
131
80.913
73.209
5.111
1.00
30.39
E


ATOM
5403
CD1
TRP
E
131
81.689
69.941
3.747
1.00
29.02
E


ATOM
5404
NE1
TRP
E
131
82.738
70.200
4.592
1.00
30.01
E


ATOM
5405
CZ2
TRP
E
131
83.340
72.119
6.095
1.00
28.79
E


ATOM
5406
CZ3
TRP
E
131
81.697
73.900
6.027
1.00
31.30
E


ATOM
5407
CH2
TRP
E
131
82.900
73.350
6.509
1.00
31.69
E


ATOM
5408
C
TRP
E
131
77.185
71.817
3.301
1.00
30.08
E


ATOM
5409
O
TRP
E
131
76.449
71.413
2.392
1.00
29.15
E


ATOM
5410
N
PHE
E
132
77.081
73.027
3.842
1.00
29.87
E


ATOM
5411
CA
PHE
E
132
76.078
73.985
3.405
1.00
30.98
E


ATOM
5412
CB
PHE
E
132
74.963
74.094
4.443
1.00
32.09
E


ATOM
5413
CG
PHE
E
132
74.041
72.918
4.461
1.00
33.03
E


ATOM
5414
CD1
PHE
E
132
72.913
72.896
3.650
1.00
35.25
E


ATOM
5415
CD2
PHE
E
132
74.306
71.822
5.273
1.00
33.31
E


ATOM
5416
CE1
PHE
E
132
72.055
71.794
3.646
1.00
35.49
E


ATOM
5417
CE2
PHE
E
132
73.460
70.717
5.279
1.00
35.47
E


ATOM
5418
CZ
PHE
E
132
72.330
70.704
4.461
1.00
35.97
E


ATOM
5419
C
PHE
E
132
76.668
75.364
3.182
1.00
32.06
E


ATOM
5420
O
PHE
E
132
77.537
75.812
3.929
1.00
29.15
E


ATOM
5421
N
ARG
E
133
76.186
76.026
2.138
1.00
34.68
E


ATOM
5422
CA
ARG
E
133
76.613
77.375
1.809
1.00
37.78
E


ATOM
5423
CB
ARG
E
133
77.281
77.420
0.434
1.00
40.14
E


ATOM
5424
CG
ARG
E
133
77.755
78.810
0.005
1.00
43.27
E


ATOM
5425
CD
ARG
E
133
78.474
78.742
−1.341
1.00
46.34
E


ATOM
5426
NE
ARG
E
133
79.096
80.006
−1.738
1.00
49.86
E


ATOM
5427
CZ
ARG
E
133
78.441
81.058
−2.226
1.00
51.63
E


ATOM
5428
NH1
ARG
E
133
77.124
81.018
−2.387
1.00
51.33
E


ATOM
5429
NH2
ARG
E
133
79.111
82.155
−2.562
1.00
52.46
E


ATOM
5430
C
ARG
E
133
75.343
78.204
1.792
1.00
38.70
E


ATOM
5431
O
ARG
E
133
74.569
78.154
0.835
1.00
38.81
E


ATOM
5432
N
ASN
E
134
75.119
78.940
2.872
1.00
39.37
E


ATOM
5433
CA
ASN
E
134
73.941
79.787
2.984
1.00
42.21
E


ATOM
5434
CB
ASN
E
134
74.040
80.952
1.988
1.00
40.37
E


ATOM
5435
CG
ASN
E
134
75.383
81.667
2.051
1.00
39.50
E


ATOM
5436
OD1
ASN
E
134
75.796
82.151
3.104
1.00
35.36
E


ATOM
5437
ND2
ASN
E
134
76.071
81.733
0.917
1.00
39.94
E


ATOM
5438
C
ASN
E
134
72.652
79.000
2.734
1.00
43.61
E


ATOM
5439
O
ASN
E
134
71.899
79.306
1.809
1.00
45.62
E


ATOM
5440
N
ASP
E
135
72.403
77.983
3.550
1.00
45.40
E


ATOM
5441
CA
ASP
E
135
71.189
77.178
3.413
1.00
47.16
E


ATOM
5442
C
ASP
E
135
71.147
76.279
2.173
1.00
48.15
E


ATOM
5443
O
ASP
E
135
70.205
75.504
1.996
1.00
49.25
E


ATOM
5444
N
GLN
E
136
72.158
76.387
1.316
1.00
48.16
E


ATOM
5445
CA
GLN
E
136
72.226
75.561
0.113
1.00
47.50
E


ATOM
5446
C
GLN
E
136
73.254
74.445
0.313
1.00
47.38
E


ATOM
5447
O
GLN
E
136
74.418
74.711
0.627
1.00
46.25
E


ATOM
5448
N
GLU
E
137
72.829
73.197
0.139
1.00
47.09
E


ATOM
5449
CA
GLU
E
137
73.749
72.079
0.308
1.00
47.41
E


ATOM
5450
CB
GLU
E
137
72.992
70.752
0.406
1.00
47.53
E


ATOM
5451
CG
GLU
E
137
73.921
69.570
0.653
1.00
49.67
E


ATOM
5452
CD
GLU
E
137
73.210
68.334
1.166
1.00
51.28
E


ATOM
5453
OE1
GLU
E
137
73.911
67.336
1.432
1.00
52.31
E


ATOM
5454
OE2
GLU
E
137
71.965
68.352
1.306
1.00
51.54
E


ATOM
5455
C
GLU
E
137
74.755
72.016
−0.833
1.00
47.37
E


ATOM
5456
O
GLU
E
137
74.397
72.163
−2.000
1.00
47.51
E


ATOM
5457
N
GLU
E
138
76.018
71.809
−0.477
1.00
47.53
E


ATOM
5458
CA
GLU
E
138
77.104
71.724
−1.444
1.00
48.48
E


ATOM
5459
CB
GLU
E
138
78.266
72.617
−1.011
1.00
49.89
E


ATOM
5460
CG
GLU
E
138
77.949
74.096
−0.973
1.00
54.83
E


ATOM
5461
CD
GLU
E
138
77.911
74.720
−2.354
1.00
57.91
E


ATOM
5462
OE1
GLU
E
138
78.953
74.686
−3.044
1.00
59.04
E


ATOM
5463
OE2
GLU
E
138
76.846
75.247
−2.748
1.00
58.96
E


ATOM
5464
C
GLU
E
138
77.593
70.284
−1.532
1.00
48.42
E


ATOM
5465
O
GLU
E
138
77.898
69.665
−0.513
1.00
48.62
E


ATOM
5466
N
THR
E
139
77.665
69.754
−2.748
1.00
47.87
E


ATOM
5467
CA
THR
E
139
78.135
68.387
−2.959
1.00
48.16
E


ATOM
5468
CB
THR
E
139
77.027
67.498
−3.556
1.00
49.05
E


ATOM
5469
OG1
THR
E
139
76.464
68.140
−4.710
1.00
51.25
E


ATOM
5470
CG2
THR
E
139
75.938
67.249
−2.525
1.00
48.03
E


ATOM
5471
C
THR
E
139
79.339
68.401
−3.895
1.00
46.96
E


ATOM
5472
O
THR
E
139
80.245
67.574
−3.779
1.00
46.46
E


ATOM
5473
N
ALA
E
140
79.339
69.346
−4.827
1.00
46.59
E


ATOM
5474
CA
ALA
E
140
80.446
69.488
−5.761
1.00
45.07
E


ATOM
5475
CB
ALA
E
140
79.997
70.244
−7.008
1.00
44.64
E


ATOM
5476
C
ALA
E
140
81.518
70.276
−5.019
1.00
43.57
E


ATOM
5477
O
ALA
E
140
81.224
71.293
−4.386
1.00
43.33
E


ATOM
5478
N
GLY
E
141
82.756
69.805
−5.091
1.00
41.31
E


ATOM
5479
CA
GLY
E
141
83.833
70.485
−4.398
1.00
38.27
E


ATOM
5480
C
GLY
E
141
84.053
69.854
−3.034
1.00
36.91
E


ATOM
5481
O
GLY
E
141
84.930
70.264
−2.272
1.00
37.78
E


ATOM
5482
N
VAL
E
142
83.245
68.849
−2.722
1.00
33.36
E


ATOM
5483
CA
VAL
E
142
83.363
68.164
−1.449
1.00
32.16
E


ATOM
5484
CB
VAL
E
142
81.978
67.844
−0.847
1.00
31.40
E


ATOM
5485
CG1
VAL
E
142
82.140
66.995
0.407
1.00
28.96
E


ATOM
5486
CG2
VAL
E
142
81.245
69.134
−0.516
1.00
33.20
E


ATOM
5487
C
VAL
E
142
84.140
66.859
−1.576
1.00
31.49
E


ATOM
5488
O
VAL
E
142
83.862
66.032
−2.450
1.00
31.67
E


ATOM
5489
N
VAL
E
143
85.118
66.684
−0.696
1.00
30.51
E


ATOM
5490
CA
VAL
E
143
85.922
65.473
−0.675
1.00
30.35
E


ATOM
5491
CB
VAL
E
143
87.367
65.731
−1.161
1.00
30.33
E


ATOM
5492
CG1
VAL
E
143
88.096
64.408
−1.348
1.00
32.44
E


ATOM
5493
CG2
VAL
E
143
87.347
66.503
−2.460
1.00
33.96
E


ATOM
5494
C
VAL
E
143
85.966
64.973
0.767
1.00
29.68
E


ATOM
5495
O
VAL
E
143
86.242
65.733
1.695
1.00
29.63
E


ATOM
5496
N
SER
E
144
85.696
63.689
0.946
1.00
28.32
E


ATOM
5497
CA
SER
E
144
85.703
63.090
2.268
1.00
25.38
E


ATOM
5498
CB
SER
E
144
84.295
62.613
2.622
1.00
26.70
E


ATOM
5499
OG
SER
E
144
84.300
61.845
3.807
1.00
28.37
E


ATOM
5500
C
SER
E
144
86.663
61.916
2.361
1.00
24.56
E


ATOM
5501
O
SER
E
144
86.824
61.148
1.412
1.00
23.42
E


ATOM
5502
N
THR
E
145
87.320
61.790
3.506
1.00
24.40
E


ATOM
5503
CA
THR
E
145
88.218
60.666
3.726
1.00
24.38
E


ATOM
5504
CB
THR
E
145
89.103
60.849
4.983
1.00
24.55
E


ATOM
5505
OG1
THR
E
145
88.273
60.815
6.155
1.00
21.59
E


ATOM
5506
CG2
THR
E
145
89.858
62.162
4.935
1.00
24.64
E


ATOM
5507
C
THR
E
145
87.256
59.539
4.055
1.00
23.78
E


ATOM
5508
O
THR
E
145
86.064
59.766
4.242
1.00
23.97
E


ATOM
5509
N
PRO
E
146
87.745
58.300
4.099
1.00
25.25
E


ATOM
5510
CD
PRO
E
146
88.993
57.713
3.585
1.00
25.42
E


ATOM
5511
CA
PRO
E
146
86.770
57.264
4.447
1.00
25.00
E


ATOM
5512
CB
PRO
E
146
87.439
55.983
3.951
1.00
26.60
E


ATOM
5513
CG
PRO
E
146
88.905
56.293
4.094
1.00
27.24
E


ATOM
5514
C
PRO
E
146
86.597
57.284
5.976
1.00
23.26
E


ATOM
5515
O
PRO
E
146
87.286
58.030
6.672
1.00
21.73
E


ATOM
5516
N
LEU
E
147
85.669
56.492
6.495
1.00
23.85
E


ATOM
5517
CA
LEU
E
147
85.476
56.419
7.936
1.00
23.63
E


ATOM
5518
CB
LEU
E
147
84.355
55.428
8.260
1.00
25.11
E


ATOM
5519
CG
LEU
E
147
83.976
55.241
9.731
1.00
28.28
E


ATOM
5520
CD1
LEU
E
147
83.392
56.530
10.270
1.00
29.44
E


ATOM
5521
CD2
LEU
E
147
82.965
54.116
9.867
1.00
28.72
E


ATOM
5522
C
LEU
E
147
86.812
55.915
8.503
1.00
22.77
E


ATOM
5523
O
LEU
E
147
87.366
54.944
8.003
1.00
23.04
E


ATOM
5524
N
ILE
E
148
87.337
56.574
9.530
1.00
21.06
E


ATOM
5525
CA
ILE
E
148
88.614
56.156
10.102
1.00
19.40
E


ATOM
5526
CB
ILE
E
148
89.588
57.355
10.200
1.00
20.05
E


ATOM
5527
CG2
ILE
E
148
90.903
56.922
10.835
1.00
19.93
E


ATOM
5528
CG1
ILE
E
148
89.854
57.918
8.803
1.00
17.58
E


ATOM
5529
CD1
ILE
E
148
90.594
59.225
8.821
1.00
20.23
E


ATOM
5530
C
ILE
E
148
88.449
55.534
11.489
1.00
17.19
E


ATOM
5531
O
ILE
E
148
87.820
56.118
12.360
1.00
15.81
E


ATOM
5532
N
ARG
E
149
89.015
54.344
11.677
1.00
15.23
E


ATOM
5533
CA
ARG
E
149
88.948
53.638
12.956
1.00
16.42
E


ATOM
5534
CB
ARG
E
149
88.906
52.128
12.724
1.00
20.12
E


ATOM
5535
CG
ARG
E
149
88.903
51.289
14.000
1.00
21.32
E


ATOM
5536
CD
ARG
E
149
88.963
49.802
13.649
1.00
22.44
E


ATOM
5537
NE
ARG
E
149
87.825
49.382
12.830
1.00
22.55
E


ATOM
5538
CZ
ARG
E
149
86.623
49.084
13.313
1.00
22.89
E


ATOM
5539
NH1
ARG
E
149
85.650
48.718
12.490
1.00
24.25
E


ATOM
5540
NH2
ARG
E
149
86.398
49.139
14.619
1.00
23.36
E


ATOM
5541
C
ARG
E
149
90.174
53.983
13.786
1.00
16.33
E


ATOM
5542
O
ARG
E
149
91.305
53.734
13.363
1.00
16.45
E


ATOM
5543
N
ASN
E
150
89.953
54.558
14.963
1.00
15.72
E


ATOM
5544
CA
ASN
E
150
91.061
54.948
15.825
1.00
15.93
E


ATOM
5545
CB
ASN
E
150
90.662
56.125
16.740
1.00
13.37
E


ATOM
5546
CG
ASN
E
150
90.278
57.383
15.955
1.00
15.55
E


ATOM
5547
OD1
ASN
E
150
90.922
57.739
14.955
1.00
14.20
E


ATOM
5548
ND2
ASN
E
150
89.233
58.068
16.414
1.00
15.61
E


ATOM
5549
C
ASN
E
150
91.576
53.786
16.670
1.00
16.79
E


ATOM
5550
O
ASN
E
150
92.694
53.838
17.180
1.00
18.80
E


ATOM
5551
N
GLY
E
151
90.764
52.745
16.813
1.00
16.63
E


ATOM
5552
CA
GLY
E
151
91.164
51.587
17.593
1.00
18.68
E


ATOM
5553
C
GLY
E
151
90.879
51.684
19.080
1.00
20.19
E


ATOM
5554
O
GLY
E
151
91.087
50.725
19.818
1.00
21.39
E


ATOM
5555
N
ASP
E
152
90.409
52.836
19.539
1.00
19.57
E


ATOM
5556
CA
ASP
E
152
90.108
52.986
20.954
1.00
19.09
E


ATOM
5557
CB
ASP
E
152
90.865
54.177
21.531
1.00
18.53
E


ATOM
5558
CG
ASP
E
152
90.498
55.481
20.856
1.00
21.27
E


ATOM
5559
OD1
ASP
E
152
89.736
55.453
19.864
1.00
20.11
E


ATOM
5560
OD2
ASP
E
152
90.984
56.531
21.321
1.00
22.57
E


ATOM
5561
C
ASP
E
152
88.605
53.156
21.182
1.00
19.23
E


ATOM
5562
O
ASP
E
152
88.177
53.840
22.113
1.00
17.78
E


ATOM
5563
N
TRP
E
153
87.816
52.522
20.318
1.00
18.88
E


ATOM
5564
CA
TRP
E
153
86.356
52.566
20.391
1.00
18.61
E


ATOM
5565
CB
TRP
E
153
85.862
52.162
21.788
1.00
17.06
E


ATOM
5566
CG
TRP
E
153
86.084
50.690
22.085
1.00
17.90
E


ATOM
5567
CD2
TRP
E
153
85.165
49.612
21.830
1.00
18.84
E


ATOM
5568
CE2
TRP
E
153
85.804
48.414
22.222
1.00
16.88
E


ATOM
5569
CE3
TRP
E
153
83.862
49.544
21.308
1.00
18.29
E


ATOM
5570
CD1
TRP
E
153
87.209
50.114
22.604
1.00
16.70
E


ATOM
5571
NE1
TRP
E
153
87.049
48.747
22.688
1.00
17.49
E


ATOM
5572
CZ2
TRP
E
153
85.189
47.164
22.109
1.00
16.54
E


ATOM
5573
CZ3
TRP
E
153
83.250
48.303
21.196
1.00
17.19
E


ATOM
5574
CH2
TRP
E
153
83.917
47.129
21.597
1.00
17.24
E


ATOM
5575
C
TRP
E
153
85.732
53.887
19.975
1.00
18.97
E


ATOM
5576
O
TRP
E
153
84.696
54.300
20.508
1.00
18.70
E


ATOM
5577
N
THR
E
154
86.378
54.546
19.016
1.00
19.20
E


ATOM
5578
CA
THR
E
154
85.876
55.794
18.444
1.00
19.92
E


ATOM
5579
CB
THR
E
154
86.442
57.072
19.129
1.00
21.42
E


ATOM
5580
OG1
THR
E
154
87.865
57.129
18.958
1.00
19.26
E


ATOM
5581
CG2
THR
E
154
86.085
57.096
20.599
1.00
22.17
E


ATOM
5582
C
THR
E
154
86.314
55.835
16.992
1.00
18.66
E


ATOM
5583
O
THR
E
154
87.270
55.156
16.603
1.00
19.45
E


ATOM
5584
N
PHE
E
155
85.609
56.626
16.193
1.00
18.54
E


ATOM
5585
CA
PHE
E
155
85.940
56.784
14.779
1.00
19.04
E


ATOM
5586
CB
PHE
E
155
84.821
56.252
13.882
1.00
20.71
E


ATOM
5587
CG
PHE
E
155
84.524
54.794
14.060
1.00
23.03
E


ATOM
5588
CD1
PHE
E
155
83.492
54.375
14.898
1.00
23.94
E


ATOM
5589
CD2
PHE
E
155
85.255
53.837
13.365
1.00
23.32
E


ATOM
5590
CE1
PHE
E
155
83.189
53.017
15.037
1.00
23.82
E


ATOM
5591
CE2
PHE
E
155
84.962
52.476
13.497
1.00
24.46
E


ATOM
5592
CZ
PHE
E
155
83.930
52.068
14.333
1.00
24.51
E


ATOM
5593
C
PHE
E
155
86.109
58.265
14.459
1.00
19.30
E


ATOM
5594
O
PHE
E
155
85.791
59.134
15.275
1.00
19.12
E


ATOM
5595
N
GLN
E
156
86.613
58.550
13.265
1.00
17.46
E


ATOM
5596
CA
GLN
E
156
86.748
59.924
12.824
1.00
17.87
E


ATOM
5597
CB
GLN
E
156
88.081
60.546
13.264
1.00
19.74
E


ATOM
5598
CG
GLN
E
156
89.330
59.948
12.640
1.00
19.80
E


ATOM
5599
CD
GLN
E
156
90.551
60.785
12.950
1.00
21.46
E


ATOM
5600
OE1
GLN
E
156
90.660
61.928
12.503
1.00
21.30
E


ATOM
5601
NE2
GLN
E
156
91.469
60.230
13.734
1.00
21.38
E


ATOM
5602
C
GLN
E
156
86.629
59.989
11.316
1.00
17.47
E


ATOM
5603
O
GLN
E
156
86.856
58.999
10.616
1.00
17.25
E


ATOM
5604
N
ILE
E
157
86.252
61.159
10.823
1.00
17.46
E


ATOM
5605
CA
ILE
E
157
86.128
61.363
9.397
1.00
18.92
E


ATOM
5606
CB
ILE
E
157
84.746
60.922
8.898
1.00
19.57
E


ATOM
5607
CG2
ILE
E
157
83.659
61.774
9.545
1.00
15.09
E


ATOM
5608
CG1
ILE
E
157
84.704
60.994
7.369
1.00
21.06
E


ATOM
5609
CD1
ILE
E
157
83.541
60.218
6.756
1.00
22.57
E


ATOM
5610
C
ILE
E
157
86.349
62.837
9.083
1.00
20.28
E


ATOM
5611
O
ILE
E
157
85.887
63.712
9.808
1.00
20.70
E


ATOM
5612
N
LEU
E
158
87.094
63.104
8.019
1.00
21.79
E


ATOM
5613
CA
LEU
E
158
87.363
64.470
7.601
1.00
23.40
E


ATOM
5614
CB
LEU
E
158
88.869
64.706
7.466
1.00
25.42
E


ATOM
5615
CG
LEU
E
158
89.621
65.141
8.731
1.00
29.38
E


ATOM
5616
CD1
LEU
E
158
89.384
64.154
9.864
1.00
27.98
E


ATOM
5617
CD2
LEU
E
158
91.118
65.263
8.412
1.00
30.79
E


ATOM
5618
C
LEU
E
158
86.664
64.738
6.271
1.00
23.62
E


ATOM
5619
O
LEU
E
158
86.938
64.081
5.264
1.00
22.86
E


ATOM
5620
N
VAL
E
159
85.747
65.702
6.290
1.00
22.98
E


ATOM
5621
CA
VAL
E
159
84.990
66.087
5.112
1.00
21.37
E


ATOM
5622
CB
VAL
E
159
83.476
66.104
5.417
1.00
20.53
E


ATOM
5623
CG1
VAL
E
159
82.684
66.407
4.149
1.00
14.20
E


ATOM
5624
CG2
VAL
E
159
83.058
64.756
6.002
1.00
15.86
E


ATOM
5625
C
VAL
E
159
85.468
67.469
4.710
1.00
22.21
E


ATOM
5626
O
VAL
E
159
85.253
68.444
5.423
1.00
22.87
E


ATOM
5627
N
MET
E
160
86.116
67.539
3.555
1.00
25.37
E


ATOM
5628
CA
MET
E
160
86.681
68.779
3.049
1.00
27.07
E


ATOM
5629
CB
MET
E
160
88.088
68.494
2.533
1.00
29.57
E


ATOM
5630
CG
MET
E
160
88.996
67.954
3.633
1.00
35.17
E


ATOM
5631
SD
MET
E
160
90.519
67.185
3.065
1.00
41.54
E


ATOM
5632
CE
MET
E
160
90.011
65.462
2.985
1.00
40.10
E


ATOM
5633
C
MET
E
160
85.848
69.466
1.979
1.00
28.93
E


ATOM
5634
O
MET
E
160
85.191
68.817
1.162
1.00
28.47
E


ATOM
5635
N
LEU
E
161
85.875
70.793
1.997
1.00
29.41
E


ATOM
5636
CA
LEU
E
161
85.123
71.574
1.031
1.00
31.54
E


ATOM
5637
CB
LEU
E
161
83.931
72.258
1.708
1.00
30.26
E


ATOM
5638
CG
LEU
E
161
83.183
73.297
0.860
1.00
30.70
E


ATOM
5639
CD1
LEU
E
161
82.515
72.618
−0.332
1.00
29.72
E


ATOM
5640
CD2
LEU
E
161
82.145
74.020
1.728
1.00
31.55
E


ATOM
5641
C
LEU
E
161
85.990
72.625
0.363
1.00
32.10
E


ATOM
5642
O
LEU
E
161
86.575
73.473
1.029
1.00
32.90
E


ATOM
5643
N
GLU
E
162
86.063
72.549
−0.960
1.00
35.11
E


ATOM
5644
CA
GLU
E
162
86.820
73.491
−1.771
1.00
38.40
E


ATOM
5645
CB
GLU
E
162
87.191
72.838
−3.105
1.00
42.17
E


ATOM
5646
CG
GLU
E
162
87.783
73.776
−4.148
1.00
48.21
E


ATOM
5647
CD
GLU
E
162
89.099
74.381
−3.711
1.00
52.47
E


ATOM
5648
OE1
GLU
E
162
90.006
73.611
−3.327
1.00
54.02
E


ATOM
5649
OE2
GLU
E
162
89.228
75.627
−3.759
1.00
56.21
E


ATOM
5650
C
GLU
E
162
85.892
74.673
−2.008
1.00
39.06
E


ATOM
5651
O
GLU
E
162
84.750
74.490
−2.422
1.00
39.27
E


ATOM
5652
N
MET
E
163
86.369
75.884
−1.747
1.00
40.73
E


ATOM
5653
CA
MET
E
163
85.520
77.049
−1.938
1.00
43.18
E


ATOM
5654
CB
MET
E
163
84.546
77.171
−0.761
1.00
45.15
E


ATOM
5655
CG
MET
E
163
85.155
76.900
0.612
1.00
47.55
E


ATOM
5656
SD
MET
E
163
86.318
78.152
1.185
1.00
52.18
E


ATOM
5657
CE
MET
E
163
85.186
79.345
1.941
1.00
50.37
E


ATOM
5658
C
MET
E
163
86.245
78.371
−2.151
1.00
43.77
E


ATOM
5659
O
MET
E
163
87.458
78.477
−1.953
1.00
41.87
E


ATOM
5660
N
THR
E
164
85.474
79.371
−2.571
1.00
45.83
E


ATOM
5661
CA
THR
E
164
85.981
80.714
−2.827
1.00
49.20
E


ATOM
5662
CB
THR
E
164
85.585
81.177
−4.241
1.00
50.11
E


ATOM
5663
OG1
THR
E
164
86.036
80.208
−5.199
1.00
49.28
E


ATOM
5664
CG2
THR
E
164
86.204
82.535
−4.559
1.00
50.19
E


ATOM
5665
C
THR
E
164
85.371
81.652
−1.785
1.00
51.14
E


ATOM
5666
O
THR
E
164
84.169
81.916
−1.802
1.00
50.64
E


ATOM
5667
N
PRO
E
165
86.198
82.170
−0.864
1.00
53.75
E


ATOM
5668
CD
PRO
E
165
87.667
82.057
−0.818
1.00
54.65
E


ATOM
5669
CA
PRO
E
165
85.719
83.072
0.185
1.00
56.16
E


ATOM
5670
CB
PRO
E
165
86.965
83.299
1.036
1.00
55.47
E


ATOM
5671
CG
PRO
E
165
88.057
83.262
0.019
1.00
55.93
E


ATOM
5672
C
PRO
E
165
85.098
84.381
−0.291
1.00
58.83
E


ATOM
5673
O
PRO
E
165
85.673
85.100
−1.112
1.00
58.35
E


ATOM
5674
N
GLN
E
166
83.912
84.666
0.239
1.00
61.77
E


ATOM
5675
CA
GLN
E
166
83.173
85.885
−0.065
1.00
63.96
E


ATOM
5676
CB
GLN
E
166
82.103
85.616
−1.123
1.00
64.28
E


ATOM
5677
CG
GLN
E
166
82.662
85.236
−2.481
1.00
66.42
E


ATOM
5678
CD
GLN
E
166
81.643
85.392
−3.596
1.00
67.38
E


ATOM
5679
OE1
GLN
E
166
81.937
85.124
−4.761
1.00
68.28
E


ATOM
5680
NE2
GLN
E
166
80.437
85.832
−3.244
1.00
66.50
E


ATOM
5681
C
GLN
E
166
82.521
86.396
1.223
1.00
65.40
E


ATOM
5682
O
GLN
E
166
81.974
85.614
2.007
1.00
65.65
E


ATOM
5683
N
ARG
E
167
82.589
87.707
1.444
1.00
65.80
E


ATOM
5684
CA
ARG
E
167
82.017
88.302
2.647
1.00
65.27
E


ATOM
5685
CB
ARG
E
167
82.353
89.795
2.706
1.00
67.87
E


ATOM
5686
CG
ARG
E
167
82.221
90.423
4.095
1.00
70.91
E


ATOM
5687
CD
ARG
E
167
83.216
89.813
5.085
1.00
73.36
E


ATOM
5688
NE
ARG
E
167
83.244
90.532
6.359
1.00
75.19
E


ATOM
5689
CZ
ARG
E
167
84.012
90.199
7.394
1.00
75.48
E


ATOM
5690
NH1
ARG
E
167
84.824
89.151
7.318
1.00
75.50
E


ATOM
5691
NH2
ARG
E
167
83.968
90.916
8.509
1.00
75.83
E


ATOM
5692
C
ARG
E
167
80.504
88.100
2.684
1.00
63.81
E


ATOM
5693
O
ARG
E
167
79.816
88.254
1.672
1.00
62.94
E


ATOM
5694
N
GLY
E
168
79.991
87.751
3.860
1.00
61.88
E


ATOM
5695
CA
GLY
E
168
78.567
87.519
4.004
1.00
58.78
E


ATOM
5696
C
GLY
E
168
78.243
86.036
3.959
1.00
57.24
E


ATOM
5697
O
GLY
E
168
77.262
85.594
4.558
1.00
57.26
E


ATOM
5698
N
ASP
E
169
79.066
85.263
3.249
1.00
54.67
E


ATOM
5699
CA
ASP
E
169
78.849
83.823
3.140
1.00
52.07
E


ATOM
5700
CB
ASP
E
169
79.799
83.186
2.116
1.00
52.03
E


ATOM
5701
CG
ASP
E
169
79.329
83.359
0.683
1.00
52.57
E


ATOM
5702
OD1
ASP
E
169
78.105
83.453
0.457
1.00
51.86
E


ATOM
5703
OD2
ASP
E
169
80.188
83.376
−0.223
1.00
52.34
E


ATOM
5704
C
ASP
E
169
79.027
83.096
4.463
1.00
49.54
E


ATOM
5705
O
ASP
E
169
79.993
83.322
5.196
1.00
49.84
E


ATOM
5706
N
VAL
E
170
78.082
82.214
4.758
1.00
46.54
E


ATOM
5707
CA
VAL
E
170
78.136
81.418
5.970
1.00
43.15
E


ATOM
5708
CB
VAL
E
170
76.903
81.669
6.871
1.00
42.70
E


ATOM
5709
CG1
VAL
E
170
76.997
80.819
8.138
1.00
41.36
E


ATOM
5710
CG2
VAL
E
170
76.814
83.146
7.227
1.00
41.14
E


ATOM
5711
C
VAL
E
170
78.172
79.948
5.555
1.00
41.66
E


ATOM
5712
O
VAL
E
170
77.216
79.432
4.972
1.00
40.25
E


ATOM
5713
N
TYR
E
171
79.289
79.287
5.833
1.00
39.16
E


ATOM
5714
CA
TYR
E
171
79.438
77.877
5.502
1.00
38.16
E


ATOM
5715
CB
TYR
E
171
80.836
77.617
4.953
1.00
38.66
E


ATOM
5716
CG
TYR
E
171
81.035
78.237
3.598
1.00
38.98
E


ATOM
5717
CD1
TYR
E
171
80.740
77.522
2.440
1.00
38.79
E


ATOM
5718
CE1
TYR
E
171
80.852
78.105
1.186
1.00
40.42
E


ATOM
5719
CD2
TYR
E
171
81.451
79.561
3.471
1.00
38.62
E


ATOM
5720
CE2
TYR
E
171
81.565
80.160
2.219
1.00
40.32
E


ATOM
5721
CZ
TYR
E
171
81.262
79.424
1.079
1.00
41.26
E


ATOM
5722
OH
TYR
E
171
81.350
80.004
−0.166
1.00
42.98
E


ATOM
5723
C
TYR
E
171
79.206
77.076
6.764
1.00
37.15
E


ATOM
5724
O
TYR
E
171
79.755
77.398
7.813
1.00
37.94
E


ATOM
5725
N
THR
E
172
78.384
76.037
6.672
1.00
35.12
E


ATOM
5726
CA
THR
E
172
78.091
75.229
7.842
1.00
34.42
E


ATOM
5727
CB
THR
E
172
76.654
75.496
8.367
1.00
35.21
E


ATOM
5728
OG1
THR
E
172
76.184
74.351
9.094
1.00
35.96
E


ATOM
5729
CG2
THR
E
172
75.706
75.790
7.226
1.00
38.35
E


ATOM
5730
C
THR
E
172
78.263
73.734
7.638
1.00
32.90
E


ATOM
5731
O
THR
E
172
77.875
73.188
6.604
1.00
31.57
E


ATOM
5732
N
CYS
E
173
78.858
73.090
8.643
1.00
30.59
E


ATOM
5733
CA
CYS
E
173
79.078
71.646
8.640
1.00
29.35
E


ATOM
5734
C
CYS
E
173
77.923
71.058
9.454
1.00
29.72
E


ATOM
5735
O
CYS
E
173
77.771
71.337
10.645
1.00
28.89
E


ATOM
5736
CB
CYS
E
173
80.424
71.299
9.287
1.00
27.53
E


ATOM
5737
SG
CYS
E
173
80.875
69.541
9.133
1.00
27.81
E


ATOM
5738
N
HIS
E
174
77.109
70.251
8.788
1.00
28.95
E


ATOM
5739
CA
HIS
E
174
75.925
69.642
9.381
1.00
28.54
E


ATOM
5740
CB
HIS
E
174
74.770
69.881
8.399
1.00
29.66
E


ATOM
5741
CG
HIS
E
174
73.457
69.311
8.823
1.00
30.98
E


ATOM
5742
CD2
HIS
E
174
72.367
69.899
9.369
1.00
31.91
E


ATOM
5743
ND1
HIS
E
174
73.124
67.988
8.630
1.00
31.68
E


ATOM
5744
CE1
HIS
E
174
71.883
67.785
9.034
1.00
33.26
E


ATOM
5745
NE2
HIS
E
174
71.401
68.929
9.487
1.00
34.66
E


ATOM
5746
C
HIS
E
174
76.173
68.151
9.650
1.00
27.83
E


ATOM
5747
O
HIS
E
174
76.438
67.375
8.728
1.00
27.35
E


ATOM
5748
N
VAL
E
175
76.085
67.753
10.917
1.00
26.27
E


ATOM
5749
CA
VAL
E
175
76.349
66.365
11.284
1.00
26.34
E


ATOM
5750
CB
VAL
E
175
77.584
66.281
12.215
1.00
23.90
E


ATOM
5751
CG1
VAL
E
175
77.807
64.850
12.663
1.00
19.67
E


ATOM
5752
CG2
VAL
E
175
78.818
66.813
11.491
1.00
19.93
E


ATOM
5753
C
VAL
E
175
75.199
65.603
11.938
1.00
27.67
E


ATOM
5754
O
VAL
E
175
74.587
66.064
12.904
1.00
26.77
E


ATOM
5755
N
GLU
E
176
74.917
64.423
11.399
1.00
29.83
E


ATOM
5756
CA
GLU
E
176
73.864
63.564
11.929
1.00
32.99
E


ATOM
5757
CB
GLU
E
176
72.842
63.231
10.839
1.00
34.86
E


ATOM
5758
CG
GLU
E
176
72.076
64.441
10.319
1.00
40.13
E


ATOM
5759
CD
GLU
E
176
71.204
64.107
9.124
1.00
44.38
E


ATOM
5760
OE1
GLU
E
176
70.292
63.265
9.269
1.00
46.31
E


ATOM
5761
OE2
GLU
E
176
71.433
64.682
8.037
1.00
47.49
E


ATOM
5762
C
GLU
E
176
74.526
62.289
12.445
1.00
32.24
E


ATOM
5763
O
GLU
E
176
75.296
61.646
11.734
1.00
32.81
E


ATOM
5764
N
HIS
E
177
74.220
61.934
13.686
1.00
31.66
E


ATOM
5765
CA
HIS
E
177
74.803
60.761
14.311
1.00
30.50
E


ATOM
5766
CB
HIS
E
177
76.147
61.161
14.927
1.00
29.59
E


ATOM
5767
CG
HIS
E
177
76.871
60.034
15.582
1.00
28.23
E


ATOM
5768
CD2
HIS
E
177
77.752
59.134
15.086
1.00
28.22
E


ATOM
5769
ND1
HIS
E
177
76.679
59.698
16.903
1.00
27.71
E


ATOM
5770
CE1
HIS
E
177
77.410
58.636
17.194
1.00
29.83
E


ATOM
5771
NE2
HIS
E
177
78.070
58.274
16.108
1.00
29.78
E


ATOM
5772
C
HIS
E
177
73.854
60.195
15.373
1.00
30.09
E


ATOM
5773
O
HIS
E
177
73.189
60.942
16.083
1.00
29.91
E


ATOM
5774
N
PRO
E
178
73.781
58.862
15.496
1.00
31.45
E


ATOM
5775
CD
PRO
E
178
74.485
57.842
14.697
1.00
31.00
E


ATOM
5776
CA
PRO
E
178
72.898
58.226
16.481
1.00
31.44
E


ATOM
5777
CB
PRO
E
178
73.370
56.779
16.467
1.00
30.89
E


ATOM
5778
CG
PRO
E
178
73.704
56.578
15.028
1.00.
31.16
E


ATOM
5779
C
PRO
E
178
72.896
58.826
17.893
1.00
31.78
E


ATOM
5780
O
PRO
E
178
71.903
58.727
18.611
1.00
32.84
E


ATOM
5781
N
SER
E
179
73.996
59.448
18.292
1.00
30.31
E


ATOM
5782
CA
SER
E
179
74.087
60.039
19.624
1.00
30.84
E


ATOM
5783
CB
SER
E
179
75.552
60.155
20.038
1.00
29.11
E


ATOM
5784
OG
SER
E
179
76.240
61.049
19.176
1.00
24.79
E


ATOM
5785
C
SER
E
179
73.452
61.424
19.717
1.00
32.75
E


ATOM
5786
O
SER
E
179
73.330
61.982
20.804
1.00
32.78
E


ATOM
5787
N
LEU
E
180
73.046
61.981
18.583
1.00
35.18
E


ATOM
5788
CA
LEU
E
180
72.477
63.317
18.578
1.00
37.31
E


ATOM
5789
CB
LEU
E
180
73.098
64.132
17.448
1.00
35.77
E


ATOM
5790
CG
LEU
E
180
74.610
64.337
17.528
1.00
36.46
E


ATOM
5791
CD1
LEU
E
180
75.097
65.018
16.259
1.00
35.16
E


ATOM
5792
CD2
LEU
E
180
74.948
65.167
18.752
1.00
34.58
E


ATOM
5793
C
LEU
E
180
70.967
63.405
18.463
1.00
40.35
E


ATOM
5794
O
LEU
E
180
70.386
63.003
17.456
1.00
40.67
E


ATOM
5795
N
GLN
E
181
70.338
63.943
19.503
1.00
42.97
E


ATOM
5796
CA
GLN
E
181
68.895
64.141
19.504
1.00
45.09
E


ATOM
5797
CB
GLN
E
181
68.466
64.877
20.776
1.00
46.73
E


ATOM
5798
CG
GLN
E
181
69.471
65.931
21.235
1.00
49.84
E


ATOM
5799
CD
GLN
E
181
68.898
66.904
22.256
1.00
52.17
E


ATOM
5800
OE1
GLN
E
181
68.074
67.760
21.920
1.00
52.91
E


ATOM
5801
NE2
GLN
E
181
69.329
66.774
23.510
1.00
51.73
E


ATOM
5802
C
GLN
E
181
68.607
65.002
18.277
1.00
45.26
E


ATOM
5803
O
GLN
E
181
67.660
64.752
17.530
1.00
46.25
E


ATOM
5804
N
SER
E
182
69.448
66.013
18.078
1.00
44.33
E


ATOM
5805
CA
SER
E
182
69.335
66.923
16.943
1.00
42.52
E


ATOM
5806
CB
SER
E
182
68.819
68.291
17.401
1.00
43.41
E


ATOM
5807
OG
SER
E
182
69.658
68.853
18.396
1.00
43.07
E


ATOM
5808
C
SER
E
182
70.725
67.068
16.337
1.00
41.70
E


ATOM
5809
O
SER
E
182
71.726
66.955
17.040
1.00
39.94
E


ATOM
5810
N
PRO
E
183
70.805
67.330
15.023
1.00
41.57
E


ATOM
5811
CD
PRO
E
183
69.680
67.554
14.098
1.00
41.72
E


ATOM
5812
CA
PRO
E
183
72.087
67.485
14.326
1.00
40.68
E


ATOM
5813
CB
PRO
E
183
71.669
67.638
12.865
1.00
40.95
E


ATOM
5814
CG
PRO
E
183
70.344
68.309
12.965
1.00
42.76
E


ATOM
5815
C
PRO
E
183
72.988
68.628
14.790
1.00
38.81
E


ATOM
5816
O
PRO
E
183
72.520
69.709
15.142
1.00
39.64
E


ATOM
5817
N
ILE
E
184
74.291
68.370
14.785
1.00
37.31
E


ATOM
5818
CA
ILE
E
184
75.270
69.368
15.177
1.00
34.30
E


ATOM
5819
CB
ILE
E
184
76.570
68.728
15.699
1.00
33.43
E


ATOM
5820
CG2
ILE
E
184
77.671
69.779
15.766
1.00
32.87
E


ATOM
5821
CG1
ILE
E
184
76.337
68.112
17.076
1.00
33.53
E


ATOM
5822
CD1
ILE
E
184
77.530
67.339
17.604
1.00
33.29
E


ATOM
5823
C
ILE
E
184
75.625
70.216
13.974
1.00
33.68
E


ATOM
5824
O
ILE
E
184
75.851
69.704
12.882
1.00
33.87
E


ATOM
5825
N
THR
E
185
75.676
71.521
14.181
1.00
34.19
E


ATOM
5826
CA
THR
E
185
76.018
72.431
13.111
1.00
33.39
E


ATOM
5827
CB
THR
E
185
74.792
73.230
12.637
1.00
33.77
E


ATOM
5828
OG1
THR
E
185
74.211
73.918
13.751
1.00
33.46
E


ATOM
5829
CG2
THR
E
185
73.758
72.297
12.016
1.00
33.35
E


ATOM
5830
C
THR
E
185
77.081
73.396
13.590
1.00
33.01
E


ATOM
5831
O
THR
E
185
76.990
73.966
14.679
1.00
33.25
E


ATOM
5832
N
VAL
E
186
78.106
73.552
12.770
1.00
32.85
E


ATOM
5833
CA
VAL
E
186
79.197
74.453
13.067
1.00
32.84
E


ATOM
5834
CB
VAL
E
186
80.503
73.684
13.300
1.00
31.58
E


ATOM
5835
CG1
VAL
E
186
81.629
74.651
13.611
1.00
30.07
E


ATOM
5836
CG2
VAL
E
186
80.316
72.697
14.441
1.00
30.84
E


ATOM
5837
C
VAL
E
186
79.329
75.317
11.836
1.00
34.14
E


ATOM
5838
O
VAL
E
186
79.403
74.812
10.719
1.00
33.50
E


ATOM
5839
N
GLU
E
187
79.329
76.626
12.029
1.00
38.05
E


ATOM
5840
CA
GLU
E
187
79.453
77.522
10.898
1.00
40.60
E


ATOM
5841
CB
GLU
E
187
78.358
78.592
10.934
1.00
43.36
E


ATOM
5842
CG
GLU
E
187
78.426
79.531
12.121
1.00
47.46
E


ATOM
5843
CD
GLU
E
187
77.657
80.822
11.886
1.00
51.49
E


ATOM
5844
OE1
GLU
E
187
76.452
80.752
11.551
1.00
52.89
E


ATOM
5845
OE2
GLU
E
187
78.262
81.908
12.039
1.00
53.48
E


ATOM
5846
C
GLU
E
187
80.819
78.182
10.877
1.00
40.49
E


ATOM
5847
O
GLU
E
187
81.496
78.285
11.901
1.00
40.26
E


ATOM
5848
N
TRP
E
188
81.221
78.610
9.688
1.00
41.52
E


ATOM
5849
CA
TRP
E
188
82.492
79.284
9.488
1.00
43.59
E


ATOM
5850
CB
TRP
E
188
83.498
78.337
8.834
1.00
41.24
E


ATOM
5851
CG
TRP
E
188
84.852
78.942
8.675
1.00
41.34
E


ATOM
5852
CD2
TRP
E
188
85.327
79.672
7.543
1.00
40.23
E


ATOM
5853
CE2
TRP
E
188
86.642
80.090
7.838
1.00
41.87
E


ATOM
5854
CE3
TRP
E
188
84.768
80.015
6.305
1.00
40.90
E


ATOM
5855
CD1
TRP
E
188
85.867
78.945
9.588
1.00
41.88
E


ATOM
5856
NE1
TRP
E
188
86.947
79.632
9.093
1.00
41.99
E


ATOM
5857
CZ2
TRP
E
188
87.411
80.835
6.938
1.00
42.93
E


ATOM
5858
CZ3
TRP
E
188
85.531
80.757
5.408
1.00
42.58
E


ATOM
5859
CH2
TRP
E
188
86.839
81.159
5.731
1.00
43.65
E


ATOM
5860
C
TRP
E
188
82.198
80.467
8.566
1.00
46.04
E


ATOM
5861
O
TRP
E
188
81.335
80.374
7.688
1.00
45.30
E


ATOM
5862
N
ARG
E
189
82.899
81.579
8.765
1.00
50.26
E


ATOM
5863
CA
ARG
E
189
82.673
82.761
7.936
1.00
54.31
E


ATOM
5864
CB
ARG
E
189
81.980
83.855
8.755
1.00
56.19
E


ATOM
5865
CG
ARG
E
189
82.820
84.460
9.880
1.00
59.58
E


ATOM
5866
CD
ARG
E
189
83.030
83.499
11.045
1.00
63.51
E


ATOM
5867
NE
ARG
E
189
83.580
84.180
12.218
1.00
66.73
E


ATOM
5868
CZ
ARG
E
189
84.771
84.771
12.255
1.00
68.44
E


ATOM
5869
NH1
ARG
E
189
85.553
84.766
11.183
1.00
69.41
E


ATOM
5870
NH2
ARG
E
189
85.178
85.378
13.363
1.00
70.13
E


ATOM
5871
C
ARG
E
189
83.950
83.322
7.313
1.00
55.74
E


ATOM
5872
O
ARG
E
189
85.043
83.182
7.866
1.00
56.16
E


ATOM
5873
N
ALA
E
190
83.796
83.962
6.156
1.00
58.53
E


ATOM
5874
CA
ALA
E
190
84.920
84.557
5.435
1.00
60.08
E


ATOM
5875
CB
ALA
E
190
84.550
84.734
3.964
1.00
59.97
E


ATOM
5876
C
ALA
E
190
85.335
85.905
6.036
1.00
61.01
E


ATOM
5877
O
ALA
E
190
84.654
86.378
6.971
1.00
62.25
E


ATOM
5878
OXT
ALA
E
190
86.338
86.479
5.558
1.00
61.85
E


ATOM
5879
C
LEU
F
1
78.718
38.094
33.366
1.00
32.03
F


ATOM
5880
O
LEU
F
1
79.818
38.571
33.658
1.00
30.77
F


ATOM
5881
N
LEU
F
1
76.219
38.100
33.307
1.00
33.21
F


ATOM
5882
CA
LEU
F
1
77.432
38.678
33.953
1.00
32.59
F


ATOM
5883
N
GLN
F
2
78.578
37.069
32.531
1.00
30.39
F


ATOM
5884
CA
GLN
F
2
79.744
36.436
31.936
1.00
28.84
F


ATOM
5885
C
GLN
F
2
79.609
36.081
30.462
1.00
27.93
F


ATOM
5886
O
GLN
F
2
78.741
35.308
30.067
1.00
27.68
F


ATOM
5887
N
PRO
F
3
80.463
36.663
29.619
1.00
28.02
F


ATOM
5888
CD
PRO
F
3
81.461
37.720
29.856
1.00
28.68
F


ATOM
5889
CA
PRO
F
3
80.370
36.332
28.198
1.00
27.76
F


ATOM
5890
CB
PRO
F
3
81.363
37.298
27.552
1.00
28.01
F


ATOM
5891
CG
PRO
F
3
82.353
37.575
28.660
1.00
28.41
F


ATOM
5892
C
PRO
F
3
80.774
34.872
28.030
1.00
27.24
F


ATOM
5893
O
PRO
F
3
81.698
34.406
28.698
1.00
27.18
F


ATOM
5894
N
PHE
F
4
80.082
34.144
27.159
1.00
25.22
F


ATOM
5895
CA
PHE
F
4
80.409
32.738
26.943
1.00
24.75
F


ATOM
5896
CB
PHE
F
4
79.135
31.905
26.849
1.00
25.85
F


ATOM
5897
CG
PHE
F
4
79.272
30.539
27.446
1.00
31.58
F


ATOM
5898
CD1
PHE
F
4
79.435
30.384
28.823
1.00
33.24
F


ATOM
5899
CD2
PHE
F
4
79.241
29.404
26.639
1.00
32.15
F


ATOM
5900
CE1
PHE
F
4
79.561
29.116
29.386
1.00
33.28
F


ATOM
5901
CE2
PHE
F
4
79.364
28.136
27.187
1.00
33.29
F


ATOM
5902
CZ
PHE
F
4
79.524
27.989
28.565
1.00
34.18
F


ATOM
5903
C
PHE
F
4
81.227
32.588
25.664
1.00
22.43
F


ATOM
5904
O
PHE
F
4
80.759
32.919
24.586
1.00
24.59
F


ATOM
5905
N
PRO
F
5
82.460
32.065
25.771
1.00
22.79
F


ATOM
5906
CD
PRO
F
5
83.191
31.820
27.029
1.00
21.18
F


ATOM
5907
CA
PRO
F
5
83.349
31.882
24.618
1.00
21.18
F


ATOM
5908
CB
PRO
F
5
84.715
32.140
25.218
1.00
20.19
F


ATOM
5909
CG
PRO
F
5
84.587
31.450
26.544
1.00
20.99
F


ATOM
5910
C
PRO
F
5
83.291
30.524
23.949
1.00
20.28
F


ATOM
5911
O
PRO
F
5
82.796
29.559
24.521
1.00
19.48
F


ATOM
5912
N
GLN
F
6
83.818
30.456
22.730
1.00
21.24
F


ATOM
5913
CA
GLN
F
6
83.848
29.200
21.983
1.00
19.98
F


ATOM
5914
CB
GLN
F
6
83.665
29.450
20.484
1.00
18.71
F


ATOM
5915
CG
GLN
F
6
82.312
30.010
20.048
1.00
18.35
F


ATOM
5916
CD
GLN
F
6
82.255
30.247
18.537
1.00
22.29
F


ATOM
5917
OE1
GLN
F
6
82.612
29.368
17.740
1.00
21.53
F


ATOM
5918
NE2
GLN
F
6
81.802
31.429
18.138
1.00
20.02
F


ATOM
5919
C
GLN
F
6
85.213
28.548
22.213
1.00
20.47
F


ATOM
5920
O
GLN
F
6
86.243
29.204
22.099
1.00
18.48
F


ATOM
5921
N
PRO
F
7
85.229
27.256
22.575
1.00
21.16
F


ATOM
5922
CD
PRO
F
7
84.071
26.494
23.084
1.00
20.59
F


ATOM
5923
CA
PRO
F
7
86.471
26.520
22.813
1.00
21.61
F


ATOM
5924
CB
PRO
F
7
86.037
25.444
23.797
1.00
23.40
F


ATOM
5925
CG
PRO
F
7
84.649
25.123
23.311
1.00
19.67
F


ATOM
5926
C
PRO
F
7
86.996
25.897
21.521
1.00
23.00
F


ATOM
5927
O
PRO
F
7
86.219
25.601
20.610
1.00
23.19
F


ATOM
5928
N
GLU
F
8
88.312
25.714
21.438
1.00
21.78
F


ATOM
5929
CA
GLU
F
8
88.904
25.068
20.279
1.00
23.12
F


ATOM
5930
CB
GLU
F
8
90.297
25.632
19.968
1.00
24.50
F


ATOM
5931
CG
GLU
F
8
91.086
24.834
18.915
1.00
26.16
F


ATOM
5932
CD
GLU
F
8
90.360
24.697
17.576
1.00
31.57
F


ATOM
5933
OE1
GLU
F
8
89.250
24.114
17.540
1.00
33.65
F


ATOM
5934
OE2
GLU
F
8
90.903
25.171
16.555
1.00
30.66
F


ATOM
5935
C
GLU
F
8
89.005
23.608
20.680
1.00
22.95
F


ATOM
5936
O
GLU
F
8
89.289
23.292
21.833
1.00
23.25
F


ATOM
5937
N
LEU
F
9
88.756
22.712
19.741
1.00
24.74
F


ATOM
5938
CA
LEU
F
9
88.815
21.292
20.047
1.00
27.30
F


ATOM
5939
CB
LEU
F
9
87.729
20.549
19.272
1.00
25.73
F


ATOM
5940
CG
LEU
F
9
86.302
21.051
19.494
1.00
29.20
F


ATOM
5941
CD1
LEU
F
9
85.338
20.235
18.645
1.00
28.18
F


ATOM
5942
CD2
LEU
F
9
85.938
20.943
20.967
1.00
29.61
F


ATOM
5943
C
LEU
F
9
90.178
20.707
19.712
1.00
28.17
F


ATOM
5944
O
LEU
F
9
90.715
20.940
18.631
1.00
26.94
F


ATOM
5945
N
PRO
F
10
90.765
19.947
20.647
1.00
30.38
F


ATOM
5946
CD
PRO
F
10
90.365
19.707
22.044
1.00
30.47
F


ATOM
5947
CA
PRO
F
10
92.076
19.355
20.370
1.00
34.24
F


ATOM
5948
CB
PRO
F
10
92.556
18.915
21.752
1.00
32.97
F


ATOM
5949
CG
PRO
F
10
91.282
18.561
22.448
1.00
31.98
F


ATOM
5950
C
PRO
F
10
91.985
18.188
19.393
1.00
35.94
F


ATOM
5951
O
PRO
F
10
90.993
17.461
19.376
1.00
38.70
F


ATOM
5952
N
TYR
F
11
93.016
18.031
18.570
1.00
37.40
F


ATOM
5953
CA
TYR
F
11
93.075
16.936
17.609
1.00
38.84
F


ATOM
5954
CB
TYR
F
11
92.126
17.176
16.434
1.00
38.73
F


ATOM
5955
CG
TYR
F
11
92.017
15.969
15.539
1.00
39.56
F


ATOM
5956
CD1
TYR
F
11
91.294
14.848
15.942
1.00
39.88
F


ATOM
5957
CE1
TYR
F
11
91.254
13.697
15.164
1.00
39.49
F


ATOM
5958
CD2
TYR
F
11
92.698
15.913
14.327
1.00
39.73
F


ATOM
5959
CE2
TYR
F
11
92.668
14.765
13.537
1.00
40.44
F


ATOM
5960
CZ
TYR
F
11
91.945
13.659
13.964
1.00
40.29
F


ATOM
5961
OH
TYR
F
11
91.921
12.514
13.200
1.00
40.03
F


ATOM
5962
C
TYR
F
11
94.498
16.781
17.077
1.00
40.23
F


ATOM
5963
O
TYR
F
11
95.102
15.708
17.300
1.00
41.88
F


ATOM
5964
OXT
TYR
F
11
94.988
17.742
16.443
1.00
40.58
F


ATOM
5965
O
HOH
H
1
37.560
11.197
17.272
1.00
17.47
H


ATOM
5966
O
HOH
H
2
81.295
26.543
20.573
1.00
15.95
H


ATOM
5967
O
HOH
H
3
43.884
23.627
16.726
1.00
14.83
H


ATOM
5968
O
HOH
H
4
89.230
61.015
16.512
1.00
19.10
H


ATOM
5969
O
HOH
H
5
92.090
40.877
18.768
1.00
15.59
H


ATOM
5970
O
HOH
H
6
57.686
14.054
4.407
1.00
20.02
H


ATOM
5971
O
HOH
H
7
87.607
31.423
22.217
1.00
11.29
H


ATOM
5972
O
HOH
H
8
31.815
41.479
5.673
1.00
23.91
H


ATOM
5973
O
HOH
H
9
46.112
3.594
18.714
1.00
20.15
H


ATOM
5974
O
HOH
H
10
86.724
67.786
15.551
1.00
22.39
H


ATOM
5975
O
HOH
H
11
42.599
14.833
17.213
1.00
16.12
H


ATOM
5976
O
HOH
H
12
93.679
37.081
11.737
1.00
15.03
H


ATOM
5977
O
HOH
H
13
50.288
0.581
25.262
1.00
13.69
H


ATOM
5978
O
HOH
H
14
96.256
37.853
25.291
1.00
12.90
H


ATOM
5979
O
HOH
H
15
90.711
30.936
37.307
1.00
31.88
H


ATOM
5980
O
HOH
H
16
80.045
39.846
25.144
1.00
33.11
H


ATOM
5981
O
HOH
H
17
80.708
45.662
11.514
1.00
41.56
H


ATOM
5982
O
HOH
H
18
42.215
0.119
11.193
1.00
15.83
H


ATOM
5983
O
HOH
H
19
95.828
50.485
5.930
1.00
27.67
H


ATOM
5984
O
HOH
H
20
48.809
37.278
14.928
1.00
36.10
H


ATOM
5985
O
HOH
H
21
47.553
−0.403
11.823
1.00
14.62
H


ATOM
5986
O
HOH
H
22
94.554
76.132
19.122
1.00
83.80
H


ATOM
5987
O
HOH
H
23
83.295
48.460
17.328
1.00
17.64
H


ATOM
5988
O
HOH
H
24
88.976
42.102
7.818
1.00
26.11
H


ATOM
5989
O
HOH
H
25
99.041
56.322
24.823
1.00
24.86
H


ATOM
5990
O
HOH
H
26
47.640
0.006
20.312
1.00
18.95
H


ATOM
5991
O
HOH
H
27
46.987
29.359
11.916
1.00
21.84
H


ATOM
5992
O
HOH
H
28
88.283
37.229
11.279
1.00
21.34
H


ATOM
5993
O
HOH
H
29
49.878
−9.043
36.424
1.00
32.47
H


ATOM
5994
O
HOH
H
30
82.777
39.366
24.935
1.00
24.79
H


ATOM
5995
O
HOH
H
31
72.919
25.704
15.123
1.00
18.09
H


ATOM
5996
O
HOH
H
32
86.830
25.153
13.558
1.00
24.14
H


ATOM
5997
O
HOH
H
33
43.152
5.651
13.774
1.00
19.96
H


ATOM
5998
O
HOH
H
34
100.654
27.732
5.367
1.00
34.73
H


ATOM
5999
O
HOH
H
35
48.550
32.122
26.894
1.00
20.17
H


ATOM
6000
O
HOH
H
36
78.728
36.578
6.822
1.00
32.92
H


ATOM
6001
O
HOH
H
37
89.361
11.980
24.953
1.00
51.75
H


ATOM
6002
O
HOH
H
38
90.411
24.657
31.926
1.00
28.29
H


ATOM
6003
O
HOH
H
39
80.690
24.233
8.462
1.00
22.43
H


ATOM
6004
O
HOH
H
40
83.769
65.973
−5.489
1.00
21.06
H


ATOM
6005
O
HOH
H
41
87.710
34.692
7.008
1.00
22.47
H


ATOM
6006
O
HOH
H
42
38.997
4.521
15.299
1.00
25.36
H


ATOM
6007
O
HOH
H
43
94.223
46.644
24.674
1.00
32.67
H


ATOM
6008
O
HOH
H
44
35.150
15.757
26.294
1.00
29.03
H


ATOM
6009
O
HOH
H
45
85.059
24.652
18.280
1.00
25.63
H


ATOM
6010
O
HOH
H
46
67.739
6.320
18.991
1.00
43.67
H


ATOM
6011
O
HOH
H
47
92.376
63.977
12.866
1.00
32.46
H


ATOM
6012
O
HOH
H
48
91.526
49.479
22.504
1.00
29.70
H


ATOM
6013
O
HOH
H
49
56.333
−2.088
24.733
1.00
28.53
H


ATOM
6014
O
HOH
H
50
100.482
53.937
3.942
1.00
52.26
H


ATOM
6015
O
HOH
H
51
48.244
18.753
22.918
1.00
44.88
H


ATOM
6016
O
HOH
H
52
32.577
−0.558
6.769
1.00
33.70
H


ATOM
6017
O
HOH
H
53
47.162
26.527
12.972
1.00
29.72
H


ATOM
6018
O
HOH
H
54
98.621
66.834
5.100
1.00
52.20
H


ATOM
6019
O
HOH
H
55
88.106
52.134
17.293
1.00
21.13
H


ATOM
6020
O
HOH
H
56
59.655
31.307
17.069
1.00
25.89
H


ATOM
6021
O
HOH
H
57
73.562
24.323
12.997
1.00
23.51
H


ATOM
6022
O
HOH
H
58
43.748
32.725
20.165
1.00
52.72
H


ATOM
6023
O
HOH
H
59
26.392
−7.072
11.400
1.00
26.20
H


ATOM
6024
O
HOH
H
60
83.955
73.751
16.805
1.00
18.19
H


ATOM
6025
O
HOH
H
61
46.229
−19.766
10.675
1.00
28.79
H


ATOM
6026
O
HOH
H
62
52.436
38.720
16.630
1.00
28.35
H


ATOM
6027
O
HOH
H
63
60.555
9.392
19.914
1.00
28.43
H


ATOM
6028
O
HOH
H
64
62.105
2.197
11.948
1.00
33.33
H


ATOM
6029
O
HOH
H
65
40.514
−12.059
13.631
1.00
21.32
H


ATOM
6030
O
HOH
H
66
65.876
23.972
14.155
1.00
21.11
H


ATOM
6031
O
HOH
H
67
84.702
18.013
5.666
1.00
19.12
H


ATOM
6032
O
HOH
H
68
64.715
11.655
15.936
1.00
28.72
H


ATOM
6033
O
HOH
H
69
85.418
74.949
14.820
1.00
27.90
H


ATOM
6034
O
HOH
H
70
77.974
25.419
23.038
1.00
42.15
H


ATOM
6035
O
HOH
H
71
65.805
8.484
20.741
1.00
44.01
H


ATOM
6036
O
HOH
H
72
51.276
26.045
10.800
1.00
28.36
H


ATOM
6037
O
HOH
H
73
65.226
22.195
25.831
1.00
36.11
H


ATOM
6038
O
HOH
H
74
101.567
46.068
1.107
1.00
53.81
H


ATOM
6039
O
HOH
H
75
32.615
31.234
1.517
1.00
21.03
H


ATOM
6040
O
HOH
H
76
42.100
−0.001
13.802
1.00
23.44
H


ATOM
6041
O
HOH
H
77
35.124
40.614
14.668
1.00
27.61
H


ATOM
6042
O
HOH
H
78
92.548
46.813
7.595
1.00
31.64
H


ATOM
6043
O
HOH
H
79
34.670
13.941
14.778
1.00
22.87
H


ATOM
6044
O
HOH
H
80
98.527
27.671
28.270
1.00
42.07
H


ATOM
6045
O
HOH
H
81
30.588
36.032
16.540
1.00
37.52
H


ATOM
6046
O
HOH
H
82
89.345
42.957
13.940
1.00
22.73
H


ATOM
6047
O
HOH
H
83
92.891
18.085
10.698
1.00
32.35
H


ATOM
6048
O
HOH
H
84
90.050
48.556
16.519
1.00
27.30
H


ATOM
6049
O
HOH
H
85
110.812
49.549
15.813
1.00
27.68
H


ATOM
6050
O
HOH
H
86
75.872
21.668
2.499
1.00
39.37
H


ATOM
6051
O
HOH
H
87
52.567
14.010
7.270
1.00
34.20
H


ATOM
6052
O
HOH
H
88
69.016
32.569
12.651
1.00
36.96
H


ATOM
6053
O
HOH
H
89
96.637
25.945
31.742
1.00
37.26
H


ATOM
6054
O
HOH
H
90
34.496
−12.998
8.560
1.00
22.82
H


ATOM
6055
O
HOH
H
91
113.021
48.469
17.945
1.00
47.59
H


ATOM
6056
O
HOH
H
92
34.266
25.052
23.930
1.00
31.02
H


ATOM
6057
O
HOH
H
93
51.464
31.946
19.300
1.00
15.75
H


ATOM
6058
O
HOH
H
94
80.054
50.912
15.041
1.00
25.94
H


ATOM
6059
O
HOH
H
95
40.413
−13.432
16.393
1.00
39.73
H


ATOM
6060
O
HOH
H
96
57.701
4.191
7.708
1.00
25.27
H


ATOM
6061
O
HOH
H
97
80.838
52.853
26.436
1.00
27.67
H


ATOM
6062
O
HOH
H
98
58.205
13.023
20.294
1.00
27.57
H


ATOM
6063
O
HOH
H
99
41.832
30.497
15.601
1.00
27.32
H


ATOM
6064
O
HOH
H
100
72.807
29.880
11.618
1.00
28.05
H


ATOM
6065
O
HOH
H
101
48.499
5.079
4.053
1.00
38.72
H


ATOM
6066
O
HOH
H
102
100.679
66.408
9.019
1.00
36.21
H


ATOM
6067
O
HOH
H
103
45.023
41.442
11.747
1.00
42.72
H


ATOM
6068
O
HOH
H
104
83.296
63.483
−2.738
1.00
27.46
H


ATOM
6069
O
HOH
H
105
85.067
29.522
34.732
1.00
35.62
H


ATOM
6070
O
HOH
H
106
72.272
53.390
15.314
1.00
38.75
H


ATOM
6071
O
HOH
H
107
80.600
27.688
5.225
1.00
26.04
H


ATOM
6072
O
HOH
H
108
71.251
18.567
16.503
1.00
29.08
H


ATOM
6073
O
HOH
H
109
88.274
65.356
19.510
1.00
26.70
H


ATOM
6074
O
HOH
H
110
43.031
4.836
7.813
1.00
38.59
H


ATOM
6075
O
HOH
H
111
101.304
35.384
4.755
1.00
43.53
H


ATOM
6076
O
HOH
H
112
44.554
10.725
19.619
1.00
21.38
H


ATOM
6077
O
HOH
H
113
115.506
34.478
5.615
1.00
46.62
H


ATOM
6078
O
HOH
H
114
36.124
−25.634
9.802
1.00
42.69
H


ATOM
6079
O
HOH
H
115
34.494
−33.304
20.170
1.00
61.12
H


ATOM
6080
O
HOH
H
116
38.663
26.161
−2.715
1.00
31.39
H


ATOM
6081
O
HOH
H
117
105.197
41.384
18.739
1.00
38.53
H


ATOM
6082
O
HOH
H
118
38.437
−12.372
18.422
1.00
32.47
H


ATOM
6083
O
HOH
H
119
45.430
15.732
9.556
1.00
32.39
H


ATOM
6084
O
HOH
H
120
70.475
9.817
−1.029
1.00
53.38
H


ATOM
6085
O
HOH
H
121
87.895
64.540
22.445
1.00
47.01
H


ATOM
6086
O
HOH
H
122
39.337
36.650
16.644
1.00
25.21
H


ATOM
6087
O
HOH
H
123
104.091
50.783
20.204
1.00
31.31
H


ATOM
6088
O
HOH
H
124
72.528
13.825
20.909
1.00
62.81
H


ATOM
6089
O
HOH
H
125
55.353
−5.411
5.747
1.00
25.46
H


ATOM
6090
O
HOH
H
126
97.848
63.704
25.177
1.00
27.84
H


ATOM
6091
O
HOH
H
127
89.799
75.117
14.074
1.00
49.56
H


ATOM
6092
O
HOH
H
128
96.226
35.565
0.211
1.00
40.25
H


ATOM
6093
O
HOH
H
129
25.125
−15.445
19.161
1.00
37.04
H


ATOM
6094
O
HOH
H
130
90.627
52.974
9.649
1.00
22.70
H


ATOM
6095
O
HOH
H
131
114.398
29.773
11.425
1.00
42.36
H


ATOM
6096
O
HOH
H
132
69.810
89.608
−0.164
1.00
53.48
H


ATOM
6097
O
HOH
H
133
99.069
30.421
4.728
1.00
31.21
H


ATOM
6098
O
HOH
H
134
37.335
49.129
5.746
1.00
43.90
H


ATOM
6099
O
HOH
H
135
77.753
73.821
17.600
1.00
50.43
H


ATOM
6100
O
HOH
H
136
44.853
33.208
11.090
1.00
21.26
H


ATOM
6101
O
HOH
H
137
88.697
80.608
−4.574
1.00
49.42
H


ATOM
6102
O
HOH
H
138
62.018
−6.136
9.010
1.00
30.19
H


ATOM
6103
O
HOH
H
139
35.964
−5.810
5.494
1.00
45.47
H


ATOM
6104
O
HOH
H
140
73.968
65.480
8.013
1.00
43.93
H


ATOM
6105
O
HOH
H
141
78.361
66.868
24.455
1.00
57.76
H


ATOM
6106
O
HOH
H
142
53.527
3.199
22.332
1.00
32.95
H


ATOM
6107
O
HOH
H
143
56.018
−6.530
25.205
1.00
42.75
H


ATOM
6108
O
HOH
H
144
82.930
52.617
28.345
1.00
32.35
H


ATOM
6109
O
HOH
H
145
28.607
−21.313
24.210
1.00
48.87
H


ATOM
6110
O
HOH
H
146
86.079
41.197
35.698
1.00
36.97
H


ATOM
6111
O
HOH
H
147
35.017
8.399
11.516
1.00
32.21
H


ATOM
6112
O
HOH
H
148
25.864
−19.905
17.166
1.00
41.53
H


ATOM
6113
O
HOH
H
149
55.504
20.659
6.959
1.00
36.63
H


ATOM
6114
O
HOH
H
150
106.046
47.260
19.571
1.00
30.60
H


ATOM
6115
O
HOH
H
151
108.769
26.147
5.447
1.00
48.82
H


ATOM
6116
O
HOH
H
152
38.689
17.576
4.331
1.00
39.07
H


ATOM
6117
O
HOH
H
153
97.787
62.580
8.740
1.00
29.61
H


ATOM
6118
O
HOH
H
154
59.501
−12.817
20.769
1.00
50.36
H


ATOM
6119
O
HOH
H
155
47.887
40.072
−4.641
1.00
51.05
H


ATOM
6120
O
HOH
H
156
60.057
16.564
27.477
1.00
40.66
H


ATOM
6121
O
HOH
H
157
67.048
27.841
20.873
1.00
39.66
H


ATOM
6122
O
HOH
H
158
37.028
32.932
18.669
1.00
37.23
H


ATOM
6123
O
HOH
H
159
121.780
18.693
−3.076
1.00
46.64
H


ATOM
6124
O
HOH
H
160
39.196
18.091
27.271
1.00
29.99
H


ATOM
6125
O
HOH
H
161
113.285
44.237
19.561
1.00
39.04
H


ATOM
6126
O
HOH
H
162
43.379
27.754
19.370
1.00
27.58
H


ATOM
6127
O
HOH
H
163
91.636
66.903
11.885
1.00
54.73
H


ATOM
6128
O
HOH
H
164
113.381
46.844
20.020
1.00
54.22
H


ATOM
6129
O
HOH
H
165
79.238
62.082
24.112
1.00
36.07
H


ATOM
6130
O
HOH
H
166
27.985
32.355
18.424
1.00
36.25
H


ATOM
6131
O
HOH
H
167
34.709
−10.661
20.615
1.00
9.89
H


ATOM
6132
O
HOH
H
168
93.577
37.339
20.182
1.00
14.03
H


ATOM
6133
O
HOH
H
169
97.912
51.662
7.309
1.00
24.22
H


ATOM
6134
O
HOH
H
170
69.616
4.375
18.521
1.00
38.01
H


ATOM
6135
O
HOH
H
171
80.870
25.194
6.002
1.00
21.84
H


ATOM
6136
O
HOH
H
172
50.564
12.887
5.906
1.00
32.25
H


ATOM
6137
O
HOH
H
173
88.207
37.288
13.919
1.00
19.68
H


ATOM
6138
O
HOH
H
174
93.800
47.651
27.174
1.00
41.65
H


ATOM
6139
O
HOH
H
175
52.842
0.304
25.210
1.00
28.07
H


ATOM
6140
O
HOH
H
176
66.457
4.742
14.051
1.00
28.64
H


ATOM
6141
O
HOH
H
177
36.948
12.416
15.109
1.00
28.66
H


ATOM
6142
O
HOH
H
178
103.292
41.793
7.607
1.00
28.51
H


ATOM
6143
O
HOH
H
179
86.476
36.035
9.339
1.00
27.43
H


ATOM
6144
O
HOH
H
180
82.262
41.159
26.845
1.00
24.13
H


ATOM
6145
O
HOH
H
181
32.348
15.030
26.400
1.00
30.06
H


ATOM
6146
O
HOH
H
182
69.916
30.709
14.482
1.00
42.81
H


ATOM
6147
O
HOH
H
183
48.060
10.142
26.751
1.00
49.12
H


ATOM
6148
O
HOH
H
184
45.863
−9.131
37.252
1.00
43.70
H


ATOM
6149
O
HOH
H
185
32.095
−3.806
34.251
1.00
41.46
H


ATOM
6150
O
HOH
H
186
108.258
31.975
8.914
1.00
33.62
H


ATOM
6151
O
HOH
H
187
99.465
64.293
8.210
1.00
54.43
H


ATOM
6152
O
HOH
H
188
74.677
30.785
27.841
1.00
28.20
H


ATOM
6153
O
HOH
H
189
44.953
0.968
35.892
1.00
32.25
H


ATOM
6154
O
HOH
H
190
88.523
27.792
36.268
1.00
30.83
H


ATOM
6155
O
HOH
H
191
37.736
8.611
11.729
1.00
38.92
H


ATOM
6156
O
HOH
H
192
35.988
45.178
12.964
1.00
33.85
H


ATOM
6157
O
HOH
H
193
77.222
68.027
1.401
1.00
27.02
H


ATOM
6158
O
HOH
H
194
63.326
−8.764
15.926
1.00
38.46
H


ATOM
6159
O
HOH
H
195
109.635
61.489
27.644
1.00
52.79
H


ATOM
6160
O
HOH
H
196
101.299
67.528
11.319
1.00
38.92
H


ATOM
6161
O
HOH
H
197
77.295
56.116
25.768
1.00
36.83
H


ATOM
6162
O
HOH
H
198
81.538
22.288
0.320
1.00
47.08
H


ATOM
6163
O
HOH
H
199
55.989
3.900
0.756
1.00
46.35
H


ATOM
6164
O
HOH
H
200
66.200
40.514
17.513
1.00
43.54
H


ATOM
6165
O
HOH
H
201
40.497
−1.046
9.238
1.00
27.84
H


ATOM
6166
O
HOH
H
202
57.171
27.504
8.258
1.00
52.74
H


ATOM
6167
O
HOH
H
203
44.592
−6.430
37.531
1.00
37.55
H


ATOM
6168
O
HOH
H
204
26.892
−1.642
9.494
1.00
55.58
H


ATOM
6169
O
HOH
H
205
83.350
58.389
2.759
1.00
46.24
H


ATOM
6170
O
HOH
H
206
112.353
45.284
9.770
1.00
30.99
H


ATOM
6171
O
HOH
H
207
86.315
23.927
16.100
1.00
41.36
H


ATOM
6172
O
HOH
H
208
67.053
45.396
12.396
1.00
31.02
H


ATOM
6173
O
HOH
H
209
111.609
60.418
8.362
1.00
52.01
H


ATOM
6174
O
HOH
H
210
91.254
47.553
32.752
1.00
41.71
H


ATOM
6175
O
HOH
H
211
88.489
39.944
11.117
1.00
34.00
H


ATOM
6176
O
HOH
H
212
104.972
69.233
16.415
1.00
37.26
H


ATOM
6177
O
HOH
H
213
23.462
39.893
6.692
1.00
56.45
H


ATOM
6178
O
HOH
H
214
84.114
54.447
−1.718
1.00
42.58
H


ATOM
6179
O
HOH
H
215
105.045
66.068
22.775
1.00
24.48
H


ATOM
6180
O
HOH
H
216
85.378
52.388
17.025
1.00
37.91
H


ATOM
6181
O
HOH
H
217
91.411
30.837
4.259
1.00
23.59
H


ATOM
6182
O
HOH
H
218
99.019
37.803
25.178
1.00
37.20
H


ATOM
6183
O
HOH
H
219
88.866
41.183
35.781
1.00
42.88
H


ATOM
6184
O
HOH
H
220
66.946
25.931
12.530
1.00
45.53
H


ATOM
6185
O
HOH
H
221
83.809
61.544
−0.645
1.00
32.51
H


ATOM
6186
O
HOH
H
222
91.766
28.386
3.286
1.00
29.97
H


ATOM
6187
O
HOH
H
223
83.302
45.674
11.423
1.00
40.65
H


ATOM
6188
O
HOH
H
224
59.198
3.628
18.904
1.00
22.61
H


ATOM
6189
O
HOH
H
225
34.553
−11.852
5.930
1.00
29.77
H


ATOM
6190
O
HOH
H
226
88.953
22.712
24.560
1.00
23.54
H


ATOM
6191
O
HOH
H
227
108.379
54.102
21.160
1.00
30.79
H


ATOM
6192
O
HOH
H
228
44.957
16.820
6.827
1.00
37.14
H


ATOM
6193
O
HOH
H
229
105.872
50.217
22.393
1.00
33.77
H


ATOM
6194
O
HOH
H
230
40.390
52.287
−1.729
1.00
62.00
H


ATOM
6195
O
HOH
H
231
103.837
27.586
24.806
1.00
50.76
H


ATOM
6196
O
HOH
H
232
50.931
9.397
25.207
1.00
40.65
H


ATOM
6197
O
HOH
H
233
64.739
2.382
27.973
1.00
46.98
H


ATOM
6198
O
HOH
H
234
38.363
0.460
8.402
1.00
28.58
H


ATOM
6199
O
HOH
H
235
73.577
50.129
18.561
1.00
36.68
H


ATOM
6200
O
HOH
H
236
100.912
58.519
6.876
1.00
36.99
H


ATOM
6201
O
HOH
H
237
100.664
26.841
26.380
1.00
36.27
H


ATOM
6202
O
HOH
H
238
82.528
48.080
12.484
1.00
44.97
H


ATOM
6203
O
HOH
H
239
70.870
44.782
13.746
1.00
26.53
H


ATOM
6204
O
HOH
H
240
71.914
−9.049
17.302
1.00
59.29
H


ATOM
6205
O
HOH
H
241
28.024
9.146
32.377
1.00
43.91
H


ATOM
6206
O
HOH
H
242
55.531
−2.470
4.880
1.00
50.20
H


ATOM
6207
O
HOH
H
243
63.362
16.623
21.334
1.00
30.95
H


ATOM
6208
O
HOH
H
244
71.813
27.548
12.914
1.00
54.77
H


ATOM
6209
O
HOH
H
245
22.793
−3.930
12.731
1.00
39.10
H


ATOM
6210
O
HOH
H
246
73.087
44.091
34.124
1.00
47.86
H


ATOM
6211
O
HOH
H
247
48.717
31.774
19.850
1.00
33.46
H


ATOM
6212
O
HOH
H
248
100.851
61.218
7.741
1.00
35.49
H


ATOM
6213
O
HOH
H
249
116.291
47.311
12.227
1.00
49.67
H


ATOM
6214
O
HOH
H
250
99.469
40.748
22.418
1.00
25.82
H


ATOM
6215
O
HOH
H
251
52.271
4.031
24.614
1.00
44.68
H


ATOM
6216
O
HOH
H
252
106.629
40.298
32.271
1.00
59.44
H


ATOM
6217
O
HOH
H
253
45.587
−9.303
3.049
1.00
26.81
H


ATOM
6218
O
HOH
H
254
52.547
−9.432
27.670
1.00
45.08
H


ATOM
6219
O
HOH
H
255
75.854
21.157
27.640
1.00
42.33
H


ATOM
6220
O
HOH
H
256
82.119
63.444
23.430
1.00
37.84
H


ATOM
6221
O
HOH
H
257
104.091
38.660
18.936
1.00
30.29
H


ATOM
6222
O
HOH
H
258
79.477
56.121
8.190
1.00
39.16
H


ATOM
6223
O
HOH
H
259
101.351
32.257
5.631
1.00
29.94
H


ATOM
6224
O
HOH
H
260
93.989
23.313
31.488
1.00
35.30
H


ATOM
6225
O
HOH
H
261
28.754
−1.723
6.977
1.00
36.90
H


ATOM
6226
O
HOH
H
262
93.007
48.370
9.901
1.00
49.06
H


ATOM
6227
O
HOH
H
263
82.990
88.137
9.529
1.00
39.70
H


ATOM
6228
O
HOH
H
264
118.031
51.582
0.542
1.00
36.21
H


ATOM
6229
O
HOH
H
265
21.682
15.046
11.602
1.00
62.29
H


ATOM
6230
O
HOH
H
266
34.210
24.576
5.314
1.00
18.89
H


ATOM
6231
O
HOH
H
267
85.829
40.095
14.911
1.00
25.26
H


ATOM
6232
O
HOH
H
268
102.070
38.308
21.059
1.00
41.79
H


ATOM
6233
O
HOH
H
269
41.071
−2.346
7.039
1.00
38.87
H


ATOM
6234
O
HOH
H
270
68.717
3.686
16.083
1.00
37.79
H


ATOM
6235
O
HOH
H
271
27.094
−12.649
12.753
1.00
29.26
H


ATOM
6236
O
HOH
H
272
36.426
24.744
4.145
1.00
45.88
H


ATOM
6237
O
HOH
H
273
88.670
31.858
5.525
1.00
39.43
H


ATOM
6238
O
HOH
H
274
90.819
38.524
36.028
1.00
30.15
H


ATOM
6239
O
HOH
H
275
90.790
49.861
10.317
1.00
39.97
H


ATOM
6240
O
HOH
H
276
77.026
11.969
13.970
1.00
44.87
H


ATOM
6241
O
HOH
H
277
36.555
12.078
12.344
1.00
40.47
H


ATOM
6242
O
HOH
H
278
52.331
7.302
24.972
1.00
49.30
H


ATOM
6243
O
HOH
H
279
92.612
33.229
3.564
1.00
40.55
H


ATOM
6244
O
HOH
H
280
83.546
64.142
25.612
1.00
50.28
H


ATOM
6245
O
HOH
H
281
28.206
−1.891
36.868
1.00
44.06
H


ATOM
6246
O
HOH
H
282
93.185
20.914
30.917
1.00
44.51
H


ATOM
6247
O
HOH
H
283
98.176
41.763
24.500
1.00
44.20
H


ATOM
6248
O
HOH
H
284
29.174
−0.123
4.304
1.00
46.75
H


ATOM
6249
O
HOH
H
285
79.206
77.643
14.919
1.00
30.21
H


ATOM
6250
O
HOH
H
286
90.531
26.085
37.436
1.00
36.96
H


ATOM
6251
O
HOH
H
287
55.726
0.396
21.054
1.00
49.55
H


ATOM
6252
O
HOH
H
288
111.246
30.915
19.699
1.00
42.91
H


ATOM
6253
O
HOH
H
289
77.000
58.921
5.300
1.00
47.04
H


ATOM
6254
O
HOH
H
290
34.339
−9.458
5.288
1.00
25.50
H


ATOM
6255
O
HOH
H
291
109.784
29.168
15.534
1.00
45.96
H


ATOM
6256
O
HOH
H
292
93.674
48.853
29.650
1.00
48.76
H


ATOM
6257
O
HOH
H
293
92.299
47.066
3.801
1.00
37.41
H


ATOM
6258
O
HOH
H
294
110.965
23.141
11.799
1.00
42.97
H


ATOM
6259
O
HOH
H
295
90.562
45.235
33.919
1.00
33.83
H


ATOM
6260
O
HOH
H
296
57.772
−10.500
25.018
1.00
49.78
H


ATOM
6261
O
HOH
H
297
54.676
36.195
11.362
1.00
54.22
H


ATOM
6262
O
HOH
H
298
107.263
59.234
5.282
1.00
56.05
H


ATOM
6263
O
HOH
H
299
70.560
48.918
1.476
1.00
49.72
H


ATOM
6264
O
HOH
H
300
84.037
38.916
5.971
1.00
39.33
H


ATOM
6265
O
HOH
H
301
86.468
41.381
11.971
1.00
45.69
H


ATOM
6266
O
HOH
H
302
24.400
11.569
23.610
1.00
36.73
H


ATOM
6267
O
HOH
H
303
73.087
79.808
7.028
1.00
46.20
H


ATOM
6268
O
HOH
H
304
72.681
43.116
14.941
1.00
51.84
H


ATOM
6269
O
HOH
H
305
84.844
42.198
15.611
1.00
26.23
H


ATOM
6270
O
HOH
H
306
54.135
19.007
24.978
1.00
27.41
H


ATOM
6271
O
HOH
H
307
67.044
10.459
18.465
1.00
44.92
H


ATOM
6272
O
HOH
H
308
82.262
49.436
14.864
1.00
39.04
H


ATOM
6273
O
HOH
H
309
114.093
50.994
16.895
1.00
43.32
H


ATOM
6274
O
HOH
H
310
64.428
3.092
30.590
1.00
43.29
H


ATOM
6275
O
HOH
H
311
81.152
70.187
18.656
1.00
34.21
H


ATOM
6276
O
HOH
H
312
74.596
81.584
−2.515
1.00
55.00
H


ATOM
6277
O
HOH
H
313
61.161
25.774
22.464
1.00
32.98
H


ATOM
6278
O
HOH
H
314
53.149
−7.019
4.754
1.00
26.01
H


ATOM
6279
O
HOH
H
315
44.571
8.317
33.567
1.00
40.32
H


ATOM
6280
O
HOH
H
316
82.293
49.769
10.587
1.00
35.22
H


ATOM
6281
O
HOH
H
317
48.467
8.859
24.614
1.00
42.38
H


ATOM
6282
O
HOH
H
318
56.588
−8.027
4.728
1.00
44.65
H


ATOM
6283
O
HOH
H
319
31.280
−23.239
26.551
1.00
42.45
H


ATOM
6284
O
HOH
H
320
82.483
40.137
7.719
1.00
39.22
H


ATOM
6285
O
HOH
H
321
82.063
19.937
23.440
1.00
35.69
H


ATOM
6286
O
HOH
H
322
106.025
63.366
22.616
1.00
31.93
H


ATOM
6287
O
HOH
H
323
46.181
9.890
8.669
1.00
38.11
H


ATOM
6288
O
HOH
H
324
71.708
75.568
6.998
1.00
41.82
H


ATOM
6289
O
HOH
H
325
108.280
34.405
3.851
1.00
30.72
H


ATOM
6290
O
HOH
H
326
32.275
40.921
14.635
1.00
40.72
H


ATOM
6291
O
HOH
H
327
37.556
15.785
5.690
1.00
42.29
H


ATOM
6292
O
HOH
H
328
85.569
33.598
37.182
1.00
31.78
H


ATOM
6293
O
HOH
H
329
33.070
−11.287
23.137
1.00
48.90
H


ATOM
6294
O
HOH
H
330
87.593
16.513
19.683
1.00
45.53
H


ATOM
6295
O
HOH
H
331
116.176
53.631
17.853
1.00
39.81
H


ATOM
6296
O
HOH
H
332
26.940
−11.377
14.930
1.00
39.40
H


ATOM
6297
O
HOH
H
333
60.033
28.679
22.456
1.00
32.84
H


ATOM
6298
O
HOH
H
334
52.472
15.182
2.562
1.00
48.72
H


ATOM
6299
O
HOH
H
335
84.377
54.588
4.646
1.00
40.99
H


ATOM
6300
O
HOH
H
336
115.759
67.454
19.970
1.00
46.15
H


ATOM
6301
O
HOH
H
337
88.969
52.684
25.112
1.00
42.31
H


ATOM
6302
O
HOH
H
338
36.351
12.852
9.875
1.00
37.11
H


ATOM
6303
O
HOH
H
339
97.702
31.578
2.653
1.00
49.82
H


ATOM
6304
O
HOH
H
340
53.964
−6.543
26.981
1.00
35.52
H


ATOM
6305
O
HOH
H
341
24.475
−17.438
17.094
1.00
38.04
H


ATOM
6306
O
HOH
H
342
58.530
0.915
19.036
1.00
43.08
H


ATOM
6307
O
HOH
H
343
77.156
37.203
39.025
1.00
48.54
H


ATOM
6308
O
HOH
H
344
49.978
−1.361
0.435
1.00
39.48
H


ATOM
6309
O
HOH
H
345
53.900
37.104
13.703
1.00
47.74
H


ATOM
6310
O
HOH
H
346
77.886
49.625
13.575
1.00
57.13
H


ATOM
6311
O
HOH
H
347
57.053
8.721
0.570
1.00
50.38
H


ATOM
6312
O
HOH
H
348
96.803
63.745
10.854
1.00
41.14
H


ATOM
6313
O
HOH
H
349
89.009
70.808
11.906
1.00
45.67
H


ATOM
6314
O
HOH
H
350
66.363
22.353
8.221
1.00
42.47
H


ATOM
6315
O
HOH
H
351
52.578
25.044
8.541
1.00
41.16
H


ATOM
6316
O
HOH
H
352
81.789
73.640
−3.536
1.00
50.48
H


ATOM
6317
O
HOH
H
353
67.632
−11.181
13.891
1.00
48.24
H


ATOM
6318
O
HOH
H
354
41.357
−5.652
22.367
1.00
14.47
H


ATOM
6319
C1
EDO
G
501
37.685
−5.096
30.876
1.00
23.96
G


ATOM
6320
O1
EDO
G
501
38.224
−4.213
31.883
1.00
23.38
G


ATOM
6321
C2
EDO
G
501
38.742
−6.046
30.406
1.00
25.29
G


ATOM
6322
O2
EDO
G
501
39.062
−6.931
31.464
1.00
26.30
G


ATOM
6323
C1
EDO
G
502
89.146
26.377
27.000
1.00
41.69
G


ATOM
6324
O1
EDO
G
502
88.631
26.508
28.343
1.00
51.10
G


ATOM
6325
C2
EDO
G
502
88.436
25.261
26.303
1.00
43.14
G


ATOM
6326
O2
EDO
G
502
88.726
24.052
26.967
1.00
41.73
G


ATOM
6327
C1
EDO
G
503
85.093
31.920
30.633
1.00
21.00
G


ATOM
6328
O1
EDO
G
503
85.283
30.597
31.203
1.00
18.65
G


ATOM
6329
C2
EDO
G
503
83.846
32.561
31.186
1.00
19.69
G


ATOM
6330
O2
EDO
G
503
84.148
33.101
32.454
1.00
20.94
G


ATOM
6331
C1
EDO
G
504
34.956
3.907
25.885
1.00
38.01
G


ATOM
6332
O1
EDO
G
504
33.976
2.838
25.869
1.00
36.69
G


ATOM
6333
C2
EDO
G
504
36.360
3.344
25.982
1.00
39.84
G


ATOM
6334
O2
EDO
G
504
36.573
2.396
24.935
1.00
33.51
G


END









Example 4
Binding of altered gluten peptides (peptide analogs) to MHC molecules is assayedwith purified HLA molecules. Binding of labeled peptide to purified HLA DQ2 molecules can be measured as described by Johansen et al. (1996) Int Immmunol (8), 177–82. Briefly, purified DQ2 molecules (50–1000 nM) are incubated with the 125-I radiolabeled indicator peptide (MB 65kDa 243–255Y, sequence (SEQ ID NO:29) KPLLIIAEDVEGEY; 20000 cpm, 1–5 nM) at pH 4.9. After incubation for 24 hours, the peptide bound to DQ2 and the non-bound peptide are separated on Sephadex G25 superfine spun columns. The radioactivity in the bound and non-bound fractions was counted in a gamma-counter, and the fraction of peptide bound to DQ2 (cpm in the bound fraction/total cpm recovered) is calculated. The binding capacities of the peptide binding inhibitors are assayed by testing their ability to inhibit the binding of the labeled indicator peptide. The concentration required to give 50% inhibition (IC50) is calculated. Since the level of IC50 may vary between separate titration experiments, the IC50 values are compared to the IC50 of a reference peptide by determining the relative binding capacity (RBC), which is the ratio: IC50 of reference peptide/IC50 of test compound. HLA-DQ2 molecules can be isolated by antibody affinity chromatography from lysates of HLA-DQ2 homozygous Epstein Barr virus transformed B-lymphoblastoid cell lines (detergent solubilized) or from water soluble, recombinant molecules produced similarly as described in Example 3 above. The recombinant molecules can be made with or without covalently linked peptide and with a biotin recognition sequence at the C-terminal end of the β-subunit that facilitates adsorption of HLA-DQ2 to several streptavidin coated supports, thereby enabling alternative ways for measurement of IC50i. A peptide analog with an IC50 value of less than 100 μM is suitable for further screenings.
Alternatively, binding of altered gluten peptides to HLA-DQ2 can also be assayed using the soluble DQ2 heterodimer produced as described in Example 3 above. The presence of the biotin recognition sequence at the C-terminal end of the subunit facilitates adsorption of HLA-DQ2 to several streptavidin coated supports, thereby enabling measurement of IC50 or Ki.
Candidate peptide analogs are further tested for their ability to inhibit proliferation of T cells specific for gluten peptides. This is done by using HLA-DQ2 restricted T cell clones (TCC) and glutaraldehyde fixed antigen presenting cells (e.g. Epstein Barr virus transformed B-lymphoid transformed cells) expressing HLA-DQ2. The antigen presenting cells are pelleted and resuspended in RPMI containing 0.05% glutaraldehyde for 90 sec, whereafter glycin to a final concentration of 0.2 M is added for 60 sec. The cells are then washed, counted, and resuspended in PBS or PBS buffered with citrate phosphate to a final pH of 4.9. The fixed APC are incubated overnight with various concentrations of peptides. The inhibitory peptides are usually added 30 min prior to the stimulatory peptide. The antigen presenting cells are then washed twice and resuspended in culture medium of RPMI-1640 supplemented with 15% v/v heat inactivated pooled human serum and the T cells are added. The experiments are performed in triplicates of 3–5×104 TCC with 5×104 fixed APC and various titrations of inhibitory and stimulatory peptides. Following an incubation period of 48 hours, each culture is pulsed with [3H]-thymidine for an additional 12–18 hours. Cultures are then harvested on fiberglass filters and counted as above. Mean CPM and standard error of the mean are calculated from data determined in triplicate cultures. Peptide analogs that inhibit proliferation to approximately 25% at a concentration of 50 μM or greater are suitable for further screening.
All publications and patent applications cited in this specification are herein incorporated by reference as if each individual publication or patent application were specifically and individually indicated to be incorporated by reference.
Although the foregoing invention has been described in some detail by way of illustration and example for purposes of clarity of understanding, it will be readily apparent to those of ordinary skill in the art in light of the teachings of this invention that certain changes and modifications may be made thereto without departing from the spirit or scope of the appended claims.

## Claims

1. A computer-assisted method for identifying potential modulators of Celiac Sprue and/or dermatitis herpetiformis, using a programmed computer comprising a processor, a data storage system, an input device, and an output device, comprising the steps of:
(a) inputting Into the programmed computer through said input device data comprising the three-dimensional coordinates of a subset of the atoms, generated from a complex of DQ2 molecule bound to an immunogenic gluten oligopeptide selected from the group consisting of PFPQPQLPY (SEQ ID NO: 12); PQPQLPYPQ (SEQ ID NO: 13); PFPQPQLPY (SEQ ID NO: 14); PQPQLPYPQ (SEQ ID NO: 15); PYPQPELPY (SEQ ID NO: 16); and PYPQPQLPY (SEQ ID NO: 17) PYPQPQLPY, thereby generating a criteria data set;
(b) comparing, using said processor, said criteria data set to a computer database of chemical structures stored in said computer data storage system;
(c) selecting from said database, using computer methods, chemical structures having a portion that is structurally similar to said criteria data set;
(d) outputting to said output device the selected chemical structures having a portion similar to said criteria data set.

2. The method according to claim 1, wherein said criteria data set is obtained from electron density maps built from crystals using phase information from one or more of multiple isomorphous heavy-atom derivatives, molecular replacement or selenomethionine incorporated multiwavelength anomalous dispersion technique.

3. The method according to claim 1, wherein said three-dimensional coordinates of a subset of the atoms in an HLA-DQ2 molecule bound to an immunogenic gluten oligopeptide selected from the group consisting of (SEQ ID NO: 12); PQPQLPYPQ (SEQ ID NO: 13); PFPQPQLPY (SEQ ID NO: 14); PQPQLPYPQ (SEQ ID NO: 15); PYPQPELPY (SEQ ID NO: 16); and PYPQPQLPY (SEQ ID NO: 17) PYPQPQLPY comprise the coordinates set forth in Table 2.