# Patent

## Title
Allergen-binding IgE monoclonal antibodies and method for preparing hypoallergens

## Abstract

The present invention relates to human IgE antibodies and derivatives thereof, which bind non-continuous planar allergenic epitope, such as in β-lactoglobulin, with high affinity and specificity. The present invention also relates to processes for making and engineering such allergen binding monoclonal antibodies and to methods for using these antibodies and derivatives thereof in the field of immunodiagnostics and immunotherapy.

## Background
This application is the National Phase of PCT/FI2008/050026 filed on Jan. 29, 2008, which claims priority under 35 U.S.C. 119(e) to U.S. Provisional Application No. 60/887,862 filed on Feb. 2, 2007, and under 35 U.S.C. 119(a) to Patent Application No. 20075059 filed in Finland on Jan. 29, 2007, all of which are hereby expressly incorporated by reference into the present application.


FIELD OF THE INVENTION
This invention relates to protein engineering technology. More particularly, the present invention relates to human IgE antibodies and derivatives thereof, which bind non-continuous allergenic epitope, a planar surface with the area of 600-900 Å2, e.g. IgE antibodies binding to bovine milk β-lactoglobulin with high affinity and specificity. The present invention also relates to processes for making and engineering such allergen-binding monoclonal antibodies with Type I interaction and to methods for using these antibodies and derivatives thereof in the field of immunodiagnostics, enabling qualitative and quantitative determination and removal of allergenic substances in biological and raw material samples, as well as the construction of focused IgE libraries towards allergens, enabling the development of allergen-specific antibodies. In immunotherapy, the present invention enables blocking the Type I surface interaction of allergenic substances by modifying amino acid residues of allergens. Hypoallergen variant can be obtained by mutating some (1-5) amino acid residues on the planar (flat) epitope surface with bulky residues (such as Arg, Tyr, Lys, Trp). The mutated residues are those which side chains are pointing outside towards solvent thus causing minimal change to the basic structure of the allergen. The purpose of the mutagenesis is to modify the flat surface to convex surface which prevent the binding of IgE-antibodies. The resulting modified allergen can be used to evoke tolerance against particular allergens in allergic patients. The present invention allows the development of human IgE VH-region derived antibodies for those therapeutic and diagnostic targets where the binding specificity is towards areas of protein structures that are not located on the protruding regions of the surface. The invention also provides means for screening or molecular modelling of substances capable of blocking the binding of an antibody to the Type I allergenic epitope. In this invention, the development, characterisation and structure determination of the human IgE antibody fragment and derivatives thereof that binds allergenic β-lactoglobulin with affinity and specificity high enough to be utilised as reagents in immunoassays are also described.
BACKGROUND OF THE INVENTION
Almost 20% of the population world-wide are suffering from allergy. Consequently, it is a health problem of increasing seriousness. Allergy is a hypersensitivity reaction against substances in air, food or water, which are normally harmless (Corry and Kheradmand, 1999). A new and foreign external agent triggers an allergic reaction, which aims at disposal of that agent from the body. In IgE-mediated allergic reactions, also called immediate or type I hypersensitivity reactions, under the first exposure of a foreign substance, allergen, to the body, IgE-bearing B-cells begin to produce soluble IgE molecules which will then bind to high-affinity IgE receptors present on the surface of a wide variety of cells, most importantly to mast cells and basophils. If the same foreign substance is encountered again, the cross-linking of the receptor-bound IgE molecules by the allergen occurs, resulting in cellular activation followed by the release of toxic products such as histamine, which will elicit the signs and symptoms of an allergic reaction.
Cow's milk allergy (CMA) is a most common cause of clinically important adverse food reactions with infants and children during the first 2 years of life (Savilahti, 1981; Host and Halken, 1990; Saarinen et al., 1999). It is characterized by a strong IgE response to milk proteins and clinical symptoms in skin and gastrointestinal tract such as atopic eczema, vomiting and diarrhoea (Vaarala et al., 1995; Saarinen, 2000). Symptoms in respiratory ducts and anaphylactic shock are also possible (Host and Halken, 1990; Schrander et al., 1993; Hill et al., 1999; Vanto et al., 1999; Saarinen, 2000). CMA is a serious problem with children, because milk is an important source of energy (up to 50%) for young children and is not very easily replaceable with non-dairy products. Nearly 85% of the milk allergic children will outgrow of their allergy by the age of 3, but remission of CMA may occur in up to one-third of older children (Sampson and Scanlon, 1989)
One of the major allergens in cow's milk is β-lactoglobulin, which belongs to the protein family known as lipocalins. Lipocalins consists a group of a small ligand binding proteins, mostly respiratory allergens such as Mus m1, Rat n1 (mouse and rat urinary proteins) and a German cockroach allergen Bla g4 (Rouvinen et al. 2001). β-lactoglobulin occurs naturally in the form of a 36 kD dimer with each subunit corresponding 162 amino acids. Totally six genetic variants of the β-lactoglobulin has been identified based on the sequence differences. The most prevalent variants A and B differ only at the position 64 (Asp→Gly) and 118 (Val→Ala) (Godovac-Zimmermann and Braunitzer, 1987). The 3D-structure of the β-lactoglobulin has been determined by X-ray diffraction (Sawyer L. et al, 1985, Brownlow, S. et al, 1997)
IgE antibodies distinctively recognise allergenic epitopes, which would be useful in clinics and immunodiagnostics for detecting and determining allergen concentrations of complex materials. Further, according to this invention, allergenic epitopes are usually different from the immunogenic epitopes of proteins. This fact has hampered the production of monoclonal antibodies capable of specific binding of allergenic epitopes by conventional methodology such as hybridoma technology. It has been recently shown that the development of allergen-specific IgE antibodies is possible by the phage display technology (Steinberger et al., 1996). This methodology is giving new tools to produce allergen-specific recombinant antibodies that can be produced in consistent quality for clinical and diagnostic applications.
The technical problem to which the present invention is related is the detection of actual binding sites of IgE antibodies in allergenic polypeptides and use of this information, e.g., to modify these polypeptides to decrease their allergenicity. Previous solutions for this problem are disclosed in U.S. Patent Application No. 2003/0175312 (Holm et al.), WO 03/096869 (Alk Abello A/S) and Jenkins et al. 2005 (J. Allergy Clin. Immunol. 115:163-170). In these documents, it is described that the putative IgE binding sites in allergenic polypeptides may be detected by sequence analysis of conserved surface structures of allergenic polypeptides. Further, in US 2005/0181446 (Roggen et al.) and Hantusch et al. 2004 (J. Allergy Clin. Immunol.) a peptide-scan approach is used to find IgE binding epitopes. However, none of these documents discloses the method of the present invention wherein an IgE binding site on an allergenic polypeptide is found based on the experimental 3D and molecular modelling data of a novel type of IgE epitope having essentially planar or flat nature. MacCallum et al. 1996 (J. Mol. Biol. 262:732-745) disclose the presence of planar surfaces on antibodies, but teach only modification of antibody structures not antigen structures. Further, the disclosure of MacCallum et al. is directed to antibodies and different kinds of antigens, such as carbohydrates and peptides, in general and does not teach anything particular on the binding between IgE antibodies and allergenic polypeptides or the surface structures of these polypeptides.
SUMMARY OF THE INVENTION
The present invention relates to human IgE antibodies and derivatives thereof, which bind to non-continuous allergenic epitope, a planar Type I surface with the area of 600-900 Å2, e.g. to IgE antibodies binding to bovine milk β-lactoglobulin with high affinity and specificity. The present invention also enables blocking the Type I surface interaction of allergenic substances by modifying amino acid residues of said surface structure or by producing a mimetope binding said surface.
We also describe in this application the development, characterisation and structure determination of the human IgE antibody fragment and derivatives thereof that binds allergenic β-lactoglobulin with affinity and specificity high enough to be utilised as reagents in immunoassays designed for the qualitative and quantitative measurement of β-lactoglobulin in biological samples, in removal of the β-lactoglobulin, in immunotherapy of allergic patients and in the construction of focused antibody libraries based on the structural data. Specifically, the present invention describes selection of human IgE antibodies specific to β-lactoglobulin by the phage display technique, the characterisation of the binding properties of the engineered antibody fragments produced in E. coli, and structure determination of the antibody-allergen immunocomplex.
This invention thus provides new reagents to be utilised in different kinds of immunoassay protocols, as well as in human immunotherapy and construction of focused antibody libraries. The invention also permits guaranteed continuous supply of these specific reagents of uniform quality, eliminating inherent batch-to-batch variation of polyclonal antisera. These advantageous effects permit the manufacture of new, specific and economical immunodiagnostic assays of uniform quality.
Consequently, one specific object of the present invention is to provide human IgE monoclonal antibodies, fragments thereof, or other derivatives of such antibodies, which bind β-lactoglobulin with affinity and specificity high enough to allow qualitative and quantitative measurement of β-lactoglobulin in biological samples, as well as their use in immunotherapy. The monovalent antibodies of the present invention demonstrate a specific binding to allergenic β-lactoglobulin.
Another object of the present invention is to provide cDNA clones encoding β-lactoglobulin-specific antibody chains, as well as constructs and methods for expression of such clones to produce β-lactoglobulin-binding antibodies, fragments thereof or other derivatives of such antibodies.
A further object of this invention is to provide methods of using such β-lactoglobulin-binding antibodies, fragments thereof or other derivatives of such antibodies, or combinations of them for qualitative and quantitative measurement of β-lactoglobulin in biological samples. Additionally, this invention provides β-lactoglobulin-binding antibodies, fragments thereof or other derivatives of such antibodies, or combinations of them for immunotherapy in allergic patients.
A further object of this invention is to provide methods of using structural data obtained for constructing focused IgE antibody libraries towards allergens for diagnostics and human IgE VH-region derived antibody libraries for therapeutic and diagnostic targets where the binding specificity is towards areas of protein structures that are not located on the protruding regions of the surface.
Other objects, features and advantages of the present invention will be become apparent from the following drawings and detailed description. It should be understood, however, that the detailed description and the specific examples, while indicating preferred embodiments of the invention, are given for illustration only, since various changes and modifications within the spirit and scope of the invention will become apparent to those skilled in the art from this detailed description.



BRIEF DESCRIPTION OF THE DRAWINGS
FIG. 1 shows a schematic presentation of an intact human IgE subclass antibody, Fab fragment and single-chain antibody (scFv). The antigen-binding site is indicated by a triangle.
FIG. 2 shows schematically the panning procedure.
FIG. 3 shows a schematic presentation of the scFv phage display vector used for the construction of scFv phage libraries.
FIG. 4 shows the deduced amino acid and nucleotide sequence of the heavy chain variable region of the D1 IgE Fab (SEQ ID NO: 2). The Complementarity Determining Regions (CDRs) are underlined. Numbering is according to Kabat (Kabat et al., 1991).
FIG. 5 shows the deduced amino acid and nucleotide sequence of the light chain variable region of the D1 IgE Fab (SEQ ID NO: 4). CDRs are underlined. Numbering is according to Kabat (Kabat et al., 1991).
FIG. 6 shows the curve obtained from the competitive ELISA of D1 IgE Fab fragment with human IgG1 subtype whose binding to immobilized, biotinylated β-lactoglobulin has been inhibited by soluble native β-lactoglobulin.
FIG. 7 shows the result from immunoprecipitation assay. The D1 IgE Fab binds the native β-lactoglobulin from cow milk. 1=Low molecular weight marker, 2-5=D1 IgE fab immobilized in proteinL beads+untreated milk sample, milk sample, heated 15 min+95° C., 30 min+95° C., 60 min+95° C. 6-7=negative controls (=empty proteinL beads+untreated milk sample or heated 60 min+95° C.) 8=purified β-lactoglobulin from Sigma 0.59=purified D1 IgE Fab 0.5 μg.
FIG. 8 shows the result of the competitive ELISA. The binding of D1 IgE Fab fragments with human IgG1 subtype to β-lactoglobulin is inhibited by patient sera.
FIG. 9 shows the binding of the D1 IgE Fab-antibody to the β-lactoglobulin. (a), A schematic view of binding an allergen (grey) to two IgE molecules (light chain L, heavy chain H)
FIG. 10 shows the different segments of the β-lactoglobulin epitope which are numbered 1-6.
FIG. 11 shows the binding of the D1 IgE Fab to β-lactoglobulin with the side view on the surface of D1/IgE-Fab fragment.
FIG. 12 shows the surface of β-lactoglobulin epitope with the CDR loops of the D1 IgE Fab and the residues of the D1 IgE Fab which make contacts with β-lactoglobulin.
FIG. 13 shows the binding of the D1 IgE Fab to β-lactoglobulin (left), the IgG antibody-antigen type binding IgG Fab 2JEL to phosphocarrier protein (middle) and IgG-allergen type binding of the BV16/Fab to the pollen allergen Bet v 1 (right).
FIG. 14 shows the potential IgE epitope from different allergens: Equ c 1, horse skin (Lascombe et al., 2000, J. Biol. Chem. 275(28):21572-21577); Bos d 5, Beta-lactoglobulin; Bet v 1, birch pollen (Spangfort et al. 2003, J. Immunol. 171(6):3084-3090); Bos d 2, bovine dander (Rautiainen et al., 1998, Biochem. Biophys. Res. Commun. 247:746-750); Cyp c 1, carp parvalbumin (Swoboda et al., 2002, J. Immunol. 168(9):4576-4584); and Hey b 6, latex (see WO02094878). The planar (flat) surfaces are indicated with thick lines/bars.
FIG. 15 shows the result of competition ELISA. The binding of the D1 IgE Fab to BLG is inhibited by a short peptide, KRVG. Ctr 1 and ctr2 are the background controls where ctr1 is the result obtained after incubation without D1 IgE Fab and ctr2 without the BLG (see Example 4).
FIG. 16 shows the surface of D1/Fab antibody and ribbon model of allergen BLG. In this figure identical residues of the D1/Fab with hevein-binding IgE-antibody (clone IC2) are shown in light grey, different residues are in dark grey; a) front view, b) side view showing extensive similarity between the light chains of two IgE antibodies binding structurally very different allergens.
FIG. 17. Antibody binding to flat, convex and concave epitopes. In the first row the solvent excluded surface (probe radius 10 Å) is shown. Because of a large probe sphere the surface show more large scale features. The surface is coloured according to the Gaussian curvature. Flat areas are in white. Antibody is shown as a ribbon model. The second row shows similar structures but now the surfaces represent interaction surface which corresponds epitope.
FIG. 18. The molecular surfaces (probe radius 10 Å) of five different allergens in two orientations. The surface is coloured according to the curvature, flat areas are in white. The putative flat area for IgE-binding are shown as a rectangle on the left. The side view is on the right and the position of the same area are shown as a line.
FIG. 19. Purification of the rBLG-His6 and its mutants. After the second IMAC-purification the protein samples were analysed on the Coomassie-stained 15% SDS-PAGE gels (with β-mercaptoethanol). The pooled fractions are shown by arrows.
FIG. 20. The purified rBLG-His6 and its mutants were analysed by western blotting followed by the detection with the rabbit anti-BLG antibody and goat AFOS-conjugated anti-rabbit antibody. 3 μg protein were subjected into the well. Lane 1=LMW, lane 2=native BLG(Sigma), lane 3=rBLG-His6, lane 4=rBLG-His6 T18Y, and lane 5=rBLG-His 6 T18Y/E45Y/L57Y.
FIG. 21. CD-spectra of the nBLG, rBLG-His6 and its mutants are shown.
FIG. 22. The binding properties of the D1 IgE Fab to different BLGs were analysed by ELISA. Biotinylated nBLG, rBLG-His6 or its mutants were immobilised on to the SA-microtitre wells. Bound D1 IgE Fab was detected using AFOS-conjugated goat anti-kappa antibody. Triple=rBLG-His6 T18Y/E45Y/L57Y mutant, Bsa=bovine serum albumin, and control-sample shows the background obtained from anti kappa-AFOS conjugate when the BLGs are immobilised but no D1 IgE Fab used.
FIG. 23. The binding properties of the IgE serum samples from allergic and non-allergic donor to different BLGs were analysed by ELISA. Biotinylated nBLG, rBLG-His6 or its mutants were immobilised on to the SA-microtitre wells. The bound IgE was detected using AFOS-conjugated goat anti-human IgE.
FIG. 24. BIAcore analysis of the nBLG, rBLG-His6 and its mutants. Binding curves of the 69.6 nM D1 IgE Fab solution for binding to different BLGs are shown. The association and dissociation constants of the D1 IgE Fab to nBLG, rBLG-His6 and its mutants are calculated and shown in Table XI.



The figures of the constructions are not in scale.
ABBREVIATIONS
cDNA complementary deoxyribonucleic acid
CDR complementarity determining region
DNA deoxyribonucleic acid
E. coli Escherichia coli 
ELISA enzyme-linked immunosorbent assay
Fab fragment with specific antigen binding
Fd variable and first constant domain of a heavy chain
Fv variable regions of an antibody with specific antigen binding
IgE immunoglobulin E
mRNA messenger ribonucleic acid
NMR nuclear magnetic resonance
PCR polymerase chain reaction
RNA ribonucleic acid
scFv single-chain antibody
supE− a genotype of bacterial strain carrying a glutamine-inserting amber suppressor tRNA
VH variable region of a heavy chain
VL variable region of a light chain
DETAILED DESCRIPTION OF THE INVENTION
The following definitions are provided for some terms used in this specification. The terms, “immunoglobulin”, “heavy chain”, “light chain” and “Fab” are used in the same way as in the European Patent Application No. 0125023.
“Antibody” in its various grammatical forms is used herein as a collective noun that refers to a population of immunoglobulin molecules and/or immunologically active portions of immunoglobulin molecules, i.e., molecules that contain an antigen binding site or a paratope.
An “antigen-binding site”, a “paratope”, is the structural portion of an antibody molecule that specifically binds an antigen.
Exemplary antibodies are those portions of an immunoglobulin molecule that contain the paratope, including those portions known as Fab and Fv.
“Fab” (fragment with specific antigen binding), a portion of antibodies can be prepared by the proteolytic reaction of papain on substantially intact antibodies by methods that are well known. See for example, U.S. Pat. No. 4,342,566. Fab fragments can also be produced by recombinant methods, which are well known to those skilled in the art. See, for example, U.S. Pat. No. 4,949,778.
“Domain” is used to describe an independently folding part of a protein. General structural definitions for domain borders in natural proteins are given in Argos, 1988.
A “variable domain” or “Fv” is used to describe those regions of the immunoglobulin molecule, which are responsible for antigen or hapten binding. Usually these consist of approximately the first 100 amino acids of the N-termini of the light and the heavy chain of the immunoglobulin molecule.
“Single-chain antibody” (scFv) is used to define a molecule in which the variable domains of the heavy and light chain of an antibody are joined together via a linker peptide to form a continuous amino acid chain synthesised from a single mRNA molecule (transcript).
“Linker” or “linker peptide” is used to describe an amino acid sequence that extends between adjacent domains in a natural or engineered protein.
A “β-lactoglobulin-binding antibody” is an antibody, which specifically recognises β-lactoglobulin and binds to it, due to interaction mediated by its variable domains. As used herein, the term “specifically binding” or “specifically recognizing” or the expression “having binding specificity to an allergenic epitope of β-lactoglobulin” refers to a low background and high affinity binding between an antibody or a fragment or derivative thereof and its target molecule (i.e. lack of non-specific binding). One of the embodiments of the present invention is a monoclonal antibody having binding specificity to an allergenic epitope of β-lactoglobulin (SEQ ID NO:8), or a functional fragment or derivative thereof having said specificity.
The term “planar (or flat) surface” refers to the surface structure as defined in Example 8.
As examples of fragments of such antibodies falling within the scope of the invention we disclose here scFv fragments of D1 IgE fab as shown in FIGS. 4 and 5. In one preferred embodiment, the present invention thus provides derivatives of β-lactoglobulin-binding antibodies, e.g. Fab fragments or scFv fragments. It will be appreciated that mutant versions of the CDR sequences or complete VL and VH sequences having one or more conservative substitutions which do not substantially affect binding capability, may alternatively be employed and are included into the scope of the invention.
For use in immunoassay, e.g. for qualitative or quantitative determination of β-lactoglobulin in biological samples, antibodies and antibody derivatives of the invention may be labelled. For these purposes, any type of label conventionally employed for antibody labelling is acceptable.
For use in immunotherapy, e.g. for blocking allergenic β-lactoglobulin in allergic patients, antibodies and antibody derivatives of the invention may be labelled. For these purposes, any pharmaceutically acceptable label conventionally employed for antibody labelling is appropriate (see, e.g., US 2007/0003579).
In another aspect, the present invention also provides DNA molecules encoding an antibody or antibody derivative of the invention, and fragments of such DNAs, which encode the CDRs of the VL and/or VH region. Such a DNA may be cloned in a vector, more particularly, for example, an expression vector which is capable of directing expression of antibody derivatives of the invention, or at least one antibody chain or a part of one antibody chain.
In a further aspect of the invention, host cells are provided, selected from bacterial cells, yeast cells, fungal cells, insect cells, plant cells and mammalian cells, containing a DNA molecule of the invention, including host cells capable of expressing an antibody or antibody derivative of the invention. Thus, antibody derivatives of the invention may be prepared by culturing host cells of the invention expressing the required antibody chain(s), and either directly recovering the desired protein or, if necessary, initially recovering and combining individual chains.
The above-indicated scFv fragments were obtained by biopanning of a human IgE scFv-phage library using allergenic recombinant β-lactoglobulin. The human IgE scFv-phage library was constructed from mRNAs isolated from lymphocytes of a milk-allergic patient. The variable region of the light and heavy chain cDNAs were synthesised using human IgE-specific primers for Fd cDNAs and human kappa (κ) and lambda (λ) light chains using human κ and λ chain specific primers. The variable regions of the light and heavy chains were amplified by PCR using human κ and λ chain specific primers for Vκ and Vλ cDNAs and human IgE specific primers for VH cDNAs, respectively. The human IgE scFv library was constructed by cloning the variable region cDNAs into a scFv phage display vector using restriction sites introduced into the PCR primers.
The human IgE scFv library was selected by phage display using a panning procedure. The human IgE scFv phage library was screened by a biotinylated allergenic native β-lactoglobulin in solution and the binders were captured on streptavidin. The elution of phages was done with 100 μM non biotinylated native β-lactoglobulin AB dimer. The phage eluate was amplified in E. coli cells. After 2 rounds of biopanning, soluble scFv fragments were produced from isolated phages. The binding specificity of the selected scFv fragments was analysed by ELISA. Several β-lactoglobulin-specific scFv fragment clones were obtained.
As described herein, the phage display technique is an efficient and feasible approach to develop human IgE recombinant anti-β-lactoglobulin antibodies for diagnostic and therapeutic applications.
While one successful selection strategy for obtaining antibody fragments of the invention has been described, numerous variations, by which antibody fragments of the invention may be obtained, will be apparent to those skilled in the art. It may prove possible to select scFv fragments of the invention directly from a phage or microbial display library of scFv fragment or its derivatives. A phage or microbial cell, which presents a scFv fragment or other antibody fragment of the invention as a fusion protein with a surface protein, represents a still further aspect of the invention.
While microbial expression of antibodies and antibody derivatives of the invention offers means for efficient and economical production of highly specific reagents of uniform quality suitable for use in immunodiagnostic assays and immunotherapy, alternatively it may prove possible to produce such a reagent, or at least a portion thereof, synthetically. By applying conventional genetic engineering techniques, initially obtained antibody fragments of the invention may be altered, e.g. new sequences linked, without substantially altering the binding characteristics. Such techniques may be employed to produce novel β-lactoglobulin-binding hybrid proteins, which retain both affinity and specificity for β-lactoglobulin as defined hereinbefore.
Planar Surface of Allergens and Production and Use of Hypoallergens
The present invention enables blocking the Type I surface interaction of allergenic substances by modifying amino acid residues on non-continuous allergenic epitope, i.e. a planar surface with the area of 600-900 Å2 on the allergenic substance (see FIGS. 14 and 16). The planar (flat) surface may contain a β-sheet on the surface of the protein such as in β-lactoglobulin and Bet v 1, or α-helixes packed near to each other such as in Fel d 1. Other allergens with the planar structure are Equ c 1 (horse skin), Bos d 2 (bovine dander), Cyp c 1 (carp parvalbumin), and Hey b 6 (latex).
Hypoallergen variant can be obtained by mutating some (1-5) amino acid residues on the planar (flat) epitope surface with bulky residues (e.g. Arg, Tyr, Lys, Trp can be mutated to Ala). The mutated residues are those which side chains are pointing outside towards solvent thus causing minimal change to the basic structure of the allergen. The purpose of the mutagenesis is to modify the flat surface to convex surface which prevent the binding of IgE-antibodies. The effect of the mutation on the planar surface can be seen as lower affinity of the allergen specific IgE-antibody towards the modified allergen, preferably the mutation decreases the affinity of the specific antibody at least tenfold, more preferably more than tenfold. The resulting modified allergen can be used to evoke tolerance against particular allergens in allergic patients. Thus, the present invention provides a modified allergen carrying the type I planar epitope which has been distorted by the directed introduction of one or several mutations thereby decreasing the affinity towards the recombinant IgE molecule at least tenfold, preferably more than tenfold.
The present invention also provides a method to create tolerance in a patient for a specific allergen with a planar allergenic epitope comprising the steps of

    
    
        a) disrupting the planar surface of the allergen with a mutation decreasing the affinity of the IgE towards the epitope more than ten folds;
        b) producing the mutated allergen (i.e. hypoallergen);
        c) administering, preferably parentally, the mutated allergen into the patient one or several times.
    
    


The present invention also provides a method for the isolation of recombinant IgE monoclonal antibodies comprising the steps of

    
    
        a) isolating mRNA from IgE producing cells from a human derived sample;
        b) synthesizing of the cDNAs encoding the IgE Fd gene region and kappa/lambda light chain genes to create an IgE expression library;
        c) screening the expressed library against a polypeptide or protein carrying the planar (flat) type I surface typical for allergens and isolating clones showing medium or high affinity (over 107M−1) towards the planar surface;
        d) isolating the DNA encoding the IgE antibody obtained from step c).

Preferably said polypeptide is β-lactoglobulin and said planar surface is defined by the structure or 3D-coordinates of β-lactoglobulin amino acids Val43-Lys47 and Leu57-Gln59 and/or amino acids around these amino acids in an antibody-β-lactoglobulin immunocomplex (see Table VIII).

    
    


The present invention further provides a method for producing a modified allergenic polypeptide, the method comprising the steps of (a) modifying nucleic acid sequence encoding said polypeptide so that in the polypeptide expressed from the modified nucleic acid the structure of allergenic epitope of said polypeptide is altered, and (b) expressing or producing the modified allergenic polypeptide from the modified nucleic acid. Preferably step (b) comprises the steps of expressing said modified nucleic acid in a suitable host in a culture system and isolating said modified polypeptide from the culture, or producing synthetically of said modified polypeptide. Preferably said modified allergenic polypeptide is β-lactoglobulin, and/or said allergenic epitope is the planar surface as defined above, more preferably planar surface is defined by the structure or 3D-coordinates of β-lactoglobulin amino acids Val43-Lys47 and Leu57-Gln59 and/or amino acids around these amino acids, in an antibody-β-lactoglobulin immunocomplex. Said allergenic epitope can also be the epitope defined by structure coordinates of β-lactoglobulin amino acids Trp19 and Tyr20 from beta-strand A and Glu44 from beta-strand B in an antibody-β-lactoglobulin immunocomplex.
The present invention further provides a method for identifying a molecule binding to an allergenic epitope of an allergen; comprising the steps of: (a) contacting a particle, such as a virus particle, comprising the allergenic epitope and a candidate binder molecule; (b) isolating those candidate binder molecules which were able to bind to said allergenic epitope. Preferably said allergen is β-lactoglobulin, said molecule is a peptide, and said allergenic epitope is the planar surface as defined above; more preferably planar surface is defined by the structure or 3D-coordinates of β-lactoglobulin amino acids Val43-Lys47, and Leu57-Gln59 and/or amino acids around these amino acids in an antibody-β-lactoglobulin immunocomplex. A good approach in this method is the use of affinity chromatography.
Crystallographic and in Silico Screening
The three-dimensional structure of the allergenic epitope of β-lactoglobulin is defined by a set of structure coordinates as set forth below. The term “structure coordinates” refers to Cartesian coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of the allergenic epitope of β-lactoglobulin in crystal form of an antibody-allergen immunocomplex. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are then used to establish the positions of the individual atoms of the allergenic epitope of β-lactoglobulin.
Those of skill in the art will understand that a set of structure coordinates for a protein or a protein-complex or a portion thereof, is a relative set of points that define a shape in three dimensions. Thus, it is possible that an entirely different set of coordinates could define a similar or identical shape. Moreover, slight variations in the individual coordinates will have little effect on overall shape.
The variations in coordinates discussed above may be generated because of mathematical manipulations of the structure coordinates. For example, the structure coordinates set forth below could be manipulated by crystallographic permutations of the structure coordinates, fractionalization of the structure coordinates, integer additions or subtractions to sets of the structure coordinates, inversion of the structure coordinates or any combination of the above.
Alternatively, modifications in the crystal structure due to mutations, additions, substitutions, and/or deletions of amino acids, or other changes in any of the components that make up the crystal could also account for variations in structure coordinates. If such variations are within an acceptable standard error as compared to the original coordinates, the resulting three-dimensional shape is considered to be the same.
Various computational analyses are therefore necessary to determine whether a molecule or molecular complex or a portion thereof is sufficiently similar to all or parts of the allergenic epitope of β-lactoglobulin described herein as to be considered the same. Such analyses may be carried out in current software applications, such as the Molecular Similarity application of QUANTA (Molecular Simulations Inc., San Diego, Calif.) version 4.1, and as described in the accompanying User's Guide.
Once the structure coordinates of a protein crystal have been determined they are useful in solving the structures of other crystals, especially crystals of other similar proteins.
Thus, in accordance with the present invention, the structure coordinates of the allergenic epitope of β-lactoglobulin, and portions thereof is stored in a machine-readable storage medium. Such data may be used for a variety of purposes, such as drug discovery and x-ray crystallographic analysis or protein crystal.
Accordingly, in one embodiment of this invention is provided a machine-readable data storage medium comprising a data storage material encoded with the structure coordinates set forth below.
For the first time, the present invention permits the use of structure-based or rational drug design techniques to design, select, and synthesize chemical entities, including inhibitory compounds that are capable of binding to the allergenic epitope of β-lactoglobulin, or any portion thereof.
Those of skill in the art will realize that association of natural ligands or substrates with the binding pockets of their corresponding receptors or enzymes is the basis of many biological mechanisms of action. The term “binding site”, as used herein, refers to a region of a molecule or molecular complex that, as a result of its shape, favourably associates with another chemical entity or compound. Similarly, many drugs exert their biological effects through association with the binding pockets of receptors and enzymes. Such associations may occur with all or any parts of the binding pockets. An understanding of such associations will help lead to the design of molecules such as drugs having more favourable associations with their target receptor or enzyme, and thus, improved biological effects. Therefore, this information is valuable in designing potential ligands or inhibitors of receptors or enzymes.
The term “associating with” or “interacting with” refers to a condition of proximity between chemical entities or compounds, or portions thereof. The association or interaction may be non-covalent, wherein the juxtaposition is energetically favoured by hydrogen bonding or van der Waals or electrostatic interactions, or it may be covalent.
In iterative molecular design, crystals of a series of protein/compound complexes are obtained and then the three-dimensional structures of each complex are solved. Such an approach provides insight into the association between the proteins and compounds of each complex. This is accomplished by selecting compounds with inhibitory activity, obtaining crystals of this new protein/compound complex, solving the three-dimensional structure of the complex, and comparing the associations between the new protein/compound complex and previously solved protein/compound complexes. By observing how changes in the compound affected the protein/compound associations, these associations may be optimized.
In some cases, iterative molecular design is carried out by forming successive protein-compound complexes and then crystallizing each new complex. Alternatively, a pre-formed protein crystal is soaked in the presence of an inhibitor, thereby forming a protein/compound complex and obviating the need to crystallize each individual protein/compound complex. Advantageously, the allergenic epitope of β-lactoglobulin crystals, may be soaked in the presence of a compound or compounds, such as antibodies, to provide β-lactoglobulin/antibody crystal complexes.
As used herein, the term “soaked” refers to a process in which the crystal is transferred to a solution containing the compound of interest.
The Storage Medium
The storage medium in which the atomic co-ordinates are provided is preferably random access memory (RAM), but may also be read-only memory (ROM e.g. CDROM), or a diskette. The storage medium may be local to the computer, or may be remote (e.g. a networked storage medium, including the internet).
The invention also provides a computer-readable medium for a computer, characterised in that the medium contains atomic co-ordinates of the allergenic epitope of β-lactoglobulin.
The atomic co-ordinates are preferably those set forth below, or variants thereof.
Any suitable computer can be used in the present invention.
Molecular Modelling Techniques
Molecular modelling techniques can be applied to the atomic co-ordinates of the allergenic epitope of β-lactoglobulin to derive a range of 3D models and to investigate the structure of ligand binding sites. A variety of molecular modelling methods are available to the skilled person for use according to the invention.
At the simplest level, visual inspection of a computer model of the allergenic epitope of β-lactoglobulin can be used, in association with manual docking of models of functional groups into its binding sites.
Software for implementing molecular modelling techniques may also be used. These molecular modelling techniques allow the construction of structural models that can be used for in silico drug design and modelling.
De Novo Compound Design
The molecular modelling steps used in the methods of the invention may use the atomic co-ordinates of the allergenic epitope of β-lactoglobulin, and models derived therefrom, to determine binding surfaces.
This preferably reveals van der Waals contacts, electrostatic interactions, and/or hydrogen bonding opportunities.
These binding surfaces will typically be used by grid-based techniques (e.g. GRID [Goodford (1985) J. Med. Chem. 28: 849-857], CERIUS2) and/or multiple copy simultaneous search (MCSS) techniques to map favourable interaction positions for functional groups. This preferably reveals positions in the allergenic epitope of β-lactoglobulin for interactions such as, but not limited to, those with protons, hydroxyl groups, amine groups, hydrophobic groups (e.g. methyl, ethyl, benzyl) and/or divalent cations.
Once functional groups or small molecule fragments which can interact with specific sites in the binding surface of the allergenic epitope of β-lactoglobulin have been identified, they can be linked in a single compound using either bridging fragments with the correct size and geometry or frameworks which can support the functional groups at favourable orientations, thereby providing a compound according to the invention. Whilst linking of functional groups in this way can be done manually, perhaps with the help of software such as QUANTA or SYBYL, the following software may be used for assistance: HOOK [Available from Molecular Simulations Inc], which links multiple functional groups with molecular templates taken from a database, and/or CAVEAT [Lauri & Bartlett (1994) Comp. Aided Mol. Design. 8: 51-66], which designs linking units to constrain acyclic molecules.
Docking
Compounds in known in silico libraries can also be screened for their ability to interact with the allergenic epitope of β-lactoglobulin by using their respective atomic co-ordinates in automated docking algorithms.
Suitable docking algorithms include: DOCK [Kuntz et al. (1982) J. Mol. Biol. 161: 269-288], AUTODOCK [Available from Oxford Molecular], MOE-DOCK [Available from Chemical Computing Group Inc.] or FLEXX [Available from Tripos Inc.]. Docking algorithms can also be used to verify interactions with ligands designed de novo.
Focused IgE-Antibody Library Towards Allergens
The amino acid sequence comparison of published IgE sequences reveals that the light chains of the known IgE antibodies binding to diverse groups of allergens are strikingly conserved (see Table VII). This gives tools to construct focused allergen specific libraries that can be utilised for the isolation of allergen specific antibodies applicable in the diagnosis of allergens. The conserved light chain sequence information is used to construct a limited pool of light chains or a single light chain with the characteristic amino acid sequences identified in the IgE antibodies. This light chain sequence information is combined with a diverse pool of IgE heavy chain genes isolated from lymphocytes of several allergic patients. The resulting antibody phage display library, in either scFv or Fab display format, is used to select allergen specific IgE antibodies essentially as described in Example 1/II and Hoogenboom et al. (1998).
Human Antibody (scFv, Fab or Whole Antibody) Libraries Containing the Human IgE VH-Regions
The IgE VH-region of the D1 IgE Fab and especially the HCDR3 loop are structurally different when compared to IgG antibodies. It is forming a loop structure that is recognizing a cleft on the BLG-allergen structure. Based on this observation it should be possible to develop human IgE VH-region containing antibodies for those therapeutic targets where the binding specificity is required towards protein structures that are not exposed on the surface, e.g., substrate binding sites of enzymes and drug resistance pumps (De Genst et al. 2006). A diverse IgE VH-pool from human lymphocytes is used as a building block to construct a functional human antibody library in a scFv, Fab or whole antibody format. Resulting libraries are selected against therapeutic targets requiring specific recognition of cleft structures.
The development and characterisation of the human β-lactoglobulin-binding recombinant antibodies and their usefulness in immunoassays is now described in more detail in the following examples.
EXAMPLE 1
The Recombinant β-Lactoglobulin-Specific scfv Fragment by Phage Display Selection
In this example the human IgE scFv library was constructed and selected by allergenic β-lactoglobulin in order to isolate scFv fragments with affinity and specificity to β-lactoglobulin (BLG). Construction of human IgE scFv phage library was prepared indirectly by constructing IgE Fab-κ and Fab-λ, libraries first, and then the particular library DNAs were used for PCR amplification of variable domains of heavy and light chains.
I. Construction of the Human IgE scFv Phage Libraries
50 ml of heparinised blood was obtained from a milk-allergic patient. Lymphocytes were isolated according to an Ig-Prime kit protocol (Novagen). Per 10 ml of blood 30 ml of lysis buffer (155 mM NH4Cl, 10 mM NH4HCO3, 0.1 mM EDTA, pH 7.4) was added and incubated on ice for 15 min with shaking occasionally. After centrifugation at 450 g for 10 min the lymphocytes, i.e. the white blood cell pellet, were collected. The pellet was washed twice with lysis buffer and after the final centrifugation the lymphocyte pellet was resuspended in D-solution. Lymphocyte RNAs were isolated using Promega's RNAgents Total RNA Isolation kit according to the manufacturer's protocol. The first strand cDNA synthesis was carried out using Promega's Reverse Transcription system kit. For the synthesis of Fd-fragment cDNA and light chain cDNAs the primers of the constant region of the epsilon (ε) chain (Cε1) and the primer of the kappa (Cκ1) and lambda (Cλ1) chain were used, respectively. Primers used for the cDNA synthesis and PCR amplifications of human IgE Fd region and light chains are showed in Table I and Table II.
PCR amplifications were carried out in two steps: a primary PCR for amplifying Fd and light chains from cDNA templates and a secondary PCR for adding restriction sites to the 5′-end of the DNA fragments obtained after a primary PCR. First the Fd region was amplified by PCR using the primers specific for the variable region of the heavy chains (VH1a-VH7a) and Cε1primer. Accordingly, the kappa and lambda light chains were amplified using specific primers for variable region of the light chains (Vκ1a-Vκ6b and Vλ1a-Vλ10) and Cκ/λ1 primer, respectively. Primers for the secondary PCR were Cκ1 and Vκ/λ1 and Cκ for the kappa light region, Vκ/λ1 and Cλ1 for the kappa light chain and Vλ1A and Cκ/λ1 for the lambda light chain. The primary PCR amplification was done at the following conditions: 1 cycle of 3 min at 93° C. for denaturation, 7 cycles of 1 min at 93° C., 30 s at 63° C. and 50 s at 58° C. for annealing and 1 min at 72° C. for elongation, 23 cycles of 1 min at 93° C., 30 s at 63° C. and 1 min at 72° C. followed by 1 cycle of 10 min at 72° C. For the secondary PCR the amplification conditions were as follows: 1 cycle of 3 min at 95° C. for denaturation, 25 cycles of 1.5 min at 94° C., 1 min at 65° C. for annealing and 1.5 min at 72° C. for elongation followed by 1 cycle of 10 min at 72° C. Between the primary and the secondary PCR and after the secondary PCR the amplified DNA fragments were purified.
The final PCR products of the different antibody fragments were pooled and digested with appropriate restriction enzymes. Digested DNA fragments, encoding IgE Fd region and κ and λ light chains, were ligated into a phagemid vector and transformed into E. coli XL-1 Blue cells to yield an Fab-κ and Fab-λ libraries of 106 independent clones. To avoid possible problems on the expression of Fab fragments on a phage particle an antibody library in scFv format was constructed. Phagemid DNAs from different libraries were isolated and used as template DNAs for amplifying the variable regions of the human IgE heavy and human light chains in order to construct human IgE scFv-κ and scFv-λ libraries.
PCR amplification of the variable region of the heavy chain was carried out using human VH specific primers (VH1-VH4 and VH1A). Amplification of the variable region of the light chains was done using the following primer pairs: Vκ1-Vκ7, Vκ2-Vκ8, Vκ3-Vκ9, Vκ-4-Vκ10, Vκ5-Vκ11 and Vκ6-Vκ11 for human kappa chain and Vλ1-Vλ8, Vλ2-Vλ9, Vλ3-Vλ9, Vλ4-Vλ9, Vλ5-Vλ10, Vλ6-Vλ10 and Vλ7-Vλ10 for human lambda chain (see Tables III and IV). The amplified DNA fragments were purified and digested in order to ligate into a scFv phage display vector (FIG. 3). Ligation mixtures were transformed into E. coli XL-1 Blue cells resulting in the human IgE scFv-κ and scFv-λ libraries with approximately 105 independent clones.
II. Selection of the Human scFv-Libraries
The human scFv-κ and scFv-λ, libraries were selected by the phage display technique (McCafferty et al., 1990, Barbas et al., 1991). To isolate β-lactoglobulin-binding antibody fragments, the human IgE scFv-κ and scFv-λ, libraries displayed on the surface of the bacteriophage were panned using an affinity panning procedure (FIG. 2). First the phage pools were allowed to react either with biotinylated, immunoreactive β-lactoglobulin or as a negative control, without antigen for 1.5 h. Thereafter, the phage pools were transferred to microtitre plate wells coated with biotin binding streptavidin. After a 30-min incubation, the wells were washed 3 times with PBS+0.05% Tween20 and the binders were eluted with soluble antigen (100 μM nonbiotinylated β-lactoglobulin AB dimer). For the next panning round the eluted phage pools were amplified by infecting E. coli XL-1 Blue cells. Two rounds of panning were performed.
III. Characterisation of the β-Lactoglobulin-Binders
After the last panning cycle scFv phage display DNA was isolated and transformed into E. coli HB2151 (supE−) cells in order to express soluble scFv fragments. Between the scFv sequence and the phage gene III sequence the scFv phage display vector contains TAG-amber stop codon which will be translated as glutamate in E. coli strains with supE+ genotype but as a stop codon in E. coli strains with supE− genotype. Sixty-two individual clones were grown in a small scale to produce soluble scFv fragments for preliminary characterisation. Clones were analysed on ELISA test using β-lactoglobulin-coated wells to catch the β-lactoglobulin-specific binders and control protein wells to see non-specific binding (data not shown). Most of the clones bound with high affinity to β-lactoglobulin. Clones were analyzed first by DNA-fingerprinting and six of the clones were sequenced (Sanger et al., 1977). Finally, one of the clones was selected for further characterisation (FIGS. 4 and 5).
EXAMPLE 2
Cloning and Characterisation of Human Fab Fragment with β-Lactoglobulin-Binding Specificity 
In this example the human IgE scFvs with β-lactoglobulin-binding specificity was converted to human Fab fragments with IgG1 subtype. Due to known difficulties in forming multimers, the D1 scFv, obtained from the scFv antibody library, was cloned and bacterially expressed as Fab fragments (Holliger et al., 1993, Desplancq et al., 1994). The resulting antibody fragments were further characterised by a competitive ELISA.
I. Cloning of the Human Fab Fragments with β-Lactoglobulin-Binding Specificity
The Fd regions were amplified by overlapping PCR. The primers used for the PCR are given in Table V.
The resulting cDNAs of the Fd region and light chains were cloned into the bacterial expression vector, pKKtac and then transformed into E. coli RV308. Soluble Fab fragment designated to D1 IgE Fab was produced by fermentation (Nevanen et al, 2001) and the Fab fragment was purified by an introduced C-terminal hexahistidinyl tag on a Sepharose column with immobilised nickel to a substantial purity (data not shown).
II. Characterisation of the Human IgE Fab Fragments
The characterisation of the purified D1 IgE Fab was performed by competitive ELISA. First, increasing amounts of the soluble, non-biotinylated β-lactoglobulin was incubated with the D1 IgE Fab, and then the reaction mixtures were applied onto Streptavidin microtitre plate wells coated with allergenic, biotinylated β-lactoglobulin. FIG. 6 shows the result of the competitive ELISA. The binding of the D1 IgE Fab (FIG. 6) to biotinylated β-lactoglobulin could be inhibited by adding increasing amounts of native β-lactoglobulin.
To study if the D1 IgE Fab is able to bind β-lactoglobulin from milk samples, the immunoprecipitation assay was performed (FIG. 7). The D1 IgE Fab was immobilized via kappa light chain to protein L beads and this complex was introduced to milk samples, which were heated for various times (0, 15, 30 and 60 min). The D1 IgE Fab bound to the protein L beads was incubated with milk samples 1 hour at room temperature and after this, the beads were washed several times with PBS+0.05% Tween20 to remove unspecific binding of the milk proteins to protein L beads. The D1 IgE Fab β-lactoglobulin complex was eluted from protein L-beads with low pH (0.1 M Glycine, pH 2.1) and the eluted fraction was neutralized with 3 M Tris, pH 8.8. A small portion of the elution fraction was analyzed with 15% SDS-PAGE followed by silver staining. The correct size bands were cut out from the SDS-PAGE gel and further analyzed by mass spectrometry to confirm that the protein, which D1 IgE Fab recognised from cow milk was β-lactoglobulin.
To study if the D1 IgE Fab recognizes the same allergenic epitope as the IgE antibodies from patient serum, the biotinylated β-lactoglobulin was first immobilised to a microtitre plate wells coated with streptavidin. The patient serum samples were incubated in the wells together with increasing concentrations of D1 IgE Fab and the amount of the bound patient serum IgE was detected with alkaline phosphatase labelled secondary antibody, which specifically recognizes the human IgE isotype. A slight inhibition can be seen in the case of each patient tested, suggesting that the epitope which D1 IgE Fab recognizes is the same as the IgE from the patient serum. The reason why the binding of the patient serum IgE is not totally blocked, might be that the β-lactoglobulin harbours a multiple IgE-epitopes.
EXAMPLE 3
I. Crystallisation of the Antibody-Allergen Immunocomplex
Crystallization and data collection Microcrystals (about 70×50×50 μm) of BLG-D1 IgE Fab were obtained with vapour diffusion method by mixing 2 μl of D1/Fab solution (concentration 1.4 mg/ml in 20 mM phosphate buffer, pH 7.0), 1 μl BLG solution (2 mg/ml in pure water), 0.5 μl of n-dodecyl-β-D-maltoside solution, and 2.5 μl of reservoir solution (14% (w/v) polyethylene glycol 3350, 0.1 M BTP (1,3-bis[tris(hydroxymethyl)methylamino]propane-hydrochloric acid) buffer, pH 5.5). The diffraction data set was collected from single crystal at the beamline ID29 in ESRF (wavelength 1.000 Å) at 100 K. The crystal belonged to the space group P212121 with unit-cell dimensions a=67.0, b=100.6, c=168.1 Å. The data set was collected at 2.8 Å resolution.
II. Structure Determination of Antibody-Allergen Immunocomplex 
The structure was solved with the molecular replacement method using Molrep program implemented in CCP4 program package. BLG monomer (PDB code 1B8E) and Fab fragment of IgG antibody against GP41 of HW virus (1DFB) (identity 92% for light and 79% for heavy chain) were used as search models. The final structure contained one dimer of BLG complexed with two Fab fragments. Model building and refinement were done with the programs O and CNS. Because of low number of reflections restraints were used to keep both Fab/D1 fragments and BLG monomers similar. BLG exist in two isomers, the electron density suggested that we have glycine at position 64 and alanine at position 118. No water molecules were added but the elongated electron density in the lipid binding cavity of BLG was modelled as an n-dodecyl-β-D-maltoside. The final structure has an R value 24.5% and an Rfree value of 29.9%. 83.5% of the residues are in the most favoured regions and 0.6% of the residues in the disallowed regions in the Ramachandran plot. All figures were generated with Pymol (Delano, W. L. The PyMol Molecular Graphics System, http://www.pymol.org).
EXAMPLE 4
Inhibition of the D1 IgE Fab binding to BLG was carried out using a short peptide, KRVG that is the longest linear BLG binding peptide in the HCDR3. In competitive ELISA the biotinylated AB dimer of BLG was immobilised onto streptavidin-coated microtitre wells. First the peptide (an inhibitor) was dissolved into 0.5% BSA-PBS and then different amounts of it were incubated with the immobilised BLG. After that the wells were either washed trice with PBS or not. D1 IgE Fab was added and followed by the washings with PBS. The bound antibody was detected with AFOS-conjugated goat anti-human kappa antibody. After addition of the substrate, p-nitrophenylphosphatase, the absorbance values were read at 405 nm. The results are shown in FIG. 15.
EXAMPLE 5
The Identification of a Flat Epitope by Calculation of Molecular Surface and Curvature 
In this example we have used commercial AMIRA program (with AmiraMol module) to calculate the solvent excluded surface (probe radius 10 Å). The surfaces are coloured according to the Gaussian curvature which is the product of the two principal curvatures. It is negative in surface areas with hyperbolic geometry (convex-concave, like near saddle points) and positive in areas with elliptic geometry (strictly convex or strictly concave).
We have also used AMIRA program to calculate molecular interface area (cutoff 3 Å). The program shows a surface which is located exactly in the middle between two proteins. In FIG. 17 examples for antibody binding to flat (BLG D1(IgE/Fab)), convex (Bet v 1-IgG/Fab; 1BV1) and concave (lysozyme-single chain camel antibody; 1MEL) epitopes are shown.
It is thus possible to calculate the molecular surface by using a large probe value (preferably 8-12 Å) for allergens if their three-dimensional structure is available. Such molecular surfaces can be rotated and looked in all directions and with the aid of curvature coloured surfaces a large flat area (600-900 Å2) can be identified. In FIG. 18 we represent molecular surfaces for five allergens. The first one is BLG (Bos d 5) and the flat epitope is shown in two orientations. In the following pictures similar flat areas from four other allergens, Bet v 1, Bos d 2, Phl p 7, and Hey b 6 are identified. These are suggested flat epitopes for IgE binding. The four allergens represent structurally very different classes. Bos d 5 and Bos d 2 are β-proteins (consisting mainly of β-strands). Bet v 1 has both β-strands and α-helices. Phl p 7 has only α-helices and Hev b 6 is a small protein with low secondary structure content.
EXAMPLE 6
Characterisation of Recombinant β-Lactoglobulin and its Mutants
Based on the D1 IgE and the BLG immunocomplex structure, mutations were designed to the flat surface epitope on the BLG in order to produce hypoallergenic variants. Two different recombinant BLG (rBLG) mutants, T18Y and T18Y/E45Y/L57Y, were constructed (Table IX). The cDNAs encoding the rBLG and its mutants were cloned into bacterial expression vector, produced in Escherichia coli cells, chromatographically purified to a substantial purity and finally their properties were characterised.
I. Cloning of the Recombinant BLGs
The bovine recombinant BLG (rBLG) cDNA was purchased from GenScript Corporation (USA) in vector pUC57 and it contained the restriction sites of SfiI/NcoI at the 5′end and HindIII at the 3′end (Table X). The rBLG cDNA was cloned into pKKTac bacterial expression vector with the fusion of the Ervinia carotovora's pectate lyase (pelB) signal sequence (Takkinen et al., 1991) as an SfiI-HindIII fragment. The hexa histidinyl (His6) tag was introduced into 3′end of the rBLG cDNA by PCR amplification using primers 1 and 2 (Table X). Phusion DNA polymerase (Finnzymes) was used in all PCR amplifications. The amplified cDNA of rBLG-His6 was digested with SfiI and HindIII (New England Biolabs) and cloned into pKKTac expression vector. Escherichia coli XL-1 Blue was used as a host strain to construct the recombinant BLG (rBLG) and its mutants.
Two different rBLG mutants, T18Y and T18Y/E45Y/L57Y (Table IX), were cloned into pKKtac vector. The cDNAs of the rBLG-His6 T18Y and T18Y/E45Y/L57Y mutant were amplified with PCR using mismatch primers 2, 3, 4 and 5 (Table X) and the original rBLG cDNA in pUC57 vector as a template. The cDNA encoding the T18Y mutant was amplified using primers 2 and 3 and the amplified cDNA was digested with StuI and HindIII (New England Biolabs) and cloned into the pKKtac/rBLG-His6 vector (see above). The cDNA encoding the T18Y/E45Y/L57Y mutant was amplified in two steps using overlapping primers. First, the cDNA fragment of 27-165 bp was amplified using primers 3 and 4 and the cDNA fragment of 147-530 bp with the 2 and 5. Then the resulting DNA fragments were combined by overlapping PCR amplification. The primer 4 and 5 have an overlapping sequence. Finally the cDNA encoding the T18Y/E45Y/L57Y mutant was digested with StuI and HindIII and cloned into pKKTac/rBLGhis expression vector.
The DNA sequences of the rBLG-His6 and its mutants were verified by DNA sequencing (ABI 3100 Genetic Analyzer, Applied Biosystems).
II. Production of the Recombinant BLGs
The rBLG-His6 and its mutants were transformed into E. coli RV308 (ATCC 31608) strain for the bacterial expression of the rBLGs. Single colonies of each clone were inoculated into 3 ml LB, 100 μg/ml ampicillin and 1% glucose and cultivated for 16 h at +37° C. with 220 rpm shaking. Then the cultivations were 1:50 diluted into 3 ml LB with ampicillin and cultivated 3 hours at +37° C. After that the protein expression was induced by the addition of IPTG to a final concentration of 1 mM and cells were cultivated for 16 h at +30° C. with 220 rpm shaking. Then the cells were harvested and the supernatants were stored for later use. The periplasmic fraction of the cells was isolated by a freeze-thaw method (Boer et al., 2007). Briefly, cells were resuspended in 20% sucrose, 30 mM Tris, 1 mM EDTA (pH 8.0) and then incubated 5 min in dry ice-ethanol bath followed by the resuspension in 5 mM MgSO4 and incubation for 5 min at +37° C., and this freezing and thawing step was repeated trice. The supernatant and the periplasmic fractions were analysed by western blotting. First the samples were run on a 15% SDS-PAGE gel (with β-mercaptoethanol) and then the proteins were transferred onto the nitrocellulose filter. The rBLGs were detected using rabbit anti-BLG antibody (Mäkinen-Kiljunen and Palosuo, 1992) followed by AFOS-conjugated goat anti-rabbit antibody (Bio-Rad).
During the bacterial production the recombinant BLGs were secreted into the periplasmic space with almost no leakage into culture medium. For the large scale production of the rBLGs the cells containing the rBLG-His6 and its mutants in pKKTac vector in E. coli RV308 strain were inoculated TB medium containing 100 μg/ml ampicillin, 1% glucose. The cells were cultivated for 16 h at +37° C. with 220 rpm shaking. Then the cell cultures were 1:50 diluted into TB medium with 100 μg/ml ampicillin. The cells were grown at +37° C. with 220 rpm shaking until the OD600 was 4 and IPTG was added to a final concentration of 0.1 mM. The induction of the cells was carried out for 6 h at +28° C. with 220 rpm shaking. Then the cells were harvested by centrifugation with 4000×g for 15 min at +4° C. The periplasmic fractions containing the recombinant BLGs were isolated by freeze-thaw method as above.
III. Purification of the rBLGs
The purification of recombinant BLGs was performed using immobilised metal affinity chromatography (IMAC) as described earlier (Porath and Olin, 1983). Briefly, periplasmic fractions containing the rBLGs were 1:2 diluted with the binding buffer (10 mM Hepes, 1M NaCl, 10% Glyserol, 1 mM imidazole, pH 7.4) and incubated with Ni2+-loaded Chelating Sepharose (Pharmacia) for 16 h at +4° C. The column matrix with bound rBLGs was loaded into the column with gravity flow and washed stepwise with 1 mM, 10 mM, 20 mM and 50 mM imidazole in the binding buffer. Finally, the rBLGs were eluted with 75 mM, 100 mM, 200 mM and 5×500 mM imidazole in the binding buffer and 2 ml fractions were collected. The eluted fractions were analysed on 15% SDS-PAGE gel (with β-mercaptoethanol). The fractions containing the desired proteins were pooled and the IMAC-purification was repeated in a smaller scale. After the second IMAC-purification the fractions were analysed again on a SDS-PAGE gel (FIG. 19). As a result the fractions containing the particular purified BLG were pooled, dialysed against 10 mM HEPES, 0.9% NaCl, pH 7.4 for 16 h at +4° C. The purified proteins were analysed by western blotting using rabbit anti-BLG antibody and AFOS-conjugated goat anti-rabbit antibody detection (FIG. 20).
IV. Circular Dichroism Measurements
For circular dichroism (CD) measurements the buffer of all rBLGs was exchanged into 5 mM Hepes (pH 7.4) using Econo Pac 10DG desalting columns (Bio-Rad) with the cut of 6000 Da. Far-UV spectrum of the native BLG (nBLG, Sigma), rBLG-His6 and the rBLG-His 6 mutants was measured with Jasco J-715 spectropolarimeter at +20° C. controlled with a Peltier thermostat (Jasco PTC-348WI) using a 1-mm quartz cell. The concentrations of the proteins were 1 mg/ml for nBLG, 0.25 mg/ml for rBLG-His6, 1.3 mg/ml for rBLG-His6 T18Y and 0.93 mg/ml for rBLG-His6 T18Y/E45Y/L57Y mutant. The CD-spectra shown are averages of three measurements (FIG. 21).
V. Characterisation of the D1 IgE Fab Binding to rBLGs by ELISA
First the rBLGs were biotinylated. The biotinylation of the rBLGs was performed with Sulfo-NHS-LC-biotin (Pierce) in a molar ratio of 2 mol biotin:1 mol protein in 10 mM Hepes, 0.9% NaCl for 30 min at RT with a gentle shaking. The unreacted biotin was removed using Econo Pac 10 DG desalting columns (Bio-Rad). The incorporation of the biotin to the rBLGs was analysed by western blotting using SA-AFOS detection.
Then 1 μg biotinylated nBLG, rBLG-His6, rBLG-His6 T18Y mutants in 110 μl 0.5% BSA/PBS were immobilised onto the streptavidin microtitre wells (Roche) for 1 h at RT. After that 100 μl 1:15000 diluted anti-BLG D1 Fab (1.6 mg/ml) in 0.5% BSA, PBS was added to the washed wells. After a 1-h incubation the wells were washed three times with PBS. The detection of the BLGs was carried out using AFOS-conjugated goat anti-human kappa antibody (Southern Biotech). Then p-nitrophenylphosphate substrate (Sigma) was added to the wells (2 mg/ml in diethanolamine buffer). The absorbance at the wavelength 405 nm was measured after 20 minutes of adding the substrate (FIG. 22).
The ELISA analysis with the serum samples (1:8 dilution in 0.5% BSA, PBS) was performed as above except the bound IgE from allergic patient serum was detected with AFOS-conjugated goat anti-human IgE (Southern Biotech). The absorbances were measured at 405 nm after a 2-h incubation of adding the substrate (FIG. 23).
VI. Analysis of the Binding Kinetics
The association and dissociation constants of the D1 IgE Fab to nBLG, rBLG-His6 and its mutants were measured by BIAcore. The biotinylated BLGs were immobilised in HBS buffer (10 mM Hepes, 0.15M NaCl, 3.4 mM EDTA, 0.005% BIAcore P20 surfactant, pH 7.4) and at a concentration of 1 μg/ml onto the streptavidin biosensor chip resulting in a surface of approximately 400-500 RU. The biotinylated nBLG was immobilised only with 200 RU onto the surface of the SA-chip. The binding kinetics of the purified D1 IgE Fab was analysed at a flow rate of 30 μl/min with the concentrations 138.9 nM, 69.6 nM, 34.8 nM, 17.4 nM, 8.7 nM, 4.3 nM, 2.2 and 1.1 nM. Regeneration of the BLG surface was performed with 100 μM nBLG (Sigma). Binding curves of the 69.6 nM D1 IgE Fab solution are shown in FIG. 24.
TABLE I: Primers used for eDNA synthesis and PCR amplification of the human IgE Fd region.







TABLE I





Primers used for cDNA synthesis and PCR


amplification of the human IgE Fd region.
















Cε1:
5′-GCTGAAGGTTTTGTTGTCGACCCAGTC-3′



(SEQ ID NO: 12) 


 


CεNotI:
5′-GAATGGTGCGGCCGCGCTGAAGGTTTTGTTGTCG-3′



(SEQ ID NO: 13)


 


VH1a:
5′-ATGGCCGCAGCTCAGGTKCAGCTGGTGCAG-3′



(SEQ ID NO: 14)


 


VH1b:
5′-ATGGCCGCAGCTCAGGTCCAGCTTGTGCAG-3′



(SEQ ID NO: 15)


 


VH1c:
5′-ATGGCCGCAGCTSAGGTCCAGCTGGTACAG-3′



(SEQ ID NO: 16)


 


VH1d:
5′-ATGGCCGCAGCTCARATGCAGCTGGTGCAG-3′



(SEQ ID NO: 17)


 


VH2a:
5′-ATGGCCGCAGCTCAGATCACCTTGAAGGAG-3′



(SEQ ID NO: 18)


 


VH2b:
5′-ATGGCCGCAGCTCAGGTCACCTTGARGGAG-3′



(SEQ ID NO: 19)


 


VH3a:
5′-ATGGCCGCAGCTGARGTGCAGCTGGTGGAG-3′



(SEQ ID NO: 20)


 


VH3b:
5′-ATGGCCGCAGCTCAGGTGCAGCTGGTGGAG-3′



(SEQ ID NO: 21)


 


VH3c:
5′-ATGGCCGCAGCTGAGGTGCAGCTGTTGGAG-3′



(SEQ ID NO: 22)


 


VH4a:
5′-ATGGCCGCAGCTCAGSTGCAGCTGCAGGAG-3′



(SEQ ID NO: 23)


 


VH4b:
5′-ATGGCCGCAGCTCAGGTGCAGCTACAGCAG-3′



(SEQ ID NO: 24)


 


VH5a:
5′-ATGGCCGCAGCTGARGTGCAGCTGGTGCAG-3′



(SEQ ID NO: 25)


 


VH6a:
5′-ATGGCCGCAGCTCAGGTACAGCTGCAGCAG-3′



(SEQ ID NO: 26)


 


VH7a:
5′-ATGGCCGCAGCTCAGGTSCAGCTGGTGCAA-3′



(SEQ ID NO: 27)


 


VH1A:
5′-TTACTCGCGGCCCAGCCGGCCATGGCCGCAGCT-3′



(SEQ ID NO: 28)









TABLE II: Primers used for cDNA synthesis and PCR amplification of human kappa and lambda chains.







TABLE II





Primers used for cDNA synthesis and PCR


amplification of human kappa and lambda chains.
















Cκ1:
5′-AGGTAGGGCGCGCCTTAACACTCTCCCCTGTTGAAGC-3′



(SEQ ID NO: 29)


 


Vκ1a:
5′-ATGGCAGCGGCTRACATCCAGATGACCCAG-3′



(SEQ ID NO: 30)


 


Vκ1b:
5′-ATGGCAGCGGCTGMCATCCAGTTGACCCAG-3′



(SEQ ID NO: 31)


 


Vκ1c:
5′-ATGGCAGCGGCTGCCATCCRGATGACCCAG-3′



(SEQ ID NO: 32)


 


Vκ1d:
5′-ATGGCAGCGGCTGTCATCTGGATGACCCAG-3′



(SEQ ID NO: 33)


 


Vκ2a:
5′-ATGGCAGCGGCTGATATTGTGATGACCCAG-3′



(SEQ ID NO: 34)


 


Vκ2b:
5′-ATGGCAGCGGCTGATRTTGTGATGACTCAG-3′



(SEQ ID NO: 35)


 


Vκ3a:
5′-ATGGCAGCGGCTGAAATTGTGTTGACRCAG-3′



(SEQ ID NO: 36)


 


Vκ3b:
5′-ATGGCAGCGGCTGAAATAGTGATGACGCAG-3′



(SEQ ID NO: 37)


 


Vκ3c:
5′-ATGGCAGCGGCTGAAATTGTAATGACACAG-3′



(SEQ ID NO: 38)


 


Vκ4a:
5′-ATGGCAGCGGCTGACATCGTGATGACCCAG-3′



(SEQ ID NO: 39)


 


Vκ5a:
5′-ATGGCAGCGGCTGAAACGACACTCACGCAG-3′



(SEQ ID NO: 40)


 


Vκ6a:
5′-ATGGCAGCGGCTGAAATTGTGCTGACTCAG-3′



(SEQ ID NO: 41)


 


Vκ6b:
5′-ATGGCAGCGGCTGATGTTGTGATGACACAG-3′



(SEQ ID NO: 42)


 


Vk/λ1:
5′-TTGTTATTGCTAGCTGCACAACCAGCAATGGCAGCGGCT-3′



(SEQ ID NO: 43)


 


Cλ1:
5′-AGGTAGGGCGCGCCTTATGAACATTCYGYAGGGGC-3′



(SEQ ID NO: 44)


 


Vλ1a:
5′-ATGGCAGCGGCTCAGTCTGTGCTGACTCAG-3′



(SEQ ID NO: 45)


 


Vλ1b:
5′-ATGGCAGCGGCTCAGTCTGTGYTGACGCAG-3′



(SEQ ID NO: 46)


 


Vλ1c:
5′-ATGGCAGCGGCTCAGTCTGTCGTGACGCAG-3′



(SEQ ID NO: 47)


 


Vλ2:
5′-ATGGCAGCGGCTCAGTCTGCCCTGACTCAG-3′



(SEQ ID NO: 48)


 


Vλ3a:
5′-ATGGCAGCGGCTTCCTATGWGCTGACTCAG-3′



(SEQ ID NO: 49)


 


Vλ3b:
5′-ATGGCAGCGGCTTCCTATGAGCTGACACAG-3′



(SEQ ID NO: 50)


 


Vλ3c:
5′-ATGGCAGCGGCTTCTTCTGAGCTGACTCAG-3′



(SEQ ID NO: 51)


 


Vλ3d:
5′-ATGGCAGCGGCTTCCTATGAGCTGATGCAG-3′



(SEQ ID NO: 52)


 


Vλ4C:
5′-ATGGCAGCGGCTCAGCYTGTGCTGACTCAA-3′



(SEQ ID NO: 53)


 


Vλ5:
5′-ATGGCAGCGGCTCAGSCTGTGCTGACTCAG-3′



(SEQ ID NO: 54)


 


Vλ6:
5′-ATGGCAGCGGCTAATTTTATGCTGACTCAG-3′



(SEQ ID NO: 55)


 


Vλ7:
5′-ATGGCAGCGGCTCAGACTGTGGTGACTCAG-3′



(SEQ ID NO: 56)


 


Vλ8:
5′-ATGGCAGCGGCTCAGACTGTGGTGACCCAG-3′



(SEQ ID NO: 57)


 


Vλ4/9:
5′-ATGGCAGCGGCTCWGCCTGTGCTGACTCAG-3′



(SEQ ID NO: 58)


 


Vλ10:
5′-ATGGCAGCGGCTCAGGCAGGGCTGACTCAG-3′



(SEQ ID NO: 59)









TABLE III: Primers used for PCR amplification of the human variable regions of the heavy chain.







TABLE III





Primers used for PCR amplification of the human


variable regions of the heavy chain.
















VH1:
5′-ATTTACTCGAGTGAGGAGACGGTGACCAGGGTGCC-3′



(SEQ ID NO: 60)


 


VH2:
5′-ATTTACTCGAGTGAAGAGACGGTGACCATTGTCCC-3′



(SEQ ID NO: 61)


 


VH3:
5′-ATTTACTCGAGTGAGGAGACGGTGACCAGGGTTCC-3′



(SEQ ID NO: 62)


 


VH4:
5′-ATTTACTCGAGTGAGGAGACGGTGACCGTGGTCCC-3′



(SEQ ID NO: 63)


 


VH1A:
5′-TTACTCGCGGCCCAGCCGGCCATGGCCGCAGCT-3′



(SEQ ID NO: 64)









TABLE IV: Primers used for PCR amplification of the human variable regions of the light chains.







TABLE IV





Primers used for PCR amplification of the human


variable regions of the light chains.
















Vκ1:
5′-TTATAGAGCTCGACATCCAGATGACCCAGTCTCC-3′



(SEQ ID NO: 65)


 


Vκ2:
5′-TTATAGAGCTCGATGTTGTGATGACTCAGTCTCC-3′



(SEQ ID NO: 66)


 


Vκ3:
5′-TTATAGAGCTCGAAATTGTGTTGACGCAGTCTCC-3′



(SEQ ID NO: 67)


 


Vκ4:
5′-TTATAGAGCTCGACATCGTGATGACCCAGTCTCC-3′



(SEQ ID NO: 68)


 


Vκ5:
5′-TTATAGAGCTCGAAACGACACTCACGCAGTCTCC-3′



(SEQ ID NO: 69)


 


Vκ6:
5′-TTATAGAGCTCGAAATTGTGCTGACTCAGTCTCC-3′



(SEQ ID NO: 70)


 


Vκ7:
5′-TATAAGCGGCCGCACGTTTGATTTCCACCTTGGTCCC-3′



(SEQ ID NO: 71)


 


Vκ8:
5′-TATAAGCGGCCGCACGTTTGATCTCCAGCTTGGTCCC-3′



(SEQ ID NO: 72)


 


Vκ9:
5′-TATAAGCGGCCGCACGTTTGATATCCACTTTGGTCCC-3′



(SEQ ID NO: 73)


 


Vκ10:
5′-TATAAGCGGCCGCACGTTTGATCTCCACCTTGGTCCC-3′



(SEQ ID NO: 74)


 


Vκ11:
5′-TATAAGCGGCCGCACGTTTAATCTCCAGTCGTGTCCC-3′



(SEQ ID NO: 75)


 


Vλ1:
5′-ATTTAGAGCTCCAGTCTGTGTTGACGCAGCCGCC-3′



(SEQ ID NO: 76)


 


Vλ2:
5′-ATTTAGAGCTCCAGTCTGCCCTGACTCAGCCTGC-3′



(SEQ ID NO: 77)


 


Vλ3:
5′-ATTTAGAGCTCTCCTATGTGCTGACTCAGCCACC-3′



(SEQ ID NO: 78)


 


Vλ4:
5′-ATTTAGAGCTCTCTTCTGAGCTGACTCAGGACCC-3′



(SEQ ID NO: 79)


 


Vλ5:
5′-ATTTAGAGCTCCACGTTATACTGACTCAACCGCC-3′



(SEQ ID NO: 80)


 


Vλ6:
5′-ATTTAGAGCTCCAGGCTGTGCTCACTCAGCCGTC-3′



(SEQ ID NO: 81)


 


Vλ7:
5′-ATTTAGAGCTCAATTTTATGCTGACTCAGCCCCA-3′



(SEQ ID NO: 82)


 


Vλ8:
5′-ATATTGCGGCCGCACCTAGGACGGTGACCTTGGTCCC-3′



(SEQ ID NO: 83)


 


Vλ9:
5′-ATATTGCGGCCGCACCTAGGACGGTCAGCTTGGTCCC-3′



(SEQ ID NO: 84)


 


Vλ10:
5′-ATATTGCGGCCGCACCTAAAACGGTGAGCTGGGTCCC-3′



(SEQ ID NO: 85)









TABLE V: Primers used for PCR amplification of the human Fd regions with IgE and IgG1 subtype.







TABLE V





Primers used for PCR amplification of the human


Fd regions with IgE and IgG1 subtype.
















5′Cε:
5′-GCTCACCGTCTCCTCAGCCTCCACACAGAGCCCATCCG-3′



(SEQ ID NO: 86)


 


3′Cε:
5′-GCATTGCATTGCGGCCGCTTAATGGTGATGGTGATGATGG



CTGAAGGTTTTGTTGTCGACCC-3′ (SEQ ID NO: 87)


 


5′Cγ:
5′-GGTCACCGTCTCCTCAGCCTCCACCAAGGGCCC-3′



(SEQ ID NO: 88)


 


3′Cγ:
5′-TTTAGTTTATGCGGCCGCTTAATGGTGATGATGATGGTGA



CAAGATTTGGGCTCTGC-3′ (SEQ ID NO: 89)


 


5′Vε:
5′-ACTCATTAGGCACCCCAGGC-3′



(SEQ ID NO: 90)


 


3′Vε:
5′-TGAGGAGACGGTGACC-3′ (SEQ ID NO: 91)


 


5′Cκ:
5′-CGAACTGTGGCTGCACC-3′ (SEQ ID NO: 92)


 


3′Cκ:
5′-AGGTAGGGCGCGCCTTAACACTCTCCCCTGTTGAAGC-3′



(SEQ ID NO: 93)


 


5′Vκ:
5′-TTGTTATTGCTAGCTGCACAACCAGCAATGGCAGACATCG



TGATGACCCAGTCTCC-3′ (SEQ ID NO: 94)


 


3′Vκ:
5′-GGTGCAGCCACAGTTCGTTTGATYTCCASCTTGGTCCC-3′.



(SEQ ID NO: 95)
















TABLE VI







The D1 IgE Fab binding epitopes of β-lactoglobulin. Core epitope:


residues which are making direct contacts with D1 IgE Fab. Extended


epitope: includes also residues which mutation may affect binding of


D1 IgE Fab. The segments are as shown in


FIG. 9d.









Segment
Core epitope
Extended epitope





1
W19-Y20
T18-Y20


2
V43-K47
Y42-K47


3
L57-Q59
E55-Q59


4
C66-Q68
E65-K70


5
P126-E127
T125-E127


6
T154-E157
T154-H161
















TABLE VII







The amino acid sequence comparison of published IgE


sequences reveals that the light chains of the


known IgE antibodies binding to diverse groups of


allergens are strikingly conserved. Conserved


amino acids are shown in bold.
















antigen



CDR-L1
(SEQ ID
CDR-L2
(SEQ ID
CDR-L3
(SEQ ID


CDR
Ig
clone
PDB
XXXXXXXXXXXXXXX..
NO)
....XXXXXXX
NO)
XXXXXXXXXXX.
NO)





Bet v 1
IgE
C-H1





QQSYSTP--RT
(111)




C-H2





AAWDDSLSGRVV
(112)




C-H3





QQRSNWP-PLT
(113)


Phl p 1
IgE
25

SQSIGN------YLNWY
 (96)
LLIYAASSLQS
  (7)
QQSNRTP--ITF
(114)




10

SQTFNN------YLNWY
 (97)
LLIYAASTLRR
(106)
QQSYSTP--LTF
(115)




43

SRTIYN------YLNWY
 (98)
LLIHAASTLQD
(107)
QQSHGTP--LTF
(116)


Phl p 2











Phl p 5
IgE
31

SQSISS------YLNWY
 (99)
LLIYAASSLQS
  (7)
QQSHSTP--YTF
(117)




14

SHSISN------YLNWY
(100)
LLIYAASSLQS
  (7)
QESFSPS--GTF
(118)




28

SQSILG------YLNWY
(101)
LLIYAASTLQS
(108)
QQSYITP--RTF
(119)




 5

SQGISS------WLAWY
(102)
LLIYSASSLQS
(109)
QQANSFP--YTF
(120)


hevein
IgE
1A4

SQSVSS-----SYLAWY
(103)
LLIYGASSRAT
(110)
QQYGSSP--LTF
(121)


hevein
IgE
1C2

SQSISS------YLNWY
(104)
LLIYAASSLQS
  (7)
QQSYSTP--RTF
(122)


Bos d 5
IgE
D1

SQGISS------RLAWY
(105)
LLIYAASSLQS
  (7)
QQYHSYP--WTF
(123)
















TABLE VIII







Structure coordinates of the epitopes of allergenic beta-


lactoglobulin in an antibody-beta-lactoglobulin immunocomplex;

















Atom











type
Resid
#
X
Y
Z
OCC
B























ATOM
1
CB
THR
A
4
−23.309
−4.747
−0.142
1.00
69.95
A


ATOM
2
OG1
THR
A
4
−22.553
−4.413
−1.318
1.00
70.24
A


ATOM
3
CG2
THR
A
4
−22.399
−5.463
0.852
1.00
69.08
A


ATOM
4
C
THR
A
4
−25.438
−4.928
−1.503
1.00
69.21
A


ATOM
5
O
THR
A
4
−25.191
−3.780
−1.887
1.00
68.89
A


ATOM
6
N
THR
A
4
−24.039
−6.943
−1.113
1.00
69.41
A


ATOM
7
CA
THR
A
4
−24.516
−5.659
−0.519
1.00
69.43
A


ATOM
8
N
GLN
A
5
−26.503
−5.615
−1.909
1.00
68.87
A


ATOM
9
CA
GLN
A
5
−27.482
−5.071
−2.843
1.00
68.15
A


ATOM
10
CB
GLN
A
5
−28.213
−3.889
−2.204
1.00
69.22
A


ATOM
11
CG
GLN
A
5
−29.389
−3.378
−3.017
1.00
71.17
A


ATOM
12
CD
GLN
A
5
−30.366
−4.488
−3.374
1.00
72.36
A


ATOM
13
OE1
GLN
A
5
−30.836
−5.225
−2.499
1.00
73.05
A


ATOM
14
NE2
GLN
A
5
−30.683
−4.610
−4.664
1.00
71.92
A


ATOM
15
C
GLN
A
5
−26.828
−4.630
−4.150
1.00
67.11
A


ATOM
16
O
GLN
A
5
−26.732
−3.435
−4.438
1.00
66.95
A


ATOM
17
N
THR
A
6
−26.374
−5.604
−4.934
1.00
66.26
A


ATOM
18
CA
THR
A
6
−25.732
−5.328
−6.216
1.00
64.71
A


ATOM
19
CB
THR
A
6
−24.481
−6.213
−6.444
1.00
64.50
A


ATOM
20
OG1
THR
A
6
−24.887
−7.549
−6.765
1.00
63.11
A


ATOM
21
CG2
THR
A
6
−23.607
−6.239
−5.198
1.00
64.44
A


ATOM
22
C
THR
A
6
−26.711
−5.608
−7.348
1.00
63.92
A


ATOM
23
O
THR
A
6
−27.769
−6.205
−7.141
1.00
63.78
A


ATOM
24
N
MET
A
7
−26.341
−5.182
−8.549
1.00
63.06
A


ATOM
25
CA
MET
A
7
−27.172
−5.377
−9.728
1.00
61.96
A


ATOM
26
CB
MET
A
7
−26.431
−4.865
−10.959
1.00
60.12
A


ATOM
27
CG
MET
A
7
−27.207
−4.975
−12.239
1.00
58.56
A


ATOM
28
SD
MET
A
7
−26.235
−4.362
−13.595
1.00
56.18
A


ATOM
29
CE
MET
A
7
−27.117
−2.858
−14.005
1.00
57.10
A


ATOM
30
C
MET
A
7
−27.521
−6.852
−9.911
1.00
62.21
A


ATOM
31
O
MET
A
7
−26.792
−7.730
−9.448
1.00
63.03
A


ATOM
32
N
LYS
A
8
−28.637
−7.121
−10.583
1.00
61.64
A


ATOM
33
CA
LYS
A
8
−29.054
−8.496
−10.821
1.00
61.39
A


ATOM
34
CB
LYS
A
8
−30.516
−8.542
−11.274
1.00
62.21
A


ATOM
35
CG
LYS
A
8
−31.481
−7.995
−10.222
1.00
64.73
A


ATOM
36
CD
LYS
A
8
−32.952
−8.076
−10.648
1.00
65.77
A


ATOM
37
CE
LYS
A
8
−33.470
−9.511
−10.688
1.00
66.53
A


ATOM
38
NZ
LYS
A
8
−32.973
−10.272
−11.870
1.00
67.48
A


ATOM
39
C
LYS
A
8
−28.147
−9.139
−11.864
1.00
60.59
A


ATOM
40
O
LYS
A
8
−26.924
−9.122
−11.720
1.00
61.07
A


ATOM
41
N
GLY
A
9
−28.729
−9.717
−12.906
1.00
59.03
A


ATOM
42
CA
GLY
A
9
−27.899
−10.326
−13.932
1.00
56.96
A


ATOM
43
C
GLY
A
9
−27.156
−9.276
−14.746
1.00
54.94
A


ATOM
44
O
GLY
A
9
−27.725
−8.245
−15.097
1.00
55.67
A


ATOM
45
N
LEU
A
10
−25.889
−9.531
−15.049
1.00
52.32
A


ATOM
46
CA
LEU
A
10
−25.090
−8.591
−15.834
1.00
50.35
A


ATOM
47
CB
LEU
A
10
−23.875
−8.150
−15.029
1.00
49.63
A


ATOM
48
CG
LEU
A
10
−22.872
−7.298
−15.807
1.00
49.13
A


ATOM
49
CD1
LEU
A
10
−23.483
−5.950
−16.144
1.00
48.82
A


ATOM
50
CD2
LEU
A
10
−21.620
−7.119
−14.984
1.00
49.11
A


ATOM
51
C
LEU
A
10
−24.619
−9.172
−17.177
1.00
49.26
A


ATOM
52
O
LEU
A
10
−24.125
−10.298
−17.231
1.00
48.64
A


ATOM
53
N
ASP
A
11
−24.755
−8.393
−18.253
1.00
48.28
A


ATOM
54
CA
ASP
A
11
−24.353
−8.835
−19.593
1.00
47.09
A


ATOM
55
CB
ASP
A
11
−25.218
−8.166
−20.666
1.00
47.90
A


ATOM
56
CG
ASP
A
11
−24.959
−8.721
−22.072
1.00
48.81
A


ATOM
57
OD1
ASP
A
11
−25.713
−8.359
−22.999
1.00
49.16
A


ATOM
58
OD2
ASP
A
11
−24.011
−9.513
−22.260
1.00
49.60
A


ATOM
59
C
ASP
A
11
−22.887
−8.534
−19.863
1.00
45.64
A


ATOM
60
O
ASP
A
11
−22.542
−7.556
−20.525
1.00
45.05
A


ATOM
61
N
ILE
A
12
−22.033
−9.405
−19.348
1.00
44.43
A


ATOM
62
CA
ILE
A
12
−20.590
−9.279
−19.493
1.00
43.31
A


ATOM
63
CB
ILE
A
12
−19.911
−10.595
−19.096
1.00
43.33
A


ATOM
64
CG2
ILE
A
12
−18.408
−10.420
−19.082
1.00
43.02
A


ATOM
65
CG1
ILE
A
12
−20.418
−11.030
−17.719
1.00
45.17
A


ATOM
66
CD1
ILE
A
12
−20.114
−12.483
−17.357
1.00
46.47
A


ATOM
67
C
ILE
A
12
−20.135
−8.893
−20.907
1.00
42.33
A


ATOM
68
O
ILE
A
12
−19.201
−8.111
−21.082
1.00
42.79
A


ATOM
69
N
GLN
A
13
−20.797
−9.433
−21.918
1.00
40.46
A


ATOM
70
CA
GLN
A
13
−20.413
−9.131
−23.286
1.00
38.91
A


ATOM
71
CB
GLN
A
13
−21.223
−9.984
−24.266
1.00
40.33
A


ATOM
72
CG
GLN
A
13
−21.016
−11.479
−24.112
1.00
41.54
A


ATOM
73
CD
GLN
A
13
−19.554
−11.868
−24.138
1.00
42.01
A


ATOM
74
OE1
GLN
A
13
−18.858
−11.822
−23.114
1.00
40.76
A


ATOM
75
NE2
GLN
A
13
−19.070
−12.230
−25.321
1.00
42.60
A


ATOM
76
C
GLN
A
13
−20.551
−7.659
−23.672
1.00
37.09
A


ATOM
77
O
GLN
A
13
−19.874
−7.181
−24.584
1.00
37.01
A


ATOM
78
N
LYS
A
14
−21.410
−6.923
−22.980
1.00
34.35
A


ATOM
79
CA
LYS
A
14
−21.611
−5.527
−23.340
1.00
30.28
A


ATOM
80
CB
LYS
A
14
−23.098
−5.198
−23.253
1.00
30.76
A


ATOM
81
CG
LYS
A
14
−23.960
−5.988
−24.226
1.00
30.07
A


ATOM
82
CD
LYS
A
14
−25.398
−5.510
−24.182
1.00
31.58
A


ATOM
83
CE
LYS
A
14
−26.266
−6.180
−25.243
1.00
33.34
A


ATOM
84
NZ
LYS
A
14
−27.727
−5.841
−25.086
1.00
33.49
A


ATOM
85
C
LYS
A
14
−20.804
−4.474
−22.596
1.00
28.04
A


ATOM
86
O
LYS
A
14
−20.754
−3.332
−23.028
1.00
27.31
A


ATOM
87
N
VAL
A
15
−20.178
−4.837
−21.486
1.00
25.96
A


ATOM
88
CA
VAL
A
15
−19.381
−3.861
−20.752
1.00
23.39
A


ATOM
89
CB
VAL
A
15
−19.232
−4.270
−19.276
1.00
23.10
A


ATOM
90
CG1
VAL
A
15
−20.589
−4.329
−18.632
1.00
23.40
A


ATOM
91
CG2
VAL
A
15
−18.528
−5.624
−19.171
1.00
23.09
A


ATOM
92
C
VAL
A
15
−17.995
−3.739
−21.396
1.00
22.23
A


ATOM
93
O
VAL
A
15
−17.168
−2.929
−20.991
1.00
20.60
A


ATOM
94
N
ALA
A
16
−17.754
−4.557
−22.411
1.00
21.06
A


ATOM
95
CA
ALA
A
16
−16.475
−4.547
−23.095
1.00
20.08
A


ATOM
96
CB
ALA
A
16
−16.431
−5.661
−24.133
1.00
18.43
A


ATOM
97
C
ALA
A
16
−16.181
−3.204
−23.757
1.00
19.05
A


ATOM
98
O
ALA
A
16
−17.085
−2.469
−24.176
1.00
18.34
A


ATOM
99
N
GLY
A
17
−14.892
−2.913
−23.867
1.00
16.89
A


ATOM
100
CA
GLY
A
17
−14.470
−1.684
−24.480
1.00
13.91
A


ATOM
101
C
GLY
A
17
−13.760
−0.779
−23.512
1.00
14.13
A


ATOM
102
O
GLY
A
17
−13.420
−1.165
−22.389
1.00
13.58
A


ATOM
103
N
THR
A
18
−13.558
0.449
−23.980
1.00
14.39
A


ATOM
104
CA
THR
A
18
−12.888
1.508
−23.251
1.00
12.62
A


ATOM
105
CB
THR
A
18
−12.402
2.559
−24.231
1.00
12.52
A


ATOM
106
OG1
THR
A
18
−11.264
2.046
−24.934
1.00
15.36
A


ATOM
107
CG2
THR
A
18
−12.035
3.850
−23.508
1.00
13.69
A


ATOM
108
C
THR
A
18
−13.764
2.168
−22.206
1.00
12.74
A


ATOM
109
O
THR
A
18
−14.978
2.296
−22.382
1.00
13.81
A


ATOM
110
N
TRP
A
19
−13.128
2.570
−21.111
1.00
10.41
A


ATOM
111
CA
TRP
A
19
−13.806
3.231
−20.014
1.00
8.52
A


ATOM
112
CB
TRP
A
19
−14.211
2.235
−18.930
1.00
7.65
A


ATOM
113
CG
TRP
A
19
−15.284
1.302
−19.337
1.00
7.67
A


ATOM
114
CD2
TRP
A
19
−16.693
1.564
−19.329
1.00
6.14
A


ATOM
115
CE2
TRP
A
19
−17.338
0.392
−19.761
1.00
6.23
A


ATOM
116
CE3
TRP
A
19
−17.470
2.677
−18.995
1.00
4.83
A


ATOM
117
CD1
TRP
A
19
−15.135
0.022
−19.770
1.00
7.58
A


ATOM
118
NE1
TRP
A
19
−16.367
−0.534
−20.027
1.00
7.80
A


ATOM
119
CZ2
TRP
A
19
−18.721
0.298
−19.861
1.00
5.58
A


ATOM
120
CZ3
TRP
A
19
−18.844
2.583
−19.095
1.00
4.02
A


ATOM
121
CH2
TRP
A
19
−19.457
1.403
−19.523
1.00
3.57
A


ATOM
122
C
TRP
A
19
−12.860
4.233
−19.391
1.00
8.93
A


ATOM
123
O
TRP
A
19
−11.666
4.215
−19.651
1.00
10.27
A


ATOM
124
N
TYR
A
20
−13.408
5.089
−18.542
1.00
9.09
A


ATOM
125
CA
TYR
A
20
−12.628
6.076
−17.841
1.00
8.07
A


ATOM
126
CB
TYR
A
20
−12.812
7.460
−18.464
1.00
9.62
A


ATOM
127
CG
TYR
A
20
−12.102
7.654
−19.781
1.00
10.80
A


ATOM
128
CD1
TYR
A
20
−12.788
7.510
−21.004
1.00
9.64
A


ATOM
129
CE1
TYR
A
20
−12.127
7.683
−22.222
1.00
9.99
A


ATOM
130
CD2
TYR
A
20
−10.739
7.976
−19.813
1.00
7.81
A


ATOM
131
CE2
TYR
A
20
−10.076
8.146
−21.028
1.00
9.67
A


ATOM
132
CZ
TYR
A
20
−10.771
7.999
−22.226
1.00
9.03
A


ATOM
133
OH
TYR
A
20
−10.102
8.158
−23.420
1.00
7.27
A


ATOM
134
C
TYR
A
20
−13.138
6.087
−16.419
1.00
8.31
A


ATOM
135
O
TYR
A
20
−14.338
5.909
−16.185
1.00
9.09
A


ATOM
136
N
SER
A
21
−12.227
6.279
−15.470
1.00
7.65
A


ATOM
137
CA
SER
A
21
−12.604
6.334
−14.059
1.00
7.21
A


ATOM
138
CB
SER
A
21
−11.463
5.836
−13.169
1.00
7.63
A


ATOM
139
OG
SER
A
21
−11.239
4.436
−13.360
1.00
8.81
A


ATOM
140
C
SER
A
21
−12.891
7.792
−13.745
1.00
7.24
A


ATOM
141
O
SER
A
21
−11.968
8.573
−13.525
1.00
7.82
A


ATOM
142
N
LEU
A
22
−14.173
8.151
−13.722
1.00
7.35
A


ATOM
143
CA
LEU
A
22
−14.608
9.525
−13.458
1.00
6.56
A


ATOM
144
CB
LEU
A
22
−16.067
9.703
−13.891
1.00
6.94
A


ATOM
145
CG
LEU
A
22
−16.419
10.956
−14.702
1.00
8.26
A


ATOM
146
CD1
LEU
A
22
−17.899
11.308
−14.465
1.00
10.43
A


ATOM
147
CD2
LEU
A
22
−15.548
12.118
−14.299
1.00
6.27
A


ATOM
148
C
LEU
A
22
−14.500
9.946
−12.003
1.00
6.17
A


ATOM
149
O
LEU
A
22
−14.001
11.027
−11.707
1.00
6.09
A


ATOM
150
N
ALA
A
23
−14.981
9.081
−11.112
1.00
5.52
A


ATOM
151
CA
ALA
A
23
−15.002
9.366
−9.686
1.00
5.14
A


ATOM
152
CB
ALA
A
23
−16.360
9.993
−9.308
1.00
1.05
A


ATOM
153
C
ALA
A
23
−14.780
8.092
−8.884
1.00
6.08
A


ATOM
154
O
ALA
A
23
−15.039
6.983
−9.372
1.00
5.25
A


ATOM
155
N
MET
A
24
−14.293
8.244
−7.654
1.00
6.12
A


ATOM
156
CA
MET
A
24
−14.073
7.086
−6.810
1.00
7.92
A


ATOM
157
CB
MET
A
24
−12.682
6.499
−7.065
1.00
10.53
A


ATOM
158
CG
MET
A
24
−11.538
7.490
−6.968
1.00
13.91
A


ATOM
159
SD
MET
A
24
−9.954
6.748
−7.475
1.00
19.85
A


ATOM
160
CE
MET
A
24
−10.155
6.742
−9.241
1.00
16.62
A


ATOM
161
C
MET
A
24
−14.258
7.449
−5.347
1.00
7.96
A


ATOM
162
O
MET
A
24
−14.166
8.621
−4.975
1.00
7.86
A


ATOM
163
N
ALA
A
25
−14.543
6.440
−4.525
1.00
6.87
A


ATOM
164
CA
ALA
A
25
−14.753
6.647
−3.098
1.00
5.96
A


ATOM
165
CB
ALA
A
25
−16.233
6.907
−2.810
1.00
5.94
A


ATOM
166
C
ALA
A
25
−14.286
5.410
−2.362
1.00
5.84
A


ATOM
167
O
ALA
A
25
−14.196
4.337
−2.949
1.00
6.04
A


ATOM
168
N
ALA
A
26
−13.973
5.568
−1.081
1.00
5.75
A


ATOM
169
CA
ALA
A
26
−13.513
4.456
−0.264
1.00
6.01
A


ATOM
170
CB
ALA
A
26
−12.011
4.329
−0.363
1.00
3.18
A


ATOM
171
C
ALA
A
26
−13.927
4.664
1.185
1.00
7.89
A


ATOM
172
O
ALA
A
26
−14.186
5.795
1.612
1.00
4.99
A


ATOM
173
N
SER
A
27
−13.982
3.567
1.938
1.00
10.42
A


ATOM
174
CA
SER
A
27
−14.376
3.623
3.336
1.00
12.99
A


ATOM
175
CB
SER
A
27
−14.720
2.216
3.850
1.00
13.33
A


ATOM
176
OG
SER
A
27
−13.559
1.482
4.189
1.00
16.45
A


ATOM
177
C
SER
A
27
−13.286
4.252
4.205
1.00
14.05
A


ATOM
178
O
SER
A
27
−13.582
4.820
5.249
1.00
13.73
A


ATOM
179
N
ASP
A
28
−12.033
4.148
3.772
1.00
16.92
A


ATOM
180
CA
ASP
A
28
−10.907
4.709
4.515
1.00
19.69
A


ATOM
181
CB
ASP
A
28
−9.980
3.601
5.011
1.00
22.47
A


ATOM
182
CG
ASP
A
28
−10.467
2.984
6.309
1.00
27.75
A


ATOM
183
OD1
ASP
A
28
−11.704
3.020
6.564
1.00
28.49
A


ATOM
184
OD2
ASP
A
28
−9.616
2.448
7.069
1.00
31.52
A


ATOM
185
C
ASP
A
28
−10.124
5.674
3.652
1.00
19.92
A


ATOM
186
O
ASP
A
28
−9.742
5.342
2.531
1.00
20.07
A


ATOM
187
N
ILE
A
29
−9.873
6.866
4.188
1.00
19.78
A


ATOM
188
CA
ILE
A
29
−9.152
7.909
3.468
1.00
19.41
A


ATOM
189
CB
ILE
A
29
−8.901
9.120
4.384
1.00
18.35
A


ATOM
190
CG2
ILE
A
29
−8.030
10.140
3.671
1.00
16.12
A


ATOM
191
CG1
ILE
A
29
−10.244
9.747
4.787
1.00
16.69
A


ATOM
192
CD1
ILE
A
29
−10.131
10.862
5.803
1.00
13.07
A


ATOM
193
C
ILE
A
29
−7.820
7.431
2.901
1.00
20.55
A


ATOM
194
O
ILE
A
29
−7.491
7.716
1.752
1.00
20.09
A


ATOM
195
N
SER
A
30
−7.065
6.702
3.714
1.00
21.94
A


ATOM
196
CA
SER
A
30
−5.754
6.183
3.329
1.00
23.62
A


ATOM
197
CB
SER
A
30
−5.203
5.341
4.461
1.00
24.48
A


ATOM
198
OG
SER
A
30
−6.132
4.313
4.756
1.00
28.16
A


ATOM
199
C
SER
A
30
−5.794
5.331
2.068
1.00
24.82
A


ATOM
200
O
SER
A
30
−4.777
5.153
1.385
1.00
23.69
A


ATOM
201
N
LEU
A
31
−6.974
4.794
1.774
1.00
26.67
A


ATOM
202
CA
LEU
A
31
−7.169
3.943
0.602
1.00
27.64
A


ATOM
203
CB
LEU
A
31
−8.567
3.303
0.645
1.00
26.50
A


ATOM
204
CG
LEU
A
31
−8.795
2.278
1.757
1.00
26.16
A


ATOM
205
CD1
LEU
A
31
−10.266
1.929
1.859
1.00
25.35
A


ATOM
206
CD2
LEU
A
31
−7.943
1.063
1.483
1.00
25.12
A


ATOM
207
C
LEU
A
31
−6.988
4.697
−0.711
1.00
28.40
A


ATOM
208
O
LEU
A
31
−6.503
4.136
−1.696
1.00
28.86
A


ATOM
209
N
LEU
A
32
−7.374
5.969
−0.715
1.00
29.73
A


ATOM
210
CA
LEU
A
32
−7.286
6.821
−1.907
1.00
30.99
A


ATOM
211
CB
LEU
A
32
−8.691
7.246
−2.360
1.00
30.24
A


ATOM
212
CG
LEU
A
32
−9.505
6.344
−3.285
1.00
29.74
A


ATOM
213
CD1
LEU
A
32
−9.570
4.958
−2.695
1.00
30.44
A


ATOM
214
CD2
LEU
A
32
−10.907
6.919
−3.502
1.00
27.92
A


ATOM
215
C
LEU
A
32
−6.459
8.081
−1.670
1.00
32.27
A


ATOM
216
O
LEU
A
32
−6.026
8.719
−2.623
1.00
31.51
A


ATOM
217
N
ASP
A
33
−6.275
8.447
−0.403
1.00
34.56
A


ATOM
218
CA
ASP
A
33
−5.508
9.636
−0.026
1.00
37.18
A


ATOM
219
CB
ASP
A
33
−5.508
9.788
1.504
1.00
38.37
A


ATOM
220
CG
ASP
A
33
−5.076
11.178
1.973
1.00
38.48
A


ATOM
221
OD1
ASP
A
33
−5.360
12.175
1.270
1.00
37.67
A


ATOM
222
OD2
ASP
A
33
−4.472
11.271
3.067
1.00
38.63
A


ATOM
223
C
ASP
A
33
−4.086
9.502
−0.553
1.00
38.68
A


ATOM
224
O
ASP
A
33
−3.396
8.516
−0.267
1.00
39.31
A


ATOM
225
N
ALA
A
34
−3.660
10.504
−1.318
1.00
40.30
A


ATOM
226
CA
ALA
A
34
−2.340
10.522
−1.937
1.00
42.39
A


ATOM
227
CB
ALA
A
34
−1.280
9.999
−0.971
1.00
42.13
A


ATOM
228
C
ALA
A
34
−2.400
9.648
−3.190
1.00
43.89
A


ATOM
229
O
ALA
A
34
−2.869
8.507
−3.141
1.00
43.68
A


ATOM
230
N
GLN
A
35
−1.927
10.193
−4.309
1.00
46.04
A


ATOM
231
CA
GLN
A
35
−1.932
9.494
−5.597
1.00
47.75
A


ATOM
232
CB
GLN
A
35
−1.183
10.333
−6.632
1.00
49.01
A


ATOM
233
CG
GLN
A
35
−1.860
10.368
−7.996
1.00
51.86
A


ATOM
234
CD
GLN
A
35
−1.440
11.582
−8.833
1.00
53.04
A


ATOM
235
OE1
GLN
A
35
−0.302
11.662
−9.323
1.00
53.42
A


ATOM
236
NE2
GLN
A
35
−2.361
12.540
−8.988
1.00
52.30
A


ATOM
237
C
GLN
A
35
−1.361
8.068
−5.563
1.00
48.50
A


ATOM
238
O
GLN
A
35
−1.853
7.183
−6.278
1.00
49.53
A


ATOM
239
N
SER
A
36
−0.342
7.847
−4.732
1.00
47.82
A


ATOM
240
CA
SER
A
36
0.282
6.533
−4.604
1.00
47.78
A


ATOM
241
CB
SER
A
36
1.714
6.688
−4.076
1.00
49.93
A


ATOM
242
OG
SER
A
36
2.479
5.493
−4.271
1.00
51.54
A


ATOM
243
C
SER
A
36
−0.535
5.662
−3.644
1.00
46.74
A


ATOM
244
O
SER
A
36
0.005
5.062
−2.717
1.00
47.36
A


ATOM
245
N
ALA
A
37
−1.839
5.597
−3.875
1.00
45.30
A


ATOM
246
CA
ALA
A
37
−2.715
4.820
−3.022
1.00
44.15
A


ATOM
247
CB
ALA
A
37
−4.078
5.486
−2.940
1.00
45.03
A


ATOM
248
C
ALA
A
37
−2.855
3.373
−3.492
1.00
43.52
A


ATOM
249
O
ALA
A
37
−2.697
3.059
−4.679
1.00
43.45
A


ATOM
250
N
PRO
A
38
−3.155
2.466
−2.548
1.00
42.24
A


ATOM
251
CD
PRO
A
38
−3.315
2.745
−1.106
1.00
41.30
A


ATOM
252
CA
PRO
A
38
−3.322
1.038
−2.821
1.00
40.88
A


ATOM
253
CB
PRO
A
38
−3.259
0.426
−1.425
1.00
41.84
A


ATOM
254
CG
PRO
A
38
−3.924
1.471
−0.588
1.00
41.59
A


ATOM
255
C
PRO
A
38
−4.609
0.669
−3.562
1.00
39.03
A


ATOM
256
O
PRO
A
38
−4.761
−0.460
−4.028
1.00
39.26
A


ATOM
257
N
LEU
A
39
−5.539
1.611
−3.666
1.00
36.16
A


ATOM
258
CA
LEU
A
39
−6.793
1.334
−4.357
1.00
32.67
A


ATOM
259
CB
LEU
A
39
−7.947
1.214
−3.366
1.00
34.76
A


ATOM
260
CG
LEU
A
39
−7.972
−0.013
−2.458
1.00
36.49
A


ATOM
261
CD1
LEU
A
39
−9.296
0.006
−1.684
1.00
39.85
A


ATOM
262
CD2
LEU
A
39
−7.859
−1.289
−3.285
1.00
37.68
A


ATOM
263
C
LEU
A
39
−7.105
2.420
−5.344
1.00
28.83
A


ATOM
264
O
LEU
A
39
−8.216
2.498
−5.854
1.00
28.46
A


ATOM
265
N
ARG
A
40
−6.116
3.262
−5.615
1.00
25.66
A


ATOM
266
CA
ARG
A
40
−6.307
4.351
−6.560
1.00
22.85
A


ATOM
267
CB
ARG
A
40
−5.431
5.533
−6.175
1.00
21.75
A


ATOM
268
CG
ARG
A
40
−5.740
6.803
−6.931
1.00
21.09
A


ATOM
269
CD
ARG
A
40
−5.789
7.968
−5.960
1.00
22.80
A


ATOM
270
NE
ARG
A
40
−5.618
9.265
−6.616
1.00
22.93
A


ATOM
271
CZ
ARG
A
40
−5.550
10.426
−5.965
1.00
22.37
A


ATOM
272
NH1
ARG
A
40
−5.643
10.462
−4.645
1.00
19.87
A


ATOM
273
NH2
ARG
A
40
−5.373
11.551
−6.634
1.00
25.01
A


ATOM
274
C
ARG
A
40
−5.945
3.844
−7.943
1.00
21.35
A


ATOM
275
O
ARG
A
40
−4.907
4.184
−8.503
1.00
21.42
A


ATOM
276
N
VAL
A
41
−6.822
3.016
−8.489
1.00
19.98
A


ATOM
277
CA
VAL
A
41
−6.593
2.442
−9.796
1.00
17.66
A


ATOM
278
CB
VAL
A
41
−6.881
0.953
−9.765
1.00
16.68
A


ATOM
279
CG1
VAL
A
41
−6.242
0.349
−8.540
1.00
16.35
A


ATOM
280
CG2
VAL
A
41
−8.355
0.716
−9.769
1.00
17.46
A


ATOM
281
C
VAL
A
41
−7.491
3.113
−10.816
1.00
16.54
A


ATOM
282
O
VAL
A
41
−8.517
3.686
−10.458
1.00
17.39
A


ATOM
283
N
TYR
A
42
−7.092
3.049
−12.081
1.00
16.55
A


ATOM
284
CA
TYR
A
42
−7.859
3.634
−13.173
1.00
15.47
A


ATOM
285
CB
TYR
A
42
−7.104
4.815
−13.788
1.00
13.88
A


ATOM
286
CG
TYR
A
42
−6.574
5.785
−12.751
1.00
12.95
A


ATOM
287
CD1
TYR
A
42
−5.266
5.683
−12.281
1.00
12.86
A


ATOM
288
CE1
TYR
A
42
−4.791
6.520
−11.269
1.00
11.80
A


ATOM
289
CD2
TYR
A
42
−7.400
6.756
−12.183
1.00
12.39
A


ATOM
290
CE2
TYR
A
42
−6.927
7.597
−11.166
1.00
12.09
A


ATOM
291
CZ
TYR
A
42
−5.623
7.458
−10.720
1.00
10.82
A


ATOM
292
OH
TYR
A
42
−5.168
8.232
−9.694
1.00
12.77
A


ATOM
293
C
TYR
A
42
−8.124
2.586
−14.236
1.00
15.00
A


ATOM
294
O
TYR
A
42
−7.191
2.015
−14.797
1.00
13.20
A


ATOM
295
N
VAL
A
43
−9.407
2.329
−14.480
1.00
15.77
A


ATOM
296
CA
VAL
A
43
−9.858
1.367
−15.478
1.00
16.87
A


ATOM
297
CB
VAL
A
43
−11.367
1.045
−15.294
1.00
18.26
A


ATOM
298
CG1
VAL
A
43
−11.814
−0.036
−16.278
1.00
18.05
A


ATOM
299
CG2
VAL
A
43
−11.628
0.610
−13.866
1.00
19.17
A


ATOM
300
C
VAL
A
43
−9.661
1.967
−16.869
1.00
17.12
A


ATOM
301
O
VAL
A
43
−9.888
3.162
−17.081
1.00
18.44
A


ATOM
302
N
GLU
A
44
−9.233
1.144
−17.817
1.00
17.63
A


ATOM
303
CA
GLU
A
44
−9.023
1.628
−19.175
1.00
18.37
A


ATOM
304
CB
GLU
A
44
−7.540
1.600
−19.526
1.00
17.78
A


ATOM
305
CG
GLU
A
44
−6.700
2.474
−18.632
1.00
19.02
A


ATOM
306
CD
GLU
A
44
−5.327
2.720
−19.212
1.00
22.11
A


ATOM
307
OE1
GLU
A
44
−4.657
1.733
−19.630
1.00
22.53
A


ATOM
308
OE2
GLU
A
44
−4.912
3.905
−19.239
1.00
22.89
A


ATOM
309
C
GLU
A
44
−9.776
0.792
−20.180
1.00
17.64
A


ATOM
310
O
GLU
A
44
−10.422
1.325
−21.078
1.00
16.88
A


ATOM
311
N
GLU
A
45
−9.704
−0.519
−19.994
1.00
18.74
A


ATOM
312
CA
GLU
A
45
−10.335
−1.452
−20.898
1.00
20.81
A


ATOM
313
CB
GLU
A
45
−9.283
−1.935
−21.902
1.00
21.48
A


ATOM
314
CG
GLU
A
45
−9.777
−2.219
−23.312
1.00
25.33
A


ATOM
315
CD
GLU
A
45
−9.527
−1.059
−24.264
1.00
27.54
A


ATOM
316
OE1
GLU
A
45
−8.411
−0.490
−24.239
1.00
27.39
A


ATOM
317
OE2
GLU
A
45
−10.440
−0.720
−25.050
1.00
29.46
A


ATOM
318
C
GLU
A
45
−10.932
−2.658
−20.163
1.00
21.59
A


ATOM
319
O
GLU
A
45
−10.384
−3.141
−19.163
1.00
20.49
A


ATOM
320
N
LEU
A
46
−12.065
−3.129
−20.673
1.00
23.36
A


ATOM
321
CA
LEU
A
46
−12.732
−4.308
−20.138
1.00
25.89
A


ATOM
322
CB
LEU
A
46
−14.129
−3.968
−19.595
1.00
24.67
A


ATOM
323
CG
LEU
A
46
−14.163
−3.256
−18.243
1.00
22.90
A


ATOM
324
CD1
LEU
A
46
−15.589
−3.016
−17.823
1.00
22.10
A


ATOM
325
CD2
LEU
A
46
−13.418
−4.094
−17.209
1.00
23.07
A


ATOM
326
C
LEU
A
46
−12.831
−5.297
−21.301
1.00
27.65
A


ATOM
327
O
LEU
A
46
−13.572
−5.079
−22.255
1.00
27.18
A


ATOM
328
N
LYS
A
47
−12.058
−6.373
−21.213
1.00
31.02
A


ATOM
329
CA
LYS
A
47
−12.015
−7.396
−22.240
1.00
34.48
A


ATOM
330
CB
LYS
A
47
−10.571
−7.543
−22.731
1.00
35.53
A


ATOM
331
CG
LYS
A
47
−10.313
−8.672
−23.702
1.00
37.60
A


ATOM
332
CD
LYS
A
47
−8.938
−8.510
−24.347
1.00
38.84
A


ATOM
333
CE
LYS
A
47
−8.324
−9.851
−24.708
1.00
39.57
A


ATOM
334
NZ
LYS
A
47
−6.998
−9.685
−25.365
1.00
40.23
A


ATOM
335
C
LYS
A
47
−12.529
−8.730
−21.701
1.00
36.80
A


ATOM
336
O
LYS
A
47
−11.854
−9.400
−20.910
1.00
36.52
A


ATOM
337
N
PRO
A
48
−13.743
−9.122
−22.117
1.00
38.18
A


ATOM
338
CD
PRO
A
48
−14.620
−8.395
−23.048
1.00
38.61
A


ATOM
339
CA
PRO
A
48
−14.376
−10.372
−21.701
1.00
39.51
A


ATOM
340
CB
PRO
A
48
−15.811
−10.197
−22.178
1.00
39.56
A


ATOM
341
CG
PRO
A
48
−15.619
−9.461
−23.448
1.00
38.54
A


ATOM
342
C
PRO
A
48
−13.698
−11.561
−22.361
1.00
40.34
A


ATOM
343
O
PRO
A
48
−13.371
−11.511
−23.541
1.00
39.26
A


ATOM
344
N
THR
A
49
−13.491
−12.622
−21.588
1.00
42.45
A


ATOM
345
CA
THR
A
49
−12.851
−13.831
−22.088
1.00
43.91
A


ATOM
346
CB
THR
A
49
−11.982
−14.493
−21.028
1.00
43.45
A


ATOM
347
OG1
THR
A
49
−12.820
−14.990
−19.981
1.00
43.90
A


ATOM
348
CG2
THR
A
49
−10.988
−13.510
−20.461
1.00
43.33
A


ATOM
349
C
THR
A
49
−13.923
−14.839
−22.466
1.00
45.42
A


ATOM
350
O
THR
A
49
−15.070
−14.753
−22.012
1.00
45.06
A


ATOM
351
N
PRO
A
50
−13.555
−15.825
−23.290
1.00
46.42
A


ATOM
352
CD
PRO
A
50
−12.200
−16.122
−23.785
1.00
46.56
A


ATOM
353
CA
PRO
A
50
−14.503
−16.851
−23.721
1.00
47.28
A


ATOM
354
CB
PRO
A
50
−13.664
−17.721
−24.651
1.00
46.60
A


ATOM
355
CG
PRO
A
50
−12.292
−17.599
−24.079
1.00
46.90
A


ATOM
356
C
PRO
A
50
−15.078
−17.634
−22.539
1.00
48.52
A


ATOM
357
O
PRO
A
50
−16.274
−17.939
−22.506
1.00
48.29
A


ATOM
358
N
GLU
A
51
−14.233
−17.944
−21.559
1.00
49.18
A


ATOM
359
CA
GLU
A
51
−14.702
−18.694
−20.400
1.00
49.93
A


ATOM
360
CB
GLU
A
51
−13.520
−19.151
−19.542
1.00
50.20
A


ATOM
361
CG
GLU
A
51
−12.405
−18.147
−19.450
1.00
52.19
A


ATOM
362
CD
GLU
A
51
−11.193
−18.543
−20.287
1.00
54.81
A


ATOM
363
OE1
GLU
A
51
−10.460
−19.478
−19.886
1.00
55.81
A


ATOM
364
OE2
GLU
A
51
−10.972
−17.930
−21.355
1.00
54.93
A


ATOM
365
C
GLU
A
51
−15.698
−17.910
−19.541
1.00
50.04
A


ATOM
366
O
GLU
A
51
−16.178
−18.410
−18.521
1.00
51.24
A


ATOM
367
N
GLY
A
52
−16.017
−16.685
−19.952
1.00
48.90
A


ATOM
368
CA
GLY
A
52
−16.967
−15.882
−19.192
1.00
46.90
A


ATOM
369
C
GLY
A
52
−16.353
−14.928
−18.179
1.00
45.73
A


ATOM
370
O
GLY
A
52
−17.063
−14.220
−17.454
1.00
44.51
A


ATOM
371
N
ASP
A
53
−15.024
−14.912
−18.119
1.00
44.59
A


ATOM
372
CA
ASP
A
53
−14.325
−14.026
−17.198
1.00
42.64
A


ATOM
373
CB
ASP
A
53
−12.937
−14.574
−16.846
1.00
43.41
A


ATOM
374
CG
ASP
A
53
−12.996
−15.915
−16.139
1.00
44.82
A


ATOM
375
OD1
ASP
A
53
−13.850
−16.091
−15.237
1.00
44.78
A


ATOM
376
OD2
ASP
A
53
−12.168
−16.794
−16.477
1.00
46.39
A


ATOM
377
C
ASP
A
53
−14.172
−12.653
−17.833
1.00
40.68
A


ATOM
378
O
ASP
A
53
−14.540
−12.445
−18.988
1.00
39.21
A


ATOM
379
N
LEU
A
54
−13.612
−11.721
−17.073
1.00
39.63
A


ATOM
380
CA
LEU
A
54
−13.411
−10.364
−17.555
1.00
37.71
A


ATOM
381
CB
LEU
A
54
−14.402
−9.437
−16.858
1.00
37.78
A


ATOM
382
CG
LEU
A
54
−14.543
−8.033
−17.426
1.00
38.04
A


ATOM
383
CD1
LEU
A
54
−14.949
−8.112
−18.888
1.00
38.98
A


ATOM
384
CD2
LEU
A
54
−15.575
−7.277
−16.618
1.00
38.45
A


ATOM
385
C
LEU
A
54
−11.980
−9.874
−17.314
1.00
36.15
A


ATOM
386
O
LEU
A
54
−11.547
−9.725
−16.170
1.00
35.39
A


ATOM
387
N
GLU
A
55
−11.241
−9.639
−18.395
1.00
33.89
A


ATOM
388
CA
GLU
A
55
−9.880
−9.144
−18.267
1.00
31.45
A


ATOM
389
CB
GLU
A
55
−9.063
−9.455
−19.513
1.00
33.59
A


ATOM
390
CG
GLU
A
55
−7.566
−9.428
−19.278
1.00
36.34
A


ATOM
391
CD
GLU
A
55
−6.790
−9.078
−20.532
1.00
39.61
A


ATOM
392
OE1
GLU
A
55
−7.034
−9.707
−21.586
1.00
41.88
A


ATOM
393
OE2
GLU
A
55
−5.930
−8.169
−20.470
1.00
41.11
A


ATOM
394
C
GLU
A
55
−9.993
−7.636
−18.096
1.00
28.49
A


ATOM
395
O
GLU
A
55
−10.872
−7.001
−18.677
1.00
27.60
A


ATOM
396
N
ILE
A
56
−9.108
−7.064
−17.295
1.00
25.67
A


ATOM
397
CA
ILE
A
56
−9.154
−5.639
−17.045
1.00
22.66
A


ATOM
398
CB
ILE
A
56
−9.662
−5.362
−15.632
1.00
21.92
A


ATOM
399
CG2
ILE
A
56
−9.571
−3.875
−15.312
1.00
20.65
A


ATOM
400
CG1
ILE
A
56
−11.087
−5.857
−15.508
1.00
20.67
A


ATOM
401
CD1
ILE
A
56
−11.338
−6.533
−14.224
1.00
20.88
A


ATOM
402
C
ILE
A
56
−7.812
−4.976
−17.202
1.00
21.00
A


ATOM
403
O
ILE
A
56
−6.832
−5.376
−16.579
1.00
19.63
A


ATOM
404
N
LEU
A
57
−7.783
−3.945
−18.038
1.00
20.06
A


ATOM
405
CA
LEU
A
57
−6.563
−3.191
−18.266
1.00
19.69
A


ATOM
406
CB
LEU
A
57
−6.454
−2.789
−19.733
1.00
16.44
A


ATOM
407
CG
LEU
A
57
−5.166
−2.067
−20.075
1.00
14.61
A


ATOM
408
CD1
LEU
A
57
−4.000
−2.961
−19.751
1.00
12.30
A


ATOM
409
CD2
LEU
A
57
−5.170
−1.661
−21.537
1.00
13.35
A


ATOM
410
C
LEU
A
57
−6.667
−1.948
−17.396
1.00
20.13
A


ATOM
411
O
LEU
A
57
−7.624
−1.187
−17.529
1.00
19.45
A


ATOM
412
N
LEU
A
58
−5.702
−1.742
−16.502
1.00
20.63
A


ATOM
413
CA
LEU
A
58
−5.752
−0.578
−15.632
1.00
22.21
A


ATOM
414
CB
LEU
A
58
−6.504
−0.928
−14.350
1.00
21.17
A


ATOM
415
CG
LEU
A
58
−5.911
−2.034
−13.479
1.00
20.12
A


ATOM
416
CD1
LEU
A
58
−4.774
−1.473
−12.644
1.00
20.35
A


ATOM
417
CD2
LEU
A
58
−6.988
−2.595
−12.557
1.00
20.30
A


ATOM
418
C
LEU
A
58
−4.398
0.017
−15.285
1.00
24.46
A


ATOM
419
O
LEU
A
58
−3.354
−0.557
−15.597
1.00
22.97
A


ATOM
420
N
GLN
A
59
−4.435
1.179
−14.632
1.00
27.45
A


ATOM
421
CA
GLN
A
59
−3.225
1.893
−14.215
1.00
29.95
A


ATOM
422
CB
GLN
A
59
−3.066
3.199
−15.014
1.00
30.32
A


ATOM
423
CG
GLN
A
59
−3.110
3.066
−16.533
1.00
29.93
A


ATOM
424
CD
GLN
A
59
−1.849
2.471
−17.121
1.00
31.13
A


ATOM
425
OE1
GLN
A
59
−1.779
2.205
−18.322
1.00
31.40
A


ATOM
426
NE2
GLN
A
59
−0.839
2.265
−16.283
1.00
30.58
A


ATOM
427
C
GLN
A
59
−3.297
2.234
−12.723
1.00
31.07
A


ATOM
428
O
GLN
A
59
−4.370
2.495
−12.190
1.00
29.29
A


ATOM
429
N
LYS
A
60
−2.146
2.228
−12.063
1.00
35.25
A


ATOM
430
CA
LYS
A
60
−2.064
2.563
−10.648
1.00
40.05
A


ATOM
431
CB
LYS
A
60
−2.547
1.406
−9.772
1.00
41.46
A


ATOM
432
CG
LYS
A
60
−1.838
0.098
−10.010
1.00
44.79
A


ATOM
433
CD
LYS
A
60
−2.453
−1.010
−9.156
1.00
47.46
A


ATOM
434
CE
LYS
A
60
−1.904
−2.379
−9.554
1.00
49.65
A


ATOM
435
NZ
LYS
A
60
−2.316
−3.473
−8.616
1.00
51.45
A


ATOM
436
C
LYS
A
60
−0.633
2.919
−10.297
1.00
42.65
A


ATOM
437
O
LYS
A
60
0.304
2.379
−10.884
1.00
42.07
A


ATOM
438
N
TRP
A
61
−0.471
3.837
−9.347
1.00
46.96
A


ATOM
439
CA
TRP
A
61
0.852
4.285
−8.938
1.00
51.03
A


ATOM
440
CB
TRP
A
61
0.742
5.554
−8.081
1.00
53.76
A


ATOM
441
CG
TRP
A
61
1.987
6.403
−8.115
1.00
57.70
A


ATOM
442
CD2
TRP
A
61
2.192
7.602
−8.887
1.00
59.81
A


ATOM
443
CE2
TRP
A
61
3.526
8.021
−8.660
1.00
60.30
A


ATOM
444
CE3
TRP
A
61
1.380
8.357
−9.752
1.00
61.20
A


ATOM
445
CD1
TRP
A
61
3.169
6.160
−7.467
1.00
57.99
A


ATOM
446
NE1
TRP
A
61
4.095
7.127
−7.790
1.00
59.69
A


ATOM
447
CZ2
TRP
A
61
4.069
9.170
−9.267
1.00
61.29
A


ATOM
448
CZ3
TRP
A
61
1.921
9.503
−10.359
1.00
62.02
A


ATOM
449
CH2
TRP
A
61
3.254
9.892
−10.112
1.00
61.97
A


ATOM
450
C
TRP
A
61
1.588
3.181
−8.192
1.00
52.67
A


ATOM
451
O
TRP
A
61
0.991
2.420
−7.428
1.00
52.42
A


ATOM
452
N
GLU
A
62
2.892
3.093
−8.438
1.00
55.20
A


ATOM
453
CA
GLU
A
62
3.733
2.075
−7.817
1.00
57.16
A


ATOM
454
CB
GLU
A
62
3.580
0.762
−8.579
1.00
57.04
A


ATOM
455
CG
GLU
A
62
3.574
−0.464
−7.708
1.00
58.73
A


ATOM
456
CD
GLU
A
62
3.273
−1.727
−8.494
1.00
60.57
A


ATOM
457
OE1
GLU
A
62
4.126
−2.144
−9.315
1.00
61.75
A


ATOM
458
OE2
GLU
A
62
2.179
−2.305
−8.296
1.00
60.52
A


ATOM
459
C
GLU
A
62
5.205
2.506
−7.812
1.00
58.20
A


ATOM
460
O
GLU
A
62
5.873
2.520
−8.851
1.00
58.37
A


ATOM
461
N
ASN
A
63
5.695
2.856
−6.625
1.00
59.00
A


ATOM
462
CA
ASN
A
63
7.072
3.309
−6.426
1.00
59.09
A


ATOM
463
CB
ASN
A
63
8.057
2.146
−6.601
1.00
60.08
A


ATOM
464
CG
ASN
A
63
9.464
2.490
−6.111
1.00
61.16
A


ATOM
465
OD1
ASN
A
63
10.420
1.746
−6.347
1.00
62.06
A


ATOM
466
ND2
ASN
A
63
9.591
3.620
−5.416
1.00
60.90
A


ATOM
467
C
ASN
A
63
7.468
4.452
−7.366
1.00
58.34
A


ATOM
468
O
ASN
A
63
8.341
4.293
−8.216
1.00
58.61
A


ATOM
469
N
GLY
A
64
6.824
5.601
−7.206
1.00
57.66
A


ATOM
470
CA
GLY
A
64
7.147
6.745
−8.035
1.00
57.23
A


ATOM
471
C
GLY
A
64
7.081
6.503
−9.532
1.00
56.69
A


ATOM
472
O
GLY
A
64
7.988
6.892
−10.271
1.00
57.24
A


ATOM
473
N
GLU
A
65
6.014
5.852
−9.982
1.00
55.45
A


ATOM
474
CA
GLU
A
65
5.816
5.581
−11.407
1.00
53.27
A


ATOM
475
CB
GLU
A
65
6.940
4.700
−11.956
1.00
54.85
A


ATOM
476
CG
GLU
A
65
6.771
4.365
−13.442
1.00
57.62
A


ATOM
477
CD
GLU
A
65
7.591
3.152
−13.876
1.00
59.68
A


ATOM
478
OE1
GLU
A
65
8.808
3.316
−14.166
1.00
60.24
A


ATOM
479
OE2
GLU
A
65
7.012
2.032
−13.913
1.00
59.19
A


ATOM
480
C
GLU
A
65
4.473
4.904
−11.675
1.00
50.57
A


ATOM
481
O
GLU
A
65
4.070
3.987
−10.961
1.00
48.97
A


ATOM
482
N
CYS
A
66
3.787
5.367
−12.714
1.00
47.19
A


ATOM
483
CA
CYS
A
66
2.503
4.803
−13.084
1.00
43.59
A


ATOM
484
C
CYS
A
66
2.756
3.455
−13.762
1.00
40.51
A


ATOM
485
O
CYS
A
66
3.625
3.345
−14.632
1.00
40.39
A


ATOM
486
CB
CYS
A
66
1.767
5.752
−14.033
1.00
44.83
A


ATOM
487
SG
CYS
A
66
−0.027
5.451
−14.082
1.00
47.82
A


ATOM
488
N
ALA
A
67
2.022
2.424
−13.346
1.00
36.07
A


ATOM
489
CA
ALA
A
67
2.194
1.093
−13.927
1.00
32.69
A


ATOM
490
CB
ALA
A
67
2.661
0.127
−12.860
1.00
31.43
A


ATOM
491
C
ALA
A
67
0.930
0.550
−14.599
1.00
30.95
A


ATOM
492
O
ALA
A
67
−0.175
0.772
−14.116
1.00
30.29
A


ATOM
493
N
GLN
A
68
1.096
−0.160
−15.714
1.00
29.19
A


ATOM
494
CA
GLN
A
68
−0.039
−0.736
−16.433
1.00
28.43
A


ATOM
495
CB
GLN
A
68
0.202
−0.729
−17.954
1.00
27.45
A


ATOM
496
CG
GLN
A
68
−1.040
−1.062
−18.789
1.00
26.69
A


ATOM
497
CD
GLN
A
68
−0.746
−1.378
−20.248
1.00
26.54
A


ATOM
498
OE1
GLN
A
68
−0.308
−2.480
−20.575
1.00
25.60
A


ATOM
499
NE2
GLN
A
68
−0.986
−0.410
−21.131
1.00
25.13
A


ATOM
500
C
GLN
A
68
−0.198
−2.170
−15.960
1.00
28.78
A


ATOM
501
O
GLN
A
68
0.779
−2.908
−15.856
1.00
30.77
A


ATOM
502
N
LYS
A
69
−1.424
−2.575
−15.668
1.00
28.41
A


ATOM
503
CA
LYS
A
69
−1.637
−3.932
−15.211
1.00
27.79
A


ATOM
504
CB
LYS
A
69
−1.709
−3.942
−13.680
1.00
29.08
A


ATOM
505
CG
LYS
A
69
−0.407
−3.533
−12.974
1.00
29.62
A


ATOM
506
CD
LYS
A
69
−0.279
−4.243
−11.611
1.00
32.13
A


ATOM
507
CE
LYS
A
69
0.997
−3.868
−10.829
1.00
32.54
A


ATOM
508
NZ
LYS
A
69
0.984
−4.540
−9.486
1.00
33.14
A


ATOM
509
C
LYS
A
69
−2.883
−4.575
−15.832
1.00
27.00
A


ATOM
510
O
LYS
A
69
−3.878
−3.904
−16.121
1.00
26.83
A


ATOM
511
N
LYS
A
70
−2.801
−5.877
−16.068
1.00
26.65
A


ATOM
512
CA
LYS
A
70
−3.911
−6.629
−16.644
1.00
27.65
A


ATOM
513
CB
LYS
A
70
−3.465
−7.395
−17.883
1.00
28.88
A


ATOM
514
CG
LYS
A
70
−3.161
−6.516
−19.080
1.00
29.87
A


ATOM
515
CD
LYS
A
70
−2.682
−7.330
−20.275
1.00
31.48
A


ATOM
516
CE
LYS
A
70
−1.275
−7.868
−20.062
1.00
33.90
A


ATOM
517
NZ
LYS
A
70
−0.764
−8.550
−21.295
1.00
34.28
A


ATOM
518
C
LYS
A
70
−4.412
−7.608
−15.599
1.00
28.24
A


ATOM
519
O
LYS
A
70
−3.702
−8.539
−15.206
1.00
28.11
A


ATOM
520
N
ILE
A
71
−5.646
−7.393
−15.163
1.00
28.75
A


ATOM
521
CA
ILE
A
71
−6.256
−8.217
−14.139
1.00
29.38
A


ATOM
522
CB
ILE
A
71
−6.784
−7.342
−12.995
1.00
29.74
A


ATOM
523
CG2
ILE
A
71
−7.449
−8.201
−11.945
1.00
29.87
A


ATOM
524
CG1
ILE
A
71
−5.634
−6.519
−12.406
1.00
31.07
A


ATOM
525
CD1
ILE
A
71
−4.411
−7.320
−12.037
1.00
29.99
A


ATOM
526
C
ILE
A
71
−7.402
−9.028
−14.688
1.00
30.07
A


ATOM
527
O
ILE
A
71
−8.092
−8.594
−15.601
1.00
30.69
A


ATOM
528
N
ILE
A
72
−7.598
−10.215
−14.126
1.00
31.03
A


ATOM
529
CA
ILE
A
72
−8.684
−11.094
−14.543
1.00
31.39
A


ATOM
530
CB
ILE
A
72
−8.157
−12.481
−15.016
1.00
30.67
A


ATOM
531
CG2
ILE
A
72
−7.592
−12.374
−16.420
1.00
29.84
A


ATOM
532
CG1
ILE
A
72
−7.117
−13.031
−14.025
1.00
31.46
A


ATOM
533
CD1
ILE
A
72
−5.791
−12.272
−13.964
1.00
30.80
A


ATOM
534
C
ILE
A
72
−9.681
−11.297
−13.395
1.00
31.89
A


ATOM
535
O
ILE
A
72
−9.339
−11.822
−12.344
1.00
31.15
A


ATOM
536
N
ALA
A
73
−10.911
−10.843
−13.601
1.00
33.09
A


ATOM
537
CA
ALA
A
73
−11.961
−10.990
−12.608
1.00
34.36
A


ATOM
538
CB
ALA
A
73
−12.854
−9.756
−12.592
1.00
32.94
A


ATOM
539
C
ALA
A
73
−12.763
−12.218
−13.018
1.00
36.37
A


ATOM
540
O
ALA
A
73
−13.492
−12.180
−14.012
1.00
35.78
A


ATOM
541
N
GLU
A
74
−12.612
−13.307
−12.264
1.00
38.55
A


ATOM
542
CA
GLU
A
74
−13.311
−14.559
−12.554
1.00
40.60
A


ATOM
543
CB
GLU
A
74
−12.599
−15.720
−11.853
1.00
42.50
A


ATOM
544
CG
GLU
A
74
−11.126
−15.861
−12.232
1.00
46.59
A


ATOM
545
CD
GLU
A
74
−10.349
−16.791
−11.301
1.00
48.06
A


ATOM
546
OE1
GLU
A
74
−10.349
−16.548
−10.074
1.00
49.47
A


ATOM
547
OE2
GLU
A
74
−9.732
−17.754
−11.803
1.00
48.88
A


ATOM
548
C
GLU
A
74
−14.765
−14.505
−12.106
1.00
41.17
A


ATOM
549
O
GLU
A
74
−15.062
−14.102
−10.983
1.00
40.92
A


ATOM
550
N
LYS
A
75
−15.676
−14.910
−12.983
1.00
42.54
A


ATOM
551
CA
LYS
A
75
−17.086
−14.895
−12.630
1.00
43.98
A


ATOM
552
CB
LYS
A
75
−17.962
−15.093
−13.872
1.00
44.43
A


ATOM
553
CG
LYS
A
75
−17.430
−16.091
−14.874
1.00
45.71
A


ATOM
554
CD
LYS
A
75
−18.037
−17.459
−14.685
1.00
46.72
A


ATOM
555
CE
LYS
A
75
−17.517
−18.420
−15.743
1.00
48.20
A


ATOM
556
NZ
LYS
A
75
−16.030
−18.585
−15.686
1.00
48.26
A


ATOM
557
C
LYS
A
75
−17.373
−15.962
−11.589
1.00
44.70
A


ATOM
558
O
LYS
A
75
−16.731
−17.012
−11.561
1.00
45.03
A


ATOM
559
N
THR
A
76
−18.335
−15.673
−10.720
1.00
45.79
A


ATOM
560
CA
THR
A
76
−18.704
−16.594
−9.656
1.00
46.49
A


ATOM
561
CB
THR
A
76
−18.482
−15.931
−8.265
1.00
46.29
A


ATOM
562
OG1
THR
A
76
−19.386
−14.829
−8.099
1.00
44.95
A


ATOM
563
CG2
THR
A
76
−17.043
−15.425
−8.139
1.00
44.80
A


ATOM
564
C
THR
A
76
−20.163
−17.048
−9.784
1.00
47.70
A


ATOM
565
O
THR
A
76
−20.834
−16.742
−10.771
1.00
48.25
A


ATOM
566
N
LYS
A
77
−20.638
−17.777
−8.775
1.00
48.61
A


ATOM
567
CA
LYS
A
77
−22.004
−18.290
−8.735
1.00
49.17
A


ATOM
568
CB
LYS
A
77
−22.063
−19.543
−7.853
1.00
49.66
A


ATOM
569
CG
LYS
A
77
−21.293
−20.737
−8.418
1.00
50.61
A


ATOM
570
CD
LYS
A
77
−21.051
−21.797
−7.360
1.00
51.96
A


ATOM
571
CE
LYS
A
77
−20.127
−22.895
−7.867
1.00
52.72
A


ATOM
572
NZ
LYS
A
77
−19.518
−23.679
−6.741
1.00
52.80
A


ATOM
573
C
LYS
A
77
−22.947
−17.220
−8.201
1.00
49.74
A


ATOM
574
O
LYS
A
77
−24.022
−17.513
−7.675
1.00
50.02
A


ATOM
575
N
ILE
A
78
−22.516
−15.971
−8.333
1.00
50.28
A


ATOM
576
CA
ILE
A
78
−23.296
−14.818
−7.895
1.00
50.17
A


ATOM
577
CB
ILE
A
78
−22.618
−14.092
−6.746
1.00
51.47
A


ATOM
578
CG2
ILE
A
78
−23.550
−13.013
−6.193
1.00
50.83
A


ATOM
579
CG1
ILE
A
78
−22.241
−15.099
−5.659
1.00
51.83
A


ATOM
580
CD1
ILE
A
78
−21.526
−14.477
−4.487
1.00
53.00
A


ATOM
581
C
ILE
A
78
−23.394
−13.860
−9.072
1.00
49.78
A


ATOM
582
O
ILE
A
78
−22.386
−13.481
−9.656
1.00
50.43
A


ATOM
583
N
PRO
A
79
−24.613
−13.438
−9.416
1.00
49.21
A


ATOM
584
CD
PRO
A
79
−25.782
−13.560
−8.530
1.00
48.92
A


ATOM
585
CA
PRO
A
79
−24.913
−12.530
−10.524
1.00
48.42
A


ATOM
586
CB
PRO
A
79
−26.114
−11.762
−10.004
1.00
48.75
A


ATOM
587
CG
PRO
A
79
−26.860
−12.841
−9.308
1.00
49.27
A


ATOM
588
C
PRO
A
79
−23.803
−11.611
−11.039
1.00
47.58
A


ATOM
589
O
PRO
A
79
−23.015
−11.999
−11.917
1.00
48.27
A


ATOM
590
N
ALA
A
80
−23.751
−10.394
−10.504
1.00
44.81
A


ATOM
591
CA
ALA
A
80
−22.765
−9.417
−10.938
1.00
41.38
A


ATOM
592
CB
ALA
A
80
−23.427
−8.058
−11.109
1.00
40.61
A


ATOM
593
C
ALA
A
80
−21.599
−9.312
−9.978
1.00
39.63
A


ATOM
594
O
ALA
A
80
−21.166
−8.219
−9.625
1.00
39.74
A


ATOM
595
N
VAL
A
81
−21.076
−10.457
−9.567
1.00
37.52
A


ATOM
596
CA
VAL
A
81
−19.950
−10.479
−8.646
1.00
35.26
A


ATOM
597
CB
VAL
A
81
−20.380
−11.038
−7.276
1.00
34.98
A


ATOM
598
CG1
VAL
A
81
−19.193
−11.110
−6.337
1.00
32.95
A


ATOM
599
CG2
VAL
A
81
−21.473
−10.175
−6.692
1.00
34.19
A


ATOM
600
C
VAL
A
81
−18.815
−11.328
−9.204
1.00
34.49
A


ATOM
601
O
VAL
A
81
−19.012
−12.490
−9.559
1.00
34.64
A


ATOM
602
N
PHE
A
82
−17.628
−10.742
−9.286
1.00
33.80
A


ATOM
603
CA
PHE
A
82
−16.471
−11.457
−9.805
1.00
34.10
A


ATOM
604
CB
PHE
A
82
−15.909
−10.758
−11.049
1.00
32.25
A


ATOM
605
CG
PHE
A
82
−16.919
−10.533
−12.134
1.00
30.18
A


ATOM
606
CD1
PHE
A
82
−17.829
−9.492
−12.048
1.00
28.63
A


ATOM
607
CD2
PHE
A
82
−16.967
−11.367
−13.245
1.00
29.67
A


ATOM
608
CE1
PHE
A
82
−18.764
−9.286
−13.051
1.00
28.96
A


ATOM
609
CE2
PHE
A
82
−17.903
−11.162
−14.248
1.00
29.77
A


ATOM
610
CZ
PHE
A
82
−18.803
−10.121
−14.151
1.00
29.10
A


ATOM
611
C
PHE
A
82
−15.401
−11.508
−8.735
1.00
35.20
A


ATOM
612
O
PHE
A
82
−15.527
−10.872
−7.695
1.00
35.28
A


ATOM
613
N
LYS
A
83
−14.344
−12.261
−8.988
1.00
37.28
A


ATOM
614
CA
LYS
A
83
−13.281
−12.354
−8.014
1.00
40.61
A


ATOM
615
CB
LYS
A
83
−13.354
−13.689
−7.282
1.00
41.61
A


ATOM
616
CG
LYS
A
83
−12.383
−13.787
−6.118
1.00
44.64
A


ATOM
617
CD
LYS
A
83
−12.342
−15.182
−5.500
1.00
45.25
A


ATOM
618
CE
LYS
A
83
−11.773
−16.211
−6.467
1.00
46.11
A


ATOM
619
NZ
LYS
A
83
−11.737
−17.558
−5.854
1.00
45.81
A


ATOM
620
C
LYS
A
83
−11.917
−12.198
−8.667
1.00
42.61
A


ATOM
621
O
LYS
A
83
−11.716
−12.622
−9.801
1.00
41.97
A


ATOM
622
N
ILE
A
84
−10.989
−11.582
−7.941
1.00
45.99
A


ATOM
623
CA
ILE
A
84
−9.634
−11.357
−8.422
1.00
50.16
A


ATOM
624
CB
ILE
A
84
−9.173
−9.929
−8.133
1.00
50.06
A


ATOM
625
CG2
ILE
A
84
−7.789
−9.706
−8.719
1.00
50.61
A


ATOM
626
CG1
ILE
A
84
−10.159
−8.929
−8.724
1.00
49.73
A


ATOM
627
CD1
ILE
A
84
−10.097
−7.572
−8.059
1.00
50.68
A


ATOM
628
C
ILE
A
84
−8.713
−12.309
−7.682
1.00
53.84
A


ATOM
629
O
ILE
A
84
−8.653
−12.295
−6.453
1.00
54.52
A


ATOM
630
N
ASP
A
85
−7.989
−13.127
−8.437
1.00
58.42
A


ATOM
631
CA
ASP
A
85
−7.077
−14.110
−7.855
1.00
62.83
A


ATOM
632
CB
ASP
A
85
−6.543
−15.030
−8.960
1.00
64.60
A


ATOM
633
CG
ASP
A
85
−6.508
−16.494
−8.540
1.00
66.46
A


ATOM
634
OD1
ASP
A
85
−6.292
−17.364
−9.421
1.00
67.24
A


ATOM
635
OD2
ASP
A
85
−6.695
−16.771
−7.330
1.00
67.13
A


ATOM
636
C
ASP
A
85
−5.909
−13.512
−7.052
1.00
64.82
A


ATOM
637
O
ASP
A
85
−5.184
−14.243
−6.373
1.00
65.69
A


ATOM
638
N
ALA
A
86
−5.725
−12.195
−7.129
1.00
66.46
A


ATOM
639
CA
ALA
A
86
−4.655
−11.533
−6.386
1.00
68.14
A


ATOM
640
CB
ALA
A
86
−4.686
−10.028
−6.644
1.00
67.64
A


ATOM
641
C
ALA
A
86
−4.843
−11.817
−4.896
1.00
69.84
A


ATOM
642
O
ALA
A
86
−5.910
−12.273
−4.477
1.00
71.12
A


ATOM
643
N
LEU
A
87
−3.814
−11.551
−4.097
1.00
71.20
A


ATOM
644
CA
LEU
A
87
−3.893
−11.792
−2.655
1.00
71.87
A


ATOM
645
CB
LEU
A
87
−2.572
−11.406
−1.967
1.00
72.10
A


ATOM
646
CG
LEU
A
87
−2.329
−11.877
−0.520
1.00
72.35
A


ATOM
647
CD1
LEU
A
87
−2.150
−13.388
−0.499
1.00
71.46
A


ATOM
648
CD2
LEU
A
87
−1.084
−11.201
0.051
1.00
72.25
A


ATOM
649
C
LEU
A
87
−5.043
−10.989
−2.045
1.00
72.03
A


ATOM
650
O
LEU
A
87
−5.599
−10.086
−2.683
1.00
71.30
A


ATOM
651
N
ASN
A
88
−5.383
−11.326
−0.802
1.00
71.95
A


ATOM
652
CA
ASN
A
88
−6.457
−10.664
−0.064
1.00
71.65
A


ATOM
653
CB
ASN
A
88
−6.299
−9.132
−0.143
1.00
73.05
A


ATOM
654
CG
ASN
A
88
−4.849
−8.670
0.032
1.00
73.75
A


ATOM
655
OD1
ASN
A
88
−4.164
−9.051
0.989
1.00
74.21
A


ATOM
656
ND2
ASN
A
88
−4.387
−7.831
−0.891
1.00
73.03
A


ATOM
657
C
ASN
A
88
−7.838
−11.067
−0.606
1.00
70.43
A


ATOM
658
O
ASN
A
88
−8.851
−10.913
0.084
1.00
70.57
A


ATOM
659
N
GLU
A
89
−7.863
−11.582
−1.839
1.00
68.18
A


ATOM
660
CA
GLU
A
89
−9.100
−11.997
−2.511
1.00
65.08
A


ATOM
661
CB
GLU
A
89
−9.798
−13.114
−1.728
1.00
67.04
A


ATOM
662
CG
GLU
A
89
−9.172
−14.497
−1.905
1.00
69.48
A


ATOM
663
CD
GLU
A
89
−9.208
−14.972
−3.357
1.00
70.72
A


ATOM
664
OE1
GLU
A
89
−8.437
−14.439
−4.191
1.00
71.05
A


ATOM
665
OE2
GLU
A
89
−10.024
−15.869
−3.664
1.00
71.34
A


ATOM
666
C
GLU
A
89
−10.076
−10.844
−2.719
1.00
61.80
A


ATOM
667
O
GLU
A
89
−11.203
−10.870
−2.224
1.00
62.02
A


ATOM
668
N
ASN
A
90
−9.630
−9.829
−3.448
1.00
57.36
A


ATOM
669
CA
ASN
A
90
−10.460
−8.671
−3.727
1.00
52.67
A


ATOM
670
CB
ASN
A
90
−9.647
−7.646
−4.533
1.00
52.48
A


ATOM
671
CG
ASN
A
90
−8.928
−6.634
−3.646
1.00
52.32
A


ATOM
672
OD1
ASN
A
90
−9.508
−5.631
−3.216
1.00
53.38
A


ATOM
673
ND2
ASN
A
90
−7.663
−6.899
−3.364
1.00
52.47
A


ATOM
674
C
ASN
A
90
−11.715
−9.096
−4.501
1.00
49.56
A


ATOM
675
O
ASN
A
90
−11.625
−9.859
−5.458
1.00
48.05
A


ATOM
676
N
LYS
A
91
−12.886
−8.639
−4.061
1.00
46.27
A


ATOM
677
CA
LYS
A
91
−14.127
−8.960
−4.756
1.00
42.55
A


ATOM
678
CB
LYS
A
91
−15.196
−9.528
−3.816
1.00
43.88
A


ATOM
679
CG
LYS
A
91
−15.043
−11.009
−3.467
1.00
46.95
A


ATOM
680
CD
LYS
A
91
−16.307
−11.537
−2.772
1.00
49.01
A


ATOM
681
CE
LYS
A
91
−16.120
−12.957
−2.226
1.00
48.98
A


ATOM
682
NZ
LYS
A
91
−17.356
−13.517
−1.586
1.00
47.83
A


ATOM
683
C
LYS
A
91
−14.667
−7.697
−5.394
1.00
39.10
A


ATOM
684
O
LYS
A
91
−14.642
−6.621
−4.797
1.00
38.37
A


ATOM
685
N
VAL
A
92
−15.150
−7.839
−6.619
1.00
35.12
A


ATOM
686
CA
VAL
A
92
−15.703
−6.721
−7.356
1.00
31.05
A


ATOM
687
CB
VAL
A
92
−15.035
−6.638
−8.732
1.00
30.40
A


ATOM
688
CG1
VAL
A
92
−15.487
−5.402
−9.460
1.00
30.11
A


ATOM
689
CG2
VAL
A
92
−13.526
−6.647
−8.558
1.00
29.54
A


ATOM
690
C
VAL
A
92
−17.210
−6.939
−7.502
1.00
28.12
A


ATOM
691
O
VAL
A
92
−17.658
−8.058
−7.731
1.00
27.38
A


ATOM
692
N
LEU
A
93
−17.991
−5.875
−7.348
1.00
25.32
A


ATOM
693
CA
LEU
A
93
−19.442
−5.972
−7.470
1.00
23.52
A


ATOM
694
CB
LEU
A
93
−20.109
−5.806
−6.107
1.00
24.09
A


ATOM
695
CG
LEU
A
93
−19.510
−6.500
−4.880
1.00
22.89
A


ATOM
696
CD1
LEU
A
93
−19.306
−7.960
−5.154
1.00
23.08
A


ATOM
697
CD2
LEU
A
93
−18.197
−5.831
−4.513
1.00
24.87
A


ATOM
698
C
LEU
A
93
−19.955
−4.875
−8.392
1.00
22.06
A


ATOM
699
O
LEU
A
93
−19.679
−3.699
−8.169
1.00
22.62
A


ATOM
700
N
VAL
A
94
−20.700
−5.250
−9.423
1.00
20.24
A


ATOM
701
CA
VAL
A
94
−21.234
−4.262
−10.359
1.00
19.43
A


ATOM
702
CB
VAL
A
94
−21.402
−4.869
−11.785
1.00
18.31
A


ATOM
703
CG1
VAL
A
94
−21.967
−3.841
−12.735
1.00
16.47
A


ATOM
704
CG2
VAL
A
94
−20.072
−5.368
−12.291
1.00
14.46
A


ATOM
705
C
VAL
A
94
−22.582
−3.795
−9.823
1.00
19.37
A


ATOM
706
O
VAL
A
94
−23.565
−4.536
−9.843
1.00
19.85
A


ATOM
707
N
LEU
A
95
−22.618
−2.563
−9.333
1.00
18.93
A


ATOM
708
CA
LEU
A
95
−23.838
−2.009
−8.766
1.00
18.77
A


ATOM
709
CB
LEU
A
95
−23.502
−0.785
−7.915
1.00
20.01
A


ATOM
710
CG
LEU
A
95
−22.774
−1.051
−6.591
1.00
20.85
A


ATOM
711
CD1
LEU
A
95
−22.627
0.263
−5.844
1.00
20.24
A


ATOM
712
CD2
LEU
A
95
−23.576
−2.041
−5.738
1.00
21.51
A


ATOM
713
C
LEU
A
95
−24.898
−1.639
−9.793
1.00
18.28
A


ATOM
714
O
LEU
A
95
−26.080
−1.907
−9.591
1.00
16.17
A


ATOM
715
N
ASP
A
96
−24.477
−1.024
−10.889
1.00
19.53
A


ATOM
716
CA
ASP
A
96
−25.413
−0.623
−11.926
1.00
21.52
A


ATOM
717
CB
ASP
A
96
−26.225
0.582
−11.460
1.00
21.47
A


ATOM
718
CG
ASP
A
96
−27.412
0.850
−12.350
1.00
22.85
A


ATOM
719
OD1
ASP
A
96
−28.132
−0.126
−12.655
1.00
25.16
A


ATOM
720
OD2
ASP
A
96
−27.635
2.020
−12.733
1.00
23.28
A


ATOM
721
C
ASP
A
96
−24.667
−0.269
−13.204
1.00
22.80
A


ATOM
722
O
ASP
A
96
−23.461
−0.023
−13.169
1.00
24.06
A


ATOM
723
N
THR
A
97
−25.383
−0.247
−14.326
1.00
22.38
A


ATOM
724
CA
THR
A
97
−24.776
0.095
−15.600
1.00
22.34
A


ATOM
725
CB
THR
A
97
−23.696
−0.931
−16.006
1.00
22.56
A


ATOM
726
OG1
THR
A
97
−23.116
−0.553
−17.264
1.00
22.90
A


ATOM
727
CG2
THR
A
97
−24.303
−2.319
−16.139
1.00
20.01
A


ATOM
728
C
THR
A
97
−25.803
0.143
−16.707
1.00
22.52
A


ATOM
729
O
THR
A
97
−26.726
−0.659
−16.711
1.00
23.66
A


ATOM
730
N
ASP
A
98
−25.642
1.083
−17.637
1.00
22.22
A


ATOM
731
CA
ASP
A
98
−26.544
1.203
−18.780
1.00
21.65
A


ATOM
732
CB
ASP
A
98
−26.949
2.671
−19.004
1.00
22.77
A


ATOM
733
CG
ASP
A
98
−25.814
3.527
−19.532
1.00
24.72
A


ATOM
734
OD1
ASP
A
98
−24.658
3.311
−19.127
1.00
27.27
A


ATOM
735
OD2
ASP
A
98
−26.075
4.434
−20.347
1.00
26.48
A


ATOM
736
C
ASP
A
98
−25.819
0.635
−20.007
1.00
21.37
A


ATOM
737
O
ASP
A
98
−26.393
0.538
−21.086
1.00
20.79
A


ATOM
738
N
TYR
A
99
−24.555
0.252
−19.815
1.00
20.65
A


ATOM
739
CA
TYR
A
99
−23.708
−0.330
−20.864
1.00
19.29
A


ATOM
740
CB
TYR
A
99
−24.451
−1.454
−21.601
1.00
16.84
A


ATOM
741
CG
TYR
A
99
−24.856
−2.627
−20.750
1.00
14.61
A


ATOM
742
CD1
TYR
A
99
−23.946
−3.617
−20.406
1.00
12.54
A


ATOM
743
CE1
TYR
A
99
−24.328
−4.698
−19.614
1.00
12.07
A


ATOM
744
CD2
TYR
A
99
−26.156
−2.742
−20.280
1.00
13.65
A


ATOM
745
CE2
TYR
A
99
−26.547
−3.814
−19.492
1.00
13.03
A


ATOM
746
CZ
TYR
A
99
−25.631
−4.792
−19.157
1.00
13.13
A


ATOM
747
OH
TYR
A
99
−26.036
−5.856
−18.365
1.00
12.49
A


ATOM
748
C
TYR
A
99
−23.194
0.667
−21.902
1.00
20.53
A


ATOM
749
O
TYR
A
99
−22.073
0.530
−22.379
1.00
20.58
A


ATOM
750
N
LYS
A
100
−24.005
1.670
−22.238
1.00
21.61
A


ATOM
751
CA
LYS
A
100
−23.649
2.654
−23.258
1.00
21.03
A


ATOM
752
CB
LYS
A
100
−24.891
3.004
−24.085
1.00
23.12
A


ATOM
753
CG
LYS
A
100
−25.705
1.800
−24.531
1.00
26.96
A


ATOM
754
CD
LYS
A
100
−24.896
0.871
−25.424
1.00
29.57
A


ATOM
755
CE
LYS
A
100
−25.436
−0.584
−25.398
1.00
33.09
A


ATOM
756
NZ
LYS
A
100
−26.875
−0.751
−25.800
1.00
33.75
A


ATOM
757
C
LYS
A
100
−23.046
3.946
−22.718
1.00
20.25
A


ATOM
758
O
LYS
A
100
−22.413
4.689
−23.461
1.00
20.17
A


ATOM
759
N
LYS
A
101
−23.236
4.228
−21.435
1.00
19.04
A


ATOM
760
CA
LYS
A
101
−22.701
5.467
−20.874
1.00
17.66
A


ATOM
761
CB
LYS
A
101
−23.837
6.492
−20.704
1.00
17.25
A


ATOM
762
CG
LYS
A
101
−24.408
7.018
−22.017
1.00
18.59
A


ATOM
763
CD
LYS
A
101
−25.507
8.052
−21.803
1.00
21.15
A


ATOM
764
CE
LYS
A
101
−26.614
7.492
−20.892
1.00
25.51
A


ATOM
765
NZ
LYS
A
101
−27.841
8.354
−20.716
1.00
25.35
A


ATOM
766
C
LYS
A
101
−21.927
5.328
−19.552
1.00
16.29
A


ATOM
767
O
LYS
A
101
−20.783
5.767
−19.457
1.00
16.64
A


ATOM
768
N
TYR
A
102
−22.541
4.723
−18.539
1.00
13.96
A


ATOM
769
CA
TYR
A
102
−21.884
4.579
−17.250
1.00
12.20
A


ATOM
770
CB
TYR
A
102
−22.552
5.485
−16.221
1.00
13.37
A


ATOM
771
CG
TYR
A
102
−23.967
5.074
−15.913
1.00
14.80
A


ATOM
772
CD1
TYR
A
102
−25.026
5.452
−16.743
1.00
15.56
A


ATOM
773
CE1
TYR
A
102
−26.332
5.040
−16.473
1.00
16.40
A


ATOM
774
CD2
TYR
A
102
−24.245
4.275
−14.810
1.00
14.91
A


ATOM
775
CE2
TYR
A
102
−25.537
3.852
−14.533
1.00
16.83
A


ATOM
776
CZ
TYR
A
102
−26.574
4.231
−15.362
1.00
17.72
A


ATOM
777
OH
TYR
A
102
−27.843
3.776
−15.086
1.00
19.73
A


ATOM
778
C
TYR
A
102
−21.870
3.163
−16.691
1.00
11.60
A


ATOM
779
O
TYR
A
102
−22.555
2.272
−17.194
1.00
11.84
A


ATOM
780
N
LEU
A
103
−21.081
2.973
−15.636
1.00
9.56
A


ATOM
781
CA
LEU
A
103
−20.979
1.690
−14.954
1.00
8.12
A


ATOM
782
CB
LEU
A
103
−20.022
0.743
−15.694
1.00
8.06
A


ATOM
783
CG
LEU
A
103
−19.983
−0.682
−15.115
1.00
7.72
A


ATOM
784
CD1
LEU
A
103
−19.586
−1.676
−16.152
1.00
8.20
A


ATOM
785
CD2
LEU
A
103
−19.049
−0.720
−13.930
1.00
7.20
A


ATOM
786
C
LEU
A
103
−20.488
1.948
−13.526
1.00
9.01
A


ATOM
787
O
LEU
A
103
−19.541
2.692
−13.313
1.00
8.51
A


ATOM
788
N
LEU
A
104
−21.136
1.319
−12.551
1.00
9.89
A


ATOM
789
CA
LEU
A
104
−20.773
1.513
−11.158
1.00
10.66
A


ATOM
790
CB
LEU
A
104
−21.958
2.088
−10.398
1.00
10.47
A


ATOM
791
CG
LEU
A
104
−22.586
3.339
−11.002
1.00
9.11
A


ATOM
792
CD1
LEU
A
104
−23.833
3.732
−10.219
1.00
8.12
A


ATOM
793
CD2
LEU
A
104
−21.576
4.465
−10.984
1.00
8.64
A


ATOM
794
C
LEU
A
104
−20.354
0.225
−10.485
1.00
11.23
A


ATOM
795
O
LEU
A
104
−21.083
−0.758
−10.534
1.00
13.70
A


ATOM
796
N
PHE
A
105
−19.202
0.232
−9.829
1.00
10.76
A


ATOM
797
CA
PHE
A
105
−18.748
−0.969
−9.153
1.00
11.87
A


ATOM
798
CB
PHE
A
105
−17.829
−1.782
−10.068
1.00
10.16
A


ATOM
799
CG
PHE
A
105
−16.489
−1.140
−10.292
1.00
9.81
A


ATOM
800
CD1
PHE
A
105
−16.337
−0.129
−11.249
1.00
8.87
A


ATOM
801
CD2
PHE
A
105
−15.391
−1.494
−9.482
1.00
8.20
A


ATOM
802
CE1
PHE
A
105
−15.118
0.521
−11.394
1.00
9.90
A


ATOM
803
CE2
PHE
A
105
−14.164
−0.857
−9.606
1.00
6.67
A


ATOM
804
CZ
PHE
A
105
−14.016
0.156
−10.563
1.00
9.33
A


ATOM
805
C
PHE
A
105
−17.996
−0.615
−7.877
1.00
14.65
A


ATOM
806
O
PHE
A
105
−17.598
0.535
−7.675
1.00
13.84
A


ATOM
807
N
CYS
A
106
−17.809
−1.620
−7.028
1.00
17.88
A


ATOM
808
CA
CYS
A
106
−17.085
−1.469
−5.774
1.00
21.18
A


ATOM
809
C
CYS
A
106
−16.159
−2.660
−5.649
1.00
24.19
A


ATOM
810
O
CYS
A
106
−16.388
−3.698
−6.272
1.00
24.79
A


ATOM
811
CB
CYS
A
106
−18.026
−1.484
−4.571
1.00
20.47
A


ATOM
812
SG
CYS
A
106
−19.182
−0.095
−4.399
1.00
22.55
A


ATOM
813
N
MET
A
107
−15.115
−2.521
−4.846
1.00
27.17
A


ATOM
814
CA
MET
A
107
−14.205
−3.625
−4.652
1.00
32.34
A


ATOM
815
CB
MET
A
107
−12.999
−3.483
−5.575
1.00
31.11
A


ATOM
816
CG
MET
A
107
−12.201
−2.228
−5.382
1.00
30.90
A


ATOM
817
SD
MET
A
107
−11.147
−1.907
−6.805
1.00
30.75
A


ATOM
818
CE
MET
A
107
−11.313
−0.129
−6.939
1.00
30.73
A


ATOM
819
C
MET
A
107
−13.779
−3.692
−3.202
1.00
36.20
A


ATOM
820
O
MET
A
107
−13.458
−2.670
−2.606
1.00
36.17
A


ATOM
821
N
GLU
A
108
−13.806
−4.894
−2.625
1.00
41.42
A


ATOM
822
CA
GLU
A
108
−13.416
−5.086
−1.225
1.00
45.26
A


ATOM
823
CB
GLU
A
108
−14.655
−5.281
−0.344
1.00
45.70
A


ATOM
824
CG
GLU
A
108
−15.475
−6.512
−0.691
1.00
47.75
A


ATOM
825
CD
GLU
A
108
−16.441
−6.901
0.412
1.00
48.53
A


ATOM
826
OE1
GLU
A
108
−17.331
−6.087
0.742
1.00
48.20
A


ATOM
827
OE2
GLU
A
108
−16.303
−8.024
0.948
1.00
50.31
A


ATOM
828
C
GLU
A
108
−12.500
−6.287
−1.055
1.00
47.65
A


ATOM
829
O
GLU
A
108
−12.474
−7.181
−1.894
1.00
47.55
A


ATOM
830
N
ASN
A
109
−11.744
−6.297
0.034
1.00
51.81
A


ATOM
831
CA
ASN
A
109
−10.852
−7.408
0.310
1.00
56.91
A


ATOM
832
CB
ASN
A
109
−9.469
−6.900
0.729
1.00
58.54
A


ATOM
833
CG
ASN
A
109
−8.779
−6.089
−0.373
1.00
60.68
A


ATOM
834
OD1
ASN
A
109
−9.271
−5.030
−0.790
1.00
61.57
A


ATOM
835
ND2
ASN
A
109
−7.636
−6.590
−0.853
1.00
60.43
A


ATOM
836
C
ASN
A
109
−11.451
−8.258
1.415
1.00
59.35
A


ATOM
837
O
ASN
A
109
−11.616
−7.800
2.544
1.00
59.16
A


ATOM
838
N
SER
A
110
−11.789
−9.494
1.072
1.00
63.16
A


ATOM
839
CA
SER
A
110
−12.367
−10.425
2.034
1.00
66.90
A


ATOM
840
CB
SER
A
110
−12.335
−11.850
1.471
1.00
66.79
A


ATOM
841
OG
SER
A
110
−12.800
−12.790
2.426
0.00
67.03
A


ATOM
842
C
SER
A
110
−11.629
−10.390
3.378
1.00
68.96
A


ATOM
843
O
SER
A
110
−12.247
−10.508
4.442
1.00
69.21
A


ATOM
844
N
ALA
A
111
−10.309
−10.228
3.324
1.00
70.87
A


ATOM
845
CA
ALA
A
111
−9.497
−10.182
4.534
1.00
73.10
A


ATOM
846
CB
ALA
A
111
−8.041
−9.886
4.178
1.00
74.11
A


ATOM
847
C
ALA
A
111
−10.027
−9.127
5.502
1.00
74.80
A


ATOM
848
O
ALA
A
111
−10.281
−9.414
6.672
1.00
75.12
A


ATOM
849
N
GLU
A
112
−10.191
−7.904
5.010
1.00
76.54
A


ATOM
850
CA
GLU
A
112
−10.699
−6.812
5.832
1.00
77.67
A


ATOM
851
CB
GLU
A
112
−9.578
−5.812
6.142
1.00
78.60
A


ATOM
852
CG
GLU
A
112
−8.796
−6.095
7.440
1.00
79.84
A


ATOM
853
CD
GLU
A
112
−8.054
−7.425
7.433
1.00
80.21
A


ATOM
854
OE1
GLU
A
112
−7.213
−7.638
6.529
1.00
80.30
A


ATOM
855
OE2
GLU
A
112
−8.305
−8.248
8.344
1.00
79.95
A


ATOM
856
C
GLU
A
112
−11.858
−6.105
5.130
1.00
77.80
A


ATOM
857
O
GLU
A
112
−11.687
−5.032
4.555
1.00
77.90
A


ATOM
858
N
PRO
A
113
−13.060
−6.710
5.164
1.00
77.88
A


ATOM
859
CD
PRO
A
113
−13.373
−8.027
5.750
1.00
77.78
A


ATOM
860
CA
PRO
A
113
−14.248
−6.130
4.527
1.00
77.56
A


ATOM
861
CB
PRO
A
113
−15.233
−7.294
4.526
1.00
77.90
A


ATOM
862
CG
PRO
A
113
−14.885
−8.010
5.793
1.00
78.21
A


ATOM
863
C
PRO
A
113
−14.791
−4.909
5.275
1.00
76.94
A


ATOM
864
O
PRO
A
113
−15.998
−4.664
5.290
1.00
77.05
A


ATOM
865
N
GLU
A
114
−13.888
−4.151
5.893
1.00
75.57
A


ATOM
866
CA
GLU
A
114
−14.258
−2.954
6.646
1.00
73.78
A


ATOM
867
CB
GLU
A
114
−14.203
−3.244
8.151
1.00
75.45
A


ATOM
868
CG
GLU
A
114
−15.247
−4.243
8.650
1.00
78.06
A


ATOM
869
CD
GLU
A
114
−15.136
−4.521
10.149
1.00
79.68
A


ATOM
870
OE1
GLU
A
114
−15.184
−3.554
10.947
1.00
80.23
A


ATOM
871
OE2
GLU
A
114
−15.006
−5.709
10.529
1.00
80.56
A


ATOM
872
C
GLU
A
114
−13.327
−1.785
6.314
1.00
71.15
A


ATOM
873
O
GLU
A
114
−13.738
−0.620
6.330
1.00
70.50
A


ATOM
874
N
GLN
A
115
−12.071
−2.110
6.017
1.00
68.29
A


ATOM
875
CA
GLN
A
115
−11.057
−1.110
5.681
1.00
64.44
A


ATOM
876
CB
GLN
A
115
−9.952
−1.083
6.757
1.00
66.01
A


ATOM
877
CG
GLN
A
115
−9.552
−2.450
7.325
1.00
66.72
A


ATOM
878
CD
GLN
A
115
−10.479
−2.918
8.444
1.00
67.94
A


ATOM
879
OE1
GLN
A
115
−10.572
−2.282
9.497
1.00
68.73
A


ATOM
880
NE2
GLN
A
115
−11.166
−4.035
8.220
1.00
68.36
A


ATOM
881
C
GLN
A
115
−10.436
−1.334
4.297
1.00
59.98
A


ATOM
882
O
GLN
A
115
−9.217
−1.230
4.120
1.00
59.29
A


ATOM
883
N
SER
A
116
−11.289
−1.638
3.322
1.00
54.28
A


ATOM
884
CA
SER
A
116
−10.852
−1.868
1.956
1.00
48.50
A


ATOM
885
CB
SER
A
116
−10.068
−3.177
1.847
1.00
49.02
A


ATOM
886
OG
SER
A
116
−10.929
−4.299
1.952
1.00
48.61
A


ATOM
887
C
SER
A
116
−12.041
−1.914
1.009
1.00
44.48
A


ATOM
888
O
SER
A
116
−12.159
−2.826
0.200
1.00
45.41
A


ATOM
889
N
LEU
A
117
−12.939
−0.946
1.123
1.00
39.02
A


ATOM
890
CA
LEU
A
117
−14.085
−0.894
0.233
1.00
33.21
A


ATOM
891
CB
LEU
A
117
−15.398
−0.842
1.023
1.00
32.48
A


ATOM
892
CG
LEU
A
117
−16.677
−0.687
0.179
1.00
32.08
A


ATOM
893
CD1
LEU
A
117
−16.989
−1.984
−0.551
1.00
32.14
A


ATOM
894
CD2
LEU
A
117
−17.843
−0.320
1.073
1.00
32.82
A


ATOM
895
C
LEU
A
117
−13.965
0.348
−0.643
1.00
29.70
A


ATOM
896
O
LEU
A
117
−14.139
1.469
−0.164
1.00
29.28
A


ATOM
897
N
ALA
A
118
−13.640
0.152
−1.917
1.00
25.59
A


ATOM
898
CA
ALA
A
118
−13.524
1.268
−2.854
1.00
21.14
A


ATOM
899
CB
ALA
A
118
−12.120
1.322
−3.465
1.00
19.41
A


ATOM
900
C
ALA
A
118
−14.566
1.083
−3.942
1.00
17.56
A


ATOM
901
O
ALA
A
118
−14.859
−0.038
−4.351
1.00
17.34
A


ATOM
902
N
CYS
A
119
−15.133
2.185
−4.402
1.00
15.41
A


ATOM
903
CA
CYS
A
119
−16.147
2.127
−5.447
1.00
14.62
A


ATOM
904
C
CYS
A
119
−15.805
3.145
−6.520
1.00
12.55
A


ATOM
905
O
CYS
A
119
−15.160
4.150
−6.239
1.00
12.39
A


ATOM
906
CB
CYS
A
119
−17.527
2.449
−4.881
1.00
16.58
A


ATOM
907
SG
CYS
A
119
−18.118
1.399
−3.507
1.00
19.89
A


ATOM
908
N
GLN
A
120
−16.242
2.902
−7.751
1.00
11.31
A


ATOM
909
CA
GLN
A
120
−15.931
3.837
−8.826
1.00
9.34
A


ATOM
910
CB
GLN
A
120
−14.691
3.382
−9.600
1.00
8.23
A


ATOM
911
CG
GLN
A
120
−13.408
3.510
−8.824
1.00
9.44
A


ATOM
912
CD
GLN
A
120
−12.192
3.228
−9.666
1.00
10.28
A


ATOM
913
OE1
GLN
A
120
−12.276
3.187
−10.895
1.00
9.16
A


ATOM
914
NE2
GLN
A
120
−11.042
3.044
−9.011
1.00
11.24
A


ATOM
915
C
GLN
A
120
−17.055
4.029
−9.808
1.00
7.85
A


ATOM
916
O
GLN
A
120
−17.935
3.191
−9.936
1.00
8.44
A


ATOM
917
N
CYS
A
121
−17.015
5.160
−10.491
1.00
6.54
A


ATOM
918
CA
CYS
A
121
−17.985
5.467
−11.505
1.00
5.28
A


ATOM
919
CB
CYS
A
121
−18.684
6.774
−11.200
1.00
3.98
A


ATOM
920
SG
CYS
A
121
−19.807
7.249
−12.559
1.00
6.72
A


ATOM
921
C
CYS
A
121
−17.230
5.594
−12.829
1.00
5.88
A


ATOM
922
O
CYS
A
121
−16.462
6.539
−13.035
1.00
6.74
A


ATOM
923
N
LEU
A
122
−17.439
4.621
−13.711
1.00
4.93
A


ATOM
924
CA
LEU
A
122
−16.796
4.583
−15.016
1.00
4.70
A


ATOM
925
CB
LEU
A
122
−16.472
3.133
−15.390
1.00
2.79
A


ATOM
926
CG
LEU
A
122
−15.544
2.308
−14.507
1.00
3.05
A


ATOM
927
CD1
LEU
A
122
−15.272
0.946
−15.164
1.00
1.00
A


ATOM
928
CD2
LEU
A
122
−14.247
3.051
−14.288
1.00
2.57
A


ATOM
929
C
LEU
A
122
−17.708
5.192
−16.085
1.00
4.56
A


ATOM
930
O
LEU
A
122
−18.909
5.334
−15.871
1.00
3.87
A


ATOM
931
N
VAL
A
123
−17.130
5.577
−17.221
1.00
5.28
A


ATOM
932
CA
VAL
A
123
−17.908
6.131
−18.327
1.00
7.18
A


ATOM
933
CB
VAL
A
123
−18.066
7.656
−18.252
1.00
5.88
A


ATOM
934
CG1
VAL
A
123
−19.103
8.011
−17.226
1.00
4.32
A


ATOM
935
CG2
VAL
A
123
−16.727
8.304
−17.961
1.00
5.09
A


ATOM
936
C
VAL
A
123
−17.262
5.806
−19.655
1.00
8.00
A


ATOM
937
O
VAL
A
123
−16.063
5.591
−19.731
1.00
9.15
A


ATOM
938
N
ARG
A
124
−18.061
5.783
−20.708
1.00
9.32
A


ATOM
939
CA
ARG
A
124
−17.546
5.467
−22.024
1.00
11.59
A


ATOM
940
CB
ARG
A
124
−18.701
5.084
−22.931
1.00
10.68
A


ATOM
941
CG
ARG
A
124
−19.397
3.813
−22.512
1.00
9.01
A


ATOM
942
CD
ARG
A
124
−18.512
2.641
−22.744
1.00
10.13
A


ATOM
943
NE
ARG
A
124
−19.251
1.379
−22.807
1.00
10.56
A


ATOM
944
CZ
ARG
A
124
−18.684
0.222
−23.122
1.00
10.23
A


ATOM
945
NH1
ARG
A
124
−17.387
0.172
−23.399
1.00
11.34
A


ATOM
946
NH2
ARG
A
124
−19.401
−0.878
−23.151
1.00
9.22
A


ATOM
947
C
ARG
A
124
−16.742
6.600
−22.646
1.00
12.71
A


ATOM
948
O
ARG
A
124
−15.653
6.378
−23.172
1.00
11.93
A


ATOM
949
N
THR
A
125
−17.265
7.817
−22.598
1.00
13.65
A


ATOM
950
CA
THR
A
125
−16.533
8.934
−23.177
1.00
14.62
A


ATOM
951
CB
THR
A
125
−17.445
9.802
−24.041
1.00
14.21
A


ATOM
952
OG1
THR
A
125
−18.544
10.273
−23.253
1.00
13.29
A


ATOM
953
CG2
THR
A
125
−17.951
8.995
−25.232
1.00
12.45
A


ATOM
954
C
THR
A
125
−15.885
9.784
−22.098
1.00
15.60
A


ATOM
955
O
THR
A
125
−16.376
9.859
−20.977
1.00
17.35
A


ATOM
956
N
PRO
A
126
−14.757
10.427
−22.422
1.00
15.78
A


ATOM
957
CD
PRO
A
126
−14.037
10.316
−23.700
1.00
16.42
A


ATOM
958
CA
PRO
A
126
−14.019
11.274
−21.488
1.00
16.99
A


ATOM
959
CB
PRO
A
126
−12.689
11.472
−22.203
1.00
17.41
A


ATOM
960
CG
PRO
A
126
−13.083
11.474
−23.641
1.00
15.72
A


ATOM
961
C
PRO
A
126
−14.717
12.596
−21.183
1.00
18.38
A


ATOM
962
O
PRO
A
126
−14.110
13.671
−21.247
1.00
18.55
A


ATOM
963
N
GLU
A
127
−15.995
12.508
−20.844
1.00
19.23
A


ATOM
964
CA
GLU
A
127
−16.789
13.686
−20.562
1.00
19.40
A


ATOM
965
CB
GLU
A
127
−17.916
13.797
−21.595
1.00
21.19
A


ATOM
966
CG
GLU
A
127
−18.145
15.195
−22.115
1.00
25.72
A


ATOM
967
CD
GLU
A
127
−17.240
15.548
−23.277
1.00
28.77
A


ATOM
968
OE1
GLU
A
127
−16.003
15.421
−23.156
1.00
31.16
A


ATOM
969
OE2
GLU
A
127
−17.774
15.970
−24.319
1.00
30.40
A


ATOM
970
C
GLU
A
127
−17.362
13.511
−19.176
1.00
18.77
A


ATOM
971
O
GLU
A
127
−17.372
12.399
−18.644
1.00
17.85
A


ATOM
972
N
VAL
A
128
−17.816
14.609
−18.581
1.00
18.87
A


ATOM
973
CA
VAL
A
128
−18.422
14.551
−17.259
1.00
19.36
A


ATOM
974
CB
VAL
A
128
−18.215
15.865
−16.488
1.00
19.07
A


ATOM
975
CG1
VAL
A
128
−18.943
15.808
−15.150
1.00
16.94
A


ATOM
976
CG2
VAL
A
128
−16.731
16.100
−16.285
1.00
19.94
A


ATOM
977
C
VAL
A
128
−19.925
14.274
−17.392
1.00
19.92
A


ATOM
978
O
VAL
A
128
−20.694
15.098
−17.885
1.00
18.96
A


ATOM
979
N
ASP
A
129
−20.335
13.095
−16.952
1.00
21.31
A


ATOM
980
CA
ASP
A
129
−21.735
12.708
−17.018
1.00
22.53
A


ATOM
981
CB
ASP
A
129
−21.839
11.213
−17.310
1.00
22.60
A


ATOM
982
CG
ASP
A
129
−23.247
10.784
−17.628
1.00
24.84
A


ATOM
983
OD1
ASP
A
129
−24.172
11.273
−16.931
1.00
25.94
A


ATOM
984
OD2
ASP
A
129
−23.428
9.955
−18.563
1.00
24.73
A


ATOM
985
C
ASP
A
129
−22.402
13.026
−15.681
1.00
23.04
A


ATOM
986
O
ASP
A
129
−22.375
12.214
−14.767
1.00
22.72
A


ATOM
987
N
ASP
A
130
−23.007
14.203
−15.568
1.00
25.17
A


ATOM
988
CA
ASP
A
130
−23.652
14.599
−14.324
1.00
27.39
A


ATOM
989
CB
ASP
A
130
−24.307
15.967
−14.483
1.00
28.36
A


ATOM
990
CG
ASP
A
130
−23.295
17.080
−14.682
1.00
30.38
A


ATOM
991
OD1
ASP
A
130
−22.407
17.253
−13.811
1.00
30.27
A


ATOM
992
OD2
ASP
A
130
−23.402
17.791
−15.707
1.00
31.41
A


ATOM
993
C
ASP
A
130
−24.689
13.589
−13.829
1.00
28.10
A


ATOM
994
O
ASP
A
130
−24.758
13.288
−12.629
1.00
27.21
A


ATOM
995
N
GLU
A
131
−25.497
13.073
−14.749
1.00
28.87
A


ATOM
996
CA
GLU
A
131
−26.528
12.098
−14.396
1.00
30.34
A


ATOM
997
CB
GLU
A
131
−27.415
11.780
−15.608
1.00
32.40
A


ATOM
998
CG
GLU
A
131
−28.620
10.891
−15.283
1.00
36.77
A


ATOM
999
CD
GLU
A
131
−29.516
10.597
−16.495
1.00
39.79
A


ATOM
1000
OE1
GLU
A
131
−29.391
9.498
−17.097
1.00
39.74
A


ATOM
1001
OE2
GLU
A
131
−30.347
11.473
−16.842
1.00
41.54
A


ATOM
1002
C
GLU
A
131
−25.902
10.804
−13.871
1.00
29.77
A


ATOM
1003
O
GLU
A
131
−26.481
10.124
−13.013
1.00
30.31
A


ATOM
1004
N
ALA
A
132
−24.724
10.462
−14.390
1.00
27.73
A


ATOM
1005
CA
ALA
A
132
−24.022
9.261
−13.961
1.00
24.94
A


ATOM
1006
CB
ALA
A
132
−22.890
8.951
−14.917
1.00
25.43
A


ATOM
1007
C
ALA
A
132
−23.485
9.459
−12.547
1.00
24.00
A


ATOM
1008
O
ALA
A
132
−23.628
8.584
−11.690
1.00
22.89
A


ATOM
1009
N
LEU
A
133
−22.875
10.613
−12.301
1.00
22.77
A


ATOM
1010
CA
LEU
A
133
−22.346
10.916
−10.978
1.00
23.19
A


ATOM
1011
CB
LEU
A
133
−21.685
12.293
−10.977
1.00
21.08
A


ATOM
1012
CG
LEU
A
133
−20.298
12.301
−11.606
1.00
20.59
A


ATOM
1013
CD1
LEU
A
133
−19.737
13.703
−11.645
1.00
20.36
A


ATOM
1014
CD2
LEU
A
133
−19.398
11.374
−10.808
1.00
20.36
A


ATOM
1015
C
LEU
A
133
−23.490
10.889
−9.976
1.00
23.95
A


ATOM
1016
O
LEU
A
133
−23.321
10.464
−8.835
1.00
24.50
A


ATOM
1017
N
GLU
A
134
−24.653
11.349
−10.428
1.00
24.99
A


ATOM
1018
CA
GLU
A
134
−25.855
11.383
−9.619
1.00
25.76
A


ATOM
1019
CB
GLU
A
134
−27.027
11.882
−10.457
1.00
28.60
A


ATOM
1020
CG
GLU
A
134
−27.242
13.373
−10.379
1.00
34.21
A


ATOM
1021
CD
GLU
A
134
−27.894
13.791
−9.068
1.00
38.01
A


ATOM
1022
OE1
GLU
A
134
−29.127
13.596
−8.931
1.00
40.41
A


ATOM
1023
OE2
GLU
A
134
−27.175
14.300
−8.173
1.00
39.41
A


ATOM
1024
C
GLU
A
134
−26.169
10.002
−9.081
1.00
25.10
A


ATOM
1025
O
GLU
A
134
−26.307
9.797
−7.877
1.00
25.75
A


ATOM
1026
N
LYS
A
135
−26.286
9.042
−9.980
1.00
23.93
A


ATOM
1027
CA
LYS
A
135
−26.581
7.696
−9.550
1.00
22.05
A


ATOM
1028
CB
LYS
A
135
−26.738
6.789
−10.767
1.00
21.87
A


ATOM
1029
CG
LYS
A
135
−27.675
7.367
−11.806
1.00
22.27
A


ATOM
1030
CD
LYS
A
135
−28.199
6.301
−12.732
1.00
23.04
A


ATOM
1031
CE
LYS
A
135
−29.081
6.926
−13.792
1.00
24.13
A


ATOM
1032
NZ
LYS
A
135
−29.705
5.909
−14.672
1.00
25.19
A


ATOM
1033
C
LYS
A
135
−25.470
7.187
−8.645
1.00
20.93
A


ATOM
1034
O
LYS
A
135
−25.715
6.338
−7.810
1.00
22.80
A


ATOM
1035
N
PHE
A
136
−24.256
7.712
−8.800
1.00
19.44
A


ATOM
1036
CA
PHE
A
136
−23.123
7.276
−7.986
1.00
17.59
A


ATOM
1037
CB
PHE
A
136
−21.804
7.753
−8.623
1.00
16.15
A


ATOM
1038
CG
PHE
A
136
−20.553
7.155
−8.008
1.00
12.06
A


ATOM
1039
CD1
PHE
A
136
−20.380
5.777
−7.924
1.00
10.59
A


ATOM
1040
CD2
PHE
A
136
−19.523
7.986
−7.562
1.00
10.64
A


ATOM
1041
CE1
PHE
A
136
−19.194
5.235
−7.408
1.00
8.70
A


ATOM
1042
CE2
PHE
A
136
−18.333
7.461
−7.045
1.00
8.38
A


ATOM
1043
CZ
PHE
A
136
−18.170
6.080
−6.970
1.00
8.38
A


ATOM
1044
C
PHE
A
136
−23.263
7.820
−6.575
1.00
17.94
A


ATOM
1045
O
PHE
A
136
−23.060
7.094
−5.610
1.00
18.11
A


ATOM
1046
N
ASP
A
137
−23.608
9.097
−6.454
1.00
18.56
A


ATOM
1047
CA
ASP
A
137
−23.777
9.705
−5.140
1.00
20.78
A


ATOM
1048
CB
ASP
A
137
−24.020
11.199
−5.283
1.00
21.98
A


ATOM
1049
CG
ASP
A
137
−22.761
11.933
−5.650
1.00
26.64
A


ATOM
1050
OD1
ASP
A
137
−22.791
13.172
−5.803
1.00
28.97
A


ATOM
1051
OD2
ASP
A
137
−21.715
11.255
−5.780
1.00
29.46
A


ATOM
1052
C
ASP
A
137
−24.916
9.055
−4.381
1.00
21.56
A


ATOM
1053
O
ASP
A
137
−24.829
8.823
−3.180
1.00
20.68
A


ATOM
1054
N
LYS
A
138
−25.978
8.757
−5.114
1.00
23.89
A


ATOM
1055
CA
LYS
A
138
−27.163
8.119
−4.575
1.00
24.77
A


ATOM
1056
CB
LYS
A
138
−28.201
7.983
−5.685
1.00
26.49
A


ATOM
1057
CG
LYS
A
138
−29.590
8.464
−5.311
1.00
29.38
A


ATOM
1058
CD
LYS
A
138
−30.440
8.746
−6.551
1.00
31.73
A


ATOM
1059
CE
LYS
A
138
−30.787
7.464
−7.309
1.00
33.18
A


ATOM
1060
NZ
LYS
A
138
−31.684
6.561
−6.512
1.00
32.38
A


ATOM
1061
C
LYS
A
138
−26.834
6.738
−4.020
1.00
24.53
A


ATOM
1062
O
LYS
A
138
−27.283
6.368
−2.933
1.00
25.44
A


ATOM
1063
N
ALA
A
139
−26.047
5.981
−4.771
1.00
23.16
A


ATOM
1064
CA
ALA
A
139
−25.684
4.640
−4.365
1.00
22.42
A


ATOM
1065
CB
ALA
A
139
−25.192
3.859
−5.557
1.00
22.54
A


ATOM
1066
C
ALA
A
139
−24.631
4.653
−3.296
1.00
22.29
A


ATOM
1067
O
ALA
A
139
−24.315
3.619
−2.725
1.00
23.95
A


ATOM
1068
N
LEU
A
140
−24.091
5.823
−3.007
1.00
22.46
A


ATOM
1069
CA
LEU
A
140
−23.050
5.906
−2.002
1.00
22.59
A


ATOM
1070
CB
LEU
A
140
−21.923
6.819
−2.494
1.00
21.49
A


ATOM
1071
CG
LEU
A
140
−20.640
6.154
−2.992
1.00
20.22
A


ATOM
1072
CD1
LEU
A
140
−20.962
5.055
−3.974
1.00
20.98
A


ATOM
1073
CD2
LEU
A
140
−19.746
7.196
−3.618
1.00
19.16
A


ATOM
1074
C
LEU
A
140
−23.552
6.400
−0.661
1.00
23.85
A


ATOM
1075
O
LEU
A
140
−22.930
6.131
0.362
1.00
24.84
A


ATOM
1076
N
LYS
A
141
−24.684
7.098
−0.660
1.00
23.81
A


ATOM
1077
CA
LYS
A
141
−25.221
7.650
0.572
1.00
23.95
A


ATOM
1078
CB
LYS
A
141
−26.479
8.488
0.275
1.00
27.33
A


ATOM
1079
CG
LYS
A
141
−27.732
7.679
−0.062
1.00
31.67
A


ATOM
1080
CD
LYS
A
141
−28.961
8.581
−0.222
1.00
34.16
A


ATOM
1081
CE
LYS
A
141
−30.252
7.750
−0.167
1.00
35.86
A


ATOM
1082
NZ
LYS
A
141
−31.508
8.520
−0.454
1.00
34.90
A


ATOM
1083
C
LYS
A
141
−25.521
6.577
1.620
1.00
22.86
A


ATOM
1084
O
LYS
A
141
−25.814
6.886
2.776
1.00
23.16
A


ATOM
1085
N
ALA
A
142
−25.425
5.320
1.202
1.00
21.93
A


ATOM
1086
CA
ALA
A
142
−25.673
4.164
2.058
1.00
20.55
A


ATOM
1087
CB
ALA
A
142
−26.646
3.227
1.371
1.00
20.26
A


ATOM
1088
C
ALA
A
142
−24.373
3.399
2.385
1.00
20.23
A


ATOM
1089
O
ALA
A
142
−24.393
2.329
2.994
1.00
20.08
A


ATOM
1090
N
LEU
A
143
−23.241
3.928
1.957
1.00
19.08
A


ATOM
1091
CA
LEU
A
143
−21.983
3.284
2.249
1.00
16.71
A


ATOM
1092
CB
LEU
A
143
−21.222
2.995
0.957
1.00
16.66
A


ATOM
1093
CG
LEU
A
143
−21.938
2.027
0.009
1.00
14.82
A


ATOM
1094
CD1
LEU
A
143
−21.160
1.904
−1.280
1.00
11.61
A


ATOM
1095
CD2
LEU
A
143
−22.080
0.661
0.683
1.00
14.87
A


ATOM
1096
C
LEU
A
143
−21.186
4.210
3.152
1.00
16.35
A


ATOM
1097
O
LEU
A
143
−21.389
5.427
3.138
1.00
16.52
A


ATOM
1098
N
PRO
A
144
−20.266
3.639
3.954
1.00
16.35
A


ATOM
1099
CD
PRO
A
144
−20.060
2.183
4.085
1.00
15.80
A


ATOM
1100
CA
PRO
A
144
−19.410
4.356
4.896
1.00
14.08
A


ATOM
1101
CB
PRO
A
144
−19.073
3.278
5.904
1.00
15.09
A


ATOM
1102
CG
PRO
A
144
−18.889
2.090
5.023
1.00
14.40
A


ATOM
1103
C
PRO
A
144
−18.185
4.926
4.221
1.00
12.91
A


ATOM
1104
O
PRO
A
144
−17.054
4.622
4.612
1.00
11.28
A


ATOM
1105
N
MET
A
145
−18.419
5.753
3.204
1.00
11.90
A


ATOM
1106
CA
MET
A
145
−17.332
6.378
2.456
1.00
10.38
A


ATOM
1107
CB
MET
A
145
−17.820
6.851
1.083
1.00
10.21
A


ATOM
1108
CG
MET
A
145
−18.395
5.753
0.207
1.00
12.43
A


ATOM
1109
SD
MET
A
145
−17.224
4.412
−0.200
1.00
13.28
A


ATOM
1110
CE
MET
A
145
−17.618
3.241
1.092
1.00
14.67
A


ATOM
1111
C
MET
A
145
−16.819
7.566
3.229
1.00
9.66
A


ATOM
1112
O
MET
A
145
−17.605
8.384
3.689
1.00
11.74
A


ATOM
1113
N
HIS
A
146
−15.506
7.663
3.388
1.00
9.91
A


ATOM
1114
CA
HIS
A
146
−14.936
8.807
4.098
1.00
9.87
A


ATOM
1115
CB
HIS
A
146
−14.282
8.358
5.403
1.00
8.49
A


ATOM
1116
CG
HIS
A
146
−15.269
7.866
6.418
1.00
9.17
A


ATOM
1117
CD2
HIS
A
146
−15.920
8.512
7.415
1.00
8.75
A


ATOM
1118
ND1
HIS
A
146
−15.717
6.565
6.448
1.00
8.57
A


ATOM
1119
CE1
HIS
A
146
−16.599
6.427
7.422
1.00
7.28
A


ATOM
1120
NE2
HIS
A
146
−16.738
7.592
8.024
1.00
8.13
A


ATOM
1121
C
HIS
A
146
−13.946
9.581
3.233
1.00
8.88
A


ATOM
1122
O
HIS
A
146
−13.035
10.211
3.741
1.00
9.73
A


ATOM
1123
N
ILE
A
147
−14.158
9.542
1.923
1.00
10.01
A


ATOM
1124
CA
ILE
A
147
−13.315
10.234
0.954
1.00
9.28
A


ATOM
1125
CB
ILE
A
147
−11.833
9.773
1.028
1.00
9.29
A


ATOM
1126
CG2
ILE
A
147
−11.765
8.271
1.046
1.00
10.92
A


ATOM
1127
CG1
ILE
A
147
−11.054
10.332
−0.163
1.00
8.05
A


ATOM
1128
CD1
ILE
A
147
−9.542
10.152
−0.042
1.00
8.07
A


ATOM
1129
C
ILE
A
147
−13.862
9.957
−0.439
1.00
9.12
A


ATOM
1130
O
ILE
A
147
−14.181
8.812
−0.772
1.00
8.68
A


ATOM
1131
N
ARG
A
148
−13.993
11.011
−1.239
1.00
8.42
A


ATOM
1132
CA
ARG
A
148
−14.501
10.878
−2.607
1.00
10.40
A


ATOM
1133
CB
ARG
A
148
−15.975
11.295
−2.724
1.00
13.43
A


ATOM
1134
CG
ARG
A
148
−16.996
10.452
−1.996
1.00
19.51
A


ATOM
1135
CD
ARG
A
148
−17.301
10.971
−0.586
1.00
23.86
A


ATOM
1136
NE
ARG
A
148
−18.387
10.192
−0.002
1.00
27.00
A


ATOM
1137
CZ
ARG
A
148
−19.646
10.211
−0.439
1.00
29.04
A


ATOM
1138
NH1
ARG
A
148
−19.986
10.987
−1.461
1.00
29.76
A


ATOM
1139
NH2
ARG
A
148
−20.561
9.416
0.115
1.00
30.58
A


ATOM
1140
C
ARG
A
148
−13.729
11.790
−3.537
1.00
9.25
A


ATOM
1141
O
ARG
A
148
−13.368
12.896
−3.151
1.00
8.09
A


ATOM
1142
N
LEU
A
149
−13.497
11.346
−4.767
1.00
8.09
A


ATOM
1143
CA
LEU
A
149
−12.792
12.171
−5.741
1.00
8.72
A


ATOM
1144
CB
LEU
A
149
−11.347
11.686
−5.954
1.00
9.94
A


ATOM
1145
CG
LEU
A
149
−10.315
11.644
−4.821
1.00
11.17
A


ATOM
1146
CD1
LEU
A
149
−10.696
10.566
−3.809
1.00
13.78
A


ATOM
1147
CD2
LEU
A
149
−8.959
11.343
−5.398
1.00
11.11
A


ATOM
1148
C
LEU
A
149
−13.520
12.142
−7.088
1.00
9.46
A


ATOM
1149
O
LEU
A
149
−14.094
11.120
−7.486
1.00
8.08
A


ATOM
1150
N
SER
A
150
−13.491
13.272
−7.785
1.00
10.68
A


ATOM
1151
CA
SER
A
150
−14.108
13.391
−9.111
1.00
12.68
A


ATOM
1152
CB
SER
A
150
−15.379
14.239
−9.041
1.00
13.11
A


ATOM
1153
OG
SER
A
150
−15.921
14.443
−10.333
1.00
15.87
A


ATOM
1154
C
SER
A
150
−13.117
14.052
−10.076
1.00
12.26
A


ATOM
1155
O
SER
A
150
−12.519
15.077
−9.746
1.00
11.98
A


ATOM
1156
N
PHE
A
151
−12.979
13.506
−11.278
1.00
12.33
A


ATOM
1157
CA
PHE
A
151
−12.035
14.073
−12.231
1.00
14.30
A


ATOM
1158
CB
PHE
A
151
−11.174
12.934
−12.804
1.00
13.88
A


ATOM
1159
CG
PHE
A
151
−10.390
12.186
−11.754
1.00
14.26
A


ATOM
1160
CD1
PHE
A
151
−9.346
12.800
−11.068
1.00
13.10
A


ATOM
1161
CD2
PHE
A
151
−10.731
10.882
−11.413
1.00
14.46
A


ATOM
1162
CE1
PHE
A
151
−8.661
12.123
−10.055
1.00
12.62
A


ATOM
1163
CE2
PHE
A
151
−10.049
10.203
−10.402
1.00
14.91
A


ATOM
1164
CZ
PHE
A
151
−9.017
10.824
−9.723
1.00
13.40
A


ATOM
1165
C
PHE
A
151
−12.621
14.952
−13.361
1.00
14.36
A


ATOM
1166
O
PHE
A
151
−13.833
14.987
−13.570
1.00
13.80
A


ATOM
1167
N
ASN
A
152
−11.736
15.671
−14.053
1.00
15.86
A


ATOM
1168
CA
ASN
A
152
−12.095
16.544
−15.164
1.00
16.02
A


ATOM
1169
CB
ASN
A
152
−11.376
17.890
−15.097
1.00
18.74
A


ATOM
1170
CG
ASN
A
152
−11.397
18.498
−13.740
1.00
23.20
A


ATOM
1171
OD1
ASN
A
152
−10.753
19.522
−13.506
1.00
22.52
A


ATOM
1172
ND2
ASN
A
152
−12.145
17.877
−12.815
1.00
27.59
A


ATOM
1173
C
ASN
A
152
−11.596
15.925
−16.447
1.00
15.17
A


ATOM
1174
O
ASN
A
152
−10.651
15.141
−16.445
1.00
14.04
A


ATOM
1175
N
PRO
A
153
−12.199
16.315
−17.574
1.00
15.08
A


ATOM
1176
CD
PRO
A
153
−13.352
17.224
−17.726
1.00
15.27
A


ATOM
1177
CA
PRO
A
153
−11.778
15.791
−18.864
1.00
13.73
A


ATOM
1178
CB
PRO
A
153
−12.503
16.701
−19.839
1.00
12.37
A


ATOM
1179
CG
PRO
A
153
−13.791
16.948
−19.133
1.00
13.31
A


ATOM
1180
C
PRO
A
153
−10.259
15.885
−18.988
1.00
13.52
A


ATOM
1181
O
PRO
A
153
−9.603
14.920
−19.377
1.00
14.15
A


ATOM
1182
N
THR
A
154
−9.684
17.029
−18.629
1.00
12.52
A


ATOM
1183
CA
THR
A
154
−8.231
17.177
−18.747
1.00
11.18
A


ATOM
1184
CB
THR
A
154
−7.763
18.587
−18.357
1.00
9.17
A


ATOM
1185
OG1
THR
A
154
−8.404
19.554
−19.196
1.00
12.66
A


ATOM
1186
CG2
THR
A
154
−6.264
18.704
−18.522
1.00
6.13
A


ATOM
1187
C
THR
A
154
−7.477
16.194
−17.883
1.00
9.97
A


ATOM
1188
O
THR
A
154
−6.415
15.722
−18.263
1.00
9.78
A


ATOM
1189
N
GLN
A
155
−8.015
15.900
−16.709
1.00
10.79
A


ATOM
1190
CA
GLN
A
155
−7.342
14.980
−15.811
1.00
11.97
A


ATOM
1191
CB
GLN
A
155
−7.960
15.067
−14.435
1.00
10.76
A


ATOM
1192
CG
GLN
A
155
−7.894
16.455
−13.894
1.00
11.68
A


ATOM
1193
CD
GLN
A
155
−8.361
16.542
−12.473
1.00
11.87
A


ATOM
1194
OE1
GLN
A
155
−9.539
16.324
−12.169
1.00
9.48
A


ATOM
1195
NE2
GLN
A
155
−7.434
16.859
−11.579
1.00
12.87
A


ATOM
1196
C
GLN
A
155
−7.391
13.550
−16.312
1.00
13.34
A


ATOM
1197
O
GLN
A
155
−6.529
12.742
−15.978
1.00
15.38
A


ATOM
1198
N
LEU
A
156
−8.403
13.235
−17.112
1.00
13.70
A


ATOM
1199
CA
LEU
A
156
−8.532
11.904
−17.662
1.00
13.24
A


ATOM
1200
CB
LEU
A
156
−9.929
11.720
−18.238
1.00
10.39
A


ATOM
1201
CG
LEU
A
156
−11.052
11.820
−17.229
1.00
11.34
A


ATOM
1202
CD1
LEU
A
156
−12.388
11.688
−17.961
1.00
11.83
A


ATOM
1203
CD2
LEU
A
156
−10.913
10.747
−16.157
1.00
9.95
A


ATOM
1204
C
LEU
A
156
−7.490
11.667
−18.752
1.00
15.89
A


ATOM
1205
O
LEU
A
156
−7.306
10.543
−19.194
1.00
16.59
A


ATOM
1206
N
GLU
A
157
−6.824
12.733
−19.184
1.00
19.18
A


ATOM
1207
CA
GLU
A
157
−5.822
12.626
−20.225
1.00
23.89
A


ATOM
1208
CB
GLU
A
157
−5.570
13.984
−20.878
1.00
21.16
A


ATOM
1209
CG
GLU
A
157
−6.829
14.699
−21.299
1.00
21.05
A


ATOM
1210
CD
GLU
A
157
−6.534
15.965
−22.071
1.00
20.58
A


ATOM
1211
OE1
GLU
A
157
−5.525
16.629
−21.756
1.00
20.06
A


ATOM
1212
OE2
GLU
A
157
−7.311
16.302
−22.983
1.00
21.31
A


ATOM
1213
C
GLU
A
157
−4.522
12.088
−19.646
1.00
28.18
A


ATOM
1214
O
GLU
A
157
−3.538
11.905
−20.362
1.00
29.82
A


ATOM
1215
N
GLU
A
158
−4.517
11.835
−18.345
1.00
32.98
A


ATOM
1216
CA
GLU
A
158
−3.330
11.319
−17.681
1.00
38.78
A


ATOM
1217
CB
GLU
A
158
−2.996
12.164
−16.458
1.00
39.64
A


ATOM
1218
CG
GLU
A
158
−2.128
13.371
−16.796
1.00
44.59
A


ATOM
1219
CD
GLU
A
158
−0.665
13.000
−17.086
1.00
46.03
A


ATOM
1220
OE1
GLU
A
158
−0.419
11.941
−17.718
1.00
47.74
A


ATOM
1221
OE2
GLU
A
158
0.236
13.780
−16.692
1.00
45.88
A


ATOM
1222
C
GLU
A
158
−3.413
9.858
−17.275
1.00
42.20
A


ATOM
1223
O
GLU
A
158
−4.325
9.435
−16.551
1.00
42.84
A


ATOM
1224
N
GLN
A
159
−2.436
9.090
−17.750
1.00
45.59
A


ATOM
1225
CA
GLN
A
159
−2.349
7.664
−17.463
1.00
47.67
A


ATOM
1226
CB
GLN
A
159
−0.942
7.158
−17.786
1.00
48.76
A


ATOM
1227
CG
GLN
A
159
0.128
8.223
−17.656
1.00
50.01
A


ATOM
1228
CD
GLN
A
159
1.465
7.645
−17.258
1.00
51.72
A


ATOM
1229
OE1
GLN
A
159
1.926
6.648
−17.829
1.00
51.63
A


ATOM
1230
NE2
GLN
A
159
2.107
8.275
−16.275
1.00
52.16
A


ATOM
1231
C
GLN
A
159
−2.664
7.412
−16.001
1.00
48.11
A


ATOM
1232
O
GLN
A
159
−3.296
6.416
−15.659
1.00
48.73
A


ATOM
1233
N
CYS
A
160
−2.224
8.329
−15.144
1.00
48.60
A


ATOM
1234
CA
CYS
A
160
−2.454
8.209
−13.709
1.00
49.21
A


ATOM
1235
C
CYS
A
160
−3.262
9.371
−13.146
1.00
50.25
A


ATOM
1236
O
CYS
A
160
−3.207
9.640
−11.947
1.00
50.25
A


ATOM
1237
CB
CYS
A
160
−1.111
8.090
−12.970
1.00
48.31
A


ATOM
1238
SG
CYS
A
160
−0.706
6.398
−12.410
1.00
47.53
A


ATOM
1239
N
HIS
A
161
−4.010
10.052
−14.017
1.00
52.12
A


ATOM
1240
CA
HIS
A
161
−4.855
11.199
−13.631
1.00
53.87
A


ATOM
1241
CB
HIS
A
161
−6.062
10.722
−12.801
1.00
51.81
A


ATOM
1242
CG
HIS
A
161
−7.069
9.939
−13.586
1.00
50.36
A


ATOM
1243
CD2
HIS
A
161
−8.422
9.928
−13.542
1.00
49.28
A


ATOM
1244
ND1
HIS
A
161
−6.712
8.997
−14.530
1.00
50.71
A


ATOM
1245
CE1
HIS
A
161
−7.802
8.440
−15.030
1.00
49.63
A


ATOM
1246
NE2
HIS
A
161
−8.853
8.987
−14.446
1.00
49.13
A


ATOM
1247
C
HIS
A
161
−4.105
12.295
−12.856
1.00
55.61
A


ATOM
1248
O
HIS
A
161
−3.703
12.089
−11.701
1.00
55.42
A


ATOM
1249
N
ILE
A
162
−3.938
13.455
−13.504
1.00
57.43
A


ATOM
1250
CA
ILE
A
162
−3.253
14.631
−12.936
1.00
58.86
A


ATOM
1251
CB
ILE
A
162
−3.873
15.962
−13.480
1.00
58.80
A


ATOM
1252
CG2
ILE
A
162
−3.183
17.170
−12.812
1.00
58.56
A


ATOM
1253
CG1
ILE
A
162
−3.750
16.023
−15.012
1.00
57.83
A


ATOM
1254
CD1
ILE
A
162
−4.369
17.271
−15.642
1.00
55.94
A


ATOM
1255
C
ILE
A
162
−3.272
14.695
−11.400
1.00
59.78
A


ATOM
1256
OT1
ILE
A
162
−2.170
14.685
−10.788
1.00
59.36
A


ATOM
1257
OT2
ILE
A
162
−4.394
14.754
−10.837
1.00
60.08
A


ATOM
1258
CB
ASP
L
1
16.550
5.554
−25.535
1.00
16.37
L


ATOM
1259
CG
ASP
L
1
16.503
7.069
−25.599
1.00
19.69
L


ATOM
1260
OD1
ASP
L
1
16.752
7.733
−24.551
1.00
21.13
L


ATOM
1261
OD2
ASP
L
1
16.236
7.600
−26.702
1.00
18.80
L


ATOM
1262
C
ASP
L
1
15.914
3.511
−24.259
1.00
13.85
L


ATOM
1263
O
ASP
L
1
16.895
2.773
−24.238
1.00
15.08
L


ATOM
1264
N
ASP
L
1
17.141
5.276
−23.136
1.00
16.84
L


ATOM
1265
CA
ASP
L
1
16.101
5.010
−24.177
1.00
15.47
L


ATOM
1266
N
ILE
L
2
14.669
3.052
−24.335
1.00
11.38
L


ATOM
1267
CA
ILE
L
2
14.423
1.626
−24.435
1.00
8.80
L


ATOM
1268
CB
ILE
L
2
12.995
1.271
−23.982
1.00
8.68
L


ATOM
1269
CG2
ILE
L
2
12.795
−0.225
−24.067
1.00
6.83
L


ATOM
1270
CG1
ILE
L
2
12.771
1.771
−22.551
1.00
9.62
L


ATOM
1271
CD1
ILE
L
2
11.413
1.456
−21.968
1.00
8.82
L


ATOM
1272
C
ILE
L
2
14.643
1.214
−25.886
1.00
8.52
L


ATOM
1273
O
ILE
L
2
14.104
1.824
−26.816
1.00
4.81
L


ATOM
1274
N
VAL
L
3
15.474
0.195
−26.078
1.00
8.21
L


ATOM
1275
CA
VAL
L
3
15.778
−0.278
−27.422
1.00
7.79
L


ATOM
1276
CB
VAL
L
3
17.284
−0.578
−27.549
1.00
5.49
L


ATOM
1277
CG1
VAL
L
3
17.627
−0.990
−28.958
1.00
1.00
L


ATOM
1278
CG2
VAL
L
3
18.072
0.648
−27.135
1.00
5.03
L


ATOM
1279
C
VAL
L
3
14.959
−1.520
−27.769
1.00
9.17
L


ATOM
1280
O
VAL
L
3
15.054
−2.547
−27.098
1.00
11.84
L


ATOM
1281
N
MET
L
4
14.133
−1.417
−28.802
1.00
8.22
L


ATOM
1282
CA
MET
L
4
13.304
−2.543
−29.202
1.00
7.73
L


ATOM
1283
CB
MET
L
4
11.923
−2.055
−29.655
1.00
9.47
L


ATOM
1284
CG
MET
L
4
11.149
−1.225
−28.653
1.00
5.71
L


ATOM
1285
SD
MET
L
4
10.934
−2.041
−27.095
1.00
9.24
L


ATOM
1286
CE
MET
L
4
9.556
−3.115
−27.385
1.00
4.45
L


ATOM
1287
C
MET
L
4
13.978
−3.286
−30.350
1.00
8.02
L


ATOM
1288
O
MET
L
4
14.298
−2.685
−31.382
1.00
6.96
L


ATOM
1289
N
THR
L
5
14.196
−4.586
−30.173
1.00
8.30
L


ATOM
1290
CA
THR
L
5
14.835
−5.392
−31.210
1.00
8.27
L


ATOM
1291
CB
THR
L
5
16.100
−6.107
−30.656
1.00
8.90
L


ATOM
1292
OG1
THR
L
5
16.842
−5.200
−29.822
1.00
10.13
L


ATOM
1293
CG2
THR
L
5
16.993
−6.557
−31.794
1.00
7.36
L


ATOM
1294
C
THR
L
5
13.831
−6.423
−31.706
1.00
8.20
L


ATOM
1295
O
THR
L
5
13.344
−7.256
−30.940
1.00
7.90
L


ATOM
1296
N
GLN
L
6
13.484
−6.333
−32.984
1.00
9.47
L


ATOM
1297
CA
GLN
L
6
12.533
−7.268
−33.580
1.00
9.71
L


ATOM
1298
CB
GLN
L
6
11.683
−6.576
−34.635
1.00
9.96
L


ATOM
1299
CG
GLN
L
6
10.217
−6.389
−34.283
1.00
10.83
L


ATOM
1300
CD
GLN
L
6
9.560
−5.379
−35.227
1.00
12.71
L


ATOM
1301
OE1
GLN
L
6
9.754
−4.156
−35.100
1.00
11.89
L


ATOM
1302
NE2
GLN
L
6
8.812
−5.888
−36.204
1.00
11.00
L


ATOM
1303
C
GLN
L
6
13.283
−8.409
−34.223
1.00
9.95
L


ATOM
1304
O
GLN
L
6
14.476
−8.311
−34.513
1.00
9.91
L


ATOM
1305
N
SER
L
7
12.580
−9.501
−34.460
1.00
10.84
L


ATOM
1306
CA
SER
L
7
13.234
−10.652
−35.045
1.00
10.80
L


ATOM
1307
CB
SER
L
7
14.081
−11.315
−33.982
1.00
9.99
L


ATOM
1308
OG
SER
L
7
15.047
−12.144
−34.575
1.00
16.72
L


ATOM
1309
C
SER
L
7
12.191
−11.624
−35.554
1.00
10.08
L


ATOM
1310
O
SER
L
7
11.206
−11.886
−34.876
1.00
12.81
L


ATOM
1311
N
PRO
L
8
12.365
−12.131
−36.779
1.00
9.04
L


ATOM
1312
CD
PRO
L
8
11.571
−13.254
−37.308
1.00
7.85
L


ATOM
1313
CA
PRO
L
8
13.490
−11.816
−37.668
1.00
9.77
L


ATOM
1314
CB
PRO
L
8
13.490
−12.991
−38.640
1.00
8.02
L


ATOM
1315
CG
PRO
L
8
12.033
−13.328
−38.732
1.00
8.29
L


ATOM
1316
C
PRO
L
8
13.241
−10.474
−38.377
1.00
10.57
L


ATOM
1317
O
PRO
L
8
12.140
−9.923
−38.302
1.00
10.48
L


ATOM
1318
N
SER
L
9
14.251
−9.939
−39.052
1.00
11.09
L


ATOM
1319
CA
SER
L
9
14.070
−8.667
−39.757
1.00
13.69
L


ATOM
1320
CB
SER
L
9
15.426
−8.033
−40.090
1.00
15.41
L


ATOM
1321
OG
SER
L
9
16.465
−9.001
−40.081
1.00
20.93
L


ATOM
1322
C
SER
L
9
13.231
−8.841
−41.031
1.00
13.61
L


ATOM
1323
O
SER
L
9
12.517
−7.923
−41.456
1.00
11.42
L


ATOM
1324
N
SER
L
10
13.316
−10.024
−41.636
1.00
14.50
L


ATOM
1325
CA
SER
L
10
12.531
−10.330
−42.833
1.00
16.25
L


ATOM
1326
CB
SER
L
10
13.280
−9.938
−44.104
1.00
16.02
L


ATOM
1327
OG
SER
L
10
14.253
−10.900
−44.437
1.00
19.67
L


ATOM
1328
C
SER
L
10
12.202
−11.817
−42.850
1.00
15.53
L


ATOM
1329
O
SER
L
10
13.002
−12.648
−42.426
1.00
15.73
L


ATOM
1330
N
LEU
L
11
11.011
−12.143
−43.329
1.00
15.59
L


ATOM
1331
CA
LEU
L
11
10.571
−13.524
−43.361
1.00
16.29
L


ATOM
1332
CB
LEU
L
11
9.730
−13.789
−42.120
1.00
16.99
L


ATOM
1333
CG
LEU
L
11
9.261
−15.225
−41.963
1.00
18.29
L


ATOM
1334
CD1
LEU
L
11
10.338
−15.994
−41.199
1.00
19.78
L


ATOM
1335
CD2
LEU
L
11
7.929
−15.276
−41.212
1.00
17.06
L


ATOM
1336
C
LEU
L
11
9.748
−13.852
−44.609
1.00
17.00
L


ATOM
1337
O
LEU
L
11
9.089
−12.978
−45.171
1.00
19.02
L


ATOM
1338
N
SER
L
12
9.786
−15.109
−45.043
1.00
17.38
L


ATOM
1339
CA
SER
L
12
8.999
−15.533
−46.200
1.00
16.83
L


ATOM
1340
CB
SER
L
12
9.893
−15.852
−47.395
1.00
16.19
L


ATOM
1341
OG
SER
L
12
10.483
−14.670
−47.897
1.00
18.96
L


ATOM
1342
C
SER
L
12
8.229
−16.772
−45.792
1.00
15.74
L


ATOM
1343
O
SER
L
12
8.820
−17.778
−45.395
1.00
16.18
L


ATOM
1344
N
ALA
L
13
6.907
−16.689
−45.893
1.00
14.50
L


ATOM
1345
CA
ALA
L
13
6.040
−17.790
−45.510
1.00
13.88
L


ATOM
1346
CB
ALA
L
13
5.435
−17.524
−44.142
1.00
11.70
L


ATOM
1347
C
ALA
L
13
4.941
−18.025
−46.520
1.00
14.84
L


ATOM
1348
O
ALA
L
13
4.414
−17.080
−47.098
1.00
15.89
L


ATOM
1349
N
SER
L
14
4.590
−19.289
−46.726
1.00
16.55
L


ATOM
1350
CA
SER
L
14
3.548
−19.653
−47.686
1.00
18.52
L


ATOM
1351
CB
SER
L
14
3.584
−21.161
−47.953
1.00
21.34
L


ATOM
1352
OG
SER
L
14
4.906
−21.598
−48.266
1.00
25.96
L


ATOM
1353
C
SER
L
14
2.187
−19.280
−47.146
1.00
17.08
L


ATOM
1354
O
SER
L
14
1.926
−19.420
−45.954
1.00
15.37
L


ATOM
1355
N
VAL
L
15
1.321
−18.795
−48.025
1.00
18.37
L


ATOM
1356
CA
VAL
L
15
−0.022
−18.426
−47.602
1.00
20.11
L


ATOM
1357
CB
VAL
L
15
−0.895
−17.953
−48.814
1.00
19.65
L


ATOM
1358
CG1
VAL
L
15
−0.468
−18.683
−50.077
1.00
21.07
L


ATOM
1359
CG2
VAL
L
15
−2.386
−18.191
−48.526
1.00
16.68
L


ATOM
1360
C
VAL
L
15
−0.660
−19.631
−46.912
1.00
20.75
L


ATOM
1361
O
VAL
L
15
−0.853
−20.677
−47.520
1.00
21.60
L


ATOM
1362
N
GLY
L
16
−0.957
−19.483
−45.628
1.00
21.09
L


ATOM
1363
CA
GLY
L
16
−1.554
−20.579
−44.901
1.00
22.33
L


ATOM
1364
C
GLY
L
16
−0.814
−20.944
−43.632
1.00
23.59
L


ATOM
1365
O
GLY
L
16
−1.451
−21.194
−42.616
1.00
25.28
L


ATOM
1366
N
ASP
L
17
0.514
−20.979
−43.657
1.00
24.99
L


ATOM
1367
CA
ASP
L
17
1.230
−21.341
−42.436
1.00
27.99
L


ATOM
1368
CB
ASP
L
17
2.693
−21.717
−42.723
1.00
28.83
L


ATOM
1369
CG
ASP
L
17
3.458
−20.625
−43.424
1.00
29.50
L


ATOM
1370
OD1
ASP
L
17
3.262
−19.441
−43.048
1.00
31.11
L


ATOM
1371
OD2
ASP
L
17
4.271
−20.954
−44.329
1.00
27.86
L


ATOM
1372
C
ASP
L
17
1.160
−20.221
−41.407
1.00
29.07
L


ATOM
1373
O
ASP
L
17
0.811
−19.091
−41.747
1.00
30.22
L


ATOM
1374
N
ARG
L
18
1.473
−20.540
−40.150
1.00
29.29
L


ATOM
1375
CA
ARG
L
18
1.428
−19.550
−39.085
1.00
28.54
L


ATOM
1376
CB
ARG
L
18
0.964
−20.185
−37.758
1.00
30.31
L


ATOM
1377
CG
ARG
L
18
2.046
−20.954
−36.997
1.00
33.86
L


ATOM
1378
CD
ARG
L
18
1.515
−21.703
−35.764
1.00
35.75
L


ATOM
1379
NE
ARG
L
18
0.691
−20.880
−34.879
1.00
38.27
L


ATOM
1380
CZ
ARG
L
18
−0.645
−20.869
−34.882
1.00
39.93
L


ATOM
1381
NH1
ARG
L
18
−1.317
−21.642
−35.726
1.00
39.27
L


ATOM
1382
NH2
ARG
L
18
−1.316
−20.085
−34.037
1.00
40.51
L


ATOM
1383
C
ARG
L
18
2.814
−18.946
−38.934
1.00
27.76
L


ATOM
1384
O
ARG
L
18
3.829
−19.658
−38.958
1.00
27.29
L


ATOM
1385
N
VAL
L
19
2.858
−17.623
−38.810
1.00
26.27
L


ATOM
1386
CA
VAL
L
19
4.124
−16.924
−38.655
1.00
24.20
L


ATOM
1387
CB
VAL
L
19
4.290
−15.843
−39.743
1.00
24.36
L


ATOM
1388
CG1
VAL
L
19
3.975
−16.440
−41.112
1.00
25.14
L


ATOM
1389
CG2
VAL
L
19
3.387
−14.671
−39.464
1.00
26.02
L


ATOM
1390
C
VAL
L
19
4.209
−16.292
−37.278
1.00
22.08
L


ATOM
1391
O
VAL
L
19
3.190
−15.978
−36.676
1.00
20.97
L


ATOM
1392
N
THR
L
20
5.432
−16.132
−36.782
1.00
21.47
L


ATOM
1393
CA
THR
L
20
5.671
−15.541
−35.469
1.00
19.88
L


ATOM
1394
CB
THR
L
20
5.991
−16.619
−34.422
1.00
17.86
L


ATOM
1395
OG1
THR
L
20
4.866
−17.480
−34.259
1.00
18.26
L


ATOM
1396
CG2
THR
L
20
6.324
−15.994
−33.100
1.00
16.28
L


ATOM
1397
C
THR
L
20
6.847
−14.575
−35.499
1.00
20.30
L


ATOM
1398
O
THR
L
20
7.946
−14.931
−35.918
1.00
20.29
L


ATOM
1399
N
ILE
L
21
6.610
−13.351
−35.055
1.00
20.44
L


ATOM
1400
CA
ILE
L
21
7.658
−12.349
−35.000
1.00
20.12
L


ATOM
1401
CB
ILE
L
21
7.236
−11.072
−35.736
1.00
20.69
L


ATOM
1402
CG2
ILE
L
21
8.406
−10.088
−35.799
1.00
18.90
L


ATOM
1403
CG1
ILE
L
21
6.759
−11.441
−37.142
1.00
21.95
L


ATOM
1404
CD1
ILE
L
21
6.285
−10.252
−37.972
1.00
22.52
L


ATOM
1405
C
ILE
L
21
7.904
−12.024
−33.528
1.00
20.23
L


ATOM
1406
O
ILE
L
21
6.961
−11.872
−32.735
1.00
19.59
L


ATOM
1407
N
THR
L
22
9.174
−11.915
−33.169
1.00
19.11
L


ATOM
1408
CA
THR
L
22
9.534
−11.605
−31.801
1.00
19.72
L


ATOM
1409
CB
THR
L
22
10.651
−12.529
−31.291
1.00
19.77
L


ATOM
1410
OG1
THR
L
22
10.343
−13.878
−31.647
1.00
20.92
L


ATOM
1411
CG2
THR
L
22
10.773
−12.442
−29.770
1.00
17.04
L


ATOM
1412
C
THR
L
22
10.009
−10.172
−31.690
1.00
20.10
L


ATOM
1413
O
THR
L
22
10.498
−9.590
−32.660
1.00
19.87
L


ATOM
1414
N
CYS
L
23
9.848
−9.617
−30.493
1.00
20.03
L


ATOM
1415
CA
CYS
L
23
10.255
−8.257
−30.192
1.00
20.14
L


ATOM
1416
C
CYS
L
23
10.753
−8.272
−28.748
1.00
20.68
L


ATOM
1417
O
CYS
L
23
10.063
−8.777
−27.861
1.00
20.07
L


ATOM
1418
CB
CYS
L
23
9.050
−7.327
−30.361
1.00
19.95
L


ATOM
1419
SG
CYS
L
23
9.273
−5.579
−29.906
1.00
24.16
L


ATOM
1420
N
ARG
L
24
11.972
−7.776
−28.521
1.00
20.89
L


ATOM
1421
CA
ARG
L
24
12.538
−7.736
−27.172
1.00
19.57
L


ATOM
1422
CB
ARG
L
24
13.771
−8.629
−27.042
1.00
21.13
L


ATOM
1423
CG
ARG
L
24
13.464
−10.092
−27.137
1.00
23.44
L


ATOM
1424
CD
ARG
L
24
14.727
−10.917
−27.090
1.00
26.37
L


ATOM
1425
NE
ARG
L
24
14.457
−12.270
−27.558
1.00
30.08
L


ATOM
1426
CZ
ARG
L
24
14.080
−12.559
−28.794
1.00
32.01
L


ATOM
1427
NH1
ARG
L
24
13.935
−11.583
−29.695
1.00
34.19
L


ATOM
1428
NH2
ARG
L
24
13.831
−13.819
−29.112
1.00
32.69
L


ATOM
1429
C
ARG
L
24
12.927
−6.335
−26.809
1.00
18.40
L


ATOM
1430
O
ARG
L
24
13.490
−5.615
−27.629
1.00
18.93
L


ATOM
1431
N
ALA
L
25
12.628
−5.958
−25.568
1.00
17.14
L


ATOM
1432
CA
ALA
L
25
12.925
−4.624
−25.063
1.00
16.03
L


ATOM
1433
CB
ALA
L
25
11.804
−4.169
−24.158
1.00
16.46
L


ATOM
1434
C
ALA
L
25
14.249
−4.594
−24.317
1.00
15.36
L


ATOM
1435
O
ALA
L
25
14.662
−5.597
−23.742
1.00
14.07
L


ATOM
1436
N
SER
L
26
14.913
−3.442
−24.343
1.00
16.19
L


ATOM
1437
CA
SER
L
26
16.195
−3.277
−23.668
1.00
16.76
L


ATOM
1438
CB
SER
L
26
16.888
−1.996
−24.132
1.00
17.23
L


ATOM
1439
OG
SER
L
26
16.373
−0.865
−23.464
1.00
20.63
L


ATOM
1440
C
SER
L
26
16.003
−3.246
−22.149
1.00
16.15
L


ATOM
1441
O
SER
L
26
16.967
−3.188
−21.394
1.00
15.95
L


ATOM
1442
N
GLN
L
27
14.749
−3.260
−21.711
1.00
15.84
L


ATOM
1443
CA
GLN
L
27
14.416
−3.291
−20.289
1.00
14.82
L


ATOM
1444
CB
GLN
L
27
14.690
−1.950
−19.615
1.00
15.42
L


ATOM
1445
CG
GLN
L
27
13.719
−0.864
−19.989
1.00
17.28
L


ATOM
1446
CD
GLN
L
27
13.715
0.267
−18.991
1.00
19.54
L


ATOM
1447
OE1
GLN
L
27
14.671
1.046
−18.916
1.00
19.13
L


ATOM
1448
NE2
GLN
L
27
12.647
0.345
−18.184
1.00
21.52
L


ATOM
1449
C
GLN
L
27
12.933
−3.625
−20.170
1.00
13.71
L


ATOM
1450
O
GLN
L
27
12.190
−3.547
−21.152
1.00
11.47
L


ATOM
1451
N
GLY
L
28
12.507
−3.998
−18.970
1.00
12.79
L


ATOM
1452
CA
GLY
L
28
11.116
−4.345
−18.765
1.00
11.73
L


ATOM
1453
C
GLY
L
28
10.230
−3.167
−19.092
1.00
12.33
L


ATOM
1454
O
GLY
L
28
10.534
−2.029
−18.728
1.00
12.44
L


ATOM
1455
N
ILE
L
29
9.136
−3.437
−19.792
1.00
11.90
L


ATOM
1456
CA
ILE
L
29
8.206
−2.389
−20.166
1.00
12.68
L


ATOM
1457
CB
ILE
L
29
8.252
−2.078
−21.664
1.00
11.70
L


ATOM
1458
CG2
ILE
L
29
9.607
−1.483
−22.023
1.00
12.24
L


ATOM
1459
CG1
ILE
L
29
7.948
−3.348
−22.465
1.00
12.26
L


ATOM
1460
CD1
ILE
L
29
7.626
−3.110
−23.937
1.00
10.24
L


ATOM
1461
C
ILE
L
29
6.800
−2.808
−19.828
1.00
14.29
L


ATOM
1462
O
ILE
L
29
5.833
−2.365
−20.458
1.00
14.88
L


ATOM
1463
N
SER
L
30
6.686
−3.681
−18.839
1.00
15.26
L


ATOM
1464
CA
SER
L
30
5.373
−4.129
−18.422
1.00
16.96
L


ATOM
1465
CB
SER
L
30
4.545
−2.903
−18.005
1.00
17.33
L


ATOM
1466
OG
SER
L
30
3.175
−3.203
−17.824
1.00
18.85
L


ATOM
1467
C
SER
L
30
4.721
−4.845
−19.600
1.00
17.57
L


ATOM
1468
O
SER
L
30
5.328
−5.689
−20.258
1.00
18.80
L


ATOM
1469
N
SER
L
31
3.476
−4.492
−19.862
1.00
16.56
L


ATOM
1470
CA
SER
L
31
2.737
−5.081
−20.956
1.00
16.37
L


ATOM
1471
CB
SER
L
31
1.472
−5.751
−20.415
1.00
16.56
L


ATOM
1472
OG
SER
L
31
0.798
−4.889
−19.505
1.00
17.23
L


ATOM
1473
C
SER
L
31
2.375
−3.971
−21.939
1.00
15.72
L


ATOM
1474
O
SER
L
31
1.424
−4.085
−22.727
1.00
14.38
L


ATOM
1475
N
ARG
L
32
3.137
−2.886
−21.882
1.00
14.57
L


ATOM
1476
CA
ARG
L
32
2.869
−1.761
−22.763
1.00
12.87
L


ATOM
1477
CB
ARG
L
32
3.232
−0.432
−22.077
1.00
12.78
L


ATOM
1478
CG
ARG
L
32
2.545
−0.190
−20.731
1.00
13.17
L


ATOM
1479
CD
ARG
L
32
2.896
1.199
−20.286
1.00
16.26
L


ATOM
1480
NE
ARG
L
32
2.682
1.484
−18.877
1.00
20.43
L


ATOM
1481
CZ
ARG
L
32
1.751
2.314
−18.409
1.00
24.20
L


ATOM
1482
NH1
ARG
L
32
0.931
2.937
−19.255
1.00
23.63
L


ATOM
1483
NH2
ARG
L
32
1.669
2.550
−17.095
1.00
21.89
L


ATOM
1484
C
ARG
L
32
3.624
−1.888
−24.086
1.00
10.58
L


ATOM
1485
O
ARG
L
32
4.626
−1.222
−24.312
1.00
11.04
L


ATOM
1486
N
LEU
L
33
3.135
−2.759
−24.950
1.00
7.55
L


ATOM
1487
CA
LEU
L
33
3.728
−2.953
−26.243
1.00
5.79
L


ATOM
1488
CB
LEU
L
33
4.558
−4.233
−26.293
1.00
6.51
L


ATOM
1489
CG
LEU
L
33
5.261
−4.460
−27.669
1.00
6.68
L


ATOM
1490
CD1
LEU
L
33
6.728
−4.722
−27.445
1.00
5.42
L


ATOM
1491
CD2
LEU
L
33
4.616
−5.605
−28.430
1.00
3.57
L


ATOM
1492
C
LEU
L
33
2.613
−3.045
−27.273
1.00
4.13
L


ATOM
1493
O
LEU
L
33
1.559
−3.640
−27.011
1.00
3.72
L


ATOM
1494
N
ALA
L
34
2.857
−2.480
−28.454
1.00
3.03
L


ATOM
1495
CA
ALA
L
34
1.857
−2.507
−29.521
1.00
3.10
L


ATOM
1496
CB
ALA
L
34
1.245
−1.114
−29.712
1.00
3.61
L


ATOM
1497
C
ALA
L
34
2.455
−2.991
−30.820
1.00
2.38
L


ATOM
1498
O
ALA
L
34
3.662
−2.950
−31.000
1.00
2.65
L


ATOM
1499
N
TRP
L
35
1.594
−3.455
−31.715
1.00
3.03
L


ATOM
1500
CA
TRP
L
35
2.016
−3.967
−33.007
1.00
4.01
L


ATOM
1501
CB
TRP
L
35
1.714
−5.459
−33.112
1.00
5.67
L


ATOM
1502
CG
TRP
L
35
2.557
−6.314
−32.225
1.00
7.10
L


ATOM
1503
CD2
TRP
L
35
3.882
−6.790
−32.507
1.00
6.96
L


ATOM
1504
CE2
TRP
L
35
4.308
−7.525
−31.380
1.00
7.48
L


ATOM
1505
CE3
TRP
L
35
4.751
−6.663
−33.604
1.00
6.37
L


ATOM
1506
CD1
TRP
L
35
2.242
−6.768
−30.973
1.00
5.81
L


ATOM
1507
NE1
TRP
L
35
3.287
−7.493
−30.459
1.00
7.49
L


ATOM
1508
CZ2
TRP
L
35
5.581
−8.140
−31.318
1.00
6.10
L


ATOM
1509
CZ3
TRP
L
35
6.012
−7.271
−33.541
1.00
5.88
L


ATOM
1510
CH2
TRP
L
35
6.411
−8.002
−32.403
1.00
5.71
L


ATOM
1511
C
TRP
L
35
1.310
−3.251
−34.147
1.00
4.05
L


ATOM
1512
O
TRP
L
35
0.074
−3.220
−34.209
1.00
2.57
L


ATOM
1513
N
TYR
L
36
2.099
−2.693
−35.055
1.00
2.93
L


ATOM
1514
CA
TYR
L
36
1.522
−1.981
−36.169
1.00
3.86
L


ATOM
1515
CB
TYR
L
36
2.035
−0.544
−36.209
1.00
1.42
L


ATOM
1516
CG
TYR
L
36
1.701
0.264
−34.970
1.00
2.49
L


ATOM
1517
CD1
TYR
L
36
0.469
0.885
−34.829
1.00
1.00
L


ATOM
1518
CE1
TYR
L
36
0.178
1.650
−33.715
1.00
1.00
L


ATOM
1519
CD2
TYR
L
36
2.635
0.427
−33.944
1.00
2.52
L


ATOM
1520
CE2
TYR
L
36
2.342
1.196
−32.819
1.00
1.93
L


ATOM
1521
CZ
TYR
L
36
1.109
1.807
−32.722
1.00
1.00
L


ATOM
1522
OH
TYR
L
36
0.838
2.597
−31.632
1.00
1.00
L


ATOM
1523
C
TYR
L
36
1.851
−2.671
−37.464
1.00
5.39
L


ATOM
1524
O
TYR
L
36
2.844
−3.388
−37.575
1.00
5.41
L


ATOM
1525
N
GLN
L
37
1.002
−2.455
−38.453
1.00
7.83
L


ATOM
1526
CA
GLN
L
37
1.207
−3.054
−39.754
1.00
9.39
L


ATOM
1527
CB
GLN
L
37
0.046
−3.980
−40.097
1.00
11.00
L


ATOM
1528
CG
GLN
L
37
0.086
−4.527
−41.501
1.00
9.81
L


ATOM
1529
CD
GLN
L
37
−1.129
−5.339
−41.803
1.00
10.26
L


ATOM
1530
OE1
GLN
L
37
−2.238
−4.815
−41.847
1.00
12.94
L


ATOM
1531
NE2
GLN
L
37
−0.941
−6.637
−41.983
1.00
13.63
L


ATOM
1532
C
GLN
L
37
1.274
−1.933
−40.766
1.00
10.97
L


ATOM
1533
O
GLN
L
37
0.415
−1.056
−40.787
1.00
11.76
L


ATOM
1534
N
GLN
L
38
2.296
−1.966
−41.609
1.00
13.25
L


ATOM
1535
CA
GLN
L
38
2.443
−0.946
−42.622
1.00
15.72
L


ATOM
1536
CB
GLN
L
38
3.562
0.023
−42.258
1.00
16.17
L


ATOM
1537
CG
GLN
L
38
3.619
1.227
−43.194
1.00
17.87
L


ATOM
1538
CD
GLN
L
38
4.854
2.054
−43.000
1.00
18.58
L


ATOM
1539
OE1
GLN
L
38
4.887
3.241
−43.360
1.00
18.70
L


ATOM
1540
NE2
GLN
L
38
5.896
1.436
−42.437
1.00
18.33
L


ATOM
1541
C
GLN
L
38
2.739
−1.530
−43.991
1.00
17.75
L


ATOM
1542
O
GLN
L
38
3.618
−2.372
−44.144
1.00
17.47
L


ATOM
1543
N
LYS
L
39
2.003
−1.051
−44.984
1.00
19.94
L


ATOM
1544
CA
LYS
L
39
2.172
−1.466
−46.360
1.00
20.60
L


ATOM
1545
CB
LYS
L
39
0.843
−1.990
−46.911
1.00
19.44
L


ATOM
1546
CG
LYS
L
39
0.372
−3.242
−46.214
1.00
18.77
L


ATOM
1547
CD
LYS
L
39
−1.043
−3.641
−46.559
1.00
18.38
L


ATOM
1548
CE
LYS
L
39
−1.314
−5.039
−45.989
1.00
19.75
L


ATOM
1549
NZ
LYS
L
39
−2.760
−5.437
−45.970
1.00
19.42
L


ATOM
1550
C
LYS
L
39
2.615
−0.225
−47.142
1.00
23.17
L


ATOM
1551
O
LYS
L
39
2.320
0.916
−46.762
1.00
22.18
L


ATOM
1552
N
PRO
L
40
3.319
−0.440
−48.258
1.00
25.17
L


ATOM
1553
CD
PRO
L
40
3.543
−1.778
−48.829
1.00
25.97
L


ATOM
1554
CA
PRO
L
40
3.846
0.591
−49.157
1.00
25.55
L


ATOM
1555
CB
PRO
L
40
4.172
−0.194
−50.417
1.00
25.75
L


ATOM
1556
CG
PRO
L
40
4.583
−1.491
−49.863
1.00
26.38
L


ATOM
1557
C
PRO
L
40
2.863
1.705
−49.444
1.00
25.25
L


ATOM
1558
O
PRO
L
40
1.775
1.467
−49.973
1.00
25.17
L


ATOM
1559
N
GLY
L
41
3.262
2.923
−49.101
1.00
24.69
L


ATOM
1560
CA
GLY
L
41
2.419
4.082
−49.343
1.00
23.52
L


ATOM
1561
C
GLY
L
41
1.056
4.091
−48.665
1.00
21.83
L


ATOM
1562
O
GLY
L
41
0.195
4.900
−49.004
1.00
20.85
L


ATOM
1563
N
LYS
L
42
0.848
3.200
−47.708
1.00
21.05
L


ATOM
1564
CA
LYS
L
42
−0.418
3.159
−47.017
1.00
20.64
L


ATOM
1565
CB
LYS
L
42
−1.022
1.758
−47.112
1.00
23.78
L


ATOM
1566
CG
LYS
L
42
−1.251
1.276
−48.549
1.00
27.37
L


ATOM
1567
CD
LYS
L
42
−1.686
−0.178
−48.582
1.00
29.55
L


ATOM
1568
CE
LYS
L
42
−1.463
−0.807
−49.960
1.00
31.53
L


ATOM
1569
NZ
LYS
L
42
−1.924
−2.247
−50.023
1.00
30.21
L


ATOM
1570
C
LYS
L
42
−0.235
3.567
−45.561
1.00
19.67
L


ATOM
1571
O
LYS
L
42
0.888
3.642
−45.057
1.00
22.24
L


ATOM
1572
N
ALA
L
43
−1.353
3.831
−44.895
1.00
17.35
L


ATOM
1573
CA
ALA
L
43
−1.379
4.238
−43.500
1.00
14.73
L


ATOM
1574
CB
ALA
L
43
−2.707
4.896
−43.197
1.00
13.07
L


ATOM
1575
C
ALA
L
43
−1.166
3.061
−42.561
1.00
13.46
L


ATOM
1576
O
ALA
L
43
−1.844
2.044
−42.655
1.00
13.73
L


ATOM
1577
N
PRO
L
44
−0.206
3.177
−41.639
1.00
11.50
L


ATOM
1578
CD
PRO
L
44
0.860
4.180
−41.480
1.00
9.68
L


ATOM
1579
CA
PRO
L
44
−0.007
2.050
−40.730
1.00
11.04
L


ATOM
1580
CB
PRO
L
44
1.101
2.552
−39.805
1.00
10.36
L


ATOM
1581
CG
PRO
L
44
1.920
3.409
−40.739
1.00
9.88
L


ATOM
1582
C
PRO
L
44
−1.307
1.721
−39.975
1.00
10.49
L


ATOM
1583
O
PRO
L
44
−2.161
2.583
−39.759
1.00
9.88
L


ATOM
1584
N
LYS
L
45
−1.453
0.459
−39.599
1.00
11.44
L


ATOM
1585
CA
LYS
L
45
−2.631
−0.005
−38.881
1.00
12.22
L


ATOM
1586
CB
LYS
L
45
−3.368
−1.063
−39.698
1.00
15.28
L


ATOM
1587
CG
LYS
L
45
−4.045
−0.532
−40.955
1.00
18.72
L


ATOM
1588
CD
LYS
L
45
−4.689
−1.651
−41.789
1.00
23.99
L


ATOM
1589
CE
LYS
L
45
−5.758
−2.410
−40.990
1.00
28.70
L


ATOM
1590
NZ
LYS
L
45
−6.539
−3.436
−41.781
1.00
30.44
L


ATOM
1591
C
LYS
L
45
−2.243
−0.599
−37.542
1.00
10.66
L


ATOM
1592
O
LYS
L
45
−1.270
−1.343
−37.433
1.00
11.06
L


ATOM
1593
N
LEU
L
46
−3.011
−0.271
−36.517
1.00
9.86
L


ATOM
1594
CA
LEU
L
46
−2.738
−0.780
−35.185
1.00
8.87
L


ATOM
1595
CB
LEU
L
46
−3.336
0.180
−34.147
1.00
9.27
L


ATOM
1596
CG
LEU
L
46
−3.140
0.020
−32.631
1.00
9.63
L


ATOM
1597
CD1
LEU
L
46
−4.354
−0.644
−32.037
1.00
9.45
L


ATOM
1598
CD2
LEU
L
46
−1.857
−0.768
−32.330
1.00
10.10
L


ATOM
1599
C
LEU
L
46
−3.382
−2.150
−35.103
1.00
8.10
L


ATOM
1600
O
LEU
L
46
−4.573
−2.287
−35.357
1.00
8.98
L


ATOM
1601
N
LEU
L
47
−2.593
−3.160
−34.757
1.00
7.67
L


ATOM
1602
CA
LEU
L
47
−3.109
−4.525
−34.662
1.00
6.84
L


ATOM
1603
CB
LEU
L
47
−2.148
−5.527
−35.320
1.00
5.42
L


ATOM
1604
CG
LEU
L
47
−1.750
−5.328
−36.793
1.00
6.34
L


ATOM
1605
CD1
LEU
L
47
−0.631
−6.286
−37.139
1.00
3.93
L


ATOM
1606
CD2
LEU
L
47
−2.960
−5.530
−37.695
1.00
5.28
L


ATOM
1607
C
LEU
L
47
−3.298
−4.949
−33.224
1.00
6.82
L


ATOM
1608
O
LEU
L
47
−4.347
−5.457
−32.860
1.00
6.11
L


ATOM
1609
N
ILE
L
48
−2.263
−4.732
−32.417
1.00
7.58
L


ATOM
1610
CA
ILE
L
48
−2.261
−5.145
−31.015
1.00
7.30
L


ATOM
1611
CB
ILE
L
48
−1.351
−6.420
−30.815
1.00
6.26
L


ATOM
1612
CG2
ILE
L
48
−1.227
−6.758
−29.342
1.00
2.73
L


ATOM
1613
CG1
ILE
L
48
−1.879
−7.611
−31.641
1.00
3.91
L


ATOM
1614
CD1
ILE
L
48
−3.265
−8.085
−31.244
1.00
5.88
L


ATOM
1615
C
ILE
L
48
−1.709
−4.047
−30.119
1.00
9.05
L


ATOM
1616
O
ILE
L
48
−0.800
−3.313
−30.513
1.00
9.25
L


ATOM
1617
N
TYR
L
49
−2.267
−3.930
−28.918
1.00
9.07
L


ATOM
1618
CA
TYR
L
49
−1.796
−2.955
−27.936
1.00
7.79
L


ATOM
1619
CB
TYR
L
49
−2.663
−1.698
−27.928
1.00
8.17
L


ATOM
1620
CG
TYR
L
49
−4.122
−1.920
−27.631
1.00
8.50
L


ATOM
1621
CD1
TYR
L
49
−4.986
−2.388
−28.610
1.00
8.58
L


ATOM
1622
CE1
TYR
L
49
−6.343
−2.525
−28.351
1.00
9.02
L


ATOM
1623
CD2
TYR
L
49
−4.650
−1.604
−26.383
1.00
6.91
L


ATOM
1624
CE2
TYR
L
49
−6.000
−1.739
−26.117
1.00
5.94
L


ATOM
1625
CZ
TYR
L
49
−6.843
−2.194
−27.102
1.00
7.73
L


ATOM
1626
OH
TYR
L
49
−8.196
−2.299
−26.855
1.00
8.78
L


ATOM
1627
C
TYR
L
49
−1.884
−3.647
−26.586
1.00
8.45
L


ATOM
1628
O
TYR
L
49
−2.469
−4.723
−26.476
1.00
7.21
L


ATOM
1629
N
ALA
L
50
−1.306
−3.042
−25.556
1.00
8.94
L


ATOM
1630
CA
ALA
L
50
−1.332
−3.661
−24.243
1.00
10.42
L


ATOM
1631
CB
ALA
L
50
−2.751
−3.633
−23.674
1.00
10.58
L


ATOM
1632
C
ALA
L
50
−0.837
−5.114
−24.366
1.00
11.72
L


ATOM
1633
O
ALA
L
50
−1.317
−6.023
−23.677
1.00
12.15
L


ATOM
1634
N
ALA
L
51
0.117
−5.322
−25.273
1.00
11.70
L


ATOM
1635
CA
ALA
L
51
0.727
−6.631
−25.523
1.00
9.42
L


ATOM
1636
CB
ALA
L
51
1.330
−7.173
−24.234
1.00
7.05
L


ATOM
1637
C
ALA
L
51
−0.173
−7.694
−26.159
1.00
9.55
L


ATOM
1638
O
ALA
L
51
0.275
−8.458
−27.015
1.00
8.26
L


ATOM
1639
N
SER
L
52
−1.439
−7.753
−25.763
1.00
9.60
L


ATOM
1640
CA
SER
L
52
−2.315
−8.771
−26.328
1.00
10.62
L


ATOM
1641
CB
SER
L
52
−2.398
−9.948
−25.363
1.00
10.40
L


ATOM
1642
OG
SER
L
52
−2.708
−9.513
−24.050
1.00
10.76
L


ATOM
1643
C
SER
L
52
−3.735
−8.345
−26.704
1.00
11.70
L


ATOM
1644
O
SER
L
52
−4.538
−9.179
−27.112
1.00
12.32
L


ATOM
1645
N
SER
L
53
−4.063
−7.070
−26.542
1.00
12.45
L


ATOM
1646
CA
SER
L
53
−5.392
−6.620
−26.887
1.00
12.61
L


ATOM
1647
CB
SER
L
53
−5.735
−5.353
−26.127
1.00
12.98
L


ATOM
1648
OG
SER
L
53
−6.024
−5.669
−24.770
1.00
11.76
L


ATOM
1649
C
SER
L
53
−5.434
−6.384
−28.380
1.00
14.27
L


ATOM
1650
O
SER
L
53
−4.563
−5.711
−28.961
1.00
16.33
L


ATOM
1651
N
LEU
L
54
−6.448
−6.972
−28.998
1.00
12.16
L


ATOM
1652
CA
LEU
L
54
−6.631
−6.882
−30.426
1.00
12.45
L


ATOM
1653
CB
LEU
L
54
−7.256
−8.181
−30.925
1.00
12.18
L


ATOM
1654
CG
LEU
L
54
−7.643
−8.244
−32.395
1.00
11.41
L


ATOM
1655
CD1
LEU
L
54
−6.376
−8.187
−33.226
1.00
14.26
L


ATOM
1656
CD2
LEU
L
54
−8.408
−9.519
−32.662
1.00
10.12
L


ATOM
1657
C
LEU
L
54
−7.505
−5.699
−30.821
1.00
13.60
L


ATOM
1658
O
LEU
L
54
−8.662
−5.606
−30.419
1.00
16.51
L


ATOM
1659
N
GLN
L
55
−6.944
−4.798
−31.616
1.00
13.48
L


ATOM
1660
CA
GLN
L
55
−7.668
−3.627
−32.096
1.00
14.51
L


ATOM
1661
CB
GLN
L
55
−6.766
−2.832
−33.036
1.00
14.61
L


ATOM
1662
CG
GLN
L
55
−7.487
−1.838
−33.930
1.00
14.24
L


ATOM
1663
CD
GLN
L
55
−8.269
−0.805
−33.149
1.00
12.97
L


ATOM
1664
OE1
GLN
L
55
−7.943
−0.504
−32.002
1.00
11.02
L


ATOM
1665
NE2
GLN
L
55
−9.292
−0.236
−33.777
1.00
13.96
L


ATOM
1666
C
GLN
L
55
−8.942
−4.053
−32.829
1.00
15.51
L


ATOM
1667
O
GLN
L
55
−8.971
−5.097
−33.496
1.00
16.22
L


ATOM
1668
N
SER
L
56
−9.994
−3.254
−32.714
1.00
15.89
L


ATOM
1669
CA
SER
L
56
−11.232
−3.609
−33.386
1.00
17.33
L


ATOM
1670
CB
SER
L
56
−12.354
−2.646
−33.030
1.00
17.45
L


ATOM
1671
OG
SER
L
56
−13.505
−2.971
−33.799
1.00
20.41
L


ATOM
1672
C
SER
L
56
−11.052
−3.599
−34.889
1.00
17.72
L


ATOM
1673
O
SER
L
56
−10.285
−2.807
−35.428
1.00
18.29
L


ATOM
1674
N
GLY
L
57
−11.779
−4.477
−35.566
1.00
19.09
L


ATOM
1675
CA
GLY
L
57
−11.685
−4.542
−37.011
1.00
19.73
L


ATOM
1676
C
GLY
L
57
−10.493
−5.311
−37.551
1.00
20.28
L


ATOM
1677
O
GLY
L
57
−10.216
−5.259
−38.749
1.00
22.53
L


ATOM
1678
N
VAL
L
58
−9.779
−6.001
−36.672
1.00
20.10
L


ATOM
1679
CA
VAL
L
58
−8.639
−6.796
−37.080
1.00
20.30
L


ATOM
1680
CB
VAL
L
58
−7.386
−6.488
−36.211
1.00
21.32
L


ATOM
1681
CG1
VAL
L
58
−6.265
−7.495
−36.511
1.00
19.34
L


ATOM
1682
CG2
VAL
L
58
−6.904
−5.074
−36.495
1.00
19.12
L


ATOM
1683
C
VAL
L
58
−9.009
−8.264
−36.925
1.00
19.94
L


ATOM
1684
O
VAL
L
58
−9.526
−8.678
−35.889
1.00
18.67
L


ATOM
1685
N
PRO
L
59
−8.757
−9.065
−37.966
1.00
21.08
L


ATOM
1686
CD
PRO
L
59
−8.083
−8.678
−39.214
1.00
20.13
L


ATOM
1687
CA
PRO
L
59
−9.054
−10.500
−37.963
1.00
21.74
L


ATOM
1688
CB
PRO
L
59
−8.499
−10.964
−39.306
1.00
21.19
L


ATOM
1689
CG
PRO
L
59
−7.436
−9.961
−39.603
1.00
21.70
L


ATOM
1690
C
PRO
L
59
−8.437
−11.242
−36.770
1.00
22.49
L


ATOM
1691
O
PRO
L
59
−7.299
−10.991
−36.380
1.00
22.11
L


ATOM
1692
N
SER
L
60
−9.207
−12.164
−36.207
1.00
22.49
L


ATOM
1693
CA
SER
L
60
−8.785
−12.928
−35.048
1.00
22.80
L


ATOM
1694
CB
SER
L
60
−9.923
−13.845
−34.621
1.00
25.54
L


ATOM
1695
OG
SER
L
60
−11.097
−13.085
−34.367
1.00
28.03
L


ATOM
1696
C
SER
L
60
−7.510
−13.747
−35.223
1.00
22.02
L


ATOM
1697
O
SER
L
60
−6.896
−14.162
−34.227
1.00
20.07
L


ATOM
1698
N
ARG
L
61
−7.108
−13.982
−36.475
1.00
20.14
L


ATOM
1699
CA
ARG
L
61
−5.897
−14.768
−36.735
1.00
19.34
L


ATOM
1700
CB
ARG
L
61
−5.785
−15.149
−38.216
1.00
19.85
L


ATOM
1701
CG
ARG
L
61
−5.642
−14.011
−39.193
1.00
19.55
L


ATOM
1702
CD
ARG
L
61
−5.201
−14.557
−40.548
1.00
18.85
L


ATOM
1703
NE
ARG
L
61
−4.882
−13.496
−41.510
1.00
18.60
L


ATOM
1704
CZ
ARG
L
61
−5.791
−12.698
−42.066
1.00
18.92
L


ATOM
1705
NH1
ARG
L
61
−7.071
−12.843
−41.760
1.00
19.33
L


ATOM
1706
NH2
ARG
L
61
−5.429
−11.749
−42.918
1.00
17.42
L


ATOM
1707
C
ARG
L
61
−4.611
−14.073
−36.265
1.00
18.31
L


ATOM
1708
O
ARG
L
61
−3.560
−14.716
−36.123
1.00
17.76
L


ATOM
1709
N
PHE
L
62
−4.711
−12.768
−36.014
1.00
16.50
L


ATOM
1710
CA
PHE
L
62
−3.591
−11.994
−35.502
1.00
14.82
L


ATOM
1711
CB
PHE
L
62
−3.683
−10.521
−35.896
1.00
13.22
L


ATOM
1712
CG
PHE
L
62
−3.259
−10.232
−37.296
1.00
11.96
L


ATOM
1713
CD1
PHE
L
62
−4.194
−10.132
−38.318
1.00
11.33
L


ATOM
1714
CD2
PHE
L
62
−1.914
−10.060
−37.597
1.00
12.51
L


ATOM
1715
CE1
PHE
L
62
−3.789
−9.860
−39.635
1.00
12.01
L


ATOM
1716
CE2
PHE
L
62
−1.494
−9.789
−38.906
1.00
12.70
L


ATOM
1717
CZ
PHE
L
62
−2.433
−9.688
−39.929
1.00
11.60
L


ATOM
1718
C
PHE
L
62
−3.708
−12.094
−33.996
1.00
15.02
L


ATOM
1719
O
PHE
L
62
−4.782
−11.897
−33.425
1.00
14.54
L


ATOM
1720
N
SER
L
63
−2.603
−12.404
−33.345
1.00
14.08
L


ATOM
1721
CA
SER
L
63
−2.637
−12.535
−31.907
1.00
13.29
L


ATOM
1722
CB
SER
L
63
−2.785
−14.020
−31.547
1.00
13.93
L


ATOM
1723
OG
SER
L
63
−2.372
−14.294
−30.217
1.00
19.30
L


ATOM
1724
C
SER
L
63
−1.341
−11.975
−31.373
1.00
12.67
L


ATOM
1725
O
SER
L
63
−0.377
−11.831
−32.122
1.00
12.77
L


ATOM
1726
N
GLY
L
64
−1.313
−11.666
−30.082
1.00
11.59
L


ATOM
1727
CA
GLY
L
64
−0.103
−11.137
−29.493
1.00
11.87
L


ATOM
1728
C
GLY
L
64
0.019
−11.587
−28.068
1.00
12.34
L


ATOM
1729
O
GLY
L
64
−0.988
−11.691
−27.376
1.00
12.02
L


ATOM
1730
N
SER
L
65
1.242
−11.885
−27.638
1.00
14.21
L


ATOM
1731
CA
SER
L
65
1.481
−12.309
−26.263
1.00
15.67
L


ATOM
1732
CB
SER
L
65
1.411
−13.821
−26.144
1.00
17.02
L


ATOM
1733
OG
SER
L
65
2.436
−14.431
−26.905
1.00
21.04
L


ATOM
1734
C
SER
L
65
2.855
−11.853
−25.844
1.00
15.90
L


ATOM
1735
O
SER
L
65
3.612
−11.325
−26.653
1.00
17.42
L


ATOM
1736
N
GLY
L
66
3.173
−12.074
−24.576
1.00
15.84
L


ATOM
1737
CA
GLY
L
66
4.464
−11.678
−24.061
1.00
15.61
L


ATOM
1738
C
GLY
L
66
4.338
−10.874
−22.793
1.00
16.12
L


ATOM
1739
O
GLY
L
66
3.241
−10.464
−22.407
1.00
16.35
L


ATOM
1740
N
SER
L
67
5.467
−10.649
−22.134
1.00
17.61
L


ATOM
1741
CA
SER
L
67
5.458
−9.888
−20.898
1.00
18.73
L


ATOM
1742
CB
SER
L
67
4.733
−10.686
−19.817
1.00
19.61
L


ATOM
1743
OG
SER
L
67
4.853
−10.060
−18.555
1.00
24.17
L


ATOM
1744
C
SER
L
67
6.866
−9.572
−20.441
1.00
18.10
L


ATOM
1745
O
SER
L
67
7.790
−10.352
−20.666
1.00
19.07
L


ATOM
1746
N
GLY
L
68
7.023
−8.430
−19.786
1.00
16.86
L


ATOM
1747
CA
GLY
L
68
8.331
−8.055
−19.293
1.00
15.58
L


ATOM
1748
C
GLY
L
68
9.251
−7.559
−20.389
1.00
14.93
L


ATOM
1749
O
GLY
L
68
9.273
−6.371
−20.712
1.00
15.09
L


ATOM
1750
N
THR
L
69
10.003
−8.474
−20.983
1.00
14.58
L


ATOM
1751
CA
THR
L
69
10.932
−8.101
−22.042
1.00
13.89
L


ATOM
1752
CB
THR
L
69
12.358
−8.443
−21.664
1.00
12.62
L


ATOM
1753
OG1
THR
L
69
12.695
−7.784
−20.444
1.00
11.61
L


ATOM
1754
CG2
THR
L
69
13.309
−7.978
−22.739
1.00
14.73
L


ATOM
1755
C
THR
L
69
10.695
−8.740
−23.398
1.00
14.85
L


ATOM
1756
O
THR
L
69
11.043
−8.165
−24.421
1.00
15.44
L


ATOM
1757
N
GLU
L
70
10.142
−9.941
−23.419
1.00
15.79
L


ATOM
1758
CA
GLU
L
70
9.921
−10.589
−24.698
1.00
17.69
L


ATOM
1759
CB
GLU
L
70
10.551
−11.987
−24.706
1.00
19.10
L


ATOM
1760
CG
GLU
L
70
10.379
−12.728
−26.021
1.00
22.22
L


ATOM
1761
CD
GLU
L
70
10.928
−14.127
−25.957
1.00
24.82
L


ATOM
1762
OE1
GLU
L
70
10.358
−14.952
−25.217
1.00
27.80
L


ATOM
1763
OE2
GLU
L
70
11.933
−14.412
−26.643
1.00
27.03
L


ATOM
1764
C
GLU
L
70
8.435
−10.656
−25.035
1.00
17.15
L


ATOM
1765
O
GLU
L
70
7.623
−11.105
−24.218
1.00
16.60
L


ATOM
1766
N
PHE
L
71
8.105
−10.191
−26.245
1.00
15.52
L


ATOM
1767
CA
PHE
L
71
6.739
−10.141
−26.776
1.00
12.84
L


ATOM
1768
CB
PHE
L
71
6.292
−8.694
−26.866
1.00
9.40
L


ATOM
1769
CG
PHE
L
71
6.236
−8.024
−25.544
1.00
9.01
L


ATOM
1770
CD1
PHE
L
71
5.043
−7.994
−24.816
1.00
6.35
L


ATOM
1771
CD2
PHE
L
71
7.395
−7.470
−24.988
1.00
7.48
L


ATOM
1772
CE1
PHE
L
71
5.002
−7.423
−23.552
1.00
7.02
L


ATOM
1773
CE2
PHE
L
71
7.368
−6.895
−23.721
1.00
8.02
L


ATOM
1774
CZ
PHE
L
71
6.168
−6.867
−22.990
1.00
7.39
L


ATOM
1775
C
PHE
L
71
6.688
−10.771
−28.153
1.00
13.30
L


ATOM
1776
O
PHE
L
71
7.689
−10.812
−28.857
1.00
14.78
L


ATOM
1777
N
THR
L
72
5.522
−11.252
−28.552
1.00
11.72
L


ATOM
1778
CA
THR
L
72
5.449
−11.884
−29.837
1.00
12.93
L


ATOM
1779
CB
THR
L
72
5.851
−13.382
−29.677
1.00
13.79
L


ATOM
1780
OG1
THR
L
72
5.871
−14.029
−30.955
1.00
16.29
L


ATOM
1781
CG2
THR
L
72
4.884
−14.093
−28.750
1.00
14.12
L


ATOM
1782
C
THR
L
72
4.112
−11.732
−30.578
1.00
14.12
L


ATOM
1783
O
THR
L
72
3.017
−11.877
−30.004
1.00
13.32
L


ATOM
1784
N
LEU
L
73
4.223
−11.418
−31.868
1.00
13.71
L


ATOM
1785
CA
LEU
L
73
3.068
−11.240
−32.746
1.00
13.61
L


ATOM
1786
CB
LEU
L
73
3.288
−10.048
−33.681
1.00
13.61
L


ATOM
1787
CG
LEU
L
73
2.285
−9.831
−34.820
1.00
12.11
L


ATOM
1788
CD1
LEU
L
73
0.937
−9.387
−34.247
1.00
11.81
L


ATOM
1789
CD2
LEU
L
73
2.831
−8.780
−35.766
1.00
11.75
L


ATOM
1790
C
LEU
L
73
2.940
−12.500
−33.577
1.00
13.74
L


ATOM
1791
O
LEU
L
73
3.887
−12.902
−34.252
1.00
14.87
L


ATOM
1792
N
THR
L
74
1.773
−13.124
−33.531
1.00
13.00
L


ATOM
1793
CA
THR
L
74
1.554
−14.347
−34.285
1.00
12.76
L


ATOM
1794
CB
THR
L
74
1.182
−15.517
−33.337
1.00
11.52
L


ATOM
1795
OG1
THR
L
74
2.251
−15.739
−32.410
1.00
9.59
L


ATOM
1796
CG2
THR
L
74
0.942
−16.779
−34.112
1.00
11.42
L


ATOM
1797
C
THR
L
74
0.431
−14.157
−35.302
1.00
14.52
L


ATOM
1798
O
THR
L
74
−0.611
−13.566
−34.999
1.00
13.39
L


ATOM
1799
N
ILE
L
75
0.655
−14.664
−36.507
1.00
16.24
L


ATOM
1800
CA
ILE
L
75
−0.324
−14.575
−37.575
1.00
19.83
L


ATOM
1801
CB
ILE
L
75
0.263
−13.885
−38.825
1.00
19.67
L


ATOM
1802
CG2
ILE
L
75
−0.818
−13.745
−39.902
1.00
18.59
L


ATOM
1803
CG1
ILE
L
75
0.850
−12.533
−38.437
1.00
19.11
L


ATOM
1804
CD1
ILE
L
75
1.501
−11.807
−39.572
1.00
17.61
L


ATOM
1805
C
ILE
L
75
−0.678
−16.002
−37.944
1.00
21.94
L


ATOM
1806
O
ILE
L
75
0.164
−16.729
−38.452
1.00
24.70
L


ATOM
1807
N
SER
L
76
−1.914
−16.408
−37.713
1.00
23.66
L


ATOM
1808
CA
SER
L
76
−2.287
−17.778
−38.016
1.00
26.41
L


ATOM
1809
CB
SER
L
76
−3.609
−18.105
−37.334
1.00
26.86
L


ATOM
1810
OG
SER
L
76
−3.430
−18.113
−35.939
1.00
28.66
L


ATOM
1811
C
SER
L
76
−2.358
−18.135
−39.491
1.00
27.72
L


ATOM
1812
O
SER
L
76
−1.348
−18.468
−40.109
1.00
26.56
L


ATOM
1813
N
SER
L
77
−3.563
−18.071
−40.048
1.00
29.97
L


ATOM
1814
CA
SER
L
77
−3.790
−18.392
−41.458
1.00
31.58
L


ATOM
1815
CB
SER
L
77
−5.293
−18.554
−41.711
1.00
33.53
L


ATOM
1816
OG
SER
L
77
−5.886
−19.442
−40.766
1.00
35.88
L


ATOM
1817
C
SER
L
77
−3.240
−17.287
−42.368
1.00
30.85
L


ATOM
1818
O
SER
L
77
−3.999
−16.466
−42.864
1.00
30.63
L


ATOM
1819
N
LEU
L
78
−1.928
−17.278
−42.596
1.00
30.53
L


ATOM
1820
CA
LEU
L
78
−1.301
−16.258
−43.429
1.00
30.15
L


ATOM
1821
CB
LEU
L
78
0.170
−16.605
−43.668
1.00
28.83
L


ATOM
1822
CG
LEU
L
78
1.088
−15.437
−44.047
1.00
28.76
L


ATOM
1823
CD1
LEU
L
78
1.268
−14.518
−42.853
1.00
28.55
L


ATOM
1824
CD2
LEU
L
78
2.440
−15.956
−44.511
1.00
28.72
L


ATOM
1825
C
LEU
L
78
−2.015
−16.083
−44.765
1.00
31.57
L


ATOM
1826
O
LEU
L
78
−2.232
−17.044
−45.496
1.00
32.52
L


ATOM
1827
N
GLN
L
79
−2.393
−14.850
−45.079
1.00
32.63
L


ATOM
1828
CA
GLN
L
79
−3.073
−14.576
−46.335
1.00
33.55
L


ATOM
1829
CB
GLN
L
79
−4.296
−13.709
−46.086
1.00
33.63
L


ATOM
1830
CG
GLN
L
79
−5.243
−14.244
−45.029
1.00
35.38
L


ATOM
1831
CD
GLN
L
79
−5.963
−15.507
−45.450
1.00
36.55
L


ATOM
1832
OE1
GLN
L
79
−6.674
−15.531
−46.457
1.00
38.30
L


ATOM
1833
NE2
GLN
L
79
−5.796
−16.564
−44.668
1.00
37.18
L


ATOM
1834
C
GLN
L
79
−2.125
−13.863
−47.304
1.00
34.40
L


ATOM
1835
O
GLN
L
79
−1.092
−13.315
−46.905
1.00
33.83
L


ATOM
1836
N
PRO
L
80
−2.473
−13.850
−48.596
1.00
34.60
L


ATOM
1837
CD
PRO
L
80
−3.736
−14.323
−49.186
1.00
34.49
L


ATOM
1838
CA
PRO
L
80
−1.641
−13.202
−49.611
1.00
34.81
L


ATOM
1839
CB
PRO
L
80
−2.377
−13.516
−50.901
1.00
35.12
L


ATOM
1840
CG
PRO
L
80
−3.816
−13.495
−50.448
1.00
35.60
L


ATOM
1841
C
PRO
L
80
−1.511
−11.705
−49.383
1.00
34.93
L


ATOM
1842
O
PRO
L
80
−0.559
−11.091
−49.858
1.00
36.49
L


ATOM
1843
N
GLU
L
81
−2.466
−11.119
−48.663
1.00
34.01
L


ATOM
1844
CA
GLU
L
81
−2.442
−9.687
−48.386
1.00
32.18
L


ATOM
1845
CB
GLU
L
81
−3.841
−9.089
−48.569
1.00
33.65
L


ATOM
1846
CG
GLU
L
81
−4.969
−10.115
−48.665
1.00
36.06
L


ATOM
1847
CD
GLU
L
81
−5.402
−10.622
−47.322
1.00
36.33
L


ATOM
1848
OE1
GLU
L
81
−6.230
−11.567
−47.274
1.00
35.64
L


ATOM
1849
OE2
GLU
L
81
−4.908
−10.059
−46.320
1.00
37.30
L


ATOM
1850
C
GLU
L
81
−1.885
−9.342
−47.007
1.00
30.05
L


ATOM
1851
O
GLU
L
81
−1.886
−8.182
−46.611
1.00
30.43
L


ATOM
1852
N
ASP
L
82
−1.403
−10.354
−46.291
1.00
27.93
L


ATOM
1853
CA
ASP
L
82
−0.807
−10.142
−44.985
1.00
26.19
L


ATOM
1854
CB
ASP
L
82
−0.855
−11.425
−44.150
1.00
26.09
L


ATOM
1855
CG
ASP
L
82
−2.219
−11.665
−43.540
1.00
26.98
L


ATOM
1856
OD1
ASP
L
82
−3.016
−10.704
−43.500
1.00
27.12
L


ATOM
1857
OD2
ASP
L
82
−2.498
−12.799
−43.086
1.00
26.87
L


ATOM
1858
C
ASP
L
82
0.639
−9.684
−45.164
1.00
25.38
L


ATOM
1859
O
ASP
L
82
1.377
−9.507
−44.191
1.00
25.53
L


ATOM
1860
N
PHE
L
83
1.034
−9.513
−46.423
1.00
24.11
L


ATOM
1861
CA
PHE
L
83
2.373
−9.055
−46.791
1.00
22.21
L


ATOM
1862
CB
PHE
L
83
2.555
−9.135
−48.304
1.00
24.70
L


ATOM
1863
CG
PHE
L
83
3.496
−8.112
−48.854
1.00
27.07
L


ATOM
1864
CD1
PHE
L
83
4.852
−8.143
−48.535
1.00
29.04
L


ATOM
1865
CD2
PHE
L
83
3.021
−7.095
−49.676
1.00
27.98
L


ATOM
1866
CE1
PHE
L
83
5.729
−7.169
−49.031
1.00
29.51
L


ATOM
1867
CE2
PHE
L
83
3.885
−6.115
−50.179
1.00
28.81
L


ATOM
1868
CZ
PHE
L
83
5.245
−6.150
−49.856
1.00
28.92
L


ATOM
1869
C
PHE
L
83
2.539
−7.611
−46.345
1.00
19.13
L


ATOM
1870
O
PHE
L
83
1.738
−6.748
−46.694
1.00
17.37
L


ATOM
1871
N
ALA
L
84
3.586
−7.348
−45.577
1.00
17.11
L


ATOM
1872
CA
ALA
L
84
3.829
−5.998
−45.083
1.00
14.54
L


ATOM
1873
CB
ALA
L
84
2.576
−5.475
−44.393
1.00
14.75
L


ATOM
1874
C
ALA
L
84
4.990
−5.969
−44.109
1.00
12.00
L


ATOM
1875
O
ALA
L
84
5.614
−6.993
−43.853
1.00
11.20
L


ATOM
1876
N
THR
L
85
5.287
−4.787
−43.580
1.00
10.99
L


ATOM
1877
CA
THR
L
85
6.343
−4.662
−42.576
1.00
9.98
L


ATOM
1878
CB
THR
L
85
7.239
−3.431
−42.768
1.00
10.55
L


ATOM
1879
OG1
THR
L
85
7.894
−3.485
−44.042
1.00
12.19
L


ATOM
1880
CG2
THR
L
85
8.290
−3.401
−41.656
1.00
9.30
L


ATOM
1881
C
THR
L
85
5.623
−4.495
−41.241
1.00
8.43
L


ATOM
1882
O
THR
L
85
4.729
−3.673
−41.120
1.00
6.48
L


ATOM
1883
N
TYR
L
86
5.997
−5.306
−40.259
1.00
8.48
L


ATOM
1884
CA
TYR
L
86
5.391
−5.245
−38.949
1.00
7.21
L


ATOM
1885
CB
TYR
L
86
5.028
−6.649
−38.460
1.00
6.82
L


ATOM
1886
CG
TYR
L
86
3.949
−7.290
−39.306
1.00
6.34
L


ATOM
1887
CD1
TYR
L
86
4.243
−7.762
−40.588
1.00
6.20
L


ATOM
1888
CE1
TYR
L
86
3.253
−8.227
−41.429
1.00
6.26
L


ATOM
1889
CD2
TYR
L
86
2.617
−7.319
−38.877
1.00
4.76
L


ATOM
1890
CE2
TYR
L
86
1.602
−7.785
−39.714
1.00
5.10
L


ATOM
1891
CZ
TYR
L
86
1.929
−8.236
−40.996
1.00
7.14
L


ATOM
1892
OH
TYR
L
86
0.941
−8.659
−41.866
1.00
6.72
L


ATOM
1893
C
TYR
L
86
6.373
−4.579
−37.995
1.00
7.26
L


ATOM
1894
O
TYR
L
86
7.579
−4.870
−38.005
1.00
4.91
L


ATOM
1895
N
TYR
L
87
5.845
−3.677
−37.174
1.00
6.41
L


ATOM
1896
CA
TYR
L
87
6.652
−2.933
−36.225
1.00
7.18
L


ATOM
1897
CB
TYR
L
87
6.676
−1.444
−36.575
1.00
8.52
L


ATOM
1898
CG
TYR
L
87
7.429
−1.033
−37.814
1.00
8.46
L


ATOM
1899
CD1
TYR
L
87
6.774
−0.864
−39.030
1.00
9.06
L


ATOM
1900
CE1
TYR
L
87
7.469
−0.430
−40.166
1.00
9.29
L


ATOM
1901
CD2
TYR
L
87
8.800
−0.765
−37.761
1.00
8.75
L


ATOM
1902
CE2
TYR
L
87
9.497
−0.336
−38.887
1.00
8.41
L


ATOM
1903
CZ
TYR
L
87
8.831
−0.172
−40.080
1.00
8.83
L


ATOM
1904
OH
TYR
L
87
9.539
0.236
−41.185
1.00
11.80
L


ATOM
1905
C
TYR
L
87
6.099
−3.031
−34.825
1.00
7.93
L


ATOM
1906
O
TYR
L
87
4.885
−2.992
−34.632
1.00
7.55
L


ATOM
1907
N
CYS
L
88
6.977
−3.152
−33.840
1.00
8.98
L


ATOM
1908
CA
CYS
L
88
6.499
−3.166
−32.469
1.00
11.08
L


ATOM
1909
C
CYS
L
88
6.912
−1.822
−31.879
1.00
9.49
L


ATOM
1910
O
CYS
L
88
7.922
−1.246
−32.288
1.00
8.19
L


ATOM
1911
CB
CYS
L
88
7.086
−4.336
−31.669
1.00
13.87
L


ATOM
1912
SG
CYS
L
88
8.894
−4.471
−31.607
1.00
20.10
L


ATOM
1913
N
GLN
L
89
6.116
−1.308
−30.948
1.00
7.20
L


ATOM
1914
CA
GLN
L
89
6.407
−0.018
−30.327
1.00
6.74
L


ATOM
1915
CB
GLN
L
89
5.560
1.069
−31.001
1.00
6.69
L


ATOM
1916
CG
GLN
L
89
5.789
2.460
−30.496
1.00
6.01
L


ATOM
1917
CD
GLN
L
89
4.544
3.052
−29.902
1.00
6.62
L


ATOM
1918
OE1
GLN
L
89
3.475
3.034
−30.516
1.00
7.04
L


ATOM
1919
NE2
GLN
L
89
4.669
3.591
−28.699
1.00
6.50
L


ATOM
1920
C
GLN
L
89
6.122
−0.056
−28.827
1.00
6.25
L


ATOM
1921
O
GLN
L
89
5.090
−0.584
−28.414
1.00
6.91
L


ATOM
1922
N
GLN
L
90
7.033
0.467
−28.002
1.00
4.40
L


ATOM
1923
CA
GLN
L
90
6.784
0.480
−26.556
1.00
2.66
L


ATOM
1924
CB
GLN
L
90
8.018
0.016
−25.758
1.00
2.41
L


ATOM
1925
CG
GLN
L
90
9.279
0.918
−25.727
1.00
1.00
L


ATOM
1926
CD
GLN
L
90
9.148
2.183
−24.860
1.00
1.97
L


ATOM
1927
OE1
GLN
L
90
8.495
2.190
−23.802
1.00
1.00
L


ATOM
1928
NE2
GLN
L
90
9.788
3.262
−25.311
1.00
1.00
L


ATOM
1929
C
GLN
L
90
6.359
1.865
−26.082
1.00
3.53
L


ATOM
1930
O
GLN
L
90
6.774
2.889
−26.635
1.00
1.89
L


ATOM
1931
N
TYR
L
91
5.507
1.893
−25.068
1.00
4.57
L


ATOM
1932
CA
TYR
L
91
5.053
3.153
−24.516
1.00
5.80
L


ATOM
1933
CB
TYR
L
91
3.646
3.498
−25.013
1.00
5.04
L


ATOM
1934
CG
TYR
L
91
2.594
2.439
−24.830
1.00
3.81
L


ATOM
1935
CD1
TYR
L
91
1.726
2.476
−23.745
1.00
2.40
L


ATOM
1936
CE1
TYR
L
91
0.722
1.522
−23.601
1.00
3.37
L


ATOM
1937
CD2
TYR
L
91
2.438
1.418
−25.774
1.00
4.35
L


ATOM
1938
CE2
TYR
L
91
1.433
0.450
−25.643
1.00
4.21
L


ATOM
1939
CZ
TYR
L
91
0.576
0.512
−24.548
1.00
4.57
L


ATOM
1940
OH
TYR
L
91
−0.437
−0.423
−24.391
1.00
5.24
L


ATOM
1941
C
TYR
L
91
5.106
3.122
−23.001
1.00
6.62
L


ATOM
1942
O
TYR
L
91
4.224
3.610
−22.314
1.00
6.77
L


ATOM
1943
N
HIS
L
92
6.187
2.565
−22.486
1.00
8.26
L


ATOM
1944
CA
HIS
L
92
6.379
2.482
−21.055
1.00
9.83
L


ATOM
1945
CB
HIS
L
92
7.304
1.307
−20.732
1.00
10.19
L


ATOM
1946
CG
HIS
L
92
7.597
1.157
−19.277
1.00
13.25
L


ATOM
1947
CD2
HIS
L
92
8.751
1.290
−18.579
1.00
14.04
L


ATOM
1948
ND1
HIS
L
92
6.617
0.877
−18.351
1.00
15.26
L


ATOM
1949
CE1
HIS
L
92
7.153
0.846
−17.143
1.00
15.88
L


ATOM
1950
NE2
HIS
L
92
8.446
1.095
−17.254
1.00
14.69
L


ATOM
1951
C
HIS
L
92
6.992
3.797
−20.592
1.00
9.20
L


ATOM
1952
O
HIS
L
92
6.559
4.372
−19.608
1.00
10.88
L


ATOM
1953
N
SER
L
93
8.020
4.257
−21.291
1.00
9.19
L


ATOM
1954
CA
SER
L
93
8.664
5.515
−20.936
1.00
10.15
L


ATOM
1955
CB
SER
L
93
9.917
5.274
−20.075
1.00
9.91
L


ATOM
1956
OG
SER
L
93
10.867
4.497
−20.754
1.00
9.93
L


ATOM
1957
C
SER
L
93
9.037
6.274
−22.212
1.00
11.08
L


ATOM
1958
O
SER
L
93
9.094
5.699
−23.300
1.00
13.59
L


ATOM
1959
N
TYR
L
94
9.258
7.575
−22.080
1.00
11.16
L


ATOM
1960
CA
TYR
L
94
9.645
8.405
−23.207
1.00
10.67
L


ATOM
1961
CB
TYR
L
94
9.220
9.831
−22.952
1.00
10.20
L


ATOM
1962
CG
TYR
L
94
7.750
10.031
−23.055
1.00
11.98
L


ATOM
1963
CD1
TYR
L
94
7.126
10.063
−24.299
1.00
13.10
L


ATOM
1964
CE1
TYR
L
94
5.764
10.284
−24.409
1.00
12.68
L


ATOM
1965
CD2
TYR
L
94
6.970
10.214
−21.913
1.00
12.34
L


ATOM
1966
CE2
TYR
L
94
5.606
10.434
−22.019
1.00
11.24
L


ATOM
1967
CZ
TYR
L
94
5.017
10.473
−23.272
1.00
10.97
L


ATOM
1968
OH
TYR
L
94
3.683
10.752
−23.393
1.00
12.39
L


ATOM
1969
C
TYR
L
94
11.152
8.359
−23.350
1.00
10.75
L


ATOM
1970
O
TYR
L
94
11.864
8.329
−22.339
1.00
12.12
L


ATOM
1971
N
PRO
L
95
11.659
8.378
−24.599
1.00
10.12
L


ATOM
1972
CD
PRO
L
95
13.096
8.523
−24.881
1.00
10.42
L


ATOM
1973
CA
PRO
L
95
10.891
8.452
−25.845
1.00
9.23
L


ATOM
1974
CB
PRO
L
95
11.939
8.828
−26.890
1.00
10.36
L


ATOM
1975
CG
PRO
L
95
13.074
9.396
−26.088
1.00
11.18
L


ATOM
1976
C
PRO
L
95
10.259
7.125
−26.181
1.00
9.78
L


ATOM
1977
O
PRO
L
95
10.742
6.054
−25.786
1.00
9.82
L


ATOM
1978
N
TRP
L
96
9.171
7.189
−26.926
1.00
9.66
L


ATOM
1979
CA
TRP
L
96
8.516
5.961
−27.329
1.00
8.38
L


ATOM
1980
CB
TRP
L
96
7.080
6.265
−27.733
1.00
6.22
L


ATOM
1981
CG
TRP
L
96
6.222
6.675
−26.553
1.00
6.85
L


ATOM
1982
CD2
TRP
L
96
4.985
7.388
−26.614
1.00
5.61
L


ATOM
1983
CE2
TRP
L
96
4.444
7.404
−25.307
1.00
5.12
L


ATOM
1984
CE3
TRP
L
96
4.276
8.003
−27.649
1.00
5.94
L


ATOM
1985
CD1
TRP
L
96
6.390
6.310
−25.232
1.00
5.28
L


ATOM
1986
NE1
TRP
L
96
5.319
6.743
−24.486
1.00
5.09
L


ATOM
1987
CZ2
TRP
L
96
3.226
8.011
−25.012
1.00
4.95
L


ATOM
1988
CZ3
TRP
L
96
3.063
8.607
−27.360
1.00
6.82
L


ATOM
1989
CH2
TRP
L
96
2.546
8.603
−26.045
1.00
6.87
L


ATOM
1990
C
TRP
L
96
9.331
5.389
−28.481
1.00
7.69
L


ATOM
1991
O
TRP
L
96
9.669
6.098
−29.427
1.00
8.74
L


ATOM
1992
N
THR
L
97
9.648
4.105
−28.400
1.00
6.85
L


ATOM
1993
CA
THR
L
97
10.472
3.511
−29.424
1.00
5.66
L


ATOM
1994
CB
THR
L
97
11.755
2.906
−28.839
1.00
5.83
L


ATOM
1995
OG1
THR
L
97
12.374
3.857
−27.979
1.00
5.11
L


ATOM
1996
CG2
THR
L
97
12.736
2.559
−29.969
1.00
9.74
L


ATOM
1997
C
THR
L
97
9.827
2.448
−30.254
1.00
5.70
L


ATOM
1998
O
THR
L
97
8.964
1.712
−29.784
1.00
5.77
L


ATOM
1999
N
PHE
L
98
10.268
2.377
−31.503
1.00
5.71
L


ATOM
2000
CA
PHE
L
98
9.779
1.385
−32.417
1.00
5.89
L


ATOM
2001
CB
PHE
L
98
9.439
2.032
−33.739
1.00
5.15
L


ATOM
2002
CG
PHE
L
98
8.181
2.801
−33.716
1.00
4.13
L


ATOM
2003
CD1
PHE
L
98
8.177
4.124
−33.316
1.00
5.60
L


ATOM
2004
CD2
PHE
L
98
6.988
2.196
−34.091
1.00
4.22
L


ATOM
2005
CE1
PHE
L
98
6.989
4.857
−33.293
1.00
7.42
L


ATOM
2006
CE2
PHE
L
98
5.793
2.907
−34.075
1.00
6.81
L


ATOM
2007
CZ
PHE
L
98
5.789
4.244
−33.673
1.00
7.48
L


ATOM
2008
C
PHE
L
98
10.838
0.332
−32.625
1.00
7.27
L


ATOM
2009
O
PHE
L
98
11.988
0.502
−32.219
1.00
8.89
L


ATOM
2010
N
GLY
L
99
10.434
−0.780
−33.218
1.00
7.92
L


ATOM
2011
CA
GLY
L
99
11.389
−1.824
−33.490
1.00
9.17
L


ATOM
2012
C
GLY
L
99
11.865
−1.576
−34.911
1.00
9.56
L


ATOM
2013
O
GLY
L
99
11.177
−0.905
−35.682
1.00
10.42
L


ATOM
2014
N
GLN
L
100
13.028
−2.109
−35.267
1.00
9.40
L


ATOM
2015
CA
GLN
L
100
13.551
−1.937
−36.604
1.00
9.59
L


ATOM
2016
CB
GLN
L
100
14.878
−2.691
−36.751
1.00
8.63
L


ATOM
2017
CG
GLN
L
100
14.688
−4.183
−36.949
1.00
13.79
L


ATOM
2018
CD
GLN
L
100
14.906
−4.984
−35.693
1.00
15.52
L


ATOM
2019
OE1
GLN
L
100
14.629
−4.519
−34.583
1.00
16.85
L


ATOM
2020
NE2
GLN
L
100
15.397
−6.213
−35.860
1.00
16.25
L


ATOM
2021
C
GLN
L
100
12.527
−2.468
−37.621
1.00
9.72
L


ATOM
2022
O
GLN
L
100
12.577
−2.128
−38.793
1.00
11.02
L


ATOM
2023
N
GLY
L
101
11.600
−3.308
−37.179
1.00
8.67
L


ATOM
2024
CA
GLY
L
101
10.612
−3.835
−38.108
1.00
10.14
L


ATOM
2025
C
GLY
L
101
10.929
−5.179
−38.768
1.00
10.68
L


ATOM
2026
O
GLY
L
101
12.091
−5.550
−38.941
1.00
10.81
L


ATOM
2027
N
THR
L
102
9.882
−5.907
−39.145
1.00
10.02
L


ATOM
2028
CA
THR
L
102
10.019
−7.212
−39.782
1.00
10.68
L


ATOM
2029
CB
THR
L
102
9.391
−8.306
−38.919
1.00
10.47
L


ATOM
2030
OG1
THR
L
102
10.062
−8.363
−37.657
1.00
12.78
L


ATOM
2031
CG2
THR
L
102
9.482
−9.642
−39.605
1.00
9.34
L


ATOM
2032
C
THR
L
102
9.302
−7.227
−41.125
1.00
12.44
L


ATOM
2033
O
THR
L
102
8.083
−7.049
−41.176
1.00
12.34
L


ATOM
2034
N
LYS
L
103
10.038
−7.460
−42.207
1.00
12.98
L


ATOM
2035
CA
LYS
L
103
9.422
−7.471
−43.528
1.00
14.84
L


ATOM
2036
CB
LYS
L
103
10.385
−6.893
−44.567
1.00
15.63
L


ATOM
2037
CG
LYS
L
103
9.767
−6.747
−45.945
1.00
18.74
L


ATOM
2038
CD
LYS
L
103
10.845
−6.785
−47.009
1.00
21.41
L


ATOM
2039
CE
LYS
L
103
10.264
−6.625
−48.396
1.00
22.44
L


ATOM
2040
NZ
LYS
L
103
9.589
−5.300
−48.528
1.00
23.85
L


ATOM
2041
C
LYS
L
103
8.974
−8.871
−43.943
1.00
14.71
L


ATOM
2042
O
LYS
L
103
9.794
−9.778
−44.132
1.00
15.12
L


ATOM
2043
N
LEU
L
104
7.666
−9.031
−44.112
1.00
14.45
L


ATOM
2044
CA
LEU
L
104
7.091
−10.325
−44.468
1.00
14.60
L


ATOM
2045
CB
LEU
L
104
5.972
−10.670
−43.481
1.00
11.99
L


ATOM
2046
CG
LEU
L
104
5.099
−11.881
−43.764
1.00
11.10
L


ATOM
2047
CD1
LEU
L
104
5.932
−13.135
−43.663
1.00
11.33
L


ATOM
2048
CD2
LEU
L
104
3.942
−11.917
−42.770
1.00
11.59
L


ATOM
2049
C
LEU
L
104
6.562
−10.423
−45.892
1.00
15.97
L


ATOM
2050
O
LEU
L
104
5.579
−9.775
−46.258
1.00
16.90
L


ATOM
2051
N
GLU
L
105
7.223
−11.236
−46.701
1.00
16.86
L


ATOM
2052
CA
GLU
L
105
6.762
−11.411
−48.063
1.00
19.59
L


ATOM
2053
CB
GLU
L
105
7.919
−11.295
−49.046
1.00
20.51
L


ATOM
2054
CG
GLU
L
105
8.883
−12.420
−48.980
1.00
20.99
L


ATOM
2055
CD
GLU
L
105
8.948
−13.134
−50.299
1.00
21.61
L


ATOM
2056
OE1
GLU
L
105
9.142
−12.436
−51.313
1.00
22.37
L


ATOM
2057
OE2
GLU
L
105
8.809
−14.376
−50.328
1.00
21.64
L


ATOM
2058
C
GLU
L
105
6.094
−12.771
−48.168
1.00
20.32
L


ATOM
2059
O
GLU
L
105
6.404
−13.685
−47.398
1.00
20.09
L


ATOM
2060
N
ILE
L
106
5.169
−12.898
−49.111
1.00
21.44
L


ATOM
2061
CA
ILE
L
106
4.446
−14.143
−49.276
1.00
23.43
L


ATOM
2062
CB
ILE
L
106
3.028
−13.889
−49.771
1.00
22.83
L


ATOM
2063
CG2
ILE
L
106
2.236
−15.179
−49.698
1.00
22.89
L


ATOM
2064
CG1
ILE
L
106
2.389
−12.769
−48.945
1.00
20.99
L


ATOM
2065
CD1
ILE
L
106
2.379
−13.024
−47.451
1.00
20.39
L


ATOM
2066
C
ILE
L
106
5.121
−15.103
−50.230
1.00
24.93
L


ATOM
2067
O
ILE
L
106
5.380
−14.771
−51.387
1.00
24.17
L


ATOM
2068
N
LYS
L
107
5.409
−16.296
−49.722
1.00
28.03
L


ATOM
2069
CA
LYS
L
107
6.045
−17.327
−50.515
1.00
30.61
L


ATOM
2070
CB
LYS
L
107
6.328
−18.571
−49.679
1.00
32.10
L


ATOM
2071
CG
LYS
L
107
7.301
−19.534
−50.336
1.00
34.09
L


ATOM
2072
CD
LYS
L
107
8.721
−19.326
−49.823
1.00
36.04
L


ATOM
2073
CE
LYS
L
107
8.846
−19.791
−48.369
1.00
36.60
L


ATOM
2074
NZ
LYS
L
107
10.213
−19.608
−47.801
1.00
37.56
L


ATOM
2075
C
LYS
L
107
5.041
−17.670
−51.579
1.00
31.41
L


ATOM
2076
O
LYS
L
107
3.827
−17.614
−51.373
1.00
31.92
L


ATOM
2077
N
ARG
L
108
5.536
−18.025
−52.734
1.00
31.09
L


ATOM
2078
CA
ARG
L
108
4.608
−18.351
−53.773
1.00
30.67
L


ATOM
2079
CB
ARG
L
108
4.218
−17.065
−54.487
1.00
29.56
L


ATOM
2080
CG
ARG
L
108
2.983
−17.166
−55.316
1.00
29.55
L


ATOM
2081
CD
ARG
L
108
3.044
−16.154
−56.428
1.00
29.00
L


ATOM
2082
NE
ARG
L
108
3.220
−16.825
−57.705
1.00
30.73
L


ATOM
2083
CZ
ARG
L
108
2.221
−17.208
−58.491
1.00
31.28
L


ATOM
2084
NH1
ARG
L
108
0.967
−16.966
−58.125
1.00
32.82
L


ATOM
2085
NH2
ARG
L
108
2.473
−17.856
−59.628
1.00
30.38
L


ATOM
2086
C
ARG
L
108
5.292
−19.314
−54.710
1.00
30.78
L


ATOM
2087
O
ARG
L
108
6.516
−19.477
−54.662
1.00
30.73
L


ATOM
2885
CB
GLN
H
1
−17.228
9.372
−41.991
1.00
38.03
H


ATOM
2886
CG
GLN
H
1
−17.154
10.882
−41.725
1.00
41.63
H


ATOM
2887
CD
GLN
H
1
−18.494
11.453
−41.221
1.00
44.22
H


ATOM
2888
OE1
GLN
H
1
−19.539
11.258
−41.860
1.00
45.30
H


ATOM
2889
NE2
GLN
H
1
−18.464
12.166
−40.083
1.00
44.03
H


ATOM
2890
C
GLN
H
1
−14.757
9.019
−41.817
1.00
31.13
H


ATOM
2891
O
GLN
H
1
−14.172
10.095
−41.886
1.00
31.51
H


ATOM
2892
N
GLN
H
1
−16.184
7.270
−42.783
1.00
34.00
H


ATOM
2893
CA
GLN
H
1
−15.992
8.747
−42.656
1.00
34.12
H


ATOM
2894
N
VAL
H
2
−14.367
8.024
−41.031
1.00
26.54
H


ATOM
2895
CA
VAL
H
2
−13.212
8.138
−40.155
1.00
23.34
H


ATOM
2896
CB
VAL
H
2
−13.245
7.012
−39.131
1.00
22.59
H


ATOM
2897
CG1
VAL
H
2
−13.829
5.784
−39.774
1.00
21.51
H


ATOM
2898
CG2
VAL
H
2
−11.850
6.738
−38.596
1.00
22.41
H


ATOM
2899
C
VAL
H
2
−11.892
8.101
−40.926
1.00
21.85
H


ATOM
2900
O
VAL
H
2
−11.568
7.107
−41.560
1.00
22.10
H


ATOM
2901
N
SER
H
3
−11.121
9.179
−40.868
1.00
20.36
H


ATOM
2902
CA
SER
H
3
−9.858
9.213
−41.596
1.00
18.47
H


ATOM
2903
CB
SER
H
3
−10.141
9.399
−43.095
1.00
18.64
H


ATOM
2904
OG
SER
H
3
−10.823
10.625
−43.336
1.00
18.79
H


ATOM
2905
C
SER
H
3
−8.909
10.315
−41.108
1.00
16.35
H


ATOM
2906
O
SER
H
3
−9.301
11.207
−40.349
1.00
14.67
H


ATOM
2907
N
LEU
H
4
−7.655
10.245
−41.545
1.00
14.24
H


ATOM
2908
CA
LEU
H
4
−6.668
11.258
−41.184
1.00
14.54
H


ATOM
2909
CB
LEU
H
4
−5.672
10.723
−40.157
1.00
13.53
H


ATOM
2910
CG
LEU
H
4
−6.211
10.379
−38.766
1.00
13.76
H


ATOM
2911
CD1
LEU
H
4
−5.092
9.717
−37.965
1.00
12.35
H


ATOM
2912
CD2
LEU
H
4
−6.742
11.635
−38.063
1.00
11.54
H


ATOM
2913
C
LEU
H
4
−5.913
11.687
−42.427
1.00
14.67
H


ATOM
2914
O
LEU
H
4
−5.243
10.867
−43.049
1.00
15.74
H


ATOM
2915
N
ARG
H
5
−6.024
12.964
−42.788
1.00
15.44
H


ATOM
2916
CA
ARG
H
5
−5.350
13.478
−43.975
1.00
17.23
H


ATOM
2917
CB
ARG
H
5
−6.361
14.004
−45.003
1.00
20.91
H


ATOM
2918
CG
ARG
H
5
−7.130
12.917
−45.748
1.00
26.83
H


ATOM
2919
CD
ARG
H
5
−7.934
13.525
−46.904
1.00
34.28
H


ATOM
2920
NE
ARG
H
5
−9.324
13.826
−46.553
1.00
38.31
H


ATOM
2921
CZ
ARG
H
5
−10.294
12.916
−46.470
1.00
41.05
H


ATOM
2922
NH1
ARG
H
5
−10.030
11.638
−46.708
1.00
41.35
H


ATOM
2923
NH2
ARG
H
5
−11.537
13.283
−46.169
1.00
42.82
H


ATOM
2924
C
ARG
H
5
−4.358
14.567
−43.655
1.00
15.33
H


ATOM
2925
O
ARG
H
5
−4.731
15.672
−43.252
1.00
15.11
H


ATOM
2926
N
GLU
H
6
−3.082
14.252
−43.830
1.00
14.48
H


ATOM
2927
CA
GLU
H
6
−2.043
15.240
−43.555
1.00
13.53
H


ATOM
2928
CB
GLU
H
6
−0.837
14.591
−42.848
1.00
10.37
H


ATOM
2929
CG
GLU
H
6
−0.242
13.379
−43.502
1.00
10.69
H


ATOM
2930
CD
GLU
H
6
−0.904
12.053
−43.105
1.00
12.25
H


ATOM
2931
OE1
GLU
H
6
−1.689
11.509
−43.910
1.00
11.59
H


ATOM
2932
OE2
GLU
H
6
−0.622
11.540
−41.999
1.00
11.51
H


ATOM
2933
C
GLU
H
6
−1.595
16.021
−44.790
1.00
11.79
H


ATOM
2934
O
GLU
H
6
−1.707
15.556
−45.914
1.00
11.18
H


ATOM
2935
N
SER
H
7
−1.120
17.236
−44.576
1.00
12.26
H


ATOM
2936
CA
SER
H
7
−0.672
18.049
−45.684
1.00
12.42
H


ATOM
2937
CB
SER
H
7
−1.867
18.735
−46.366
1.00
9.88
H


ATOM
2938
OG
SER
H
7
−2.516
19.601
−45.461
1.00
8.60
H


ATOM
2939
C
SER
H
7
0.302
19.099
−45.169
1.00
13.19
H


ATOM
2940
O
SER
H
7
0.463
19.295
−43.950
1.00
11.90
H


ATOM
2941
N
GLY
H
8
0.934
19.777
−46.120
1.00
13.68
H


ATOM
2942
CA
GLY
H
8
1.892
20.813
−45.801
1.00
13.72
H


ATOM
2943
C
GLY
H
8
3.277
20.422
−46.251
1.00
13.27
H


ATOM
2944
O
GLY
H
8
4.133
21.279
−46.429
1.00
14.46
H


ATOM
2945
N
GLY
H
9
3.493
19.125
−46.446
1.00
13.04
H


ATOM
2946
CA
GLY
H
9
4.802
18.651
−46.855
1.00
13.75
H


ATOM
2947
C
GLY
H
9
5.258
19.190
−48.193
1.00
14.12
H


ATOM
2948
O
GLY
H
9
4.449
19.475
−49.070
1.00
14.64
H


ATOM
2949
N
GLY
H
10
6.569
19.324
−48.335
1.00
12.90
H


ATOM
2950
CA
GLY
H
10
7.147
19.815
−49.562
1.00
11.12
H


ATOM
2951
C
GLY
H
10
8.640
19.951
−49.395
1.00
12.16
H


ATOM
2952
O
GLY
H
10
9.231
19.397
−48.460
1.00
14.47
H


ATOM
2953
N
LEU
H
11
9.254
20.695
−50.301
1.00
11.81
H


ATOM
2954
CA
LEU
H
11
10.695
20.902
−50.264
1.00
11.20
H


ATOM
2955
CB
LEU
H
11
11.194
21.229
−51.666
1.00
11.52
H


ATOM
2956
CG
LEU
H
11
12.655
21.626
−51.772
1.00
9.91
H


ATOM
2957
CD1
LEU
H
11
13.531
20.399
−51.735
1.00
9.46
H


ATOM
2958
CD2
LEU
H
11
12.840
22.394
−53.039
1.00
11.08
H


ATOM
2959
C
LEU
H
11
10.970
22.065
−49.336
1.00
10.64
H


ATOM
2960
O
LEU
H
11
10.341
23.103
−49.445
1.00
11.74
H


ATOM
2961
N
VAL
H
12
11.895
21.898
−48.412
1.00
11.07
H


ATOM
2962
CA
VAL
H
12
12.199
22.984
−47.500
1.00
11.68
H


ATOM
2963
CB
VAL
H
12
11.525
22.744
−46.117
1.00
11.62
H


ATOM
2964
CG1
VAL
H
12
11.994
21.426
−45.533
1.00
11.18
H


ATOM
2965
CG2
VAL
H
12
11.831
23.881
−45.177
1.00
10.48
H


ATOM
2966
C
VAL
H
12
13.714
23.124
−47.362
1.00
11.68
H


ATOM
2967
O
VAL
H
12
14.449
22.135
−47.333
1.00
11.18
H


ATOM
2968
N
GLN
H
13
14.178
24.364
−47.284
1.00
13.31
H


ATOM
2969
CA
GLN
H
13
15.606
24.628
−47.187
1.00
15.00
H


ATOM
2970
CB
GLN
H
13
15.919
26.019
−47.755
1.00
15.90
H


ATOM
2971
CG
GLN
H
13
16.193
26.029
−49.271
1.00
16.90
H


ATOM
2972
CD
GLN
H
13
16.243
27.430
−49.863
1.00
18.00
H


ATOM
2973
OE1
GLN
H
13
16.870
28.332
−49.308
1.00
18.96
H


ATOM
2974
NE2
GLN
H
13
15.597
27.611
−51.009
1.00
18.93
H


ATOM
2975
C
GLN
H
13
16.152
24.501
−45.777
1.00
13.89
H


ATOM
2976
O
GLN
H
13
15.469
24.805
−44.806
1.00
14.83
H


ATOM
2977
N
PRO
H
14
17.402
24.044
−45.647
1.00
13.23
H


ATOM
2978
CD
PRO
H
14
18.348
23.638
−46.699
1.00
13.82
H


ATOM
2979
CA
PRO
H
14
18.001
23.893
−44.319
1.00
12.61
H


ATOM
2980
CB
PRO
H
14
19.445
23.511
−44.630
1.00
11.95
H


ATOM
2981
CG
PRO
H
14
19.321
22.762
−45.916
1.00
13.51
H


ATOM
2982
C
PRO
H
14
17.895
25.206
−43.561
1.00
12.29
H


ATOM
2983
O
PRO
H
14
18.215
26.265
−44.089
1.00
13.56
H


ATOM
2984
N
GLY
H
15
17.415
25.127
−42.329
1.00
11.52
H


ATOM
2985
CA
GLY
H
15
17.278
26.320
−41.529
1.00
10.23
H


ATOM
2986
C
GLY
H
15
15.918
26.977
−41.625
1.00
11.22
H


ATOM
2987
O
GLY
H
15
15.526
27.715
−40.724
1.00
9.73
H


ATOM
2988
N
ARG
H
16
15.186
26.719
−42.702
1.00
12.69
H


ATOM
2989
CA
ARG
H
16
13.877
27.342
−42.854
1.00
14.66
H


ATOM
2990
CB
ARG
H
16
13.435
27.319
−44.314
1.00
18.56
H


ATOM
2991
CG
ARG
H
16
14.241
28.208
−45.227
1.00
21.98
H


ATOM
2992
CD
ARG
H
16
13.934
29.663
−44.974
1.00
25.86
H


ATOM
2993
NE
ARG
H
16
14.396
30.485
−46.095
1.00
32.22
H


ATOM
2994
CZ
ARG
H
16
13.815
30.518
−47.295
1.00
34.94
H


ATOM
2995
NH1
ARG
H
16
12.732
29.783
−47.529
1.00
36.64
H


ATOM
2996
NH2
ARG
H
16
14.333
31.255
−48.274
1.00
36.71
H


ATOM
2997
C
ARG
H
16
12.875
26.594
−42.005
1.00
14.25
H


ATOM
2998
O
ARG
H
16
13.233
25.638
−41.321
1.00
14.28
H


ATOM
2999
N
SER
H
17
11.623
27.037
−42.029
1.00
13.56
H


ATOM
3000
CA
SER
H
17
10.585
26.376
−41.248
1.00
12.76
H


ATOM
3001
CB
SER
H
17
10.251
27.185
−39.976
1.00
10.97
H


ATOM
3002
OG
SER
H
17
9.880
28.517
−40.261
1.00
10.44
H


ATOM
3003
C
SER
H
17
9.338
26.116
−42.083
1.00
12.50
H


ATOM
3004
O
SER
H
17
8.999
26.880
−42.990
1.00
11.82
H


ATOM
3005
N
LEU
H
18
8.672
25.012
−41.763
1.00
12.08
H


ATOM
3006
CA
LEU
H
18
7.480
24.574
−42.471
1.00
12.12
H


ATOM
3007
CB
LEU
H
18
7.854
23.397
−43.366
1.00
12.29
H


ATOM
3008
CG
LEU
H
18
6.806
22.856
−44.314
1.00
15.26
H


ATOM
3009
CD1
LEU
H
18
6.544
23.892
−45.426
1.00
16.99
H


ATOM
3010
CD2
LEU
H
18
7.298
21.565
−44.932
1.00
14.85
H


ATOM
3011
C
LEU
H
18
6.409
24.131
−41.469
1.00
12.46
H


ATOM
3012
O
LEU
H
18
6.740
23.668
−40.376
1.00
13.86
H


ATOM
3013
N
ARG
H
19
5.134
24.269
−41.837
1.00
11.69
H


ATOM
3014
CA
ARG
H
19
4.053
23.858
−40.949
1.00
11.63
H


ATOM
3015
CB
ARG
H
19
3.108
25.010
−40.584
1.00
13.15
H


ATOM
3016
CG
ARG
H
19
2.323
24.705
−39.311
1.00
17.79
H


ATOM
3017
CD
ARG
H
19
1.220
25.700
−39.011
1.00
20.71
H


ATOM
3018
NE
ARG
H
19
0.145
25.586
−39.985
1.00
24.55
H


ATOM
3019
CZ
ARG
H
19
−1.106
25.997
−39.786
1.00
26.15
H


ATOM
3020
NH1
ARG
H
19
−1.453
26.559
−38.629
1.00
27.90
H


ATOM
3021
NH2
ARG
H
19
−2.011
25.833
−40.750
1.00
23.19
H


ATOM
3022
C
ARG
H
19
3.232
22.752
−41.554
1.00
10.59
H


ATOM
3023
O
ARG
H
19
2.636
22.908
−42.622
1.00
11.48
H


ATOM
3024
N
LEU
H
20
3.195
21.625
−40.856
1.00
8.72
H


ATOM
3025
CA
LEU
H
20
2.431
20.459
−41.299
1.00
6.73
H


ATOM
3026
CB
LEU
H
20
3.193
19.198
−40.933
1.00
5.77
H


ATOM
3027
CG
LEU
H
20
3.855
18.376
−42.018
1.00
6.73
H


ATOM
3028
CD1
LEU
H
20
4.504
19.241
−43.114
1.00
5.43
H


ATOM
3029
CD2
LEU
H
20
4.875
17.511
−41.312
1.00
4.29
H


ATOM
3030
C
LEU
H
20
1.076
20.433
−40.599
1.00
5.76
H


ATOM
3031
O
LEU
H
20
0.984
20.689
−39.406
1.00
6.95
H


ATOM
3032
N
SER
H
21
0.026
20.111
−41.329
1.00
5.05
H


ATOM
3033
CA
SER
H
21
−1.271
20.061
−40.691
1.00
5.74
H


ATOM
3034
CB
SER
H
21
−2.160
21.227
−41.124
1.00
5.27
H


ATOM
3035
OG
SER
H
21
−2.582
21.072
−42.462
1.00
8.84
H


ATOM
3036
C
SER
H
21
−1.929
18.744
−41.036
1.00
5.36
H


ATOM
3037
O
SER
H
21
−1.707
18.214
−42.121
1.00
2.68
H


ATOM
3038
N
CYS
H
22
−2.698
18.215
−40.083
1.00
7.14
H


ATOM
3039
CA
CYS
H
22
−3.415
16.950
−40.221
1.00
9.56
H


ATOM
3040
C
CYS
H
22
−4.910
17.166
−39.980
1.00
9.14
H


ATOM
3041
O
CYS
H
22
−5.308
17.596
−38.894
1.00
7.69
H


ATOM
3042
CB
CYS
H
22
−2.922
15.911
−39.204
1.00
11.39
H


ATOM
3043
SG
CYS
H
22
−3.763
14.298
−39.439
1.00
13.19
H


ATOM
3044
N
THR
H
23
−5.731
16.873
−40.989
1.00
8.90
H


ATOM
3045
CA
THR
H
23
−7.184
17.020
−40.872
1.00
9.76
H


ATOM
3046
CB
THR
H
23
−7.819
17.476
−42.177
1.00
10.09
H


ATOM
3047
OG1
THR
H
23
−7.296
18.758
−42.534
1.00
12.65
H


ATOM
3048
CG2
THR
H
23
−9.335
17.552
−42.022
1.00
8.41
H


ATOM
3049
C
THR
H
23
−7.862
15.714
−40.488
1.00
9.51
H


ATOM
3050
O
THR
H
23
−7.682
14.686
−41.152
1.00
9.77
H


ATOM
3051
N
ALA
H
24
−8.664
15.771
−39.430
1.00
7.58
H


ATOM
3052
CA
ALA
H
24
−9.375
14.601
−38.941
1.00
6.53
H


ATOM
3053
CB
ALA
H
24
−9.189
14.512
−37.453
1.00
5.54
H


ATOM
3054
C
ALA
H
24
−10.873
14.590
−39.280
1.00
6.84
H


ATOM
3055
O
ALA
H
24
−11.472
15.630
−39.561
1.00
6.30
H


ATOM
3056
N
SER
H
25
−11.468
13.402
−39.268
1.00
7.53
H


ATOM
3057
CA
SER
H
25
−12.891
13.275
−39.529
1.00
9.12
H


ATOM
3058
CB
SER
H
25
−13.207
13.521
−41.003
1.00
10.49
H


ATOM
3059
OG
SER
H
25
−12.900
12.376
−41.778
1.00
13.85
H


ATOM
3060
C
SER
H
25
−13.392
11.900
−39.138
1.00
8.68
H


ATOM
3061
O
SER
H
25
−12.610
10.959
−39.071
1.00
9.15
H


ATOM
3062
N
GLY
H
26
−14.694
11.803
−38.863
1.00
7.31
H


ATOM
3063
CA
GLY
H
26
−15.294
10.534
−38.512
1.00
5.63
H


ATOM
3064
C
GLY
H
26
−15.259
10.129
−37.052
1.00
6.29
H


ATOM
3065
O
GLY
H
26
−15.746
9.043
−36.718
1.00
6.85
H


ATOM
3066
N
PHE
H
27
−14.676
10.970
−36.195
1.00
5.39
H


ATOM
3067
CA
PHE
H
27
−14.602
10.703
−34.764
1.00
3.21
H


ATOM
3068
CB
PHE
H
27
−13.394
9.836
−34.430
1.00
3.38
H


ATOM
3069
CG
PHE
H
27
−12.069
10.493
−34.681
1.00
6.17
H


ATOM
3070
CD1
PHE
H
27
−11.388
11.128
−33.649
1.00
7.13
H


ATOM
3071
CD2
PHE
H
27
−11.485
10.459
−35.948
1.00
8.80
H


ATOM
3072
CE1
PHE
H
27
−10.129
11.725
−33.872
1.00
8.38
H


ATOM
3073
CE2
PHE
H
27
−10.224
11.053
−36.192
1.00
7.26
H


ATOM
3074
CZ
PHE
H
27
−9.546
11.687
−35.145
1.00
7.99
H


ATOM
3075
C
PHE
H
27
−14.534
12.027
−34.038
1.00
3.40
H


ATOM
3076
O
PHE
H
27
−14.437
13.059
−34.677
1.00
2.87
H


ATOM
3077
N
THR
H
28
−14.622
12.007
−32.710
1.00
5.40
H


ATOM
3078
CA
THR
H
28
−14.601
13.243
−31.932
1.00
6.21
H


ATOM
3079
CB
THR
H
28
−15.466
13.120
−30.668
1.00
6.55
H


ATOM
3080
OG1
THR
H
28
−16.790
12.732
−31.047
1.00
7.06
H


ATOM
3081
CG2
THR
H
28
−15.537
14.448
−29.940
1.00
5.57
H


ATOM
3082
C
THR
H
28
−13.178
13.618
−31.539
1.00
8.34
H


ATOM
3083
O
THR
H
28
−12.650
13.174
−30.513
1.00
7.70
H


ATOM
3084
N
PHE
H
29
−12.586
14.471
−32.366
1.00
9.20
H


ATOM
3085
CA
PHE
H
29
−11.219
14.939
−32.223
1.00
8.64
H


ATOM
3086
CB
PHE
H
29
−11.023
16.179
−33.108
1.00
6.86
H


ATOM
3087
CG
PHE
H
29
−9.588
16.496
−33.401
1.00
5.50
H


ATOM
3088
CD1
PHE
H
29
−8.792
15.590
−34.095
1.00
4.60
H


ATOM
3089
CD2
PHE
H
29
−9.033
17.706
−32.999
1.00
4.43
H


ATOM
3090
CE1
PHE
H
29
−7.466
15.879
−34.382
1.00
5.04
H


ATOM
3091
CE2
PHE
H
29
−7.706
18.005
−33.281
1.00
4.00
H


ATOM
3092
CZ
PHE
H
29
−6.923
17.089
−33.977
1.00
5.16
H


ATOM
3093
C
PHE
H
29
−10.706
15.231
−30.821
1.00
9.74
H


ATOM
3094
O
PHE
H
29
−9.661
14.697
−30.422
1.00
8.35
H


ATOM
3095
N
ARG
H
30
−11.421
16.073
−30.077
1.00
12.71
H


ATOM
3096
CA
ARG
H
30
−10.984
16.465
−28.728
1.00
14.89
H


ATOM
3097
CB
ARG
H
30
−11.880
17.577
−28.172
1.00
18.34
H


ATOM
3098
CG
ARG
H
30
−13.328
17.141
−28.001
1.00
25.22
H


ATOM
3099
CD
ARG
H
30
−14.242
18.281
−27.550
1.00
30.89
H


ATOM
3100
NE
ARG
H
30
−14.174
18.521
−26.112
1.00
34.44
H


ATOM
3101
CZ
ARG
H
30
−14.768
19.538
−25.477
1.00
37.44
H


ATOM
3102
NH1
ARG
H
30
−15.486
20.435
−26.150
1.00
36.31
H


ATOM
3103
NH2
ARG
H
30
−14.647
19.660
−24.153
1.00
37.84
H


ATOM
3104
C
ARG
H
30
−10.960
15.307
−27.739
1.00
14.44
H


ATOM
3105
O
ARG
H
30
−10.426
15.442
−26.641
1.00
14.72
H


ATOM
3106
N
HIS
H
31
−11.522
14.170
−28.134
1.00
13.78
H


ATOM
3107
CA
HIS
H
31
−11.580
13.006
−27.263
1.00
13.18
H


ATOM
3108
CB
HIS
H
31
−12.850
12.186
−27.530
1.00
14.12
H


ATOM
3109
CG
HIS
H
31
−14.089
12.735
−26.899
1.00
14.52
H


ATOM
3110
CD2
HIS
H
31
−14.314
13.900
−26.247
1.00
14.13
H


ATOM
3111
ND1
HIS
H
31
−15.279
12.046
−26.883
1.00
13.70
H


ATOM
3112
CE1
HIS
H
31
−16.190
12.761
−26.244
1.00
15.24
H


ATOM
3113
NE2
HIS
H
31
−15.628
13.888
−25.850
1.00
14.50
H


ATOM
3114
C
HIS
H
31
−10.408
12.073
−27.426
1.00
12.58
H


ATOM
3115
O
HIS
H
31
−10.392
10.995
−26.834
1.00
14.16
H


ATOM
3116
N
HIS
H
32
−9.434
12.467
−28.229
1.00
12.49
H


ATOM
3117
CA
HIS
H
32
−8.304
11.585
−28.478
1.00
12.89
H


ATOM
3118
CB
HIS
H
32
−8.545
10.851
−29.808
1.00
13.05
H


ATOM
3119
CG
HIS
H
32
−9.697
9.889
−29.761
1.00
12.70
H


ATOM
3120
CD2
HIS
H
32
−10.988
10.023
−30.149
1.00
12.40
H


ATOM
3121
ND1
HIS
H
32
−9.592
8.631
−29.209
1.00
12.19
H


ATOM
3122
CE1
HIS
H
32
−10.768
8.029
−29.258
1.00
13.35
H


ATOM
3123
NE2
HIS
H
32
−11.633
8.852
−29.822
1.00
12.35
H


ATOM
3124
C
HIS
H
32
−6.976
12.326
−28.504
1.00
12.49
H


ATOM
3125
O
HIS
H
32
−6.920
13.476
−28.918
1.00
14.67
H


ATOM
3126
N
GLY
H
33
−5.914
11.687
−28.026
1.00
11.48
H


ATOM
3127
CA
GLY
H
33
−4.611
12.327
−28.063
1.00
10.32
H


ATOM
3128
C
GLY
H
33
−4.052
12.137
−29.461
1.00
8.82
H


ATOM
3129
O
GLY
H
33
−4.339
11.127
−30.101
1.00
10.42
H


ATOM
3130
N
MET
H
34
−3.276
13.086
−29.965
1.00
7.85
H


ATOM
3131
CA
MET
H
34
−2.721
12.935
−31.320
1.00
6.64
H


ATOM
3132
CB
MET
H
34
−3.173
14.090
−32.218
1.00
4.40
H


ATOM
3133
CG
MET
H
34
−4.710
14.204
−32.374
1.00
4.44
H


ATOM
3134
SD
MET
H
34
−5.426
12.756
−33.283
1.00
3.13
H


ATOM
3135
CE
MET
H
34
−4.669
12.931
−34.869
1.00
3.16
H


ATOM
3136
C
MET
H
34
−1.201
12.896
−31.281
1.00
6.08
H


ATOM
3137
O
MET
H
34
−0.575
13.439
−30.381
1.00
5.25
H


ATOM
3138
N
THR
H
35
−0.607
12.267
−32.274
1.00
6.01
H


ATOM
3139
CA
THR
H
35
0.828
12.175
−32.290
1.00
7.01
H


ATOM
3140
CB
THR
H
35
1.292
10.851
−31.608
1.00
9.35
H


ATOM
3141
OG1
THR
H
35
2.719
10.707
−31.709
1.00
10.60
H


ATOM
3142
CG2
THR
H
35
0.633
9.661
−32.289
1.00
10.35
H


ATOM
3143
C
THR
H
35
1.383
12.231
−33.710
1.00
5.93
H


ATOM
3144
O
THR
H
35
0.672
11.965
−34.690
1.00
4.87
H


ATOM
3145
N
TRP
H
36
2.659
12.591
−33.812
1.00
5.33
H


ATOM
3146
CA
TRP
H
36
3.335
12.655
−35.097
1.00
3.82
H


ATOM
3147
CB
TRP
H
36
4.005
14.005
−35.327
1.00
1.93
H


ATOM
3148
CG
TRP
H
36
3.059
15.064
−35.776
1.00
3.01
H


ATOM
3149
CD2
TRP
H
36
2.500
15.209
−37.090
1.00
2.59
H


ATOM
3150
CE2
TRP
H
36
1.656
16.338
−37.063
1.00
1.00
H


ATOM
3151
CE3
TRP
H
36
2.632
14.491
−38.285
1.00
2.19
H


ATOM
3152
CD1
TRP
H
36
2.540
16.079
−35.029
1.00
1.86
H


ATOM
3153
NE1
TRP
H
36
1.699
16.849
−35.796
1.00
1.16
H


ATOM
3154
CZ2
TRP
H
36
0.953
16.773
−38.178
1.00
1.00
H


ATOM
3155
CZ3
TRP
H
36
1.930
14.923
−39.395
1.00
1.00
H


ATOM
3156
CH2
TRP
H
36
1.100
16.057
−39.334
1.00
1.00
H


ATOM
3157
C
TRP
H
36
4.406
11.617
−35.091
1.00
3.68
H


ATOM
3158
O
TRP
H
36
5.195
11.544
−34.152
1.00
4.93
H


ATOM
3159
N
VAL
H
37
4.429
10.803
−36.130
1.00
3.07
H


ATOM
3160
CA
VAL
H
37
5.465
9.794
−36.254
1.00
4.69
H


ATOM
3161
CB
VAL
H
37
4.895
8.340
−36.114
1.00
5.17
H


ATOM
3162
CG1
VAL
H
37
5.994
7.335
−36.345
1.00
4.96
H


ATOM
3163
CG2
VAL
H
37
4.315
8.126
−34.732
1.00
4.23
H


ATOM
3164
C
VAL
H
37
6.075
10.005
−37.645
1.00
4.66
H


ATOM
3165
O
VAL
H
37
5.371
10.340
−38.593
1.00
5.19
H


ATOM
3166
N
ARG
H
38
7.383
9.846
−37.776
1.00
5.35
H


ATOM
3167
CA
ARG
H
38
8.000
10.039
−39.082
1.00
5.57
H


ATOM
3168
CB
ARG
H
38
8.897
11.272
−39.068
1.00
7.67
H


ATOM
3169
CG
ARG
H
38
10.129
11.136
−38.196
1.00
6.25
H


ATOM
3170
CD
ARG
H
38
10.940
12.385
−38.305
1.00
6.36
H


ATOM
3171
NE
ARG
H
38
12.058
12.368
−37.388
1.00
9.42
H


ATOM
3172
CZ
ARG
H
38
12.969
13.319
−37.330
1.00
8.80
H


ATOM
3173
NH1
ARG
H
38
12.879
14.351
−38.151
1.00
9.68
H


ATOM
3174
NH2
ARG
H
38
13.947
13.249
−36.439
1.00
9.99
H


ATOM
3175
C
ARG
H
38
8.822
8.842
−39.497
1.00
4.93
H


ATOM
3176
O
ARG
H
38
9.135
7.964
−38.693
1.00
4.06
H


ATOM
3177
N
GLN
H
39
9.203
8.840
−40.759
1.00
5.54
H


ATOM
3178
CA
GLN
H
39
9.986
7.751
−41.295
1.00
7.45
H


ATOM
3179
CB
GLN
H
39
9.056
6.716
−41.914
1.00
6.58
H


ATOM
3180
CG
GLN
H
39
9.751
5.495
−42.440
1.00
6.23
H


ATOM
3181
CD
GLN
H
39
8.780
4.490
−42.991
1.00
7.57
H


ATOM
3182
OE1
GLN
H
39
8.002
4.790
−43.895
1.00
9.72
H


ATOM
3183
NE2
GLN
H
39
8.809
3.288
−42.446
1.00
7.92
H


ATOM
3184
C
GLN
H
39
10.949
8.280
−42.342
1.00
8.66
H


ATOM
3185
O
GLN
H
39
10.532
8.690
−43.433
1.00
9.98
H


ATOM
3186
N
ALA
H
40
12.237
8.275
−42.001
1.00
10.55
H


ATOM
3187
CA
ALA
H
40
13.281
8.761
−42.901
1.00
11.32
H


ATOM
3188
CB
ALA
H
40
14.598
8.882
−42.161
1.00
9.49
H


ATOM
3189
C
ALA
H
40
13.412
7.792
−44.062
1.00
12.45
H


ATOM
3190
O
ALA
H
40
13.185
6.595
−43.904
1.00
12.06
H


ATOM
3191
N
PRO
H
41
13.774
8.298
−45.250
1.00
14.18
H


ATOM
3192
CD
PRO
H
41
14.084
9.704
−45.562
1.00
13.94
H


ATOM
3193
CA
PRO
H
41
13.926
7.458
−46.440
1.00
14.90
H


ATOM
3194
CB
PRO
H
41
14.757
8.333
−47.364
1.00
13.64
H


ATOM
3195
CG
PRO
H
41
14.172
9.691
−47.081
1.00
13.81
H


ATOM
3196
C
PRO
H
41
14.565
6.108
−46.165
1.00
16.86
H


ATOM
3197
O
PRO
H
41
15.683
6.018
−45.644
1.00
16.32
H


ATOM
3198
N
GLY
H
42
13.830
5.053
−46.508
1.00
18.46
H


ATOM
3199
CA
GLY
H
42
14.317
3.699
−46.294
1.00
19.28
H


ATOM
3200
C
GLY
H
42
14.764
3.427
−44.863
1.00
20.26
H


ATOM
3201
O
GLY
H
42
15.795
2.798
−44.637
1.00
21.03
H


ATOM
3202
N
LYS
H
43
14.000
3.899
−43.884
1.00
20.62
H


ATOM
3203
CA
LYS
H
43
14.351
3.665
−42.487
1.00
19.70
H


ATOM
3204
CB
LYS
H
43
14.981
4.923
−41.890
1.00
20.93
H


ATOM
3205
CG
LYS
H
43
16.185
5.411
−42.686
1.00
22.44
H


ATOM
3206
CD
LYS
H
43
17.345
4.434
−42.632
1.00
23.53
H


ATOM
3207
CE
LYS
H
43
17.977
4.468
−41.247
1.00
27.18
H


ATOM
3208
NZ
LYS
H
43
19.111
3.504
−41.050
1.00
28.98
H


ATOM
3209
C
LYS
H
43
13.071
3.280
−41.758
1.00
17.81
H


ATOM
3210
O
LYS
H
43
11.991
3.297
−42.361
1.00
17.97
H


ATOM
3211
N
GLY
H
44
13.189
2.923
−40.483
1.00
15.15
H


ATOM
3212
CA
GLY
H
44
12.023
2.520
−39.718
1.00
13.55
H


ATOM
3213
C
GLY
H
44
11.220
3.666
−39.138
1.00
12.70
H


ATOM
3214
O
GLY
H
44
11.564
4.831
−39.331
1.00
13.60
H


ATOM
3215
N
LEU
H
45
10.150
3.342
−38.418
1.00
10.34
H


ATOM
3216
CA
LEU
H
45
9.312
4.371
−37.823
1.00
8.11
H


ATOM
3217
CB
LEU
H
45
8.006
3.765
−37.319
1.00
6.67
H


ATOM
3218
CG
LEU
H
45
7.016
3.285
−38.384
1.00
6.00
H


ATOM
3219
CD1
LEU
H
45
5.807
2.634
−37.700
1.00
6.82
H


ATOM
3220
CD2
LEU
H
45
6.567
4.447
−39.220
1.00
4.53
H


ATOM
3221
C
LEU
H
45
10.010
5.088
−36.680
1.00
8.20
H


ATOM
3222
O
LEU
H
45
10.840
4.514
−35.975
1.00
8.35
H


ATOM
3223
N
GLU
H
46
9.683
6.361
−36.516
1.00
6.89
H


ATOM
3224
CA
GLU
H
46
10.261
7.134
−35.440
1.00
5.45
H


ATOM
3225
CB
GLU
H
46
11.459
7.906
−35.946
1.00
6.53
H


ATOM
3226
CG
GLU
H
46
12.370
8.384
−34.853
1.00
8.96
H


ATOM
3227
CD
GLU
H
46
13.090
9.655
−35.223
1.00
11.41
H


ATOM
3228
OE1
GLU
H
46
13.534
9.759
−36.407
1.00
7.77
H


ATOM
3229
OE2
GLU
H
46
13.211
10.539
−34.320
1.00
13.45
H


ATOM
3230
C
GLU
H
46
9.241
8.109
−34.864
1.00
5.60
H


ATOM
3231
O
GLU
H
46
8.712
8.967
−35.575
1.00
6.68
H


ATOM
3232
N
TRP
H
47
8.978
7.981
−33.571
1.00
4.36
H


ATOM
3233
CA
TRP
H
47
8.028
8.841
−32.886
1.00
3.67
H


ATOM
3234
CB
TRP
H
47
7.788
8.320
−31.481
1.00
4.95
H


ATOM
3235
CG
TRP
H
47
6.989
9.246
−30.659
1.00
4.60
H


ATOM
3236
CD2
TRP
H
47
7.482
10.057
−29.587
1.00
4.44
H


ATOM
3237
CE2
TRP
H
47
6.387
10.818
−29.102
1.00
4.11
H


ATOM
3238
CE3
TRP
H
47
8.748
10.217
−28.989
1.00
2.69
H


ATOM
3239
CD1
TRP
H
47
5.649
9.529
−30.784
1.00
3.52
H


ATOM
3240
NE1
TRP
H
47
5.285
10.475
−29.846
1.00
5.11
H


ATOM
3241
CZ2
TRP
H
47
6.520
11.730
−28.042
1.00
1.81
H


ATOM
3242
CZ3
TRP
H
47
8.883
11.122
−27.938
1.00
1.00
H


ATOM
3243
CH2
TRP
H
47
7.770
11.869
−27.475
1.00
1.00
H


ATOM
3244
C
TRP
H
47
8.579
10.237
−32.816
1.00
2.64
H


ATOM
3245
O
TRP
H
47
9.745
10.425
−32.486
1.00
5.55
H


ATOM
3246
N
VAL
H
48
7.744
11.227
−33.084
1.00
2.44
H


ATOM
3247
CA
VAL
H
48
8.222
12.605
−33.075
1.00
1.81
H


ATOM
3248
CB
VAL
H
48
7.825
13.292
−34.408
1.00
1.31
H


ATOM
3249
CG1
VAL
H
48
8.401
14.689
−34.498
1.00
1.00
H


ATOM
3250
CG2
VAL
H
48
8.286
12.444
−35.562
1.00
1.00
H


ATOM
3251
C
VAL
H
48
7.708
13.413
−31.883
1.00
3.22
H


ATOM
3252
O
VAL
H
48
8.488
13.833
−31.032
1.00
2.46
H


ATOM
3253
N
ALA
H
49
6.398
13.621
−31.823
1.00
3.27
H


ATOM
3254
CA
ALA
H
49
5.802
14.384
−30.745
1.00
4.78
H


ATOM
3255
CB
ALA
H
49
5.819
15.866
−31.110
1.00
3.76
H


ATOM
3256
C
ALA
H
49
4.356
13.912
−30.505
1.00
5.83
H


ATOM
3257
O
ALA
H
49
3.700
13.365
−31.406
1.00
4.82
H


ATOM
3258
N
SER
H
50
3.874
14.135
−29.285
1.00
4.82
H


ATOM
3259
CA
SER
H
50
2.526
13.768
−28.922
1.00
4.97
H


ATOM
3260
CB
SER
H
50
2.516
12.512
−28.059
1.00
5.14
H


ATOM
3261
OG
SER
H
50
2.568
11.365
−28.878
1.00
6.92
H


ATOM
3262
C
SER
H
50
1.815
14.898
−28.220
1.00
5.98
H


ATOM
3263
O
SER
H
50
2.435
15.801
−27.670
1.00
5.57
H


ATOM
3264
N
LEU
H
51
0.495
14.816
−28.224
1.00
7.39
H


ATOM
3265
CA
LEU
H
51
−0.340
15.847
−27.652
1.00
8.22
H


ATOM
3266
CB
LEU
H
51
−0.651
16.828
−28.769
1.00
9.05
H


ATOM
3267
CG
LEU
H
51
−1.506
18.005
−28.376
1.00
10.34
H


ATOM
3268
CD1
LEU
H
51
−0.678
18.875
−27.452
1.00
11.80
H


ATOM
3269
CD2
LEU
H
51
−1.934
18.776
−29.592
1.00
10.62
H


ATOM
3270
C
LEU
H
51
−1.646
15.252
−27.116
1.00
9.09
H


ATOM
3271
O
LEU
H
51
−2.244
14.386
−27.757
1.00
11.36
H


ATOM
3272
N
SER
H
52
−2.112
15.730
−25.970
1.00
7.37
H


ATOM
3273
CA
SER
H
52
−3.364
15.220
−25.428
1.00
7.34
H


ATOM
3274
CB
SER
H
52
−3.453
15.487
−23.920
1.00
6.67
H


ATOM
3275
OG
SER
H
52
−3.234
16.851
−23.580
1.00
6.96
H


ATOM
3276
C
SER
H
52
−4.573
15.823
−26.142
1.00
8.92
H


ATOM
3277
O
SER
H
52
−4.423
16.691
−27.009
1.00
9.13
H


ATOM
3278
N
GLY
H
53
−5.769
15.369
−25.764
1.00
8.62
H


ATOM
3279
CA
GLY
H
53
−6.986
15.856
−26.388
1.00
6.90
H


ATOM
3280
C
GLY
H
53
−7.165
17.339
−26.198
1.00
5.00
H


ATOM
3281
O
GLY
H
53
−7.542
18.062
−27.120
1.00
4.67
H


ATOM
3282
N
SER
H
54
−6.900
17.800
−24.990
1.00
4.14
H


ATOM
3283
CA
SER
H
54
−7.025
19.224
−24.690
1.00
6.17
H


ATOM
3284
CB
SER
H
54
−7.028
19.434
−23.173
1.00
6.62
H


ATOM
3285
OG
SER
H
54
−5.841
18.929
−22.561
1.00
4.64
H


ATOM
3286
C
SER
H
54
−5.842
19.957
−25.320
1.00
7.53
H


ATOM
3287
O
SER
H
54
−5.965
21.101
−25.751
1.00
6.08
H


ATOM
3288
N
GLY
H
55
−4.697
19.277
−25.368
1.00
8.59
H


ATOM
3289
CA
GLY
H
55
−3.516
19.868
−25.956
1.00
9.92
H


ATOM
3290
C
GLY
H
55
−2.648
20.537
−24.916
1.00
10.79
H


ATOM
3291
O
GLY
H
55
−1.634
21.174
−25.232
1.00
8.31
H


ATOM
3292
N
THR
H
56
−3.050
20.398
−23.659
1.00
12.24
H


ATOM
3293
CA
THR
H
56
−2.303
20.999
−22.558
1.00
12.50
H


ATOM
3294
CB
THR
H
56
−3.195
21.164
−21.302
1.00
11.85
H


ATOM
3295
OG1
THR
H
56
−3.497
19.879
−20.739
1.00
11.11
H


ATOM
3296
CG2
THR
H
56
−4.483
21.866
−21.670
1.00
11.04
H


ATOM
3297
C
THR
H
56
−1.089
20.152
−22.191
1.00
11.96
H


ATOM
3298
O
THR
H
56
−0.203
20.601
−21.466
1.00
11.88
H


ATOM
3299
N
LYS
H
57
−1.052
18.924
−22.695
1.00
11.02
H


ATOM
3300
CA
LYS
H
57
0.062
18.047
−22.407
1.00
9.97
H


ATOM
3301
CB
LYS
H
57
−0.400
16.818
−21.626
1.00
8.17
H


ATOM
3302
CG
LYS
H
57
−1.011
17.145
−20.277
1.00
9.71
H


ATOM
3303
CD
LYS
H
57
−1.297
15.893
−19.467
1.00
10.00
H


ATOM
3304
CE
LYS
H
57
−2.760
15.785
−19.084
1.00
11.05
H


ATOM
3305
NZ
LYS
H
57
−3.188
16.841
−18.138
1.00
12.83
H


ATOM
3306
C
LYS
H
57
0.698
17.628
−23.707
1.00
9.96
H


ATOM
3307
O
LYS
H
57
0.085
16.933
−24.507
1.00
11.40
H


ATOM
3308
N
THR
H
58
1.930
18.069
−23.929
1.00
9.40
H


ATOM
3309
CA
THR
H
58
2.626
17.714
−25.154
1.00
8.99
H


ATOM
3310
CB
THR
H
58
2.922
18.939
−26.023
1.00
8.49
H


ATOM
3311
OG1
THR
H
58
4.147
19.530
−25.596
1.00
9.58
H


ATOM
3312
CG2
THR
H
58
1.826
19.960
−25.889
1.00
6.38
H


ATOM
3313
C
THR
H
58
3.938
17.060
−24.777
1.00
9.30
H


ATOM
3314
O
THR
H
58
4.415
17.236
−23.663
1.00
8.22
H


ATOM
3315
N
HIS
H
59
4.508
16.305
−25.717
1.00
9.24
H


ATOM
3316
CA
HIS
H
59
5.769
15.595
−25.519
1.00
8.03
H


ATOM
3317
CB
HIS
H
59
5.499
14.189
−24.981
1.00
11.10
H


ATOM
3318
CG
HIS
H
59
5.068
14.158
−23.547
1.00
14.76
H


ATOM
3319
CD2
HIS
H
59
3.838
14.042
−22.991
1.00
16.75
H


ATOM
3320
ND1
HIS
H
59
5.960
14.219
−22.500
1.00
15.55
H


ATOM
3321
CE1
HIS
H
59
5.300
14.135
−21.355
1.00
16.99
H


ATOM
3322
NE2
HIS
H
59
4.012
14.026
−21.626
1.00
16.44
H


ATOM
3323
C
HIS
H
59
6.534
15.505
−26.841
1.00
6.73
H


ATOM
3324
O
HIS
H
59
5.947
15.238
−27.892
1.00
4.86
H


ATOM
3325
N
PHE
H
60
7.844
15.735
−26.776
1.00
6.24
H


ATOM
3326
CA
PHE
H
60
8.691
15.707
−27.963
1.00
6.73
H


ATOM
3327
CB
PHE
H
60
9.258
17.098
−28.259
1.00
6.25
H


ATOM
3328
CG
PHE
H
60
8.223
18.165
−28.368
1.00
8.88
H


ATOM
3329
CD1
PHE
H
60
7.732
18.795
−27.226
1.00
10.51
H


ATOM
3330
CD2
PHE
H
60
7.700
18.516
−29.604
1.00
10.03
H


ATOM
3331
CE1
PHE
H
60
6.724
19.760
−27.311
1.00
9.17
H


ATOM
3332
CE2
PHE
H
60
6.697
19.474
−29.701
1.00
10.91
H


ATOM
3333
CZ
PHE
H
60
6.207
20.099
−28.543
1.00
11.27
H


ATOM
3334
C
PHE
H
60
9.851
14.743
−27.810
1.00
6.57
H


ATOM
3335
O
PHE
H
60
10.119
14.263
−26.720
1.00
6.46
H


ATOM
3336
N
ALA
H
61
10.524
14.469
−28.922
1.00
8.14
H


ATOM
3337
CA
ALA
H
61
11.684
13.589
−28.956
1.00
10.25
H


ATOM
3338
CB
ALA
H
61
11.711
12.818
−30.262
1.00
9.23
H


ATOM
3339
C
ALA
H
61
12.891
14.521
−28.863
1.00
11.89
H


ATOM
3340
O
ALA
H
61
12.857
15.623
−29.413
1.00
13.75
H


ATOM
3341
N
ASP
H
62
13.953
14.094
−28.188
1.00
13.51
H


ATOM
3342
CA
ASP
H
62
15.124
14.953
−28.047
1.00
15.64
H


ATOM
3343
CB
ASP
H
62
16.236
14.230
−27.277
1.00
18.66
H


ATOM
3344
CG
ASP
H
62
16.077
14.365
−25.771
1.00
23.55
H


ATOM
3345
OD1
ASP
H
62
16.797
13.650
−25.022
1.00
26.30
H


ATOM
3346
OD2
ASP
H
62
15.234
15.197
−25.333
1.00
25.44
H


ATOM
3347
C
ASP
H
62
15.657
15.493
−29.364
1.00
14.78
H


ATOM
3348
O
ASP
H
62
15.992
16.672
−29.464
1.00
16.08
H


ATOM
3349
N
SER
H
63
15.706
14.648
−30.379
1.00
13.12
H


ATOM
3350
CA
SER
H
63
16.222
15.072
−31.667
1.00
13.50
H


ATOM
3351
CB
SER
H
63
16.283
13.885
−32.615
1.00
14.56
H


ATOM
3352
OG
SER
H
63
14.980
13.365
−32.822
1.00
18.30
H


ATOM
3353
C
SER
H
63
15.397
16.165
−32.326
1.00
13.14
H


ATOM
3354
O
SER
H
63
15.734
16.635
−33.411
1.00
12.97
H


ATOM
3355
N
VAL
H
64
14.325
16.594
−31.686
1.00
12.76
H


ATOM
3356
CA
VAL
H
64
13.498
17.595
−32.324
1.00
13.21
H


ATOM
3357
CB
VAL
H
64
12.316
16.857
−33.044
1.00
12.72
H


ATOM
3358
CG1
VAL
H
64
10.991
17.103
−32.335
1.00
13.63
H


ATOM
3359
CG2
VAL
H
64
12.269
17.237
−34.479
1.00
10.90
H


ATOM
3360
C
VAL
H
64
13.021
18.673
−31.340
1.00
13.76
H


ATOM
3361
O
VAL
H
64
12.543
19.749
−31.732
1.00
11.87
H


ATOM
3362
N
LYS
H
65
13.172
18.384
−30.052
1.00
16.05
H


ATOM
3363
CA
LYS
H
65
12.772
19.323
−29.013
1.00
17.75
H


ATOM
3364
CB
LYS
H
65
13.103
18.787
−27.617
1.00
20.48
H


ATOM
3365
CG
LYS
H
65
12.768
19.806
−26.531
1.00
24.24
H


ATOM
3366
CD
LYS
H
65
12.539
19.177
−25.177
1.00
26.75
H


ATOM
3367
CE
LYS
H
65
12.065
20.228
−24.186
1.00
29.20
H


ATOM
3368
NZ
LYS
H
65
11.806
19.649
−22.835
1.00
30.30
H


ATOM
3369
C
LYS
H
65
13.467
20.654
−29.196
1.00
16.93
H


ATOM
3370
O
LYS
H
65
14.672
20.707
−29.452
1.00
17.42
H


ATOM
3371
N
GLY
H
66
12.701
21.725
−29.040
1.00
15.98
H


ATOM
3372
CA
GLY
H
66
13.255
23.047
−29.210
1.00
15.03
H


ATOM
3373
C
GLY
H
66
13.106
23.481
−30.652
1.00
15.31
H


ATOM
3374
O
GLY
H
66
13.118
24.669
−30.945
1.00
17.76
H


ATOM
3375
N
ARG
H
67
12.972
22.540
−31.574
1.00
12.33
H


ATOM
3376
CA
ARG
H
67
12.823
22.955
−32.950
1.00
11.57
H


ATOM
3377
CB
ARG
H
67
13.784
22.198
−33.856
1.00
11.70
H


ATOM
3378
CG
ARG
H
67
15.254
22.497
−33.600
1.00
9.21
H


ATOM
3379
CD
ARG
H
67
16.113
21.818
−34.641
1.00
6.92
H


ATOM
3380
NE
ARG
H
67
15.869
20.379
−34.681
1.00
6.37
H


ATOM
3381
CZ
ARG
H
67
15.526
19.713
−35.778
1.00
7.25
H


ATOM
3382
NH1
ARG
H
67
15.386
20.350
−36.934
1.00
9.14
H


ATOM
3383
NH2
ARG
H
67
15.300
18.413
−35.719
1.00
6.47
H


ATOM
3384
C
ARG
H
67
11.402
22.732
−33.415
1.00
12.38
H


ATOM
3385
O
ARG
H
67
10.849
23.543
−34.143
1.00
13.55
H


ATOM
3386
N
PHE
H
68
10.804
21.632
−32.983
1.00
12.18
H


ATOM
3387
CA
PHE
H
68
9.448
21.319
−33.381
1.00
11.31
H


ATOM
3388
CB
PHE
H
68
9.351
19.850
−33.769
1.00
11.86
H


ATOM
3389
CG
PHE
H
68
9.971
19.516
−35.099
1.00
12.06
H


ATOM
3390
CD1
PHE
H
68
10.973
20.313
−35.653
1.00
11.71
H


ATOM
3391
CD2
PHE
H
68
9.583
18.351
−35.776
1.00
11.05
H


ATOM
3392
CE1
PHE
H
68
11.584
19.953
−36.859
1.00
11.42
H


ATOM
3393
CE2
PHE
H
68
10.186
17.981
−36.980
1.00
9.57
H


ATOM
3394
CZ
PHE
H
68
11.188
18.779
−37.527
1.00
9.82
H


ATOM
3395
C
PHE
H
68
8.436
21.611
−32.291
1.00
12.02
H


ATOM
3396
O
PHE
H
68
8.684
21.376
−31.110
1.00
12.67
H


ATOM
3397
N
THR
H
69
7.283
22.127
−32.693
1.00
11.69
H


ATOM
3398
CA
THR
H
69
6.233
22.416
−31.735
1.00
10.64
H


ATOM
3399
CB
THR
H
69
6.103
23.948
−31.456
1.00
10.59
H


ATOM
3400
OG1
THR
H
69
4.719
24.297
−31.351
1.00
14.40
H


ATOM
3401
CG2
THR
H
69
6.737
24.771
−32.569
1.00
11.79
H


ATOM
3402
C
THR
H
69
4.910
21.841
−32.244
1.00
9.62
H


ATOM
3403
O
THR
H
69
4.450
22.170
−33.337
1.00
9.39
H


ATOM
3404
N
ILE
H
70
4.316
20.962
−31.440
1.00
7.95
H


ATOM
3405
CA
ILE
H
70
3.044
20.325
−31.773
1.00
6.64
H


ATOM
3406
CB
ILE
H
70
2.937
18.914
−31.124
1.00
5.97
H


ATOM
3407
CG2
ILE
H
70
2.930
19.046
−29.621
1.00
3.75
H


ATOM
3408
CG1
ILE
H
70
1.667
18.200
−31.605
1.00
5.93
H


ATOM
3409
CD1
ILE
H
70
1.677
16.710
−31.399
1.00
5.04
H


ATOM
3410
C
ILE
H
70
1.897
21.189
−31.254
1.00
5.92
H


ATOM
3411
O
ILE
H
70
2.041
21.831
−30.219
1.00
7.78
H


ATOM
3412
N
SER
H
71
0.775
21.205
−31.970
1.00
4.08
H


ATOM
3413
CA
SER
H
71
−0.408
21.972
−31.570
1.00
3.29
H


ATOM
3414
CB
SER
H
71
−0.267
23.449
−31.943
1.00
1.76
H


ATOM
3415
OG
SER
H
71
0.300
23.593
−33.232
1.00
5.75
H


ATOM
3416
C
SER
H
71
−1.645
21.384
−32.230
1.00
2.94
H


ATOM
3417
O
SER
H
71
−1.545
20.614
−33.185
1.00
1.59
H


ATOM
3418
N
ARG
H
72
−2.812
21.764
−31.728
1.00
3.54
H


ATOM
3419
CA
ARG
H
72
−4.081
21.231
−32.216
1.00
4.48
H


ATOM
3420
CB
ARG
H
72
−4.441
20.016
−31.343
1.00
4.63
H


ATOM
3421
CG
ARG
H
72
−5.849
19.970
−30.810
1.00
5.35
H


ATOM
3422
CD
ARG
H
72
−5.940
19.277
−29.466
1.00
4.98
H


ATOM
3423
NE
ARG
H
72
−5.546
17.865
−29.437
1.00
6.58
H


ATOM
3424
CZ
ARG
H
72
−6.289
16.841
−29.867
1.00
7.67
H


ATOM
3425
NH1
ARG
H
72
−7.484
17.035
−30.386
1.00
7.98
H


ATOM
3426
NH2
ARG
H
72
−5.854
15.598
−29.742
1.00
9.34
H


ATOM
3427
C
ARG
H
72
−5.167
22.289
−32.161
1.00
5.09
H


ATOM
3428
O
ARG
H
72
−5.086
23.194
−31.351
1.00
5.98
H


ATOM
3429
N
ASP
H
73
−6.164
22.196
−33.036
1.00
7.54
H


ATOM
3430
CA
ASP
H
73
−7.261
23.166
−33.032
1.00
10.50
H


ATOM
3431
CB
ASP
H
73
−7.214
24.030
−34.297
1.00
12.67
H


ATOM
3432
CG
ASP
H
73
−8.309
25.111
−34.327
1.00
13.54
H


ATOM
3433
OD1
ASP
H
73
−9.429
24.831
−33.863
1.00
12.69
H


ATOM
3434
OD2
ASP
H
73
−8.049
26.231
−34.832
1.00
14.66
H


ATOM
3435
C
ASP
H
73
−8.613
22.447
−32.957
1.00
11.07
H


ATOM
3436
O
ASP
H
73
−9.191
22.093
−33.983
1.00
11.19
H


ATOM
3437
N
ASN
H
74
−9.122
22.262
−31.748
1.00
11.92
H


ATOM
3438
CA
ASN
H
74
−10.390
21.589
−31.565
1.00
13.93
H


ATOM
3439
CB
ASN
H
74
−10.538
21.139
−30.115
1.00
13.39
H


ATOM
3440
CG
ASN
H
74
−9.502
20.112
−29.727
1.00
15.07
H


ATOM
3441
OD1
ASN
H
74
−9.020
19.368
−30.581
1.00
15.70
H


ATOM
3442
ND2
ASN
H
74
−9.163
20.045
−28.444
1.00
14.48
H


ATOM
3443
C
ASN
H
74
−11.579
22.456
−31.962
1.00
16.05
H


ATOM
3444
O
ASN
H
74
−12.340
22.924
−31.116
1.00
18.94
H


ATOM
3445
N
SER
H
75
−11.727
22.683
−33.257
1.00
16.45
H


ATOM
3446
CA
SER
H
75
−12.820
23.484
−33.786
1.00
16.17
H


ATOM
3447
CB
SER
H
75
−12.491
24.974
−33.745
1.00
17.32
H


ATOM
3448
OG
SER
H
75
−11.878
25.333
−32.521
1.00
20.43
H


ATOM
3449
C
SER
H
75
−12.884
23.070
−35.223
1.00
17.41
H


ATOM
3450
O
SER
H
75
−13.954
22.830
−35.774
1.00
19.91
H


ATOM
3451
N
ASN
H
76
−11.703
22.992
−35.825
1.00
16.64
H


ATOM
3452
CA
ASN
H
76
−11.568
22.611
−37.217
1.00
15.45
H


ATOM
3453
CB
ASN
H
76
−10.637
23.590
−37.947
1.00
17.04
H


ATOM
3454
CG
ASN
H
76
−9.302
23.775
−37.232
1.00
20.41
H


ATOM
3455
OD1
ASN
H
76
−8.938
23.003
−36.336
1.00
21.95
H


ATOM
3456
ND2
ASN
H
76
−8.558
24.796
−37.636
1.00
21.39
H


ATOM
3457
C
ASN
H
76
−11.019
21.196
−37.340
1.00
13.63
H


ATOM
3458
O
ASN
H
76
−10.672
20.771
−38.436
1.00
11.77
H


ATOM
3459
N
ASN
H
77
−10.934
20.479
−36.222
1.00
11.14
H


ATOM
3460
CA
ASN
H
77
−10.419
19.112
−36.239
1.00
11.22
H


ATOM
3461
CB
ASN
H
77
−11.383
18.193
−36.977
1.00
12.73
H


ATOM
3462
CG
ASN
H
77
−12.674
17.980
−36.224
1.00
16.20
H


ATOM
3463
OD1
ASN
H
77
−13.517
17.176
−36.630
1.00
17.08
H


ATOM
3464
ND2
ASN
H
77
−12.840
18.702
−35.109
1.00
18.52
H


ATOM
3465
C
ASN
H
77
−9.064
19.001
−36.919
1.00
11.03
H


ATOM
3466
O
ASN
H
77
−8.846
18.114
−37.748
1.00
10.80
H


ATOM
3467
N
THR
H
78
−8.157
19.900
−36.565
1.00
8.71
H


ATOM
3468
CA
THR
H
78
−6.852
19.919
−37.178
1.00
7.47
H


ATOM
3469
CB
THR
H
78
−6.651
21.223
−37.953
1.00
9.54
H


ATOM
3470
OG1
THR
H
78
−7.779
21.447
−38.801
1.00
11.42
H


ATOM
3471
CG2
THR
H
78
−5.401
21.149
−38.813
1.00
9.06
H


ATOM
3472
C
THR
H
78
−5.704
19.757
−36.208
1.00
7.12
H


ATOM
3473
O
THR
H
78
−5.692
20.332
−35.119
1.00
4.88
H


ATOM
3474
N
LEU
H
79
−4.728
18.959
−36.626
1.00
6.47
H


ATOM
3475
CA
LEU
H
79
−3.548
18.700
−35.823
1.00
6.13
H


ATOM
3476
CB
LEU
H
79
−3.339
17.188
−35.672
1.00
3.73
H


ATOM
3477
CG
LEU
H
79
−2.217
16.691
−34.754
1.00
2.93
H


ATOM
3478
CD1
LEU
H
79
−0.978
16.427
−35.533
1.00
1.00
H


ATOM
3479
CD2
LEU
H
79
−1.970
17.684
−33.647
1.00
2.62
H


ATOM
3480
C
LEU
H
79
−2.385
19.345
−36.562
1.00
6.55
H


ATOM
3481
O
LEU
H
79
−2.199
19.119
−37.743
1.00
6.69
H


ATOM
3482
N
TYR
H
80
−1.621
20.167
−35.863
1.00
6.40
H


ATOM
3483
CA
TYR
H
80
−0.495
20.836
−36.469
1.00
7.17
H


ATOM
3484
CB
TYR
H
80
−0.607
22.341
−36.206
1.00
6.40
H


ATOM
3485
CG
TYR
H
80
−1.840
22.956
−36.818
1.00
7.53
H


ATOM
3486
CD1
TYR
H
80
−1.955
23.089
−38.195
1.00
7.52
H


ATOM
3487
CE1
TYR
H
80
−3.110
23.592
−38.784
1.00
7.14
H


ATOM
3488
CD2
TYR
H
80
−2.920
23.351
−36.028
1.00
7.68
H


ATOM
3489
CE2
TYR
H
80
−4.083
23.855
−36.607
1.00
8.61
H


ATOM
3490
CZ
TYR
H
80
−4.169
23.970
−37.994
1.00
8.93
H


ATOM
3491
OH
TYR
H
80
−5.332
24.446
−38.576
1.00
10.76
H


ATOM
3492
C
TYR
H
80
0.859
20.317
−35.945
1.00
9.01
H


ATOM
3493
O
TYR
H
80
0.945
19.633
−34.909
1.00
7.86
H


ATOM
3494
N
LEU
H
81
1.906
20.667
−36.691
1.00
9.72
H


ATOM
3495
CA
LEU
H
81
3.289
20.356
−36.370
1.00
9.06
H


ATOM
3496
CB
LEU
H
81
3.706
18.993
−36.914
1.00
8.70
H


ATOM
3497
CG
LEU
H
81
5.192
18.669
−36.656
1.00
7.92
H


ATOM
3498
CD1
LEU
H
81
5.449
18.645
−35.145
1.00
7.49
H


ATOM
3499
CD2
LEU
H
81
5.574
17.343
−37.284
1.00
3.90
H


ATOM
3500
C
LEU
H
81
4.127
21.444
−37.021
1.00
10.37
H


ATOM
3501
O
LEU
H
81
4.178
21.552
−38.256
1.00
9.62
H


ATOM
3502
N
GLN
H
82
4.756
22.259
−36.172
1.00
11.89
H


ATOM
3503
CA
GLN
H
82
5.627
23.362
−36.590
1.00
12.40
H


ATOM
3504
CB
GLN
H
82
5.477
24.554
−35.643
1.00
11.73
H


ATOM
3505
CG
GLN
H
82
6.116
25.822
−36.160
1.00
13.56
H


ATOM
3506
CD
GLN
H
82
5.432
26.305
−37.406
1.00
13.55
H


ATOM
3507
OE1
GLN
H
82
4.204
26.380
−37.451
1.00
13.14
H


ATOM
3508
NE2
GLN
H
82
6.214
26.645
−38.426
1.00
12.96
H


ATOM
3509
C
GLN
H
82
7.081
22.901
−36.562
1.00
12.65
H


ATOM
3510
O
GLN
H
82
7.633
22.606
−35.497
1.00
11.89
H


ATOM
3511
N
MET
H
83
7.685
22.850
−37.742
1.00
13.04
H


ATOM
3512
CA
MET
H
83
9.072
22.442
−37.893
1.00
13.26
H


ATOM
3513
CB
MET
H
83
9.203
21.476
−39.076
1.00
13.61
H


ATOM
3514
CG
MET
H
83
8.251
20.267
−39.014
1.00
13.89
H


ATOM
3515
SD
MET
H
83
8.630
18.987
−40.303
1.00
10.43
H


ATOM
3516
CE
MET
H
83
7.431
19.442
−41.574
1.00
10.13
H


ATOM
3517
C
MET
H
83
9.944
23.664
−38.135
1.00
12.74
H


ATOM
3518
O
MET
H
83
9.885
24.244
−39.221
1.00
12.35
H


ATOM
3519
N
ASP
H
84
10.726
24.064
−37.129
1.00
12.16
H


ATOM
3520
CA
ASP
H
84
11.614
25.219
−37.276
1.00
13.74
H


ATOM
3521
CB
ASP
H
84
11.416
26.247
−36.155
1.00
15.64
H


ATOM
3522
CG
ASP
H
84
9.972
26.738
−36.035
1.00
19.86
H


ATOM
3523
OD1
ASP
H
84
9.331
27.059
−37.079
1.00
19.64
H


ATOM
3524
OD2
ASP
H
84
9.480
26.817
−34.875
1.00
22.08
H


ATOM
3525
C
ASP
H
84
13.066
24.762
−37.284
1.00
14.11
H


ATOM
3526
O
ASP
H
84
13.414
23.741
−36.691
1.00
13.48
H


ATOM
3527
N
ASN
H
85
13.907
25.541
−37.956
1.00
14.96
H


ATOM
3528
CA
ASN
H
85
15.328
25.250
−38.101
1.00
14.80
H


ATOM
3529
CB
ASN
H
85
16.078
25.539
−36.798
1.00
16.03
H


ATOM
3530
CG
ASN
H
85
17.589
25.441
−36.957
1.00
17.56
H


ATOM
3531
OD1
ASN
H
85
18.199
26.153
−37.758
1.00
20.22
H


ATOM
3532
ND2
ASN
H
85
18.199
24.552
−36.196
1.00
20.29
H


ATOM
3533
C
ASN
H
85
15.508
23.795
−38.510
1.00
14.22
H


ATOM
3534
O
ASN
H
85
16.154
23.012
−37.800
1.00
15.62
H


ATOM
3535
N
VAL
H
86
14.941
23.442
−39.666
1.00
12.38
H


ATOM
3536
CA
VAL
H
86
15.013
22.073
−40.172
1.00
10.44
H


ATOM
3537
CB
VAL
H
86
14.026
21.831
−41.351
1.00
8.45
H


ATOM
3538
CG1
VAL
H
86
12.606
22.045
−40.891
1.00
3.18
H


ATOM
3539
CG2
VAL
H
86
14.357
22.741
−42.521
1.00
8.04
H


ATOM
3540
C
VAL
H
86
16.388
21.635
−40.632
1.00
10.36
H


ATOM
3541
O
VAL
H
86
17.037
22.310
−41.426
1.00
10.28
H


ATOM
3542
N
ARG
H
87
16.819
20.493
−40.116
1.00
11.49
H


ATOM
3543
CA
ARG
H
87
18.094
19.917
−40.487
1.00
13.66
H


ATOM
3544
CB
ARG
H
87
18.714
19.147
−39.319
1.00
14.95
H


ATOM
3545
CG
ARG
H
87
18.626
19.789
−37.937
1.00
17.51
H


ATOM
3546
CD
ARG
H
87
19.444
18.934
−36.976
1.00
19.96
H


ATOM
3547
NE
ARG
H
87
19.129
19.055
−35.552
1.00
22.00
H


ATOM
3548
CZ
ARG
H
87
19.207
20.173
−34.840
1.00
24.13
H


ATOM
3549
NH1
ARG
H
87
19.579
21.315
−35.415
1.00
26.64
H


ATOM
3550
NH2
ARG
H
87
18.951
20.135
−33.537
1.00
23.82
H


ATOM
3551
C
ARG
H
87
17.815
18.929
−41.619
1.00
15.16
H


ATOM
3552
O
ARG
H
87
16.659
18.641
−41.938
1.00
15.01
H


ATOM
3553
N
ASP
H
88
18.881
18.392
−42.201
1.00
17.98
H


ATOM
3554
CA
ASP
H
88
18.781
17.421
−43.289
1.00
20.08
H


ATOM
3555
CB
ASP
H
88
20.197
17.139
−43.812
1.00
23.69
H


ATOM
3556
CG
ASP
H
88
21.061
18.413
−43.875
1.00
29.04
H


ATOM
3557
OD1
ASP
H
88
20.911
19.212
−44.842
1.00
30.25
H


ATOM
3558
OD2
ASP
H
88
21.887
18.620
−42.944
1.00
31.49
H


ATOM
3559
C
ASP
H
88
18.110
16.141
−42.770
1.00
19.34
H


ATOM
3560
O
ASP
H
88
17.316
15.507
−43.471
1.00
17.14
H


ATOM
3561
N
GLU
H
89
18.435
15.802
−41.524
1.00
20.05
H


ATOM
3562
CA
GLU
H
89
17.928
14.626
−40.835
1.00
20.41
H


ATOM
3563
CB
GLU
H
89
18.623
14.491
−39.484
1.00
23.61
H


ATOM
3564
CG
GLU
H
89
20.141
14.591
−39.567
1.00
30.26
H


ATOM
3565
CD
GLU
H
89
20.637
16.031
−39.604
1.00
33.35
H


ATOM
3566
OE1
GLU
H
89
20.360
16.764
−38.625
1.00
36.26
H


ATOM
3567
OE2
GLU
H
89
21.304
16.423
−40.595
1.00
34.20
H


ATOM
3568
C
GLU
H
89
16.415
14.647
−40.636
1.00
18.53
H


ATOM
3569
O
GLU
H
89
15.821
13.677
−40.171
1.00
18.64
H


ATOM
3570
N
ASP
H
90
15.783
15.757
−40.968
1.00
16.04
H


ATOM
3571
CA
ASP
H
90
14.350
15.813
−40.832
1.00
13.47
H


ATOM
3572
CB
ASP
H
90
13.901
17.237
−40.509
1.00
13.36
H


ATOM
3573
CG
ASP
H
90
14.319
17.678
−39.111
1.00
13.47
H


ATOM
3574
OD1
ASP
H
90
14.207
16.875
−38.153
1.00
12.70
H


ATOM
3575
OD2
ASP
H
90
14.747
18.841
−38.960
1.00
13.27
H


ATOM
3576
C
ASP
H
90
13.639
15.296
−42.083
1.00
11.74
H


ATOM
3577
O
ASP
H
90
12.421
15.162
−42.082
1.00
11.55
H


ATOM
3578
N
THR
H
91
14.379
15.000
−43.150
1.00
10.83
H


ATOM
3579
CA
THR
H
91
13.739
14.477
−44.359
1.00
9.48
H


ATOM
3580
CB
THR
H
91
14.758
14.316
−45.534
1.00
7.81
H


ATOM
3581
OG1
THR
H
91
15.200
15.615
−45.947
1.00
7.57
H


ATOM
3582
CG2
THR
H
91
14.111
13.659
−46.748
1.00
6.29
H


ATOM
3583
C
THR
H
91
13.084
13.138
−44.019
1.00
8.73
H


ATOM
3584
O
THR
H
91
13.738
12.204
−43.531
1.00
8.19
H


ATOM
3585
N
ALA
H
92
11.776
13.068
−44.241
1.00
8.36
H


ATOM
3586
CA
ALA
H
92
11.017
11.852
−43.951
1.00
8.03
H


ATOM
3587
CB
ALA
H
92
11.149
11.491
−42.471
1.00
6.60
H


ATOM
3588
C
ALA
H
92
9.548
12.009
−44.290
1.00
6.21
H


ATOM
3589
O
ALA
H
92
9.092
13.092
−44.669
1.00
3.46
H


ATOM
3590
N
ILE
H
93
8.823
10.905
−44.157
1.00
6.09
H


ATOM
3591
CA
ILE
H
93
7.399
10.905
−44.390
1.00
6.84
H


ATOM
3592
CB
ILE
H
93
6.920
9.571
−44.932
1.00
6.37
H


ATOM
3593
CG2
ILE
H
93
5.416
9.615
−45.139
1.00
6.16
H


ATOM
3594
CG1
ILE
H
93
7.606
9.289
−46.259
1.00
7.33
H


ATOM
3595
CD1
ILE
H
93
7.328
7.897
−46.781
1.00
8.98
H


ATOM
3596
C
ILE
H
93
6.796
11.126
−43.023
1.00
6.45
H


ATOM
3597
O
ILE
H
93
6.982
10.309
−42.134
1.00
7.71
H


ATOM
3598
N
TYR
H
94
6.127
12.254
−42.828
1.00
7.32
H


ATOM
3599
CA
TYR
H
94
5.536
12.521
−41.527
1.00
8.20
H


ATOM
3600
CB
TYR
H
94
5.547
14.022
−41.207
1.00
7.72
H


ATOM
3601
CG
TYR
H
94
6.930
14.526
−40.868
1.00
6.95
H


ATOM
3602
CD1
TYR
H
94
7.942
14.513
−41.825
1.00
6.29
H


ATOM
3603
CE1
TYR
H
94
9.235
14.867
−41.513
1.00
6.51
H


ATOM
3604
CD2
TYR
H
94
7.252
14.927
−39.569
1.00
7.60
H


ATOM
3605
CE2
TYR
H
94
8.552
15.290
−39.241
1.00
8.06
H


ATOM
3606
CZ
TYR
H
94
9.544
15.250
−40.232
1.00
7.37
H


ATOM
3607
OH
TYR
H
94
10.844
15.565
−39.926
1.00
7.51
H


ATOM
3608
C
TYR
H
94
4.128
11.974
−41.467
1.00
8.37
H


ATOM
3609
O
TYR
H
94
3.231
12.385
−42.217
1.00
8.36
H


ATOM
3610
N
TYR
H
95
3.950
11.015
−40.572
1.00
7.89
H


ATOM
3611
CA
TYR
H
95
2.658
10.387
−40.373
1.00
7.44
H


ATOM
3612
CB
TYR
H
95
2.824
8.887
−40.112
1.00
7.20
H


ATOM
3613
CG
TYR
H
95
3.349
8.085
−41.279
1.00
6.80
H


ATOM
3614
CD1
TYR
H
95
2.508
7.660
−42.295
1.00
6.39
H


ATOM
3615
CE1
TYR
H
95
2.994
6.925
−43.365
1.00
8.93
H


ATOM
3616
CD2
TYR
H
95
4.689
7.757
−41.360
1.00
6.07
H


ATOM
3617
CE2
TYR
H
95
5.186
7.027
−42.419
1.00
8.64
H


ATOM
3618
CZ
TYR
H
95
4.336
6.608
−43.425
1.00
10.04
H


ATOM
3619
OH
TYR
H
95
4.834
5.866
−44.482
1.00
13.38
H


ATOM
3620
C
TYR
H
95
1.888
10.998
−39.209
1.00
6.27
H


ATOM
3621
O
TYR
H
95
2.431
11.316
−38.153
1.00
4.94
H


ATOM
3622
N
CYS
H
96
0.593
11.129
−39.431
1.00
8.19
H


ATOM
3623
CA
CYS
H
96
−0.370
11.655
−38.470
1.00
7.75
H


ATOM
3624
C
CYS
H
96
−1.075
10.462
−37.805
1.00
6.55
H


ATOM
3625
O
CYS
H
96
−1.678
9.647
−38.505
1.00
6.33
H


ATOM
3626
CB
CYS
H
96
−1.396
12.450
−39.250
1.00
8.73
H


ATOM
3627
SG
CYS
H
96
−2.753
13.021
−38.248
1.00
18.02
H


ATOM
3628
N
ALA
H
97
−1.024
10.343
−36.482
1.00
5.62
H


ATOM
3629
CA
ALA
H
97
−1.708
9.217
−35.842
1.00
6.65
H


ATOM
3630
CB
ALA
H
97
−0.705
8.135
−35.433
1.00
4.88
H


ATOM
3631
C
ALA
H
97
−2.591
9.600
−34.652
1.00
7.14
H


ATOM
3632
O
ALA
H
97
−2.270
10.525
−33.889
1.00
6.80
H


ATOM
3633
N
LYS
H
98
−3.706
8.876
−34.504
1.00
7.33
H


ATOM
3634
CA
LYS
H
98
−4.695
9.107
−33.435
1.00
6.92
H


ATOM
3635
CB
LYS
H
98
−6.118
9.141
−34.047
1.00
7.96
H


ATOM
3636
CG
LYS
H
98
−7.243
8.683
−33.099
1.00
8.65
H


ATOM
3637
CD
LYS
H
98
−8.577
8.713
−33.793
1.00
7.93
H


ATOM
3638
CE
LYS
H
98
−9.632
8.044
−32.957
1.00
8.38
H


ATOM
3639
NZ
LYS
H
98
−9.289
6.614
−32.781
1.00
11.17
H


ATOM
3640
C
LYS
H
98
−4.631
8.081
−32.291
1.00
5.55
H


ATOM
3641
O
LYS
H
98
−4.677
6.876
−32.522
1.00
4.02
H


ATOM
3642
N
ALA
H
99
−4.526
8.582
−31.063
1.00
5.94
H


ATOM
3643
CA
ALA
H
99
−4.466
7.744
−29.870
1.00
6.05
H


ATOM
3644
CB
ALA
H
99
−3.893
8.530
−28.713
1.00
5.32
H


ATOM
3645
C
ALA
H
99
−5.851
7.215
−29.498
1.00
6.38
H


ATOM
3646
O
ALA
H
99
−6.880
7.829
−29.806
1.00
6.74
H


ATOM
3647
N
LYS
H
100
−5.863
6.073
−28.823
1.00
6.25
H


ATOM
3648
CA
LYS
H
100
−7.109
5.446
−28.432
1.00
6.98
H


ATOM
3649
CB
LYS
H
100
−6.862
4.012
−27.966
1.00
7.85
H


ATOM
3650
CG
LYS
H
100
−8.137
3.260
−27.666
1.00
8.20
H


ATOM
3651
CD
LYS
H
100
−7.854
1.843
−27.230
1.00
10.16
H


ATOM
3652
CE
LYS
H
100
−7.573
0.930
−28.401
1.00
11.45
H


ATOM
3653
NZ
LYS
H
100
−8.683
0.917
−29.389
1.00
10.69
H


ATOM
3654
C
LYS
H
100
−7.833
6.209
−27.337
1.00
7.43
H


ATOM
3655
O
LYS
H
100
−9.067
6.222
−27.292
1.00
7.57
H


ATOM
3656
N
ARG
H
101
−7.068
6.848
−26.455
1.00
6.66
H


ATOM
3657
CA
ARG
H
101
−7.667
7.591
−25.355
1.00
5.82
H


ATOM
3658
CB
ARG
H
101
−7.125
7.080
−24.033
1.00
7.35
H


ATOM
3659
CG
ARG
H
101
−6.901
5.583
−24.024
1.00
8.88
H


ATOM
3660
CD
ARG
H
101
−6.708
5.089
−22.605
1.00
10.61
H


ATOM
3661
NE
ARG
H
101
−7.985
4.767
−21.985
1.00
11.45
H


ATOM
3662
CZ
ARG
H
101
−8.324
5.114
−20.755
1.00
13.93
H


ATOM
3663
NH1
ARG
H
101
−7.479
5.808
−19.996
1.00
17.72
H


ATOM
3664
NH2
ARG
H
101
−9.504
4.753
−20.281
1.00
12.33
H


ATOM
3665
C
ARG
H
101
−7.432
9.085
−25.459
1.00
4.76
H


ATOM
3666
O
ARG
H
101
−6.777
9.534
−26.393
1.00
6.34
H


ATOM
3667
N
VAL
H
102
−7.960
9.848
−24.501
1.00
3.31
H


ATOM
3668
CA
VAL
H
102
−7.815
11.302
−24.516
1.00
1.00
H


ATOM
3669
CB
VAL
H
102
−8.656
12.030
−23.457
1.00
2.44
H


ATOM
3670
CG1
VAL
H
102
−9.799
12.724
−24.127
1.00
1.07
H


ATOM
3671
CG2
VAL
H
102
−9.099
11.083
−22.353
1.00
1.00
H


ATOM
3672
C
VAL
H
102
−6.434
11.817
−24.301
1.00
1.00
H


ATOM
3673
O
VAL
H
102
−6.142
12.932
−24.688
1.00
1.36
H


ATOM
3674
N
GLY
H
103
−5.592
11.034
−23.650
1.00
1.00
H


ATOM
3675
CA
GLY
H
103
−4.246
11.501
−23.422
1.00
2.80
H


ATOM
3676
C
GLY
H
103
−3.334
10.895
−24.457
1.00
5.14
H


ATOM
3677
O
GLY
H
103
−3.778
10.171
−25.335
1.00
5.99
H


ATOM
3678
N
ALA
H
104
−2.057
11.224
−24.381
1.00
7.98
H


ATOM
3679
CA
ALA
H
104
−1.081
10.647
−25.281
1.00
11.22
H


ATOM
3680
CB
ALA
H
104
0.259
11.310
−25.052
1.00
12.12
H


ATOM
3681
C
ALA
H
104
−1.080
9.230
−24.730
1.00
13.71
H


ATOM
3682
O
ALA
H
104
−0.454
8.956
−23.703
1.00
16.89
H


ATOM
3683
N
THR
H
105
−1.808
8.339
−25.383
1.00
12.18
H


ATOM
3684
CA
THR
H
105
−1.913
6.979
−24.889
1.00
10.87
H


ATOM
3685
CB
THR
H
105
−3.137
6.300
−25.540
1.00
11.27
H


ATOM
3686
OG1
THR
H
105
−4.258
7.186
−25.458
1.00
11.02
H


ATOM
3687
CG2
THR
H
105
−3.497
5.020
−24.828
1.00
11.22
H


ATOM
3688
C
THR
H
105
−0.646
6.143
−25.097
1.00
10.95
H


ATOM
3689
O
THR
H
105
−0.193
5.472
−24.173
1.00
11.18
H


ATOM
3690
N
GLY
H
106
−0.080
6.193
−26.303
1.00
9.89
H


ATOM
3691
CA
GLY
H
106
1.108
5.422
−26.610
1.00
8.03
H


ATOM
3692
C
GLY
H
106
0.873
4.532
−27.821
1.00
9.08
H


ATOM
3693
O
GLY
H
106
1.806
4.189
−28.551
1.00
8.94
H


ATOM
3694
N
TYR
H
107
−0.381
4.152
−28.041
1.00
9.04
H


ATOM
3695
CA
TYR
H
107
−0.722
3.318
−29.178
1.00
7.70
H


ATOM
3696
CB
TYR
H
107
−1.167
1.918
−28.728
1.00
7.28
H


ATOM
3697
CG
TYR
H
107
−2.176
1.870
−27.621
1.00
6.75
H


ATOM
3698
CD1
TYR
H
107
−3.531
1.704
−27.889
1.00
7.50
H


ATOM
3699
CE1
TYR
H
107
−4.461
1.622
−26.868
1.00
9.33
H


ATOM
3700
CD2
TYR
H
107
−1.773
1.954
−26.308
1.00
7.00
H


ATOM
3701
CE2
TYR
H
107
−2.680
1.871
−25.281
1.00
8.83
H


ATOM
3702
CZ
TYR
H
107
−4.029
1.706
−25.552
1.00
11.18
H


ATOM
3703
OH
TYR
H
107
−4.940
1.646
−24.498
1.00
13.47
H


ATOM
3704
C
TYR
H
107
−1.793
4.036
−29.970
1.00
8.28
H


ATOM
3705
O
TYR
H
107
−2.670
4.694
−29.404
1.00
8.79
H


ATOM
3706
N
PHE
H
108
−1.707
3.904
−31.290
1.00
8.59
H


ATOM
3707
CA
PHE
H
108
−2.618
4.594
−32.194
1.00
7.43
H


ATOM
3708
CB
PHE
H
108
−1.803
5.633
−32.928
1.00
6.07
H


ATOM
3709
CG
PHE
H
108
−0.641
6.100
−32.138
1.00
3.15
H


ATOM
3710
CD1
PHE
H
108
−0.828
6.931
−31.033
1.00
3.84
H


ATOM
3711
CD2
PHE
H
108
0.631
5.640
−32.428
1.00
1.87
H


ATOM
3712
CE1
PHE
H
108
0.251
7.304
−30.206
1.00
1.62
H


ATOM
3713
CE2
PHE
H
108
1.720
5.998
−31.621
1.00
2.47
H


ATOM
3714
CZ
PHE
H
108
1.529
6.834
−30.503
1.00
1.15
H


ATOM
3715
C
PHE
H
108
−3.343
3.712
−33.189
1.00
7.78
H


ATOM
3716
O
PHE
H
108
−2.716
3.093
−34.041
1.00
7.98
H


ATOM
3717
N
ASP
H
109
−4.671
3.703
−33.092
1.00
7.48
H


ATOM
3718
CA
ASP
H
109
−5.522
2.904
−33.958
1.00
6.76
H


ATOM
3719
CB
ASP
H
109
−6.827
2.525
−33.251
1.00
8.37
H


ATOM
3720
CG
ASP
H
109
−7.497
3.708
−32.566
1.00
9.76
H


ATOM
3721
OD1
ASP
H
109
−7.446
4.836
−33.080
1.00
12.11
H


ATOM
3722
OD2
ASP
H
109
−8.092
3.513
−31.496
1.00
11.64
H


ATOM
3723
C
ASP
H
109
−5.867
3.540
−35.287
1.00
6.63
H


ATOM
3724
O
ASP
H
109
−6.497
2.904
−36.137
1.00
7.36
H


ATOM
3725
N
LEU
H
110
−5.466
4.782
−35.500
1.00
5.24
H


ATOM
3726
CA
LEU
H
110
−5.786
5.398
−36.781
1.00
5.19
H


ATOM
3727
CB
LEU
H
110
−7.013
6.295
−36.650
1.00
4.04
H


ATOM
3728
CG
LEU
H
110
−7.465
6.907
−37.979
1.00
4.58
H


ATOM
3729
CD1
LEU
H
110
−7.936
5.827
−38.912
1.00
1.00
H


ATOM
3730
CD2
LEU
H
110
−8.592
7.914
−37.717
1.00
6.43
H


ATOM
3731
C
LEU
H
110
−4.624
6.200
−37.298
1.00
5.51
H


ATOM
3732
O
LEU
H
110
−4.076
7.038
−36.592
1.00
6.65
H


ATOM
3733
N
TRP
H
111
−4.247
5.957
−38.538
1.00
4.26
H


ATOM
3734
CA
TRP
H
111
−3.132
6.702
−39.088
1.00
4.57
H


ATOM
3735
CB
TRP
H
111
−1.912
5.790
−39.296
1.00
3.02
H


ATOM
3736
CG
TRP
H
111
−1.291
5.208
−38.059
1.00
1.95
H


ATOM
3737
CD2
TRP
H
111
0.081
5.316
−37.665
1.00
1.00
H


ATOM
3738
CE2
TRP
H
111
0.246
4.528
−36.503
1.00
1.00
H


ATOM
3739
CE3
TRP
H
111
1.189
6.001
−38.187
1.00
1.00
H


ATOM
3740
CD1
TRP
H
111
−1.890
4.389
−37.140
1.00
2.44
H


ATOM
3741
NE1
TRP
H
111
−0.971
3.975
−36.206
1.00
1.00
H


ATOM
3742
CZ2
TRP
H
111
1.482
4.401
−35.851
1.00
1.00
H


ATOM
3743
CZ3
TRP
H
111
2.412
5.882
−37.549
1.00
1.00
H


ATOM
3744
CH2
TRP
H
111
2.553
5.084
−36.387
1.00
2.97
H


ATOM
3745
C
TRP
H
111
−3.534
7.310
−40.423
1.00
5.19
H


ATOM
3746
O
TRP
H
111
−4.602
7.016
−40.963
1.00
4.62
H


ATOM
3747
N
GLY
H
112
−2.669
8.178
−40.933
1.00
6.36
H


ATOM
3748
CA
GLY
H
112
−2.917
8.808
−42.209
1.00
7.94
H


ATOM
3749
C
GLY
H
112
−1.848
8.270
−43.134
1.00
9.94
H


ATOM
3750
O
GLY
H
112
−0.962
7.545
−42.674
1.00
7.59
H


ATOM
3751
N
ARG
H
113
−1.911
8.609
−44.420
1.00
12.17
H


ATOM
3752
CA
ARG
H
113
−0.918
8.130
−45.387
1.00
14.63
H


ATOM
3753
CB
ARG
H
113
−1.415
8.357
−46.821
1.00
19.69
H


ATOM
3754
CG
ARG
H
113
−2.716
7.645
−47.220
1.00
26.76
H


ATOM
3755
CD
ARG
H
113
−3.136
7.992
−48.682
1.00
32.39
H


ATOM
3756
NE
ARG
H
113
−3.098
9.435
−48.981
1.00
36.17
H


ATOM
3757
CZ
ARG
H
113
−3.435
9.974
−50.154
1.00
39.14
H


ATOM
3758
NH1
ARG
H
113
−3.844
9.194
−51.153
1.00
40.77
H


ATOM
3759
NH2
ARG
H
113
−3.348
11.291
−50.334
1.00
39.73
H


ATOM
3760
C
ARG
H
113
0.459
8.801
−45.236
1.00
13.93
H


ATOM
3761
O
ARG
H
113
1.454
8.288
−45.747
1.00
14.13
H


ATOM
3762
N
GLY
H
114
0.508
9.949
−44.560
1.00
12.46
H


ATOM
3763
CA
GLY
H
114
1.763
10.660
−44.373
1.00
10.52
H


ATOM
3764
C
GLY
H
114
2.053
11.683
−45.468
1.00
9.35
H


ATOM
3765
O
GLY
H
114
1.436
11.642
−46.527
1.00
8.23
H


ATOM
3766
N
THR
H
115
2.963
12.618
−45.192
1.00
8.71
H


ATOM
3767
CA
THR
H
115
3.398
13.635
−46.151
1.00
6.50
H


ATOM
3768
CB
THR
H
115
3.021
15.043
−45.753
1.00
7.27
H


ATOM
3769
OG1
THR
H
115
1.952
14.999
−44.822
1.00
9.76
H


ATOM
3770
CG2
THR
H
115
2.636
15.855
−46.966
1.00
7.54
H


ATOM
3771
C
THR
H
115
4.925
13.624
−46.129
1.00
7.01
H


ATOM
3772
O
THR
H
115
5.554
13.574
−45.055
1.00
2.98
H


ATOM
3773
N
LEU
H
116
5.511
13.699
−47.318
1.00
6.85
H


ATOM
3774
CA
LEU
H
116
6.953
13.701
−47.463
1.00
6.07
H


ATOM
3775
CB
LEU
H
116
7.352
13.132
−48.812
1.00
5.44
H


ATOM
3776
CG
LEU
H
116
8.812
13.352
−49.199
1.00
5.58
H


ATOM
3777
CD1
LEU
H
116
9.727
12.426
−48.399
1.00
3.24
H


ATOM
3778
CD2
LEU
H
116
8.941
13.099
−50.685
1.00
5.27
H


ATOM
3779
C
LEU
H
116
7.531
15.082
−47.350
1.00
7.43
H


ATOM
3780
O
LEU
H
116
7.132
15.997
−48.059
1.00
9.44
H


ATOM
3781
N
VAL
H
117
8.481
15.228
−46.443
1.00
9.93
H


ATOM
3782
CA
VAL
H
117
9.151
16.500
−46.275
1.00
11.48
H


ATOM
3783
CB
VAL
H
117
9.107
16.966
−44.817
1.00
11.24
H


ATOM
3784
CG1
VAL
H
117
9.929
18.231
−44.648
1.00
11.87
H


ATOM
3785
CG2
VAL
H
117
7.675
17.217
−44.418
1.00
11.74
H


ATOM
3786
C
VAL
H
117
10.587
16.250
−46.706
1.00
11.33
H


ATOM
3787
O
VAL
H
117
11.247
15.342
−46.187
1.00
10.03
H


ATOM
3788
N
THR
H
118
11.049
17.032
−47.677
1.00
11.55
H


ATOM
3789
CA
THR
H
118
12.412
16.898
−48.182
1.00
13.80
H


ATOM
3790
CB
THR
H
118
12.469
16.720
−49.714
1.00
12.54
H


ATOM
3791
OG1
THR
H
118
11.597
15.658
−50.113
1.00
17.37
H


ATOM
3792
CG2
THR
H
118
13.880
16.398
−50.147
1.00
11.46
H


ATOM
3793
C
THR
H
118
13.156
18.177
−47.889
1.00
15.05
H


ATOM
3794
O
THR
H
118
12.809
19.235
−48.422
1.00
16.32
H


ATOM
3795
N
VAL
H
119
14.176
18.102
−47.048
1.00
14.62
H


ATOM
3796
CA
VAL
H
119
14.932
19.302
−46.763
1.00
15.25
H


ATOM
3797
CB
VAL
H
119
15.212
19.441
−45.249
1.00
15.70
H


ATOM
3798
CG1
VAL
H
119
15.740
18.137
−44.684
1.00
18.79
H


ATOM
3799
CG2
VAL
H
119
16.205
20.559
−45.013
1.00
14.10
H


ATOM
3800
C
VAL
H
119
16.242
19.309
−47.544
1.00
15.85
H


ATOM
3801
O
VAL
H
119
17.170
18.567
−47.232
1.00
15.88
H


ATOM
3802
N
SER
H
120
16.297
20.129
−48.589
1.00
17.32
H


ATOM
3803
CA
SER
H
120
17.511
20.245
−49.385
1.00
18.51
H


ATOM
3804
CB
SER
H
120
17.491
19.307
−50.597
1.00
18.68
H


ATOM
3805
OG
SER
H
120
17.034
19.984
−51.754
1.00
16.68
H


ATOM
3806
C
SER
H
120
17.669
21.665
−49.879
1.00
19.18
H


ATOM
3807
O
SER
H
120
16.789
22.509
−49.698
1.00
16.51
H


ATOM
3808
N
SER
H
121
18.808
21.908
−50.518
1.00
21.95
H


ATOM
3809
CA
SER
H
121
19.120
23.215
−51.069
1.00
23.17
H


ATOM
3810
CB
SER
H
121
20.568
23.602
−50.719
1.00
22.76
H


ATOM
3811
OG
SER
H
121
20.655
24.126
−49.404
1.00
23.27
H


ATOM
3812
C
SER
H
121
18.890
23.299
−52.584
1.00
23.84
H


ATOM
3813
O
SER
H
121
18.862
24.394
−53.122
1.00
24.66
H





REMARK A = monomer A of allergen;


REMARK L = light chain of antibody, variable domain;


REMARK H = heavy chain of antibody, variable domain













TABLE IX





Amino acid sequences of the rBLG-His6, rBLG-His6


T18Y and rBLG-His6 T18Y/E45Y/L57Y are shown. The


His6 tag is in italics, mutated amino acids are


bolded and underlined.















rBLG-His6:


(SEQ ID NO: 9)








1
LIVTQTMKGL DIQKVAGTWY SLAMAASDIS LLDAQSABLR


41
VYVEELKBTB EGDLEILLQK WENGECAQKK IIAEKTKIPA


81
VFKIDALNEN KVLVLDTDYK KYLLFCMENS AEPEQSLVCQ


121
CLVRTBEVDD EALEKFDKAL KALBMHIRLS FNBTQLEEQC


161
HIHHHHHH







rBLG-His6 T18Y:


(SEQ ID NO: 10)








1
LIVTQTMKGL DIQKVAGYWY SLAMAASDIS LLDAQSABLR


41
VYVEELKBTB EGDLEILLQK WENGECAQKK IIAEKTKIPA


81
VFKIDALNEN KVLVLDTDYK KYLLFCMENS AEBEQSLVCQ


121
CLVRTPEVDD EALEKFDKAL KALBMHIRLS FNPTQLEEQC


161
HIHHHHHH







rBLG-His6 T18Y/E45Y/L57Y:


(SEQ ID NO: 11)








1
LIVTQTMKGL DIQKVAGYWY SLAMAASDIS LLDAQSAPLR


41
VYVEYLKPTP EGDLEIYLQK WENGECAQKK IIAEKTKIPA


81
VFKIDALNEN KVLVLDTDYK KYLLFCMENS AEPEQSLVCQ


121
CLVRTPEVDD EALEKFDKAL KALPMHIRLS FNPTQLEEQC


161
HIHHHHHH
















TABLE X





The primers used for the PCR amplification of rBLG-His6,


rBLG-His6 T18Y and rBLG-His6 T18Y/E45Y/L57Y mutant.


Restriction enzyme sites are shown in italics.


Overlapping areas and stop codons are underlined.


Mutated codons are bolded, underlined and in italics.

















             SfiI        NcoI


Primer 1.
GAA TCC GC  GCC ATG GCC CTG ATT GTG



ACC (SEQ ID NO: 124)


 



        HindIII Stop


Primer 2.
TTA CTC AAG CTT TTA ATG GTG ATG GTG ATG ATG AAT ATG



GCA CTG TTC TTC CAG C (SEQ ID NO: 125)


 



           StuI


Primer 3.
CC ATG AAA GGC CTG GAT ATT CAG AAA GTG GCG GGC  



TGG TAT AGC C (SEQ ID NO: 126)


 



Overlapping area with the primer 5


Primer 4.
  AAT TTC CAG ATC GCC TTC CGG GGT CGG TTT CAG  



TTC CAC ATA CAC ACG C (SEQ ID NO: 127)


 



Overlapping area with the primer 4


Primer 5.
 GGC GAT CTG GAA ATT   CTG CAG AAA TGG G



(SEQ ID NO: 124)
















TABLE XI







The association and dissociation constants of the D1 IgE Fab


to nBLG, rBLG-His6 and its mutants (see FIG. 24).















Triple



nBLG
rBLGhis
T18Y
mutant

















Kd (1/s)
4.8e−3
 8.2e−3
8.2e−2
—



Ka (1/Ms)
1.8e6
9.61e5
1.3e5
—



KD (M)
2.7e−9
 8.5e−9
6.1e−7
—



KA (1/M)
3.2e8
 1.2e8
1.6e6
—










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## Claims

1. A method for selecting a modified β-lactoglobulin as a hypoallergen candidate, the method comprising the steps of:
(a) modifying an unmodified nucleic acid sequence encoding unmodified β-lactoglobulin represented by SEQ ID NO: 8 to produce a modified nucleic acid sequence encoding a modified β-lactoglobulin, wherein the modified β-lactoglobulin comprises an amino acid mutation in 1-5 amino acids in one or more of the following amino acid regions of SEQ ID NO:8: 18-20, 42-47, 55-59, 65-70, 125-127, and 154-161;
(b) expressing or producing the modified β-lactoglobulin from the modified nucleic acid sequence;
(c) contacting the modified β-lactoglobulin with an IgE antibody specific for unmodified β-lactoglobulin;
(d) comparing binding affinity of the modified β-lactoglobulin to the IgE antibody to binding affinity of unmodified β-lactoglobulin to the IgE antibody; and
(e) selecting the modified β-lactoglobulin as a hypoallergen candidate if the binding affinity of the modified β-lactoglobulin to the IgE antibody is decreased by at least tenfold compared to the binding affinity of the IgE antibody to the unmodified β-lactoglobulin.

2. A method for producing a modified allergenic polypeptide, the method comprising the steps of:
(a) modifying an unmodified nucleic acid sequence encoding an unmodified β-lactoglobulin polypeptide (SEQ ID NO:8) to produce a modified nucleic acid sequence encoding a modified β-lactoglobulin polypeptide wherein the modified β-lactoglobulin polypeptide comprises a T18Y mutation or a T18Y/E45Y/L57Y mutation; and
(b) expressing or producing the modified β-lactoglobulin polypeptide from the modified nucleic acid.

3. A method according to claim 1, wherein the modified β-lactoglobulin comprises an amino acid mutation in at least amino acid region 18-20.

4. A method according to claim 1, wherein the modified β-lactoglobulin comprises an amino acid mutation in at least amino acid region 42-47.

5. A method according to claim 1, wherein the modified β-lactoglobulin comprises an amino acid mutation in at least amino acid region 55-59.

6. A method according to claim 1, wherein the modified β-lactoglobulin comprises an amino acid mutation in at least amino acid region 65-70.

7. A method according to claim 1, wherein the modified β-lactoglobulin comprises an amino acid mutation in at least amino acid region 154-161.